ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
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Q9GL50 | MESRQDITNQEELWKMKPRKNLEDDYLNEDSRENSMPKRPMLVHLHQTAHFDEFDCPPELQHKQELFPKWHLPIKIAAIVSSLTFLYTLLREVIHPFVTSHQQYFYKIPILVINKVLPMVSITLLALVYLPGVIAAIVQLHNGTKYKKFPHWLDRWMVTRKQFGLLSFFFAVLHAVYSLSYPMRRSYRYKLLNWAYQQVQQNKEDAWIEHDVWRMEIYVSLGIVTLAILALLAVTSIPSVSDSLTWREFHYIQSTLGIVSLLLGTIHALIFAWNKWVDIKQFIWYTPPTFMIAVFLPTVVLICKVILLLPCLRRKILKIR... | Function: Metalloreductase that has the ability to reduce both Fe(3+) to Fe(2+) and Cu(2+) to Cu(1+). Uses NAD(+) as acceptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 39918
Sequence Length: 338
Subcellular Location: Endosome membrane
EC: 1.16.1.-
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Q8NFT2 | MESISMMGSPKSLSETFLPNGINGIKDARKVTVGVIGSGDFAKSLTIRLIRCGYHVVIGSRNPKFASEFFPHVVDVTHHEDALTKTNIIFVAIHREHYTSLWDLRHLLVGKILIDVSNNMRINQYPESNAEYLASLFPDSLIVKGFNVVSAWALQLGPKDASRQVYICSNNIQARQQVIELARQLNFIPIDLGSLSSAREIENLPLRLFTLWRGPVVVAISLATFFFLYSFVRDVIHPYARNQQSDFYKIPIEIVNKTLPIVAITLLSLVYLAGLLAAAYQLYYGTKYRRFPPWLETWLQCRKQLGLLSFFFAMVHVAYS... | Function: Metalloreductase that has the ability to reduce both Fe(3+) to Fe(2+) and Cu(2+) to Cu(1+). Uses NAD(+) as acceptor (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 56056
Sequence Length: 490
Subcellular Location: Endosome membrane
EC: 1.16.1.-
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Q658P3 | MPEEMDKPLISLHLVDSDSSLAKVPDEAPKVGILGSGDFARSLATRLVGSGFKVVVGSRNPKRTARLFPSAAQVTFQEEAVSSPEVIFVAVFREHYSSLCSLSDQLAGKILVDVSNPTEQEHLQHRESNAEYLASLFPTCTVVKAFNVISAWTLQAGPRDGNRQVPICGDQPEAKRAVSEMALAMGFMPVDMGSLASAWEVEAMPLRLLPAWKVPTLLALGLFVCFYAYNFVRDVLQPYVQESQNKFFKLPVSVVNTTLPCVAYVLLSLVYLPGVLAAALQLRRGTKYQRFPDWLDHWLQHRKQIGLLSFFCAALHALYS... | Function: Endosomal ferrireductase required for efficient transferrin-dependent iron uptake in erythroid cells. Participates in erythroid iron homeostasis by reducing Fe(3+) to Fe(2+). Can also reduce of Cu(2+) to Cu(1+), suggesting that it participates in copper homeostasis. Uses NADP(+) as acceptor. May play a role d... |
Q8CI59 | MSGEMDKPLISRRLVDSDGSLAEVPKEAPKVGILGSGDFARSLATRLVGSGFSVVVGSRNPKRTAGLFPSLAQVTFQEEAVSSPEVIFVAVFREHYSSLCSLADQLAGKILVDVSNPTEKEHLQHRQSNAEYLASLFPACTVVKAFNVISAWALQAGPRDGNRQVLICSDQPEAKRTISEMARAMGFTPLDMGSLASAREVEAIPLRLLPSWKVPTLLALGLFVCFYTYNFIRDVLQPYIRKDENKFYKMPLSVVNTTLPCVAYVLLSLVYLPGVLAAALQLRRGTKYQRFPDWLDHWLQHRKQIGLLSFFFAMLHALYS... | Function: Endosomal ferrireductase required for efficient transferrin-dependent iron uptake in erythroid cells. Participates in erythroid iron homeostasis by reducing Fe(3+) to Fe(2+). Also mediates reduction of Cu(2+) to Cu(1+), suggesting that it participates in copper homeostasis. Uses NADP(+) as acceptor. May play ... |
Q687X5 | MEKTCIDALPLTMNSSEKQETVCIFGTGDFGRSLGLKMLQCGYSVVFGSRNPQKTTLLPSGAEVLSYSEAAKKSGIIIIAIHREHYDFLTELTEVLNGKILVDISNNLKINQYPESNAEYLAHLVPGAHVVKAFNTISAWALQSGALDASRQVFVCGNDSKAKQRVMDIVRNLGLTPMDQGSLMAAKEIEKYPLQLFPMWRFPFYLSAVLCVFLFFYCVIRDVIYPYVYEKKDNTFRMAISIPNRIFPITALTLLALVYLPGVIAAILQLYRGTKYRRFPDWLDHWMLCRKQLGLVALGFAFLHVLYTLVIPIRYYVRWR... | Cofactor: Can also utilize FMN . Can also utilize riboflavin.
Function: Integral membrane protein that functions as NADPH-dependent ferric-chelate reductase, using NADPH from one side of the membrane to reduce a Fe(3+) chelate that is bound on the other side of the membrane. Mediates sequential transmembrane electron t... |
P27105 | MAEKRHTRDSEAQRLPDSFKDSPSKGLGPCGWILVAFSFLFTVITFPISIWMCIKIIKEYERAIIFRLGRILQGGAKGPGLFFILPCTDSFIKVDMRTISFDIPPQEILTKDSVTISVDGVVYYRVQNATLAVANITNADSATRLLAQTTLRNVLGTKNLSQILSDREEIAHNMQSTLDDATDAWGIKVERVEIKDVKLPVQLQRAMAAEAEASREARAKVIAAEGEMNASRALKEASMVITESPAALQLRYLQTLTTIAAEKNSTIVFPLPIDMLQGIIGAKHSHLG | Function: Regulates ion channel activity and transmembrane ion transport. Regulates ASIC2 and ASIC3 channel activity.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 31731
Sequence Length: 288
Subcellular Location: Cell membrane
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P54116 | MSDKRQSSHVQSQRIPESFRENSKTELGACGWILVAASFFFVIITFPISIWICIKIVKEYERVIIFRLGRILQGGAKGPGLFFILPCTDSLIKVDMRTISFDIPPQEVLTKDSVTISVDGVVYYRVQNATLAVANITNADSATRLLAQTTLRNALGTKNLSQILSDREEIAHHMQSTLDDATDDWGIKVERVEIKDVKLPVQLQRAMAAEAEAAREARAKVIAAEGEMNASRALKEASMVITESPAALQLRYLQTLTTIAAEKNSTIVFPLPVDMLQGIMGSNH | Function: Regulates ion channel activity and transmembrane ion transport. Regulates ASIC2 and ASIC3 channel activity.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 31375
Sequence Length: 284
Subcellular Location: Cell membrane
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Q8WXE9 | MTTLDHVIATHQSEWVSFNEEPPFPAHSQGGTEEHLPGLSSSPDQSESSSGENHVVDGGSQDHSHSEQDDSSEKMGLISEAASPPGSPEQPPPDLASAISNWVQFEDDTPWASTSPPHQETAETALPLTMPCWTCPSFDSLGRCPLTSESSWTTHSEDTSSPSFGCSYTDLQLINAEEQTSGQASGADSTDNSSSLQEDEEVEMEAISWQASSPAMNGHPAPPVTSARFPSWVTFDDNEVSCPLPPVTSPLKPNTPPSASVIPDVPYNSMGSFKKRDRPKSTLMNFSKVQKLDISSLNRTPSVTEASPWRATNPFLNETL... | Function: Adapter protein involved in endocytic machinery. Involved in the synaptic vesicle recycling. May facilitate clathrin-coated vesicle uncoating.
PTM: Phosphorylated in vitro by PKD.
Sequence Mass (Da): 101165
Sequence Length: 905
Domain: The Asn-Pro-Phe (NPF) motifs, which are found in proteins involved in the ... |
O59179 | MRRILLSMIVLIFLASPILAKNIVYVAQIKGQITSYTYDQFDRYITIAEQDNAEAIIIELDTPGGRADAMMNIVQRIQQSKIPVIIYVYPPGASAASAGTYIALGSHLIAMAPGTSIGACRPILGYSQNGSIIEAPPKITNYFIAYIKSLAQESGRNATIAEEFITKDLSLTPEEALKYGVIEVVARDINELLKKSNGMKTKIPVNGRYVTLNFTNVEVRYLAPSFKDKLISYITDPNVAYLLLTLGIWALIIGFLTPGWHVPETVGAIMIILAIIGFGYFGYNSAGILLIIVAMLFFIAEALTPTFGLFTVAGLITFII... | Function: Protease that cleaves its substrates preferentially near hydrophobic or aromatic amino acid residues. Can degrade casein and the stomatin homolog PH1511 (in vitro).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 48281
Sequence Length: 441
Subcellular Location: Membrane
EC: 3.4.21.-
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P0DKI7 | MELQYISYFQPTSSVVALLLALVSILSSVVVLRKTFLNNYSSSPASSTKTAVLSHQRQQSCALPISGLLHIFMNKNGLIHVTLGNMADKYGPIFSFPTGSHRTLVVSSWEMVKECFTGNNDTAFSNRPIPLAFKTIFYACGGIDSYGLSSVPYGKYWRELRKVCVHNLLSNQQLLKFRHLIISQVDTSFNKLYELCKNSEDNHGNYTTTTTTAAGMVRIDDWLAELSFNVIGRIVCGFQSGPKTGAPSRVEQFKEAINEASYFMSTSPVSDNVPMLGWIDQLTGLTRNMKHCGKKLDLVVESIINDHRQKRRFSRTKGGD... | Function: Bifunctional protein involved in the biosynthesis of morphinan-type benzylisoquinoline alkaloids. Required for the isomerization of (S)- to (R)-reticuline. The cytochrome P450 module is responsible for the conversion of (S)-reticuline to 1,2-dehydroreticuline while the oxidoreductase module converts 1,2-dehyd... |
F1BVB7 | MIPNSSSSSILSLLVLLLFSTSSSWATNSIHEDFLNCLSIYKSSFPIPIYTSKNSSFNTLFRSSARNLRFLSPNSTQKPEFIITPTLESHVQTTVVCSKKHGLDLKVRSGGHDVEGLSYVSDSPYVMIDLVDFRNITVNVKNATAWIQAGSSLGEVYYKVGNESKNTLGFPAGFCPTVGVGGHISGGGFGSLVRKYGLASDQVIDARIVTVNGEILNKETMGKDLYWAIRGGGANNFGVLLSWKVKLVPVTPIVTVATIDRTLEQGATNLVHKWQFVADRLHEDVYIGLTMVTANTSRAGEKTVVAQFSFLFLGNTDRLL... | Cofactor: Binds 1 FAD per subunit in a bicovalent manner.
