entry
stringlengths 6
10
| entry_name
stringlengths 5
11
| protein_name
stringlengths 3
2.44k
| sequence
stringlengths 2
35.2k
| function
stringlengths 7
11k
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A0LNN5
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SFMCT_SYNFM
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L-lactate transporter (SfMCT)
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MADQQTTMPRWVPLLLGLLGSTTCGMLLYAWSVFIKPLNAEFGWSRAEIAMAFAICCLIFGLMTFPAGRLSDKMGPRKVVMTGGVLLAIGFILSGFIQSKYQLYITYGVIAGFGGGMIYLPPIATAPKWWPDRRALATGFAVVGLGLGSFLMGPLATYIIEKPGMGWRYVFWYCGVAMGIMALIAGAFLEPPPAGWKPAGYTPPAPPAGAAAPKVTRDWTYEEAKGDTKFWLLYLAYFCGSFAGLMVIGHLAGFGRDAGLTAMAAAGAVSSLAFSNAATRILSGWFVDKIGIRVYFAALFALQTAAMIAIFQLGGSVVGLSIVAIVIGWNYGAMFTLFPATCLQFYGPTAQGSNYGLLFTACGLAGFAGPWVGGWLKDTTGTYYLPFLCAAALCALGTAIVFMTKPPEKKHA
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Proton-coupled L-lactate specific transporter.
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A0LU48
|
DOP_ACIC1
|
Depupylase (EC 3.4.-.-)
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MHRVMGIETEYGISVPHQPNANAMAASSQVVNAYAPIGAPAQRQARWDFEEENPLRDARGFEVAREAADPSQLTDEDLGLANVILTNGARLYVDHAHPEYSTPEVTNPRDAVLWDKAGERIMAEAARRAADLPMGWTIQLYKNNTDNKGASYGCHENYLMNRSTPFADIVRHLIPFFVTRQVFCGAGRVGIGADGRGEGFQLSQRADFFEVEVGLETTLKRPIINTRDEPHADPEKYRRLHVIIGDANMSEIATYLKLGTTALVLAMIEDGFLSQDFSVESPVGALRAVSHDPTLRYQLRLHDGRRLTAVQLQMEYLEQARKYVEDRFGTDVDDMTRDVLDRWETTLVRLADDPMQLSRDLDWVAKLSILEGYRQRENLPWSAHKLQLVDLQYHDVRPDRGLYNRLVARGRMNLLVDEAAVRTAMHEPPNDTRAYFRGRCLAKFGAEIAAASWDSVIFDLPGRDSLQRVPTLEPLRGTRAHVGDLLDRCRSATELVAALTGGR
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Displays depupylase (DPUP) activity, removing conjugated Pup from target proteins is thus involved in the recycling of Pup and may function similarly to deubiquitinases (DUBs) in eukaryotes to prevent or promote proteasomal degradation of certain proteins. Is also able to catalyze the deamidation of the C-terminal glutamine to glutamate in a variant of the prokaryotic ubiquitin-like protein Pup however, since Pup from A.cellulolyticus possesses a C-terminal glutamate, this deamidase activity may be of no significance in vivo.
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A0M8Q6
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IGLC7_HUMAN
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Immunoglobulin lambda constant 7 (Ig lambda-7 chain C region)
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GQPKAAPSVTLFPPSSEELQANKATLVCLVSDFNPGAVTVAWKADGSPVKVGVETTKPSKQSNNKYAASSYLSLTPEQWKSHRSYSCRVTHEGSTVEKTVAPAECS
|
Constant region of immunoglobulin light chains. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen.
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A0M8R6
|
CAV1_PAPAN
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Caveolin-1
|
MSGGKYVDSEGHLYTVPIREQGNIYKPNNKAMADELSEKQVYDAHTKEIDLVNRDPKHLNDDVVKIDFEDVIAEPEGTHSFDGIWKASFTTFTVTKYWFYRLLSALFGIPMALVWGIYFAILSFLHIWAVVPCIKSFLIEIQCISRVYSIYVHTVCDPLFEAVGKIFSNVRINLQKEI
|
May act as a scaffolding protein within caveolar membranes. Forms a stable heterooligomeric complex with CAV2 that targets to lipid rafts and drives caveolae formation. Mediates the recruitment of CAVIN proteins (CAVIN1/2/3/4) to the caveolae (By similarity). Interacts directly with G-protein alpha subunits and can functionally regulate their activity (By similarity). Involved in the costimulatory signal essential for T-cell receptor (TCR)-mediated T-cell activation. Its binding to DPP4 induces T-cell proliferation and NF-kappa-B activation in a T-cell receptor/CD3-dependent manner (By similarity). Recruits CTNNB1 to caveolar membranes and may regulate CTNNB1-mediated signaling through the Wnt pathway (By similarity). Negatively regulates TGFB1-mediated activation of SMAD2/3 by mediating the internalization of TGFBR1 from membrane rafts leading to its subsequent degradation (By similarity).
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A0M8R7
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MET_PAPAN
|
Hepatocyte growth factor receptor (HGF receptor) (EC 2.7.10.1) (HGF/SF receptor) (Proto-oncogene c-Met) (Scatter factor receptor) (SF receptor) (Tyrosine-protein kinase Met)
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MKAPAVLVPGILVLLFTLVQRSNGECKEALAKSEMNVNMKYQLPNFTAETAIQNVILHEHHIFLGATNYIYVLNEEDLQKVAEYKTGPVLEHPDCFPCQDCSSKANLSGGVWKDNINMALVVDTYYDDQLISCGSVNRGTCQRHVFPHNHTADIQSEVHCIFSPQIEEPSQCPDCVVSALGAKVLSSVKDRFINFFVGNTINSSYFPHHPLHSISVRRLKETKDGFMFLTDQSYIDVLPEFRDSYPIKYIHAFESNNFIYFLTVQRETLNAQTFHTRIIRFCSLNSGLHSYMEMPLECILTEKRKKRSTKKEVFNILQAAYVSKPGAQLARQIGASLNDDILFGVFAQSKPDSAEPMDRSAMCAFPIKYVNDFFNKIVNKNNVRCLQHFYGPNHEHCFNRTLLRNSSGCEARRDEYRAEFTTALQRVDLFMGQFSEVLLTSISTFVKGDLTIANLGTSEGRFMQVVVSRSGPSTPHVNFLLDSHPVSPEVIVEHPLNQNGYTLVVTGKKITKIPLNGLGCRHFQSCSQCLSAPPFVQCGWCHDKCVRSEECPSGTWTQQICLPAIYKVFPTSAPLEGGTRLTICGWDFGFRRNNKFDLKKTRVLLGNESCTLTLSESTMNILKCTVGPAMNKHFNMSIIISNGHGTTQYSTFSYVDPIITSISPKYGPMAGGTLLTLTGNYLNSGNSRHISIGGKTCTLKSVSNSILECYTPAQTISTEFAVKLKIDLANRETSIFSYREDPIVYEIHPTKSFISGGSTITGVGKNLHSVSVPRMVINVHEAGRNFTVACQHRSNSEIICCTTPSLQQLNLQLPLKTKAFFMLDGILSKYFDLIYVHNPVFKPFEKPVMISMGNENVLEIKGNDIDPEAVKGEVLKVGNKSCENIHLHSEAVLCTVPNDLLKLNSELNIEWKQAISSTVLGKVIVQPDQNFTGLIAGVVSISIALLLLLGLFLWLKKRKQIKDLGSELVRYDARVHTPHLDRLVSARSVSPTTEMVSNESVDYRATFPEDQFPNSSQNGSCRQVQYPLTDMSPILTSGDSDISSPLLQNTVHIDLSALNPELVQAVQHVVIGPSSLIVHFNEVIGRGHFGCVYHGTLLDNDGKKIHCAVKSLNRITDIGEVSQFLTEGIIMKDFSHPNVLSLLGICLRSEGSPLVVLPYMKHGDLRNFIRNETHNPTVKDLIGFGLQVAKGMKYLASKKFVHRDLAARNCMLDEKFTVKVADFGLARDMYDKEYYSVHNKTGAKLPVKWMALESLQTQKFTTKSDVWSFGVLLWELMTRGAPPYPDVNTFDITVYLLQGRRLLQPEYCPDPLYEVMLKCWHPKAEMRPSFSELVSRISAIFSTFIGEHYVHVNATYVNVKCVAPYPSLLSSEDNADDEVDT
|
Receptor tyrosine kinase that transduces signals from the extracellular matrix into the cytoplasm by binding to hepatocyte growth factor/HGF ligand. Regulates many physiological processes including proliferation, scattering, morphogenesis and survival. Ligand binding at the cell surface induces autophosphorylation of MET on its intracellular domain that provides docking sites for downstream signaling molecules. Following activation by ligand, interacts with the PI3-kinase subunit PIK3R1, PLCG1, SRC, GRB2, STAT3 or the adapter GAB1. Recruitment of these downstream effectors by MET leads to the activation of several signaling cascades including the RAS-ERK, PI3 kinase-AKT, or PLCgamma-PKC. The RAS-ERK activation is associated with the morphogenetic effects while PI3K/AKT coordinates prosurvival effects. During embryonic development, MET signaling plays a role in gastrulation, development and migration of muscles and neuronal precursors, angiogenesis and kidney formation. In adults, participates in wound healing as well as organ regeneration and tissue remodeling. Promotes also differentiation and proliferation of hematopoietic cells (By similarity).
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A0M8S6
|
CAV2_FELCA
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Caveolin-2
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MGLETEKADVQLFMDDDSYSRHSGVDYADPDKFADSGSDRDPHRLNSNLKVGFEDVIAEPVSTHSFDKVWICSHALFEISKYVIYKFLTLFLAIPLAFAAGILFATLSCLHIWIIMPFVKTCLMVLPSVQTIWKSITDVVIAPLCTSVGRSFSSVSLQLSHD
|
May act as a scaffolding protein within caveolar membranes. Interacts directly with G-protein alpha subunits and can functionally regulate their activity. Acts as an accessory protein in conjunction with CAV1 in targeting to lipid rafts and driving caveolae formation. The Ser-36 phosphorylated form has a role in modulating mitosis in endothelial cells. Positive regulator of cellular mitogenesis of the MAPK signaling pathway. Required for the insulin-stimulated nuclear translocation and activation of MAPK1 and STAT3, and the subsequent regulation of cell cycle progression (By similarity).
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A0M8S7
|
CAV1_FELCA
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Caveolin-1
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MSGGKYVDSEGHLYTVPIREQGNIYKPNNKAMAEEINEKQVYDAHTKEIDLVNRDPKHLNDDVVKIDFEDVIAEPEGTHSFDGIWKASFTTFTVTKYWFYRLLSALFGIPMALIWGIYFAILSFLHIWAVVPCIKSFLIEIQCISRVYSIYVHTFCDPFFEAVGKIFSNIRINMQKEI
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May act as a scaffolding protein within caveolar membranes. Forms a stable heterooligomeric complex with CAV2 that targets to lipid rafts and drives caveolae formation. Mediates the recruitment of CAVIN proteins (CAVIN1/2/3/4) to the caveolae (By similarity). Interacts directly with G-protein alpha subunits and can functionally regulate their activity (By similarity). Involved in the costimulatory signal essential for T-cell receptor (TCR)-mediated T-cell activation. Its binding to DPP4 induces T-cell proliferation and NF-kappa-B activation in a T-cell receptor/CD3-dependent manner (By similarity). Recruits CTNNB1 to caveolar membranes and may regulate CTNNB1-mediated signaling through the Wnt pathway (By similarity). Negatively regulates TGFB1-mediated activation of SMAD2/3 by mediating the internalization of TGFBR1 from membrane rafts leading to its subsequent degradation (By similarity).
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A0M8S8
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MET_FELCA
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Hepatocyte growth factor receptor (HGF receptor) (EC 2.7.10.1) (HGF/SF receptor) (Proto-oncogene c-Met) (Scatter factor receptor) (SF receptor) (Tyrosine-protein kinase Met)
|
MKAPAVLAPGILVLLFTLVQKSYGECREALVKSEMNVNMKYQLPNFTAETPIQNVVLHKHHIYLGAVNYIYVLNDKDLQKVAEYKTGPVLEHPDCFPCQDCSHKANLSGGVWKDNINMALLIDTYYDDQLISCGSVHRGTCQRHVLPPSNTADILSKVHCMYSPQADEESSHCPDCVVSALGTKVLISEKGRFINFFVGNTINSSYLTDHSLHSISVRRLKETQDGFKFLTDQSYIDVLPEFRDSYPIKYIHAFESNRFIYFLTVQRETLDAQTFHTRIIRFCSVDSGLHSYMEMPLECILTEKRRKRSTREEVFNILQAAYVSKPGAHLAKQIGANLNDDILYGVFAQSKPDSAEPMNRSAVCAFPIKYVNEFFNKIVNKNNVRCLQHFYGPNHEHCFNRTLLRNSSGCEVRSDEYRTEFTTALQRVDLFMGQFNQVLLTSISTFIKGDLTIANLGTSEGRFMQVVVSRSGSSTPHVNFRLDSHPVSSEAIVEHPLNQNGYTLVVTGKKITKIPLNGLGCEHFQSCSQCLSAPPFVQCGWCHDKCVQLEECPSGTWTQEICLPTIYEVFPTSAPLEGGTMLTVCGWDFGFRRNNKFDLKKTRVFLGNESCTLTLSESTTNMLKCTVGPAVNEHFNISIIISNGRGTAQYSTFSYVDPVITSIFPSYGPKTGGTLLTLTGKYLNSGNSRHISIGGKTCTLKSVSDSILECYTPAQTIPTEFPIKLKIDLANREMNSFSYQEDPIVYAIHPTKSFISGGSTITAVGKNLNSVSVLRMVISVHETRRNFTVACHHRSNSEIICCTTPSLQQLNLQLPLKTKAFFMLDGIHSKYFDLIYVHNPVFKPFEKPVMISIGNENVLEIKGNDIDPEAVKGEVLKVGNKSCETIYSDSEAVLCKVPNDLLKLNNELNIEWKQAVSSTILGKVIVQPDQNFTGLIVGVISISIILLLLLGVFLWLKKRKQIKDLGSELVRYDARVHTPHLDRLVSARSVSPTTEMVSNESVDYRATFPEDQFPNSSQNGSCRQVQYPLTDLSPMLNSGDSDISSPLLQNTVHIDLSALNPELVQAVQHVVIGPSSLIVHFNEVIGRGHFGCVYHGTLLDSDDKKIHCAVKSLNRITDIGEVSQFLTEGIIMKDFSHPNVLSLLGICLRSEGSPLVVLPYMKHGDLRNFIRNETHNPTVKDLIGFGLQVAKGMKYLASKKFVHRDLAARNCMLDEKFTVKVADFGLARDMYDKEYYSVHNKTGAKLPVKWMALESLQTQKFTTKSDVWSFGVLLWELMTRGAPPYPDVNTFDITVYLLQGRRLLQPEYCPDPLYEVMLKCWHPKAELRPSFSELVSRISAIFSTFIGEHYVHVNATYVNVKCVAPYPSLLSSQDNIDGEGDT
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Receptor tyrosine kinase that transduces signals from the extracellular matrix into the cytoplasm by binding to hepatocyte growth factor/HGF ligand. Regulates many physiological processes including proliferation, scattering, morphogenesis and survival. Ligand binding at the cell surface induces autophosphorylation of MET on its intracellular domain that provides docking sites for downstream signaling molecules. Following activation by ligand, interacts with the PI3-kinase subunit PIK3R1, PLCG1, SRC, GRB2, STAT3 or the adapter GAB1. Recruitment of these downstream effectors by MET leads to the activation of several signaling cascades including the RAS-ERK, PI3 kinase-AKT, or PLCgamma-PKC. The RAS-ERK activation is associated with the morphogenetic effects while PI3K/AKT coordinates prosurvival effects. During embryonic development, MET signaling plays a role in gastrulation, development and migration of muscles and neuronal precursors, angiogenesis and kidney formation. In adults, participates in wound healing as well as organ regeneration and tissue remodeling. Promotes also differentiation and proliferation of hematopoietic cells (By similarity).
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A0M8T2
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WNT2_FELCA
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Protein Wnt-2
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MNAPLGGIWPWLPLLLTWLTPEVSSSWWYMRATGGSSRVMCDNVPGLVSRQRQLCHRHPDVMRAIGLGVAEWTAECQHQFRQHRWNCNTLDRDHSLFGRVLLRSSRESAFVYAVSSAGVVFAITRACSQGELKSCSCDPKKKGTAKDSKGNFDWGGCSDNIDYGIKFARAFVDAKERKGKDARALMNLHNNRAGRKAVKRFLKQECKCHGVSGSCTLRTCWLAMADFRKTGDYLWRKYNGAIQVVMNQDGTGFTVANKRFKKPTKNDLVYFENSPDYCIRDRDAGSLGTAGRVCNLTSRGMDSCEVMCCGRGYDTSHVTRMTKCECKFHWCCAVRCQDCLEALDVHTCKAPKSVDWAAPT
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Ligand for members of the frizzled family of seven transmembrane receptors. Functions in the canonical Wnt signaling pathway that results in activation of transcription factors of the TCF/LEF family (By similarity). Functions as upstream regulator of FGF10 expression. Plays an important role in embryonic lung development. May contribute to embryonic brain development by regulating the proliferation of dopaminergic precursors and neurons (By similarity).
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A0MD28
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RPOA_PRRSS
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Replicase polyprotein 1ab (ORF1ab polyprotein) [Cleaved into: Nsp1 (EC 3.4.22.-); Nsp1-alpha papain-like cysteine proteinase (EC 3.4.22.-) (PCP1-alpha); Nsp1-beta papain-like cysteine proteinase (EC 3.4.22.-) (PCP1-beta); Nsp2 cysteine proteinase (EC 3.4.19.12) (EC 3.4.22.-) (CP2) (CP); Non-structural protein 3 (Nsp3); Serine protease nsp4 (3CLSP) (EC 3.4.21.-) (3C-like serine proteinase) (Nsp4); Non-structural protein 5-6-7 (Nsp5-6-7); Non-structural protein 5 (Nsp5); Non-structural protein 6 (Nsp6); Non-structural protein 7-alpha (Nsp7-alpha); Non-structural protein 7-beta (Nsp7-beta); Non-structural protein 8 (Nsp8); RNA-directed RNA polymerase (Pol) (RdRp) (EC 2.7.7.48) (Nsp9); Helicase nsp10 (Hel) (EC 3.6.4.12) (EC 3.6.4.13) (Nsp10); Uridylate-specific endoribonuclease nsp11 (EC 4.6.1.-) (Non-structural protein 11) (Nsp11); Non-structural protein 12 (Nsp12)]
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MSGTFSRCMCTPAARVFWNAGQVFCTRCLSARPLLSPELQDTDLGVVGLFYKPKDKIHWKVPIGIPQVECTPSGCCWLSAVFPLARMTSGNHNFLQRLVKVADVLYRDGCLAPRHLRELQVYERGCSWYPITGPVPGMGLFANSMHVSDQPFPGATHVLTNSPLPQRACRQPFCPFEEAHSDVYRWKKFVIFTDSSPNGRFRMMWTPESDDSAALEVLPPELERQVEILTRSFPAHHPINLADWELTESPENGFSFGTSHSCGHIVQNPNVFDGKCWLTCFLGQSAEVCYHEEHLANALGYQTKWGVHGKYLQRRLQVRGMRAVVDPDGPIHVEALSCSQSWVRHLTLNNDVTPGFVRLTSIRIVSNTEPTAFRIFRFGAHKWYGAAGKRARAKRATKSGKDSALAPKIAPPVPTCGITTYSPPTDGSCGWHVLAAIVNRMINGDFTSPLPQYNRPEDDWASDYDLAQAIQCLQLPATVVRNRACPNAKYLIKLNGVHWEVEVRSGMAPRSLSRECVVGVCSEGCVAPPYPADGLPKRALEALASAYRLPSDCVSSGIADFLADPPPQEFWTLDKMLTSPSPERSGFSSLYKLLLEVVPQKCGATEGAFVYAVERMLKDCPSPEQAMALLAKIKVPSSKAPSVSLDECFPAGVPADFEPAFQERPRSPGAAVALCSPDAKGFEGTASEEAQESGHKAVHAVPLAEGPNNEQVQVVAGEQLELGGCGLAIGSAQSSSDSKRENMHNSREDEPLDLSHPAPAATTTLVGEQTPDNPGSDASALPIAVRGFVPTGPILRHVEHCGTESGDSSSPLDLSFAQTLDQPLDLSLAAWPVKATASDPGWVRGRCEPVFLKPRKAFSDGDSALQFGELSESSSVIEFDQTKDTLVADAPVDLTTSNEALSAVDPSEFVELRRPRHSAQALIDRGGPLADVHAKIKNRVYEQCLQACEPGSRATPATREWLDKMWDRVDMKTWRCTSQFQAGRILASLKFLPDMIQDTPPPVPRKNRASDNAGLKQLVARWDKKLSVTPPPKSAGLVLDQTVPPPTDIQQEDATPSDGLSHASDFSSRVSTSWSWKGLMLSGTRLAGSAGQRLMTWVFEVYSHLPAFILTLFSPRGSMAPGDWLFAGVVLLALLLCRSYPILGCLPLLGVFSGSLRRVRLGVFGSWMAFAVFLFSTPSNPVGSSCDHDSPECHAELLALEQRQLWEPVRGLVVGPSGLLCVILGKLLGGSRHLWHVILRLCMLTDLALSLVYVVSQGRCHKCWGKCIRTAPAEVALNVFPFSRATRNSLTSLCDRFQTPKGVDPVHLATGWRGCWRGESPIHQPHQKPIAYANLDEKKISAQTVVAVPYDPSQAIKCLKVLQAGGAIVDQPTPEVVRVSEIPFSAPFFPKVPVNPDCRIVVDSDTFVAAVRCGYSTAQLVLGRGNFAKLNQTPLRDSASTKTTGGASYTLAVAQVSVWTLVHFILGLWFTSPQVCGRGTADPWCSNPFSYPAYGPGVVCSSRLCVSADGVTLPLFSAVAQLSGREVGIFILVLVSLTALAHRLALKADMLVVFSAFCAYAWPMSSWLICFFPILLKWVTLHPLTMLWVHSFLVFCMPAAGILSLGITGLLWAVGRFTQVAGIITPYDIHQYTSGPRGAAAVATAPEGTYMAAVRRAALTGRTLIFTPSAVGSLLEGAFRTHKPCLNTVNVVGSSLGSGGVFTIDGRKTVVTAAHVLNGDTARVTGDSYNRMHTFKTSGDYAWSHADDWQGVAPVVKVAKGYRGRAYWQTSTGVEPGVIGEGFAFCFTNCGDSGSPVISESGDLIGIHTGSNKLGSGLVTTPEGETCAIKETKLSDLSRHFAGPSVPLGDIKLSPAIVPDVTSIPSDLASLLASVPVMEGGLSTVQLLCVFFLLWRMMGHAWTPIVAVGFFLLNEILPAVLVRAVFSFALFILAWATPWSAQVLMIRLLTASLNRNKLSLAFYALGGVVGLAAEIGAFAGRLPELSQALSTYCFLPRVLAMASYVPIIIIGGLHALGVILWLFKYRCLHNMLVGDGSFSSAFFLRYFAEGNLRKGVSQSCGMSNESLTAALACKLSQADLDFLSSLTNFKCFVSASNMKNAAGQYIEAAYAKALRQELASLVQVDKMKGILSKLEAFAETATPSLDAGDVVVLLGQHPHGSILDINVGTERKTVSVQETRSLGGSKFSVCTVVSNTPVDALTGIPLQTPTPLFENGPRHRGEEDDLRVERMKKHCVSLGFHNINGKVYCKIWDKSTGDTFYTDDSRYTQDLAFQDRSADYRDRDYEGVQTAPQQGFDPKSETPIGTVVIGGITYNRYLIKGKEVLVPKPDNCLEAAKLSLEQALAGMGQTCDLTAAEVEKLRRIISQLQGLTTEQALNCLLAASGLTRCGRGGLVVTETAVKIVKYHSRTFTLGPLDLKVTSEAEVKKSTEQGHAVVANLCSGVILMRPHPPSLVDVLLKPGLDTKPGIQPGHGAGNMGVDGSTWDFETAPTKAELELSKQIIQACEVRRGDAPNLQLPYKLYPVRGDPERHGGRLINTRFGDLSYKTPQDTKSAIHAACCLHPNGAPVSDGKSTLGTTLQHGFELYVPTVPYSVMEYLDSRPDTPFMCTKHGTSKAAAEDLQKYDLSTQGFVLPGVLRLVRRFIFGHIGKAPPLFLPSTYPAKNSMAGINGQRFPTKDVQSIPEIDEMCARAVKENWQTVTPCTLKKQYCSKPKTRTILGTNNFIALAHRSALSGVTQAFMKKAWKSPIALGKNKFKELHCTVAGRCLEADLASCDRSTPAIVRWFVANLLYELAGCEEYLPSYVLNCCHDLVATQDGAFTKRGGLSSGDPVTSVSNTVYSLIIYAQHMVLSALKMGHEIGLKFLEEQLKFEDLLEIQPMLVYSDDLVLYAERPTFPNYHWWVEHLDLMLGFRTDPKKTVITDKPSFLGCRIEAGRQLVPNRDRILAALAYHMKAQNASEYYASAAAILMDSCACIDHDPEWYEDLICGIARCARQDGYSFPGPAFFMSMWEKLRSHNEGKKFRHCGICDAKADHASACGLDLCLFHSHFHQHCPVTLSCGHHAGSRECSQCQSPVGAGRSPLDAVLKQIPYKPPRTVIMKVGNKTTALDPGRYQSRRGLVAVKRGIAGNEVDLPDGDYQVVPLLPTCKDINMVKVACNVLLSKFIVGPPGSGKTTWLLSQVQDDDVIYTPTHQTMFDIVSALKVCRYSIPGASGLPFPPPARSGPWVRLVASGHVPGRTSYLDEAGYCNHLDILRLLSKTPLVCLGDLQQLHPVGFDSYCYVFDQMPQKQLTTIYRFGPNICAAIQPCYREKLESKARNTRVVFTTWPVAFGQVLTPYHKDRIGSAITIDSSQGATFDIVTLHLPSPKSLNKSRALVAITRARHGLFIYDPHNQLQEFFNLIPERTDCNLVFSRGDDLVVLSADNAVTTVAKALGTGPSRFRVSDPRCKSLLAACSASLEGSCMPLPQVAHNLGFYFSPDSPAFAPLPKELAPHWPVVTHQNNRAWPDRLVASMRPIDARYSKPMVGAGYVVGPSTFLGTPGVVSYYLTLYIRGEPQALPETLVSTGRIATDCREYLDAAEEEAAKELPHAFIGDVKGTTVGGCHHITSKYLPRTLPKDSVAVVGVSSPGRAAKAMCTLTDVYLPELRPYLQPETASKCWKLKLDFRDVRLMVWKGATAYFQLEGLTWSALPDYARFIQLPKDAVVYIDPCIGPATANRKVVRTTDWRADLAVTPYDYGAQNILTTAWFEDLGPQWKILGLQPFRRAFGFENTEDWAILARRMSDGKDYTDYNWDCVRERPHAIYGRARDHTYHFAPGTELQVELGKPRLPPGREP
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[Replicase polyprotein 1ab]: Contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products. [Nsp1-beta papain-like cysteine proteinase]: Plays a role in blocking host mRNA nuclear export to the cytoplasm and subversion of host protein synthesis. Additionally, inhibits the interferon-activated JAK/STAT signal transduction by mediating the ubiquitination and subsequent proteasomal degradation of host KPNA1. [Nsp2 cysteine proteinase]: Multifunctional protein that acts as a viral protease and as a viral antagonist of host immune response. Cleaves the nsp2/nsp3 site in the viral polyprotein. Displays deubiquitinating activity that cleaves both ubiquitinated and ISGylated products and therefore inhibits ubiquitin and ISG15-dependent host innate immunity. Deubiquitinates also host NFKBIA, thereby interfering with NFKBIA degradation and impairing subsequent NF-kappa-B activation. [Serine protease nsp4]: Cleaves the majority of cleavage sites present in the C-terminus of the polyprotein. Triggers host apoptosis through caspase-3, -8, and -9 activations. Subverts host innate immune responses through its protease activity. Targets the NF-kappa-B essential modulator NEMO and mediates its cleavage. Blocks host interferon beta induction and downstream signaling by cleaving mitochondrial MAVS, dislodging it from the mitochondria. Impairs host defense by cleaving host mRNA-decapping enzyme DCP1A to attenuate its antiviral activity. [Uridylate-specific endoribonuclease nsp11]: Plays a role in viral transcription/replication and prevents the simultaneous activation of host cell dsRNA sensors, such as MDA5/IFIH1, OAS, and PKR (By similarity). Acts by degrading the 5'-polyuridines generated during replication of the poly(A) region of viral genomic and subgenomic RNAs. Catalyzes a two-step reaction in which a 2'3'-cyclic phosphate (2'3'-cP) is first generated by 2'-O transesterification, which is then hydrolyzed to a 3'-phosphate (3'-P) (By similarity). If not degraded, poly(U) RNA would hybridize with poly(A) RNA tails and activate host dsRNA sensors (By similarity).
