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stringlengths 6
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stringlengths 11
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Q05016 | MSQGRKAAERLAKKTVLITGASAGIGKATALEYLEASNGDMKLILAARRLEKLEELKKTIDQEFPNAKVHVAQLDITQAEKIKPFIENLPQEFKDIDILVNNAGKALGSDRVGQIATEDIQDVFDTNVTALINITQAVLPIFQAKNSGDIVNLGSIAGRDAYPTGSIYCASKFAVGAFTDSLRKELINTKIRVILIAPGLVETEFSLVRYRGNEEQAKNVYKDTTPLMADDVADLIVYATSRKQNTVIADTLIFPTNQASPHHIFRG | Function: NADP-dependent dehydrogenase with broad substrate specificity acting on 3-hydroxy acids. Catalyzes the NADP-dependent oxidation of L-allo-threonine to L-2-amino-3-keto-butyrate, which is spontaneously decarboxylated into aminoacetone. Also acts on D-threonine, L-serine, D-serine, D-3-hydroxyisobutyrate, L-3-hydroxyisobutyrate, D-glycerate and L-glycerate.
Catalytic Activity: L-allo-threonine + NADP(+) = aminoacetone + CO2 + NADPH
Sequence Mass (Da): 29158
Sequence Length: 267
Subcellular Location: Cytoplasm
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P38430 | MNKLVDAHCHVITDPDNTFCGDDGGSQGTLRCVMSSNPYDWNNLKKLAGRSTSKNDICVGFGVHPWYSHLFYVGSRRDKVSHYQDVLEYKNEEQFDSLVQVLPEPLDLEEYIKREFNDTLVSVIGEIGLDKLFRLPANGFYMQNEKARLTTVKVKLSHQETVFRRFCRLARHTSKPISIHDVKCHGKLNDICNEELLTYHSVKICLHSYTGSKETLLGQWLKKFPPDRIFVSLSKWINFKDPEEGDALVRSLPSTCILTETDYPIDNPDPSYQKALTEQLQYLNAQIARAWDETLDASQAALRVYENFQKFIK | Cofactor: Binds 2 divalent metal cations per subunit.
Function: Putative deoxyribonuclease.
Sequence Mass (Da): 36032
Sequence Length: 313
EC: 3.1.21.-
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Q9USP2 | MVRKYGIFIDAGSSGSRLLIYSWDYDTDSSLSDKVKKLPLIETGIGDGGKWSLKVQPGISSFANNPKHVGKKHLKELLDFAAHAIPKDVHKETPVFLSATAGMRLLGVDAQNKILSHACRYIKKNYDFDIPNCSNSIRVIDGKAEGMYGWLATNYLLKTLEEKDTSTVGFLDMGGASVQIAFELPPSQLKNYKDSISTVHIGLQNGQQLEYPLFVTTWLGFGANEAYRRYLGLLIESENGKVGNTLSDPCSLRGRTYDIDGIEFAGTGDLKQCLKLTYNLLNKDKPCSMDPCNFDGISIPPVDFANTEFVGVSEFWYTTNDVFDMGGSYHFPNFYKKVDEYCGTEWETMLSRLYNKELTPSTDENKLEKLCFKASWALNVLHEGFDVPKSNTSSNDAKDGLSVIPAYHSPFTSLEKIERTEVSWTLGQVLLYASNQQLLAKPEYANYYMDPYGKLIASPSKHWMRLFPNKLFFILSFIFCLFFLFSLVLFGYDPKRRQRFKKFLLRLQRRKAPYIMSANGSYEDIADFSDDLEMSSPSKWHGPPIRTTSSHVLADRLSFTASRERTPRSPFP | Cofactor: Divalent metal cations. Ca(2+), Mg(2+) or Mn(2+).
Function: Catalyzes the hydrolysis of phosphoanhydride bonds of nucleoside tri- and di-phosphates. Required for Golgi glycosylation and cell wall integrity. Involved in N-mannosylation of proteins in Golgi.
Catalytic Activity: a ribonucleoside 5'-triphosphate + 2 H2O = a ribonucleoside 5'-phosphate + 2 H(+) + 2 phosphate
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 64680
Sequence Length: 572
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Golgi apparatus
EC: 3.6.1.5
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P40009 | MLIENTNDRFGIVIDAGSSGSRIHVFKWQDTESLLHATNQDSQSILQSVPHIHQEKDWTFKLNPGLSSFEKKPQDAYKSHIKPLLDFAKNIIPESHWSSCPVFIQATAGMRLLPQDIQSSILDGLCQGLKHPAEFLVEDCSAQIQVIDGETEGLYGWLGLNYLYGHFNDYNPEVSDHFTFGFMDMGGASTQIAFAPHDSGEIARHRDDIATIFLRSVNGDLQKWDVFVSTWLGFGANQARRRYLAQLINTLPENTNDYENDDFSTRNLNDPCMPRGSSTDFEFKDTIFHIAGSGNYEQCTKSIYPLLLKNMPCDDEPCLFNGVHAPRIDFANDKFIGTSEYWYTANDVFKLGGEYNFDKFSKSLREFCNSNWTQILANSDKGVYNSIPENFLKDACFKGNWVLNILHEGFDMPRIDVDAENVNDRPLFQSVEKVEERELSWTLGRILLYASGSILAGNDDFMVGIAPSERRTKLTGKKFIPGKLLESDQLRKQSSSLSNKGFLMWFAIICCIFYLIFHRSHIIRRRFSGLYNITKDFKTGIRRRLKFLRRSDPFSRLEEGELGTDVDGFKDVYRMKSSSMFDLGKSSATMQREHEPQRTASQSANLAPSNLRPAFSMADFSKFKDSRLYD | Cofactor: A divalent cation Ca(2+), Mg(2+) or Mn(2+).
Function: Catalyzes the hydrolysis of phosphoanhydride bonds of nucleoside tri- and di-phosphates. Has equal high activity toward ADP/ATP, GDP/GTP, and UDP/UTP and approximately 50% less toward CDP/CTP and thiamine pyrophosphate. Has no activity toward GMP. Required for Golgi glycosylation and cell wall integrity. Together with CDC55, required for adenovirus E4orf4 (early region 4 open reading frame 4) induced toxicity, the apyrase activity is not required for this function. Plays a role in sphingolipid synthesis.
Catalytic Activity: a ribonucleoside 5'-triphosphate + 2 H2O = a ribonucleoside 5'-phosphate + 2 H(+) + 2 phosphate
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 71852
Sequence Length: 630
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Golgi apparatus
EC: 3.6.1.5
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O31809 | MFSPTSKITTAQATIIIINYMLAAGVLTLPRTVTEQTQSPDGWISVLLGGVLAVIAGMIIAKLSQQYPKETFYEYSRHIVGKWLGHLISIVFITYFLALGAFEVRVMSEIVDFFLLEGTPSWAIIMTVLWIGLYSITQGLDPIARLFEMIFPITVIIFLTIALMSLGIFEINNLRPVLGDGIMPVLRGVKTTNLSFTCSEIMFILVAFMKKPKNAVKAVVIGTGVVTSFYMITMIMVIGALSVEGVVTRTWPGLDLMRSFEIPGLIFERFESFLLVIWIMQLFATFIITFYAASLGVSQVFKKKPLSCMFGLLPVIYILSCMPKNENDVFILGDTVSHIALYIFGALPILLLVISKWRKRGEK | Function: Involved in the germinative response to L-alanine. Could be an amino acid transporter (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 40471
Sequence Length: 363
Subcellular Location: Cell membrane
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O31810 | MKSKLKRQLPAMVIVCLLMICVTGCWSSREIEDLGLTFAIAIDKGKETNTEKELKEEGGSYPKKDNITLTYQFVNEKAAGAGTSGGGGSGQGAQKAYINISETGDSLQQIGSEVALRRDREVFSPHLKVVVMSEDVLHTFPIDEMLDQFFRDNEIRLSCLVLSAKGEARDALQLKENGEIPAFRLIGLGENEHKVSRILPPMTLAKLIGKLHSGSSFLLQNVVAANGAVKYSGAAVINGKSKKMIGTLNEYETEGITWIRGEGKGGVVKSHDKKSQQTLAYDINKIKSRIQPIVKGKDISFHVDIESEGDLVENWNTKEALDTQFIDRLETTIENEVKKIVGQVLKKIQHDYKADVAGFDESFRLTYPHLWKRVKNNWDDTFSKADITYSVNVTITHFGTVKTQ | Function: May be involved in spore germination.
Location Topology: Lipid-anchor
Sequence Mass (Da): 44824
Sequence Length: 404
Subcellular Location: Cell membrane
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P76193 | MKRASLLTLTLIGAFSAIQAAWAVDYPLPPTGSRLVGQNQTYTVQEGDKNLQAIARRFDTAAMLILEANNTIAPVPKPGTTITIPSQLLLPDAPRQGIIVNLAELRLYYYPPGENIVQVYPIGIGLQGLETPVMETRVGQKIPNPTWTPTAGIRQRSLERGIKLPPVVPAGPNNPLGRYALRLAHGNGEYLIHGTSAPDSVGLRVSSGCIRMNAPDIKALFSSVRTGTPVKVINEPVKYSVEPNGMRYVEVHRPLSAEEQQNVQTMPYTLPAGFTQFKDNKAVDQKLVDKALYRRAGYPVSVSSGATPAASNAPSVESAQNGEPEQGNMLRVTQ | Function: Responsible, at least in part, for generating a meso-diaminopimelyl-3-a meso-diaminopimelyl-3 cross-link.
Sequence Mass (Da): 36082
Sequence Length: 334
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Periplasm
EC: 2.-.-.-
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Q3E7B9 | MWRSYLVFLFFMTPRIQTYCPVPVLRSMAVLNIISPLIIFVSPIKKQDSLHSSACYANLTLVEKLQLWHSMSND | Function: May be involved in the regulation of telomere length.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 8604
Sequence Length: 74
Subcellular Location: Membrane
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Q53684 | MRTRITLALAVLLLLLAGCSPGAPADGPVTLRFQSLAWQPDSVAATKELVGEWNATHPDVKVEYIQGSWDSVHDQLLTSFEGGEAPDVIHDASDDLADFAYGGYLADLSGLLPARLASDIPRGSWETATFGRGVYGVPFLQEPRVLIADADRLRAAKVRIPTPGHPWSWPEFRQVAKKLTGPGRYGVAWPLKEPVSATLNLSLSAGGRLFHRGADDKVTVRFEAGDEVVARTIHDQVAVDREHAPASTLGSGGADTLPGLFGGRYAMVPLGFSYRQQIVRQAPEDFHWQVLPAPAGAGGLTQGVSPQTLSVSADCPHKKEAVAFIDFLLRPRNMVRLALGDWMLPTGTQALKDPALHTARHGWATGTALAARLRPAPAQSVRGYPEWKDKVATPAYQRYYSGASTLADVRHAWSGTATWCWPATSADPPPGVPRAGKRNIRDATSRLPSTP | Function: May participate in oleandomycin glycosylation and secretion during antibiotic production.