Function: Catalyzes the oxidation of different tetrahydroprotoberberines, such as (S)-canadine, (S)-scoulerine and (S)-tetrahydropalmatine.
PTM: The FAD cofactor is bound via a bicovalent 6-S-cysteinyl, 8alpha-N1-histidyl FAD linkage.
Catalytic Activity: (S)-can... |
P46675 | MSGEEEVDYTTLPLEERLTYKLWKARLEAYKELNQLFRNSVGDISRDDNIQIYWRDPTLFAQYITDSNVVAQEQAIVALNSLIDAFASSSLKNAHNITLISTWTPLLVEKGLTSSRATTKTQSMSCILSLCGLDTSITQSVELVIPFFEKKLPKLIAAAANCVYELMAAFGLTNVNVQTFLPELLKHVPQLAGHGDRNVRSQTMNLIVEIYKVTGNNSDLLEEILFKKLKPIQVKDLHKLFAKVGDEPSSSKMLFEWEKRELEKKRSQEEEARKRKSILSNDEGEYQIDKDGDTLMGMETDMPPSKQQSGVQIDTFSMLP... | Function: Binds to the plus end of microtubules and regulates microtubule dynamics and microtubule organization. May play a role in the attachment, organization, and/or dynamics of microtubule ends at the spindle pole body. Stabilizes both cytoplasmic and nuclear microtubules. Promotes mitotic spindle elongation in ana... |
A0A0D1CVS5 | MSTASPLHHGHGNGSYANSPAPTGVTGRDAGVAAAAVADSAVRSGSVPASASGSAPGSASGSMYGEAHTQHHTGHHHYSAHHTHSHGALTSPVNGGHSSSWSPYGYPAAPVYGGSPSPYGHNAYSQYASGYGYANGTAHHVATAPTTPSATSTAYHTGVNGMMMHHGQHAGYGYSSHHLGSHTPTHTHTHSSAYFMNGDGAHSHLNSSAHLTSPSYTTAPQYSTQLPLAGRHRVTTTLWEDEGTLCFQVDARGVCVARRHDNNMINGTKLLNVCGMSRGKRDGILKNEKERIVVKVGAMHLKGVWISFARAKQLAEQNGI... | Function: Transcription factor that regulates asexual reproduction . Binds the StuA-response elements (StRE) with the consensus sequence 5'-(A/T)CGCG(T/A)N(A/C)-3' at the promoters of target genes (By similarity). Regulates dimorphism, virulence, and the sporulation program . Required for mating, gall induction, and sp... |
Q05319 | MKQPTLIRPRLRHRRSTPAAATKMCPKRHWLVNNRAAGSRGSGGAAARSRRSLDQIVEVLVALIVVNCLATAAAALITPPDSLESLGSLGIPSSSASSSEDDDDMSSGFYRIPHRLEGYPQLQQLQRGQNFKISPKPCSFGRVEGTCMFVWECIKSEGKHVGMCVDSFMFGSCCTHNYTDNIVLPQTAFSYTRPTKPLTLRPRPPAAPYKPMISGMTTIERPHGAGTLVIRPSGPHHQGTLARPHPPPYQSKPTTASDLHGSASHPSSSSSSSSSSNPNSIWHTSTQQQQQQQHQQNQQNHWQMTTEPSFITKPRPTGWT... | Function: Hormone dependent protease required for epithelial morphogenesis, including the formation of bristles, legs, and wings. Has a dual function, detaches imaginal disk cells from extracellular matrices through its extracellular proteolytic domain and transmits an outside-to-inside signal to its intracellular doma... |
O06837 | MTRSLTMNSSLPAIDGLRLPHQMLIGGQWVNAQSDKTLNVYNPATGDTLTDVPDGDVEDVNAAVESAAATLQSDAWRRMPPSARERILLRLADLLEAHGDELARLETLNNGKLLIYSKMMEVGASAQWLRYMAGWATKLTGSTLDLSLPLPPDVRSRASTQRVPVGVVAAIIPWNFPLLMAVWKIAPALACGNTVVLKPAEETPLTALRLAELAMEAGLPAGALNVVTGRGETAGDALVRHPKVAKVAFTGSTEVGRIIGSACGRSLKAVSLELGGKSPVIVLADCDPQEAAEGAAAAIFFNHGQVCTAGSRLYVHESIY... | Function: Phenylacetaldehyde dehydrogenase that catalyzes the last step in the aerobic styrene degradation pathway by mediating oxidation of phenylacetaldehyde to phenylacetic acid.
Catalytic Activity: 2-phenylacetaldehyde + H2O + NAD(+) = 2-phenylacetate + 2 H(+) + NADH
Sequence Mass (Da): 53497
Sequence Length: 502
P... |
O18495 | MQMKATILIVLVALFMIQQSEAGWLRKAAKSVGKFYYKHKYYIKAAWQIGKHALGDMTDEEFQDFMKEVEQAREEELQSRQ | Function: Bactericidal against several Gram-positive and Gram-negative bacteria. Plays a significant role in the innate immune mechanisms of S.clava.
PTM: Contains L-DOPA (3',4'-dihydroxyphenylalanine).
Sequence Mass (Da): 9560
Sequence Length: 81
Subcellular Location: Secreted
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Q6J9G0 | MGMTRMLLECSLSDKLCVIQEKQYEVIIVPTLLVTIFLILLGVILWLFIREQRTQQQRSGPQGIAPVPPPRDLSWEAGHGGNVALPLKETSVENFLGATTPALAKLQVPREQLSEVLEQICSGSCGPIFRANMNTGDPSKPKSVILKALKEPAGLHEVQDFLGRIQFHQYLGKHKNLVQLEGCCTEKLPLYMVLEDVAQGDLLSFLWTCRRDVMTMDGLLYDLTEKQVYHIGKQVLLALEFLQEKHLFHGDVAARNILMQSDLTAKLCGLGLAYEVYTRGAISSTQTIPLKWLAPERLLLRPASIRADVWSFGILLYEMV... | Function: Probable tyrosine protein-kinase, which has strong transforming capabilities on a variety of cell lines. When overexpressed, it can also induce tumor cell invasion as well as metastasis in distant organs. May act by activating both MAP kinase and phosphatidylinositol 3'-kinases (PI3K) pathways (By similarity)... |
Q6J9G1 | MGEKGHLSRVLLECSLSDKLCVVREKQYEVIIVPALLVGGFLILLAIILWLFIRGQRSQRQSPGPRGTASVPASRGRSQEAAGHGEKVLLPLKETSVEGFLRAATPRLAKLQVPREQLLEVLEQIHSGSCGTLYHATMTTKDHPKPKSVVLKALEDPVGLQEVQDFIGRIQFYQYLGKHKNLVQLEGCCTERLPLYMMLEDVVPGDLLSFLWTCRRDVMTMDGLLYDLTEKQIYHIGKQILLALEFLQEKHLFHGDVAARNILIQSDLTPKLCHLGLAYEVHAHGAISSARSSTIPLKWLAPERLLLRPASIRGDIWSFG... | Function: Probable tyrosine protein-kinase, which has strong transforming capabilities on a variety of cell lines including NIH 3T3 fibroblasts and on athymic nude mice. When overexpressed, it can also induce tumor cell invasion as well as metastasis in distant organs. May act by activating both MAP kinase and phosphat... |
P13895 | MASLRRLTELLCLPVTATAADIKTAYRRTALKYHPDKGGDEEKMKELNTLMEEFRETEGLRADETLEDSDPEPEESGYATFENVSVPDIDGAFFKLMKLKKCMQTYFSVNERRKQDIRPEYFELFKAFQDVPWKVLEDFFTSEMF | Function: Promotes efficient viral genome replication by accelerating both G1 and S phase progression of the cell cycle.
Sequence Mass (Da): 16988
Sequence Length: 145
Domain: The common region of ST and LT proteins comprises the J domain. This domain is essential for multiple viral activities, including virion assembl... |
P24852 | MELTSEEYEELRGLLGTPDIGNADTLKKAFLKACKVHHPDKGGNEEAMKRLLYLYNKAKIAASATTSQVWYFLIIGYISLKNKNIYLPKIFWLRFQNMAPHSGNSGGKNSIKALMSKICIVMRN | Function: Promotes efficient viral genome replication by accelerating both G1 and S phase progression of the cell cycle.
Sequence Mass (Da): 14011
Sequence Length: 124
Domain: The common region of ST and LT proteins comprises the J domain. This domain is essential for multiple viral activities, including virion assembl... |
P03080 | MDRILTKEEKQALISLLDLEPQYWGDYGRMQKCYKKKCLQLHPDKGGNEELMQQLNTLWTKLKDGLYRVRLLLGPSQVRRLGKDQWNLSLQQTFSGTYFRRLCRLPITCLRNKGISTCNCILCLLRKQHFLLKKSWRVPCLVLGECYCIDCFALWFGLPVTNMLVPLYAQFLAPIPVDWLDLNVHEVYNPASGP | Function: Promotes efficient viral genome replication by accelerating both G1 and S phase progression of the cell cycle. Inhibits host PP2A by binding to the A subunit, thereby displacing lower affinity regulatory B subunit. Inactivation of PP2A in turn results in the transactivation of cyclin A and cyclin D1 promoters... |
Q6EZC2 | MLKILWTYILFLLFISASARAEKPWYFDAIGLTETTMSLTDKNTPVVVSVVDSGVAFIGGLSDSEFAKFSFTQDGSPFPVKKSEALYIHGTAMASLIASRYGIYGVYPHALISSRRVIPDGVQDSWIRAIESIMSNVFLAPGEEKIINISGGQKGVASASVWTELLSRMGRNNDRLIVAAVGNDGADIRKLSAQQRIWPAAYHPVSSVNKKQDPVIRVAALAQYRKGETPVLHGGGITGSRFGNNWVDIAAPGQNITFLRPDAKTGTGSGTSEATAIVSGVLAAMTSCNPRATATELKRTLLESADKYPSLVDKVTEGRV... | Function: Protease subunit of subtilase cytotoxin SubAB5 . An endoprotease specific for host endoplasmic reticulum (ER) chaperone BiP/HSPA5, has no activity on human HSP70 or HSPA8 . Cleaves between 'Leu-416' and 'Leu-417' of BiP/HSPA5 in the hinge between BiP's ATPase and protein-binding domains . This induces host ER... |
Q6EZC3 | MTIKRFFVCAGIMGCLSLNPAMAEWTGDARDGMFSGVVITQFHTGQIDNKPYFCIEGKQSAGSSISACSMKNSSVWGASFSTLYNQALYFYTTGQPVRIYYKPGVWTYPPFVKALTSNALVGLSTCTTSTECFGPDRKKNS | Function: Receptor-binding subunit of subtilase cytotoxin SubAB5. Required for receptor-binding and thus correct trafficking in the host cell . Has specificity for host glycans terminating in the sialic acid N-glycolyl-alpha-neuraminic acid (Neu5Gc); each subunit in the SubB pentamer binds one Neu5Gc . The protease sub... |
P29599 | AQSVPWGISRVQAPAAHNRGLTGSGVKVAVLDTGISTHPDLNIRGGASFVPGEPSTQDGNGHGTHVAGTIAALNNSIGVLGVAPSAELYAVKVLGADGRGAISSIAQGLEWAGNNGMHVANLSLGSPSPSATLEQAVNSATSRGVLVVAASGNSGASSISYPARYANAMAVGATDQNNNRASFSQYGAGLDIVAPGVNVQSTYPGSTYASLNGTSMATPHVAGAAALVKQKNPSWSNVQIRNHLKNTATSLGSTNLYGSGLVNAEAATR | Cofactor: Binds 2 calcium ions per subunit.