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A0MES8
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ABI4_ARATH
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Ethylene-responsive transcription factor ABI4 (ERF ABI4) (Protein ABSCISIC ACID INSENSITIVE 4) (Protein GLUCOSE INSENSITIVE 6) (Protein IMPAIRED SUCROSE INDUCTION 3) (Protein SALOBRENO 5) (Protein SUCROSE UNCOUPLED 6) (Protein SUGAR INSENSITIVE 5)
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MDPLASQHQHNHLEDNNQTLTHNNPQSDSTTDSSTSSAQRKRKGKGGPDNSKFRYRGVRQRSWGKWVAEIREPRKRTRKWLGTFATAEDAARAYDRAAVYLYGSRAQLNLTPSSPSSVSSSSSSVSAASSPSTSSSSTQTLRPLLPRPAAATVGGGANFGPYGIPFNNNIFLNGGTSMLCPSYGFFPQQQQQQNQMVQMGQFQHQQYQNLHSNTNNNKISDIELTDVPVTNSTSFHHEVALGQEQGGSGCNNNSSMEDLNSLAGSVGSSLSITHPPPLVDPVCSMGLDPGYMVGDGSSTIWPFGGEEEYSHNWGSIWDFIDPILGEFY
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Transcription regulator that probably binds to the GCC-box pathogenesis-related promoter element. Binds also to the S-box (5'-CACTTCCA-3') photosynthesis-associated nuclear genes-related (PhANGs-related) promoter element, and thus acts as a transcription inhibitor. Involved in the regulation of gene expression by stress factors and by components of stress signal transduction pathways. May have a function in the deetiolation process. Confers sensitivity to abscisic acid (ABA), and regulates the ABA signaling pathway during seed germination, upon nitrate-mediated lateral root inhibition, in hexokinase-dependent sugar responses (including feed-back regulation of photosynthesis and mobilization of storage lipid during germination), and in response to osmotic stress mediated by NaCl, KCl or mannitol. Plays a role in sucrose sensing or signaling, especially at low fluence far red light. Also involved in plant response to glucose treatment, especially at low concentration and in young seedlings. Required for the trehalose-mediated root inhibition and starch accumulation in cotyledons, probably by inhibiting starch breakdown. However, seems to not be involved in sugar-mediated senescence. Required for the ABA-dependent beta-amino-butyric acid (BABA) signaling pathway. BABA primes ABA synthesis and promotes resistance to drought and salt, and leads to a prime callose accumulation that confers resistance against necrotrophic pathogens such as A.brassicicola and P.cucumerina. Seems to be involved in resistance to S.sclerotiorum probably by regulating the ABA-mediated stomatal closure apparently by antagonistic interaction with oxalate. Negative regulator of low water potential-induced Pro accumulation whose effect is decreased by high levels of sugar.
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A0MGZ7
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H6S3B_DANRE
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Heparan-sulfate 6-O-sulfotransferase 3-B (HS 6-OST-3-B) (EC 2.8.2.-)
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MNDKPNKWIFIPILAILFVMIGYQYVCPAGGQACHFRTGDKLVRIAPLATPDPTTDDLYREQDPEEDNPPKCASKFNFTERDLTRDVDFNIKGDDVIVFLHIQKTGGTTFGRHLVRNIRLEQPCDCKAGQKKCTCHRPGKQESWLFSRFSTGWSCGLHADWTELTNCVPVIMDKRQPPKRKRNFYYITMLRDPVSRYLSEWKHVQRGATWKTSLHMCDGRSPTQDELPTCYNGDDWSGVTLHDFMDCPSNLANNRQVRMLADLSLVGCYNLSTMNESERNPILLASAKSNLKNMAFYGLTEFQRKTQYLFERTFHLRFISAFTQINSTRAANVELRDDMRSRIEQLNMLDMQLYEFAKDLFLQRYQFVRQRERQEERLKRREERRWIRERRVNQSKEPIVENQTRVTTTEDYASQVVRW
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6-O-sulfation enzyme which catalyzes the transfer of sulfate from 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to position 6 of the N-sulfoglucosamine residue (GlcNS) of heparan sulfate.
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A0MLS4
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GHRL_PAPHA
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Appetite-regulating hormone (Growth hormone secretagogue) (Growth hormone-releasing peptide) (Motilin-related peptide) [Cleaved into: Ghrelin; Obestatin]
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MPSPGTVCSLLLLGMLWLDLAMAGSSFLSPEHQRAQQRKESKKPPAKLQPRALGGWLRPEDGDQAEGAEDELEIQFNAPFDVGIKLSGVQYQQHSQALGKFLQDILWEEAKEAPADK
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[Ghrelin]: Ghrelin is the ligand for growth hormone secretagogue receptor type 1 (GHSR). Induces the release of growth hormone from the pituitary. Has an appetite-stimulating effect, induces adiposity and stimulates gastric acid secretion. Involved in growth regulation (By similarity). [Obestatin]: Obestatin may be the ligand for GPR39. May have an appetite-reducing effect resulting in decreased food intake. May reduce gastric emptying activity and jejunal motility (By similarity).
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A0MLS5
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BMAL1_HORSE
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Basic helix-loop-helix ARNT-like protein 1 (Aryl hydrocarbon receptor nuclear translocator-like protein 1) (Brain and muscle ARNT-like 1)
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MADQRMDISSTISDFMSPGATDLLSSPLGTSGMDCNRKRKGSSTDYQESMDTDKDDPHGRLEYTEHQGRIKNAREAHSQIEKRRRDKMNSFIDELASLVPTCNAMSRKLDKLTVLRMAVQHMKTLRGATNPYTEANYKPTFLSDDELKHLILRAADGFLFVVGCDRGKILFVSESVFKILNYSQNDLIGQSLFDYLHPKDIAKVKEQLSSSDTAPRERLIDAKTGLPVKTDITPGPSRLCSGARRSFFCRMKCNRPSVKVEDKDFPSTCSKKKADRKSFCTIHSTGYLKSWPPTKMGLDEDNEPDNEGCNLSCLVAIGRLHSHVVPQPVNGEIRVKSMEYVSRHAIDGKFVFVDQRATAILAYLPQELLGTSCYEYFHQDDIGHLAECHRQVLQTREKITTNCYKFKIKDGSFITLRSRWFSFMNPWTKEVEYIVSTNTVVLANVLEGGDPTFPQLTASPHSMDSMLPSGEGGPKRTHPTVPGIPGGTRAGAGKIGRMIAEEVMEIHRIRGSSPSSCGSSPLNITSTPPPDASSPGGKKILNGGTPDIPSSGLPPGQAQENPGYPYSDSSSILGENPHIGIDMIDNDQGSSSPSNDEAAMAVIMSLLEADAGLGGPVDFSDLPWPL
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Transcriptional activator which forms a core component of the circadian clock. The circadian clock, an internal time-keeping system, regulates various physiological processes through the generation of approximately 24 hour circadian rhythms in gene expression, which are translated into rhythms in metabolism and behavior. It is derived from the Latin roots 'circa' (about) and 'diem' (day) and acts as an important regulator of a wide array of physiological functions including metabolism, sleep, body temperature, blood pressure, endocrine, immune, cardiovascular, and renal function. Consists of two major components: the central clock, residing in the suprachiasmatic nucleus (SCN) of the brain, and the peripheral clocks that are present in nearly every tissue and organ system. Both the central and peripheral clocks can be reset by environmental cues, also known as Zeitgebers (German for 'timegivers'). The predominant Zeitgeber for the central clock is light, which is sensed by retina and signals directly to the SCN. The central clock entrains the peripheral clocks through neuronal and hormonal signals, body temperature and feeding-related cues, aligning all clocks with the external light/dark cycle. Circadian rhythms allow an organism to achieve temporal homeostasis with its environment at the molecular level by regulating gene expression to create a peak of protein expression once every 24 hours to control when a particular physiological process is most active with respect to the solar day. Transcription and translation of core clock components (CLOCK, NPAS2, BMAL1, BMAL2, PER1, PER2, PER3, CRY1 and CRY2) plays a critical role in rhythm generation, whereas delays imposed by post-translational modifications (PTMs) are important for determining the period (tau) of the rhythms (tau refers to the period of a rhythm and is the length, in time, of one complete cycle). A diurnal rhythm is synchronized with the day/night cycle, while the ultradian and infradian rhythms have a period shorter and longer than 24 hours, respectively. Disruptions in the circadian rhythms contribute to the pathology of cardiovascular diseases, cancer, metabolic syndromes and aging. A transcription/translation feedback loop (TTFL) forms the core of the molecular circadian clock mechanism. Transcription factors, CLOCK or NPAS2 and BMAL1 or BMAL2, form the positive limb of the feedback loop, act in the form of a heterodimer and activate the transcription of core clock genes and clock-controlled genes (involved in key metabolic processes), harboring E-box elements (5'-CACGTG-3') within their promoters. The core clock genes: PER1/2/3 and CRY1/2 which are transcriptional repressors form the negative limb of the feedback loop and interact with the CLOCK|NPAS2-BMAL1|BMAL2 heterodimer inhibiting its activity and thereby negatively regulating their own expression. This heterodimer also activates nuclear receptors NR1D1, NR1D2, RORA, RORB and RORG, which form a second feedback loop and which activate and repress BMAL1 transcription, respectively. BMAL1 positively regulates myogenesis and negatively regulates adipogenesis via the transcriptional control of the genes of the canonical Wnt signaling pathway. Plays a role in normal pancreatic beta-cell function regulates glucose-stimulated insulin secretion via the regulation of antioxidant genes NFE2L2/NRF2 and its targets SESN2, PRDX3, CCLC and CCLM. Negatively regulates the mTORC1 signaling pathway regulates the expression of MTOR and DEPTOR. Controls diurnal oscillations of Ly6C inflammatory monocytes rhythmic recruitment of the PRC2 complex imparts diurnal variation to chemokine expression that is necessary to sustain Ly6C monocyte rhythms. Regulates the expression of HSD3B2, STAR, PTGS2, CYP11A1, CYP19A1 and LHCGR in the ovary and also the genes involved in hair growth. Plays an important role in adult hippocampal neurogenesis by regulating the timely entry of neural stem/progenitor cells (NSPCs) into the cell cycle and the number of cell divisions that take place prior to cell-cycle exit. Regulates the circadian expression of CIART. The CLOCK-BMAL1 heterodimer regulates the circadian expression of SERPINE1/PAI1, VWF, B3, CCRN4L/NOC, NAMPT, DBP, MYOD1, PPARGC1A, PPARGC1B, SIRT1, GYS2, F7, NGFR, GNRHR, BHLHE40/DEC1, ATF4, MTA1 and also genes implicated in glucose and lipid metabolism. Promotes rhythmic chromatin opening, regulating the DNA accessibility of other transcription factors. The NPAS2-BMAL1 heterodimer positively regulates the expression of MAOA, F7 and LDHA and modulates the circadian rhythm of daytime contrast sensitivity by regulating the rhythmic expression of adenylate cyclase type 1 (ADCY1) in the retina. The preferred binding motif for the CLOCK-BMAL1 heterodimer is 5'-CACGTGA-3', which contains a flanking adenine nucleotide at the 3-prime end of the canonical 6-nucleotide E-box sequence. CLOCK specifically binds to the half-site 5'-CAC-3', while BMAL1 binds to the half-site 5'-GTGA-3'. The CLOCK-BMAL1 heterodimer also recognizes the non-canonical E-box motifs 5'-AACGTGA-3' and 5'-CATGTGA-3'. Essential for the rhythmic interaction of CLOCK with ASS1 and plays a critical role in positively regulating CLOCK-mediated acetylation of ASS1. Plays a role in protecting against lethal sepsis by limiting the expression of immune checkpoint protein CD274 in macrophages in a PKM2-dependent manner (By similarity). Regulates the diurnal rhythms of skeletal muscle metabolism via transcriptional activation of genes promoting triglyceride synthesis (DGAT2) and metabolic efficiency (COQ10B) (By similarity).
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A0MQA3
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ASP5_TOXGO
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Aspartic protease 5 (EC 3.4.23.-)
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MEAGAMGGSSFLSFSSGPSAETSPSSLSPPTSSSPSPSPQLVSDSVESLHAKRPLAQSSRSSSRTAASTCFCWQGEGQENEAAPTISQEERRGGSMTAASAGHLETAREEAARCLGCSYTGEERRGASSATSVLSLGGERGRPPSRSSSLWTFSGLLSPLAFRSRRCCPQFSSSSSPLSPLPHPRGAPASACGSAVITDRAGRPASPLSFSRLASPVSDPSGVCPPRVVAARVWRLLSSVLFSLVNCARLFPRRLSRRPDPLRKPRAQVWSASSRSLQALLLATVALFAACSSLHGSSLLGAQAASPTPPFLSLSSSPRSLASDSAKKGSNAPEQSREQRGEREGERQRPDKGEENGETEETFPAASGVVPAPGLKVADLPRTGPPVDLLGLPIRKKVFRARLYGSMFSYAYYFLDILVGTPPQRASVILDTGSSLLAFPCAGCSECGQHLDPAMDTSRSATGEWIDCKEQERCFGSCSGGTPLGGLGGGGVSSMRRCMYTQTYSEGSAIRGIYFSDVVALGEVEQKNPPVRYDFVGCHTQETNLFVTQKAAGIFGISFPKGHRQPTLLDVMFGHTNLVDKKMFSVCISEDGGLLTVGGYEPTLLVAPPESESTPATEALRPVAGESASRRISEKTSPHHAALLTWTSIISHSTYRVPLSGMEVEGLVLGSGVDDFGNTMVDSGTDLSSIFPPIKVSFGDEKNSQVWWWPEGYLYRRTGGYFCDGLDDNKVSASVLGLSFFKNKQVLFDREQDRVGFAAAKCPSFFLDQRPRGPDSGDGPKGRPTAPFTVPPLRVPVPMDGGGVPGDAKQPEGLPLSPQQLWVAAALVVVAILIAVTVILLHTIKRPSRSSAVVPAPSAPRLPFAQNSKSAGRFARGLGHGALGVGNPVYVQRTQRYREVQEAQPHTADAYYDVEEDRFTGEDDGDFFGDDSVPSAEEQETAPSLSLREESSPFSASQSTLLDLPLGGE
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In tachyzoites, plays an essential role in the export of several dense granule proteins into the host cell by cleaving the localization motif RRLxx (termed Toxoplasma export element (TEXEL)) located downstream of the N-terminal secretory signal sequence. However, can also regulate the export of proteins that lack the TEXEL motif, such as GRA24. Requires Arg at P3 and P2, and Leu at P1 in the substrate TEXEL motif and, specifically, cleaves after Leu. Cleaves GRA16 proteolytic cleavage is essential for the correct trafficking of GRA16 from the parasite into the infected host nucleus. Cleaves GRA19 and GRA20. Cleaves MYR1. Cleaves LCAT, GRA44, GRA46, GRA46, ROP35/WNG1 and ROP34/WNG2. By regulating the export of dense granule proteins into the host cell, regulates multiple processes during tachyzoite infection of host cells, including recruitment of host mitochondria to the parasitophorous vacuole (PV), formation of the nanotubular network (NTN) or intravacuolar network (IVN) which are membranous tubules that bud from the PV membrane into the vacuolar lumen and, up-regulation of host cell genes to facilitate the parasite infection and modulate the host innate immune response. At the bradyzoite stage, also involved in the formation of the cyst wall.
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A0MQH0
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DICER_CRIGR
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Endoribonuclease Dicer (EC 3.1.26.3)
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MKSPALQPLSMAGLQLMTPASSPMGPFFGLPWQQEAIHDNIYTPRKYQVELLEAALDHNTIVCLNTGSGKTFIAVLLTKELAHQIRGDLNPRAKRTVFLVNSANQVAQQVSAVRTHSDLKVGEYSNLEVNASWTKERWSQEFTKHQVLIMTCYVALNVLKNGYLSLSDINLLVFDECHLAILDHPYREIMKLCESCPSCPRILGLTASILNGKCDPEELEEKIQKLEKILKSNAETATDLVVLDRYASQPCEIVVDCGPFTDRSGLYERLLMELEEAINFINDCNVSVHSKERDSTLISKQILSDCRAVLVVLGPWCADKVAGMMVRELQKYIKHEQEELHRKFLLFTDTLLRKIHALCEEHFSPASLDLKYVTPKVMKLLEILRKYKPYERQQFESVEWYNNRNQDNYVSWSDSEDDDDDEEIEEKEKPETNFPSPFTNILCGIIFVERRYTAVVLNRLIKEAGKQDPELAYISSNFITGHGIGKNQPRSKQMEAEFRKQEEVLRKFRAHETNLLIATSVVEEGVDIPKCNLVVRFDLPTEYRSYVQSKGRARAPISNYVMLADTDKIQSFEEDLKTYKAIEKILRNKCSKSVDGAEADVDAVVDDDDVFPPYVLRPDDGGPRVTINTAIGHVNRYCARLPSDPFTHLAPKCRTQELPDGTFYSTLYLPINSPLRASIVGPPMGCVRLAERVVALICCEKLHKIGELDEHLMPVGKETVKYEEELDLHDEEETSVPGRPGSTKRRQCYPKAIPECLRESYPKPDQPCYLYVIGMVLTTPLPDELNFRRRKLYPPEDTTRCFGILTAKPIPQIPHFPVYTRSGEVTISIELKKSGFTLSQQMLELITRLHQYIFSHILRLEKPALEFKPTGAESAYCVLPLNVVNDSSTLDIDFTFMEDIEKSEARIGIPSTKYSKETPFVFKLEDYQDAVIIPRYRNFDQPHRFYVADVYTDLTPLSKFPSPEYETFAEYYKTKYNLDLTNLNQPLLDVDHTSSRLNLLTPRHLNQKGKALPLSSAEKRKAKWESLQNKQILVPELCAIHPIPASLWRKAVCLPSILYRLHCLLTAEELRAQTASDAGVGVRSLPADFRYPNLDFGWKKSIDSKSFISTCNSSLAENDNYCKHSTIIVPENAAHQGATRTPLENHDQMSVNCRRLPAESSGKLQIEVSTDLTAINGLSYNKNLANGSYDLVNRDFCQGNQLNYFKQEIPVQPTTSYPIQNLYHYENQPKPSNECTLLSNKYLDGNANTSTSDGSPAVSTMPAVMSAGRALKDRMDSEQSPSAGYSSRTLGPNPGLILQALTLSNASDGFNLERLEMLGDSFLKHAITTYLFCTYPDAHEGRLSYMRSKKVSNCNLYRLGKKKGLPSRMVVSIFDPPVNWLPPGYVVNQDKSNAEKWEKDEMTKDCLLANGKLGKDCEEEEALTWRAPKEEAEYEDDFLEYDQEHIQFIDSMLMGSGAFVKKISLSPFSTSDSAYEWKMPKKSSLGSMPFSSDLEDFDYSSWDAMCYLDPSKAVEEDDFVVGFWNPSEENCGVDTGKQSISYDLHTEQCIADKSIADCVEALLGCYLTSCGERAAQLFLCSLGLKVLPVIKRTSREKALYPAQENFSSQQKSLSGSCAATAASPRSSAGKDLEYGCLKIPPRCMFDHPDAEKTLNHLISGFENFEKKINYRFKNKAYLLQAFTHASYHYNTITDCYQRLEFLGDAILDYLITKHLYEDPRQHSPGVLTDLRSALVNNTIFASLAVKYDYHKYFKAVSPELFHVIDDFVQFQLEKNEMQGMDSELRRSEEDEEKEEDIEVPKAMGDIFESLAGAIYMDSGMSLEVVWQVYYPMMRPLIEKFSANVPRSPVRELLEMEPETAKFSPAERTYDGKVRVTVEVVGKGKFKGVGRSYRIAKSAAARRALRSLKANQPQVPNS
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Double-stranded RNA (dsRNA) endoribonuclease playing a central role in short dsRNA-mediated post-transcriptional gene silencing. Cleaves naturally occurring long dsRNAs and short hairpin pre-microRNAs (miRNA) into fragments of twenty-one to twenty-three nucleotides with 3' overhang of two nucleotides, producing respectively short interfering RNAs (siRNA) and mature microRNAs. SiRNAs and miRNAs serve as guide to direct the RNA-induced silencing complex (RISC) to complementary RNAs to degrade them or prevent their translation. Gene silencing mediated by siRNAs, also called RNA interference, controls the elimination of transcripts from mobile and repetitive DNA elements of the genome but also the degradation of exogenous RNA of viral origin for instance. The miRNA pathway on the other side is a mean to specifically regulate the expression of target genes (By similarity).
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A0MSJ1
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CRA1B_DANRE
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Collagen alpha-1(XXVII) chain B
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MEPDNTPSSRLRAAGVGGRAVFFCMVLYCTCCLRLAQAQSADVDVLQRLGLVGKRPPQGFIPIKSGVILTTRARIDVPVSSVIPVSLGSTFSIILSVCSHRINNAFLFTIVTKRKRLHLGVQFIPGQILVYLGQNSSVNFDYNVHNGQWHNLALEIQGQKVTLYTSCGNTSIQANLDFQNEETLDSEGSFRLGKMSQNSVQFEGAICQFDIHPSAQAAHNYCKYIKKQCREADTYRPNLPPLLPLLPLDPNRSTIQTPKVVTDINERHLSLTRDKMNINHEGQTTVPPMITQPTLQLPLQTTAQTTASIRNRTSQISPKPTQQNRKKAKKERNKLHILKEHQISVTDSPTSQQQNQVDIPTTTTPELSSTFRVSEMTTLAAQRPLPKETSFFEAKATFFESVTPAAMDGLQTFDLEPTQYSLLELTGLKGEPGLPGPPGPPGQPGLPGKRGPRGPSGPHGKPGPPGTPGPKGKKGNPGISPGRAPSGIKGDPGLVGLPGQPGQPGRKGQKGHPGPSGHPGDQGIRGPDGSPGAKGYPGRQGLPGPIGNMGPKGVRGFIGIPGIFGLPGADGERGLPGVPGKKGKMGRPGFPGDFGERGPPGPDGNPGEIGAPGPVGIPGFIGDMGPVGMVGPPGLIGPKGVPGNPGEPGLKGDKGELGLPGEPGEPGFQGDKGIQGSPGLPGVQGKPGPQGKIGDRGPDGLPGPLGPEGFPGDIGPPGQNGVEGPKGNAGVRGIPGPGGLPGLEGDQGPVGPAGAPGLEGRPGRKGISGNPGEEGMKGEPGMTGNPGMLGERGPVGFVGPFGEMGLAGEKGDRGETGQPGPPGEKGAMGHPGAPGERGLSGPAGAPGPHGSRGLSGTRGPKGTRGARGPDGPVGEKGMMGMKGPEGPPGKQGLSGQMGKIGETGEAGPTGFTGVQGPTGPPGAKGILGEPGPQGSPGVLGPLGEIGAIGLPGKAGDQGLPGEPGEKGAVGSPGNIGEQGLIGPRGDPGVDGEAGPSGPDGAKGEQGDVGLEGESGEKGVIGFKGTEGRTGDPGLIGVKGPEGKPGKIGERGKPGEKGSKGHQGQLGEMGALGEQGDTGFIGPKGSRGTTGFMGAPGKMGQQGEPGLVGYEGHQGPQGSLGSPGPKGEKGEQGDDGKVEGPPGPSGDIGPVGNRGDRGEPGDPGYPGLEGVQGERGKEGAPGVPGNSGPRGFPGPKGSKGNKGPKGKNSPRGESGNRGSPGPVGVPGPRGVIGREGFEGEPGLDGAAGKDGAKGMPGDLGRDGDVGLPGKPGPQGNAGAPGLPGVQGSFGPKGERGITGHSGPPGKRGLNGGMGFPGKQGDQGFKGQPGDAGEQGFPGVLGIFGPQGPPGDFGPVGIQGPKGPQGLMGMQGAIGPVGIIGPSGNPGPQGDKGNKGEMGVQGPRGPPGPRGPPGPPGLPAVAFSHENEALGAALHVFDSRSALRSEMYQDTDLPLLDQGSEIFKTLHYLSILIHSIKNPLGTQENPARMCRDLLECEHRLNDGTYWIDPNLGCSSDNIEVTCSFTSGGQTCLKPVTASKLEIGVSLIQMNFIHLLSSEAVQIITVHCLNVSVWASEDSKTPSSSMVYFKAWDGQIIEAGGFIEPDLLKDECWITDGRWHQTQFIFRTQDPNLLPIVEIYNLPSTKPGSHYHLEVGPVCFL
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May play a role during the calcification of cartilage and the transition of cartilage to bone (By similarity). Together with col27a1a, plays a role in development of the notochord and axial skeleton. {ECO:0000250, ECO:0000269|PubMed:20041163}.
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A0MTA1
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APEX1_DANRE
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DNA-(apurinic or apyrimidinic site) endonuclease (EC 3.1.11.2) (APEX nuclease) (APEN) (Apurinic-apyrimidinic endonuclease 1) (AP endonuclease 1) (zAP1)
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MPKRAKKNEEGVDGEADNGTAAAKKEKKGKEPEAPILYEDPPEKLTSKDGRAANMKITSWNVDGLRAWVKKNGLDWVRKEDPDILCLQETKCAEKALPADITGMPEYPHKYWAGSEDKEGYSGVAMLCKTEPLNVTYGIGKEEHDKEGRVITAEFPDFFLVTAYVPNASRGLVRLDYRKTWDVDFRAYLCGLDARKPLVLCGDLNVAHQEIDLKNPKGNRKNAGFTPEEREGFTQLLEAGFTDSFRELYPDQAYAYTFWTYMMNARSKNVGWRLDYFVLSSALLPGLCDSKIRNTAMGSDHCPITLFLAV
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Functions as a apurinic/apyrimidinic (AP) endodeoxyribonuclease in the DNA base excision repair (BER) pathway of DNA lesions induced by oxidative and alkylating agents. Initiates repair of AP sites in DNA by catalyzing hydrolytic incision of the phosphodiester backbone immediately adjacent to the damage, generating a single-strand break with 5'-deoxyribose phosphate and 3'-hydroxyl ends. May also play a role in the epigenetic regulation of gene expression by participating in DNA demethylation. Required for passage through the midblastula transition MBT. May also act as an endoribonuclease involved in the control of single-stranded RNA metabolism. Has no redox activity. Binds DNA and RNA.
