ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
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-h... |
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 | MVRKYGIFIDAGSSGSRLLIYSWDYDTDSSLSDKVKKLPLIETGIGDGGKWSLKVQPGISSFANNPKHVGKKHLKELLDFAAHAIPKDVHKETPVFLSATAGMRLLGVDAQNKILSHACRYIKKNYDFDIPNCSNSIRVIDGKAEGMYGWLATNYLLKTLEEKDTSTVGFLDMGGASVQIAFELPPSQLKNYKDSISTVHIGLQNGQQLEYPLFVTTWLGFGANEAYRRYLGLLIESENGKVGNTLSDPCSLRGRTYDIDGIEFAGTGDLKQCLKLTYNLLNKDKPCSMDPCNFDGISIPPVDFANTEFVGVSEFWYTTN... | 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 ... |
P40009 | MLIENTNDRFGIVIDAGSSGSRIHVFKWQDTESLLHATNQDSQSILQSVPHIHQEKDWTFKLNPGLSSFEKKPQDAYKSHIKPLLDFAKNIIPESHWSSCPVFIQATAGMRLLPQDIQSSILDGLCQGLKHPAEFLVEDCSAQIQVIDGETEGLYGWLGLNYLYGHFNDYNPEVSDHFTFGFMDMGGASTQIAFAPHDSGEIARHRDDIATIFLRSVNGDLQKWDVFVSTWLGFGANQARRRYLAQLINTLPENTNDYENDDFSTRNLNDPCMPRGSSTDFEFKDTIFHIAGSGNYEQCTKSIYPLLLKNMPCDDEPCLF... | 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... |
O31809 | MFSPTSKITTAQATIIIINYMLAAGVLTLPRTVTEQTQSPDGWISVLLGGVLAVIAGMIIAKLSQQYPKETFYEYSRHIVGKWLGHLISIVFITYFLALGAFEVRVMSEIVDFFLLEGTPSWAIIMTVLWIGLYSITQGLDPIARLFEMIFPITVIIFLTIALMSLGIFEINNLRPVLGDGIMPVLRGVKTTNLSFTCSEIMFILVAFMKKPKNAVKAVVIGTGVVTSFYMITMIMVIGALSVEGVVTRTWPGLDLMRSFEIPGLIFERFESFLLVIWIMQLFATFIITFYAASLGVSQVFKKKPLSCMFGLLPVIYILS... | 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 | MKSKLKRQLPAMVIVCLLMICVTGCWSSREIEDLGLTFAIAIDKGKETNTEKELKEEGGSYPKKDNITLTYQFVNEKAAGAGTSGGGGSGQGAQKAYINISETGDSLQQIGSEVALRRDREVFSPHLKVVVMSEDVLHTFPIDEMLDQFFRDNEIRLSCLVLSAKGEARDALQLKENGEIPAFRLIGLGENEHKVSRILPPMTLAKLIGKLHSGSSFLLQNVVAANGAVKYSGAAVINGKSKKMIGTLNEYETEGITWIRGEGKGGVVKSHDKKSQQTLAYDINKIKSRIQPIVKGKDISFHVDIESEGDLVENWNTKEA... | 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 | MKRASLLTLTLIGAFSAIQAAWAVDYPLPPTGSRLVGQNQTYTVQEGDKNLQAIARRFDTAAMLILEANNTIAPVPKPGTTITIPSQLLLPDAPRQGIIVNLAELRLYYYPPGENIVQVYPIGIGLQGLETPVMETRVGQKIPNPTWTPTAGIRQRSLERGIKLPPVVPAGPNNPLGRYALRLAHGNGEYLIHGTSAPDSVGLRVSSGCIRMNAPDIKALFSSVRTGTPVKVINEPVKYSVEPNGMRYVEVHRPLSAEEQQNVQTMPYTLPAGFTQFKDNKAVDQKLVDKALYRRAGYPVSVSSGATPAASNAPSVESAQ... | 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 | MRTRITLALAVLLLLLAGCSPGAPADGPVTLRFQSLAWQPDSVAATKELVGEWNATHPDVKVEYIQGSWDSVHDQLLTSFEGGEAPDVIHDASDDLADFAYGGYLADLSGLLPARLASDIPRGSWETATFGRGVYGVPFLQEPRVLIADADRLRAAKVRIPTPGHPWSWPEFRQVAKKLTGPGRYGVAWPLKEPVSATLNLSLSAGGRLFHRGADDKVTVRFEAGDEVVARTIHDQVAVDREHAPASTLGSGGADTLPGLFGGRYAMVPLGFSYRQQIVRQAPEDFHWQVLPAPAGAGGLTQGVSPQTLSVSADCPHKKE... | 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 | MTFPNVKFIGNKRVLSIQSSVSHGYVGNRSATFPLQLHEWEVDVVPTVHFSNHLGYGATRGSACIPEEVHDLLNALLQDNGIVYDAILTGFVPNHDIIQVIFDCVLAYKKDHPKVLWLLDPVMGDQGKMYVDTNVISTYKAMIPHAFAITPNAFEVEILTDIVIHTQMDAKRGLEKIYQLYGIQNAIITSFEVEESPGTLFCMGYSCEHGKPQLFLYQFPSLSGVFTGTGDLFSGLLLAKYREELDKRKHQQSDETKQTKRPTVLACAVGQVLSCMHTVLVNTKTYADEILLEDPKIASDEFLLSNARELRLIQSRTALL... | 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
Sequen... |
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 | MMNKKNNKYKSDSLDSKEDKVDLYQDAMISNLISVNNKSTSDSDAKKPTENRIELLKNAYKGGTLKPMIDFDDHNTETFMDKRITKNLLDARSLFLSMGVKLIYIKSGTTGHTFKAISRSNKNVVFAVKVCAYPKDDYGGIKSSSRPENVEIRMLKILSYFVVNRLTPHLVLPIGTFHTDIEKFINIPEGVIDLKDEKNDMYKKFIERYHDGEFEKFVSVLISEWCNGGDLLDYIRKNYDSMTLETWTVVIFQLLFTLALIHEKFPAFRHNDMKANNILVEKTDNKHEGPDKWYRYSLGSHVFIIPGIGIQIKIWDFDFA... | 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-Y... |
Q11082 | MSLSGQLWKMVNSTSPNAAATVGNIAYCYVLPCICAIGIVGNITNLMVLASRRLRAVSYMYLRALAVADLLCMLFVLVFVSTEYLAKNGSSINQYKLYQIYQCHLMLTLINWALGAGVYVVVALSLERYISIVFPMHFRTWNSPQRATRAIVIAFLIPAIFYVPYAITRYKGKQRFDLLQNVTIYSMDDHPIYTTFYWQIYKWTREAILRFLPIIILTVLNIQIMIAFRKRQKMFQQLTNKRKEQGTQKDDTLMYMLGGTVLMSLVCNIPAAINLLLIDETLKKRLDYQIFRAVANILEITNHASQFYVFCACSTDYRTT... | 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 | MSTDGNNNKKGSKEGPKSSEISKFDLAKENPKLAEWMDDCIKRMNSLYKDTNINICNVMTGHEIISIIRMVEAIFMEESNLCEAEAPIKVIGDIHAQYQDMNRLFDLIGRVPEEKLMFLGDYVDRGPQGIEVLILLFCLKIRYRDRIYLLRGNHETPSVNKIYGFYVECQYKYGIGLWWDFQSCFNRMPMSGLISKRVLCMHGGLSPELINLDTIRNIPRPCEPLDRGLLIDLLWSDPTNKGEGWFHSIRGISYMFGKGVVEQACKSLEIDLIIRAHQVVQDGYEMMTGRRLITVFSVPNYCAQFTNAAAVVCLNANLQI... | 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 | MRNPFLTFRAPTRKTGDYLVSKFVKKDNFSSLRLARAYTFSTRSTAVSQFSLLSLSQRSFQSLKINKGIPEKHKIPLISSKQFSVTSKRSQNGSSGSNSDANGRKNGQKNDDSKKKGLNGNDPKKVFEIALNGNTILGGILVAYILYNVLSPNANMQEITWQDFRQQFLDKGLVERLVVVNRNMVRVILRGGVASGSGQYYFSIGSIDSFDRKLEDAQRQLGIPPSEFVPVAYHDEVSVLATLLSFAPTLLIIGSVIYLSRRASGAAGGGQGGIFGIGKSRAKMFNHETDIKIKFADVAGVDEAKEEIMEFVKFLKNPKF... | 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. Fu... |