Location Topology: Lipid-anchor
Sequence Mass (Da): 48542
Sequence Length: 451
Subcellular Location: Cell membrane
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O74860 | MTFPNVKFIGNKRVLSIQSSVSHGYVGNRSATFPLQLHEWEVDVVPTVHFSNHLGYGATRGSACIPEEVHDLLNALLQDNGIVYDAILTGFVPNHDIIQVIFDCVLAYKKDHPKVLWLLDPVMGDQGKMYVDTNVISTYKAMIPHAFAITPNAFEVEILTDIVIHTQMDAKRGLEKIYQLYGIQNAIITSFEVEESPGTLFCMGYSCEHGKPQLFLYQFPSLSGVFTGTGDLFSGLLLAKYREELDKRKHQQSDETKQTKRPTVLACAVGQVLSCMHTVLVNTKTYADEILLEDPKIASDEFLLSNARELRLIQSRTALLSKKSIYEAEFLPGFEEGEDV | Function: Required for synthesis of pyridoxal-5-phosphate from vitamin B6.
Catalytic Activity: ATP + pyridoxal = ADP + H(+) + pyridoxal 5'-phosphate
Sequence Mass (Da): 38080
Sequence Length: 340
Subcellular Location: Cytoplasm
EC: 2.7.1.35
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P77475 | MYERYAGLIFDMDGTILDTEPTHRKAWREVLGHYGLQYDIQAMIALNGSPTWRIAQAIIELNQADLDPHALAREKTEAVRSMLLDSVEPLPLVDVVKSWHGRRPMAVGTGSESAIAEALLAHLGLRHYFDAVVAADHVKHHKPAPDTFLLCAQRMGVQPTQCVVFEDADFGIQAARAAGMDAVDVRLL | Cofactor: Magnesium. Can also use other divalent metal cations as manganese, cobalt or zinc.
Function: Catalyzes strongly the dephosphorylation of fructose-1-phosphate (Fru1P) and slightly the dephosphorylation of 6-phosphogluconate (6P-Glu). It has low beta-phosphoglucomutase activity.
Sequence Mass (Da): 20780
Sequence Length: 188
EC: 3.1.3.-
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Q726N6 | MKFLGIDYGQRRTGIAVTDAGGRMAFPRRTIAMTTRDAFFVELLGMVEVECPDAFVVGLPRLPGGEETLTTRQVRNFVERLKRRTTLPVYFMPEELSSFEAEDDLRDAGLRGRRLEAVVDQQAAVRILESFLAVPEERRSLA | Function: Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA.
Sequence Mass (Da): 16036
Sequence Length: 142
Subcellular Location: Cytoplasm
EC: 3.1.-.-
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B8E227 | MRVLAIDWGEKYIGLAISDPLRIIAQGLDVWEIKDEEDFVNRLKKLIKEYNVSEIVLGYPISLRGHENEKTKKIEYVAERIKTVVNLPIKFVDERFTTMEAERVLLEGDIKRRDRKLLKNKQAAVIILQKYLDSLSLDTKI | Function: Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA.
Sequence Mass (Da): 16470
Sequence Length: 141
Subcellular Location: Cytoplasm
EC: 3.1.-.-
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A2BW38 | MKYSKPKSKSILSLDIGTKRIGLAYCDSLFITVNILPALRREKNKNEFKTIKSHIKKLNLTGFIVGLPLDDKGRMTSQAFDCKTYGEYLFNELKLPFSFVNEHSSTWESENRFGVKKDKSGLIDSLSAKVILEQWIQEGPELKELMGNKQI | Function: Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA.
Sequence Mass (Da): 17248
Sequence Length: 151
Subcellular Location: Cytoplasm
EC: 3.1.-.-
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Q46LD7 | MIQPKPCSVLSLDIGDKRIGIAGCDPLGISITHLPAIFRDSFEKDLKEFEKICFDRRVEGLICGNPLDMNGMETKQSIRCKKYGIKLAKCLKLPLAFINEHCSTVEAKEKFSLKNDKTGRIDSAAAAILLQQWLIEGPDLDDSN | Function: Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA.
Sequence Mass (Da): 16010
Sequence Length: 144
Subcellular Location: Cytoplasm
EC: 3.1.-.-
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C3K3K0 | MALRLILGFDYGTKQIGVAVGQVITGQARELCTLKAQNGIPDWNQVEALIKEWKPDAVVVGLPLNMDGTPSDMCLRAEKFARRLNGRYNIPFYTHDERLTTFEAKGERRDRGGQKGSYRDNPVDAIAAALLLQGWLDENTALFES | Function: Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA.
Sequence Mass (Da): 16168
Sequence Length: 145
Subcellular Location: Cytoplasm
EC: 3.1.-.-
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A1JPT6 | MANRTIVAFDFGTKSIGVAIGQEVTGTARALTSFKAQDGTPDWQKVEKLLKEWQPDLVVVGLPLNMDGTEQPLTARARRFANRLHGRFGVQIALQDERLSTVEARANLFDSGGYRALDKGSVDAASAVIILESWFDEQAG | Function: Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA.
Sequence Mass (Da): 15264
Sequence Length: 140
Subcellular Location: Cytoplasm
EC: 3.1.-.-
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Q5NPF1 | MDEKREENILKKQEELRLFQEALPRKGRLAGLDVGTKTIGLALCDSQWIIASPAETIRRKKFTLDLELLRQFVEKQQVKGLVIGLPLNLDGSDSPRTQSVRAFAKNVAPLSLPVLMWDERWSTKAVTRTLLEADASRARRSEVVDKMAAAYILQGAIDSFAMF | Function: Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA.
Sequence Mass (Da): 18356
Sequence Length: 163
Subcellular Location: Cytoplasm
EC: 3.1.-.-
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P46339 | MINNRENMSVSERLISSRQNRQLDEVRGRMIVTACALIMIAASVAITIFLGVKGLQSFLVNGVSPIEFLTSLNWNPTDSDPKYGVLPFIFGSFAVTILSALIAAPLGIAGAIFMTEIAPNWGKKVLQPVIELLVGIPSVVYGFIGLTVLVPFIAQFKSSGTGHSLLAGTIVLSVMILPTITSISADAMASLPKSLREGSYALGATRWQTIRKVLVPAAFPTLMTAVVLGMARAFGEALAVQMVIGNTRVLPESPFDTAGTLTTIITLNMGHTTYGSVENNTLWSMGLVLLVMSFLFILLIRYLSSRRKV | Function: Part of the binding-protein-dependent transport system YqgGHIJK. Probably responsible for the translocation of the substrate across the membrane (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 33193
Sequence Length: 309
Subcellular Location: Cell membrane
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P46340 | MNRKITDKLATGMFGLCAAIIAAILVGLFSYIIINGVSQLSFQFITTKSSAIAAGGGIRDQLFNSFYILFITMLITIPLGVGGGVFMAEYAPNNKVTDFIRTCIEVLSSLPSIVIGMFGLLMFVNLTGWGYTIIGGALALTVFNLPVMVRVTEDAIRSVPKDLKEASLALGVSRWHTVKTVLIPSAIPSIITGAILASGRVFGEAAALLFTAGLTTPRLNFTEWNPFSETSPLNIFRPAETLAVHIWNVNTQGMIPDAEAIANGGSAVLVISVLVFNLAARWLGTMIYKKLTAN | Function: Part of the binding-protein-dependent transport system YqgGHIJK. Probably responsible for the translocation of the substrate across the membrane (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 31436
Sequence Length: 294
Subcellular Location: Cell membrane
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Q5UQV6 | MSPEQWGIYGWTFSHAVALGYPINPTEEDKLRYYTFFNSYRYVLPCGKCRINYADHLNKYPLTDEVLSSRENLVKWTIDIHNVVNYYTGKKMLTYPEAIEAIEKTLTPKKKSSYNWFFIILIIIGIIVIIYLMYIVFKKKLNK | Function: FAD-dependent sulfhydryl oxidase that catalyzes disulfide bond formation.
Catalytic Activity: O2 + 2 R'C(R)SH = H2O2 + R'C(R)S-S(R)CR'
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 16981
Sequence Length: 143
Subcellular Location: Membrane
EC: 1.8.3.2
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Q5UQJ6 | MMNKKNNKYKSDSLDSKEDKVDLYQDAMISNLISVNNKSTSDSDAKKPTENRIELLKNAYKGGTLKPMIDFDDHNTETFMDKRITKNLLDARSLFLSMGVKLIYIKSGTTGHTFKAISRSNKNVVFAVKVCAYPKDDYGGIKSSSRPENVEIRMLKILSYFVVNRLTPHLVLPIGTFHTDIEKFINIPEGVIDLKDEKNDMYKKFIERYHDGEFEKFVSVLISEWCNGGDLLDYIRKNYDSMTLETWTVVIFQLLFTLALIHEKFPAFRHNDMKANNILVEKTDNKHEGPDKWYRYSLGSHVFIIPGIGIQIKIWDFDFASIDGIVENKKVNADWTKKINISKKKNMYYDMHYFFNTLISKRFFPQFYEGGVPQEIVDFVHRIVPEEFRNGSDNINKKGRILVDVEYTTPFKVIMTDPLFEKYRYNQYYFHPQRNMAPKKSILFQQGNGSKQPVPKKSTGQKPTKKV | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 54371
Sequence Length: 467
Subcellular Location: Virion
EC: 2.7.11.1
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O32052 | MMTGTLGTLVPIILMFAVLYFLLIRPQQKQQKAVRQMQEELKKGDSVVTIGGLHGTVDSIDESKVVIKTGDNTRLTFDRRAIREVSAAE | Function: The SecYEG-SecDF-YajC-YidC holo-translocon (HTL) protein secretase/insertase is a supercomplex required for protein secretion, insertion of proteins into membranes, and assembly of membrane protein complexes. While the SecYEG complex is essential for assembly of a number of proteins and complexes, the SecDF-YajC-YidC subcomplex facilitates these functions.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 9904
Sequence Length: 89
Subcellular Location: Cell membrane
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Q11082 | MSLSGQLWKMVNSTSPNAAATVGNIAYCYVLPCICAIGIVGNITNLMVLASRRLRAVSYMYLRALAVADLLCMLFVLVFVSTEYLAKNGSSINQYKLYQIYQCHLMLTLINWALGAGVYVVVALSLERYISIVFPMHFRTWNSPQRATRAIVIAFLIPAIFYVPYAITRYKGKQRFDLLQNVTIYSMDDHPIYTTFYWQIYKWTREAILRFLPIIILTVLNIQIMIAFRKRQKMFQQLTNKRKEQGTQKDDTLMYMLGGTVLMSLVCNIPAAINLLLIDETLKKRLDYQIFRAVANILEITNHASQFYVFCACSTDYRTTFLQKFPCFKTDYANRDRLRSFVRRTQSVIQKQGSVEHTTNSKVWIMFKNKFQRDSLSHHSRKFSRHMPIEQDTVDIQLASGEQSTSGEMCEADTLIKYGGTAQLCNDENNTTFL | Function: Not known. Putative receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 50027
Sequence Length: 434
Subcellular Location: Cell membrane
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P48458 | MSTDGNNNKKGSKEGPKSSEISKFDLAKENPKLAEWMDDCIKRMNSLYKDTNINICNVMTGHEIISIIRMVEAIFMEESNLCEAEAPIKVIGDIHAQYQDMNRLFDLIGRVPEEKLMFLGDYVDRGPQGIEVLILLFCLKIRYRDRIYLLRGNHETPSVNKIYGFYVECQYKYGIGLWWDFQSCFNRMPMSGLISKRVLCMHGGLSPELINLDTIRNIPRPCEPLDRGLLIDLLWSDPTNKGEGWFHSIRGISYMFGKGVVEQACKSLEIDLIIRAHQVVQDGYEMMTGRRLITVFSVPNYCAQFTNAAAVVCLNANLQISFQQMIPPPLPEGTKAKAAPAIAIDPNIDAARADKDAIKPFVKE | Cofactor: Binds 2 manganese ions per subunit.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 41208
Sequence Length: 364
EC: 3.1.3.16
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Q9HGM3 | MRNPFLTFRAPTRKTGDYLVSKFVKKDNFSSLRLARAYTFSTRSTAVSQFSLLSLSQRSFQSLKINKGIPEKHKIPLISSKQFSVTSKRSQNGSSGSNSDANGRKNGQKNDDSKKKGLNGNDPKKVFEIALNGNTILGGILVAYILYNVLSPNANMQEITWQDFRQQFLDKGLVERLVVVNRNMVRVILRGGVASGSGQYYFSIGSIDSFDRKLEDAQRQLGIPPSEFVPVAYHDEVSVLATLLSFAPTLLIIGSVIYLSRRASGAAGGGQGGIFGIGKSRAKMFNHETDIKIKFADVAGVDEAKEEIMEFVKFLKNPKFYERLGAKIPRGAILSGPPGTGKTLLAKATAGEANVPFLSVSGSEFLEMFVGVGPSRVRDLFATARKNAPCIIFIDEIDAIGKARGRGGQFGSNDERESTLNQLLVEMDGFTSSEHIVVFAGTNRPDVLDPALLRPGRFDRQITIDRPDIGGREQIFKVHLKHIKAADNIDLIAKRLAVLTSGFTGADIMNVCNEGALIAARSNSNEVQMVHFEQAIERVTAGLEKKSRVLSPEEKNTVAHHEAGHAVAGWFMEYVDPLLKVSIIPRAQALGYASYLPKDQYLMSRGQILDQMGMALAGRVSEEIFFGPEKITSGASDDFQKVTRMAQAYVTQYGMSPTVGTIAYPIDTRETVQKPFSEATAQMIDEEIRKLVKHAYERTKKLLLEHKQGLENIAQRLLQKEVITYNEVETILGPRPYAYKHLNISELMRQSEYKNDHDPRNPPIPPSPQQPSA | Cofactor: Binds 1 zinc ion per subunit.