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A0MTQ2
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BAPA_SPHMI
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Beta-peptidyl aminopeptidase BapA (EC 3.4.11.25) [Cleaved into: Beta-peptidyl aminopeptidase BapA alpha subunit; Beta-peptidyl aminopeptidase BapA beta subunit]
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MHYLKFPAIIAGMLLAGAASAEGPRARDLGVPFAGKPGANNAITDVAGVEVGYVSLISGEGKLERGKGPVRTGVTAVLPRGKESRTPVYAGWETSNAAGEMTGTVWLEERGYFDGPMMITNTHSVGVVRDAVVGWLADVKWPGAWFTPVVAETYDGMLNDINGFHVKPEHALRAIQTAASGPVAEGNVGGGVGMQCFGFKGGTGTASRVVEMDGKSYTVGVLVQCNFGMRPWLRVAGAPVGEELAGKYLPETRGTQTAAATNNGVAPGDGSIIVVMATDAPMLPHQLKRLAKRAAAGMGRMGDAGSNGSGDIFVAFSTANANVQSVGGNVISVETMPNDKLTLIFEAATQATEEAITNVLVAADTLTGVNGYTIQRLPHAELRAILKKYRRLAAAK
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Beta-aminopeptidase that can cleave synthetic beta-peptides which consist of backbone-elongated beta-amino acid residues that are not processed by common proteolytic enzymes. Can cleave the beta-peptides beta-homoVal-beta-homoAla-beta-homoLeu and beta-homoAla-beta-homoLeu. Requires a beta-amino acid at the N-terminus of peptide substrates and cleaves the peptide bond between the N-terminal beta-amino acid and the amino acid at the second position of tripeptidic substrates of the general structure H-betahXaa-Ile-betahTyr-OH according to the following preferences with regard to the side chain of the N-terminal beta-amino acid: aliphatic and aromatic > OH-containing > hydrogen, basic and polar. beta-homoVal-beta-homoAla-beta-homoLeu and beta-homoAla-beta-homoLeu.
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A0MZ66
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SHOT1_HUMAN
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Shootin-1 (Shootin1)
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MNSSDEEKQLQLITSLKEQAIGEYEDLRAENQKTKEKCDKIRQERDEAVKKLEEFQKISHMVIEEVNFMQNHLEIEKTCRESAEALATKLNKENKTLKRISMLYMAKLGPDVITEEINIDDEDSTTDTDGAAETCVSVQCQKQIKELRDQIVSVQEEKKILAIELENLKSKLVEVIEEVNKVKQEKTVLNSEVLEQRKVLEKCNRVSMLAVEEYEEMQVNLELEKDLRKKAESFAQEMFIEQNKLKRQSHLLLQSSIPDQQLLKALDENAKLTQQLEEERIQHQQKVKELEEQLENETLHKEIHNLKQQLELLEEDKKELELKYQNSEEKARNLKHSVDELQKRVNQSENSVPPPPPPPPPLPPPPPNPIRSLMSMIRKRSHPSGSGAKKEKATQPETTEEVTDLKRQAVEEMMDRIKKGVHLRPVNQTARPKTKPESSKGCESAVDELKGILGTLNKSTSSRSLKSLDPENSETELERILRRRKVTAEADSSSPTGILATSESKSMPVLGSVSSVTKTALNKKTLEAEFNSPSPPTPEPGEGPRKLEGCTSSKVTFQPPSSIGCRKKYIDGEKQAEPVVVLDPVSTHEPQTKDQVAEKDPTQHKEDEGEIQPENKEDSIENVRETDSSNC
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Involved in the generation of internal asymmetric signals required for neuronal polarization and neurite outgrowth. Mediates netrin-1-induced F-actin-substrate coupling or 'clutch engagement' within the axon growth cone through activation of CDC42, RAC1 and PAK1-dependent signaling pathway, thereby converting the F-actin retrograde flow into traction forces, concomitantly with filopodium extension and axon outgrowth. Plays a role in cytoskeletal organization by regulating the subcellular localization of phosphoinositide 3-kinase (PI3K) activity at the axonal growth cone. Also plays a role in regenerative neurite outgrowth. In the developing cortex, cooperates with KIF20B to promote both the transition from the multipolar to the bipolar stage and the radial migration of cortical neurons from the ventricular zone toward the superficial layer of the neocortex. Involved in the accumulation of phosphatidylinositol 3,4,5-trisphosphate (PIP3) in the growth cone of primary hippocampal neurons.
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A0MZ67
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SHOT1_RAT
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Shootin-1 (Shootin1)
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MNSSDEEKQLQLITSLKEQAIGEYEDLRAENQKTKETCDKIRQERDEAVKKLEEFQKISHMVIEEVNFMQNHLEIEKTCRESAEALATKLNKENKTLKRISMLYMAKLGPDVITEEINIDDDDPGTDTDAAAETCVSVQCQKQIKELRDQIVSVQEEKKVLAIELESLKSKLGEVMEEVNKVKQEKAVLNSEVLEQRKVLEKCNRVSVLAVEEYEELQVNLELEKDLRKKAESFAQEMFIEQNKLKRQSHLLLQSSLPDQQLLKALDENAKLIQQLEEERIQHQQKVKELEERLENEALHKEIHNLRQQLELLEDDKRELEQKYQSSEEKARNLKHSVDELQKRVNQSENSVPPPPPPPPPLPPPPPNPIRSLMSMIRKRSHPSGGSTKKEKATQPETAEEVTDLKRQAVEEMMDRIKKGVHLRPVNQTARPKAKPDSLKGSESAVDELKGILGTLNKSTSSRSLKSLGPENSETELERILRRRKLTAEADSSSPTGILATSESKSMPVLGSVSSVTKSALNKKTLEAEFNNPCPLTPEPGEGPRKLEGCTNSKVTFQPPSKGGYRRKCVGSENQSEPVVVLDPVSTHEPQTKDQAAEKDPTQCKEEERGETQPEFKEDSSGGKTGETDSSNC
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Involved in the generation of internal asymmetric signals required for neuronal polarization and neurite outgrowth. Mediates netrin-1-induced F-actin-substrate coupling or 'clutch engagement' within the axon growth cone through activation of CDC42, RAC1 and PAK1-dependent signaling pathway, thereby converting the F-actin retrograde flow into traction forces, concomitantly with filopodium extension and axon outgrowth. Plays a role in cytoskeletal organization by regulating the subcellular localization of phosphoinositide 3-kinase (PI3K) activity at the axonal growth cone. Also plays a role in regenerative neurite outgrowth. In the developing cortex, cooperates with KIF20B to promote both the transition from the multipolar to the bipolar stage and the radial migration of cortical neurons from the ventricular zone toward the superficial layer of the neocortex. Involved in the accumulation of phosphatidylinositol 3,4,5-trisphosphate (PIP3) in the growth cone of primary hippocampal neurons (By similarity).
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A0NLY7
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ISAHY_ROSAI
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Isatin hydrolase (EC 3.5.2.20) (Isatin amidohydrolase) (Isatin hydrolase isoform b) (IH-b)
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MSAQSALSGLGAKLLSGEVEVVDCTGVLGPNTPILQLPPDFAKNTPKVEIHKISEYDSDGPFFAWNWMVLGEHSGTHFDAPHHWITGKDYSDGFTDTLDVQRLIAPVNVIDCSKESAADPDFLLTADLIKAWEAEHGEIGAGEWVVMRTDWDKRAGDEAAFLNADETGPHSPGPTPDAIEYLLSKKIVGWGSQCIGTDAGQAGGMEPPFPAHNLLHRDNCFGLASLANLDKLPAKGAILIAAPLKIERGTGSPIRALALVPKA
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Involved in the degradation of the plant hormone indole-3-acetic acid (IAA). Catalyzes the hydrolysis of the cyclic amide bond (lactam) of isatin (1H-indole-2,3-dione) to yield isatinate (2-(2-aminophenyl)-2-oxoacetate).
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A0PC02
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UCP1_OCHDA
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Mitochondrial brown fat uncoupling protein 1 (UCP 1) (Solute carrier family 25 member 7) (Thermogenin)
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MVGTTATDVAPTMGVKIFSAGVAACLADVITFPLDTAKVRLQIQGECQTTSGIRYKGVLGTITTLAKTEGPLKLYSGLPAGLQRQISFASLRIGLYDTVQEFWGGEEATPSLRSKICAGLTTGGVAVFIGQPTEVVKVRLQAQSHLHGLKPRYTGTYNAYRIIATTESLSTLWKGTTPNLLRNIIINCTELVTYDLMKGALVRNDILADDVPCHLLSALIAGFCTTLLSSPVDVVKTRFINSPQGQYTSVPSCAMSMLTKEGPTAFFKGFAPSFLRLASWNVIMFVCFEKLKRELMKSRQTVDCAT
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Mitochondrial protein responsible for thermogenic respiration, a specialized capacity of brown adipose tissue and beige fat that participates in non-shivering adaptive thermogenesis to temperature and diet variations and more generally to the regulation of energy balance. Functions as a long-chain fatty acid/LCFA and proton symporter, simultaneously transporting one LCFA and one proton through the inner mitochondrial membrane. However, LCFAs remaining associated with the transporter via their hydrophobic tails, it results in an apparent transport of protons activated by LCFAs. Thereby, dissipates the mitochondrial proton gradient and converts the energy of substrate oxydation into heat instead of ATP. Regulates the production of reactive oxygen species/ROS by mitochondria.
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A0PJ25
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GLYC_BCNVU
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Pre-glycoprotein polyprotein GP complex (Pre-GP-C) [Cleaved into: Stable signal peptide (SSP); Glycoprotein G1 (GP1); Glycoprotein G2 (GP2)]
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MGQLVSFIGEIPAIVHEALNVALIAVSIIAIMKGLINIWKSGLFQLIMFLILAGRSCSISIGHHLELQHFIINSTSLLPSMPTLCRINATNSLIRGPFSAQWGLDIFIGDLTILVNPEPGSKTKRMTATNITGCFPNNEDPDSVAQVLSWFFRGVHHDFHLDPTILCDESVTVFRIQMNLTERMYCDRIVSKLARLFGSFGDYCSKVGKKLVIIRNVTWSNQCHEDHVGSMQLILQNAHNQVMRFRKLQNFFSWSLVDSAGNSMPGGYCLEKWMLVASELKCFGNTAVAKCNINHDSEFCDMLRLFDYNKKAIVNLQDKTKAQLDSLIDAVNSLISDNLITKNKIRELMNIPYCNYTKFWYVNHTGLNVHSLPKCWHVRNGSYLNESDFRNEWIIESDHLVSEILAKEYEERQKRTPLSLVDLCFWSTLFYTASIFLHLLHIPTHRHIIGEGCPKPHRLTSDSLCACGFFQLKGRPTRWARIP
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[Glycoprotein G2]: Class I viral fusion protein that directs fusion of viral and host endosomal membranes, leading to delivery of the nucleocapsid into the cytoplasm. Membrane fusion is mediated by irreversible conformational changes induced upon acidification in the endosome. {ECO:0000255|HAMAP-Rule:MF_04084}. Stable signal peptide (SSP): cleaved and functions as a signal peptide. In addition, it is also retained as the third component of the GP complex. The SSP is required for efficient glycoprotein expression, post-translational maturation cleavage of GP1 and GP2, glycoprotein transport to the cell surface plasma membrane, formation of infectious virus particles, and acid pH-dependent glycoprotein-mediated cell fusion. {ECO:0000255|HAMAP-Rule:MF_04084}. [Glycoprotein G1]: Interacts with the host receptor. {ECO:0000255|HAMAP-Rule:MF_04084}.
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A0PJK1
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SC5AA_HUMAN
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Sodium/mannose cotransporter SLC5A10 (Sodium/glucose cotransporter 5) (Na(+)/glucose cotransporter 5) (Solute carrier family 5 member 10)
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MAANSTSDLHTPGTQLSVADIIVITVYFALNVAVGIWSSCRASRNTVNGYFLAGRDMTWWPIGASLFASSEGSGLFIGLAGSGAAGGLAVAGFEWNATYVLLALAWVFVPIYISSEIVTLPEYIQKRYGGQRIRMYLSVLSLLLSVFTKISLDLYAGALFVHICLGWNFYLSTILTLGITALYTIAGGLAAVIYTDALQTLIMVVGAVILTIKAFDQIGGYGQLEAAYAQAIPSRTIANTTCHLPRTDAMHMFRDPHTGDLPWTGMTFGLTIMATWYWCTDQVIVQRSLSARDLNHAKAGSILASYLKMLPMGLIIMPGMISRALFPDDVGCVVPSECLRACGAEVGCSNIAYPKLVMELMPIGLRGLMIAVMLAALMSSLTSIFNSSSTLFTMDIWRRLRPRSGERELLLVGRLVIVALIGVSVAWIPVLQDSNSGQLFIYMQSVTSSLAPPVTAVFVLGVFWRRANEQGAFWGLIAGLVVGATRLVLEFLNPAPPCGEPDTRPAVLGSIHYLHFAVALFALSGAVVVAGSLLTPPPQSVQIENLTWWTLAQDVPLGTKAGDGQTPQKHAFWARVCGFNAILLMCVNIFFYAYFA
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[Isoform 1]: Electrogenic Na+-coupled sugar symporter that actively transports D-mannose or D-fructose at the plasma membrane, with a Na+ to sugar coupling ratio of 1:1. Transporter activity is driven by a transmembrane Na+ electrochemical gradient set by the Na+/K+ pump. Exclusively recognizes sugar substrates having a pyranose ring with an axial hydroxyl group on carbon 2. Has likely evolved to enable renal reabsorption of D-mannose, an important constituent of oligosaccharide chains of glycoproteins. Contributes to dietary D-fructose reabsorption from glomerular filtrate across the brush border of the kidney.
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A0PJY2
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FEZF1_HUMAN
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Fez family zinc finger protein 1 (Zinc finger protein 312B)
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MDSSCHNATTKMLATAPARGNMMSTSKPLAFSIERIMARTPEPKALPVPHFLQGALPKGEPKHSLHLNSSIPCMIPFVPVAYDTSPKAGVTGSEPRKASLEAPAAPAAVPSAPAFSCSDLLNCALSLKGDLARDALPLQQYKLVRPRVVNHSSFHAMGALCYLNRGDGPCHPAAGVNIHPVASYFLSSPLHPQPKTYLAERNKLVVPAVEKYPSGVAFKDLSQAQLQHYMKESAQLLSEKIAFKTSDFSRGSPNAKPKVFTCEVCGKVFNAHYNLTRHMPVHTGARPFVCKVCGKGFRQASTLCRHKIIHTQEKPHKCNQCGKAFNRSSTLNTHTRIHAGYKPFVCEFCGKGFHQKGNYKNHKLTHSGEKQFKCNICNKAFHQVYNLTFHMHTHNDKKPFTCPTCGKGFCRNFDLKKHVRKLHDSSLGLARTPAGEPGTEPPPPLPQQPPMTLPPLQPPLPTPGPLQPGLHQGHQ
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Transcription repressor. Involved in the axonal projection and proper termination of olfactory sensory neurons (OSN). Plays a role in rostro-caudal patterning of the diencephalon and in prethalamic formation. Expression is required in OSN to cell-autonomously regulate OSN axon projections. Regulates non-cell-autonomously the layer formation of the olfactory bulb development and the interneurons. May be required for correct rostral migration of the interneuron progenitors (By similarity).
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A0PK00
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T120B_HUMAN
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Transmembrane protein 120B
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MSGQLERCEREWHELEGEFQELQETHRIYKQKLEELAALQTLCSSSISKQKKHLKDLKLTLQRCKRHASREEAELVQQMAANIKERQDVFFDMEAYLPKKNGLYLNLVLGNVNVTLLSNQAKFAYKDEYEKFKLYLTIILLLGAVACRFVLHYRVTDEVFNFLLVWYYCTLTIRESILISNGSRIKGWWVSHHYVSTFLSGVMLTWPNGPIYQKFRNQFLAFSIFQSCVQFLQYYYQRGCLYRLRALGERNHLDLTVEGFQSWMWRGLTFLLPFLFCGHFWQLYNAVTLFELSSHEECREWQVFVLAFTFLILFLGNFLTTLKVVHAKLQKNRGKTKQP
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Necessary for efficient adipogenesis. Does not show ion channel activity.
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A0PK11
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CLRN2_HUMAN
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Clarin-2
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MPGWFKKAWYGLASLLSFSSFILIIVALVVPHWLSGKILCQTGVDLVNATDRELVKFIGDIYYGLFRGCKVRQCGLGGRQSQFTIFPHLVKELNAGLHVMILLLLFLALALALVSMGFAILNMIQVPYRAVSGPGGICLWNVLAGGVVALAIASFVAAVKFHDLTERIANFQEKLFQFVVVEEQYEESFWICVASASAHAANLVVVAISQIPLPEIKTKIEEATVTAEDILY
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Plays a key role to hearing function. Required for normal organization and maintenance of the stereocilia bundle and for mechano-electrical transduction.
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A0PVU7
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KGD_MYCUA
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Multifunctional 2-oxoglutarate metabolism enzyme (2-hydroxy-3-oxoadipate synthase) (HOA synthase) (HOAS) (EC 2.2.1.5) (2-oxoglutarate carboxy-lyase) (2-oxoglutarate decarboxylase) (Alpha-ketoglutarate decarboxylase) (KG decarboxylase) (KGD) (EC 4.1.1.71) (Alpha-ketoglutarate-glyoxylate carboligase) [Includes: 2-oxoglutarate dehydrogenase E1 component (ODH E1 component) (EC 1.2.4.2) (Alpha-ketoglutarate dehydrogenase E1 component) (KDH E1 component); Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex (EC 2.3.1.61) (2-oxoglutarate dehydrogenase complex E2 component) (ODH E2 component) (OGDC-E2) (Dihydrolipoamide succinyltransferase)]
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MANISSPFGQNEWLVEEMYRKFRDDPSSVDPSWHEFLVDYNPESTQEATEPAVVKPAAAPAKPAPAPAPAKPAAGPPAAGNGSPAAAPSAKPAAAPAKAPAPPPAEGDEMQVLRGAAAAVVKNMSASLDVPTATSVRAVPAKLLIDNRIVINNQLKRNRGGKISFTHLLGYALVQAVKKFPNMNRHYLDVDGKPNAVTPAHTNLGLAIDLQGKDGKRALVVAGIKRCETMRFAQFVTAYEDIVRRARDGKLTAEDFSGVTISLTNPGTIGTVHSVPRLMAGQGAIIGVGAMEYPAEFQGASEERIAELGIGKLITLTSTYDHRIIQGAESGDFLRTIHQMLLADEFWDEIFRELSIPYLPVRWRPDNPDSIVDKNARIIELIAAYRNRGHLMADIDPLRLDKTRFRSHPDLDVCTHGLTLWDLDRSFKVGGCFAGPQNMKLRDVLSILRDTYCRHVGVEYTHILEPEQQQWLQQRVEAKHVKPTVAQQKYVLSKLNAAEAFETFLQTKYVGQKRFSLEGAESVIPMMDAAIDQCAEYGLDEVVIGMPHRGRLNVLANIVGKPYSQIFSEFEGNLNPSQAHGSGDVKYHLGATGVYLQMFGDNDIQVSLTANPSHLEAVDPVLEGLVRAKQDLLEHGETDTENQRAFSVVPMMLHGDAAFAGQGVVAETLNLANLPGYRVGGTIHIIVNNQIGFTTAPEYSRSTEYCTDVAKTIGAPIFHVNGDDPEACVWVARLAVDFRQRFNKDVIIDMLCYRRRGHNEGDDPSMTNPRMYDVVDTKRGVRKSYTEALIGRGDISIKEAEDALRDYQGQLEQVFNEVRELEKHGAQPSESVESDQMIPAGLATAVDKSLLARIGDAFLAVPDGFTTHPRVQPVLEKRREMAYEGKIDWAFAELLALGSLVAEGKLVRFSGQDTRRGTFSQRHSVIIDRHTREEFTPLQLLTTNKDGSPTGGKFLVYDSPLSEYAAVGFEYGYTVGNPDAVVLWEAQFGDFVNGAQSIIDEFISSGEAKWGQLSNVVLLLPHGHEGQGPDHTSGRIERFLQLWAEGSMTIAMPSTPSNYFHLLRRHALDGIQRPLIVFTPKSMLRNKAAVSDIKDFTEIKFRSVLEEPTYEDGVGDRNLVNRILLTSGKIYYEMVARKAKDKREDVAIVRVEQLAPLPRRRLRETLDRYPNAKEFFWVQEEPANQGAWPRFGLELPELLPEKLSGVKRISRRAMSAPSSGSSKVHAVEQQEILDTAFG
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Shows three enzymatic activities that share a first common step, the attack of thiamine-PP on 2-oxoglutarate (alpha-ketoglutarate, KG), leading to the formation of an enamine-thiamine-PP intermediate upon decarboxylation. Thus, displays KGD activity, catalyzing the decarboxylation from five-carbon 2-oxoglutarate to four-carbon succinate semialdehyde (SSA). Also catalyzes C-C bond formation between the activated aldehyde formed after decarboxylation of alpha-ketoglutarate and the carbonyl of glyoxylate (GLX), to yield 2-hydroxy-3-oxoadipate (HOA), which spontaneously decarboxylates to form 5-hydroxylevulinate (HLA). And is also a component of the 2-oxoglutarate dehydrogenase (ODH) complex, that catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). The KG decarboxylase and KG dehydrogenase reactions provide two alternative, tightly regulated, pathways connecting the oxidative and reductive branches of the TCA cycle (By similarity).
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A0Q5Y3
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CAS9_FRATN
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CRISPR-associated endonuclease Cas9 (EC 3.1.-.-)
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MNFKILPIAIDLGVKNTGVFSAFYQKGTSLERLDNKNGKVYELSKDSYTLLMNNRTARRHQRRGIDRKQLVKRLFKLIWTEQLNLEWDKDTQQAISFLFNRRGFSFITDGYSPEYLNIVPEQVKAILMDIFDDYNGEDDLDSYLKLATEQESKISEIYNKLMQKILEFKLMKLCTDIKDDKVSTKTLKEITSYEFELLADYLANYSESLKTQKFSYTDKQGNLKELSYYHHDKYNIQEFLKRHATINDRILDTLLTDDLDIWNFNFEKFDFDKNEEKLQNQEDKDHIQAHLHHFVFAVNKIKSEMASGGRHRSQYFQEITNVLDENNHQEGYLKNFCENLHNKKYSNLSVKNLVNLIGNLSNLELKPLRKYFNDKIHAKADHWDEQKFTETYCHWILGEWRVGVKDQDKKDGAKYSYKDLCNELKQKVTKAGLVDFLLELDPCRTIPPYLDNNNRKPPKCQSLILNPKFLDNQYPNWQQYLQELKKLQSIQNYLDSFETDLKVLKSSKDQPYFVEYKSSNQQIASGQRDYKDLDARILQFIFDRVKASDELLLNEIYFQAKKLKQKASSELEKLESSKKLDEVIANSQLSQILKSQHTNGIFEQGTFLHLVCKYYKQRQRARDSRLYIMPEYRYDKKLHKYNNTGRFDDDNQLLTYCNHKPRQKRYQLLNDLAGVLQVSPNFLKDKIGSDDDLFISKWLVEHIRGFKKACEDSLKIQKDNRGLLNHKINIARNTKGKCEKEIFNLICKIEGSEDKKGNYKHGLAYELGVLLFGEPNEASKPEFDRKIKKFNSIYSFAQIQQIAFAERKGNANTCAVCSADNAHRMQQIKITEPVEDNKDKIILSAKAQRLPAIPTRIVDGAVKKMATILAKNIVDDNWQNIKQVLSAKHQLHIPIITESNAFEFEPALADVKGKSLKDRRKKALERISPENIFKDKNNRIKEFAKGISAYSGANLTDGDFDGAKEELDHIIPRSHKKYGTLNDEANLICVTRGDNKNKGNRIFCLRDLADNYKLKQFETTDDLEIEKKIADTIWDANKKDFKFGNYRSFINLTPQEQKAFRHALFLADENPIKQAVIRAINNRNRTFVNGTQRYFAEVLANNIYLRAKKENLNTDKISFDYFGIPTIGNGRGIAEIRQLYEKVDSDIQAYAKGDKPQASYSHLIDAMLAFCIAADEHRNDGSIGLEIDKNYSLYPLDKNTGEVFTKDIFSQIKITDNEFSDKKLVRKKAIEGFNTHRQMTRDGIYAENYLPILIHKELNEVRKGYTWKNSEEIKIFKGKKYDIQQLNNLVYCLKFVDKPISIDIQISTLEELRNILTTNNIAATAEYYYINLKTQKLHEYYIENYNTALGYKKYSKEMEFLRSLAYRSERVKIKSIDDVKQVLDKDSNFIIGKITLPFKKEWQRLYREWQNTTIKDDYEFLKSFFNVKSITKLHKKVRKDFSLPISTNEGKFLVKRKTWDNNFIYQILNDSDSRADGTKPFIPAFDISKNEIVEAIIDSFTSKNIFWLPKNIELQKVDNKNIFAIDTSKWFEVETPSDLRDIGIATIQYKIDNNSRPKVRVKLDYVIDDDSKINYFMNHSLLKSRYPDKVLEILKQSTIIEFESSGFNKTIKEMLGMKLAGIYNETSNN
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CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). In type II CRISPR systems correct processing of pre-crRNA requires a trans-encoded small RNA (tracrRNA), endogenous ribonuclease 3 (rnc) and this protein. The tracrRNA serves as a guide for ribonuclease 3-aided processing of pre-crRNA. Subsequently Cas9/crRNA/tracrRNA endonucleolytically cleaves linear or circular dsDNA target complementary to the spacer Cas9 is inactive in the absence of the 2 guide RNAs (gRNA). Cas9 recognizes a short motif in the CRISPR repeat sequences (the PAM or protospacer adjacent motif) to help distinguish self versus nonself, as targets within the bacterial CRISPR locus do not have PAMs. PAM recognition is also required for catalytic activity. Cuts target DNA when Cas9 and gRNAs are mixed. Plays a role in repression of expression of endogenous bacterial lipoprotein FTN_1103. Cas9 plays a possibly non-enzymatic role in the degradation of FTN_1103 mRNA, which is dependent on formation of an RNA:RNA complex of tracrRNA and scaRNA (the latter is not found in all type II CRISPR-Cas systems).