O49312 | MCNNNNTSCVNISSMLQPEDIFSRRCIWVNGPVIVGAGPSGLAVAADLKRQEVPFVILERANCIASLWQNRTYDRLKLHLPKQFCQLPNLPFPEDIPEYPTKYQFIEYLESYATHFDLRPKFNETVQSAKYDKRFGLWRVQTVLRSELLGYCEFEYICRWLVVATGENAEKVVPEFEGLEDFGGDVLHAGDYKSGERYRGKRVLVVGCGNSGMEVSLDLCNHDASPSMVVRSSVHVLPREVLGKSTFELSVTMMKWMPVWLVDKTLLVLTRLLLGNTDKYGLKRPEIGPLELKNTAGKTPVLDIGAISMIKSGKIKIVAG... | 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 metaboli... |
Q9SVU0 | MENMFRLMDQDQDLTNNRCIWVNGPVIVGAGPSGLATAACLHEQNVPFVVLERADCIASLWQKRTYDRLKLHLPKQFCQLPKMPFPEDFPEYPTKRQFIDYLESYATRFEINPKFNECVQTARFDETSGLWRVKTVSKSESTQTEVEYICRWLVVATGENAERVMPEIDGLSEFSGEVIHACDYKSGEKFAGKKVLVVGCGNSGMEVSLDLANHFAKPSMVVRSSLHVMPREVMGKSTFELAMKMLRWFPLWLVDKILLVLSWMVLGNIEKYGLKRPEMGPMELKSVKGKTPVLDIGAIEKIRLGKINVVPGIKRFNGNK... | 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 metaboli... |
B8ANW0 | MQGQQKQNAGGGGGDNASPCIVLDGPIIVGAGPSGLAVAATLRQHGAPFTVVERSGGVADLWTNRTYDRLRLHLPKVFCELPHVAFPPDFPTYPTKHDFLRYLHSYAARFAIAPLLRRTVTRAWYDHPASLWRVTTTTTSSSATSVITEYASPWLVVASGENAEVVVPKVKGRERFAGEALHSSEYRSGERFRGMRVLVVGCGNSGMEMCLDLCEHGAMPFMSVRSGVHVLPREMFGASTFGIAMKLLRWLPIKMVDRFLLLVARMVLGDTEKYGLKRPKLGPLEIKNITGKSPVLDVGAWSLIKSGNIKIVPEVESFSG... | 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 later... |
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 | MRKAFTRIRLRNNRYAAYIIGFSFLAVSIILGISCGSLHIPIPAVFRVFWHQGFGGSIGSDDPMYTNIMMNIRLPRVVLAALVGAALSIAGAAFQGLLKNPLADPYTLGVSSGASVGAVVTLFLGLHLPVIGGFTLPVLSVAAALATMAAVLFFSRLVHASMSVSTLILTGVITNSFLGAFISLIIALTGDNLLPIVHWLLGSVSMRGWSYVILFLPFFLLGTILLIINGRELNVMTYGEDKAKLLGVSVQQRKMMILIAGSLLTGSAVAVSGTIGFVGLVIPHITRLLWGTDHRHLLPLSALLGAGFLVLADLLSRTII... | 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 | MRLRWKFLFHFFGQMLIVILLLTVMLVASFFYLDARFSDAESNSGLTKATTDTLEAYLDVNEDGTWEVDNFLKKSVDKQHGWMQIIDSEGNTDYSYGVPKDVPGTYTKKELLSIYKTKKLHNYKLNYWAINIEDKSYLLLSGWKSKSEQLLTSVEKREQKIDSLAHYKSSTIDYIKRKKGAIYLLDSNGKILDSINSTKSERKTMNQLELLKYSSKPWNYKREISVKILNKDRWMVATVPNPVYVTDQEFNKSFLKVVLKAMFLVMAVLFMYIIWMTVWYMFRFGLPIFHTIRWLVNLSKGKLEEPRNREGRPVSKNKKG... | 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 ... |