Function: Acts as a component of the m-AAA protease complex which is a ATP-dependent metalloprotease mediating degradation of non-assembled mitochondrial inner membrane proteins. The complex is necessary for the assembly of mitochondrial respiratory chain and ATPase complexes. Function both in post-translational assembly and in the turnover of mistranslated or misfolded polypeptides (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 85369
Sequence Length: 773
Subcellular Location: Mitochondrion membrane
EC: 3.4.24.-
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O49312 | MCNNNNTSCVNISSMLQPEDIFSRRCIWVNGPVIVGAGPSGLAVAADLKRQEVPFVILERANCIASLWQNRTYDRLKLHLPKQFCQLPNLPFPEDIPEYPTKYQFIEYLESYATHFDLRPKFNETVQSAKYDKRFGLWRVQTVLRSELLGYCEFEYICRWLVVATGENAEKVVPEFEGLEDFGGDVLHAGDYKSGERYRGKRVLVVGCGNSGMEVSLDLCNHDASPSMVVRSSVHVLPREVLGKSTFELSVTMMKWMPVWLVDKTLLVLTRLLLGNTDKYGLKRPEIGPLELKNTAGKTPVLDIGAISMIKSGKIKIVAGIAKFGPGKVELVDGRVLQIDSVILATGYRSNVPSWLKENDLGEIGIEKNPFPKGWKGKAGLYAVGFTGRGLSGASFDAMSVAHDIANSWKEETKQQIKTVATRHRRCISHF | Function: Involved in auxin biosynthesis. Belongs to the set of redundant YUCCA genes probably responsible for auxin biosynthesis in roots.
Catalytic Activity: H(+) + indole-3-pyruvate + NADPH + O2 = (indol-3-yl)acetate + CO2 + H2O + NADP(+)
Sequence Mass (Da): 48148
Sequence Length: 431
Pathway: Plant hormone metabolism; auxin biosynthesis.
EC: 1.14.13.168
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Q9SVU0 | MENMFRLMDQDQDLTNNRCIWVNGPVIVGAGPSGLATAACLHEQNVPFVVLERADCIASLWQKRTYDRLKLHLPKQFCQLPKMPFPEDFPEYPTKRQFIDYLESYATRFEINPKFNECVQTARFDETSGLWRVKTVSKSESTQTEVEYICRWLVVATGENAERVMPEIDGLSEFSGEVIHACDYKSGEKFAGKKVLVVGCGNSGMEVSLDLANHFAKPSMVVRSSLHVMPREVMGKSTFELAMKMLRWFPLWLVDKILLVLSWMVLGNIEKYGLKRPEMGPMELKSVKGKTPVLDIGAIEKIRLGKINVVPGIKRFNGNKVELVNGEQLDVDSVVLATGYRSNVPYWLQENEFFAKNGFPKTVADNNGWKGRTGLYAVGFTRKGLSGASMDAVKIAQDIGSVWQLETKQPTKRSRGSLRRCISQQF | Function: Involved in auxin biosynthesis. Belongs to the set of redundant YUCCA genes probably responsible for auxin biosynthesis in roots.
Catalytic Activity: H(+) + indole-3-pyruvate + NADPH + O2 = (indol-3-yl)acetate + CO2 + H2O + NADP(+)
Sequence Mass (Da): 48110
Sequence Length: 426
Pathway: Plant hormone metabolism; auxin biosynthesis.
EC: 1.14.13.168
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B8ANW0 | MQGQQKQNAGGGGGDNASPCIVLDGPIIVGAGPSGLAVAATLRQHGAPFTVVERSGGVADLWTNRTYDRLRLHLPKVFCELPHVAFPPDFPTYPTKHDFLRYLHSYAARFAIAPLLRRTVTRAWYDHPASLWRVTTTTTSSSATSVITEYASPWLVVASGENAEVVVPKVKGRERFAGEALHSSEYRSGERFRGMRVLVVGCGNSGMEMCLDLCEHGAMPFMSVRSGVHVLPREMFGASTFGIAMKLLRWLPIKMVDRFLLLVARMVLGDTEKYGLKRPKLGPLEIKNITGKSPVLDVGAWSLIKSGNIKIVPEVESFSGNGARFVDGNEMAFDAVIFATGYRSNVPSWLQEDGELFTEEGKLRSSGSSSEWRWRGPNGLYCVGFSGRGLLGAGADALRAAADIAGRWQETQQAAANISSV | Function: Involved in auxin biosynthesis . Converts the indole-3-pyruvic acid (IPA) produced by the TAA family to indole-3-acetic acid (IAA) (By similarity). Seems not able to use tryptamine (TAM) as substrate (By similarity). Probably responsible for auxin biosynthesis in leaves and involved in the regulation of lateral leaf growth (Ref.3). Required for maintaining water homeostasis and an appropriate root to shoot ratio (By similarity). Required for the inhibition of root growth by ethylene in etiolated seedlings (By similarity). Functions downstream of the ethylene-response transcription factor EIL1 (By similarity).
Catalytic Activity: H(+) + indole-3-pyruvate + NADPH + O2 = (indol-3-yl)acetate + CO2 + H2O + NADP(+)
Sequence Mass (Da): 45720
Sequence Length: 421
Subcellular Location: Endoplasmic reticulum
EC: 1.14.13.168
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O32100 | MLSFSLFIPSAAAAQTEENTDVAPNQYEKKDIEIDTNYLHEDTYYEEKTELPEEQKDITFDKPKDKDAELIKDLFTSTNAEDSNTIAAQSKQLGITFAEKPMTKTSSTETEDEQETSSLLLPMIYVVLILLGIAGIVFLIPKVTAQENKKA | Function: Required for YukE secretion. Probable component or regulator of the ESX/ESAT-6-like secretion system (BsEss).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 16915
Sequence Length: 151
Subcellular Location: Cell membrane
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O34451 | MRKAFTRIRLRNNRYAAYIIGFSFLAVSIILGISCGSLHIPIPAVFRVFWHQGFGGSIGSDDPMYTNIMMNIRLPRVVLAALVGAALSIAGAAFQGLLKNPLADPYTLGVSSGASVGAVVTLFLGLHLPVIGGFTLPVLSVAAALATMAAVLFFSRLVHASMSVSTLILTGVITNSFLGAFISLIIALTGDNLLPIVHWLLGSVSMRGWSYVILFLPFFLLGTILLIINGRELNVMTYGEDKAKLLGVSVQQRKMMILIAGSLLTGSAVAVSGTIGFVGLVIPHITRLLWGTDHRHLLPLSALLGAGFLVLADLLSRTIIEPIELPIGIITSLAGAPVFALILIRQHRGGRSL | Function: Probably part of an ABC transporter complex. Probably responsible for the translocation of the substrate across the membrane (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 37497
Sequence Length: 353
Subcellular Location: Cell membrane
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O34805 | MKKRAGIWAALLLAAVMLAGCGNPADQKDSKAKQKTEVFPVTIDDASNQDVTIKKEPKKIVSLMPSNTEITYALGLGDKVVGVTTNDTYPKEVKKVEKVGDMNVNVEKVISLKPDLVLAHESSMSASADAIKQLKDAGITVLTVNDAQSFSEVYKSIEMIGEAGGAEKKADQLVKSMKSDLKDIQEKAKTISKDEEKSVFIEVSPDPDIYTTGKDTFMNEMLNVIHAKNAAADQTGWVQMTDEAIVKLNPDAIVTTDGVKAKAVEKRDGWSEINAVKHHRVYDVDPDLVTRSGPRLIEGVEELAESIYPDTFKE | Function: Probably part of an ABC transporter complex.
Location Topology: Lipid-anchor
Sequence Mass (Da): 34239
Sequence Length: 314
Subcellular Location: Cell membrane
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O34940 | MDAVLEADTRAVIGEGPLWDEENGRLYWVDILGSELHIFDPEEKINRSIKFKSFVTALAKYSKDELIMTMKDGFYLYHLRDDSLEKIKQPKDMHESLRFNDAKCDPYGRLWAGTTSMEGEQKQASLYRLNLDGSLVKIKDQVSTSNGLDWDRERNLMYYIDTPTQEIVRYSYDPQSGDVSNPEPVYRFDQSDGLPDGMTIDQNGMLWVALFGGSRVVHIDPFQKKEINSISVPAKYVTCCAFGGRDLKTLYITTATEQMTEKERYEQPHAGGLFSAQLETGGYQPVPFAGDV | Cofactor: Binds 1 divalent metal cation per subunit.