Function: Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides.
Catalytic Activity: Hydrolysis of proteins with broad specificity for peptide bonds, and a preference for a large uncharged residue in P1. Hydrolyzes... |
A0A0B2XGM8 | MPTSANKVETAWSALLAGAAETRQEHLAPSPLFILRQTLFCVLAAYLFCGAGMVWNDWIDRDIDANVARTKNRPLASGKVTTAQAFVWMALQVIASCAVLHVMLDGKDV | Function: Polyprenyl transferase; part of the gene cluster that mediates the biosynthesis of the immunosuppressants subglutinols, meroterpenoids consisting of an alpha-pyrone (4-hydroxy-5,6-dimethyl-2-pyrone) moiety attached to a decalin core fused to a five-membered cyclic ether carrying a prenylside chain . The first... |
E9F5E9 | MSPSAPNTNELNSPVLETQPLAGDAALLHSSIAAGYEEIIRAPFDYLLNLPGKDVRSKMISAFNEWLCIPADKLEVIKRIVMLLHNASLLIDDIQDSSKLRRGLPVSHHIFGVPQTINAANYAYFLAQQELPKLGDPKAFEIYTEELLSLHRGQGMDIYWREASKCPTEEEYFSMVSHKTGGLFRLAIRLMQLASDKNWFVFHTRDFVPLVNVLGVIFQIRDDYLNLQSHAYTVNKGFGEDLTEGKYSFPIIHSIRSDPTNIQLSSILKQRTTDVDVKLFAVECIKATGSFEHCKEKIAELVAEARQLIKEMGNSVPGSA... | Cofactor: Binds 3 Mg(2+) ions per subunit.
Function: Geranylgeranyl pyrophosphate synthase; part of the gene cluster that mediates the biosynthesis of the immunosuppressants subglutinols, meroterpenoids consisting of an alpha-pyrone (4-hydroxy-5,6-dimethyl-2-pyrone) moiety attached to a decalin core fused to a five-mem... |
P16396 | MKNMSCKLVVSVTLFFSFLTIGPLAHAQNSSEKEVIVVYKNKAGKETILDSDADVEQQYKHLPAVAVTADQETVKELKQDPDILYVENNVSFTAADSTDFKVLSDGTDTSDNFEQWNLEPIQVKQAWKAGLTGKNIKIAVIDSGISPHDDLSIAGGYSAVSYTSSYKDDNGHGTHVAGIIGAKHNGYGIDGIAPEAQIYAVKALDQNGSGDLQSLLQGIDWSIANRMDIVNMSLGTTSDSKILHDAVNKAYEQGVLLVAASGNDGNGKPVNYPAAYSSVVAVSATNEKNQLASFSTTGDEVEFSAPGTNITSTYLNQYYA... | Function: Serine protease . Involved in the production of the competence and sporulation stimulating factor CSF . In addition, is essential for swarming motility . Plays a key role in DegU-mediated swarming motility . The protease activity is dispensable for swarming . Not essential for growth or sporulation .
PTM: May... |
E9F5F0 | MSQRQFKVIIIGGSVTGLTLAHSLHKIGIDYVVLEKRDTVTPQEGASIGILPNGARILDQLGLYEAIEDEAPPLGATRIHFPDGFAFTSLYPKKILENFGYPIAFLERRQLLRILYDALPDKTRIHVNKTMSTIEHFTKDEITGARVLTKEGDVYEGDLIVGADGIHSQTRGEIWRRINSSKSEFEPAECIDKCILIEYSCCFGISKCVTGLIAGEQVMHMRNGRTLVVIPSKDEVVFWFLVEKLDRKYTYSEAPRFTIDDATALCSQVFTLPIGNGIKFEDVWNKREVVNMLSLEESCLSTWSTGRLVCIGDSIHKVSI... | Function: FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of the immunosuppressants subglutinols, meroterpenoids consisting of an alpha-pyrone (4-hydroxy-5,6-dimethyl-2-pyrone) moiety attached to a decalin core fused to a five-membered cyclic ether carrying a prenylside chain . The ... |
E9F5F1 | MTRLSLQIIAGLAGQAWLVNSDTPSHDAFASCLSDASVPIATKGTPEWTQHTTPFNTRLQYEPIAVAVPTEISQIAAAVTCAKTNGIPVTAKSGGHSFTSLGLGGEDGHLVIQLDRMYNVELAQNGTAMIQAGARLGHVAVELYNQGKRALSHGYCPAVGVGGHAAHGGYGMVSRKYGLTLDWMKDATVVLHNGTIVYCSESEHSDLFWAIRGAGSSFGIVAEYGFETFPAPEKVTNFGIVLDWNPETAPAGLLAFQDFAQTMPSELSCQIDVRSTGYTLNGSYVGNEASLREALVPLLGKIGGHLEVHEGNWLEYVKFW... | Function: FAD-linked oxidoreductase; part of the gene cluster that mediates the biosynthesis of the immunosuppressants subglutinols, meroterpenoids consisting of an alpha-pyrone (4-hydroxy-5,6-dimethyl-2-pyrone) moiety attached to a decalin core fused to a five-membered cyclic ether carrying a prenylside chain . The fi... |
A0LZD4 | MNIHEYQGKEILNSFGVRIQRGTVARNAKEAVEAAKELTEKTGTGWHVIKAQVHAGGRGKGGGVKLAKNLKEVEEIAGEIIGMNLVTPQTSAEGKKVHQVLVTEDVYYPGDNEPEEYYMSVLLNRATGRNMIMYSTEGGMDIETVAEETPELIFTEEIDPATGLLGFQARRIAFNLGLSGKGFKEMTKFVMSLYEAFEKSDSSLFEINPVLKTSDDLIMAVDAKVTLDDNALFRHKDYAEMRDVREENATEVEAREVGLNYVDLDGNVGCMVNGAGLAMATMDLIKQAGGEPANFLDVGGTADAKRVEEAFRLILKDDKV... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specif... |
P53592 | MNLHEYQSKHLLKKYNIPVPASEVVFNPDAAVDAAAKIGGDRWVVKAQVHAGGRGKAGGVRLVKNKEELKSAVKALLGTRLVTYQTDERGQPVNQILVEQTSDIARELYLGAVIDRASQRIVFMASTEGGVEIEKVAEKSPEKILKVTIDPAIGLQPFQCRQLFFGLGLQDLKQMRSFTDIVMGLYRLFTERDLSLLEINPLVITGSGELICLDAKINIDDSALYRQSELREMRDTTQEDEHETMAQQWELNYIKLDGNIGCMVNGAGLAMATMDLIKLSGGDPANFLDVGGSATKERVTEAFKIIVSDKNVKGILVNIF... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specif... |
Q883Z4 | MNLHEYQGKQLFAEYGLPVSKGYAVDTPEAAAEACDKIGGTEWVVKAQVHAGGRGKAGGVKLVRSKEDAAAFAQQWLGKRLVTYQTDANGQPVTKILVESCTDIAKELYLGAVVDRSSRRIVFMASTEGGVDIEKIAHDTPEKILKATIDPLVGAQPFQGRDLAFQLGLEGKQVTQFAKIFTGLAKLFQDHDLALLEVNPLVIKADGDLHCLDAKINIDANAMYRQPKLKGFHDPSQDDPREAHAAKFELNYVALEGNIGCMVNGAGLAMGTMDIVNLHGGKPANFLDVGGGATKERVTEAFKIILSDTNVAAVLVNIFG... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specif... |
Q8ZVF3 | MKLHEYEAKELFSKYGVKIPPGKVALTPEEVLKIAREIGAPVVLKAQVVVAGRGKAGGIKVANSPEEAYELSKRMFGMNIKGLIVKKLYVTKFVEVEREMYLSLIIDRASRRYLFLASPVGGMDIEEIAKTSPEKIKRVYVDPATGLRDYHVRSIVSWLGFKQGTSQWQQAASIVQAMYRIMVDYDAELVESNPLAVTKEGEVIPLDARVIVDDNALFKHPELEKALEEDPRDVTEFEAYAKKIGFHYVELDGDVGIIGNGAGLTMATMDLVYHFGGRPANFLDIGGGASREVVKEAVKVLLHHPRVKVIFVNIFGGITR... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specif... |
Q84W65 | MAAAMSSSCCASSLRLIPFKRTLFSSIHYPAKTLLLRPLKPSEVPSFRRTIITFQKISTGIVPPPSASSSPSSYGDLQPIEELPPKLQEIVKLFQSVQEPKAKYEQLMFYGKNLTPLDSQFKTRENKVEGCVSQVWVRAFFDEERNVVYEADSDSVLTKGLAALLVKGLSGRPVPEILRITPDFAVLLGLQQSLSPSRNNGLLNMLKLMQKKALHLEVKGEEDSSSGESSESSFVSIPETKDEANVPEVDLESKPDLVEDLGTEKIDDSESGSNVVALGSRGMRIREKLEKELDPVELEVEDVSYQHAGHAAVRGSAGDD... | Function: Participates in cysteine desulfurization mediated by NFS2 in chloroplast and NIFS1 in mitochondrion . Activates the cysteine desulfurase activity of NFS2 . Cysteine desulfurization mobilizes sulfur from L-cysteine to yield L-alanine and supplies the inorganic sulfur for iron-sulfur (Fe-S) cluster formation. G... |
Q9FXE3 | MNTSSSFKALASPPLISTSRPTTKSFPNPRFTSRFSPKPITCMRDSLNLGSNPKAPSPFSLATVSVDAPLGTKTSDKLRILVSEFRSLTEPIDRVKRLLNYAATLAPLDESARISENRVTGCTTQVWLEIKMDEFGRMRFKADSDSEISKGFCSCLIWILDGAKPEEVMGVRSEDLSEMNVGVHGKEQSRVNTWHNVLMSMQKRTMTLVATDVAHQRGQRPPHQHDLLFKYVNGSYMESSKVHDYSISLLPLYYDFII | Function: Participates in cysteine desulfurization mediated by NFS2. Can activate the cysteine desulfurase activity of NFS2 in vitro. Cysteine desulfurization mobilizes sulfur from L-cysteine to yield L-alanine and supplies the inorganic sulfur for iron-sulfur (Fe-S) cluster formation.
