ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q9FJP9 | MSSVLRLLGRRICNPAAEKVRLSSSLSGGGDFPILNGHKAAQDLSKDTLKSQDITKEKEGQHKEVKKEFKIYRWNPDKPNSKPFLQSFFVDLSSCGPMVLDVLQKIKAEDDASLSYRRSCREGICGSCSMNIDGTNTVACLKPINPNTSKPTIITPLPHMYVIKDLVVDLTNFYQQYKSMEPWLKTRKPPKDGREHRQSPKDRKKLDGLYECILCACCTTSCPSYWWNPEEFPGPAALLQAYRWISDSRDEYREERLQAITESETKVYRCRAIKNCTATCPKGLNPASAILKMKSKHLLSDPLVRTESV | Cofactor: Binds 1 [2Fe-2S] cluster.
Function: Iron-sulfur protein (IP) subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).
Catalytic Activity: a quinone + succinate ... |
P80213 | MLQVFDIIGPIMIGPSESITAGAVRIXKI | Cofactor: Binds 1 [4Fe-4S] cluster.
Catalytic Activity: L-serine = NH4(+) + pyruvate
Sequence Mass (Da): 3082
Sequence Length: 29
Pathway: Carbohydrate biosynthesis; gluconeogenesis.
EC: 4.3.1.17
|
O44074 | MLRGSTSVCRSLELVTQAARYASAATAAAPTGKRIKTFEIYRFNPEEPGAKPKLQKFDVDLDKCGTMVLDALIKIKNEVDPTLTFRRSCREGICGSCAMNIAGENTLACICNIDQNTSKTTKIYPLPHMFVIKDLVPDMNLFYAQYASIQPWLQKKTKINLGEKQQYQSIKEQEKLDGLYECILCACCSASCPSYWWNADKYLGPAVLMQAYRWIIDSRDDSAAERLARMQDGFSAFKCHTIMNCTKTCPKHLNPARAIGEIKMLLTKMKTKPAPLPTPANF | Cofactor: Binds 1 [2Fe-2S] cluster.
Function: Iron-sulfur protein (Ip) subunit of the mitochondrial electron transport chain complex II which, together with the flavoprotein (Fp) subunit forms the catalytic core of the complex . During the free-living egg-larvae stages, which occur in an aerobic environment, complex II... |
Q75CI4 | MVFRAGIGRIGLIRGLATQAAEVSATRYKSFKIYRWNPDTPAEKPRMQEYKVDLNKCGPMVLDALIKIKNEQDPTLTFRRSCREGICGSCAMNIGGRNTLACLCKIDQAENKDVKIYPLPHMYVVKDLVPDLTNFYKQYKSIQPYLQKASKPADGREHLQSIADRKKLDGLYECILCACCSTACPSYWWNNEQYLGPAVLMQAYRWMVDSRDGAGAGRREQLQNAMSVYRCHTIMNCTRTCPKGLNPGKAIAEIKKALAFA | Cofactor: Binds 1 [2Fe-2S] cluster.
Function: Iron-sulfur protein (IP) subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).
Catalytic Activity: a quinone + succinate ... |
P08066 | MSEQKTIRFIITRQDTADSTPYDEEFEIPYRPNLNVISALMEIRRNPVNVKGEKTTPVTWDMNCLEEVCGACSMVINGKPRQSCTALIDQLEQPIRLKPMKTFPVVRDLQVDRSRMFDSLKKVKAWIPIDGTYDLGPGPRMPEKRRQWAYELSKCMTCGVCLEACPNVNSKSKFMGPAPMSQVRLFNAHPTGAMNKSERLEALMDEGGLADCGNSQNCVQSCPKGIPLTTSIAALNRDTNLQAFRNFFGSDRV | Cofactor: Binds 1 [2Fe-2S] cluster.
Catalytic Activity: a quinone + succinate = a quinol + fumarate
Sequence Mass (Da): 28418
Sequence Length: 253
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle; fumarate from succinate (bacterial route): step 1/1.