Sequence Mass (Da): 33204
Sequence Length: 292
Subcellular Location: Cytoplasm
EC: 3.1.1.-
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O34989 | MRLRWKFLFHFFGQMLIVILLLTVMLVASFFYLDARFSDAESNSGLTKATTDTLEAYLDVNEDGTWEVDNFLKKSVDKQHGWMQIIDSEGNTDYSYGVPKDVPGTYTKKELLSIYKTKKLHNYKLNYWAINIEDKSYLLLSGWKSKSEQLLTSVEKREQKIDSLAHYKSSTIDYIKRKKGAIYLLDSNGKILDSINSTKSERKTMNQLELLKYSSKPWNYKREISVKILNKDRWMVATVPNPVYVTDQEFNKSFLKVVLKAMFLVMAVLFMYIIWMTVWYMFRFGLPIFHTIRWLVNLSKGKLEEPRNREGRPVSKNKKGKIKQPYRFFGEIFESMDQLTETLRRDKRNREKIQATREEWIAGLSHDLKTPLSSIYGYSMMLESKQYDWSPEEVKEMGQVVREKSEYMSKLIEDLNLTYRLKNDALPIERKLTSLIPFFKNVIEDFKKNPFSEGYDISFVSKEEHIEFALDEAWFRRILENLLGNAVKHNGKGTEIQVILEQTKNHISLKVKDNGKGMDEETITHLFNRYYRGTNTKDSTAGTGLGLAIAKELVHLHNGTIHVNSRTNIGTVITILFKKQ | Function: Member of the two-component regulatory system YvrG/YvrH that positively regulates 7 transcriptional units (wprA, wapA-yxxG, dltABCDE, sunA, sunT-bdbA-yolJ-bdbB, sigO-rsoA, and sigX-rsiX), and negatively regulates the lytABC operon. Probably activates YvrH by phosphorylation.
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 67799
Sequence Length: 580
Subcellular Location: Cell membrane
EC: 2.7.13.3
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P94504 | MENASILIVDDEKAIVDMIKRVLEKEGYRNILDAASAEEAIPVVKANKVDLIVLDVMMGGMSGFEACTLIREYSDAPIFFLTARSSDADKLSGFAVGADDYITKPFNPLELAARIRAHLKRTYQSKETSSNQTYTYDYFTFSPQNAELIVGGEAVACSAQLLQLLQYFCEHPNVVLSKDQIYEKVWGYPSYGDNNTVMVHIRKLREKIERDPSNPEYIVTVRGLGYRFIPNPEGKRS | Function: Member of the two-component regulatory system YvrG/YvrH that positively regulates 7 transcriptional units (wprA, wapA-yxxG, dltABCDE, sunA, sunT-bdbA-yolJ-bdbB, sigO-rsoA, and sigX-rsiX), and negatively regulates the lytABC operon.
PTM: Phosphorylated by YvrG.
Sequence Mass (Da): 26679
Sequence Length: 237
Subcellular Location: Cytoplasm
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O34686 | MKHQNPSKRLLRLSIKYLLAAAAVVLTYFAVIYILFSLAGTSYRSAAHVLLFAVVFLVLGLCFEPFERLMIHSFTFFKTGKRLFILLAGIVQLLFLWMTAHTTDQLISDIWLSTTEEMIVAAVFLILDKCNSALPS | Function: Negatively regulates RNA polymerase sigma factor SigO-dependent transcription. Prevents the expression or secretion of OxdC under nonstress conditions. May act as an anti-sigma factor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 15360
Sequence Length: 136
Subcellular Location: Cell membrane
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P42421 | MNKIMIVEDSEDIRGLLQNYLEKYGYQTVVAADFTAVLDVFLREKPDVVLLDINLPAYDGYYWCRQIRQHSTSPIIFISARSGEMDQVMAIENGGDDYIEKPFSYDIVLAKIKSQIRRAYGEYAAKQGEKVVEYAGVQLFVERFELRFQDEKSELSKKESKLLEVLLERGEKVTSRDRLMEKTWDTDIFIDDNTLNVYITRLRKKLRELNAPVSIEAVRGEGYQLRAQS | Function: Probable member of the two-component regulatory system YxdK/YxdJ. Positively regulates the expression of the yxdLMyxeA operon by direct interaction with its promoter region. Could also indirectly regulate the expression of the dlt operon.
PTM: Phosphorylated by YxdK.
Sequence Mass (Da): 26600
Sequence Length: 229
Subcellular Location: Cytoplasm
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P42422 | MKLFLRSHAVLILLFLLQGLFVFFYYWFAGLHSFSHLFYILGVQLLILAGYLAYRWYKDRGVYHWLSSGQEGTDIPYLGSSVFCSELYEKQMELIRLQHQKLHETEAKLDARVTYMNQWVHQVKTPLSVINLIIQEEDEPVFEQIKKEVRQIEFGLETLLYSSRLDLFERDFKIEAVSLSELLQSVIQSYKRFFIQYRVYPKMNVCDDHQIYTDAKWLKFAIGQVVTNAVKYSAGKSDRLELNVFCDEDRTVLEVKDYGVGIPSQDIKRVFDPYYTGENGRRFQESTGIGLHLVKEITDKLNHTVDISSSPGEGTSVRFSFLTKM | Function: Probable member of the two-component regulatory system YxdK/YxdJ. May activate YxdJ in response to the antibacterial protein LL-37.
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 37989
Sequence Length: 325
Subcellular Location: Cell membrane
EC: 2.7.13.3
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P42424 | MTFLQFAYKNVTRNKRAYLAFFLSSAFSVLIFFTFAMFLFHPALKEGYLNNIAKKGLTAAEWMIFVFSFLFVLYSVNAFLKSRNKEFGILLMQGITPGQLRKLITAENMIIGVMSIAAGIIGGFIFSKTFFTVGAYILEMDALPLYMPWKALGITACGFLLLFFFLSQFTILFVRSNTVIKLIKGTGKVKPEPKPSVLLSLFGIACLCGGYGMVLKGNVHGAEPFIILLLTVIGTYFFFSQSSIWILRALKKWKTFYLRGKNIIWVSDLVYRLKDNARLFFIVSIISAVAFTATGVLAMYKSTVGAEESAYEMEYLSYSNNPKEQTHLKDIDHELKTHGFTYTKDKIDVSYVRYQEGETVPPVYMISESDAAKYFHVKVNGLKEDEAVYFPGTYDRNFKNEAPDQLKLLNQKGELSDQKLSVKEVKKPLISLNAIIAVNDQTFDQLKSLGDKASLYGYSYDHWKDSLEISQSLQNEIYGNYIDVHSDFASKAGTYYDTVQLPSLSLFIGLFIAIVFFVAAASFLYFRLFTDLDEDRERYRSLAKIGLSEREMAQSVTIQLAILFFFPFVIAVMHTLFALRTLAVEGYSDVAGPLSLTIGGFFIFQLLFFLAVRSSYLKKMNK | Function: Part of the ABC transporter complex YxdLM which could be involved in peptide resistance.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 70477
Sequence Length: 622
Subcellular Location: Cell membrane
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P54941 | MKKNILLVGMLVLLLMFVSACSGTASKGSSSDSASEKTEMRTYKSPKGNVNIPAHPKRIVTDFYAGELLSVGANVVGSGSWSFDNPFLKSKLKNVKDVGDPISVEKVMELQPDLIVVMNEENVDKLKKIAPTVVIPYNTAKNVEDTVSMFGDIAGAKDQAKSFMADFNKKAEAAKKKIAGVIDKDATFGIYENTDKGEFWVFNDNGGRGGQAVYNALGLKAPEKIEQDVIKKGEMKQLSQEVIPEYAADYMFITDYNPKGESKTLDKLENSSIWKNLDAVKHNRVFINDFDSFYPYDPISVSKQVDIITDMLIKRAEENKK | Function: Part of the ABC transporter complex FhuCBGD involved in iron(3+)-hydroxamate import. Binds the iron(3+)-hydroxamate complex and transfers it to the membrane-bound permease. Partially required for the transport of desferrioxamine.
Location Topology: Lipid-anchor
Sequence Mass (Da): 35507
Sequence Length: 321
Subcellular Location: Cell membrane
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Q5ISE2 | MANNNLNRPLNTNVADSSNSSSTPGTAPPPSSSDPQVLGHQAPSSSASSLTEDCSSSFARDLNSYNNGQSGATGAVSWEAPHEPSEANAVSQIHPRNGEHSLQQKPKPQKVSGSSSLATSERYKTELCRPFEESGICKYGHKCQFAHGYRELRTLSRHPKYKTEPCRTFHSVGFCPYGTRCHFIHNQPEQQPVLSESTLEEPSSFNGSNVLHLGVNGEQQPGLQSDSPSGFLSVNSQALQAPLQLNQQALSSGGVMPSSHPAAANLRMMCCRTSSSTTAHDADKDPDKDADKDPSNNSANDALAFPQEPGDFSPVAFQNPNTATTTPTAFYNNQQQMGLAASAQFQMPLARPLPSATIFGQASVGPALTPGAAMAPGAALAPAAALTPAAALAPGAAMALGAAMATGAAMATGAALTPGAALALGAAMAAGAALAPGAAMAPGAAMATGAALAFGAAMATGTTLTPGAAMALGAAMATGAALAPGAAVAPRAALAPRAAFAPGAAALAPRAALPPGAALTPGAALAPGAALAPRAALPPGATLRPGAALIPRAALAPGAALAPGAALTPGAALAPGATLAPRAALAPGAALAPRITITSRAAITPGVAIAPGVATASTGILAPGAATATVGNTSSTTITAATAAEGAAPHFTFQLPDVESESESESLEFDVVTSTLDSLLVSDDEDEDDFLRRSSSSSSLNESEFDNTNSSRRLPIFSRFSDSEK | Function: Placenta-specific zinc-finger RNA-binding protein that destabilizes cytoplasmic AU-rich element (ARE)-containing mRNA transcripts by promoting their poly(A) tail removal or deadenylation, and hence provide a mechanism for attenuating protein synthesis . Binds to the 3'-UTR ARE of placental target mRNAs, such as TNF, HBEGF and LIPG . Involved in placental expression of many genes important for normal placental physiology .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 72346
Sequence Length: 725
Domain: Contains long series of C-terminal alanine-rich repeats that serve to maintain the protein in the cytoplasm.
Subcellular Location: Cytoplasm
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Q8VD12 | MILGSLSRAGPLPLLRQPPIMQPPMDLKQILPFPLEPAPTLGLFSNYSTMDPVQKAVLSHTFGGPLLKTKRPVISCNVCQIRFNSQSQAEAHYKGNRHARRVKGIEAAKTRGREPSVRESGDPAPAGSIPPSGDGVAPRPVSMENGLGPAPGSPEKQPGSPSPPSVPESGQGVTKGEGGTSVPASLPGGSKEEEEKAKRLLYCALCKVAVNSLSQLEAHNKGTKHKTILEARSGLGPIKAYPRLGPPTPGEPEAPAQDRTFHCEICNVKVNSEVQLKQHISSRRHRDGVAGKPNPLLSRHKKPRGAAELAGTLTFSKELPKSLAGGLLPSPLAVAAVMAAAAGSPLSLRPAPAAPLLQGPPITHPLLHPAPGPIRTAHGPILFSPY | Function: RNA-binding protein that affects the localization and the translation of a subset of mRNA. May play a role in adipogenesis through binding to the 3'-UTR of CEBPA mRNA and regulation of its translation. Targets ITPR1 mRNA to dendrites in Purkinje cells, and may regulate its activity-dependent translation. With ELAVL1, binds the 3'-UTR of p53/TP53 mRNAs to control their nuclear export induced by CDKN2A. Hence, may regulate p53/TP53 expression and mediate in part the CDKN2A anti-proliferative activity. May also bind CCNB1 mRNA. Alternatively, may also regulate p53/TP53 activity through direct protein-protein interaction. Interacts with p53/TP53 and promotes cell-cycle arrest over apoptosis enhancing preferentially the DNA binding and transactivation of p53/TP53 on cell-cycle arrest target genes over proapoptotic target genes. May also regulate the ubiquitination and stability of CDKN1A promoting DNA damage-induced cell cycle arrest. Also plays a role in megakaryocytes differentiation.