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
Su... |
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 memb... |
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:... |
P42422 | MKLFLRSHAVLILLFLLQGLFVFFYYWFAGLHSFSHLFYILGVQLLILAGYLAYRWYKDRGVYHWLSSGQEGTDIPYLGSSVFCSELYEKQMELIRLQHQKLHETEAKLDARVTYMNQWVHQVKTPLSVINLIIQEEDEPVFEQIKKEVRQIEFGLETLLYSSRLDLFERDFKIEAVSLSELLQSVIQSYKRFFIQYRVYPKMNVCDDHQIYTDAKWLKFAIGQVVTNAVKYSAGKSDRLELNVFCDEDRTVLEVKDYGVGIPSQDIKRVFDPYYTGENGRRFQESTGIGLHLVKEITDKLNHTVDISSSPGEGTSVRFS... | 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... |
P42424 | MTFLQFAYKNVTRNKRAYLAFFLSSAFSVLIFFTFAMFLFHPALKEGYLNNIAKKGLTAAEWMIFVFSFLFVLYSVNAFLKSRNKEFGILLMQGITPGQLRKLITAENMIIGVMSIAAGIIGGFIFSKTFFTVGAYILEMDALPLYMPWKALGITACGFLLLFFFLSQFTILFVRSNTVIKLIKGTGKVKPEPKPSVLLSLFGIACLCGGYGMVLKGNVHGAEPFIILLLTVIGTYFFFSQSSIWILRALKKWKTFYLRGKNIIWVSDLVYRLKDNARLFFIVSIISAVAFTATGVLAMYKSTVGAEESAYEMEYLSYSN... | 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 | MKKNILLVGMLVLLLMFVSACSGTASKGSSSDSASEKTEMRTYKSPKGNVNIPAHPKRIVTDFYAGELLSVGANVVGSGSWSFDNPFLKSKLKNVKDVGDPISVEKVMELQPDLIVVMNEENVDKLKKIAPTVVIPYNTAKNVEDTVSMFGDIAGAKDQAKSFMADFNKKAEAAKKKIAGVIDKDATFGIYENTDKGEFWVFNDNGGRGGQAVYNALGLKAPEKIEQDVIKKGEMKQLSQEVIPEYAADYMFITDYNPKGESKTLDKLENSSIWKNLDAVKHNRVFINDFDSFYPYDPISVSKQVDIITDMLIKRAEENK... | 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
S... |
Q5ISE2 | MANNNLNRPLNTNVADSSNSSSTPGTAPPPSSSDPQVLGHQAPSSSASSLTEDCSSSFARDLNSYNNGQSGATGAVSWEAPHEPSEANAVSQIHPRNGEHSLQQKPKPQKVSGSSSLATSERYKTELCRPFEESGICKYGHKCQFAHGYRELRTLSRHPKYKTEPCRTFHSVGFCPYGTRCHFIHNQPEQQPVLSESTLEEPSSFNGSNVLHLGVNGEQQPGLQSDSPSGFLSVNSQALQAPLQLNQQALSSGGVMPSSHPAAANLRMMCCRTSSSTTAHDADKDPDKDADKDPSNNSANDALAFPQEPGDFSPVAFQNP... | 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 ... |
Q8VD12 | MILGSLSRAGPLPLLRQPPIMQPPMDLKQILPFPLEPAPTLGLFSNYSTMDPVQKAVLSHTFGGPLLKTKRPVISCNVCQIRFNSQSQAEAHYKGNRHARRVKGIEAAKTRGREPSVRESGDPAPAGSIPPSGDGVAPRPVSMENGLGPAPGSPEKQPGSPSPPSVPESGQGVTKGEGGTSVPASLPGGSKEEEEKAKRLLYCALCKVAVNSLSQLEAHNKGTKHKTILEARSGLGPIKAYPRLGPPTPGEPEAPAQDRTFHCEICNVKVNSEVQLKQHISSRRHRDGVAGKPNPLLSRHKKPRGAAELAGTLTFSKELP... | 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... |