Sequence Mass (Da): 28968
Sequenc... |
Q9EXP1 | MAQLPDPQKLLRNFSRCSNWEEKYLYIIELGAGLAPLSDAQRQDGNRVSGCQSQVWIDLASNEQGNVVLHGDSDAAIVKGLIAIVFSLYQGLSVREIVELDVRPFFASLALTQHLTPSRSQGLEAMLRAVRARASALI | Function: Participates in cysteine desulfuration mediated by SufS. Cysteine desulfuration mobilizes sulfur from L-cysteine to yield L-alanine and constitutes an essential step in sulfur metabolism for biosynthesis of a variety of sulfur-containing biomolecules. Functions as a sulfur acceptor for SufS, by mediating the ... |
P56729 | MARKKFSGLEIXLIVLFAIVLSIAIALVVVXASKXPAVIKLPSDPIPTLRMEMTYHTDYMLE | Function: Plays an important role in the final stage of carbohydrate digestion. Isomaltase activity is specific for both alpha-1,4- and alpha-1,6-oligosaccharides (By similarity).
PTM: The precursor is proteolytically cleaved when exposed to pancreatic proteases in the intestinal lumen.
Location Topology: Single-pass t... |
Q223E5 | MNHRLVALSVASLALLAPLTVPAQGLRPSSATVGAGVLAPARVPAATGLAADYIVAVVNSEPITNNEVRAALQRVLQQLAQQGNPQVDSKTLVRQVLERLINEKAQLQLARESGIAADEAAIDQAEQNIARQNQLTVAELRRRLTQEGGVPGQFRNQLRDQILLTRLREREVEPRARVSELEIDQFLREQQSSTPAVQQINLAQVLVSVPDTATPVQVTALQARAQRALARARAGEDFVTLVREFSDASDKASLANGGELGLRTADRYPPLFLEATHNLAVGEISALVRSGAGFHILKVLEKKSAALPAMTVTQSRARHI... | Function: Chaperone involved in the correct folding and assembly of outer membrane proteins. Recognizes specific patterns of aromatic residues and the orientation of their side chains, which are found more frequently in integral outer membrane proteins. May act in both early periplasmic and late outer membrane-associat... |
Q0VMV4 | MINKTLHTKHTLLGLLAMAVLMIPVWSQAKVQMLDRIVAVVNDGAIMASELDERINTIALQFQEKGQQLPSPAILREQVLDRMILERLQLQLAERAGIKVDEASLNEALAGIARQNDMSLEDFAATLREDGYSWTQFREQIRQDMVISRLQQRSVASRIQITDREVDRFLSSELGKQMFQEDFRLGHILIRVPSEARPQQISQARAKAKEIIERLEAGSDFQQLAIALSDGPNALEGGDLGWRPAAQWPTLFAENAINLKKGEFSQPLRSGAGFHILKMIDRKGGAEKVVTQYHVRHVLIKADALTSAEQAQQRAIRLHD... | Function: Chaperone involved in the correct folding and assembly of outer membrane proteins. Recognizes specific patterns of aromatic residues and the orientation of their side chains, which are found more frequently in integral outer membrane proteins. May act in both early periplasmic and late outer membrane-associat... |
Q0AC82 | MTAITRITLTGALLAAALLLAALQPARAETLDRIVAVVDDQVVLASELERELATIANQLRSRGQRLPPRDVFQRQVLERLITQRVQLSRAQRVGITVDDATLDAAMQRMARQNNMTLGQFRQAVEQEGFEYNYFREGIREEIAISRLRQAQVEEQVTVTPQEVEEVLETLDDENQEYRLGHILVATPEAASTAQLEEARERIEQLREQIIAGETDFEGAATAFSDAASAMEGGDLGWRLHSQLPSLFAEAIDEGLQAGEVSGVLQNSSGFHLVKLMDQRTQGGERVTETRARHILIRTDGDVITDEDARLRLRSLLERIE... | Function: Chaperone involved in the correct folding and assembly of outer membrane proteins. Recognizes specific patterns of aromatic residues and the orientation of their side chains, which are found more frequently in integral outer membrane proteins. May act in both early periplasmic and late outer membrane-associat... |
Q5P7I9 | MRRISSRLSLVLFAALSCATALFPAHAANPRSVEVDHIAAVVNNEVITARELRERVEQAIHQLNRQGTPQPPADVLERQLLERLVLERAQLQLARETSLQVDEATLERAIARIAESNRLTIAQLQAALEKDGVSWSRFRDNIRTEILLTRLREREVDNRIVVTDAEVDNFLANNADALSGEEFELAHILIRVPEAATQQQMAGLVARAETAKQRLNSGDDFARVAASYSDAPDAMNGGALGWRSRDRLPPLFAEAVRELSPGSVSPVLRSSAGLHIVKLLDRRGGAAAGPQQLEQTRARHILIRTSEILNDSEAESRLLG... | Function: Chaperone involved in the correct folding and assembly of outer membrane proteins. Recognizes specific patterns of aromatic residues and the orientation of their side chains, which are found more frequently in integral outer membrane proteins. May act in both early periplasmic and late outer membrane-associat... |
Q493R5 | MKFWKIFILIFTLKTNIVLGALKTVDKIVALVNHNIILDSDIRHNIYMIQDNILNGNDNILQDISHYQKILDQLIIDNLIFQISDQQKINIDHTQLNQMINCILNLYDMTFDKFRAYLYDIGLNYEKFYFQQYQHMLKKQICDHVMHDRAHILTNEINKIVKKSNIIDINKQFKLRHITFSLPIQPTPSQIDRIEYFARLLIKKKEFNNNIKELIRTYSNKNIIQIIKVHETEWVSWKDIPIIFDKYLQTINKGDVIGPIISCDGIHIVEIQDIRYKQIMLPVTKVTAKIFGIQNSCENISIVEQLLQIKENMEKSNTAF... | Function: Chaperone involved in the correct folding and assembly of outer membrane proteins. Recognizes specific patterns of aromatic residues and the orientation of their side chains, which are found more frequently in integral outer membrane proteins. May act in both early periplasmic and late outer membrane-associat... |
Q7VU12 | MMRSLHSLRRMSGTVLALMLAAGLPLSAAQAQPAKPAPKGDQKPATPAPSEQFVDGIAAIVNKDVITLREVREASKLASADLQKRGIQVPDERTLQKQVLQRLIMERLERQEADRMGIRVDEAQVDQAINMIASRNKITPAAMRAEIEKSGVTWEQYRKSLRDDIRMDRLRQRAVDANIIISDAEVDAFLKDQERNPAAAQATRAPAPQQPQPQPRQPAQSGPAMLVLAQILVRVPEGSSPDQVAALRKKAEGLLARAKKGDDFASLAAANSDGPEALQGGMMGARPLDGWPDLFVKAAGSLSAGQVSGLVQSGNGFHIL... | Function: Chaperone involved in the correct folding and assembly of outer membrane proteins. Recognizes specific patterns of aromatic residues and the orientation of their side chains, which are found more frequently in integral outer membrane proteins. May act in both early periplasmic and late outer membrane-associat... |
P57240 | MKICIFIFFYIFSSIFYVLAKNNQVDNITAIVNDEIILNSDVNEILVFLKKSKKKFIIPLKSDFLKEKVLEKLIVDSLILQEANSKNINITKEQIDTVIKNIALKKHISVDHFKKQILLRNIKNPSYYDNFIKKIEILLKMKTIQDYELHKRINISEQEVNTIFKKLIKDNEKFKKINLSYILLPSLKQDSDNAVRNRTKIAENIVYKLKKGYDFEKLLIECEKNKSTFIVKKMFWKPLLDIQNSFFKTLNIFKKGQILGPIVGDKGLYILKVNDIHHKKENIVTEFYMQHCLIKPSVILTNTEAKKKIFNIYENIKKGI... | Function: Chaperone involved in the correct folding and assembly of outer membrane proteins. Recognizes specific patterns of aromatic residues and the orientation of their side chains, which are found more frequently in integral outer membrane proteins. May act in both early periplasmic and late outer membrane-associat... |
Q8KA01 | MKVYFFLILYVFLSFFSITYSKELEIDKIIAIVNNQIILNSDVNQVLFSLKEEDQRVKIPLKINFLRNKIIKKLITETLILEEAKKFNIVVTDDQVNNVLSKYALKKNITIEELKRNILMNNTNTSFSYNDYFNKIKNSLKVKIIQDYVLHNRVHISEKEVDLFLNKLINTQNELKKIDINCIFLPFIKEKNKIFIKNTKILADHFAKKIKKDASFNYYYEYFKKNNNIFLSKEIRSKSLKYLKKIFLNKLKIIKKNQILGPILGLKGFYILKINKIENENKENLTTEFHIQHCLIRPSVILDDKQAKNSIYYIYNNIKN... | Function: Chaperone involved in the correct folding and assembly of outer membrane proteins. Recognizes specific patterns of aromatic residues and the orientation of their side chains, which are found more frequently in integral outer membrane proteins. May act in both early periplasmic and late outer membrane-associat... |
Q8A0L8 | MESKKPLILVSNDDGVMAKGISELVKFLRPLGEIVVMAPDSPRSGSGSALTVTHPVHYQLVKREVGLTVYKCTGTPTDCIKLALGSVLDRKPDLIVGGINHGDNSAINVHYSGTMGVVIEGCLKGIPSIGFSLCNHRPDADFEPSGPYIRKIAAMILEKGLPPLTCLNVNFPDTPNLKGVKVCEQAKGCWVNEWVTCPRLDDHNYFWLTGSFTDHELENENNDHWALENGYVAITPTTVDMTAYGFIDELNGYCQQLEF | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates.
Catalytic Activity: a ribonucleoside 5'-phosphate + H2O = a ribonucleoside + phosphate
Sequence Mass (Da): 28365
Sequence Length: 259
Subcellular Location: Cytoplasm
EC: 3.1.3.5
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Q7VXN2 | MRILVSNDDGYNAPGLEALVEALSGLGELTVVAPETNHSGASNSLTLNRPLTVRTAANGFIYVNGTPSDCVHVALTGLMDARPDLVVSGINNGANMGDDTLYSGTVAAASEGYLFGIPSIAFSLIEKGWQHIESAARAARQVVERQIAQPLAAPVLLNVNIPNRRYEDMKGYAVTRLGKRHPSEPVVRTTTPYGDTVYWVGPVGLAADATPGTDFHATAQGQVSVTPLRLDLTQHSQLDDVRNWAEPLCVNA | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates.
Catalytic Activity: a ribonucleoside 5'-phosphate + H2O = a ribonucleoside + phosphate
Sequence Mass (Da): 26787
Sequence Length: 252
Subcellular Location: Cytoplasm
EC: 3.1.3.5
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Q89L02 | MRILCTNDDGIHAPGLKVVEEIARALSDDVWVVAPELDQSGVSHSLSLNDPLRLREVGPRHFAVRGTPTDCVIMGARHILGTKPPDLVLSGVNKGRNVAEDVVYSGTIAGALEGTILGLPSFALSQEFSVETRERPPWDTARTFGPDILRKVMAAGIPKETVINVNFPSCAPEDVLGIRVTRQGKRNLGFLRIDERRDGRNNPYFWIGFERAAMMDTPAEGTDLAALRERYVSVTPLRLDRTNEAFSEALGAALK | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates.