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A0Q7Q2
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CS12A_FRATN
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CRISPR-associated endonuclease Cas12a (EC 3.1.21.1) (EC 4.6.1.22) (CRISPR-associated endonuclease Cpf1) (FnCas12a) (FnCpf1)
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MSIYQEFVNKYSLSKTLRFELIPQGKTLENIKARGLILDDEKRAKDYKKAKQIIDKYHQFFIEEILSSVCISEDLLQNYSDVYFKLKKSDDDNLQKDFKSAKDTIKKQISEYIKDSEKFKNLFNQNLIDAKKGQESDLILWLKQSKDNGIELFKANSDITDIDEALEIIKSFKGWTTYFKGFHENRKNVYSSNDIPTSIIYRIVDDNLPKFLENKAKYESLKDKAPEAINYEQIKKDLAEELTFDIDYKTSEVNQRVFSLDEVFEIANFNNYLNQSGITKFNTIIGGKFVNGENTKRKGINEYINLYSQQINDKTLKKYKMSVLFKQILSDTESKSFVIDKLEDDSDVVTTMQSFYEQIAAFKTVEEKSIKETLSLLFDDLKAQKLDLSKIYFKNDKSLTDLSQQVFDDYSVIGTAVLEYITQQIAPKNLDNPSKKEQELIAKKTEKAKYLSLETIKLALEEFNKHRDIDKQCRFEEILANFAAIPMIFDEIAQNKDNLAQISIKYQNQGKKDLLQASAEDDVKAIKDLLDQTNNLLHKLKIFHISQSEDKANILDKDEHFYLVFEECYFELANIVPLYNKIRNYITQKPYSDEKFKLNFENSTLANGWDKNKEPDNTAILFIKDDKYYLGVMNKKNNKIFDDKAIKENKGEGYKKIVYKLLPGANKMLPKVFFSAKSIKFYNPSEDILRIRNHSTHTKNGSPQKGYEKFEFNIEDCRKFIDFYKQSISKHPEWKDFGFRFSDTQRYNSIDEFYREVENQGYKLTFENISESYIDSVVNQGKLYLFQIYNKDFSAYSKGRPNLHTLYWKALFDERNLQDVVYKLNGEAELFYRKQSIPKKITHPAKEAIANKNKDNPKKESVFEYDLIKDKRFTEDKFFFHCPITINFKSSGANKFNDEINLLLKEKANDVHILSIDRGERHLAYYTLVDGKGNIIKQDTFNIIGNDRMKTNYHDKLAAIEKDRDSARKDWKKINNIKEMKEGYLSQVVHEIAKLVIEYNAIVVFEDLNFGFKRGRFKVEKQVYQKLEKMLIEKLNYLVFKDNEFDKTGGVLRAYQLTAPFETFKKMGKQTGIIYYVPAGFTSKICPVTGFVNQLYPKYESVSKSQEFFSKFDKICYNLDKGYFEFSFDYKNFGDKAAKGKWTIASFGSRLINFRNSDKNHNWDTREVYPTKELEKLLKDYSIEYGHGECIKAAICGESDKKFFAKLTSVLNTILQMRNSKTGTELDYLISPVADVNGNFFDSRQAPKNMPQDADANGAYHIGLKGLMLLGRIKNNQEGKKLNLVIKNEEYFEFVQNRNN
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CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Has endonuclease activity on pre-crRNA and dsDNA, using different active sites. A single-RNA guided endonuclease that is also capable of guiding crRNA processing correct processing of pre-crRNA requires only this protein and the CRISPR locus. pre-crRNA processing proceeds by an intramolecular nucleophilic attack on the scissile phosphate by the 2'-OH of the upstream ribonucleotide, the divalent cation (which is bound by the crRNA) is probably required for ordering the crRNA pseudoknot and/or increasing RNA binding. RNA mutagenesis studies show pre-crRNA cleavage is highly sequence- and structure-specific. Forms a complex with crRNA and complementary dsDNA, where the crRNA displaces the non-target DNA strand and directs endonucleolytic cleavage of both strands of the DNA. Cleavage results in staggered 5-base 5' overhangs 14-18 and 21-23 bases downstream of the PAM (protospacer adjacent motif) on the non-target and target strands respectively. Both target and non-target strand DNA are probably independently cleaved in the same active site. When this protein is expressed in E.coli it prevents plasmids homologous to the first CRISPR spacer from transforming, formally showing it is responsible for plasmid immunity.
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A0QNE0
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GYRB_MYCS2
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DNA gyrase subunit B (EC 5.6.2.2)
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MAAQKNNAPKEYGADSITILEGLEAVRKRPGMYIGSTGERGLHHLIWEVVDNAVDEAMAGFATRVDVKIHADGSVEVRDDGRGIPVEMHATGMPTIDVVMTQLHAGGKFDGETYAVSGGLHGVGVSVVNALSTRLEATVLRDGYEWFQYYDRSVPGKLKQGGETKETGTTIRFWADPEIFETTDYNFETVARRLQEMAFLNKGLTIELTDERVTAEEVVDDVVKDTAEAPKTADEKAAEATGPSKVKHRVFHYPGGLVDYVKHINRTKTPIQQSIIDFDGKGPGHEVEIAMQWNAGYSESVHTFANTINTHEGGTHEEGFRAALTSVVNRYAKDKKLLKDKDPNLTGDDIREGLAAVISVKVAEPQFEGQTKTKLGNTEVKSFVQKICNEQLQHWFEANPAEAKTVVNKAVSSAQARIAARKARELVRRKSATDIGGLPGKLADCRSTDPSKSELYVVEGDSAGGSAKSGRDSMFQAILPLRGKIINVEKARIDRVLKNTEVQSIITALGTGIHDEFDISKLRYHKIVLMADADVDGQHISTLLLTLLFRFMKPLVENGHIFLAQPPLYKLKWQRSEPEFAYSDRERDGLLEAGRAAGKKINVDDGIQRYKGLGEMDAKELWETTMDPSVRVLRQVTLDDAAAADELFSILMGEDVEARRSFITRNAKDVRFLDV
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A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner. {ECO:0000255|HAMAP-Rule:MF_01898, ECO:0000269|PubMed:8878580}.
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A0QNG1
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PKNB_MYCS2
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Serine/threonine-protein kinase PknB (EC 2.7.11.1)
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MTTPQHLSDRYELGEILGFGGMSEVHLARDLRLHRDVAVKVLRADLARDPSFYLRFRREAQNAAALNHPAIVAVYDTGEAETPNGPLPYIVMEYVDGVTLRDIVHTDGPIAPRRAIEIIADACQALNFSHQHGIIHRDVKPANIMISKNNAVKVMDFGIARALADTGNSVTQTAAVIGTAQYLSPEQARGETVDARSDVYSLGCVLYEILTGEPPFIGDSPVAVAYQHVREDPVPPSRRHADVTPELDAVVLKALAKNPDNRYQTAAEMRADLIRVHEGQAPDAPKVLTDAERTSMLAAPPADRAGAATQDMPVPRPAGYSKQRSTSVARWLIAVAVLAVLTVVVTVAINMVGGNPRNVQVPDVAEQSADDAQAALQNRGFKTVIDRQPDNEVPPGLVIGTDPEAGSELGAGEQVTINVSTGPEQALVPDVAGLTPTQARQKLKDAGFEKFRESPSPSTPEQKGRVLATNPQANQTAAIINEITIVVGAGPEDAPVLSCAGQNAESCKAILAAGGFTNTVVVEVDNPAAAGQVVGTEPADGQSVPKDTVIQIRVSKGNQFVMPDLVGQFWSDAYPRLTALGWTGVLDKGPDVRDSGQRTNAVVTQSPSAGTPVNKDAKITLSFAA
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Protein kinase that regulates many aspects of mycobacterial physiology. Is a key component of a signal transduction pathway that regulates cell growth, cell shape and cell division via phosphorylation of target proteins (By similarity). Probably phosphorylates RseA.
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A0QP27
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MMPL3_MYCS2
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Trehalose monomycolate exporter MmpL3 (TMM exporter MmpL3) (MmpL3 transporter) (Mycobacterial membrane protein large 3)
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MFAWWGRTVYQFRYIVIGVMVALCLGGGVYGISLGNHVTQSGFYDEGSQSVAASLIGDEVYGRDRTSHVVAILTPPDDKKVTDKAWQKKVTEELDQVVKDHEDQIVGWVGWLKAPDTTDPTVSAMKTQDLRHTFISIPLQGDDDDEILKNYQVVEPELQQVNGGDIRLAGLNPLASELTGTIGEDQKRAEVAAIPLVAVVLFFVFGTVIAAALPAIIGGLAIAGALGIMRLVAEFTPVHFFAQPVVTLIGLGIAIDYGLFIVSRFREEIAEGYDTEAAVRRTVMTSGRTVVFSAVIIVASSVPLLLFPQGFLKSITYAIIASVMLAAILSITVLAAALAILGPRVDALGVTTLLKIPFLANWQFSRRIIDWFAEKTQKTKTREEVERGFWGRLVNVVMKRPIAFAAPILVVMVLLIIPLGQLSLGGISEKYLPPDNAVRQSQEQFDKLFPGFRTEPLTLVMKREDGEPITDAQIADMRAKALTVSGFTDPDNDPEKMWKERPANDSGSKDPSVRVIQNGLENRNDAAKKIDELRALQPPHGIEVFVGGTPALEQDSIHSLFDKLPLMALILIVTTTVLMFLAFGSVVLPIKAALMSALTLGSTMGILTWMFVDGHGSGLMNYTPQPLMAPMIGLIIAVIWGLSTDYEVFLVSRMVEARERGMSTAEAIRIGTATTGRLITGAALILAVVAGAFVFSDLVMMKYLAFGLLIALLLDATIIRMFLVPAVMKLLGDDCWWAPRWMKRVQEKLGLGETELPDERKRPTVRESETDQRALVGVGAPPPPPRPHDPTHPAPEPVRPMPPMRSNAPSAAGTARISTPPQPPQPPQAPAQQAGDEPATTRFAMARNAVRNAVNSAVHGGAGSAAAPTERAPRPGGPAQPPAPPQREEREIESWLGALRGPAPAKNVPQPPAQPQRPSTDTTRAMPPQGRPPAGPADRGNENAPTTAFSAQRPPNGGAPADATTAIPTPPQREQEPSTEKLNTREDAPEDPETKRRGGGMSAQDLLRREGRL
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Transports trehalose monomycolate (TMM) to the cell wall. Flips TMM across the inner membrane. Membrane potential is not required for this function. Transports probably phosphatidylethanolamine (PE) as well. Binds specifically both TMM and PE, but not trehalose dimycolate (TDM). Binds also diacylglycerol (DAG) and other phospholipids, including phosphatidylglycerol (PG), phosphatidylinositol (PI), and cardiolipin (CDL). Contributes to membrane potential, cell wall composition, antibiotic susceptibility and fitness.
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A0QQ53
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STF0_MYCS2
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Trehalose 2-sulfotransferase (EC 2.8.2.37)
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MSDHPTAYLVLASQRSGSTLLVESLRATGVAGEPQEFFQYLPNTSMSPQPREWFADVEDQSILRLLDPLIEGKPDLAPATIWRDYIQTVGRTPNGVWGGKLMWNQTPLLVQRAKDLPDRSGSGLLSAIRDVVGSDPVLIHIHRPDVVSQAVSFWRAVQTRVWRGRPDPVRDARAEYHAGAIAHVITMLRAQEEGWRAWFTEENVEPIDVDYPYLWRNLTEVVGTVLEALGQDPRLAPKPVLERQADQRSDEWVERYRRDAQRDGLPL
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Catalyzes the sulfuryl group transfer from 3'-phosphoadenosine-5'-phosphosulfate (PAPS) to trehalose, leading to trehalose-2-sulfate (T2S). The sulfation of trehalose is the first step in the biosynthesis of sulfolipid-1 (SL-1), a major cell wall glycolipid in pathogenic mycobacteria. Cannot use free glucose and unnatural stereoisomers of trehalose (alpha,beta (neo-trehalose) and beta,beta (iso-trehalose)) as substrates.
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A0QQF4
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TTFA_MYCS2
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Trehalose monomycolate transport factor A (TMM transport factor A)
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MVPLWFTLSALCFVGAAVLLYVDIDRRRGLGRRRKSWAKSHGFDYEYESEDLLKRWKRGVMSTVGDVTAKNVVLGQIRGEAVFIFDIEEVATVIALHRKVGTNVVVDLRLKGLKEPRENDIWLLGAIGPRMVYSTNLDAARRACDRRMVTFAHTAPDCAEIMWNEQNWTLVAMPVTSNRAQWDEGLRTVRQFNDLLRVLPPVPQNGSQAALPRRGGSPSRPLAPTPAGRRELPPGRADVPPARGDVSRFAPRPEAGRSDAFRRPPPARNGREASHFQR
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Required for MmpL3-dependent trehalose monomycolate (TMM) transport to the cell wall. Required for growth and cell elongation.
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A0QQJ4
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FGD_MYCS2
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F420-dependent glucose-6-phosphate dehydrogenase (FGD) (G6PD) (EC 1.1.98.2)
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MAELKLGYKASAEQFAPRELVELAVLAESAGMDSATVSDHFQPWRHEGGHAPFSLAWMTAVGERTKNLVLGTSVLTPTFRYNPAVIAQAFATMGCLYPGRIFLGVGTGEALNEIATGYAGEWPEFKERFARLRESVRLMRELWLGDRVDFDGEYYRTKGASIYDVPEGGIPVYIAAGGPVVAKYAGRAGDGFICTSGKGEELYAEKLIPAVKEGAAAADRDADAIDRMIEIKISYDTDPELALENTRFWAPLSLTAEQKHSIDDPIEMEKAADALPIEQVAKRWIVASDPDEAVEKVGQYVKWGLNHLVFHAPGHDQRRFLELFKRDLEPRLRKLA
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Catalyzes the coenzyme F420-dependent oxidation of glucose 6-phosphate (G6P) to 6-phosphogluconolactone. Appears to have a role in resistance to oxidative stress, via its consumption of G6P that serves as a source of reducing power to combat oxidative stress in mycobacteria. Cannot use NAD, NADP, FAD or FMN instead of coenzyme F420 as an electron acceptor. Exhibits nearly no activity with D-mannose-6-phosphate or D-fructose-6-phosphate as substrate.
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A0QR29
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MSPA_MYCS2
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Porin MspA
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MKAISRVLIAMVAAIAALFTSTGTSHAGLDNELSLVDGQDRTLTVQQWDTFLNGVFPLDRNRLTREWFHSGRAKYIVAGPGADEFEGTLELGYQIGFPWSLGVGINFSYTTPNILIDDGDITAPPFGLNSVITPNLFPGVSISADLGNGPGIQEVATFSVDVSGAEGGVAVSNAHGTVTGAAGGVLLRPFARLIASTGDSVTTYGEPWNMN
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The major porin in this organism, forms a water-filled channel which favors the permeation of cations, amino acids, iron Fe(3+) and less efficiently phosphate. Does not transport Fe-ExoMS, the predominant siderophore. Plays a role in transport of beta-lactamase and hydrophilic fluoroquinolone antibiotics such as norfloxacin as well as chloramphenicol. There are about 2400 porins in wild-type, 800 in an mspA deletion and 150 in a double mspA-mspC deletion. Different conductance values with maxima at 2.3 and 4.6 nanosiemens might be caused by a simultaneous reconstitution of MspA channels into the membrane or by the existence of different MspA conformations.
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A0QTP2
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SIGH_MYCS2
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ECF RNA polymerase sigma factor SigH (ECF sigma factor SigH) (Alternative RNA polymerase sigma factor SigH) (RNA polymerase sigma-H factor) (Sigma-H factor)
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MTDVDRVEPETPPEREETDAELTARFERDAIPLLDQLYGGALRMTRNPADAEDLLQETMVKAYAGFRSFREGTNLKAWLYRILTNTYINSYRKKQRQPSEYPTDEITDWQLASNAEHSSTGLRSAEVEALEALPDTEIKAALQALPEEFRMAVYYADVEGFPYKEIAEIMETPIGTVMSRLHRGRRQLRDLLAGVARDRGFIRGPQLGEPEEVTS
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Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. Extracytoplasmic function (ECF) sigma factors are held in an inactive form by an anti-sigma factor until released. This sigma factor is involved in heat shock and oxidative stress responses.
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A0QUA1
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MBTM_MYCS2
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Medium/long-chain-fatty-acid--[acyl-carrier-protein] ligase MbtM (EC 6.2.1.20) (EC 6.2.1.47) (Fatty acyl-[acyl-carrier-protein] synthetase) (Fatty acyl-ACP synthetase) (Mycobactin fatty acyl-AMP ligase) (Mycobactin synthetase protein M)
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MNVLSAALTEAMTTSSADLVVFEPETRTWHRHPWGQVHLRAQNVAERIGQDGSSAVGIVGEPTVEGVAAILGALLAGSAVSILPGLVRGADPDQWADSTLNRFANIGVTTVFSHGSYLEQLRTRDSSLVIHDDAEVAHAQRSTTLELGAPLGEFAVLQGTAGSTGTPRTAQLRPDAVLANLRGLAERVGLAGSDIGCSWLPLYHDMGLTFLLSAAVGGTETWQAPTTAFASAPFSWVHWLTESRATLTAAPNMAYGLIGKYSRRLTDVDLSAMRFALNGGEPVDIDGTARFGTELSRFGFDPGALSPSYGLAESSCAVTVPVPGVGLKVDEITVTTEAGSSTQKLAVLGHAIAGMEVRLQPGDEDAGVVDREVGEVEIRGTSMMSGYRGEAPLDPGEWFPTGDLGYLTDDGLVICGRKKELITVAGRNIFPTEIERIAARVKGVREGAVVAVGTNERAVRPGLVIAAEFRGPDEAGARSEVVQRVASECGVVPADVVFLAPGSLPRTSSGKLRRLEVKRQLEESKG
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Activates lipidic moieties required for mycobactin biosynthesis. Converts medium- to long-chain aliphatic fatty acids into acyl adenylate, which is further transferred on to the phosphopantetheine arm of the carrier protein MbtL. Shows a strong preference for palmitic acid (C16) and cannot use short-chain fatty acids. Proceeds via a Bi Uni Uni Bi ping-pong mechanism. During the first half-reaction (adenylation), fatty acid binds first to the free enzyme, followed by ATP and the release of pyrophosphate to form the adenylate intermediate. During the second half-reaction (ligation), holo-MbtL binds to the enzyme followed by the release of products AMP and acylated MbtL.
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A0QUZ2
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MUTT1_MYCS2
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8-oxo-(d)GTP phosphatase (8-oxo-(d)GTPase) (EC 3.6.1.69) (8-oxo-(d)GDP phosphatase) (EC 3.6.1.58) (Diadenosine hexaphosphate hydrolase) (Ap6A hydrolase) (EC 3.6.1.61) (MsMutT1)
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MMPVDDLQEIPLSKDTTEKSKHTVRAAGAVLWRDASEHGGTTGHPATVEVAVIHRPRYDDWSLPKGKLDQGETEPVAAAREIHEETGHTAVLGRRLGRVTYPIPQGTKRVWYWAAKSTGGDFSPNDEVDKLVWLPVDAAMDQLQYPDDRKVLRRFVKRPVDTKTVLVVRHGTAGRRSRYKGDDRKRPLDKRGRAQAEALVAQLMAFGATTLYAADRVRCHQTIEPLAQELDQLIHNEPLLTEEAYAADHKAARKRLLEIAGRPGNPVICTQGKVIPGLIEWWCERAKVRPETTGNRKGSTWVLSLSDGELVGADYLSPPDEK
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Catalyzes the conversion of 8-oxo-dGTP to 8-oxo-dGDP, and 8-oxo-GTP to 8-oxo-GDP. At high enzyme concentrations, can also catalyze the conversion of 8-oxo-dGDP to 8-oxo-dGMP, and 8-oxo-GDP to 8-oxo-GMP. In addition, catalyzes the hydrolysis of the diadenosine polyphosphates diadenosine hexaphosphate (Ap6A), diadenosine pentaphosphate (Ap5A) and diadenosine tetraphosphate (Ap4A).
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A0QVH8
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RIP1_MYCS2
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Zinc metalloprotease Rip1 (EC 3.4.24.-) (Regulator of sigma KLM proteases) (S2P endopeptidase) (Site-2-type intramembrane protease) (site-2 protease Rip1) (S2P protease Rip1)
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MMFGIGIVLFALAILVSVALHECGHMWVARATGMKVRRYFVGFGPTLWSTRRANRLGSTEYGIKAIPLGGFCDIAGMTSVDEIAPEDRPYAMYKQKVWKRVAVLFAGPAMNFVIGLVLIYGIAIVWGLPNLHQPTTAIVGETGCVAPQITLEEMGECTGPGPAALAGIQAGDEIVKVGDTEVKDFAGMAAAVRKLDGPTRIEFKRDGRVMDTVVDVTPTQRFTSADASAPSTVGAIGVSAVPVQPPAQYNPITAVPATFAFTGDLAVELGKSLAKIPTKIGALVEAIGGGERDKETPISVVGASIIGGETVDAGLWVAFWFFLAQLNFVLGAINLVPLLPFDGGHIAVATYEKIRNMIRSARGMVAAGPVNYLKLMPATYVVLAVVAGYMLLTVTADLVNPLSIFQ
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A probable intramembrane site-2 protease (S2P) that cleaves type-2 transmembrane proteins within their membrane-spanning domains. Degrades PbpB (PBP3, FtsI) under conditions of oxidatives stress degradation is inhibited by Wag31-PbpB interaction. Also cleaves anti-sigma factors RskA, RslA and RslM. Site-1 proteases have not yet been identified in this organism. Regulated intramembrane proteolysis (RIP) occurs when an extracytoplasmic signal (possibly oxidative stress) triggers a concerted proteolytic cascade to transmit information and elicit cellular responses. The membrane-spanning regulatory substrate protein (includes anti-sigma factors RskA, RslA, RsmA, and PbpB) is first cut extracytoplasmically (site-1 protease, S1P), then within the membrane itself (site-2 protease, S2P, this entry), while cytoplasmic proteases finish degrading the regulatory protein, liberating the effector protein (ECF sigma factors SigK, SigL and SigM).
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A0QWG5
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ACYLT_MYCS2
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Phosphatidylinositol mannoside acyltransferase (PIM acyltransferase) (EC 2.3.1.265)
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MTLSGRIPLGGQVTDLGYAAGWRLVRAMPEAMAQGVFGAGARYAARNGGPEQLRRNLARVVGKPPADVPDDLIRASLASYARYWREAFRLPAMDHGRLGEQLDVIDIDHLWSALDAGRGAVLALPHSGNWDMAGVWLVQNYGPFTTVAERLKPESLYRRFVEYRESLGFEVLPLTGGERPPFEVLAERLTDNRPICLMAERDLTRSGVQVDFFGEATRMPAGPAKLAIETGAALFPVHCWFEGDGWGMRVYPELDTSSGDVTAITQALADRFAANIATYPADWHMLQPQWIADLSDERRARLGT
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Catalyzes the transfer of a palmitoyl moiety from palmitoyl-CoA to the 6-position of the mannose ring linked to the 2-position of myo-inositol in phosphatidyl-myo-inositol monomannoside (PIM1) or dimannoside (PIM2).
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A0QWG6
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PIMA_MYCS2
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Phosphatidyl-myo-inositol mannosyltransferase (EC 2.4.1.345) (Alpha-mannosyltransferase) (GDP-mannose-dependent alpha-(1-2)-phosphatidylinositol mannosyltransferase) (Guanosine diphosphomannose-phosphatidyl-inositol alpha-mannosyltransferase) (Phosphatidylinositol alpha-mannosyltransferase) (PI alpha-mannosyltransferase)
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MRIGMVCPYSFDVPGGVQSHVLQLAEVLRDAGHEVSVLAPASPHVKLPDYVVSGGKAVPIPYNGSVARLRFGPATHRKVKKWIAEGDFDVLHIHEPNAPSLSMLALQAAEGPIVATFHTSTTKSLTLSVFQGILRPYHEKIIGRIAVSDLARRWQMEALGSDAVEIPNGVDVASFADAPLLDGYPREGRTVLFLGRYDEPRKGMAVLLAALPKLVARFPDVEILIVGRGDEDELREQAGDLAGHLRFLGQVDDATKASAMRSADVYCAPHLGGESFGIVLVEAMAAGTAVVASDLDAFRRVLADGDAGRLVPVDDADGMAAALIGILEDDQLRAGYVARASERVHRYDWSVVSAQIMRVYETVSGAGIKVQVSGAANRDETAGESV
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Involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM). Catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 2 of the carrier lipid phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). In contrary to PimB, the mannosyltransferase PimA is unable to transfer a mannose residue to the position 6 of the phosphatidyl-myo-inositol of PIM1.
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A0QWT2
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COABC_MYCS2
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Coenzyme A biosynthesis bifunctional protein CoaBC (DNA/pantothenate metabolism flavoprotein) (Phosphopantothenoylcysteine synthetase/decarboxylase) (PPCS-PPCDC) [Includes: Phosphopantothenoylcysteine decarboxylase (PPC decarboxylase) (PPC-DC) (EC 4.1.1.36) (CoaC); Phosphopantothenate--cysteine ligase (EC 6.3.2.5) (CoaB) (Phosphopantothenoylcysteine synthetase) (PPC synthetase) (PPC-S)]
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MSARKRIVVGVAGGIAAYKACTVVRQLTEAGHSVRVVPTESALRFVGAATFEALSGNPVHTGVFTDVHEVQHVRIGQQADLVVIAPATADLLARAVAGRADDLLTATLLTARCPVLFAPAMHTEMWLHPATVDNVATLRRRGAVVLEPASGRLTGADSGPGRLPEAEEITTLAQLLLERADALPYDMAGVKALVTAGGTREPLDPVRFIGNRSSGKQGYAVARVLAQRGADVTLIAGNTAGLIDPAGVEMVHIGSATQLRDAVSKHAPDANVLVMAAAVADFRPAHVAAAKIKKGASEPSSIDLVRNDDVLAGAVRARADGQLPNMRAIVGFAAETGDANGDVLFHARAKLERKGCDLLVVNAVGENRAFEVDHNDGWLLSADGTESALEHGSKTLMATRIVDSIAAFLKSQDG
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Catalyzes two sequential steps in the biosynthesis of coenzyme A. In the first step cysteine is conjugated to 4'-phosphopantothenate to form 4-phosphopantothenoylcysteine. In the second step the latter compound is decarboxylated to form 4'-phosphopantotheine. {ECO:0000255|HAMAP-Rule:MF_02225}.
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A0QX20
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ACNA_MYCS2
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Aconitate hydratase A (ACN) (Aconitase) (EC 4.2.1.3) ((2R,3S)-2-methylisocitrate dehydratase) ((2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate dehydratase) (Iron-responsive protein-like) (IRP-like) (Probable 2-methyl-cis-aconitate hydratase) (EC 4.2.1.99) (RNA-binding protein)
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MSSENTGKSSLNSFGARDTLTVGDQSYEIYRLNAVPGTEKLPYSLKVLAENLLRTEDGANITKDHIEAIANWDPNAEPSIEIQFTPARVIMQDFTGVPCIVDLATMREAVAALGGDPNKVNPLAPAELVIDHSVILDVFGNASAFERNVELEYERNAERYQFLRWGQGAFDDFKVVPPGTGIVHQVNIEYLARTVMVRDGVAYPDTCVGTDSHTTMVNGLGVLGWGVGGIEAEAAMLGQPVSMLIPRVVGFKLSGEIKPGVTATDVVLTVTDMLRRHGVVGKFVEFYGKGVAEVPLANRATLGNMSPEFGSTAAIFPIDEETINYLRLTGRTDEQLALVEAYAKAQGMWHDPEREPVFSEYLELDLSTVVPSISGPKRPQDRIELTDAKNAFRKDIHNYVEQNHPTPETKLDEAVEESFPASDPVSLSFADDGAPDMRPSAANGATGRPTNPVLVHSEERGDFVLDHGAVVVAGITSCTNTSNPSVMLGAALLAKKAVEKGLTTKPWVKTNMAPGSQVVTDYYNKAGLWPYLEKLGYYLGGYGCTTCIGNTGPLPEEISKAINDNDLAVTAVLSGNRNFEGRISPDVKMNYLASPPLVIAYGIAGTMDFDFESDPLGQDSEGNDVFLRDIWPSAAEIEETIASSINREMFTESYADVFKGDDRWRSLPTPEGDTFEWDPASTYVRKAPYFDGMPAEPEPVSDIKGARVLALLGDSVTTDHISPAGAIKPGTPAAQYLDANGVERKDYNSLGSRRGNHEVMIRGTFANIRLRNQLLDDVSGGYTRDFTQPGGPQAFIYDASENYKKAGIPLVVLGGKEYGSGSSRDWAAKGTVLLGVKAVITESFERIHRSNLIGMGVIPLQFPAGESAASLKLDGTETYDIEGIEELNSGKTPKTVHVTATKEDGSKVEFDAVVRIDTPGEADYYRNGGILQYVLRNMLKSSK
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Involved in the catabolism of short chain fatty acids (SCFA) via the tricarboxylic acid (TCA)(acetyl degradation route) and probably via the 2-methylcitrate cycle I (propionate degradation route). Catalyzes the reversible isomerization of citrate to isocitrate via cis-aconitate. The apo form of AcnA functions as a RNA-binding regulatory protein. Could catalyze the hydration of 2-methyl-cis-aconitate to yield (2R,3S)-2-methylisocitrate.