PTM: Ubiquitinated upon prolonged exposure to genotoxic stress, which leads to proteasomal degradation of ZNF385A and releases p53/TP53 from cell-cycle arrest target gene promoters.
Sequence Mass (Da): 40447
Sequence Length: 386
Subcellular Location: Cytoplasm
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Q9Y2Y4 | MSLPPIRLPSPYGSDRLVQLAARLRPALCDTLITVGSQEFPAHSLVLAGVSQQLGRRGQWALGEGISPSTFAQLLNFVYGESVELQPGELRPLQEAARALGVQSLEEACWRARGDRAKKPDPGLKKHQEEPEKPSRNPERELGDPGEKQKPEQVSRTGGREQEMLHKHSPPRGRPEMAGATQEAQQEQTRSKEKRLQAPVGQRGADGKHGVLTWLRENPGGSEESLRKLPGPLPPAGSLQTSVTPRPSWAEAPWLVGGQPALWSILLMPPRYGIPFYHSTPTTGAWQEVWREQRIPLSLNAPKGLWSQNQLASSSPTPGSLPQGPAQLSPGEMEESDQGHTGALATCAGHEDKAGCPPRPHPPPAPPARSRPYACSVCGKRFSLKHQMETHYRVHTGEKPFSCSLCPQRSRDFSAMTKHLRTHGAAPYRCSLCGAGCPSLASMQAHMRGHSPSQLPPGWTIRSTFLYSSSRPSRPSTSPCCPSSSTT | Function: DNA-binding protein that binds to the to a 5'-TGTACAGTGT-3' core sequence. May function as a transcriptional transactivator and transcriptional repressor. Probably exerts its repressor effect by preventing GATA3 from binding to DNA. May play a role in regulating the differentiation and activation of helper T-cells (By similarity).
Sequence Mass (Da): 52963
Sequence Length: 487
Domain: The C-terminal zinc finger domain functions as a transcriptional transactivator.
Subcellular Location: Nucleus
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Q9JKD9 | MPQTPTRLVSPYGSDRLVQLAARLRPALCDTLITVGGLEFPAHSLVLAGASPRLGCRGRWALVEDISPSTFAQILTFVYGESIELQPGELGDLEEAAKALGVQALEEACQRAQKGKDEDELDPGLKRHQQSEDFMRGSERGLGSPGEKQKPEKDFRSNGREQEMSHKHKAPGERPEMAGATRMMSSEEVMRGIESHKGSEESLRGCPDPLSPPGSLLTSLIPRPWWAEVPRLGEGQSALWSILLWPSRYGAPFSHSTPITAAWQVRPQDQRIPLTLNHSKALWSQNQLASSSPTPGSFPQGTESLSPWQIETSGQGFTGTLATCVSQERTLNCPSHQHPPLPSPARSRPYSCSVCGKRFSLKHQMETHYRVHTGEKPFSCSLCPQRSRDFSAMTKHLRTHGAAPYRCPLCRAGCPSLASMQAHMRGHSPSRLPPGWTIRSTFLYSSSRPTRASSSPGSPTSSAAT | Function: DNA-binding protein that binds to the to a 5'-TGTACAGTGT-3' core sequence. May function as a transcriptional transactivator and transcriptional repressor (By similarity). Probably exerts its repressor effect by preventing GATA3 from binding to DNA. May play a role in regulating the differentiation and activation of helper T-cells.
Sequence Mass (Da): 50828
Sequence Length: 465
Domain: The C-terminal zinc finger domain functions as a transcriptional transactivator.
Subcellular Location: Nucleus
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Q9SAC0 | MAVYHLLLSSPPSLLLLPPSPRRPNLTLIRRIPAHPRLGNSTSLLSSSSPVIRKILVRSTLREDQPIASDSESSPTLLIGEDSAAFELGKQKLVSWVYFGVVLGVVLFILNVVWIDNSTGFGKSFIDAVSNISGSPEVAMLMLILIFAIVHSGLASLRDIGEKLIGERAFRVLFAGISLPLAMSTIVYFINHRYDGSQLWQLQGVPGVHEAIWVANFVSFFFLYPSTFNLLEVAAVDKPKMHLWETGIMRITRHPQMVGQIVWCLAHTLWIGNTVAASASLGLIAHHLFGAWNGDRRLAKRYGEDFESIKKRTSVIPFAAIFEGRQVLPEDYYKEFVRLPYLAITALTVGAYFAHPLMQGASFRLHW | Function: Isomerase involved in the biosynthesis of carotenoids. Catalyzes the cis- to trans-conversion of the 15-cis-bond in 9,15,9'-tri-cis-zeta-carotene.
Catalytic Activity: 9,9',15-tri-cis-zeta-carotene = 9,9'-di-cis-zeta-carotene
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 40851
Sequence Length: 367
Subcellular Location: Plastid
EC: 5.2.1.12
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B4FHU1 | MASQLRLHLAATPPLLPHRRPHLARPLCPTLNPIRAPLPPLSRVLSHARPARAVGGGIEPKEGVVAEGDESGGGPVLVGEDSAAFELKDQSVASWAYFAGILGAVLVALNVLWIDPSTGVGTKFLDAVASVSDSHEVVMLLLTIIFAVVHSGMASLRESGEKIVGERVYRVLFAGISLPLAVTTIVYFINHRYDGTQLWQVQGITGIHELLWFSSFISFFFLYPSTFNLLEVAAVDKPKLHMWETGIMRITRHPQMVGQVIWCLAHTLWIGNSVAVAASVGLISHHLFGAWNGDRRLLSRYGEAFEVLKKRTSVMPFAAIIDGRQKLPKDYHKEFFRLPYVAITMLTLGAYFAHPLMQASSYQLPW | Function: Isomerase involved in the biosynthesis of carotenoids. Catalyzes the cis- to trans-conversion of the 15-cis-bond in 9,15,9'-tri-cis-zeta-carotene.
Catalytic Activity: 9,9',15-tri-cis-zeta-carotene = 9,9'-di-cis-zeta-carotene
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 40319
Sequence Length: 366
Subcellular Location: Plastid
EC: 5.2.1.12
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Q9H0M4 | MMTTLQNKEECGKGPKRIFAPPAQKSYSLLPCSPNSPKEETPGISSPETEARISLPKASLKKKEEKATMKNVPSREQEKKRKAQINKQAEKKEKEKSSLTNAEFEEIVQIVLQKSLQECLGMGSGLDFAETSCAQPVVSTQSDKEPGITASATDTDNANGEEVPHTQEISVSWEGEAAPEIRTSKLGQPDPAPSKKKSNRLTLSKRKKEAHEKVEKTQGGHEHRQEDRLKKTVQDHSQIRDQQKGEISGFGQCLVWVQCSFPNCGKWRRLCGNIDPSVLPDNWSCDQNTDVQYNRCDIPEETWTGLESDVAYASYIPGSIIWAKQYGYPWWPGMIESDPDLGEYFLFTSHLDSLPSKYHVTFFGETVSRAWIPVNMLKNFQELSLELSVMKKRRNDCSQKLGVALMMAQEAEQISIQERVNLFGFWSRFNGSNSNGERKDLQLSGLNSPGSCLEKKEKEEELEKEEGEKTDPILPIRKRVKIQTQKTKPRGLGGDAGTADGRGRTLQRKIMKRSLGRKSTAPPAPRMGRKEGQGNSDSDQPGPKKKFKAPQSKALAASFSEGKEVRTVPKNLGLSACKGACPSSAKEEPRHREPLTQEAGSVPLEDEASSDLDLEQLMEDVGRELGQSGELQHSNSDGEDFPVALFGK | Function: Dual histone methylation reader specific for PRDM9-catalyzed histone marks (H3K4me3 and H3K36me3) . Facilitates the repair of PRDM9-induced meiotic double-strand breaks (DSBs) (By similarity). Essential for male fertility and spermatogenesis (By similarity). Required for meiosis prophase I progression in male but not in female germ cells (By similarity).
Sequence Mass (Da): 72007
Sequence Length: 648
Domain: The CW-TYPE zinc finger mediates its binding to trimethylated histone H3K4me3.
Subcellular Location: Nucleus
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Q6IR42 | MMAALQTHKEYEKGTKKTFAPPTQKLHSEKPQPSSWKEDAPGTSSPEAETKPSLLKASLKKEQKPTTEHGPNRGQERKLKAQDQPAKKKGKERTLTSAEFEEIFQIVLQKSLQECLETSSCVQHIRPTKLDEEPGIVPPATDKKDADPEKVITPDTPKIASSLEEEVNSEMGTSKLGQPVTEPSKKKFNRLSLSKQKKKAEDEKMEKIQDGRECSLKEKQKIVIQDQSQIRGPQKEEESGFGHCVIWVQCSSPKCEKWRQLRGNIDPSVLPDDWSCDQNPDPNYNRCDIPEESWAGCESDVAYASYVPGSIIWAKQYGYPWWPGMIEADPDLGEYFLFASHLDSLPSKYHVTFFGETVSRAWIPVRMLKNFQELSLELVKKCKNKNSNQKLEAAIAMAHRAEQTSIQERVNLFGFWSRYNGADISEEGEDLTLCESNNPESCLEKEEKDLEEEKEEEEEKKDPTLPRPKPAKMQTKKPKSRGPAGGPDGTPKKKTAKKSLVSESTVPPVPTLGGKEEQGNSDLDHPVPKKKFKAPENKTSATNLSEEKEIKIVSKCPTPSAQHGACPLGKEGLVPHMPPTQEAASFPPDDDCSSDLDLEQLMEDIGEPEERGEMQQRGSSEEFLAALFEE | Function: Dual histone methylation reader specific for PRDM9-catalyzed histone marks (H3K4me3 and H3K36me3) that facilitates the repair of PRDM9-induced meiotic double-strand breaks (DSBs) . Essential for male fertility and spermatogenesis . Required for meiosis prophase I progression in male but not in female germ cells .
Sequence Mass (Da): 70569
Sequence Length: 630
Domain: The CW-TYPE zinc finger mediates its binding to trimethylated histone H3K4me3.