Catalytic Activity: a ribonucleoside 5'-phosphate + H2O = a ribonucleoside + phosphate
Sequence Mass (Da): 27898
Sequence Length: 255
Subcellular Location: Cytoplasm
EC: 3.1.3.5
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C0ZGV3 | MRILVTNDDGIDALGIKRLVEALLTLEGAEVSIVAPVEEKSGVGHGITYRSALSPEQRDFYGMPVKAWAVNGNPADCVKAAYHLLFEHGKKPDIVFSGINVGTNLGRDIYYSGTCSGAREAVILGVPGVALSYDNWFDQDNYGDVVEMIRPLVKEFSDRAIKGELASEVFWNINIPHVPLAEVKGMVPATLSMNHYEDKYSEEAEGYYLAREYPQVMPLAEPLDYDLLKHGYIAITPVHIDATDRTLLKQMDNWALLKAWGKQEE | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates.
Catalytic Activity: a ribonucleoside 5'-phosphate + H2O = a ribonucleoside + phosphate
Sequence Mass (Da): 29431
Sequence Length: 265
Subcellular Location: Cytoplasm
EC: 3.1.3.5
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Q2FLE8 | MISGSPPDSTPSHHHFSLKRPCILLTNDDGVNSEGLWAAYDALFEWADVVVCAPATQQSAVGRSLSIFEPLRVNTVSRGDITAYAVGGKPTDSVILALFALGVKPDLVVSGINIGENLSYEAITTSGTVGAALEAANHGYPAVAFSLQIEDQKEKFDDARHLADRFSESKGVVRDVIRRILEKGFPSFTHVMNVNIPSIITGGYEITHLAEHLFITGVEKRLDPRGKPYYWINGPLVTDAPEGTDVHAIHKGNISITPITLDCTAYAGTDDLRRLFSLE | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates.
Catalytic Activity: a ribonucleoside 5'-phosphate + H2O = a ribonucleoside + phosphate
Sequence Mass (Da): 30199
Sequence Length: 279
Subcellular Location: Cytoplasm
EC: 3.1.3.5
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Q57979 | MEILIVNDDGIYSPSLIALYNALKEKFSDANITIVAPTNQQSGIGRAISLFEPLRMTKVKLAKDIVGYAVSGTPTDCVILGIYQILKKVPDLVISGINIGENLGTEIMTSGTLGAAFEAAHHGAKSIASSLQITSDHLKFKELDIPINFEIPAKITAKIAEKYLDYDMPCDVLNINIPENATLETPIEITRLARKMYTTHVEERIDPRGRSYYWIDGYPIFEEEEDTDVYVLRKKRHISITPLTLDTTIKNLDEFKEKYGKILCEM | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates.
Catalytic Activity: a ribonucleoside 5'-phosphate + H2O = a ribonucleoside + phosphate
Sequence Mass (Da): 29771
Sequence Length: 266
Subcellular Location: Cytoplasm
EC: 3.1.3.5
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Q8TY72 | MRILITNDDGIASPGLRAAVRACRSVGEVTVVAPATQQSGVGRSISLLEPVRVEEIEVEGVDALAISGTPADAVLIGAFSIMDEPPDLVVSGINLGENVSADVTTSGTVGAALEAYGNGIPAIAISQEVRDARARVDNNAKNVDFTLAIRVLKALLEAIRGANWEGVLNVNVPDPDRWNGEIKVVPLAFTMYRPRIEKRYDPRGRRYYWIDGEIIQDPPEGTDLYELQRGSIVITPLTTDVTGDLDAAENVIKELRRALRG | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates.
Catalytic Activity: a ribonucleoside 5'-phosphate + H2O = a ribonucleoside + phosphate
Sequence Mass (Da): 28082
Sequence Length: 261
Subcellular Location: Cytoplasm
EC: 3.1.3.5
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A2SF75 | MRILVANDDGYLAPGLAALVEACRGLGELDVVAPEQNSSGTSNALTLQRPLSVWTAANGYRYLNGTPSDCVHVALTGLLPQRPDLVVSGINNGANMGDDTLYSGTVAAAMEGYLFGIPSIAFSLSEKGWTHLDTAARVARRLIEQVIALPPVPGAWLLNVNIPDRPYEDLRGLRTTRLGRRHASEPVIRQSNPRGEPIYWIGAAGDAREAGAGTDFHAVAQGHVSVTPLQVDLTDHTCLPAWGSWLERAGEGGR | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates.
Catalytic Activity: a ribonucleoside 5'-phosphate + H2O = a ribonucleoside + phosphate
Sequence Mass (Da): 27067
Sequence Length: 254
Subcellular Location: Cytoplasm
EC: 3.1.3.5
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A5UMJ5 | MKALISNDDGVNATGILAAKNAIEDLCEVCVVAPETQQSGIGHAITLYDPLRINPTTLRDKSQAYGVTGTPTDAVTFGLFEIMGEKPDIMISGINTGFNIGKAELTTSGTIGAALEAASFGIPSIAISQEVTRDYIKFENGTVDIDFSFAGKMLRKLVKIVFKKGLPDGIDLLNVNIPENPVDEEFEVAKLGNRMYTPIIQRRLDPRGKPYYWIGGDPYNSDCEGTDGHCLKKLNKATITPLTIDLTGEMDLIKEWLK | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates.
Catalytic Activity: a ribonucleoside 5'-phosphate + H2O = a ribonucleoside + phosphate
Sequence Mass (Da): 28044
Sequence Length: 258
Subcellular Location: Cytoplasm
EC: 3.1.3.5
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Q2NI97 | MNILITNDDGLTSNGIIAARNSVEDLGQTTLVAPLTQQSGVGHAITLMKPLRAIKTELSDKTYGYAVTGTPTDCVILAVKSIMDKKPDLIISGMNIGENLSRSITTSGTLGATFEAASFGIPAIAVSLQVNREDLKFRTGVNFIDYSHAESIVNKLAKKVIKHGMPEGVDILNLNIPANPDSDEIIQSNFADRMFSTDVEKRIDPYGHPYYWIVGDLIDDGIEGTDVHTLHILNQPAVTPISIDMDAQVNISKWLD | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates.
Catalytic Activity: a ribonucleoside 5'-phosphate + H2O = a ribonucleoside + phosphate
Sequence Mass (Da): 27750
Sequence Length: 256
Subcellular Location: Cytoplasm
EC: 3.1.3.5
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Q2S1H7 | MSSPASGDEPRILLCNDDGIHAPGIQSLASALDGLGELFVVAPTTEQSAVGHAITVRDPVRAHREEFEVPSGPIPAWGVTGTPADSVKLACHELLDAPPDLVVSGINQGPNTAVNVLYSGTVSAATEASILGLDSLAISLCEWSKPQFEVAGQWARRIVEWALDRGLPQGVLLNVNVPALSAEQIEGVALTRQARSRWEEGFERRTDPADRPYYWLAGTFVNLDDGPETDLSAIERGYVSVTPIQHDMTAHDAFEAFGTWDWDESAGPDGSE | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates.
Catalytic Activity: a ribonucleoside 5'-phosphate + H2O = a ribonucleoside + phosphate
Sequence Mass (Da): 29108
Sequence Length: 272
Subcellular Location: Cytoplasm
EC: 3.1.3.5
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P92946 | MQLSSLSHTSITHKDKKKKMGIELQNHQSHHEEASPAEEPMSRWLINTPEPPSMWQELIGYIRTNVLAKKKHKRNKTKNSSSNLVYSCLKSAFPILSWGRQYKLNLFKKDLMAGLTLASLCIPQSIGYANLAGLDPEYGLYTSVVPPLIYSTMGTSRELAIGPVAVVSLLLSSMVRDLQDPVTDPIAYRKIVFTVTFFAGAFQAIFGLFRLGFLVDFLSHAALVGFMAGAAIVIGLQQLKGLFGLTHFTNKTDVVSVLSSVFHSLHHPWQPLNFVIGSSFLIFILLARFIGKRNNKLFWIPAMAPLISVVLATLIVYLSN... | Function: Low-affinity H(+)/sulfate cotransporter that may be involved in the distribution of sulfate from vascular bundles to the palisade cells of the leaves. Plays a central role in the regulation of sulfate assimilation.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 74498
Sequence Length: 677
S... |
Q0ILJ3 | MPRRPSGGGGGAGPAAAAVRKVPLRKLLRAASVACGVQFGWALQLSLLTPYVQELGIPHAFASLVWLCGPLSGLLVQPLVGHLSDRIAPAASPLGRRRPFIAAGAASIAAAVLTVGFSADLGRIFGDSITPGSTRLGAIIVYLVGFWLLDVGNNATQGPCRAFLADLTENDPRRTRIANAYFSLFMALGNILGYATGAYSGWYKIFPFTVTPSCSISCANLKSAFLLDIIILVVTTCITVASVQEPQSFGSDEADHPSTEQEAFLWELFGSFRYFTLPVWMVLIVTALTWIGWFPFILFDTDWMGREIYRGSPDDPSITQ... | Function: Responsible for the transport of sucrose into the cell, with the concomitant uptake of protons (symport system). May also transport other glucosides (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 53215
Sequence Length: 501
Pathway: Glycan biosynthesis; sucrose metabolism.