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A0QX22
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RIPA_MYCS2
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Peptidoglycan endopeptidase RipA (EC 3.4.-.-) (Resuscitation-promoting factor interaction partner A) (Rpf-interacting protein A)
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MRRTVRALATRVHGRVCAVPLVVGMLLATALYGGGPAAADPAAPDNLATLVAKVASADQKLQELGAAIQTQQETVNKAIVDVQAARDAAAAAQRELEAGQRGVADANAAIEAAQKRFDSFAAATYMNGPSRSYLTATDPADIVNTTATGQALIASSQQVMAKLQRARTEQVNRESAARLAKEKADQAARDAESSQDNAVAALKQAQQTFNAQQGELERLAAERAAAQAELDSVRKVSATGNAAPAAAPAAAPAPAAAPAPVPNSAPAPVPGAQPNPQAAAGNWDRAPSGPASSGQNWAVWDPTLPAIPSAFVSGDPIAIINAVLGIASTSAQVTADMGRSFLQKLGILPTPTGFTNGAIPRVYGREAVEYVIRRGMSQIGVPYSWGGGNAAGPSRGIDSGAGTVGFDCSGLMLYMFAGVGIKLDHYSGSQYNAGRKIPSSQMRRGDMIFYGPNASQHVAMYLGNGQMLEAPYTGSHVKVSPVRTSGMTPYVTRLIEY
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Peptidoglycan endopeptidase that cleaves the bond between D-glutamate and meso-diaminopimelate. Binds and degrades high-molecular weight peptidoglycan. Required for normal separation of daughter cells after cell division and for cell wall integrity (By similarity). {ECO:0000250, ECO:0000269|PubMed:18463693}.
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A0QXD8
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ELTD_MYCS2
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Erythritol/L-threitol dehydrogenase (EC 1.1.1.-)
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MSNQVPEKMQAVVCHGPHDYRLEEVAVPQRKPGEALIRVEAVGICASDLKCYHGAAKFWGDENRPAWAETMVIPGHEFVGRVVELDDEAAQRWGIAVGDRVVSEQIVPCWECLFCKRGQYHMCQPHDLYGFKRRTPGAMASYMVYPAEALVHKVSPDIPAQHAAFAEPLSCSLHAVERAQITFEDTVVVAGCGPIGLGMIAGAKAKSPMRVIALDMAPDKLKLAEKCGADLTINIAEQDAEKIIKDLTGGYGADVYIEGTGHTSAVPQGLNLLRKLGRYVEYGVFGSDVTVDWSIISDDKELDVLGAHLGPYCWPAAIKMIESGALPMDEICTHQFPLTEFQKGLDLVASGKESVKVSLIPA
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Catalyzes the NAD-dependent reversible oxidation of erythritol and L-threitol. Involved in the degradation pathways of erythritol and L-threitol, that allow M.smegmatis to grow on these compounds as the sole carbon source.
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A0QXE4
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DERK_MYCS2
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D-erythrulose kinase (EC 2.7.1.210)
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MTKLFNDPARFTEDMLVGFLDANSRYVVGVPGGVVRAQTTRPGKVAVVIGGGSGHYPAFCGTVGPGFADGAVVGNIFTSPSAEEAASVARAAHSDAGVLLTTGNYAGDVMNFNLAVDQLRSEGIEAQYFAVTDDVASAERGQEAKRRGIAGDFTVFKCASAAAEEGLDLAGVVRVAEAANAATRTLGVAFDGCTLPGADHPLFTVPEGHMGLGLGIHGEPGVSEEKMPTAAGLAATLVDGVLGDRPDAPEKRIAVILNGLGRTKYEELFVVWGEVSRLLRDRGYTIVEPEVGELVTSLDMAGCSLTVMWLDEELERYWAAPADTPAYKKGAAQQHVSGERRSEATARSASSGPKLAELSDEDGRAGARLVARAFDAMAEALADAEEELGRIDAVAGDGDHGRGMVKGSSAAREAAASALSEGAGQGSVLNAAGKAWAAKAGGTSGVLWGALLTALGARLGDTGRPDSSVIAAGVRDAYDALIRLGGAAPGDKTMLDAMLPFTEELERRVAQDESWQSAWRAAADVATEAARATADLRPKIGRARPLAERSVGTPDAGATSLALCARTVADCVTLSTQGEN
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Catalyzes the phosphorylation of D-erythrulose to D-erythrulose-4P. Involved in the degradation pathways of erythritol and D-threitol, that allow M.smegmatis to grow on these compounds as the sole carbon source.
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A0QXX7
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KATG2_MYCS2
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Catalase-peroxidase 2 (CP 2) (EC 1.11.1.21) (Peroxidase/catalase 2)
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MSSDTSDSRPPNPDTKTASTSESENPAIPSPKPKSGAPLRNQDWWPNQIDVSRLHPHPPQGNPLGEDFDYAEEFAKLDVNALKADLTALMTQSQDWWPADYGHYGGLFIRMSWHSAGTYRIHDGRGGGGQGAQRFAPINSWPDNVSLDKARRLLWPIKQKYGNKISWADLLVFTGNVALESMGFKTFGFGFGREDIWEPEEILFGEEDEWLGTDKRYGGGEQRQLAEPYGATTMGLIYVNPEGPEGQPDPLAAAHDIRETFGRMAMNDEETAALIVGGHTFGKTHGAGDASLVGPEPEAAPIEQQGLGWKSSYGTGKGPDTITSGLEVVWTNTPTKWDNSFLEILYGYEWELTKSPAGAWQFTAKDGAGAGTIPDPFGGPGRNPTMLVTDISMRVDPIYGKITRRWLDHPEELSEAFAKAWYKLLHRDMGPISRYLGPWVAEPQLWQDPVPAVDHPLVDDQDIAALKSTVLDSGLSTGQLIKTAWASAASYRNTDKRGGANGARVRLEPQKNWDVNEPAELATVLPVLERIQQDFNASASGGKKVSLADLIVLAGSAAIEKAAKDGGYNVTVPFAPGRTDASQENTDVESFAVLEPRADGFRNYVRPGEKVQLEKMLLERAYFLGVTAPQLTALVGGLRALDVNHGGTKHGVFTDRPGALTNDFFVNLLDMGTEWKTSETTENVYEGVDRKTGQLKWTATANDLVFGSHSVLRAVAEVYAQSDNGERFVNDFVKAWVKVMNNDRFDLK
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Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. May play a role in the intracellular survival of mycobacteria.
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A0QYC2
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DTHD_MYCS2
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D-threitol dehydrogenase (EC 1.1.1.403)
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MTQAQELSVDFDFRLDGKVALVTGAASGIGAAIASAYATKGARIAAVDLNAEGAEALAAQLGGDRGAHRGFACDVADAASVQAAADAVAAEFGRIDILVNSAGVARLAPAEELSLQDWDSTLAINLSGTFLMCQAVGKRMLEAGGGAIVNMASQAATVALDQHVAYCASKFGVVGVSKVLAAEWGGRGVRVNTISPTVVLTELGHKAWDGPRGDALKKLIPTGRFAYPDEIAAAAVFLASDAAAMINGADLVIDGGYTIK
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Catalyzes the NAD-dependent reversible oxidation of D-threitol. Involved in the degradation pathway of D-threitol, that allows M.smegmatis to grow on this compound as the sole carbon source. Does not catalyze the oxidation of xylitol, L-sorbitol, and L-sorbose.
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A0QYE8
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GUAB1_MYCS2
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GMP reductase (EC 1.7.1.7) (Guanosine 5'-monophosphate reductase) (GMPR)
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MRFLDGHTPAYDLTYNDVFVVPGRSDVASRFDVDLSTVDGSGTTIPVVVANMTAVAGRRMAETVARRGGIVVLPQDLPITAVSETVDFVKSRDLVVDTPVTLSPEDSVSDANALLHKRAHGAAVVVFEGRPIGLVTEANCAGVDRFARVRDIALSDFVTAPVGTDPREVFDLLEHAPIDVAVMTAPDGTLAGVLTRTGAIRAGIYTPAVDAKGRLRIAAAVGINGDVGAKAQALAEAGADLLVIDTAHGHQAKMLDAIKAVASLDLGLPLVAGNVVSAEGTRDLIEAGASIVKVGVGPGAMCTTRMMTGVGRPQFSAVVECAAAARQLGGHVWADGGVRHPRDVALALAAGASNVMIGSWFAGTYESPGDLLFDRDDRPYKESYGMASKRAVAARTAGDSSFDRARKGLFEEGISTSRMSLDPARGGVEDLLDHITSGVRSTCTYVGAANLPELHEKVVLGVQSAAGFAEGHPLPAGW
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Involved in the purine-salvage pathway. Catalyzes the NADPH-dependent conversion of GMP to IMP. Is not essential for viability, but may contribute to the regulation of the purine nucleotide pool by recycling GMP to IMP.
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A0QZ13
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LNT_MYCS2
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Apolipoprotein N-acyltransferase (ALP N-acyltransferase) (EC 2.3.1.269) (LntMs)
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MIPAVTDDDPLEDPLDDDVAPGLDDAEPEPEPRDEHDEPSRPATGSRIGGWVARRGSRFGKGVLDRCAPLSAAIGGGLALWLSFPPIGWWFTAFPGLALLGWVLTRTATTKAGGFGYGVLFGLAFYVPLLPWISGLVGAVPWLALAFAESLFCGLFGLGAVVVVRLPGWPLWFATLWVAAEWAKSTFPFGGFPWGASSYGQTNGPLLALARIGGAPLVSFAVALIGFSLTLLTAQIVWWWRHGHKPGVPAPAVMLPGVAIAASLLVTALVWPQVRQSGTGAGDDTAVTVAAVQGNVPRLGLEFNAQRRAVLDNHVKETLRLADDVKAGRAAQPMFVIWPENSSDIDPLLNADASAQITTAAEAIDAPILVGGVVRADGYTPDNPVANNTVIVWEPTDGPGERHDKQIVQPFGEYLPWRGFFKHLSSYADRAGYFVPGTGTGVVHAAGVPIGITTCWEVIFDRAARESVLNGAQVLAVPSNNATFDEAMSAQQLAFGKLRAVEHDRYVVVAGTTGISAVIAPDGHEISRTEWFQPAYLDNQIRLKTDLTPATKWGPIVQAVLVIAGVAVLLIAILHNGRFAPRMLRRRSATTVKR
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Catalyzes the phospholipid dependent N-acylation of the N-terminal cysteine of apolipoprotein, the last step in lipoprotein maturation. Can transfer a number of fatty acids (C16 and C19, palmitic and probably tuberculostearic acids respectively are shown). Enhances the polyprenol monophosphomannose (PPM) synthase activity of Ppm1 (AC A0QZ12) without itself having PPM synthase catalytic activity.
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A0QZ48
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PUP_MYCS2
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Prokaryotic ubiquitin-like protein Pup (Bacterial ubiquitin-like modifier)
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MAQEQTKRGGGGGEDDDLPGASAAGQERREKLTEETDDLLDEIDDVLEENAEDFVRAYVQKGGQ
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Protein modifier that is covalently attached to lysine residues of substrate proteins, thereby targeting them for proteasomal degradation. The tagging system is termed pupylation. Among the identified substrates are the SodA and Ino1 proteins.
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A0QZ49
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DOP_MYCS2
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Pup deamidase/depupylase (EC 3.4.-.-) (EC 3.5.1.119) (Deamidase of protein Pup)
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MQRIIGTEVEYGISSPSDPTANPILTSTQAVLAYAAAAGIQRAKRTRWDYEVESPLRDARGFDLSRSSGPPPIVDADEVGAANMILTNGARLYVDHAHPEYSAPECTDPMDAVIWDKAGERVMEAAARHVASVPGAAKLQLYKNNVDGKGASYGSHENYLMSRQTPFSAVIAGLTPFMVSRQVVTGSGRVGIGPSGDEPGFQLSQRADYIEVEVGLETTLKRGIINTRDEPHADADKYRRLHVIIGDANLAETSTYLKLGTTSLVLDLIEEGVDLSDLALARPVHAVHVISRDPSLRATVALADGRELTALALQRIYLDRVAKLVDSRDPDPRASHVIETWANVLDLLERDPMECAEILDWPAKLRLLEGFRQRENLTWQAPRLHLVDLQYSDVRLDKGLYNRLVARGSMKRLVTEQQVLDAVENPPTDTRAYFRGECLRRFGADIAAASWDSVIFDLGGDSLVRIPTLEPLRGSKAHVGALLDSVDSAVELVEQLTN
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Specifically catalyzes the deamidation of the C-terminal glutamine of the prokaryotic ubiquitin-like protein Pup to glutamate, thereby rendering Pup competent for conjugation. Probably also displays depupylase (DPUP) activity, removing conjugated Pup from target proteins thus may be involved in the recycling of Pup and may function similarly to deubiquitinases (DUBs) in eukaryotes to prevent or promote proteasomal degradation of certain proteins.
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A0QZY0
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MSHC_MYCS2
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L-cysteine:1D-myo-inositol 2-amino-2-deoxy-alpha-D-glucopyranoside ligase (L-Cys:GlcN-Ins ligase) (EC 6.3.1.13) (Mycothiol ligase) (MSH ligase)
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MQSWSAPAIPVVPGRGPALRLFDSADRQVRPVTPGPTATMYVCGITPYDATHLGHAATYLTFDLVHRLWLDAGHTVQYVQNVTDVDDPLFERAERDGIDWRTLGDRETQLFREDMAALRVLPPHDYVAATDAIAEVVEMVEKLLASGAAYIVEDAEYPDVYFRADATAQFGYESGYDRDTMLTLFAERGGDPDRPGKSDQLDALLWRAERPGEPSWPSPFGRGRPGWHVECSAIALTRIGTGLDIQGGGSDLIFPHHEYSAAHAESVTGERRFARHYVHTGMIGWDGHKMSKSRGNLVLVSQLRAQGVDPSAIRLGLFSGHYREDRFWSNEVLDEANARLARWRSATALPEAPDATDVIARVRQYLADDLDTPKALAALDGWCTDALSYGGHDTESPRLVATTVDALLGVDL
|
Catalyzes the ATP-dependent condensation of GlcN-Ins and L-cysteine to form L-Cys-GlcN-Ins.
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A0R066
|
ILVE_MYCS2
|
Branched-chain-amino-acid aminotransferase (BCAT) (EC 2.6.1.42)
|
MNSGPLEFTVSANTNPATDAVRESILANPGFGKYYTDHMVSIDYTVDEGWHNAQVIPYGPIQLDPSAIVLHYGQEIFEGLKAYRWADGSIVSFRPEANAARLQSSARRLAIPELPEEVFIESLRQLIAVDEKWVPPAGGEESLYLRPFVIATEPGLGVRPSNEYRYLLIASPAGAYFKGGIKPVSVWLSHEYVRASPGGTGAAKFGGNYAASLLAQAQAAEMGCDQVVWLDAIERRYVEEMGGMNLFFVFGSGGSARLVTPELSGSLLPGITRDSLLQLATDAGFAVEERKIDVDEWQKKAGAGEITEVFACGTAAVITPVSHVKHHDGEFTIADGQPGEITMALRDTLTGIQRGTFADTHGWMARLN
|
Catalyzes the reversible transfers of an amino group from glutamate to the alpha-ketoacid of the respective amino acid in the final step in the biosynthesis of branchedchain amino acids. The amino acids can be ranked in the following order with respect to their efficiency as amino donor: Leu > Ile > Val.
|
A0R152
|
RNE_MYCS2
|
Ribonuclease E (RNase E) (EC 3.1.26.12)
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MAEDAHTEDLSTQTPQQEGLPERLRVHSLARVLGTTSRRVLDALAEFDGRQRSAHSTVDKADAERVRAALTESPAAETPPEEAPAAETPVADLVVVQAEQVEVVTVSEAGPAEPAEPAEPEAPAAEAEAEAETEVADEAETPEPTFRGAVLVGDEPESRLILEHANIPPARETQTERPDYLPLFVAPQPVSFEPAVVDDEDEDDDTETGAESDFDSGADSDSDDDQADRPRRRRRGRRGRGRGRGEQNDDATSDADTDSTEDQTDGDEQESGEDSDDSGDEDSTTTEGGTRRRRRRRRRKSGSGDSDDAVSPDDPPNTVVHERAPRTERSDKSDDSEIQGISGSTRLEAKRQRRRDGRDAGRRRPPILSEAEFLARREAVERTMIVRDKVRTEPPHEGARYTQIAVLEDGVVVEHFVTSAASASLVGNIYLGIVQNVLPSMEAAFVDIGRGRNGVLYAGEVNWEAAGLGGQNRKIEQALKPGDYVVVQVSKDPVGHKGARLTTQVSLAGRYLVYVPGASSTGISRKLPDTERQRLKEILREVVPSDAGVIIRTASEGVKEEDIRSDVERLQKRWSEIEAKAAEVTEKKAGAAVALYEEPDVLVKVIRDLFNEDFSSLIVSGDEAWNTINSYVEAVAPDLMPRLTKYEPAGPDAPDVFAVHRIDEQLAKAMDRKVWLPSGGTLVIDRTEAMTVVDVNTGKFTGSGGNLEQTVTRNNLEAAEEIVRQLRLRDIGGIVVIDFIDMVLESNRDLVLRRLTEALARDRTRHQVSEVTSLGLVQLTRKRLGTGLVEAFSTACTHCGGRGIVLHGDPIDSASSNGGRKSDSSGGGGSGGGRRGKRGKKGAARTEEVHVAKVPDHTPGEHPMFKAMAAANGKHEGDEDHEDHEDHETAEDTTAAEVRDDTRDEHDADERAHVVTAAVGAAGDEDLDDSDEDSDLDSDEESDDESDEDEIELDDDEDELDEDIEVIGDSDDSDDSDDSDEDDDSDDSDDDSDEDEDSDSDEDEEPVREVYEPPVTAPRARVRRRAAARPAGPPSHD
|
Endoribonuclease that plays a central role in RNA processing and decay. Plays a major role in pre-16S rRNA maturation, probably generating the mature 5'-end, and a minor role in pre-5S and pre-23S rRNA maturation. Probably also processes tRNA (By similarity). RNase E and HupB jointly contribute to cellular adaptation to changing growth conditions and survival during antibiotic treatment. Overexpression or depletion leads to changes in gene expression overexpression induces metabolic slowdown and cell stress while depleted strains grow less well than induced strains.
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A0R1E8
|
PKS5_MYCS2
|
Mycocerosic acid synthase-like polyketide synthase (MAS-like PKS) (EC 2.3.1.-) (Polyketide synthase Pks5)
|
MTQNCVAPVAIIGMACRLPGAINSPQQLWEALLRGDDFVTEIPTGRWDAEEYYDPEPGVPGRSVSKWGAFLDDPAAFDPEFFGITEREAAAIDPQHRLLLETAWEAVEHSGLNPAGLAGSATGVFMGLTHNDYAHLAADAKALEGPYGFTGTSFSLASGRIAYALGVHGPAITVDTACSSSLSAIHMACRSLHDGESDVALAGGVSVLLEPRKAAGGSAAGMLSPTGHCHAFDTAADGFVSAEGCVVLTLKRLDDAVADGDRILAVIRGTATNQDGRTVNIATPSADAQAKVYRMALKAAGVEPGTVGLVEAHGTGTPVGDPLEFSSLAEVYGTDGPCALGSIKTNFGHTQSAAGALGVMKAVLALQHNVIPQNLHFTRLPDQMAEIETGLFVPETITPWPVREGQPRRAAVSAYGLSGTNVHAVLEQAPESPAETAAEAISPKAGNALVFPVSASSADALRSTAQHLADWLLRSGDGNGRGPAIDLGDLAYTLARRRGFRAARSAVLAGDRGTLVEGLRQIADGEAMPQQAVTNDDRGPVWVFSGQGSQWASMGAELLDREPAFAAAIAELEPLIAAESDFSVTEALTASETVTGIDRVQPTIFAVQVALAAAMRSHGVVPGAVIGHSMGEVAASVVSGALSLEDGVKVICRRTRLMTRIAGSGAMAMVELPAQQVLSELASRGVDDVVLSVVASPQSTVVGGATASVRELIEMWESRGVMAREIAVDVASHSPQVDPILDDLIEALADLDPAEPEIPYYSATLYDPRDYADYDAYYWADNLRHTVRFSAAVQAALEDGHRVFAELSPHPLLTHPVEQTARSLDMPLAVFAAMRRQQEMPHGLLGFVADLHSAGAAVDFSVLYPTGRLLDAPLPAWTHSTLLLDRELESSAPGVPSVSVHPLLGSHVVLPQEPEEHLWQGDVGTEAHPWLSDHRVHQVAVLPGAAYCEMALAAVTPVLGDTGEVHDLKFHDMLLLDDATPVWVSAAVTAPGTAEFGVETHQSGDRTQRATAVLRGDVDAERPAAHSIDALLAAHPNRVDGDELRAGFGTVGIGHGAAFAGLSEAYVATAAEPTVVAAVALPGPLRSGQRGYTVHPALLDACFQSVIAHPEVQNIASGMLLPLGVRRLRAYGSTRNVRYCLSRIVKADSFGVEADLELLDADGTVLLSAMGLQLGTGNSDKAEEERLLDERLLTIEWQQRELPRPEGSETVDAGSWLVILAGDDDENPRAAGVVSALIGAGMPTTTMAWSHDADHDAQAAALTARLDEQPLAGVAVIVGDSETGTDAHDVGADARRGADHVRHLVRIARTLADAVGEPPRLYVVTHRSQHVLDTDEPYLEHSGLRGLIRVVGMEHPRLRATQIDVDDSTAHEALVRQLLSGSPEDETAWRDGQWYAARLCPSPLRAAERRTAVADNASEGMRLVVRNPGDLESMELVTFERGTPGPGQIEVAVKASSINFADVLVAFGRCPSFDGRLPELGSEFGGVVTAVGPGVTTHRVGDRVGGVSANGCWSNFVTCEADLATKLPEGISEHEAAAVGLAYGTVWLGLTELARMSAGDKILIHSATGGVGQAAIAVARAAGAEIYATAGSEKRRQLLRDWGIEHVYDSRTTAFADQIRTDTDGYGVDIVLNSVTGPAQRAGLELLAFGGRFVEIGKRDIYADTRLGLFPFRRNLSFYAVDLALMTVTHPQKIRDLLATVYRLIADGTLPLPEITHYPLEEAATAIRIMGGAQHTGKLVIDIPDTGQSQVVVPPEQVPVFRGDGAYVITGGLGGLGLFLAERMAAAGCGRIVVNSRSAPSTRSSEIIELIRATGADIVVECGDIAEPDTALRLVAAATQTGLPLRGVLHAAAVVEDATLANITDELVEHDWAPKVYGAWNLHQAVQSGGPATSELDWFCAFSSAAALVGSPGQGAYAAANSWLDAFMQWRRAQGLPATSIAWGAWGEIGRGTAMAEGDNAIAPDEGAYAFEAILRHDRVYNGYAPVLGASWLTAFAQRSPFAELFLADTQGASETRKLRSELAALPREEWPTHLRRLIAEQVGLLLRRTVDPDRPLSEYGLDSLGHLELRTRIETETGVRVSAMDMTTIRGLAQRLCEMLDTDDAVSAPS
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Polyketide synthase involved in the biosynthesis of 2,4-dimethyl-2-eicosenoic acid, a lipid component of the lipooligosaccharides (LOS) which are not located at the bacterial surface but rather in deeper compartments of the cell envelope of M.smegmatis.
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A0R2B1
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KGD_MYCS2
|
Multifunctional 2-oxoglutarate metabolism enzyme (2-hydroxy-3-oxoadipate synthase) (HOA synthase) (HOAS) (EC 2.2.1.5) (2-oxoglutarate carboxy-lyase) (2-oxoglutarate decarboxylase) (Alpha-ketoglutarate decarboxylase) (KG decarboxylase) (KGD) (EC 4.1.1.71) (Alpha-ketoglutarate-glyoxylate carboligase) [Includes: 2-oxoglutarate dehydrogenase E1 component (ODH E1 component) (EC 1.2.4.2) (Alpha-ketoglutarate dehydrogenase E1 component) (KDH E1 component); Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex (EC 2.3.1.61) (2-oxoglutarate dehydrogenase complex E2 component) (ODH E2 component) (OGDC-E2) (Dihydrolipoamide succinyltransferase)]
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MSSSPSPFGQNEWLVEEMYRKFRDDPSSVDPSWHEFLVDYSPEPTTDSASNGRTTTAAPVTPPTPAPAPAPEPKAAPKPAAKTEAKPAKPAKSATPAKGDESQILRGAAAAVVKNMNASLEVPTATSVRAIPAKLMIDNRVVINNHLKRTRGGKISFTHLLGYAIVQAVKKFPNMNRHFAVVDGKPTAITPAHTNLGLAIDLQGKDGNRSLVVAAIKRCETMRFGQFIAAYEDIVRRARDGKLTAEDFSGVTISLTNPGTLGTVHSVPRLMQGQGAIIGAGAMEYPAEFQGASEERIADLGIGKLITLTSTYDHRIIQGAESGDFLRTIHQLLLDDDFFDEIFRELGIPYEPVRWRTDNPDSIEDKNARVIELIAAYRNRGHLMADIDPLRLDNTRFRSHPDLDVNSHGLTLWDLDREFKVDGFAGVQRKKLRDILSVLRDAYCRHVGVEYTHILEPEQQRWIQERVETKHDKPTVAEQKYILSKLNAAEAFETFLQTKYVGQKRFSLEGAETVIPMMDAVIDQCAEHGLDEVVIAMPHRGRLNVLANIVGKPYSQIFSEFEGNLNPSQAHGSGDVKYHLGATGTYIQMFGDNDIEVSLTANPSHLEAVDPVLEGLVRAKQDLLDTGEEGSDNRFSVVPLMLHGDAAFAGQGVVAETLNLALLRGYRTGGTIHIVVNNQIGFTTAPTDSRSSEYCTDVAKMIGAPIFHVNGDDPEACAWVARLAVDFRQAFKKDVVIDMLCYRRRGHNEGDDPSMTQPYMYDVIDTKRGSRKAYTEALIGRGDISMKEAEDALRDYQGQLERVFNEVRELEKHEIEPSESVEADQQIPSKLATAVDKAMLQRIGDAHLALPEGFTVHPRVRPVLEKRREMAYEGRIDWAFAELLALGSLIAEGKLVRLSGQDTQRGTFTQRHAVIVDRKTGEEFTPLQLLATNPDGTPTGGKFLVYNSALSEFAAVGFEYGYSVGNPDAMVLWEAQFGDFVNGAQSIIDEFISSGEAKWGQLSDVVLLLPHGHEGQGPDHTSGRIERFLQLWAEGSMTIAMPSTPANYFHLLRRHGKDGIQRPLIVFTPKSMLRNKAAVSDIRDFTESKFRSVLEEPMYTDGEGDRNKVTRLLLTSGKIYYELAARKAKENREDVAIVRIEQLAPLPRRRLAETLDRYPNVKEKFWVQEEPANQGAWPSFGLTLPEILPDHFTGLKRISRRAMSAPSSGSSKVHAVEQQEILDTAFG
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Shows three enzymatic activities that share a first common step, the attack of thiamine-PP on 2-oxoglutarate (alpha-ketoglutarate, KG), leading to the formation of an enamine-thiamine-PP intermediate upon decarboxylation. Thus, displays KGD activity, catalyzing the decarboxylation from five-carbon 2-oxoglutarate to four-carbon succinate semialdehyde (SSA). Also catalyzes C-C bond formation between the activated aldehyde formed after decarboxylation of alpha-ketoglutarate and the carbonyl of glyoxylate (GLX), to yield 2-hydroxy-3-oxoadipate (HOA), which spontaneously decarboxylates to form 5-hydroxylevulinate (HLA). And is also a component of the 2-oxoglutarate dehydrogenase (ODH) complex, that catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). The KG decarboxylase and KG dehydrogenase reactions provide two alternative, tightly regulated, pathways connecting the oxidative and reductive branches of the TCA cycle.