Q9Y2Y4 | MSLPPIRLPSPYGSDRLVQLAARLRPALCDTLITVGSQEFPAHSLVLAGVSQQLGRRGQWALGEGISPSTFAQLLNFVYGESVELQPGELRPLQEAARALGVQSLEEACWRARGDRAKKPDPGLKKHQEEPEKPSRNPERELGDPGEKQKPEQVSRTGGREQEMLHKHSPPRGRPEMAGATQEAQQEQTRSKEKRLQAPVGQRGADGKHGVLTWLRENPGGSEESLRKLPGPLPPAGSLQTSVTPRPSWAEAPWLVGGQPALWSILLMPPRYGIPFYHSTPTTGAWQEVWREQRIPLSLNAPKGLWSQNQLASSSPTPGS... | 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-... |
Q9JKD9 | MPQTPTRLVSPYGSDRLVQLAARLRPALCDTLITVGGLEFPAHSLVLAGASPRLGCRGRWALVEDISPSTFAQILTFVYGESIELQPGELGDLEEAAKALGVQALEEACQRAQKGKDEDELDPGLKRHQQSEDFMRGSERGLGSPGEKQKPEKDFRSNGREQEMSHKHKAPGERPEMAGATRMMSSEEVMRGIESHKGSEESLRGCPDPLSPPGSLLTSLIPRPWWAEVPRLGEGQSALWSILLWPSRYGAPFSHSTPITAAWQVRPQDQRIPLTLNHSKALWSQNQLASSSPTPGSFPQGTESLSPWQIETSGQGFTGT... | 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 activat... |
Q9SAC0 | MAVYHLLLSSPPSLLLLPPSPRRPNLTLIRRIPAHPRLGNSTSLLSSSSPVIRKILVRSTLREDQPIASDSESSPTLLIGEDSAAFELGKQKLVSWVYFGVVLGVVLFILNVVWIDNSTGFGKSFIDAVSNISGSPEVAMLMLILIFAIVHSGLASLRDIGEKLIGERAFRVLFAGISLPLAMSTIVYFINHRYDGSQLWQLQGVPGVHEAIWVANFVSFFFLYPSTFNLLEVAAVDKPKMHLWETGIMRITRHPQMVGQIVWCLAHTLWIGNTVAASASLGLIAHHLFGAWNGDRRLAKRYGEDFESIKKRTSVIPFAA... | 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 Len... |
B4FHU1 | MASQLRLHLAATPPLLPHRRPHLARPLCPTLNPIRAPLPPLSRVLSHARPARAVGGGIEPKEGVVAEGDESGGGPVLVGEDSAAFELKDQSVASWAYFAGILGAVLVALNVLWIDPSTGVGTKFLDAVASVSDSHEVVMLLLTIIFAVVHSGMASLRESGEKIVGERVYRVLFAGISLPLAVTTIVYFINHRYDGTQLWQVQGITGIHELLWFSSFISFFFLYPSTFNLLEVAAVDKPKLHMWETGIMRITRHPQMVGQVIWCLAHTLWIGNSVAVAASVGLISHHLFGAWNGDRRLLSRYGEAFEVLKKRTSVMPFAAI... | 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 Len... |
Q9H0M4 | MMTTLQNKEECGKGPKRIFAPPAQKSYSLLPCSPNSPKEETPGISSPETEARISLPKASLKKKEEKATMKNVPSREQEKKRKAQINKQAEKKEKEKSSLTNAEFEEIVQIVLQKSLQECLGMGSGLDFAETSCAQPVVSTQSDKEPGITASATDTDNANGEEVPHTQEISVSWEGEAAPEIRTSKLGQPDPAPSKKKSNRLTLSKRKKEAHEKVEKTQGGHEHRQEDRLKKTVQDHSQIRDQQKGEISGFGQCLVWVQCSFPNCGKWRRLCGNIDPSVLPDNWSCDQNTDVQYNRCDIPEETWTGLESDVAYASYIPGSI... | 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... |
Q6IR42 | MMAALQTHKEYEKGTKKTFAPPTQKLHSEKPQPSSWKEDAPGTSSPEAETKPSLLKASLKKEQKPTTEHGPNRGQERKLKAQDQPAKKKGKERTLTSAEFEEIFQIVLQKSLQECLETSSCVQHIRPTKLDEEPGIVPPATDKKDADPEKVITPDTPKIASSLEEEVNSEMGTSKLGQPVTEPSKKKFNRLSLSKQKKKAEDEKMEKIQDGRECSLKEKQKIVIQDQSQIRGPQKEEESGFGHCVIWVQCSSPKCEKWRQLRGNIDPSVLPDDWSCDQNPDPNYNRCDIPEESWAGCESDVAYASYVPGSIIWAKQYGYP... | 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 cel... |