EC: 1.3.5.1
|
Q6FWS8 | MFMLRVSRRGLATATSVPRLKTFKIYRWNPDKPTEKPHLQEYKVDLEDCGPMVLDALLKIKNEQDATLTFRRSCREGICGSCAMNIGGANTLACLCKIDQDESKTTKIYPLPHMFIVKDLVPDLTGFYQQYKSIQPYLQRTDYPADGKEVLQSIDDRKKLDGLYECILCACCSTSCPSYWWNQEEYLGPAVLMQAYRWLIDSRDQATKARRTMLQNSMSLYRCHTIMNCTRTCPKGLNPGRSIAEIKKQLAFD | Cofactor: Binds 1 [2Fe-2S] cluster.
Function: Iron-sulfur protein (IP) subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).
Catalytic Activity: a quinone + succinate ... |
P48932 | MIIKNLNQKIITIDNSSPYQKFIRIYRWNPNLNLNPWFSIFPISTNNCGPMILDALIQIKNIQDSSLTFRRSCREGICGSCSMNIDGTNSLACLRSLNTKSNFITIYPLPHTYIIKDLVPDLSNFYAQYKLIKPWLINKIGFSLKENLQSKIDRLELDGLYECILCACCSASCPSYWWNQDKYLGPAILLQAYRWIVDSRDNSTENRLNFLNNKMRLFRCHTIMNCSKTCPKSLNPGKAIASIKYRIINN | Cofactor: Binds 1 [2Fe-2S] cluster.
Function: Iron-sulfur protein (IP) subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).
Catalytic Activity: a quinone + succinate ... |
Q9S9W2 | MEKKLPRRLEGKVAIVTASTQGIGFGITERFGLEGASVVVSSRKQANVDEAVAKLKSKGIDAYGIVCHVSNAQHRRNLVEKTVQKYGKIDIVVCNAAANPSTDPILSSKEAVLDKLWEINVKSSILLLQDMAPHLEKGSSVIFITSIAGFSPQGAMAMYGVTKTALLGLTKALAAEMAPDTRVNAVAPGFVPTHFASFITGSSEVREGIEEKTLLNRLGTTGDMAAAAAFLASDDSSYITGETLVVAGGMPSRL | Function: Involved with IBR3 and IBR10 in the peroxisomal beta-oxidation of indole-3-butyric acid (IBA) to form indole-3-acetic acid (IAA), a biologically active auxin. May be responsible for catalyzing the dehydrogenation step in the conversion of IBA . May be involved in the peroxisomal activation of 2,4-dichlorophen... |
O86487 | MNNKKTATNRKGMIPNRLNKFSIRKYSVGTASILVGTTLIFGLSGHEAKAAEHTNGELNQSKNETTAPSENKTTKKVDSRQLKDNTQTATADQPKVTMSDSATVKETSSNMQSPQNATANQSTTKTSNVTTNDKSSTTYSNETDKSNLTQAKDVSTTPKTTTIKPRTLNRMAVNTVAAPQQGTNVNDKVHFSNIDIAIDKGHVNQTTGKTEFWATSSDVLKLKANYTIDDSVKEGDTFTFKYGQYFRPGSVRLPSQTQNLYNAQGNIIAKGIYDSTTNTTTYTFTNYVDQYTNVRGSFEQVAFAKRKNATTDKTAYKMEV... | Function: Cell surface-associated calcium-binding protein which plays an important role in adhesion and pathogenesis . Mediates interactions with components of the extracellular matrix such as host NRXN1 to promote bacterial adhesion .
Location Topology: Peptidoglycan-anchor
Sequence Mass (Da): 102915
Sequence Length: ... |
Q99W48 | MNNKKTATNRKGMIPNRLNKFSIRKYSVGTASILVGTTLIFGLSGHEAKAAEHTNGELNQSKNETTAPSENKTTEKVDSRQLKDNTQTATADQPKVTMSDSATVKETSSNMQSPQNATASQSTTQTSNVTTNDKSSTTYSNETDKSNLTQAKNVSTTPKTTTIKQRALNRMAVNTVAAPQQGTNVNDKVHFTNIDIAIDKGHVNKTTGNTEFWATSSDVLKLKANYTIDDSVKEGDTFTFKYGQYFRPGSVRLPSQTQNLYNAQGNIIAKGIYDSKTNTTTYTFTNYVDQYTNVSGSFEQVAFAKRENATTDKTAYKMEV... | Function: Cell surface-associated calcium-binding protein which plays an important role in adhesion and pathogenesis. Mediates interactions with components of the extracellular matrix such as host NRXN1 to promote bacterial adhesion.