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A0R2E6
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GPGS_MYCS2
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Glucosyl-3-phosphoglycerate synthase (GpgS) (EC 2.4.1.266)
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MGHRWLTDHSWNRPSWTVADLEAAKAGRTVSVVLPALNEEETVGSVVETIKPLLGGLVDELIVLDSGSTDETEIRAVAAGAKVVSREAALPEVPPQPGKGEVLWRSLAATTGDIIAFVDSDLIDPDPMFVPKLLGPLLTCDGVHLVKGFYRRPLKVSGAEDANGGGRVTELVARPLLASLRPELNCVLQPLGGEYAGTRELLTSVPFAPGYGVEIGLLVDTYDRLGLDGIAQVNLGVRAHRNRPLTELASMSRQVIATLLSRCGISDSGVGLTQFFADGDDFTPRVSSVSLADRPPMTTLRPR
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Involved in the biosynthesis of 6-O-methylglucose lipopolysaccarides (MGLPs). Catalyzes the transfer of the glucose moiety from a nuleotide sugar such as UDP-alpha-D-glucose to the position 2 of 3-phospho-D-glycerate (3-PGA) to form glucosyl-3-phosphoglycerate (GPG). It can use UDP-glucose, ADP-glucose and GDP-glucose as sugar donor substrates with decreasing affinity and with 3-PGA as an acceptor. D-glycerate can only be an acceptor with ADP-glucose and at a very low rate.
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A0R2K8
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PIME_MYCS2
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Polyprenol-phosphate-mannose-dependent alpha-(1-2)-phosphatidylinositol pentamannoside mannosyltransferase (EC 2.4.1.-) (Alpha-mannosyltransferase) (Alpha-ManT) (PPM-dependent mannosyltransferase) (Polyprenol-phosphate-mannose alpha-mannosyltransferase) (PPM alpha-mannosyltransferase)
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MRVNGYRGAKVGAVDTTSPPEVPASARLQRLAPMLLVVSILARLAWTYLVPNGANFVDLHVYVGGADALDGPGALYDYVYADQTPDFPLPFTYPPFAAIVFYPLHLLPFGVVAFIWQIGIIAALYGVVRVSQRLMGLQSQRRVAMLWTALGIWTEPLRSTFDYGQVNVVLVLAVLCAVSTTRWWLSGLLVGLAAGIKLTPAVAGLYFLGARRWAAVACSAAVFFATVGVSWLVVGAQARRYFTELLGDADRIGPIGTSFNQSWRGGISRILGHDAGFGPLVLIGIGITAVLALLAWRAIGGAQDRLGGILVVSLFGLVLSPISWTHHWVWLIPLMMWLLHGPLSALRGARILGWGWLALTLLGVPWLLSFAQPTIWEIGRPWYLAWAGLVYIVATLATLGWIAFSRKGSG
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Catalyzes the alpha-1,2 addition of a mannose residue from polyprenol-phosphate-mannose (PPM) to a monoacyl phosphatidylinositol tetramannoside (AcPIM4) to generate a monoacyl phosphatidylinositol pentamannoside (AcPIM5).
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A0R2N3
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NDP_MYCS2
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NAD-dependent protein deacylase Sir2 (EC 2.3.1.286) (Regulatory protein SIR2 homolog)
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MQVTVLSGAGISAESGVPTFRDAETGLWAQVDPYEISSTDGWQRNPEKVWAWYLWRHYMMARVAPNEAHRTVAAWEDHLDVRVVTQNIDDLHERAGSTNVYHLHGSLFEFRCDACGSAFEGNLPEMPEPVETIDPPVCPCSGLIRPSVVWFGEPLPDAAWNRSVLAVSSADVVIVVGTSSIVYPAAGLPEAALAAGKPVIEVNPERTPLSDSATVSLRETASEALPTLLQRLPELLNRSA
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NAD-dependent lysine deacetylase and desuccinylase that specifically removes acetyl and succinyl groups on target proteins. Modulates the activities of several proteins which are inactive in their acylated form. {ECO:0000255|HAMAP-Rule:MF_01121}. Involved in non-homologous end joining (NHEJ) repair of blunt, 5' overhang and 3' overhang DNA double strand breaks (DSB). Overexpression increases the efficiency of NHEJ of the above DSBs 2-fold with no effect on repair fidelity.
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A0R3F9
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PAT_MYCS2
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Acetyltransferase Pat (EC 2.3.1.-) (GCN5-related N-acetyltransferase) (GNAT) (Protein acetyltransferase) (Pat)
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MAELTEVRAADLAALEFFTGCRPSALEPLATQLRPLKAEPGQVLIRQGDPALTFMLIESGRVQVSHAVADGPPIVLDIEPGLIIGEIALLRDAPRTATVVAAEPVIGWVGDRDAFDTILHLPGMFDRLVRIARQRLAAFITPIPVQVRTGEWFYLRPVLPGDVERTLNGPVEFSSETLYRRFQSVRKPTRALLEYLFEVDYADHFVWVMTEGALGPVIADARFVREGHNATMAEVAFTVGDDYQGRGIGSFLMGALIVSANYVGVQRFNARVLTDNMAMRKIMDRLGAVWVREDLGVVMTEVDVPPVDTVPFEPELIDQIRDATRKVIRAVSQ
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Catalyzes specifically the acetylation of the epsilon-amino group of a highly conserved lysine residue in acetyl-CoA synthetase (ACS) and of the universal stress protein (USP) MSMEG_4207. Acetylation results in the inactivation of ACS activity and could be important for mycobacteria to adjust to environmental changes.
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A0R3R7
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LIGD_MYCS2
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Multifunctional non-homologous end joining protein LigD (NHEJ DNA polymerase) [Includes: DNA repair polymerase (Pol) (Polymerase/primase); 3'-phosphoesterase (3'-ribonuclease/3'-phosphatase) (PE); DNA ligase (Lig) (EC 6.5.1.1) (Polydeoxyribonucleotide synthase [ATP])]
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MARHPWGMERYERVRLTNPDKVLYPATGTTKAEVFDYYLSIAQVMVPHIAGRPVTRKRWPNGVAEEAFFEKQLASSAPSWLERGSITHKSGTTTYPIINTREGLAWVAQQASLEVHVPQWRFEDGDQGPATRIVFDLDPGEGVTMTQLCEIAHEVRALMTDLDLETYPLTSGSKGLHLYVPLAEPISSRGASVLARRVAQQLEQAMPKLVTATMTKSLRAGKVFLDWSQNNAAKTTIAPYSLRGRDHPTVAAPRTWDEIADPELRHLRFDEVLDRLDEYGDLLAPLDADAPIADKLTTYRSMRDASKTPEPVPKEIPKTGNNDKFVIQEHHARRLHYDLRLERDGVLVSFAVPKNLPETTAENRLAVHTEDHPIEYLAFHGSIPKGEYGAGDMVIWDSGSYETEKFRVPEELDNPDDSHGEIIVTLHGEKVDGRYALIQTKGKNWLAHRMKDQKNARPEDFAPMLATEGSVAKYKAKQWAFEGKWDGYRVIIDADHGQLQIRSRTGREVTGEYPQFKALAADLAEHHVVLDGEAVALDESGVPSFGQMQNRARSTRVEFWAFDILWLDGRSLLRAKYSDRRKILEALADGGGLIVPDQLPGDGPEAMEHVRKKRFEGVVAKKWDSTYQPGRRSSSWIKDKIWNTQEVVIGGWRQGEGGRSSGIGALVLGIPGPEGLQFVGRVGTGFTEKELSKLKDMLKPLHTDESPFNAPLPKVDARGVTFVRPELVGEVRYSERTSDGRLRQPSWRGLRPDKTPDEVVWE
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With Ku forms a non-homologous end joining (NHEJ) repair enzyme which repairs blunt-end and 5'-overhang DNA double strand breaks (DSB) with about 50% fidelity, and DSB with non-complementary 3' ends. Plays a partial role in NHEJ during 3'-overhang repair. NHEJ repairs DSB with blunt ends and 5' overhangs with a high level of nucleotide insertion/deletion, without a need for microhomology. Acts as a DNA ligase on singly nicked dsDNA, as a DNA-directed DNA polymerase on 5' overhangs, and adds non-templated nucleotides to 3' overhangs (terminal transferase). Fills in gaps in dsDNA, prefers a 5'-phosphate in the gap. Site-directed mutations leading to ligase loss alter the bias from insertion to deletion mutations, and indicate another ligase (LigC1 and/or LigC2) can compensate. The preference of the polymerase domain for rNTPs over dNTPs may be advantageous in dormant cells, where the dNTP pool may be limiting. {ECO:0000250, ECO:0000269|PubMed:15778718, ECO:0000269|PubMed:16446439, ECO:0000269|PubMed:16476729, ECO:0000269|PubMed:16949369, ECO:0000269|PubMed:17174332, ECO:0000269|PubMed:17360246, ECO:0000269|PubMed:18281464}. The ligase activity is required for replication of viruses with short cos ends (4 bases) such as Mycobacterium phage Omega and Corndog, but not D29 which has a 9 base cos end. Stimulates dsDNA end joining by LigD when expressed with endogenous or Mycobacterium phage Omega Ku, can reconstitute NHEJ in S.cerevisiae.
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A0R4M9
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OTSA_MYCS2
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Trehalose-6-phosphate synthase (TPS) (EC 2.4.1.15) (EC 2.4.1.347) (Alpha,alpha-trehalose-phosphate synthase [UDP-forming]) (Osmoregulatory trehalose synthesis protein A) (OtsA)
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MSPESGHETISGTSDFVVVANRLPVDLERLPDGTTRWKRSPGGLVTALEPLLRKRRGSWIGWAGVADSDEEPIVQDGLQLHPVRLSADDVAKYYEGFSNATLWPLYHDLIVKPEYHREWWDRYVEVNRRFAEATARAAAEGATVWIQDYQLQLVPKMLRMLRPDVTIGFFLHIPFPPVELFMQMPWRTEIVEGLLGADLVGFHLPGGAQNFLVLSRRLVGANTSRASIGVRSRFGEVQVGFRTVKVGAFPISIDSAELDGKARNRAIRQRARQIRAELGNPRKIMLGVDRLDYTKGIDVRLRALSELLEEKRIKRDDTVLVQLATPSRERVESYIAMREDIERQVGHINGEYGEVGHPIVHYLHRPIPRDELIAFFVAADVMLVTPLRDGMNLVAKEYVACRSDLGGALVLSEFTGAAAELRQAYLVNPHDLEGVKDKIEAAVNQNPEEGKRRMRALRRQVLAHDVDRWARSFLDALAATGETGDSGVTGESTPAPESDSGSF
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Involved in the production of glycogen and alpha-glucan via the TreS-Pep2 branch involved in the biosynthesis of maltose-1-phosphate (M1P), and probably in the osmoprotection via the biosynthesis of trehalose (Ref.4, PubMed:27513637). Catalyzes the transfer of glucose from UDP-glucose (UDP-Glc) to glucose-6-phosphate (Glc-6-P) to form trehalose-6-phosphate (Ref.4). ADP-Glc, CDP-Glc, GDP-Glc and TDP-Glc are also glucosyl donors, however, when the pyrimidine sugar nucleotides (CDP-Glc, TDP-Glc and UDP-Glc) are used as substrates, there is an absolute requirement for a high molecular weight polyanion for activity (Ref.4).
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A0R4Q6
|
CP142_MYCS2
|
Steroid C26-monooxygenase (EC 1.14.15.28) (Cholest-4-en-3-one C26-monooxygenase) (Cholest-4-en-3-one C26-monooxygenase [(25R)-3-oxocholest-4-en-26-oate forming]) (Cholesterol C26-monooxygenase) (Cholesterol C26-monooxygenase [(25R)-3beta-hydroxycholest-5-en-26-oate forming]) (Cytochrome P450 142) (Steroid C27-monooxygenase)
|
MTQMLTRPDVDLVNGMFYADGGAREAYRWMRANEPVFRDRNGLAAATTYQAVLDAERNPELFSSTGGIRPDQPGMPYMIDMDDPQHLLRRKLVNAGFTRKRVMDKVDSIGRLCDTLIDAVCERGECDFVRDIAAPLPMAVIGDMLGVLPTERDMLLKWSDDLVCGLSSHVDEAAIQKLMDTFAAYTEFTKDVITKRRAEPTDDLFSVLVNSEVEGQRMSDDEIVFETLLILIGGDETTRHTLSGGTEQLLRHRDQWDALVADVDLLPGAIEEMLRWTSPVKNMCRTLTADTVFHGTELRAGEKIMLMFESANFDESVFGDPDNFRIDRNPNSHVAFGFGTHFCLGNQLARLELRLMTERVLRRLPDLRLADDAPVPLRPANFVSGPESMPVVFTPSAPVLA
|
Involved in the utilization of cholesterol as the sole carbon and energy source by degrading the side chain. Primarily catalyzes the sequential oxidation of the terminal methyl of cholest-4-en-3-one into (25R)-26-hydroxycholest-4-en-3-one (alcohol), (25R)-26-oxocholest-4-en-3-one (aldehyde), to finally yield the carboxylic acid (25R)-3-oxocholest-4-en-26-oate. Also able to sequentially oxidize cholesterol itself, not only cholest-4-en-3-one.
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A0R4Y3
|
CP125_MYCS2
|
Steroid C26-monooxygenase (EC 1.14.15.29) (Cholest-4-en-3-one C26-monooxygenase) (Cholest-4-en-3-one C26-monooxygenase [(25S)-3-oxocholest-4-en-26-oate forming]) (Cholesterol C26-monooxygenase) (Cholesterol C26-monooxygenase [(25S)-3beta-hydroxycholest-5-en-26-oate forming]) (Cytochrome P450 125) (Steroid C27-monooxygenase)
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MPTPNIPSDFDFLDATLNLERLPVEELAELRKSEPIHWVDVPGGTGGFGDKGYWLVTKHADVKEVSRRSDVFGSSPDGAIPVWPQDMTREAVDLQRAVLLNMDAPQHTRLRKIISRGFTPRAIGRLEDELRSRAQKIAQTAAAQGAGDFVEQVSCELPLQAIAELLGVPQDDRDKLFRWSNEMTAGEDPEYADVDPAMSSFELISYAMKMAEERAVNPTEDIVTKLIEADIDGEKLSDDEFGFFVVMLAVAGNETTRNSITHGMIAFAQNPDQWELYKKERPETAADEIVRWATPVSAFQRTALEDVELGGVQIKKGQRVVMSYRSANFDEEVFEDPHTFNILRSPNPHVGFGGTGAHYCIGANLARMTINLIFNAIADNMPDLKPIGAPERLKSGWLNGIKHWQVDYTGAGKASVSGAPGTCPVAH
|
Involved in the utilization of cholesterol as the sole carbon and energy source by degrading the side chain. Primarily catalyzes the sequential oxidation of the terminal methyl of cholest-4-en-3-one into (25S)-26-hydroxycholest-4-en-3-one (alcohol), (25S)-26-oxocholest-4-en-3-one (aldehyde), to finally yield the carboxylic acid (25S)-3-oxocholest-4-en-26-oate. Also able to sequentially oxidize cholesterol itself, not only cholest-4-en-3-one.
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A0R564
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DISA_MYCS2
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DNA integrity scanning protein DisA (Cyclic-di-AMP synthase) (c-di-AMP synthase) (Diadenylate cyclase) (EC 2.7.7.85)
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MAVKSGARSGRNVVHLARPTLRETLGRLAPGTPLRDGLERILRGRTGALIVLGYDDSVEAICDGGFVLDVRYAPTRLRELSKMDGAVVLSSDGSRILRANVQLVPDPSIPTDESGTRHRSAERTAIQTGYPVISVSHSMSIVTVYVAGERHVVPDSATILSRANQTIATLERYKGRLDEVSRQLSTAEIEDFVTLRDVMTVVQRLEMVRRISLEIDADVVELGTDGRQLKLQLDELVGDNETARELIVRDYHANPDPPTAAQVAATLEELDSLSDSELLDFTVLARVFGYPSTAEAQDSAMSSRGYRAMAAIPRLQFAHVDLLVRSFGSLQNLLAASADDLQSVDGIGSMWARHIREGLSLLAESTIADRLA
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Participates in a DNA-damage check-point. DisA forms globular foci that rapidly scan along the chromosomes searching for lesions. {ECO:0000255|HAMAP-Rule:MF_01438}. Has also diadenylate cyclase activity, catalyzing the condensation of 2 ATP molecules into cyclic di-AMP (c-di-AMP). c-di-AMP likely acts as a signaling molecule that may couple DNA integrity with a cellular process. {ECO:0000255|HAMAP-Rule:MF_01438, ECO:0000269|PubMed:23760274}.
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A0R5D9
|
TOP1_MYCS2
|
DNA topoisomerase 1 (EC 5.6.2.1) (DNA topoisomerase I)
|
MAGGDRGSGGTGNVRRLVIVESPTKARKIAGYLGSNYVVESSRGHIRDLPRNAADVPAKFKSEPWARLGVNVDQNFEPLYIVSPEKKSTVTELKGLLKDVDELYLATDGDREGEAIAWHLLETLKPRVPVKRMVFHEITEPAIRNAAENPRDLDIALVDAQETRRILDRLYGYEVSPVLWKKVAPKLSAGRVQSVATRIIVQRERERMAFHSASYWDVTAELDASVSDPSASPPKFTAKLNTVDGRRVATGRDFDSLGQLKRPDEVLVLDEASAGALASGLRGAQLAVTSVEQKPYTRRPYAPFMTSTLQQEAARKLRFSSERTMSIAQRLYENGYITYMRTDSTTLSESAINAARTQARQLYGEEYVHPSPRQYTRKVKNAQEAHEAIRPAGDVFQTPGQLHSALDTDEFRLYELIWQRTVASQMADARGTTLSLRIGGSASSGEQVVFNASGRTITFPGFLKAYVESIDELAGGESDDAESRLPNLTQGQRVDAADLSADGHQTSPPARYTEASLIKALEELGIGRPSTYSSIIKTIQDRGYVQKKGSALVPSWVAFAVVGLLEQHFGRLVDYDFTAAMEDELDEIANGQEQRTNWLNNFYFGGEHGVEGSIARAGGLKQLVGGNLEGIDAREVNSIKVFDDSEGRPVYVRVGRNGPYLERMVDDPDNPGEQKPQRANLKEDLTPDELTPELAEKLFATPQEGRSLGIDPETGHEIVAKDGRFGPYVTEVLPEPEDGGDDGTAGTPAKKGKKPTGPKPRTGSLFRSMDLETVTLEDALKLLSLPRVVGVDPTTNEEITAQNGRYGPYLKRGTDSRSLATEDQIFTITLDEALKIYAEPKRRGRQAASAPPLRELGNDPVSGKPMVIKDGRFGPYVTDGETNASLRKGDDVLTITDERASELLADRRARGPVKKKAPAKKAAKKAPAKKAAAKKA
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Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA supercoils. Finally, in the religation step, the DNA 3'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone (By similarity). {ECO:0000255|HAMAP-Rule:MF_00952, ECO:0000269|PubMed:9593741}. Relaxes negatively (but not positively) supercoiled DNA, concatanates and knots circular ssDNA at 52 but not 37 degrees Celsius. Preferentially nicks supercoiled DNA at C(G/T)CTT, cutting between the TT residues, binds ss and dsDNA with the recognition site.
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A0R5M8
|
EGTD_MYCS2
|
Histidine N-alpha-methyltransferase (EC 2.1.1.44) (Histidine trimethyltransferase)
|
MTLSLANYLAADSAAEALRRDVRAGLTAAPKSLPPKWFYDAVGSDLFDQITRLPEYYPTRTEAQILRTRSAEIIAAAGADTLVELGSGTSEKTRMLLDAMRDAELLRRFIPFDVDAGVLRSAGAAIGAEYPGIEIDAVCGDFEEHLGKIPHVGRRLVVFLGSTIGNLTPAPRAEFLSTLADTLQPGDSLLLGTDLVKDTGRLVRAYDDAAGVTAAFNRNVLAVVNRELSADFDLDAFEHVAKWNSDEERIEMWLRARTAQHVRVAALDLEVDFAAGEEMLTEVSCKFRPENVVAELAEAGLRQTHWWTDPAGDFGLSLAVR
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Catalyzes the SAM-dependent triple methylation of the alpha-amino group of histidine to form hercynine, a step in the biosynthesis pathway of ergothioneine. Among all the proteinogenic amino acids, only L-histidine is a substrate.
|
A0R607
|
DPRE1_MYCS2
|
Decaprenylphosphoryl-beta-D-ribose oxidase (EC 1.1.98.3) (Decaprenylphospho-beta-D-ribofuranose 2-dehydrogenase) (Decaprenylphosphoryl-beta-D-ribofuranose 2'-epimerase subunit DprE1) (Decaprenyl-phosphoribose 2'-epimerase subunit 1) (Decaprenylphosphoryl-beta-D-ribofuranose 2'-oxidase) (Decaprenylphosphoryl-beta-D-ribose 2-epimerase flavoprotein subunit) (FAD-dependent decaprenylphosphoryl-beta-D-ribofuranose 2-oxidase)
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MSTTEFPTTTKRLMGWGRTAPTVASVLSTSDPEVIVRAVTRAAEEGGRGVIARGLGRSYGDNAQNGGGLVIDMPALNRIHSIDSGTRLVDVDAGVSLDQLMKAALPHGLWVPVLPGTRQVTVGGAIGCDIHGKNHHSAGSFGNHVRSMELLTANGEVRHLTPAGPDSDLFWATVGGNGLTGIILRATIEMTPTETAYFIADGDVTGSLDETIAFHSDGSEANYTYSSAWFDAISKPPKLGRAAISRGSLAKLDQLPSKLQKDPLKFDAPQLLTLPDIFPNGLANKFTFMPIGELWYRKSGTYRNKVQNLTQFYHPLDMFGEWNRAYGSAGFLQYQFVVPTEAVEEFKSIIVDIQRSGHYSFLNVFKLFGPGNQAPLSFPIPGWNVCVDFPIKAGLHEFVTELDRRVLEFGGRLYTAKDSRTTAETFHAMYPRIDEWIRIRRSVDPDGVFASDMARRLQLL
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Component of the DprE1-DprE2 complex that catalyzes the 2-step epimerization of decaprenyl-phospho-ribose (DPR) to decaprenyl-phospho-arabinose (DPA), a key precursor that serves as the arabinose donor required for the synthesis of cell-wall arabinans. DprE1 catalyzes the first step of epimerization, namely FAD-dependent oxidation of the C2' hydroxyl of DPR to yield the keto intermediate decaprenyl-phospho-2'-keto-D-arabinose (DPX). The intermediate DPX is then transferred to DprE2 subunit of the epimerase complex, most probably through a 'substrate channel' at the interface of DprE1-DprE2 complex (By similarity). Can also use farnesyl-phosphoryl-beta-D-ribofuranose (FPR) as substrate in vitro. Appears to be essential for the growth of M.smegmatis.
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A0R618
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FAA32_MYCS2
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Long-chain-fatty-acid--AMP ligase FadD32 (FAAL) (EC 6.2.1.20) (Acyl-AMP synthetase)
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MPFHNPFIKDGQIKFPDGSSIVAHVERWAKVRGDKLAYRFLDFSTERDGVPRDLTWAQFSARNRAVAARLQQVTQPGDRVAILCPQNLDYLVAFFGALYAGRIAVPLFDPSEPGHVGRLHAVLDNCHPSAILTTTEAAEGVRKFFRTRPANQRPRVIAVDAVPDDVASTWVNPDEPDETTIAYLQYTSGSTRIPTGVQITHLNLATNVVQVIEALEGEEGDRGLSWLPFFHDMGLITALLAPMIGHYFTFMTPAAFVRRPERWIRELARKEGDTGGTISVAPNFAFDHAAARGVPKPGSPPLDLSNVKAVLNGSEPISAATVRRFNEAFGPFGFPPKAIKPSYGLAEATLFVSTTPSAEEPKIITVDRDQLNSGRIVEVDADSPKAVAQASAGKVGIAEWAVIVDAESATELPDGQVGEIWISGQNMGTGYWGKPEESVATFQNILKSRTNPSHAEGATDDATWVRTGDYGAFYDGDLYITGRVKDLVIIDGRNHYPQDLEYSAQEASKAIRTGYVAAFSVPANQLPDEVFENAHSGIKRDPDDTSEQLVIVAERAPGAHKLDIGPITDDIRAAIAVRHGVTVRDVLLTAAGAIPRTSSGKIGRRACRAAYLDGSLRAGKVANDFPDATD
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Involved in the biosynthesis of mycolic acids (By similarity). Catalyzes the activation of long-chain fatty acids as acyl-adenylates (acyl-AMP), which are then transferred to the phosphopantetheine arm of the polyketide synthase Pks13 for further chain extension (By similarity). Can use decanoate (C10), dodecanoate (C12) and tetradecanoate (C14).
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A0R6D0
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NFNB_MYCS2
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Nitroreductase NfnB (NR NfnB) (EC 1.-.-.-) (FMN-dependent NAD(P)H nitroreductase)
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MSVPTLPTGPTVDLAQAAERLIKGRRAVRAFRPDEVPEETMRAVFELAGHAPSNSNTQPWHVEVVSGAARDRLAEALVTAHAEERVTVDFPYREGLFQGVLQERRADFGSRLYAALGIARDQTDLLQGYNTESLRFYGAPHVAMLFAPNNTEARIAGDMGIYAQTLMLAMTAHGIASCPQALLSFYADTVRAELGVENRKLLMGISFGYADDTAAVNGVRIPRAGLSETTRFSR
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Confers resistance to antitubercular drugs benzothiazinone (BTZ) and dinitrobenzamide (DNB). Inactivates BTZ and DNB by reducing an essential nitro group of these compounds to amino group or to hydroxyl amine, respectively, using NADH or NADPH as source of reducing equivalents two electrons are transferred. Able to reduce the nitro group of bicyclic nitroimidazole PA-824, but not of quinone menadione, nitrofurazone, methyl-4-nitrobenzoate, 4-nitrobenzene methyl sulfonate or 4-nitroacetophenone.