... |
Q9SV13 | MGTEDYTFPQGAEELHRRHHTVEAPQPQPFLKSLQYSVKETLFPDDPFRQFKNQNASRKFVLGLKYFLPIFEWAPRYNLKFFKSDLIAGITIASLAIPQGISYAKLANLPPILGLYSSFVPPLVYAVLGSSRDLAVGTVAVASLLTGAMLSKEVDAEKDPKLYLHLAFTATFFAGVLEASLGIFRLGFIVDFLSHATIVGFMGGAATVVSLQQLKGIFGLKHFTDSTDVISVMRSVFSQTHEWRWESGVLGCGFLFFLLSTRYFSIKKPKFFWVAAMAPLTSVILGSLLVYFTHAERHGVQVIGDLKKGLNPLSGSDLIF... | Function: H(+)/sulfate cotransporter that may play a role in the regulation of sulfate assimilation.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 72748
Sequence Length: 658
Subcellular Location: Membrane
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O04289 | MSSKRASQYHQVEIPPPQPFLKSLKNTLNEILFADDPFRRIRNESKTSKKIELGLRHVFPILEWARGYSLEYLKSDVISGITIASLAIPQGISYAQLANLPPILGLYSSLVPPLVYAIMGSSRDLAVGTVAVASLLTAAMLGKEVNAVVNPKLYLHLAFTATFFAGLMQTCLGLLRLGFVVEILSHAAIVGFMGGAATVVCLQQLKGLLGLHHFTHSTDIVTVLRSIFSQSHMWRWESGVLGCCFLIFLLTTKYISKKRPKLFWISAMSPLVSVIFGTIFLYFLHDQFHGIQFIGELKKGINPPSITHLVFTPPYVMLAL... | Function: H(+)/sulfate cotransporter that may play a role in the regulation of sulfate assimilation.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 71270
Sequence Length: 646
Subcellular Location: Membrane
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Q9SXS2 | MEVHKVVAPPHKSTVAKLKTKLKETFFPDDPLRQFRGQPNRTKLIRAAQYIFPILQWCPEYSFSLLKSDVVSGLTIASLAIPQGISYAKLANLPPIVGLYSSFVPPLVYAVLGSSRDLAVGPVSIASLILGSMLRQQVSPVDDPVLFLQLAFSSTFFAGLFQASLGILRLGFIIDFLSKATLIGFMGGAAIIVSLQQLKGLLGITHFTKHMSVVPVLSSVFQHTNEWSWQTIVMGVCFLLFLLSTRHLSMKKPKLFWVSAGAPLLSVIVSTLLVFVFRAERHGISVIGKLPEGLNPPSWNMLQFHGSHLALVAKTGLVTG... | Function: H(+)/sulfate cotransporter that may play a role in the regulation of sulfate assimilation.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 69070
Sequence Length: 631
Subcellular Location: Membrane
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Q9LW86 | MGHGTNRVEDMASPNNGTAGETVVEIHSVCLPPKKTAFQKLKKRVGDVFFPDDPLQRFRNQTWRNRVILGLQSLFPIFTWGSQYDLKLLRSDVISGLTIASLAIPQGISYAKLANLPPIVGLYSSFVPPLIYAVLGSSRHLAVGPVSIASLVMGSMLSESVSPTQDSILYLKLAFTSTFFAGVFQASLGLLRLGFMIDFLSKATLIGFTAGAAVIVSLQQLKGLLGIVHFTGKMQIVPVMSSVFNHRSEWSWETIVMGIGFLSILLTTRHISMRKPKLFWISAASPLASVIISTLLVYLIRSKTHAISFIGHLPKGLNPP... | Function: H(+)/sulfate cotransporter that may play a role in the regulation of sulfate assimilation.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 71177
Sequence Length: 653
Subcellular Location: Membrane
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Q94LW6 | MENTITSSTSSPKGRGVNFSTPRGFGSKFKSKCKETFFPDDPFKPISQEPNRLLKTKKLLEYFVPIFEWLPKYDMQKLKYDVLAGITITSLAVPQGISYAKLASIPPIIGLYSSFVPPFVYAVFGSSNNLAVGTVAACSLLIAETFGEEMIKNEPELYLHLIFTATLITGLFQFAMGFLRLGILVDFLSHSTITGFMGGTAIIILLQQLKGIFGLVHFTHKTDVVSVLHSILDNRAEWKWQSTLAGVCFLVFLQSTRYIKQRYPKLFWVSAMGPMVVVVVGCVVAYLVKGTAHGIATVGPLKKGLNPPSIQLLNFDSKYL... | Function: H(+)/sulfate cotransporter that may play a role in the regulation of sulfate assimilation.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 70360
Sequence Length: 634
Subcellular Location: Membrane
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P53393 | MSSLGTEQFSERSQWVLNSPNPPPLTKKFLGPLKDNKFFTSSSSKKETRAVSFLASLFPILSWIRTYSATKFKDDLLSGLTLASLSIPQSIGYANLAKLDPQYGLYTSVIPPVIYALMGSSREIAIGPVAVVSMLLSSLVPKVIDPDAHPNDYRNLVFTVTLFAGIFQTAFGVLRLGFLVDFLSHAALVGFMAGAAIVIGLQQLKGLLGLTHFTTKTDAVAVLKSVYTSLHQQITSSENWSPLNFVIGCSFLIFLLAARFIGRRNKKFFWLPAIAPLLSVILSTLIVFLSKGDKHGVNIIKHVQGGLNPSSVHKLQLNGP... | Function: Low-affinity H(+)/sulfate cotransporter which may be involved in the internal transport of sulfate between cellular or subcellular compartments within the plant.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 69786
Sequence Length: 644
Subcellular Location: Membrane
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Q9FY46 | MSYASLSVKDLTSLVSRSGTGSSSSLKPPGQTRPVKVIPLQHPDTSNEARPPSIPFDDIFSGWTAKIKRMRLVDWIDTLFPCFRWIRTYRWSEYFKLDLMAGITVGIMLVPQAMSYAKLAGLPPIYGLYSSFVPVFVYAIFGSSRQLAIGPVALVSLLVSNALGGIADTNEELHIELAILLALLVGILECIMGLLRLGWLIRFISHSVISGFTSASAIVIGLSQIKYFLGYSIARSSKIVPIVESIIAGADKFQWPPFVMGSLILVILQVMKHVGKAKKELQFLRAAAPLTGIVLGTTIAKVFHPPSISLVGEIPQGLPT... | Function: H(+)/sulfate cotransporter that may play a role in the regulation of sulfate assimilation.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 75096
Sequence Length: 685
Subcellular Location: Plastid
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Q8GYH8 | MSLAVKDLSTASSSSSKAIPVKIIPLQYPDSTSSDPHCHSIPFNDFFSRWTAKIKRMTFFDWIDAIFPCFLWIRTYRWHQYFKLDLMAGITVGIMLVPQAMSYARLAGLQPIYGLYSSFVPVFVYAVFGSSRQLAVGPVALVSLLVSNALSGIVDPSEELYTELAILLALMVGIFESIMGFLRLGWLIRFISHSVISGFTTASAVVIGLSQLKYFLGYSVSRSSKIMPVIDSIIAGADQFKWPPFLLGCTILVILLVMKHVGKAKKELRFIRAAGPLTGLALGTIIAKVFHPPSITLVGDIPQGLPKFSFPKSFDHAKLL... | Function: H(+)/sulfate cotransporter that may play a role in the regulation of sulfate assimilation.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 74662
Sequence Length: 677
Subcellular Location: Membrane
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B8AF63 | MDSAAGGGGLTAIRLPYRHLRDAEMELVSLNGGTPRGGSPKDPDATHQQGPPAARTTTTRKLVLACMVAAGVQFGWALQLSLLTPYIQTLGIDHAMASFIWLCGPITGFVVQPCVGVWSDKCRSKYGRRRPFILAGCLMICFAVTLIGFSADLGYILGDTTEHCSTYKGSRFRAAIIFVLGFWMLDLANNTVQGPARALLADLSGPDQCNSANAIFCTWMAVGNVLGFSSGASGNWHKWFPFLMTRACCEACSNLKAAFLVAVVFLLFCMSVTLYFAEEIPLEPTDAQRLSDSAPLLNGSRDDNNASNEPRNGALPNGHT... | Function: Responsible for the transport of sucrose into the cell, with the concomitant uptake of protons (symport system). May also transport other glucosides (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 63484
Sequence Length: 595
Pathway: Glycan biosynthesis; sucrose metabolism.
... |
Q1MTR8 | MIVLNALSYLGIVLGFIGMTVSIASALYYISEFVEEHSRLAKAFLCRLVYFIMAVMVFLVIFDGFPFWLSAFSIFSHYIYKINFDTFPFFSFKRMRFLLACFLIVANHILWVRFFQVHEFPIKPRGLTYDFVGQRLLTSRASFSQVASFMGVCVWSVPIGIFVSFTAADNTLPTITTPSSSSPDAYSSGSSRRTSNVLRQAYKKLGIFVERSLTSLGLSDRSSERYV | Function: May play a role in retention of a subset of membrane proteins in the early Golgi compartments.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 25801
Sequence Length: 227
Subcellular Location: Golgi apparatus
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P38869 | MLLELISYAGTVSGFLFLTLSIASGLYYISELVEEHTEPTRRFLTRAIYGIILILILLLLLDGFPFKLTLFSIACYIVYYQNLKSFPFISLTSPTFLLSCVCVVLNHYFWFKYFNDTEVPPQFKFDPNYIPRRRASFAEVASFFGICVWFIPFALFVSLSAGDYVLPTTSEQHMAKKNDDITTNNQPKFRKRAVGLARVVINSVRKYIYSLARVFGYEIEPDFDRLAV | Function: Plays a role in retention of a subset of membrane proteins in the early Golgi compartments. Facilitates endoplasmic reticulum to Golgi transport of mannosyltransferases MNN2 and MNN5.
PTM: N-glycosylated.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 26284
Sequence Length: 228
Subcellular... |
Q8L960 | MASVAASSSISFAASFLKIKAFPLSPRFFPIRTLRCSVSSSSSEPIEFDISFAPPKPKPSSTHGGVTPQQLFIPWIVRSDDGTLKLQSQPPARLIHNLAIDATTQNPKKKDKSKKKQPQATSSSSATTTASSPASHSEVKPKLSKAARRFYNENFKEQPQRLSKVLAAAGVASRRTSEELIFDGKVTVNGILCNTPQTRVDPSRDIIYVNGNRIPKKLPPKVYFALNKPKGYICSSGEKEIKSAISLFDEYLSSWDKRNPGTPKPRLFTVGRLDVATTGLIVVTNDGDFAQKLSHPSSSLPKEYITTVVGDIHKRHLMAI... | Function: Responsible for synthesis of pseudouridine in chloroplastic 23S ribosomal RNA (Probable). Necessary for normal chloroplast rRNA processing and translation. Required for normal chloroplast development and maintenance. May function in other plastids, such as root amyloplasts .
Sequence Mass (Da): 45108
Sequence... |
F2Z472 | MKSIFFSLSLLLLLEKKAAGIELYAGGTKGHFLVKTSPLMFIGKNQFLYGHKEEQEEAPEESIFVQTKHHEYGQDADADMGGALSSQELTSLKEDIVCEEEDELAQQKSQLPSQSQIKSQTQVKSYAAQLKSQPGQLKTIGQVKSQTMLKSHGAPLKSFKARLNLREDIPQQVKGRGYGLAEDLAQVRQQPAKVHRLKGKHRQSRKTAAFYPQFRRRSRPYPRYFVQFQEQLQGSVHHTKSFYPGPGMCYCPRGGVILYQDAFTD | Function: Component of the copulatory plug.
PTM: Glycosylated.
Sequence Mass (Da): 29967
Sequence Length: 265
Subcellular Location: Secreted
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Q06677 | MSDPFAHLLTSLKNKDSASASKETTPQSSNSPSITGSAVADVARTDKSPNDSLHSISAPPLIPSPKVDFSAPPLVPTNSTTKSNTANNTPPSALANTDDDFNQLFGMGTVTTTDTIQKPDEDYYGSKEDHLYNGDDALVDEVKDMEIARLMSLGLSIEEATEFYENDVTYERYLEILKSKQKERNDLAIRKKESGIKMEKSGLSNIVGTDSNNLFSMATDFFNKGKKLVDQWTSFPPEANDRLNNYSKTHDKVEDYDLPQVNDSPNRILFEDNEVVENLPPADNPDQDLLTDFETKIDITKRTAPDVSHSSSPTSGILIE... | Function: Cofactor for the uncoating of clathrin-coated vesicles (CCVs) by Hsp70-type chaperones (SSA1/2/3 and SSB1/2). Coat disassembly is important for fusion of vesicles with target membranes and for recycling components of clathrin coats to the cytoplasm for further rounds of vesicle formation. Binds to assembled c... |
Q8SWI4 | MVRRSLYFLAVMGVVRSSSGLYIPSVVLQELGIASSQGCLMIAETNNGNFGIVSSGLENPVYITESPQGHREVSWQPVRGEDRAVPIYAPSAEEVRESISSVRGSEPGQYIAPQPTGFVPASTPVFGTIESASTAGAAVPVEGVFVASTENPASTGSSSTSTCPPKGTAGTTDNKGKAGGAAADDKSKSSSSSSSKKKKKGAKSLVALGAVATTALFSIVM | Function: Spore wall component.