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 o... |
B8A4F0 | MHPCSSVLHLLLRCMRGCCRHTRSRVPRRLRRHVSYIRLIFKSLYFNSLTNSDVVTDSILEPVFWMVEVVTRWFGMVFVFLVVALTSSVVFIAYFCLLPLVLHTYSPGWMIWHICYGHWNLVMIVFHYYKATKTPPGYPPKMKTDVPFVSVCKKCIIPKPARSHHCGICKTCILKMDHHCPWLNNCVGHFNHRYFFSFCLFLTLGCMYCSVSGRHLFIDAYNTIDQLKHLEAEKQGVPVTGIGLLIGIVPSAGVAGKAVQVAQEVSQPPYTYKDRMFHKSVIYMWVLTSTVSVALGALTLWHALLITRGETSIERHINGK... | 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 .
Ca... |
Q7ZVN4 | MKNREYQQIDPQALATPTPTPPPRSLPEHKPRRARRKWEVFPGKNRFYCDGRIIVARQSGVLPLTLGLILLTSGLFFIFDCPFLVKHLTSCIPAIGGVLFVFVIISLLQTSFTDPGILPRATPEEAADIEKQIDNPTGSSSSYRPPPRTKEVVINQQVVKLKYCFTCKIFRPPRTSHCSLCDNCVERFDHHCPWVGNCVGKRNYRFFYTFIVSLSFLTAFIFGCVTTHLALRSQGGNGLVNALQSSPASALELVVCFFSVWSILGLSGFHTYLVAANLTTNEDIKGSWSGKSGNEDVGNPYSYNSMIKNCCSVLCGPMPP... | 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... |
F1Q7H8 | MAPSHAVRCCQRGLSWIPVIFINLVVCWSYYAYVVELCIYTIPNVNEQVIYLVVFHAFFFMFMWSYWKTISSKPTNPSKEFCLPKAEKELYEKEERPEAQQDILKRVARELPIYTFTGSGAIRYCDRCQLIKPDRCHHCSTCDKCVLKMDHHCPWVNNCVGFSNYKFFVLFLAYSMLYCVYIAATVLQYFIKFWTNQLPDTHAKFHVLFLFFVAAMFFISILSLFSYHLWLVGKNRTTIEAFRAPVFRNGPDKNGFTLGFRKNITQVFGDQKKYWCLPIFSSLGDGYTFPTRLVTVDVEHGNIEHQTIKCTVDGQTNARP... | 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: ... |
Q8LGB6 | MSKNNKKKRRWDLKNGGILLEELIASFDGKTNPIRCFSSDQILKATDNFSESRIISSWGYFIWYKGVIEERQVSIKKWSSQNLSSFTEAYRDISVSSQMSGHKNALKLIGCCLEFDLPALVCEYTEHGPLNRDGGLSSGVVLPWKVRLKIAKEIASSVTYLHTAFPETIVHRNINPTNIFIDENWTAKLSDFWFCVAIPEGELYVEDDVKGVIGFVDPDYYWTMKVTEKVDIYSFGVVMLVLLSGRAAVFNGPDEAPMSLNDHVSEVMEKGEFDEIVDKEIWNDLGGDDDLVLRRSQVKAFLRLALRCVRYKKEDPVSGM... | 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 ... |
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 membra... |
Q94BZ1 | MAEEYAECLLEKNFHEDCSGCKVDQMKRLRRGFPFWELFTVWIIVLCTALPISSLFPFLYFMIDDFNIAKKEEDIGFYAGFVGCSFMLGRAFTSVAWGLVADRYGRKPVILIGTASVVVFNTLFGLSLNFWMAIITRFCLGSFNGLLGPIKAYAMEIFRDEYQGLALSAVSTAWGIGLIIGPAIGGFLAQPAKQYPSLFSQDSIFGKFPFFLPCLAISVFAFLVTIVSSRIPETLHNHKFNDDESYDALKDLSDDPESNKVAERNGKSSLLNNWPLISSIIVYCVFSLHDMAYTEIFSLWANSPRKYGGLGYSTADVGSV... | 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 ... |