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A0R6E0
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TRES_MYCS2
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Trehalose synthase/amylase TreS (EC 3.2.1.1) (EC 5.4.99.16) (Maltose alpha-D-glucosyltransferase) (MTase)
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MEEHTQGSHVEAGIVEHPNAEDFGHARTLPTDTNWFKHAVFYEVLVRAFYDSNADGIGDLRGLTEKLDYIKWLGVDCLWLPPFYDSPLRDGGYDIRDFYKVLPEFGTVDDFVTLLDAAHRRGIRIITDLVMNHTSDQHEWFQESRHNPDGPYGDFYVWSDTSDRYPDARIIFVDTEESNWTFDPVRRQFYWHRFFSHQPDLNYDNPAVQEAMLDVLRFWLDLGIDGFRLDAVPYLFEREGTNCENLPETHAFLKRCRKAIDDEYPGRVLLAEANQWPADVVAYFGDPDTGGDECHMAFHFPLMPRIFMAVRRESRFPISEILAQTPPIPDTAQWGIFLRNHDELTLEMVTDEERDYMYAEYAKDPRMKANVGIRRRLAPLLENDRNQIELFTALLLSLPGSPVLYYGDEIGMGDIIWLGDRDSVRTPMQWTPDRNAGFSKATPGRLYLPPNQDAVYGYHSVNVEAQLDSSSSLLNWTRNMLAVRSRHDAFAVGTFRELGGSNPSVLAYIREVTRQQGDGGAKTDAVLCVNNLSRFPQPIELNLQQWAGYIPVEMTGYVEFPSIGQLPYLLTLPGHGFYWFQLREPDPEPGAQQ
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Catalyzes the reversible interconversion of maltose and trehalose by transglucosylation. Maltose is the preferred substrate. To a lesser extent, also displays amylase activity, catalyzing the endohydrolysis of (1->4)-alpha-D-glucosidic linkages in glycogen and maltooligosaccharides such as maltoheptaose, to produce maltose which then can be converted to trehalose. TreS plays a key role in the utilization of trehalose for the production of glycogen and alpha-glucan via the TreS-Pep2 branch involved in the biosynthesis of maltose-1-phosphate (M1P). Might also function as a sensor and/or regulator of trehalose levels within the cell. Thus, when trehalose levels in the cell become dangerously low, TreS can expedite the conversion of glycogen to maltose via its amylase activity and then convert the maltose to trehalose but this enzyme also can expedite or promote the conversion of trehalose to glycogen when cytoplasmic trehalose levels become too high. Is also able to catalyze the hydrolytic cleavage of alpha-aryl glucosides, as well as alpha-glucosyl fluoride in vitro.
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A0R758
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LERK_MYCS2
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L-erythrulose 1-kinase (EC 2.7.1.209)
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MTYLLNSPDDFADEAVRGLVAANPDLLTEVPGGVVRSTETPKGQPALVIGGGSGHYPAFAGWVGPGMGHGAPCGNIFSSPSASEVYSVVRNAENGGGVILGFGNYAGDVLHFGLAAEKLRHEGIDVRIVTVSDDIASNSPENHRDRRGVAGDLPVFKIAGAAIEAGADLDEAERVAWKANDATRSFGLAFEGCTLPGATEPLFHVEKGWMGVGLGIHGEPGVRDNRLGTAAEVADMLFDEVTAEEPPRGENGYDGRVAVILNGLGTVKYEELFVVYGRIAERLAQQGFTVVRPEVGEFVTSLDMAGVSLTMVFLDDELERLWTAPVETPAYRRGAMPAVDRTPRTTTWDAAETTIPEASEGSRECARNIVAVLETFQQVCADNEAELGRIDAVAGDGDHGQGMSFGSRGAAQAARDAVDRNAGARTTLLLAGQAWADAAGGTSGALWGAALTSAGGVFSDTDGADEQAAVDAICAGIDAILRLGGAQPGDKTMVDAAVPFRDALVKAFDTQAGPAITSAARVAREAAEKTADITARRGRARVLGEKSVGTPDPGALSFAMLMKALGEHLTR
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Kinase that has a preference for L-erythrulose, producing L-erythrulose-1P. Involved in the degradation pathway of L-threitol, that allows M.smegmatis to grow on this compound as the sole carbon source. Is also able to phosphorylate D-erythrulose and dihydroxyacetone in vitro.
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A0RV30
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FBPAP_CENSY
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Fructose-1,6-bisphosphate aldolase/phosphatase (FBP A/P) (FBP aldolase/phosphatase) (EC 3.1.3.11) (EC 4.1.2.13)
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MRITVSAIKADVGGIGGHTLPSSGLLDAVRRKVSSSSLLIDHYIGYCGDDVHIVMTHTRGTDNSDIHKLAWDAFMEGTRVAKEEGLYGAGQDLLRDSFSGNVKGMGPGVAELEFEERANEAFTVFAADKTEPGAFNYPFYRMFVDSLSNTGLIVNKSLAEGVVINIMDVSKARTARLVLWEDKPTIEAALMYPGRFVVSSVETRDGEPIASASTDRLHNIAGTYVGKDDPICLVRTQKRFPATEEAGSCFNNPHYVAGNTRGSHHMPLMPVRLNSPASINFCIPIVEALVFSMHEGRLTGPFDGFSTPDWDDVRRTATRRAHAMRRQGFVHPATLVPDELEYAEGYRSRMDVLDSKMVPLKDSGPAGTGRAYEDPD
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Catalyzes two subsequent steps in gluconeogenesis: the aldol condensation of dihydroxyacetone phosphate (DHAP) and glyceraldehyde-3-phosphate (GA3P) to fructose-1,6-bisphosphate (FBP), and the dephosphorylation of FBP to fructose-6-phosphate (F6P).
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A0S864
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3NBA_BOIIR
|
Irditoxin subunit A (IrTxA)
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MKTLLLAVAVVAFVCLGSADQLGLGRQQIDWGQGQAVGPPYTLCFECNRMTSSDCSTALRCYRGSCYTLYRPDENCELKWAVKGCAETCPTAGPNERVKCCRSPRCNDD
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This bird and reptile-specific postsynaptic neurotoxin inhibits the chick muscle alpha-1-beta-1-gamma-delta (CHRNA1-CHRNB1-CHRNG-CHNRD) nicotinic acetylcholine receptor (nAChR) 100-fold more compared with the mouse receptor. In vivo, produces rapid flaccid paralysis, dyspnea and increased respiratory rate in geckos. At sublethal doses geckos were immobilized for up to three days and then recovered. Chicks injected with lethal doses showed rapid onset of inactivity, dyspnea and neck droop, and no extended paralysis with survival was seen.
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A0S865
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3NBB_BOIIR
|
Irditoxin subunit B (IrTxB)
|
MKTLLLAVAVVAFVCLGSADQLGLGRQQIDWGKGQAKGPPYTLCFECNRETCSNCFKDNRCPPYHRTCYTLYRPDGNGEMKWAVKGCAKTCPTAQPGESVQCCNTPKCNDY
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This bird and reptile-specific postsynaptic neurotoxin inhibits the chick muscle alpha-1-beta-1-gamma-delta (CHRNA1-CHRNB1-CHRNG-CHRND) nicotinic acetylcholine receptor (nAChR) 100-fold more compared with the mouse receptor. In vivo, produces rapid flaccid paralysis, dyspnea and increased respiratory rate in geckos. At sublethal doses geckos were immobilized for up to three days and then recovered. Chicks injected with lethal doses showed rapid onset of inactivity, dyspnea and neck droop, and no extended paralysis with survival was seen.
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A0SVK0
|
DOG1_ARATH
|
Protein DELAY OF GERMINATION 1 (GLUCOSE SENSING QTL 5)
|
MGSSSKNIEQAQDSYLEWMSLQSQRIPELKQLLAQRRSHGDEDNDNKLRKLTGKIIGDFKNYAAKRADLAHRCSSNYYAPTWNSPLENALIWMGGCRPSSFFRLVYALCGSQTEIRVTQFLRNIDGYESSGGGGGASLSDLSAEQLAKINVLHVKIIDEEEKMTKKVSSLQEDAADIPIATVAYEMENVGEPNVVVDQALDKQEEAMARLLVEADNLRVDTLAKILGILSPVQGADFLLAGKKLHLSMHEWGTMRDRRRRDCMVDTEVIFDACTTVNSGPRPTETTNNERN
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Required for the induction of seed dormancy. The level of DOG1 protein in freshly harvested seeds determines the level of seed dormancy. Determines the temperature window for germination by regulating the expression of micropylar endosperm-weakening genes through temperature control of the gibberellins metabolism. Regulates seed dormancy and flowering time through an influence on levels of microRNAs miR156 and miR172. Regulator of seed maturation interfering with abscisic acid signaling components and activating ABI5. In cv. Cvi-1, enhances glucose induction of ABI4.
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A0SYQ0
|
PTGES_CANLF
|
Prostaglandin E synthase (EC 5.3.99.3) (Glutathione peroxidase PTGES) (EC 1.11.1.-) (Glutathione transferase PTGES) (EC 2.5.1.18) (Microsomal prostaglandin E synthase 1) (MPGES-1)
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MPPPVLALVSGQALPAFLLCSTLLVIKMYVVAVITGQVRLRKKAFANPEDALRHGGLQYCRSDQDVDRCLRAHRNDMETIYPFLFLGFVYSFLGPDPFIAQMHFLVFFLGRMVHTVAYLGKLRAPTRSLAYTVAQLPCASMALQIVWEAACHL
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Terminal enzyme of the cyclooxygenase (COX)-2-mediated prostaglandin E2 (PGE2) biosynthetic pathway. Catalyzes the glutathione-dependent oxidoreduction of prostaglandin endoperoxide H2 (PGH2) to prostaglandin E2 (PGE2) in response to inflammatory stimuli (By similarity). Plays a key role in inflammation response, fever and pain (By similarity). Catalyzes also the oxidoreduction of endocannabinoids into prostaglandin glycerol esters and PGG2 into 15-hydroperoxy-PGE2. In addition, displays low glutathione transferase and glutathione-dependent peroxidase activities, toward 1-chloro-2,4-dinitrobenzene and 5-hydroperoxyicosatetraenoic acid (5-HPETE), respectively (By similarity).
|
A0T2N3
|
APJB_DANRE
|
Apelin receptor B (Angiotensin II receptor-like 1b) (Angiotensin receptor-like 1b) (G-protein coupled receptor APJ B) (Protein grinch)
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MNAMDNMTADYSPDYFDDAVNSSMCEYDEWEPSYSLIPVLYMLIFILGLTGNGVVIFTVWRAQSKRRAADVYIGNLALADLTFVVTLPLWAVYTALGYHWPFGVALCKISSYVVLLNMYASVFCLTCLSLDRYMAIVHSLTSTQLRTRGHMRASLTAIWLLSGVLAAPTLLFRTTVYDVETNRTSCAMDFNLVVSQPGQETYWIAGLSISSTALGFLIPLLAMMVCYGFIGCTVTRHFNSLRKEDQRKRRLLKIITTLVVVFAACWMPFHVVKTMDALSYLNLAPDSCTFLNLLLLAHPYATCLAYVNSCLNPLLYAFFDLRFRSQCLCLLNLKKALHASPASSLSSQKTEAQSLATKV
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Receptor for apelin receptor early endogenous ligand (apela) and apelin (apln) hormones coupled to G proteins that inhibit adenylate cyclase activity. Plays a key role in early development such as gastrulation, blood vessels formation and heart morphogenesis by acting as a receptor for apela hormone, promoting endoderm and mesendoderm cell migration and regulating the migration of cells fated to become myocardial progenitors, respectively. Positively regulates angioblast migration toward the embryonic midline, i.e. the position of the future vessel formation, during vasculogenesis. May promote sinus venosus (SV)-derived endothelial cells migration into the developing heart to promote coronary blood vessel development (By similarity). Required for cardiovascular development, particularly for intersomitic vein angiogenesis by acting as a receptor for apln hormone (By similarity). Plays a role in various processes in adults such as regulation of blood vessel formation, blood pressure, heart contractility and heart failure (By similarity). Acts redundantly with agtrl1a in heart development.
|
A1A278
|
MANA_BIFAA
|
Mannan endo-1,4-beta-mannosidase (EC 3.2.1.78) (Beta-mannanase) (Mannanase 26A) (Man26A) (Mannanase A) (ManA)
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MKTTVTKLLATVAAASTIFGMSTLPAFAAEGKSASNGNSVNISDVNATAETRALFDKLKNSGKGDLRFGQQHATDENISSSASQGDVYETTGKYPAVFGWDAGLALRGAEKPGSGADKNANAKALAQNITDADSKGAIVTLSAHWCNPGTGKDFNDTTAVASELLPGGKYSGTFNKELDAIAATAQRAKRSDGTLIPIIFRPLHENNGSWFWWGATHASASEYKELYRYIVDYLRDVKDVHNLLYAYSPGGVFNGDSTDYLATYPGDQWVDVLGYDEYDSDDSADDSSAWINTVVKDMKMVSDQASQRGKIVALTEFGRSGDRKFKESGTGDKDTKFFSELAEALAENVPSTAYMMTWANFGGGGDNFQAYTSWKGSDGEADFKAFADSNKNLMASKDNVDYSNAPAAAMQNGSARIVTPVDGNRVTDTKVVVRVKTEGVKYSDLDLNSAIVTTDRGQNVKLKYSCNGYFTGILDLNAAGINLDQSKLTLTPQVKTKDGKTLAAADGNGSVTVKLGAKPEQTVDNVEDFDSYDNEAELQSVYSPSHSTKSNLTLVDSPEDNGTKAGNIHYDFVSYPEYNGFQRSHTPKQDWSGFSKLNMFLKADGSDHKFVVQVNAGGVTFEAYPKIDGTDGHVVSLNFGDADGNGGDFAPASWDTAHAGMKLSQKLLSKVGSFALYINDNGGNRPKSGDLTLDSIKLDGKRDAYAPNTNPTPGNTAKAQSVDDFSGYSDDAAAQSAWGNRGHTEVLSLDEGPTDGSKALRFKYDFSNGGWYDVAKYLDGANWSGESVLAFQVKGDGSGNAIGLQIGTSDGKYFLASVKLDFTGWKQIEIPLVDNANLTQSWPEDANKDNPMTEDDLASIKELVFASQQWNSESDGLDSSIADIKVEPAENTSNEQTPKDESKTEVKADKEQEQSEDTSADVTAQDPATCPISDEDSKGSTGNTTVTVKPTPDTKEPADNTGKDGLSRTGSNIISAIAAVAVLLLGGCAVLIARKRKGGDIE
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Beta-mannanase likely involved in the utilization of carbohydrates in the human gut. Catalyzes the hydrolysis of different beta-1,4-linked mannans, such as ivory nut mannan, konjac glucomannan, as well as carob and guar gum galactomannans, to a mixture of oligosaccharides. The dominant product from ivory nut mannan is found to be mannotriose mannobiose and mannotetraose are produced to a lesser extent. Does not hydrolyze mannobiose, and hydrolyzes mannotriose at a significantly lower rate than the longer oligosaccharides.
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A1A399
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BGAL_BIFAA
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Beta-galactosidase BgaB (Beta-gal) (EC 3.2.1.23) (Beta-Gal II)
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MSARRNFEWPELLTADGRGIAFGGDYNPDQWSEDIWDDDIRLMKQAGVNTVALAIFSWDRIQPTEDRWDFGWLDRIIDKLGNAGIVVDLASATATAPLWLYESHPEVLPRDKYGHPVNAGSRQSWSPTSPVFKEYALTLCRKLAERYGTNPYVTAWHMGNEYGWNNREDYSDNALEAFRAWCRRKYGTIDALNQAWGTTFWGQEMNGFDEVLIPRFMGADSMVNPGQKLDFERFGNDMLLDFYKAERDAIAEICPDKPFTTNFMVSTDQCCMDYAAWAKEVNFVSNDHYFHEGESHLDELACSDALMDSLALGKPWYVMEHSTSAVQWKPLNTRKRKGETVRDSLAHVAMGADAINFFQWRASAFGAEAFHSAMVPHAGEDTKLFRQVCELGASLHTLADAGVQGTELAHSDTAILFSAESEWATRSQTLPSMKLNHWHDVRDWYRAFLDAGSRADIVPLAYDWSSYKTVVLPTVLILSAADTQRLADFAAAGGRVVVGYATGLIDEHFHTWLGGYPGAGDGLLRSMLGVRGEEFNILGAEAEGEPGEIRLSSADDSAALDGTTTRLWQNDVNVTGEHAQVLATYAGEEADEWELDGTAAVTRNPYGSGEAYFVGCDLDVADLTKLVRAYLAASSQENADVLHTVRASADATFDFYLPRGKKTVELQGIEGEPVILFQTDREEKPGSYTVRRNGVLVVRR
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Involved in the hydrolysis of transgalactooligosaccharides (TOS). Highly active towards Gal(beta1-4)Gal and Gal(beta1-4)-Gal-containing oligosaccharides. Low activity towards Gal(beta1-3)Gal, lactose and Gal(beta1-3)GalOMe. No activity towards Gal(beta1-6)Gal, Gal(beta1-4)Man, Gal(alpha1-4)Gal, Gal(alpha1-3)Gal(beta1-4)Gal, lactulose, 3'fucosyllactose, lacto-N-fucopentaose I, lacto-N-fucopentaose II, cellobiose, maltose or sucrose. No transglycosylation activity is found at high substrate concentrations (100 mg/ml) and only low transglycosylation activity at lower substrate concentrations (10 mg/ml).
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A1A4I4
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PKN1_BOVIN
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Serine/threonine-protein kinase N1 (EC 2.7.11.13) (Protein kinase C-like 1) (Protein kinase C-like PKN) (Protein kinase PKN-alpha) (Protein-kinase C-related kinase 1) (Serine-threonine protein kinase N)
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MASDAVQSEPRSWSLLEQLGLAGADLAAPGVQQQLELERERLRREIRKELKLKEGAENLRRATTDLGRNLGPVELVLRGSSRRLALLHQQLQELHAHVVLPDPAVGVHDAPQSPGTGDSACSATNLSRVAGLEKQLAIELKVKQGAENMIQTYSNGSTKDRKLLLTAQQMLQDSKTKIDIIRMQLHRALQACQLESQAAPDEAQGSPDLGAVELRIEELRHHFRVEHAVAEGAKNVLRLLSAAKAPDRKAVSEAQEKLTESNQKLGLLREALERRLGELPADHPKGRLLREELAAASSAAFSARLAGPFPATHYSTLSKPAPLTGTLEVRVVGCRDLPETIPWNPSPSVGGPGTPDSRTPFLSRPARGLYSRTGSLSGRSSLKAEAENTNEVSTVLKLDNTVVGQTSWKPCGPNAWDQSFTLELERARELELAVFWRDQRGLCALKFLKLEDFLDNERHEVQLDMEPQGCLVAEVTFRNPVIERIPRLRRQKKIFSKQQGKAFQRARQMNIDVATWVRLLRRLIPNATATGTFSPGASPGPEARSTGDISVEKLNLGTETDSSPQKSPLGPPSSPSSLSSPIQATTTTPELPSETQETPGPTLCSPLRKSPLTLEDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLMCEKRILAAVTNAGHPFLVNLFGCFQTPEHVCFVMEYSAGGDLMLHIHSDVFSEPRAVFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGYGDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSAEAIGIMRRLLRRNPERRLGSSERDAEDVKKQPFFRTLGWDALLARRLPPPFVPTLAGRTDVSNFDEEFTGEAPTLSPPRDARPLTATEQAAFRDFDFVAGSC
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PKC-related serine/threonine-protein kinase involved in various processes such as regulation of the intermediate filaments of the actin cytoskeleton, cell migration, tumor cell invasion and transcription regulation. Part of a signaling cascade that begins with the activation of the adrenergic receptor ADRA1B and leads to the activation of MAPK14. Regulates the cytoskeletal network by phosphorylating proteins such as VIM and neurofilament proteins NEFH, NEFL and NEFM, leading to inhibit their polymerization. Phosphorylates 'Ser-575', 'Ser-637' and 'Ser-669' of MAPT/Tau, lowering its ability to bind to microtubules, resulting in disruption of tubulin assembly. Acts as a key coactivator of androgen receptor (ANDR)-dependent transcription, by being recruited to ANDR target genes and specifically mediating phosphorylation of 'Thr-11' of histone H3 (H3T11ph), a specific tag for epigenetic transcriptional activation that promotes demethylation of histone H3 'Lys-9' (H3K9me) by KDM4C/JMJD2C. Phosphorylates HDAC5, HDAC7 and HDAC9, leading to impair their import in the nucleus. Phosphorylates 'Thr-38' of PPP1R14A, 'Ser-159', 'Ser-163' and 'Ser-170' of MARCKS, and GFAP. Able to phosphorylate RPS6 in vitro.
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A1A4I9
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UFL1_BOVIN
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E3 UFM1-protein ligase 1 (EC 2.3.2.-) (E3 UFM1-protein transferase 1)
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MADAWEEIRRLAADFQRAQFAEATQRLSERNCIEIVNKLIAQKQLEVVHTLDGKEYITPAQISKEMRDELHVRGGRVNIVDLQQAINVDLTHIENRIGDIVKSEKHVQLVLGQLIDENYLDRLAEEVNDKLQESGQVTIAELCKTYDLPGNFLTQALTQRLGRIINGHIDLDNRGVIFTEAFVSRHKARIRGLFSAITRPTAVNSLISRYGFQEQLLYSVLEELVNDGRLRGTVVGGRQDKAVFIPDIYSRTQSTWVDSFLRQNGYLEFDALSRLGIPDAMSYIKKRYKTTQLLFLKAACVGQGLVDQVEASVEEAISSGTWVDIAPLLPSSLSVEDAAILLQHVMRALSKQASAVVFSDTIVVSEKFINDCTDLFSELMHQKAEKEMKNNPVHLITEEDLKQISILESINTSKKDKKDERRRKATEGSGSVRGGGGSNAREYKIKKTKKKGRKDDDSDDESSHTGKKKPEITFMFQDEIEDFLRKHLQDAPEEFISELAEYLIKPLNKTYLEVVHSVYMSSTSSASGTGRKRTIKDLQEEVSNLYNNIRLFEKGMKFFTDDTQAALTKHLLKTVCTDITNLVFNFLASDLMMAVDDPATITSEVRKKILSKLSEETKVALTKLHNSLNEKSIEDFLACLDSAAEACDIMLKKGDKKRERQVLFQHRQALVEQLKVTEDPALTLHLTSVLLFQFSTHSMLHAPGRCVPQIIAFLSSKIPEDQHALLVKYQGLVVKHLVSQNKKTGQGEDPLSDELDKEQEDIINTTRKELQELSSSIKDLVLKSRKSSVTEE
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E3 protein ligase that mediates ufmylation, the covalent attachment of the ubiquitin-like modifier UFM1 to lysine residues on target proteins, and which plays a key role in reticulophagy (also called ER-phagy) induced in response to endoplasmic reticulum stress (By similarity). In response to endoplasmic reticulum stress, recruited to the endoplasmic reticulum membrane by DDRGK1, and mediates ufmylation of proteins such as RPN1 and RPL26/uL24, thereby promoting reticulophagy of endoplasmic reticulum sheets (By similarity). Ufmylation-dependent reticulophagy inhibits the unfolded protein response (UPR) via ERN1/IRE1-alpha (By similarity). Ufmylation in response to endoplasmic reticulum stress is essential for processes such as hematopoiesis, blood vessel morphogenesis or inflammatory response. Regulates inflammation in response to endoplasmic reticulum stress by promoting reticulophagy, leading to inhibit the activity of the NF-kappa-B transcription factor. Mediates ufmylation of DDRGK1 and CDK5RAP3 the role of these modifications is however unclear: as both DDRGK1 and CDK5RAP3 act as substrate adapters for ufmylation, it is uncertain whether ufmylation of these proteins is a collateral effect or is required for ufmylation (By similarity). Catalyzes ufmylation of various subunits of the ribosomal complex or associated components, such as RPS3/uS3, RPS20/uS10, RPL10/uL16, RPL26/uL24 and EIF6 (By similarity). Anchors CDK5RAP3 in the cytoplasm, preventing its translocation to the nucleus which allows expression of the CCND1 cyclin and progression of cells through the G1/S transition (By similarity). Also involved in the response to DNA damage: recruited to double-strand break sites following DNA damage and mediates monoufmylation of histone H4 (By similarity). Catalyzes ufmylation of TRIP4, thereby playing a role in nuclear receptor-mediated transcription (By similarity). Required for hematopoietic stem cell function and hematopoiesis. Required for cardiac homeostasis (By similarity).
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A1A4J1
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PFKAL_BOVIN
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ATP-dependent 6-phosphofructokinase, liver type (ATP-PFK) (PFK-L) (EC 2.7.1.11) (6-phosphofructokinase type B) (Phosphofructo-1-kinase isozyme B) (PFK-B) (Phosphohexokinase)
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MASVDLEKLRTTGAGKAIGVLTSGGDAQGMNAAVRAVTRMGIYVGAKVFLIYEGYEGLVEGGENIKQANWLSVSNIIQLGGTVIGSARCKAFTTREGRRAAAYNLVQRGITNLCVIGGDGSLTGANIFRSEWGSLLEELVSEGKISEGTAQTYSHLNIAGLVGSIDNDFCGTDMTIGTDSALHRIMEVIDAITTTAQSHQRTFVLEVMGRHCGYLALVSALASGADWLFIPEAPPEDGWENFMCERLGETRSRGSRLNIIIIAEGAIDRNGKPISSRYVKDLVVQRLGFDTRVTVLGHVQRGGTPSAFDRILSSKMGMEAVMALLEATPDTPACVVSLSGNQSVRLPLMECVQMTKEVQKAMDEKRFDEAIQLRGGSFENNWNIYKLLSHQKISKEKTNFSLAILNVGAPAAGMNAAVRSAVRSGISQGHTVYVVHDGFEGLAKNQVQEVSWHDVAGWLGRGGSMLGTKRTLPKGFMEKIVENIRLHNIHALLVIGGFEAYEGVLQLVEARGRYEELCIVMCVIPATISNNVPGTDFSLGSDTAVNAAMESCDRIKQSASGTKRRVFIVETMGGYCGYLATVTGIAVGADAAYVFEDPFNIQDLKANVEHMTEKMKTEIQRGLVLRNEKCHEHYTTEFLYNLYSSEGKGVFDCRTNVLGHLQQGGAPTPFDRNYGTKLGVKAIIWMSEKLRAVYRNGRVFANASDSACVIGLQKKVVAFSPVTELKKDTDFEHRMPREQWWLNLRLMLKMLAHYRISMADYVSGELEHVTRRTLSIETGF
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Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis (By similarity). Negatively regulates the phagocyte oxidative burst in response to bacterial infection by controlling cellular NADPH biosynthesis and NADPH oxidase-derived reactive oxygen species. Upon macrophage activation, drives the metabolic switch toward glycolysis, thus preventing glucose turnover that produces NADPH via pentose phosphate pathway (By similarity).