Location Topology: Lipid-anchor
Sequence Mass (Da): 22506
Sequence Length: 221
Subcellular Location: Spore wall
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Q9UH65 | MGSLKEELLKAIWHAFTALDQDHSGKVSKSQLKVLSHNLCTVLKVPHDPVALEEHFRDDDEGPVSNQGYMPYLNRFILEKVQDNFDKIEFNRMCWTLCVKKNLTKNPLLITEEDAFKIWVIFNFLSEDKYPLIIVSEEIEYLLKKLTEAMGGGWQQEQFEHYKINFDDSKNGLSAWELIELIGNGQFSKGMDRQTVSMAINEVFNELILDVLKQGYMMKKGHRRKNWTERWFVLKPNIISYYVSEDLKDKKGDILLDENCCVESLPDKDGKKCLFLVKCFDKTFEISASDKKKKQEWIQAIHSTIHLLKLGSPPPHKEAR... | Function: Phosphatidylinositol 3,4,5-trisphosphate-dependent guanine nucleotide exchange factor (GEF) which, independently of RAS, transduces signals from tyrosine kinase receptors to RAC. It also mediates signaling of membrane ruffling. Regulates the actin cytoskeleton as an effector or adapter protein in response to ... |
B2UKT4 | MMTATEIRQSFLDFFREKQHTVVPSASLMPQSPGLLFTNAGMNQFVPYFLGVWTPPWTPARATDTQKCIRAGGKHNDLEDVGYDSYHHTFFEMLGNWSFGDYFKREAIRWAWELVVERWGFPAERLYATVYAPDKSKGDPGEFDREAWDFWAELFRSRGLDPDVHIVHGNVKDNFWMMGETGPCGPCSELHVDLTPEGNTKGSLVNKDSDQCIEIWNLVFIQYNAESDGSMRNLPACHVDTGMGFERACSIMQCTNGFKDFSRKPSNYATDVFRPLFDRLEVLSGRKYADVYPAPGSKRVDAEDGTLQEAIAFRVIADHL... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain.
Catal... |
Q0VNK2 | MKSAELRQAFLDYFASQGHTKVSSSSLVPANDPTLLFTNAGMNQFKDVFLGRESRDYTRATSSQRCVRAGGKHNDLENVGYTARHHTFFEMLGNFSFGDYFKREAIKFAWEFLTGTLGLPEERLWVTVHVSDDEAADIWLKEMGVSAERFSRLDEDNFWQMGDTGPCGPSSEIFYDHGADVPGGPPGSADEDLDRYIEIWNLVFMQYDRQPDGELQPLPKPSVDTGMGLERIAAVLQGVHSNYEIDLFQALLQAAAKATGCTDLEEKSLRVIADHIRSASFLICDGVIPSNEGRGYVLRRIIRRALRHGHKLGQDKPFFS... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain.
Catal... |
A6TQZ4 | MKKMGLNEIRKLFLDFYEEKEHYVQSSYPLVPHNDKSLLLINAGMAPLKNYFSGVETPPSKRMATCQKCIRTGDIENVGKTSRHATFFEMLGSFAFGDYFKTESIQWGWEFATKYLEMPEDKIWASVYEEDDEAYGIWENQIKMPKERIVRLGKEDNFWEIGVGPCGPCSELYFDRGDKYSCGHDDCKPGCDCDRFVEFWNHVFTQFDKDEAGNYNLLPNPNIDTGMGLERVACIMQDVDSIFEVDTMKHILNSVCTATNTQYNKDVKTNISLRIITDHLRSITFMIGDGILPSNEGRGYVLRRLLRRAARHGKLLGVSK... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain.
Catal... |
O67323 | MSLSAHEIRELFLSFFEKKGHTRVKSAPLVPENDPTLLFVNAGMVPFKNVFLGLEKRPYKRATSCQKCLRVSGKHNDLEQVGYTSRHHTFFEMLGNFSFGDYFKKEAIEYAWEFVTEVLKLPKEKLYVSVYKDDEEAYRIWNEHIGIPSERIWRLGEEDNFWQMGDVGPCGPSSEIYVDRGEEYEGDERYLEIWNLVFMQYNRDENGVLTPLPHPNIDTGMGLERIASVLQGKNSNFEIDIIFPLIQFGEEVSGKKYGEKFETDVALRVIADHLRAITFAISDGVIPSNEGRGYVIRRILRRAMRFGYKLGIENPFLYKG... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain.
Catal... |
P36428 | MRLVKAASLLISSTKPPSRVFYSSHLRRPFFSHFRFSSSSSTSSSVAVMPGSEPSETQWPAKRVRDTYVDFFRGKGHKFWPSSPVVPHNDPTLLFANAGMNQYKPIFLGTADPNTELSKLSRACNTQKCIRAGGKHNDLDDVGKDTYHHTFFEMLGNWSFGDYFKKEAIEWAWELLTKVYGLPTDRIYATYFGGDEKAGLQPDNEARDIWLKVLPSGRVLPFGCKDNFWEMGDTGPCGPCTEIHYDRIGNRDAASLVNNDDPTCLEIWNLVFIQFNRESDGSLKPLPAKHVDTGMGFERLTSVLQNKMSNYDTDVFMPIF... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged tRNA(Ala) via its editing domain.
Catalytic Activity: ATP + L... |
O28029 | MTLDEEYLDITFLTENGFVRKRCPKCGKHFWTADPEREICGDPPCESYSFIGNPVFKKPFELDEMREYYLNFFERRGHGRIERYPVVARWRTDIYLTIASIADFQPFVTSGVAPPPANPLTISQPCIRLDDLDSVGRTGRHLTLFEMMAHHAFNYPGKEIYWKNETVAYCTELLNELGVKKEDIVYKEEPWAGGGNAGPCLEAIVGGLEVATLVFMNLEEHPEGDIEIKGARYRKMDNYIVDTGYGLERFVWASKGTPTVYDAIFPEVVDTIIDNSNVSFNREDERVRRIVAESSKLAGIMGELRGERLNQLRKSVADTV... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Incorrectly charged aminoacyl-tRNA(Ala) is also edited in situ by the editing domain.
Cataly... |
B1GZ43 | MDKLSSKIRAEFLGFFKNSGCAVVPSDSLIPAGDKTLLFTSAGMVQFKQHFLGQSKDSFTRATSCQKCFRTSDIDQVGTTARHLTFFEMLGNFSFGDYFKKEAAAWAWEFLTKNMSLPKDKLYITIYKDDDEVAGIWKNIAPANKIIKMDEKTNFWNMGETGPCGPCSEILIDLGQETGCGSPACCPECNCDRYLEIWNLVFTQFDKQPDGSLKNLPRKNIDTGMGLERLSATVNGRKNVFDTDLFMPVMENAAEILKIKNEGSNISKLRMIADHSRAITFLISDGILPSNEGRGYVLRRILRRALRQGKFYGYNKPYIN... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain.
Catal... |
B0S104 | MKNYGLNEIRKKFLDYFGERGHLVIKSFPLIPQDDKSLLLINAGMAPLKKYFTGEKKLKKDRATSSQRCIRTADIDEVGKTQRHGTFFEMLGNFSFGDYFKREAITWAWDFLTNELEVPKDILWVSVYEEDEEAYNIWVNEVGISPERVVKLGKADNFWELDQGPCGPCSEIHVDRGFEFDPREDAKPGDEGERFLEVWNLVFTQFNKTADGKYERIAHPNIDTGMGLERITMVLENADNIFEIGLVKDIIKTIEEISGVKYKENHKNDVSIRIIADHVRAMTFLIYDGVIPSNEQRGYVLRRLIRRACRHGKLLGINDS... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain.
Catal... |
A6H0Y3 | MTSKEIRQQYLKFFESKGHLIVPSAPIVLKDDPTLMFNNSGMAQFKEYFLGNGTPKSPRIADTQKCLRVSGKHNDLEDVGFDTYHHTMFEMLGNWSFGDYFKKEAINWAWELLTEVYKIPKQNLYVSVFEGSKEDNVPFDQEAWDIWKGLIDEDRIILGNKKDNFWEMGDQGPCGPCSEIHVDLRTPEEKAQVSGKSLVNNDHPQVVEIWNNVFMEFNRKADGSLEKLPAQHVDTGMGFERLCMALQGKTSNYDTDVFTPLIEKVTQITGYKYTSNEVKNISEEQNKTNIAIRVIVDHVRAVAFAIADGQLPSNTGAGYV... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain.
Catal... |
Q0RF65 | MDTAEIRSRFLNHFARRGHTIVPSASLVAQDPTLLLVNAGMVPFKPYFLGDLATPWPRATSVQKVVRTVDIENVGRTARHASFFQMCGNFSFGDYFKAEAIPFAFELLVDGFGFKPDDLWATVYLDDDEAEGIWRELLPAERIQRRGKEDNFWSMGVPGPCGPCSEIYFDRGAAYGREGGPIADEERYLEVWNLVFMQYERGEGAGYDYPILRELPARNIDTGMGLERMATILQGVDNLYEIDISRPVLDLAGQLTGRRYGADPADDVRLRVVADHSRTAAMLIADGVVPSNEGRGYVLRRLLRRAVRDARLLGAREPVM... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain.
Catal... |
B0TZY8 | MISTKELRNKFISYFESKNHSHQPSSSLIPFGDDTLLFTNAGMVQFKDVFLGLEKRDFSRAVTVQKCLRAGGKHNDLDNVGYTARHHTFFEMLGNFSFGDYFKKDAISFAWEFLTKEIKLPVEKLWVTIYATDDEAFDVWHNHIGLPKERIIRIDSNDNFWSMGDTGPCGPCTEIFYDHGEDVAGGLPGTPDEDGDRYIEIWNIVFMQFNRHADGTVTDLPKPSVDTGMGLERIAAVLQDVHSNYDIDLFQALIKKAQEVTNADDINSPSLKVVADHIRSCAFLIADGVLPSNEGRGYVLRRIIRRAIRHGNKLGAKDIF... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain.
Catal... |
A9A565 | MDKKEILKEFSADPDKYYNVKLFQEQGFIRKSCAKCGRFFWTLNADRDLCPDDGLDTYSFIGEPPTSKRFDYTQSWKQVEEFFVKNNHTSVSRYPVVCRWRDDLYFTIASVVDFQRVMGSKVVFEFPANPLVVPQTCLRFKDLENVGVTGRHFSSFCMIGQHSVPDLGGYWKDECVDLDYRLLTEQFGINKDEVVFVEDVWAGGGSFGPSLEYFVQGLELGNAVFTEFQGELGKHTTLDQRVIDMGAGLERFAWITMGTPTAYDCCFGPINEKLFGTIGIDSDSEILRKYFTEIAKEIDHYDDLNQVRRLAVKNAGITDE... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain.