Q8NF64 | MNSMNPMKPALPPAPHGDGSFAYESVPWQQSATQPAGSLSVVTTVWGVGNATQSQVLGNPMGPAGSPSGSSMMPGVAGGSSALTSPQCLGQQAFAEGGANKGYVQQGVYSRGGYPGAPGFTTGYAGGPGGLGLPSHAARPSTDFTQAAAAAAVAAAAATATATATATVAALQEKQSQELSQYGAMGAGQSFNSQFLQHGGPRGPSVPAGMNPTGIGGVMGPSGLSPLAMNPTRAAGMTPLYAGQRLPQHGYPGPPQAQPLPRQGVKRTYSEVYPGQQYLQGGQYAPSTAQFAPSPGQPPAPSPSYPGHRLPLQQGMTQSL... | 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 p... |
Q86UQ0 | MWAPREQLLGWTAEALPAKDSAWPWEEKPRYLGPVTFEDVAVLFTEAEWKRLSLEQRNLYKEVMLENLRNLVSLAESKPEVHTCPSCPLAFGSQQFLSQDELHNHPIPGFHAGNQLHPGNPCPEDQPQSQHPSDKNHRGAEAEDQRVEGGVRPLFWSTNERGALVGFSSLFQRPPISSWGGNRILEIQLSPAQNASSEEVDRISKRAETPGFGAVTFGECALAFNQKSNLFRQKAVTAEKSSDKRQSQVCRECGRGFSRKSQLIIHQRTHTGEKPYVCGECGRGFIVESVLRNHLSTHSGEKPYVCSHCGRGFSCKPYLI... | 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 | MFPGLAAAAAAHRCSWAALCRLGGGRAATRGRSQGWKNVMTFESFTYVVPDIHPHLSIINQVKLYSTNVQKGGQGSQTPKADKVPSLTQTVENIGAELKAPLKQDPLQVRVKAVLKKRDYGSKYTKNNFITGVRAINEFCLKSSDLEQLRKIRRRSPHDDTESFTVFLRSDVEAKALEVWGSLEALAREKKLRKEAEIEYRERLFRNQRILREYGDFLGNTKPRSRAVSVFLKGPGKVVMVAICINGLNCFFKFLAWIYTGSASMFSEAIHSLSDTCNQGLLALGISKSVQTPDPSHPYGFSNMRYISSLISGVGIFMMG... | 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) =... |
Q55FL1 | MSIFAYSILAGLAPLLSSSIPFFTLRNRNINASVFHILLCISAGLLFAVASLELIPESMNLALRSFEESTKTQTSLKSTTTKTTTTTTTIGNIKLQKSFISNSEDSLNEFHSLDNEINKPPIEGLNLNNLNQATNLDNNEEDNDNLDNDGENEIENDHDHDHQEDEGGDNDHDHESEEKKEFLKIPMYGIGFGFAILIIVESIFSSIDGGGGGGGHHSHSHGSLSSSSSNDVISDYISNNNSNNINNNDDDNNNNNNNNDDDDDSVELLERNVVNKDNSNNINNINNNNDDEDIIVINKSIENTPNIASPVMNKDNNNND... | 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 | MSTPDNHGKKAPQFAAFKPLTTVQNANDCCCDGACSSTPTLSENVSGTRYSWKVSGMDCAACARKVENAVRQLAGVNQVQVLFATEKLVVDADNDIRAQVESALQKAGYSLRDEQAAEEPQASRLKENLPLITLIVMMAISWGLEQFNHPFGQLAFIATTLVGLYPIARQALRLIKSGSYFAIETLMSVAAIGALFIGATAEAAMVLLLFLIGERLEGWAASRARQGVSALMALKPETATRLRKGEREEVAINSLRPGDVIEVAAGGRLPADGKLLSPFASFDESALTGESIPVERATGDKVPAGATSVDRLVTLEVLSE... | 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... |