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A1A4K3
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DDB1_BOVIN
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DNA damage-binding protein 1 (Damage-specific DNA-binding protein 1)
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MSYNYVVTAQKPTAVNGCVTGHFTSAEDLNLLIAKNTRLEIYVVTAEGLRPVKEVGMYGKIAVMELFRPKGESKDLLFILTAKYNACILEYKQSGESIDIITRAHGNVQDRIGRPSETGIIGIIDPECRMIGLRLYDGLFKVIPLDRDNKELKAFNIRLEELHVIDVKFLYGCQAPTICFVYQDPQGRHVKTYEVSLREKEFNKGPWKQENVEAEASMVIAVPEPFGGAIIIGQESITYHNGDKYLAIAPPIIKQSTIVCHNRVDPNGSRYLLGDMEGRLFMLLLEKEEQMDGTVTLKDLRVELLGETSIAECLTYLDNGVVFVGSRLGDSQLVKLNVDSNEQGSYVVAMETFTNLGPIVDMCVVDLERQGQGQLVTCSGAFKEGSLRIIRNGIGIHEHASIDLPGIKGLWPLRSDPNRETDDTLVLSFVGQTRVLMLNGEEVEETELMGFVDDQQTFFCGNVAHQQLIQITSASVRLVSQEPKALVSEWKEPQGKNISVASCNSSQVVVAVGRALYYLQIHPQELRQISHTEMEHEVACLDITPLGDSNGMSPLCAIGLWTDISARIAKLPSFELLHKEMLGGEIIPRSILMTTFESSHYLLCALGDGALFYFGLNIETGLLSDRKKVTLGTQPTVLRTFRSLSTTNVFACSDRPTVIYSSNHKLVFSNVNLKEVNYMCPLNSDGYPDSLALANNSTLTIGTIDEIQKLHIRTVPLYESPRKICYQEVSQCFGVLSSRIEVQDTSGGTTALRPSASTQALSSSVSSSKLFSSSTAPHETSFGEEVEVHNLLIIDQHTFEVLHAHQFLQNEYALSLVSCKLGKDPNTYFIVGTAMVYPEEAEPKQGRIVVFQYSDGKLQTVAEKEVKGAVYSMVEFNGKLLASINSTVRLYEWTTEKELRTECNHYNNIMALYLKTKGDFILVGDLMRSVLLLAYKPMEGNFEEIARDFNPNWMSAVEILDDDNFLGAENAFNLFVCQKDSAATTDEERQHLQEVGLFHLGEFVNVFCHGSLVMQNLGETSTPTQGSVLFGTVNGMIGLVTSLSESWYNLLLDMQNRLNKVIKSVGKIEHSFWRSFHTERKTEPATGFIDGDLIESFLDISRPKMQEVVANLQYDDGSGMKREATADDLIKVVEELTRIH
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Protein, which is both involved in DNA repair and protein ubiquitination, as part of the UV-DDB complex and DCX (DDB1-CUL4-X-box) complexes, respectively. Core component of the UV-DDB complex (UV-damaged DNA-binding protein complex), a complex that recognizes UV-induced DNA damage and recruit proteins of the nucleotide excision repair pathway (the NER pathway) to initiate DNA repair. The UV-DDB complex preferentially binds to cyclobutane pyrimidine dimers (CPD), 6-4 photoproducts (6-4 PP), apurinic sites and short mismatches. Also functions as a component of numerous distinct DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. The functional specificity of the DCX E3 ubiquitin-protein ligase complex is determined by the variable substrate recognition component recruited by DDB1. DCX(DDB2) (also known as DDB1-CUL4-ROC1, CUL4-DDB-ROC1 and CUL4-DDB-RBX1) may ubiquitinate histone H2A, histone H3 and histone H4 at sites of UV-induced DNA damage. The ubiquitination of histones may facilitate their removal from the nucleosome and promote subsequent DNA repair. DCX(DDB2) also ubiquitinates XPC, which may enhance DNA-binding by XPC and promote NER. DCX(DTL) plays a role in PCNA-dependent polyubiquitination of CDT1 and MDM2-dependent ubiquitination of TP53 in response to radiation-induced DNA damage and during DNA replication. DCX(ERCC8) (the CSA complex) plays a role in transcription-coupled repair (TCR). The DDB1-CUL4A-DTL E3 ligase complex regulates the circadian clock function by mediating the ubiquitination and degradation of CRY1 (By similarity). DDB1-mediated CRY1 degradation promotes FOXO1 protein stability and FOXO1-mediated gluconeogenesis in the liver (By similarity). By acting on TET dioxygenses, essential for oocyte maintenance at the primordial follicle stage, hence essential for female fertility (By similarity). Maternal factor required for proper zygotic genome activation and genome reprogramming (By similarity).
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A1A4K5
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ENPP2_BOVIN
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Ectonucleotide pyrophosphatase/phosphodiesterase family member 2 (E-NPP 2) (EC 3.1.4.39) (Autotaxin) (Extracellular lysophospholipase D) (LysoPLD)
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MARRRSCQLHQVISLFTFAVGVNICLGVTANRIKRAEGWGEGPPTVLSDSPSINISGSCKGRCFELQEAGPPDCRCDNLCKSYSSCCLDFDELCLKTAGGWECTKDRCGEVRNEDHACHCSEDCLARGDCCTNYQVVCKGESHWVDDDCEEIKTPECPAGFVRPPLIIFSVDGFRASYMKKGSKVMPNIEKLRSCGTHSPYMRPVYPTKTFPNLYTLATGLYPESHGIVGNSMYDPVFDAHFNLRGREKFNHRWWGGQPLWITATKQGVIAGTFFWPVVIPHERRILTILQWLTLPDHERPSVYAFYSEQPDFSGHKYGPFGPEMTNPLRDIDKTVGQLMDGLKQLKLHRCVNVIFVGDHGMEDVTCDRTEFLSNYLTNVDDIILVPGTLGRIRPKFNNHAKYDPKVIIANLTCKKPDQHFKPYLKQHLPKRLHYANNRRIEDVHLLVERRWHVARKPLEVYKKPSGKCFFQGDHGFDNKVNSMQTVFVGYGPTFKYKTKVPPFENIELYNVMCDLLGLKPAPNNGTHGSLNHLLRTNTFRPTVPEEVTRPNYPGVMYLQSDFDLGCTCDDKAEPKNKLDELNKHLHIKESTEAETRKFRGSKNEIKENVNGNFEPRKERHLLYGRPAVLYRTRYDILYHTDFESGYSEIFLMPLWTSYTVSKQADVSDIPAHLTNCVRPDVRVSPSFSQSCLAYKNDKQMSYGFLFPPYLSSSPEAKYDAFLVTNMVPMYPAFKRIWNYFQRVLVKKYASERNGVNVISGPIFDYDYDGLHDTQDKIKQYVEGSSVPVPTHYYSILTSCLDFTQPADRCDGPLSVSAFVLPHRPDNDESCNSSEDESKWVEELLKMHTARVRDIEHLTSLDFFRKTSRSYPEILTLKTYLQTYESEI
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Hydrolyzes lysophospholipids to produce the signaling molecule lysophosphatidic acid (LPA) in extracellular fluids. Major substrate is lysophosphatidylcholine. Can also act on sphingosylphosphorylcholine producing sphingosine-1-phosphate, a modulator of cell motility. Can hydrolyze, in vitro, bis-pNPP, to some extent pNP-TMP, and barely ATP. Involved in several motility-related processes such as angiogenesis and neurite outgrowth. Acts as an angiogenic factor by stimulating migration of smooth muscle cells and microtubule formation. Stimulates migration of melanoma cells, probably via a pertussis toxin-sensitive G protein. May have a role in induction of parturition. Possible involvement in cell proliferation and adipose tissue development. Tumor cell motility-stimulating factor (By similarity). Required for LPA production in activated platelets, cleaves the sn-1 lysophospholipids to generate sn-1 lysophosphatidic acids containing predominantly 18:2 and 20:4 fatty acids (By similarity). Shows a preference for the sn-1 to the sn-2 isomer of 1-O-alkyl-sn-glycero-3-phosphocholine (lyso-PAF) (By similarity).
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A1A4L1
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THEM4_BOVIN
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Acyl-coenzyme A thioesterase THEM4 (Acyl-CoA thioesterase THEM4) (EC 3.1.2.2) (Thioesterase superfamily member 4)
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MLRSCTAGLRSIWALRGRREGAPRLSMDLQPARRLFSTEKVIHKDWALPNPSWSKDLKLLFDQFMKKCEDGSWERLPSYKRRSTQESEDFKTYFLDPKLVEEERLSQAQLFTRGFEDGLGFEYVIFKNNDEKRTVCLFQGGPYLQGVPGLLHGGAMATMIDIALGSCTGGAVMTANLNINFKRPVPLCSVVVINSQLDKLEGRKLFLSCNVRSVDEKTLYSEATGLFIKLDPEKSST
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Has acyl-CoA thioesterase activity towards medium and long-chain (C14 to C18) fatty acyl-CoA substrates, and probably plays a role in mitochondrial fatty acid metabolism (By similarity). Plays a role in the apoptotic process, possibly via its regulation of AKT1 activity (By similarity).
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A1A4L8
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MOCS3_BOVIN
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Adenylyltransferase and sulfurtransferase MOCS3 (Molybdenum cofactor synthesis protein 3) [Includes: Molybdopterin-synthase adenylyltransferase (EC 2.7.7.80) (Adenylyltransferase MOCS3) (Sulfur carrier protein MOCS2A adenylyltransferase); Molybdopterin-synthase sulfurtransferase (EC 2.8.1.11) (Sulfur carrier protein MOCS2A sulfurtransferase) (Sulfurtransferase MOCS3)]
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MAAREEVLALQAEVAQREEELSSLKQRLAAALSTGQESARSVPVSPLPPRAALSREEIRRYSRQLVLPELGMQGQLRLAAAAVLVVGCGGLGCPLAQYLAAAGVGRLGLVDYDVVEASNLARQVLHGEALAGQAKVFSAAAALRRLNSAVECVPYAQALTPATALDLVRRYDVVADCSDNAPTRYLVSDACVLAGRPLVSASALRFEGQLTVYHYGGGPCYRCVFPRPPPAETVTSCADGGVLGAVTGVLGCLQALEVLKTAAGLGPSYSGRLLLFDALRGDFRCIRLRRRRPDCAACGERPTVTDLQDYESFCGSSATDKCRSLRLLSPEERISIMDYKRLLDSRSPHLLLDVRPQVEVDICRLPHALHIPLKSLERRDAESLKVLGEAIREGKQGAQEGASVPIYVICKLGNDSQKAVKILQSWADLDSLTVKDVVGGLMAWAAKIDGTFPQY
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Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Also essential during biosynthesis of the molybdenum cofactor. Acts by mediating the C-terminal thiocarboxylation of sulfur carriers URM1 and MOCS2A. Its N-terminus first activates URM1 and MOCS2A as acyl-adenylates (-COAMP), then the persulfide sulfur on the catalytic cysteine is transferred to URM1 and MOCS2A to form thiocarboxylation (-COSH) of their C-terminus. The reaction probably involves hydrogen sulfide that is generated from the persulfide intermediate and that acts as nucleophile towards URM1 and MOCS2A. Subsequently, a transient disulfide bond is formed. Does not use thiosulfate as sulfur donor NFS1 probably acting as a sulfur donor for thiocarboxylation reactions. {ECO:0000255|HAMAP-Rule:MF_03049}.
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A1A4N1
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S29A3_BOVIN
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Equilibrative nucleoside transporter 3 (Solute carrier family 29 member 3)
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MAIISEDDFRHTSNSTYRTASSSLRADQEALLEKLLDRPPPSLQRPEDRFNGTYIIFFSLGIGGLLPWNFFVTAQEYWIFKLSNCSSPAAGEEPKDSDILNYFESYLAVASTVPSVLCLALNFLLVNRVPIRVRVLASLTVMLAIFIVMTVLVKVDTSSWTHSFFTITITCMAILSGTSTIFNSSVFGMTGSFPMRNSQALISGGAMGGTLSAVASLVDLAVASDVTDSTLAFFLTADIFLALCIGLYLLLPRLDYARYYMKPVWPTVFSGEEQLPQDSPSPTSVAPGSSDPQTPPLGPILKKTTGLGFCIIYLFFITSLIFPAICTNIESLSKGSGSPWSTKFFVPLTTFLLYNFADLCGRQVTAWIQVPGPRSKALPGLALLRTCFVPLFVFCNYQPRGHLHTVLFQSDVYPVLFTSLLGLSNGYLSTLALIYGPKIVPRELAEATGVVMTFYMGLGLVLGSACSALLVHLI
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Uniporter that mediates the facilitative transport of nucleoside across lysosomal and mitochondrial membranes. Functions as a non-electrogenic Na(+)-independent transporter. Substrate transport is pH-dependent and enhanced under acidic condition, probably reflecting the location of the transporter in acidic intracellular compartments. Proton is not a cotransporting ion but most likely change the ionization state of the transporter which dictates transport-permissible/impermissible conformation for nucleoside translocation. May direct the nucleoside transport from lysosomes to cytosol or cytosol to mitochondria to facilitate the fundamental function of salvage synthesis of nucleic acids. Involved in the transport of nucleosides (adenosine, guanosine, uridine, thymidine, cytidine and inosine) and deoxynucleosides (deoxyadenosine, deoxycytidine). Also mediates transport of purine nucleobases (adenine, guanine) and pyrimidine nucleobases (uracil). Also able to transport monoamine neurotransmitters dopamine, serotonin, noradrenaline and tyramine. Capable of transporting ATP (By similarity). Mediates nucleoside export from lysosomes in macrophages, which regulates macrophage functions and numbers (By similarity).
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A1A4Q9
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NUD16_BOVIN
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U8 snoRNA-decapping enzyme (EC 3.6.1.62) (IDP phosphatase) (IDPase) (EC 3.6.1.64) (Inosine diphosphate phosphatase) (Nucleoside diphosphate-linked moiety X motif 16) (Nudix motif 16) (m7GpppN-mRNA hydrolase)
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MAGMRRLELSEALHLGPGWRHACHALLYAPDPGLLFGRIPLRYAVLMQMRFDGRLGFPGGFVDLRDGSLEDGLNRELGEELGEAAGAFRVERADYRSSHAGSRPRVVAHFYTKLLTLEQLTAVEMGAPRARDHGLEVLGLVRVPLYTLRDGVGGLPAFLENTFIGNAREQLLEAVQNLGLLEPGSFARLKISTPP
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RNA-binding and decapping enzyme that catalyzes the cleavage of the cap structure of snoRNAs and mRNAs in a metal-dependent manner. Part of the U8 snoRNP complex that is required for the accumulation of mature 5.8S and 28S rRNA. Has diphosphatase activity and removes m7G and/or m227G caps from U8 snoRNA and leaves a 5'monophosphate on the RNA. Catalyzes also the cleavage of the cap structure on mRNAs. Does not hydrolyze cap analog structures like 7-methylguanosine nucleoside triphosphate (m7GpppG). Also hydrolysis m7G- and m227G U3-capped RNAs but with less efficiencies. Has broad substrate specificity with manganese or cobalt as cofactor and can act on various RNA species. Binds to the U8 snoRNA metal is not required for RNA-binding. May play a role in the regulation of snoRNAs and mRNAs degradation. Acts also as a phosphatase hydrolyzes the non-canonical purine nucleotides inosine diphosphate (IDP) and deoxyinosine diphosphate (dITP) as well as guanosine diphosphate (GDP), deoxyguanosine diphosphate (dGDP), xanthine diphosphate (XDP), inosine triphosphate (ITP) and deoxyinosine triphosphate (ITP) to their respective monophosphate derivatives and does not distinguish between the deoxy- and ribose forms. The order of activity with different substrates is IDP > dIDP >> GDP = dGDP > XDP = ITP = dITP. Binds strongly to GTP, ITP and XTP. Participates in the hydrolysis of dIDP/IDP and probably excludes non-canonical purines from RNA and DNA precursor pools, thus preventing their incorporation into RNA and DNA and avoiding chromosomal lesions (By similarity). Exhibits decapping activity towards NAD-capped RNAs and FAD-capped RNAs (By similarity). Exhibits decapping activity towards NAD-capped RNAs and FAD-capped RNAs (By similarity). Exhibits decapping activity towards dpCoA-capped RNAs in vitro (By similarity).
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A1A4R9
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AP2A_BOVIN
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Transcription factor AP-2-alpha (AP2-alpha) (AP-2 transcription factor) (Activating enhancer-binding protein 2-alpha) (Activator protein 2) (AP-2)
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MLWKLTDNIKYEDCEDRHDGASNGTARLPQLGTVGQSPYTSAPPLSHTPNADFQPPYFPPPYQPIYPQSQDPYSHVNDPYSLNPLHAQPQPQHPGWPGQRQSQESGLLHTHRGLPHQLSGLDPRRDYRRHEDLLHGPHGLGSGLGDLPIHSLPHAIEDVPHVEDPGINIPDQTVIKKGPVSLSKSNSNAVSAIPINKDNLFGGVVNPNEVFCSVPGRLSLLSSTSKYKVTVAEVQRRLSPPECLNASLLGGVLRRAKSKNGGRSLREKLDKIGLNLPAGRRKAANVTLLTSLVEGEAVHLARDFGYVCETEFPAKAVAEFLNRQHSDPNEQVTRKNMLLATKQICKEFTDLLAQDRSPLGNSRPNPILEPGIQSCLTHFNLISHGFGSPAVCAAVTALQNYLTEALKAMDKMYLSNNPNSHTDNNAKSSDKEEKHRK
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Sequence-specific DNA-binding protein that interacts with inducible viral and cellular enhancer elements to regulate transcription of selected genes. AP-2 factors bind to the consensus sequence 5'-GCCNNNGGC-3' and activate genes involved in a large spectrum of important biological functions including proper eye, face, body wall, limb and neural tube development. They also suppress a number of genes including MCAM/MUC18, C/EBP alpha and MYC. AP-2-alpha is the only AP-2 protein required for early morphogenesis of the lens vesicle. Together with the CITED2 coactivator, stimulates the PITX2 P1 promoter transcription activation. Associates with chromatin to the PITX2 P1 promoter region (By similarity).
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A1A4S6
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RHG10_HUMAN
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Rho GTPase-activating protein 10 (GTPase regulator associated with focal adhesion kinase 2) (Graf-related protein 2) (Rho-type GTPase-activating protein 10)
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MGLQPLEFSDCYLDSPWFRERIRAHEAELERTNKFIKELIKDGKNLIAATKSLSVAQRKFAHSLRDFKFEFIGDAVTDDERCIDASLREFSNFLKNLEEQREIMALSVTETLIKPLEKFRKEQLGAVKEEKKKFDKETEKNYSLIDKHLNLSAKKKDSHLQEADIQVEQNRQHFYELSLEYVCKLQEIQERKKFEFVEPMLSFFQGMFTFYHQGHELAKDFNHYKMELQINIQNTRNRFEGTRSEVEELMNKIRQNPKDHKRASQFTAEGYLYVQEKRPAPFGSSWVKHYCMYRKAAKKFNMIPFEHRSGGKLGDGEVFFLKECTKRHTDSIDRRFCFDIEAADRPGVSLTMQAFSEEERKQWLEALGGKEALSHSFNTAIIPRPEGNAQLDKMGFTIIRKCISAVETRGINDQGLYRVVGVSSKVQRLLSMLMDVKTCNEVDLENSADWEVKTITSALKQYLRSLPEPLMTYELHGDFIVPAKSGSPESRVNAIHFLVHKLPEKNKEMLDILVKHLTNVSNHSKQNLMTVANLGVVFGPTLMRPQEETVAALMDLKFQNIVVEILIENHEKIFRTPPDTTFPEPTCLSASPPNAPPRQSKRQGQRTKRPVAVYNLCLELEDGDNPYPSKEDTPTSSLDSLSSPSPVTTAVPGPPGPDKNHLLADGGSFGDWASTIPGQTRSSMVQWLNPQSPTTTSSNSAVTPLSPGSSPFPFSPPATVADKPPESIRSRKARAVYPCEAEHSSELSFEIGAIFEDVQTSREPGWLEGTLNGKRGLIPQNYVKLL
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GTPase activator for the small GTPases RhoA and Cdc42 by converting them to an inactive GDP-bound state. Essential for PTKB2 regulation of cytoskeletal organization via Rho family GTPases. Inhibits PAK2 proteolytic fragment PAK-2p34 kinase activity and changes its localization from the nucleus to the perinuclear region. Stabilizes PAK-2p34 thereby increasing stimulation of cell death (By similarity). {ECO:0000250, ECO:0000269|PubMed:11432776}.
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A1A4Y4
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IRGM_HUMAN
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Immunity-related GTPase family M protein (EC 3.6.5.-) (Immunity-related GTPase family M protein 1) (Interferon-inducible protein 1) (LPS-stimulated RAW 264.7 macrophage protein 47 homolog) (LRG-47)
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MEAMNVEKASADGNLPEVISNIKETLKIVSRTPVNITMAGDSGNGMSTFISALRNTGHEGKASPPTELVKATQRCASYFSSHFSNVVLWDLPGTGSATTTLENYLMEMQFNRYDFIMVASAQFSMNHVMLAKTAEDMGKKFYIVWTKLDMDLSTGALPEVQLLQIRENVLENLQKERVCEY
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Immunity-related GTPase that plays important roles in innate immunity and inflammatory response. Acts as a dynamin-like protein that binds to intracellular membranes and promotes remodeling and trafficking of those membranes (By similarity). Required for clearance of acute protozoan and bacterial infections by interacting with autophagy and lysosome regulatory proteins, thereby promoting the fusion of phagosomes with lysosomes for efficient degradation of cargo including microbes. Regulates selective autophagy, including xenophagy and mitophagy, both directly and indirectly. Directly regulates autophagy by acting as a molecular adapter that promotes the coassembly of the core autophagy machinery to mediate antimicrobial defense: IRGM (1) activates AMPK, which in turn phosphorylates ULK1 and BECN1 to induce autophagy, (2) promotes the coassembly of ULK1 and BECN1, enhancing BECN1-interacting partners and (3) influences the composition of the BECN1 complex, by competing with the negative regulators BCL2 and RUBCN, to trigger autophagy. Also activates autophagy by promoting recruitment of STX17 to autophagosomes. In collaboration with ATG8 proteins, regulate lysosomal biogenesis, a fundamental process for any autophagic pathway, by promoting TFEB dephosphorylation. Also modulates autophagy by assisting with autophagosome formation and preventing lysosomal deacidification (By similarity). While activating autophagy, acts as a key negative regulator of the inflammatory and interferon responses both by (1) promoting mitophagy and (2) mediating autophagy-dependent degradation of effectors of the inflammatory response. Promotes degradation of damaged and IFNG/IFN-gamma-stressed mitochondria via mitophagy, preventing cytosolic release of ligands that activate inflammation. Acts as a suppressor of inflammation by promoting recruitment of inflammation effectors, such as CGAS, RIGI/RIG-I and NLRP3, to autophagosome membranes, leading to their SQSTM1/p62-dependent autophagic degradation. Also directly inhibits assembly of the NLRP3 inflammasome by preventing the association between NLRP3 and PYCARD. Acts as a negative regulator of antiviral innate immune response by suppressing the RIPK2-dependent pro-inflammatory response: mediates recruitment of RIPosomes, composed of RIPK2 and NOD1 or NOD2, to autophagosome membranes, promoting their SQSTM1/p62-dependent autophagic degradation. [Isoform IRGMd]: Acts as a positive regulator of mitophagy in response to intracellular mycobacteria infection: specifically binds cardiolipin, leading to its translocation to mitochondria, where it promotes affected mitochondrial fission and mitophagy. (Microbial infection) Following infection by hepatitis C virus (HCV), promotes HCV-triggered membrane remodeling, leading to autophagy and Golgi fragmentation, a step required for HCV replication.
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A1A519
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F170A_HUMAN
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Protein FAM170A (Zinc finger domain-containing protein) (Zinc finger protein ZNFD)
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MKRRQKRKHLENEESQETAEKGGGMSKSQEDALQPGSTRVAKGWSQGVGEVTSTSEYCSCVSSSRKLIHSGIQRIHRDSPQPQSPLAQVQERGETPPRSQHVSLSSYSSYKTCVSSLCVNKEERGMKIYYMQVQMNKGVAVSWETEETLESLEKQPRMEEVTLSEVVRVGTPPSDVSTRNLLSDSEPSGEEKEHEERTESDSLPGSPTVEDTPRAKTPDWLVTMENGFRCMACCRVFTTMEALQEHVQFGIREGFSCHVFHLTMAQLTGNMESESTQDEQEEENGNEKEEEEKPEAKEEEGQPTEEDLGLRRSWSQCPGCVFHSPKDRNS
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Acts as a nuclear transcription factor that positively regulates the expression of heat shock genes. Binds to heat shock promoter elements (HSE).
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A1A546
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ISX_MOUSE
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Intestine-specific homeobox
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MAGPTIHRDMEKSSGYCEAPENLGLSFSIEAILKKPTERRSLPRPQSICKEDSRQTTIPGSKLERPPQDQPQEEKKNKRRVRTTFTTEQLQELEKLFHFTHYPDIHVRSQLASRINLPEARVQIWFQNQRAKWRKQEKSGNLSAPQQPGEAGLALPSNMDVSGPVLTPTAMTTLVPPTECCLLSQTQLPSSWFPTQIPLVPWHPWDLQPLPGPLTQHPCVPTFMFPPLHPKWGSICATST
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Transcription factor that regulates gene expression in intestine. May participate in vitamin A metabolism most likely by regulating BCO1 expression in the intestine.
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A1A547
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PGRP3_MOUSE
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Peptidoglycan recognition protein 3 (Peptidoglycan recognition protein I-alpha) (PGLYRPIalpha) (PGRP-I-alpha) (Peptidoglycan recognition protein intermediate alpha)
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MLVSWDHPKMLPRLLGFLALSLLACGNPTIVSRKEWGASSLTCRVPLSLPVPYLIIEQVTRMQCQDQITCSQVVRVLQSQYVHNKGWCDIAFNFLVGDDGKVYEGVGWYVQGLHTQGYNNVSLGIAFFGSKIGSPSPAALSATEDLIFFAIQNGYLSPKYIQPFLLKEETCLVPQHSEIPKKACPNITPRSAWEARETHCPQMNLPAKFVIIIHTAGKSCNESADCLVRVRDTQSFHIDNQDFCDIAYHFLVGQDGEVYEGVGWNIEGSHTYGYNDIALGIAFMGNFVEKPPNEASLKAAQSLIQCAVAKGYLTSNYLLMGHSDVSNILSPGQALYNIIKTWPHFKH
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Pattern receptor that binds to murein peptidoglycans (PGN) of Gram-positive bacteria. Has bactericidal activity towards Gram-positive bacteria. May kill Gram-positive bacteria by interfering with peptidoglycan biosynthesis. Binds also to Gram-negative bacteria, and has bacteriostatic activity towards Gram-negative bacteria. Plays a role in innate immunity (By similarity).
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A1A5B4
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ANO9_HUMAN
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Anoctamin-9 (Transmembrane protein 16J) (Tumor protein p53-inducible protein 5) (p53-induced gene 5 protein)
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MQGEESLRILVEPEGDSFPLMEISTCETEASEQWDYVLVAQRHTQRDPRQARQQQFLEELRRKGFHIKVIRDQKQVFFGIRADNSVFGLYRTLLLEPEGPAPHAELAAPTTIPVTTSLRIRIVNFVVMNNKTSAGETFEDLMKDGVFEARFPLHKGEGRLKKTWARWRHMFREQPVDEIRNYFGEKVALYFVWLGWYTYMLVPAALTGLLVFLSGFSLFEASQISKEICEAHDILMCPLGDHSRRYQRLSETCTFAKLTHLFDNDGTVVFAIFMALWATVFLEIWKRQRARVVLHWDLYVWDEEQEEMALQLINCPDYKLRPYQHSYLRSTVILVLTLLMICLMIGMAHVLVVYRVLASALFSSSAVPFLEEQVTTAVVVTGALVHYVTIIIMTKINRCVALKLCDFEMPRTFSERESRFTIRFFTLQFFTHFSSLIYIAFILGRINGHPGKSTRLAGLWKLEECHASGCMMDLFVQMAIIMGLKQTLSNCVEYLVPWVTHKCRSLRASESGHLPRDPELRDWRRNYLLNPVNTFSLFDEFMEMMIQYGFTTIFVAAFPLAPLLALFSNLVEIRLDAIKMVWLQRRLVPRKAKDIGTWLQVLETIGVLAVIANGMVIAFTSEFIPRVVYKYRYSPCLKEGNSTVDCLKGYVNHSLSVFHTKDFQDPDGIEGSENVTLCRYRDYRNPPDYNFSEQFWFLLAIRLAFVILFEHVALCIKLIAAWFVPDIPQSVKNKVLEVKYQRLREKMWHGRQRLGGVGAGSRPPMPAHPTPASIFSARSTDV
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Has calcium-dependent phospholipid scramblase activity scrambles phosphatidylserine, phosphatidylcholine and galactosylceramide (By similarity). Does not exhibit calcium-activated chloride channel (CaCC) activity. Can inhibit the activity of ANO1.
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