Subcellular Location: Nucleus
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E7F021 | MFKNVFGSGFLVRTAHVILTWVITLILFLHDTDLRRQEETGELTLPVLFVLLVLVSVLLYFAVSLMDPGFVLTDDCDLQFTLGIAEETQDMIPQTTKSIRLRRCGHCLVQQPMRSKHCQTCQHCVRRYDHHCPWIENCVGERNHRWFVLYLAVQFVVLLWGLYMAWSGFSHASTWQQWLRTNGVLLGAAAVVAILALTVLLLLGSHLYLVSLNTTTWEFMSRHRISYLKHCGADENPFDKGILRNLWGFFCAWEPVVWEHVYFKQGNDPI | Function: Palmitoyltransferase that catalyzes the addition of palmitate onto various protein substrates (By similarity). Has a palmitoyltransferase activity toward gephyrin/GPHN, regulating its clustering at synapses and its function in gamma-aminobutyric acid receptor clustering (By similarity). Acts as an inhibitor of the NLRP3 inflammasome by mediating palmitoylation of NLRP3, thereby promoting NLRP3 degradation by the chaperone-mediated autophagy (CMA) process (By similarity).
Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 31240
Sequence Length: 270
Domain: The DHHC domain is required for palmitoyltransferase activity.
Subcellular Location: Golgi apparatus membrane
EC: 2.3.1.225
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B8A4F0 | MHPCSSVLHLLLRCMRGCCRHTRSRVPRRLRRHVSYIRLIFKSLYFNSLTNSDVVTDSILEPVFWMVEVVTRWFGMVFVFLVVALTSSVVFIAYFCLLPLVLHTYSPGWMIWHICYGHWNLVMIVFHYYKATKTPPGYPPKMKTDVPFVSVCKKCIIPKPARSHHCGICKTCILKMDHHCPWLNNCVGHFNHRYFFSFCLFLTLGCMYCSVSGRHLFIDAYNTIDQLKHLEAEKQGVPVTGIGLLIGIVPSAGVAGKAVQVAQEVSQPPYTYKDRMFHKSVIYMWVLTSTVSVALGALTLWHALLITRGETSIERHINGKEAKRLAKRGRVYRNPFSYGKLNNWKVFFGVEKRSHWLTRVLLPSGHAPYGDGLTWDIYPLKKDMMPV | Function: Palmitoyl acyltransferase that mediates palmitoylation of proteins and is required during embryonic heart development. Involved in the proliferation of neural stem cells by regulating the FGF/ERK pathway (By similarity). Involved in the proliferation of neural stem cells by regulating the FGF/ERK pathway .
Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 44531
Sequence Length: 387
Domain: The DHHC domain is required for palmitoyltransferase activity.
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.3.1.225
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Q7ZVN4 | MKNREYQQIDPQALATPTPTPPPRSLPEHKPRRARRKWEVFPGKNRFYCDGRIIVARQSGVLPLTLGLILLTSGLFFIFDCPFLVKHLTSCIPAIGGVLFVFVIISLLQTSFTDPGILPRATPEEAADIEKQIDNPTGSSSSYRPPPRTKEVVINQQVVKLKYCFTCKIFRPPRTSHCSLCDNCVERFDHHCPWVGNCVGKRNYRFFYTFIVSLSFLTAFIFGCVTTHLALRSQGGNGLVNALQSSPASALELVVCFFSVWSILGLSGFHTYLVAANLTTNEDIKGSWSGKSGNEDVGNPYSYNSMIKNCCSVLCGPMPPSLIDRRGFVPSDDSVQTSPVEIELPAAKNDINMVGRAVTSGRPPPPPPPPLVVTLQQPAISMQNHSTA | Function: Palmitoyltransferase that catalyzes the addition of palmitate onto various protein substrates, such as CGAS, HRAS and LCK.
Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 42712
Sequence Length: 388
Domain: The DHHC domain is required for palmitoyltransferase activity.
Subcellular Location: Golgi apparatus membrane
EC: 2.3.1.225
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F1Q7H8 | MAPSHAVRCCQRGLSWIPVIFINLVVCWSYYAYVVELCIYTIPNVNEQVIYLVVFHAFFFMFMWSYWKTISSKPTNPSKEFCLPKAEKELYEKEERPEAQQDILKRVARELPIYTFTGSGAIRYCDRCQLIKPDRCHHCSTCDKCVLKMDHHCPWVNNCVGFSNYKFFVLFLAYSMLYCVYIAATVLQYFIKFWTNQLPDTHAKFHVLFLFFVAAMFFISILSLFSYHLWLVGKNRTTIEAFRAPVFRNGPDKNGFTLGFRKNITQVFGDQKKYWCLPIFSSLGDGYTFPTRLVTVDVEHGNIEHQTIKCTVDGQTNARPLSESQNHLLCNDEGQKDSSMAAIEVCQPVCVTLENES | Function: Palmitoyltransferase that could catalyze the addition of palmitate onto various protein substrates. Catalyzes palmitoylation of Cys residues on protein substrates and has a preference for acyl-CoA with C16 fatty acid chains but may also utilize acyl-CoA with C14 and C18 fatty acid chains.
Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 41414
Sequence Length: 357
Domain: The DHHC domain is required for palmitoyltransferase activity.
Subcellular Location: Golgi apparatus membrane
EC: 2.3.1.225
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Q8LGB6 | MSKNNKKKRRWDLKNGGILLEELIASFDGKTNPIRCFSSDQILKATDNFSESRIISSWGYFIWYKGVIEERQVSIKKWSSQNLSSFTEAYRDISVSSQMSGHKNALKLIGCCLEFDLPALVCEYTEHGPLNRDGGLSSGVVLPWKVRLKIAKEIASSVTYLHTAFPETIVHRNINPTNIFIDENWTAKLSDFWFCVAIPEGELYVEDDVKGVIGFVDPDYYWTMKVTEKVDIYSFGVVMLVLLSGRAAVFNGPDEAPMSLNDHVSEVMEKGEFDEIVDKEIWNDLGGDDDLVLRRSQVKAFLRLALRCVRYKKEDPVSGMLEVAKELKLIEKLS | Function: Together with RPP13L4/ZAR1, involved in the ambient temperature (above 22 degrees Celsius)-sensitive aerial organ development . Together with RPP13L4/ZAR1, involved in the regulation of the ambient temperature-sensitive intersection of growth and immune response in the absence of pathogens, by repressing the transcription of SNC1 . Probable non-functional kinase required for recognition of the Pseudomonas syringae type III effector HopZ1a by RPP13L4/ZAR1 and, together with SZE1 and SZE2, to trigger subsequent defense responses . May function as a decoy to trap HopZ1a in the ZAR1 complex for recognition by the plant immune system .
Sequence Mass (Da): 37957
Sequence Length: 334
Domain: The protein kinase domain is predicted to be catalytically inactive.
Subcellular Location: Cytoplasm
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C0P381 | MKLVLVVLAFIALVSSVSCTQTGGCSCGQQQSHEQQHHPQQHHPQKQQHQPPPQHHQQQQHQQQQVHMQPQKHQQQQEVHVQQQQQQPQHQQQQQQQQHQQQHQCEGQQQHHQQSQGHVQQHEQSHEQHQGQSHEQQHQQQFQGHDKQQQPQQPQQYQQGQEKSQQQQCHCQEQQQTTRCSYNYYSSSSNLKNCHEFLRQQCSPLVMPFLQSRLIQPSSCQVLQQQCCHDLRQIEPQYIHQAIYNMVQSIIQEEQQQQPCELCGSQQATQSAVAILTAAQYLPSMCGLYHSYYQNNPCSSNDISGVCN | Function: Zeins are major seed storage proteins.
Location Topology: Lipid-anchor
Sequence Mass (Da): 36005
Sequence Length: 308
Subcellular Location: Cell membrane
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Q08245 | MSEIQNKAETAAQDVQQKLEETKESLQNKGQEVKEQAEASIDNLKNEATPEAEQVKKEEQNIADGVEQKKTEAANKVEETKKQASAAVSEKKETKKEGGFLKKLNRKIASIFN | Function: Acts antagonistically to MID2 in signaling cell wall stress to the PKC1-MPK1 cell integrity pathway.
PTM: Phosphorylation of Ser-25 is induced 2-fold in response to mating pheromone.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 12589
Sequence Length: 113
Subcellular Location: Cell membrane
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Q94BZ1 | MAEEYAECLLEKNFHEDCSGCKVDQMKRLRRGFPFWELFTVWIIVLCTALPISSLFPFLYFMIDDFNIAKKEEDIGFYAGFVGCSFMLGRAFTSVAWGLVADRYGRKPVILIGTASVVVFNTLFGLSLNFWMAIITRFCLGSFNGLLGPIKAYAMEIFRDEYQGLALSAVSTAWGIGLIIGPAIGGFLAQPAKQYPSLFSQDSIFGKFPFFLPCLAISVFAFLVTIVSSRIPETLHNHKFNDDESYDALKDLSDDPESNKVAERNGKSSLLNNWPLISSIIVYCVFSLHDMAYTEIFSLWANSPRKYGGLGYSTADVGSVLAFSGFGLLIFQLSLYSYAERLLGPIIVTRISGSLAMVVLSCYPLIAKLSGLALTVTVTSASVAKSVLGTSAITGLFILQNKAVRQDQRGAANGIAMTAMSLFKAIGPAAAGIIFSWSEKRQGAAFLPGTQMVFFILNVVLALGVVLTFKPFLAETQQ | Function: Major facilitator superfamily (MFS) transporter probably involved in 2,4-dichlorophenoxyacetic acid (2,4-D) export . K(+) may be the physiological substrate of the transporter .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 52299
Sequence Length: 478
Subcellular Location: Cell membrane
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G5EGI7 | MKNLLLITFFVVSTVTALGGRGSKSALVLVAARSSENHPLHATDPITIWCAPDNPQVVIKTAHFIRSSDNEKLEAALNPTKKNATYTFGSPSVKDAGEYKCELDTPHGKISHKVFIYSRPVVHSHEHFTEHEGHEFHLESTGTTVEKGESVTLTCPVTGYPKPVVKWTKDSAPLALSQSVSMEGSTVIVTNANYTDAGTYSCEAVNEYTVNGKTSKMLLVVDKMVDVRSEFQWVYPLAVILITIFLLVVIIVFCEWRNKKSTSKA | Function: Probably not involved in maintaining the position of ASI and ASH head neuron cell bodies and ventral nerve cord axons of PVQ, PVP, RMEV, AVK and HSN neurons.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 29170
Sequence Length: 265
Subcellular Location: Cell membrane
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B3LPE4 | MIPRTRTLLQSKIPITRYFARCWAPRVRYNVCRTLPAAALHTNIIAHNEVKKDDKKVHLGSFKVDKPKMMIAFTCKKCNTRSSHTMSKQAYEKGTVLISCPHCKVRHLIADHLKIFHDHHVTVEQLMKANGEQVSQDVGDLEFEDIPDSLKDVLGKYAKNNSENASQLPHPSQK | Cofactor: Binds 1 zinc ion per subunit.