Q54LY6 | MTSLETYNDNVKTALIMCFLSGLSTAIGGLYVIFIKQQSHKLLGHLLSFSSGVMIYISFMDLLPESIAEIGFYNANIWFFVGIIFFAVILRFVPHDHDESGDSNHAHSHNGASIEKHSSEKKEVVDDDDDDNNGKDKKQKQQKQKQQKQQQQQKQNIAKSKNKKKSKDDYLNSVGIATAIGVSLHNFPEGVAVYLACLKGIDVGLPLMLAIAAHNIPEGMAVAAPIFSATGSKWKAFKYCLYSGLCEPVGAIIFGLIFKEYMTPYLIQSMLAAVAGIMVFMVIKELLPAAFKYVSVDESAFSNIIGMIFFFFSIHFLHSM... | 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 L... |
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 L... |
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 L... |
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 L... |
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 L... |
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 m... |
P14375 | MTHDNIDILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPVLIMTAYSSVETAVEALKTGALDYLIKPLDFDNLQATLEKALAHTHSIDAETPAVTASQFGMVGKSPAMQHLLSEIALVAPSEATVLIHGDSGTGKELVARAIHASSARSEKPLVTLNCAALNESLLESELFGHEKGAFTGADKRREGRFVEADGGTLFLDEIGDISPMMQVRLLRAIQEREVQRVGSNQIISVDVRLIAATHRDLAAEVNAGRFRQDLYYRLNVVAIEVPSLRQRREDIP... | 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... |
P14377 | MRFMQRSKDSLAKWLSAILPVVIVGLVGLFAVTVIRDYGRASEADRQALLEKGNVLIRALESGSRVGMGMRMHHVQQQALLEEMAGQPGVLWFAVTDAQGIIILHSDPDKVGRALYSPDEMQKLKPEENSRWRLLGKTETTPALEVYRLFQPMSAPWRHGMHNMPRCNGKAVPQVDAQQAIFIAVDASDLVATQSGEKRNTLIILFALATVLLASVLSFFWYRRYLRSRQLLQDEMKRKEKLVALGHLAAGVAHEIRNPLSSIKGLAKYFAERAPAGGEAHQLAQVMAKEADRLNRVVSELLELVKPTHLALQAVDLNTL... | 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-h... |
Q8NEG5 | MLRRGYKASERRRHLSERLSWHQDQALSSSIYLLREMGPTGFLLREEEPEYMDFRVFLGNPHVCNCSTFPKGGELCKHICWVLLKKFKLPRNHESALQLGLGEREISDLLRGIHRVQTPQPGTNDENEHVEEDGYIKQKEIDSEDICSICQELLLEKKLPVTFCRFGCGNSIHIKCMKILANYQSTSNTSMLKCPLCRKEFAPLKLILEEFKNSSKLVAAAEKERLDKHLGIPCNNCKQFPIEGKCYKCTECIEYHLCQECFDSCCHLSHTFTFREKRNQKWRSLEKRADEVVKYIDTKNEIEEKMSHFQEKQGQVYTPK... | 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 Act... |
Q9D9X6 | MLRGGCKASEKRRHLSESLSWQQDQALSSSIYLLRQIGPTGFLLKEEEPEKGDFRVLLGNPHECSCPTFLKRGELCKHICWVLLKKFKLPRNHESAFQLGLTEGEINDLLRGIHQVQAPQLRASDETAQVEEDGYLKQKDINAGDICPICQEVLLEKKLPVTFCRFGCGNNVHIKCMRILANYQDTGSDSSVLRCPLCREEFAPLKVILEEFKNSNKLITISEKERLDKHLGIPCNNCNQLPIEGRCYKCTECVEYHLCQECFDSCCHSSHAFASREKRNQRWRSVEKRSEVMKYLNTENEGEAKPGCFQEKQGQFYTPK... | 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-ubiquit... |
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