Catal... |
A6Q576 | MDIRKEFLNYFASKAHTIYPSAPLVPEDPTLLFTNAGMVPFKKIFTGEMPAEVPRATSCQTCIRAGGKHNDLENVGYTARHHTFFEMLGNFSFGDYFKEEAIAYAWEFVTEVLELPVEKLWVTVHESDDEAEKIWQKFVKKDRIKRFGDKDNFWQMGDTGPCGPCSEIFYDQGEEHFKGPEDYLGGDGDRFLEIWNLVFMQYERNEAGELLPLPKPSIDTGMGLERITAIKEGVLSNYDSSLFMPLIDAISDLSKKKYIYKEGASFRVIADHIRAVTFLLSQGVMFSNEGRGYVLRRILRRGVRHGYLLGLKEPFMYRLA... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain.
Catal... |
A1SJC7 | MDTAEIRRRFVAHFEHNTTVGAHTPVPSASLLLDDPNLLFVNAGMVPFKPYFLGQEAPPYPRATSVQKCVRTPDIEDVGKTTRHGTFFEMCGNFSFGDYFKEGAIELAWDLVTRPLADGGWGLEESKLYPSVYEDDPEAVALWKKVTGLPEERIIRLGKRENYWSMGVPGPGGPCSEILYDRGPDYGPDGDFGPKGEDRYLEIWNLVFMQDELSAVRSKEDFDIAGSLPKKNIDTGMGLERVAFLLQGKANMYEIDVMFPVIQKAEELTGRRYGADHDDDVRFRVVADHVRSSMMLIGDGVTPGNEARGYVLRRLLRRAV... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain.
Catal... |
B2J876 | MSSNPQYLSGNEIRNTFLNFFAQRSHQILPSASLVPEDPTVLLTIAGMLPFKPIFLGQRTPEFKRATTSQKCIRTNDIENVGRTKRHHTFFEMLGNFSFGDYFKEQAIAWGWEISTQVFGFSPQNLVVSVFEDDDEAFAIWRDQIGVPVARIKRLGEDDNFWVSGPTGPCGPCSEIYYDFHPERGDENIDLEDDSRFIEFYNLVFMQYNRDVLGNLTPLQNKNIDTGMGLERMAQILQKVPNNYETDLIFPIIQTAAQIAGIDYHSSDEKTKVSLKVIGDHVRSVVHMIADEIRASNVGRGYVLRRLIRRVVRHGRLIGI... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain.
Catal... |
B1ZZ40 | MTSAEIRQSFLDFFARQGHTIVPSSSLLPDSPGLLFTNAGMNQFVPIFLGDRAPDVSKWAGARPAKDTRAADTQKCIRAGGKHNDLEDVGFDTYHHTMFEMLGNWSFGDYFKKESITWGWELITKVWGIPAKRLFATVYSPDKSKNDPSDFDQEAYDIWAGVFKKEGLDPAVHIVHGNKKDNFWMMGDTGPCGPCSEIHFNLLPSDDEVEGRKLVNAGVPRCIEIWNHVFIQFNANADGTFSPLAAKHVDTGMGFERVAGIYATTKGFKDFSRDPSNYNADVFAPLFAKIEELSKKTYNGTVPTRREGLGEQENIDIAFR... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain.
Catal... |
B3CST3 | MTTFLNINQIRTTFIEFFKKYGHHHASSSSLVPGNDPSLFFVNAGIVQFKDYVRAPETSKYSRVVTCQKCVRAGGKHNDLESVGYTARHHTFFEMLGNFSFGEDNAKADFMQLIWNFLTKELFIDEDRLIVTVYHTDHETAKLWRSIAGLDDSRIIRIKTDDNFWSMGPVGPCGPCTEIFYDHGDKIPGGLPGTKDENGGRYVEIWNIVFMQYEQLNESTRVELAKRCIDTGAGLERIATVLQGVYDNYDIDLFKNLIANIEHLTKIKSVGEANFSHRIIADHLRASAFLIADGVMPSNDGRGYVLRRIMRRAMNQIHQL... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain.
Catal... |
P40825 | MTSTTGLRNLTLSFKKQLTTSTRTIMTIGDKQKWTATNVRNTFLDYFKSKEHKFVKSSPVVPFDDPTLLFANAGMNQYKPIFLGTVDPASDFYTLKRAYNSQKCIRAGGKHNDLEDVGKDSYHHTFFEMLGNWSFGDYFKKEAITYSWTLLTEVYGIPKDRLYVTYFEGDEKLGLEPDTEARELWKNVGVPDDHILPGNAKDNFWEMGDQGPCGPCSEIHYDRIGGRNAASLVNMDDPDVLEVWNLVFIQFNREQDGSLKPLPAKHIDTGMGFERLVSVLQDVRSNYDTDVFTPLFERIQEITSVRPYSGNFGENDKDGI... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged tRNA(Ala) via its editing domain.
Catalytic Activity: ATP + L... |
Q1C420 | MSKSTAEIRQAFLDFFHSKGHQVVSSSTLVPNNDPTLLFTNAGMNQFKDVFLGLDKRAYSRATTSQRCVRAGGKHNDLENVGYTARHHTFFEMLGNFSFGDYFKHDAINFAWELLTSEQWFNLPKEKLWVTVYETDDEAYNIWANEVGVPHERIIRIGDNKGGAFASDNFWQMGDTGPCGPCSEIFFDHGDHIWGGPPGSAEEDGDRYIEIWNIVFMQFNRQSDGTMLPLPKPSVDTGMGLERIAAVLQHVNSNYEIDLFRDLIAAVADVTGATDLSSKSLRVIADHIRSCAFLISDGVIPSNENRGYVLRRIIRRAIRH... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain (By si... |
Q8ZBT8 | MSKSTAEIRQAFLDFFHSKGHQVVSSSTLVPNNDPTLLFTNAGMNQFKDVFLGLDKRAYSRATTSQRCVRAGGKHNDLENVGYTARHHTFFEMLGNFSFGDYFKHDAINFAWELLTSEQWFNLPKEKLWVTVYETDDEAYNIWANEVGVPHERIIRIGDNKGGAFASDNFWQMGDTGPCGPCSEIFFDHGDHIWGGPPGSAEEDGDRYIEIWNIVFMQFNRQSDGTMLPLPKPSVDTGMGLERIAAVLQHVNSNYEIDLFRDLIAAVADVTGATDLSSKSLRVIADHIRSCAFLISDGVIPSNENRGYVLRRIIRRAIRH... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain.
Catal... |
O02495 | MDAQGDAGAQGGSQGGPRPSNKRLQQTQAQVDEVVGIMKVNVEKVLERDQKLSQLDDRADALQEGASQFEKSAATLKRKYWWKNIKMMIIMCAIVVILIIIIVLWAGGK | Function: Involved in the targeting and/or fusion of transport vesicles to their target membrane. Acts in neuronal exocytosis of synaptic transmission. Likely to have a role in cholinergic transmisson. Required for viability, coordinated movement and M3 pharynx motor neuron function.
Location Topology: Single-pass type... |
Q92356 | MSEPYDPYIPAEPSAAVRSGNAAASSTPNMKTAAIQQQIDDTVGIMRENISKVSERGERLDSLQDKTDNLAVSAQGFRRGANRVRKKMWWKDMRMRLCIIIGIIILLVVIIVPIATKFHGK | Function: Involved in membrane trafficking during cytokinesis and cell elongation.
Location Topology: Single-pass type IV membrane protein
Sequence Mass (Da): 13469
Sequence Length: 121
Subcellular Location: Membrane
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Q6TMJ9 | MSEPVNKVKQTQQQVDDVTNTMHIAVGKMLDNQQKVSELTDKSENMKQGAQQFKKKTNEIKRLMWCRNIKLTLIIIAVVVLLLVVIIVPIVLKFT | Function: Involved in the targeting and/or fusion of transport vesicles to their target membrane.
Location Topology: Single-pass type IV membrane protein
Sequence Mass (Da): 10876
Sequence Length: 95
Subcellular Location: Cytoplasmic vesicle
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Q54GB3 | MSNNPNNSGQPNKTQSILQEVDKVKDVMHNNIGLMLNNHDKASNLQDKTASMSNNARLFKKQTVTIRRQMWCRNMKLQLIIIAVVILVLAVILIPIIMKFV | Function: Involved in the targeting and/or fusion of transport vesicles to their target membrane.
Location Topology: Single-pass type IV membrane protein
Sequence Mass (Da): 11499
Sequence Length: 101
Subcellular Location: Cytoplasmic vesicle
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A6X270 | MAYAPQLRLYNTLTRMKEEFSPLDADNVRMYVCGPTVYDFAHIGNARPVIVFDVLFRLLRHVYGAEHVTYARNITDVDDKINARAARDYPDLAFNEAIRRVTESTNAQFQADVTALGNLQPSVQPRATEHMDEMRAMIDRLVKLGVAYVAEDHVLFSPSAMNERKGPRYGALARRSLDEMLAGARVDVASYKRDEMDFVLWKPSKEGEPGWSSPAGIAVLGRPGWHIECSAMSMAKLLEPFGGGLKCDDPLKNQFDIHGGGIDLVFPHHENEIAQSCCAFGTERMANIWMHNGFLQVEGQKMSKSLGNFITIRDVLNEGL... | Cofactor: Binds 1 zinc ion per subunit.
Catalytic Activity: ATP + L-cysteine + tRNA(Cys) = AMP + diphosphate + L-cysteinyl-tRNA(Cys)
Sequence Mass (Da): 56738
Sequence Length: 505
Subcellular Location: Cytoplasm
EC: 6.1.1.16
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P57558 | MLKIFNTLTSTKEIFTPIKKNRVNLYVCGVTVYDFCHIGHGRTFVVFDMIVRYLRFSGFQVKYVRNITDIDDKIISKSTKEKKKINTFTASMIKEMHKDFDLLGISVPDEEPRVTDYIDNIIRIITTLIKKKHAYIHKNGDVIFSIDSDPNYGTLSRQSLTSLESGSRIPLNNMKKNPLDFILWKSSNKEEYSWDSPWGKGRPGWHIECSAITNVFFNNSIDIHGGGSDLLFPHHENERSQSICFNNKSMINFWMHTGMVILNNKKMSKSLGNVYFLRNILKDCDAEVLRYFFLSTHYRHPIYYCEKNLDQAYTSLKYLY... | Cofactor: Binds 1 zinc ion per subunit.
Catalytic Activity: ATP + L-cysteine + tRNA(Cys) = AMP + diphosphate + L-cysteinyl-tRNA(Cys)
Sequence Mass (Da): 54541
Sequence Length: 464
Subcellular Location: Cytoplasm
EC: 6.1.1.16
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