Function: Involved in protein import into mitochondria. Acts as a Hsp70-specific chaperone that prevents self-aggregation of the matrix Hsp70 chaperones SSC1 (mtHSP70) and SSQ1, thereby maintaining their function in mitochondrial protein import and Fe/S protein biosynthesis. May act together with PAM18 as co-chaperone to facilitate recognition and folding of imported proteins by SSC1 in the mitochondrial matrix (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 19855
Sequence Length: 174
Subcellular Location: Mitochondrion inner membrane
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Q8NF64 | MNSMNPMKPALPPAPHGDGSFAYESVPWQQSATQPAGSLSVVTTVWGVGNATQSQVLGNPMGPAGSPSGSSMMPGVAGGSSALTSPQCLGQQAFAEGGANKGYVQQGVYSRGGYPGAPGFTTGYAGGPGGLGLPSHAARPSTDFTQAAAAAAVAAAAATATATATATVAALQEKQSQELSQYGAMGAGQSFNSQFLQHGGPRGPSVPAGMNPTGIGGVMGPSGLSPLAMNPTRAAGMTPLYAGQRLPQHGYPGPPQAQPLPRQGVKRTYSEVYPGQQYLQGGQYAPSTAQFAPSPGQPPAPSPSYPGHRLPLQQGMTQSLSVPGPTGLHYKPTEQFNGQGASFNGGSVSYSQPGLSGPTRSIPGYPSSPLPGNPTPPMTPSSSVPYMSPNQEVKSPFLPDLKPNLNSLHSSPSGSGPCDELRLTFPVRDGVVLEPFRLQHNLAVSNHVFQLRDSVYKTLIMRPDLELQFKCYHHEDRQMNTNWPASVQVSVNATPLTIERGDNKTSHKPLYLKHVCQPGRNTIQITVTACCCSHLFVLQLVHRPSVRSVLQGLLKKRLLPAEHCITKIKRNFSSGTIPGTPGPNGEDGVEQTAIKVSLKCPITFRRIQLPARGHDCRHIQCFDLESYLQLNCERGTWRCPVCNKTALLEGLEVDQYMLGILIYIQNSDYEEITIDPTCSWKPVPVKPDMHIKEEPDGPALKRCRTVSPAHVLMPSVMEMIAALGPGAAPFAPLQPPSVPAPSDYPGQGSSFLGPGTFPESFPPTTPSTPTLAEFTPGPPPISYQSDIPSSLLTSEKSTACLPSQMAPAGHLDPTHNPGTPGLHTSNLGAPPGPQLHHSNPPPASRQSLGQASLGPTGELAFSPATGVMGPPSMSGAGEAPEPALDLLPELTNPDELLSYLGPPDLPTNNNDDLLSLFENN | Function: Increases ligand-dependent transcriptional activity of AR and other nuclear hormone receptors.
Sequence Mass (Da): 96537
Sequence Length: 920
Domain: The C-terminal proline-rich domain possesses a significant intrinsic transcriptional activity. This activity is inhibited by the N-terminus in the full-length protein.
Subcellular Location: Nucleus
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Q86UQ0 | MWAPREQLLGWTAEALPAKDSAWPWEEKPRYLGPVTFEDVAVLFTEAEWKRLSLEQRNLYKEVMLENLRNLVSLAESKPEVHTCPSCPLAFGSQQFLSQDELHNHPIPGFHAGNQLHPGNPCPEDQPQSQHPSDKNHRGAEAEDQRVEGGVRPLFWSTNERGALVGFSSLFQRPPISSWGGNRILEIQLSPAQNASSEEVDRISKRAETPGFGAVTFGECALAFNQKSNLFRQKAVTAEKSSDKRQSQVCRECGRGFSRKSQLIIHQRTHTGEKPYVCGECGRGFIVESVLRNHLSTHSGEKPYVCSHCGRGFSCKPYLIRHQRTHTREKSFMCTVCGRGFREKSELIKHQRIHTGDKPYVCRD | Function: May play a role in hematopoietic stem/progenitor cell differentiation. May play a role as a DNA binding-dependent transcriptional repressor.
Sequence Mass (Da): 41189
Sequence Length: 364
Domain: The KRAB domain mediates interaction with TRIM28.
Subcellular Location: Nucleus
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Q5IRJ6 | MFPGLAAAAAAHRCSWAALCRLGGGRAATRGRSQGWKNVMTFESFTYVVPDIHPHLSIINQVKLYSTNVQKGGQGSQTPKADKVPSLTQTVENIGAELKAPLKQDPLQVRVKAVLKKRDYGSKYTKNNFITGVRAINEFCLKSSDLEQLRKIRRRSPHDDTESFTVFLRSDVEAKALEVWGSLEALAREKKLRKEAEIEYRERLFRNQRILREYGDFLGNTKPRSRAVSVFLKGPGKVVMVAICINGLNCFFKFLAWIYTGSASMFSEAIHSLSDTCNQGLLALGISKSVQTPDPSHPYGFSNMRYISSLISGVGIFMMGAGLSWYHGIMGLLHPQPMESLLWAYCILAGSLVSEGATLLVAINELRRSAQAKGTTFYKYVMESRDPSTNVILLEDTAAVLGVIIAATCMGLTSITGNPLYDSLGSLGVGTLLGVVSAFLIYTNTEALLGRSIQPEQVQRLTELLESDPSVRAIHDVKATDLGLGKVRFKAEVDFDGRVVTRSYLEKQDFDQMMQEIQEVKTPEQLEAFMLKHGENIIDTLGAEVDRLEKELKKRNPEVRHVDLEIL | Function: Acts as a zinc transporter involved in intracellular zinc homeostasis (By similarity). Functions as a secondary coactivator for nuclear receptors by cooperating with p160 coactivators subtypes . Plays a role in transcriptional activation of Wnt-responsive genes .
Catalytic Activity: 2 H(+)(out) + Zn(2+)(in) = 2 H(+)(in) + Zn(2+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 62875
Sequence Length: 567
Subcellular Location: Mitochondrion membrane
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Q55FL1 | MSIFAYSILAGLAPLLSSSIPFFTLRNRNINASVFHILLCISAGLLFAVASLELIPESMNLALRSFEESTKTQTSLKSTTTKTTTTTTTIGNIKLQKSFISNSEDSLNEFHSLDNEINKPPIEGLNLNNLNQATNLDNNEEDNDNLDNDGENEIENDHDHDHQEDEGGDNDHDHESEEKKEFLKIPMYGIGFGFAILIIVESIFSSIDGGGGGGGHHSHSHGSLSSSSSNDVISDYISNNNSNNINNNDDDNNNNNNNNDDDDDSVELLERNVVNKDNSNNINNINNNNDDEDIIVINKSIENTPNIASPVMNKDNNNNDKDKNRNSNKSDIKNSGSINNGNNSGNNNNNNKSKLTITTFIALSIHSFVDGVVISSAFSSSPHVGARVALAIVIHKIPDGLVLSSLILSQKKFNSGIFSNPFFYFLLISCMTPLGSFISSFLFGGLSLSSGAFVLGFGAGTFIYITSTAILPEILSNQIVKKSTSLFSIFLGYLLFIFLDSQFHGAH | Function: May transport divalent cations (By similarity). May participate, with dstA, in the regulation of the differentiation of stalk cells during development.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 55173
Sequence Length: 507
Subcellular Location: Membrane
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P37617 | MSTPDNHGKKAPQFAAFKPLTTVQNANDCCCDGACSSTPTLSENVSGTRYSWKVSGMDCAACARKVENAVRQLAGVNQVQVLFATEKLVVDADNDIRAQVESALQKAGYSLRDEQAAEEPQASRLKENLPLITLIVMMAISWGLEQFNHPFGQLAFIATTLVGLYPIARQALRLIKSGSYFAIETLMSVAAIGALFIGATAEAAMVLLLFLIGERLEGWAASRARQGVSALMALKPETATRLRKGEREEVAINSLRPGDVIEVAAGGRLPADGKLLSPFASFDESALTGESIPVERATGDKVPAGATSVDRLVTLEVLSEPGASAIDRILKLIEEAEERRAPIERFIDRFSRIYTPAIMAVALLVTLVPPLLFAASWQEWIYKGLTLLLIGCPCALVISTPAAITSGLAAAARRGALIKGGAALEQLGRVTQVAFDKTGTLTVGKPRVTAIHPATGISESELLTLAAAVEQGATHPLAQAIVREAQVAELAIPTAESQRALVGSGIEAQVNGERVLICAAGKHPADAFTGLINELESAGQTVVLVVRNDDVLGVIALQDTLRADAATAISELNALGVKGVILTGDNPRAAAAIAGELGLEFKAGLLPEDKVKAVTELNQHAPLAMVGDGINDAPAMKAAAIGIAMGSGTDVALETADAALTHNHLRGLVQMIELARATHANIRQNITIALGLKGIFLVTTLLGMTGLWLAVLADTGATVLVTANALRLLRRR | Function: Confers resistance to zinc, cadmium and lead . Couples the hydrolysis of ATP with the export of zinc, cadmium or lead, with highest activity when the metals are present as metal-thiolate complexes . Can also bind nickel, copper, cobalt and mercury .
Catalytic Activity: ATP + H2O + Pb(2+)(in) = ADP + H(+) + Pb(2+)(out) + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 76840
Sequence Length: 732
Domain: Has two high-affinity metal-binding sites, one in the N-terminal region and another in the transmembrane region. Both sites are able to access and bind metal ion independently of each other. The N-terminal metal-binding site is not strictly necessary for activity and metal selectivity, but is needed for maximal activity and may be involved in regulation. The metal-binding site in the transmembrane region is essential for activity of the pump.
Subcellular Location: Cell inner membrane
EC: 7.2.2.-
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Q54LY6 | MTSLETYNDNVKTALIMCFLSGLSTAIGGLYVIFIKQQSHKLLGHLLSFSSGVMIYISFMDLLPESIAEIGFYNANIWFFVGIIFFAVILRFVPHDHDESGDSNHAHSHNGASIEKHSSEKKEVVDDDDDDNNGKDKKQKQQKQKQQKQQQQQKQNIAKSKNKKKSKDDYLNSVGIATAIGVSLHNFPEGVAVYLACLKGIDVGLPLMLAIAAHNIPEGMAVAAPIFSATGSKWKAFKYCLYSGLCEPVGAIIFGLIFKEYMTPYLIQSMLAAVAGIMVFMVIKELLPAAFKYVSVDESAFSNIIGMIFFFFSIHFLHSMLPHDHGGAGDGGHGHSHGGHGHSHGHGHSHGGHSHDSQHVESPQSSSFNAFA | Function: May transport divalent cations (By similarity). May participate, with dstA, in the regulation of the differentiation of stalk cells during development.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 40690
Sequence Length: 372
Subcellular Location: Membrane
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Q4FQ27 | MNNTSKLLNLSNVSYYIGQQRLLSHINIDIAVNETISVIGPNGAGKSTLVKLILGLIEPTSGQVTPSAPLQIGYVPQRFSVPPILPLRVSDLLAQAHKKRLMAEQRQFIFDKLSLTHLLSRQMLHLSGGETQRVLLARALLDKPNLLILDEPMQGLDPETEVWLYQFIDELPEFLRCAMLVVSHDLHWVMKGSRRVICLNKHICCEGQPSELAISSEFQKLFGHHYEQPYVHQPHACEHHAPS | Function: Part of the ABC transporter complex ZnuABC involved in zinc import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP(in) + H2O(in) + Zn(2+)(out) = ADP(in) + H(+)(in) + phosphate(in) + Zn(2+)(in)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 27387
Sequence Length: 243
Subcellular Location: Cell inner membrane
EC: 7.2.2.20
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Q1Q889 | MNNTSKLLNLSNVSYYIGQQRLLSNINIDIAVNETVSVIGPNGAGKSTLVKLILGLIVPTSGQVTPSEPLQIGYVPQRFSVPPILPLRVSDLLAQACKKRLTAEQRQFIFDKLSLTHLLSRQMLHLSGGETQRVLLARALLDKPNLLILDEPMQGLDPETEVWLYQFIDELPEFLRCAMLVVSHDLHWVMKGSRRVICLNKHICCEGQPSELAISSEFQKLFGHHYEQPYVHQPHACEHHAPS | Function: Part of the ABC transporter complex ZnuABC involved in zinc import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP(in) + H2O(in) + Zn(2+)(out) = ADP(in) + H(+)(in) + phosphate(in) + Zn(2+)(in)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 27314
Sequence Length: 243
Subcellular Location: Cell inner membrane
EC: 7.2.2.20
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Q92P76 | MLNFRSPETMPLVSLANAGVRRNGRWLVRGVDFSISRGEIVTLIGPNGSGKSTTAKTAIGVLKPDEGHVERLAGLKVGYVPQKLAVDWTLPLTVERLMTLTGPLKGREIEESLAATGMLHMAKAEVQHLSGGEFQRALLARAIARKPDLLVLDEPVQGVDFSGEIALYELIKQIRNRTGCGILLISHDLHIVMAETDTVVCLNGHVCCRGTPQVVSQSPEYLKLFGRRAAGALAVYSHHHDHTHLPDGRVLHADGSITESCFPGDGHHHHEEADNIHDHDPDCGCGHHARLQGYDGTEKRDA | Function: Part of the ABC transporter complex ZnuABC involved in zinc import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP(in) + H2O(in) + Zn(2+)(out) = ADP(in) + H(+)(in) + phosphate(in) + Zn(2+)(in)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 32851
Sequence Length: 302
Subcellular Location: Cell inner membrane
EC: 7.2.2.20
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Q9ZCC4 | MQKPIIEFRNVSKKFGNKTPISKVSFIVKKNNITTLIGPNGAGKTTIVRLMLGLEKPTSGEVIIDRKLKIGYVPQKFGLTTDIPITVKKFLDLLAPSHFNKNIKEISSFIDLEHIKKQEISKLSGGQFQKVVLACSIINNPDLIILDEPLQSLDVTSQQEFYQLIHFIRKKLNITVFMISHDLFTVIKNSDQVICLNGHICCSGVPHEITPNSEFSNALSSLGFYTHNHDHKH | Function: Part of the ABC transporter complex ZnuABC involved in zinc import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP(in) + H2O(in) + Zn(2+)(out) = ADP(in) + H(+)(in) + phosphate(in) + Zn(2+)(in)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 26205
Sequence Length: 233
Subcellular Location: Cell inner membrane
EC: 7.2.2.20
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Q5LUR8 | MNTPVIAAEGLSIRVDGRTVLADISVAVAAGEIVTIVGPNGSGKSTFLRALIGALPAASGRVIRAPGLRIGYVPQKLAIDATLPITVSRFLSLPRRVPQDVAAEALARAGVPDLANRQMTDLSGGQFQRVLLARAVLERPHLLLLDEATQGLDQPGSAAFYEQIEEVRQDLGCAVVMVSHDLHVVMAASDRVLCMNGHICCEGTPEVVADAPEYRALFGTGTRGALALYRHQHSHRHDDDCGHDHGAEHMHPHGDR | Function: Part of the ABC transporter complex ZnuABC involved in zinc import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP(in) + H2O(in) + Zn(2+)(out) = ADP(in) + H(+)(in) + phosphate(in) + Zn(2+)(in)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 27296
Sequence Length: 256
Subcellular Location: Cell inner membrane
EC: 7.2.2.20
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Q8ZNV7 | MTSLVSLENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKHNGQLRIGYVPQKLYLDTTLPLTVNRFLRLRPGTQKTDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNHHICCSGAPEVVSMHPEFISMFGPRGAEQLGIYRHHHNHRHDLQGRIVLRRGNGHS | Function: Part of the ABC transporter complex ZnuABC involved in zinc import. Responsible for energy coupling to the transport system (Probable). Seems to be important for the virulence.
Catalytic Activity: ATP(in) + H2O(in) + Zn(2+)(out) = ADP(in) + H(+)(in) + phosphate(in) + Zn(2+)(in)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 27666
Sequence Length: 251
Subcellular Location: Cell inner membrane
EC: 7.2.2.20
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P14375 | MTHDNIDILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPVLIMTAYSSVETAVEALKTGALDYLIKPLDFDNLQATLEKALAHTHSIDAETPAVTASQFGMVGKSPAMQHLLSEIALVAPSEATVLIHGDSGTGKELVARAIHASSARSEKPLVTLNCAALNESLLESELFGHEKGAFTGADKRREGRFVEADGGTLFLDEIGDISPMMQVRLLRAIQEREVQRVGSNQIISVDVRLIAATHRDLAAEVNAGRFRQDLYYRLNVVAIEVPSLRQRREDIPLLAGHFLQRFAERNRKAVKGFTPQAMDLLIHYDWPGNIRELENAVERAVVLLTGEYISERELPLAIASTPIPLGQSQDIQPLVEVEKEVILAALEKTGGNKTEAARQLGITRKTLLAKLSR | Function: Member of the two-component regulatory system ZraS/ZraR. When activated by ZraS it acts in conjunction with sigma-54 to regulate the expression of zraP. Positively autoregulates the expression of the zraSR operon.
PTM: Phosphorylated by ZraS.
Sequence Mass (Da): 48395
Sequence Length: 441
Subcellular Location: Cytoplasm
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P14377 | MRFMQRSKDSLAKWLSAILPVVIVGLVGLFAVTVIRDYGRASEADRQALLEKGNVLIRALESGSRVGMGMRMHHVQQQALLEEMAGQPGVLWFAVTDAQGIIILHSDPDKVGRALYSPDEMQKLKPEENSRWRLLGKTETTPALEVYRLFQPMSAPWRHGMHNMPRCNGKAVPQVDAQQAIFIAVDASDLVATQSGEKRNTLIILFALATVLLASVLSFFWYRRYLRSRQLLQDEMKRKEKLVALGHLAAGVAHEIRNPLSSIKGLAKYFAERAPAGGEAHQLAQVMAKEADRLNRVVSELLELVKPTHLALQAVDLNTLINHSLQLVSQDANSREIQLRFTANDTLPEIQADPDRLTQVLLNLYLNAIQAIGQHGVISVTASESGAGVKISVTDSGKGIAADQLDAIFTPYFTTKAEGTGLGLAVVHNIVEQHGGTIQVASQEGKGSTFTLWLPVNITRKDPQG | Function: Member of the two-component regulatory system ZraS/ZraR. May function as a membrane-associated protein kinase that phosphorylates ZraR in response to high concentrations of zinc or lead in the medium.
PTM: Autophosphorylated.
Location Topology: Multi-pass membrane protein
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
Sequence Mass (Da): 51032
Sequence Length: 465
Subcellular Location: Cell inner membrane
EC: 2.7.13.3
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Q8NEG5 | MLRRGYKASERRRHLSERLSWHQDQALSSSIYLLREMGPTGFLLREEEPEYMDFRVFLGNPHVCNCSTFPKGGELCKHICWVLLKKFKLPRNHESALQLGLGEREISDLLRGIHRVQTPQPGTNDENEHVEEDGYIKQKEIDSEDICSICQELLLEKKLPVTFCRFGCGNSIHIKCMKILANYQSTSNTSMLKCPLCRKEFAPLKLILEEFKNSSKLVAAAEKERLDKHLGIPCNNCKQFPIEGKCYKCTECIEYHLCQECFDSCCHLSHTFTFREKRNQKWRSLEKRADEVVKYIDTKNEIEEKMSHFQEKQGQVYTPKHIVRSLPLQLITKNSKLLAPGYQCLLCLKAFHLGQHTRLLPCTHKFHRKCIDNWLFHKCNSCPIDGQVIYNPLTWKNSAVNGQAHQSVSNRDIIHLSKQKEPDLFIPGTGLVLKQNRLGILPSIPQCNFDELNTPQSPKDAYENTTIDNLCSIKLDNSNSKKLTYDYKISQHFPRYLQDLPTVSFGKIPSQTLLPPIVHKNIVCPTAMESPCISGKFHTSLSRMTKGCKCNNHNLKKTPATKIREDNKRSTLLPEDFNLIVNWSTAKLSLSKRYSNCMGEITRKCSHLSRQPVSHSVNTKSTELSLIIEGVQL | Function: E3 ubiquitin-protein ligase involved in the regulation of Fas-, DR3- and DR4-mediated apoptosis. Functions in conjunction with the UBE2D1, UBE2D3 and UBE2E1 E2 ubiquitin-conjugating enzymes.
PTM: Polyubiquitinated. Polyubiquitination is followed by degradation via the proteasome (By similarity).
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 72732
Sequence Length: 633
Domain: The SWIM-type zinc finger is required for ubiquitination activity.
EC: 2.3.2.27
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Q9D9X6 | MLRGGCKASEKRRHLSESLSWQQDQALSSSIYLLRQIGPTGFLLKEEEPEKGDFRVLLGNPHECSCPTFLKRGELCKHICWVLLKKFKLPRNHESAFQLGLTEGEINDLLRGIHQVQAPQLRASDETAQVEEDGYLKQKDINAGDICPICQEVLLEKKLPVTFCRFGCGNNVHIKCMRILANYQDTGSDSSVLRCPLCREEFAPLKVILEEFKNSNKLITISEKERLDKHLGIPCNNCNQLPIEGRCYKCTECVEYHLCQECFDSCCHSSHAFASREKRNQRWRSVEKRSEVMKYLNTENEGEAKPGCFQEKQGQFYTPKHVVKSLPLLMITKKSKLLAPGYQCRLCLKSFSFGQYTRLLPCTHKFHRKCIDNWLLHKCNSCPIDRQVIYNPLIWKGIATDGQAHQLASSKDIACLSKQQEPKLFIPGTGLVLKGKRMGVLPSIPQYNSKVLTTLQNPSDNYQNITMDDLCSVKLDNSNSRKLVFGYKISKQFPTYLKNPTTGQTPSQTFLPSLPHKNIICLTGRESPHIYEKDHIGQSQKTSRGYEHINYNTRKSLGSRLRQHKRSSALSSEDLNLTINLGTTKLSLSKRQNNSMGKVRQKLGHPPRRPAYPPLQTQNAALSLIMQGIQL | Function: E3 ubiquitin-protein ligase involved in the regulation of Fas-, DR3- and DR4-mediated apoptosis. Functions in conjunction with the UBE2D1, UBE2D3 and UBE2E1 E2 ubiquitin-conjugating enzymes.
PTM: Polyubiquitinated. Polyubiquitination is followed by degradation via the proteasome.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 71793
Sequence Length: 631
Domain: The SWIM-type zinc finger is required for ubiquitination activity.
EC: 2.3.2.27
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