Location Topology: Peptidoglycan-anchor
Sequence Mass (Da): 103293
Sequence Length: 95... |
Q9N4A7 | MTTVRQRIDTQHRDAIHDAQLNIYGSRLATCGSDRLVKIFEVRPNGQSYPMAELVGHSGPVWKVSWAHPKYGGLLASASYDKKVIIWNEQQGRWQKAYEWAAHEASTTCVAFAPHQYGLMLASASADGDIGILRYDNSSNEWISSKIQKCHEQGVNSVCWAPGSADPAAKKRLVSAGNDKNVKIWAFDDATNEWILEKTLAGHTDFVREAAWCPVTNNGQHTIVSCGMEGNLVLFRTSNIETEEWKAKLLETAPCALYHSSFSPCGSFLSVAGDDNVITIWRENLQGQWIKVPRDNKEREGMSQAVGAPGAQR | Function: Functions as a component of the nuclear pore complex (NPC) and the COPII coat (By similarity). Required for the nuclear import of hcp-4 during mitotic prophase, this step is essential for centrosome assembly and resolution .
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 34692
Sequence Len... |
Q9V3J4 | MVSLLQEIDTEHEDMVHHAALDFYGLLLATCSSDGSVRIFHSRKNNKALAELKGHQGPVWQVAWAHPKFGNILASCSYDRKVIVWKSTTPRDWTKLYEYSNHDSSVNSVDFAPSEYGLVLACASSDGSVSVLTCNTEYGVWDAKKIPNAHTIGVNAISWCPAQAPDPAFDQRVTSRSAAVKRLVSGGCDNLVKIWREDNDRWVEEHRLEAHSDWVRDVAWAPSIGLPRSQIATASQDRHVIVWSSNADLSEWTSTVLHTFDDAVWSISWSTTGNILAVTGGDNNVTLWKENTEGQWIRINYESGTAIQSKQPSHLPHSHS... | Function: Functions as a component of the nuclear pore complex (NPC) and the COPII coat (By similarity). At the endoplasmic reticulum, SEC13 is involved in the biogenesis of COPII-coated vesicles (By similarity). Recruited to transcriptionally active chromatin at the time of transcription initiation by RNA polymerase I... |
Q5B563 | MAAAQVISNSGHDDMIHDAGLDYYGRRLATCSSDKTIKIFEIEGDTHKLVETLKGHEGPVWCVEWAHPKFGTILASSSYDGKVLIWREQHQSSTAPIGSGAWTKVFDFSLHTASVNMISWAPHETGCLLACASSDGHVSVLEFRDNSWTHQIFHAHGMGVNSISWAPAASPGSLVSSNPGIGQQRRFVTGGSDNLLKIWDYNPETKTYNATQTLEGHSDWVRDVAWSPSILSKSYIASASQDKTVRVWTADASNPGQWTSQVLEFDNVLWRVSWSPSGNILAVSGGDNKVSLWKENLRGQWEKVKDIEE | Function: Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules. It also functions as a co... |
P55735 | MVSVINTVDTSHEDMIHDAQMDYYGTRLATCSSDRSVKIFDVRNGGQILIADLRGHEGPVWQVAWAHPMYGNILASCSYDRKVIIWREENGTWEKSHEHAGHDSSVNSVCWAPHDYGLILACGSSDGAISLLTYTGEGQWEVKKINNAHTIGCNAVSWAPAVVPGSLIDHPSGQKPNYIKRFASGGCDNLIKLWKEEEDGQWKEEQKLEAHSDWVRDVAWAPSIGLPTSTIASCSQDGRVFIWTCDDASSNTWSPKLLHKFNDVVWHVSWSITANILAVSGGDNKVTLWKESVDGQWVCISDVNKGQGSVSASVTEGQQN... | Function: Functions as a component of the nuclear pore complex (NPC) and the COPII coat. At the endoplasmic reticulum, SEC13 is involved in the biogenesis of COPII-coated vesicles . Required for the exit of adipsin (CFD/ADN), an adipocyte-secreted protein from the endoplasmic reticulum (By similarity).
Location Topolog... |
Q6CSZ5 | MVTINNAHSELIHDAVLDYYGKRLATCSSDHTVKIFEVEGETHKLVDTLQGHEGPVWQVDWAHPKFGVILASCSYDGKVLIWKEVNGRWSQIAAHEVHSASVNSIQWAPHEYGPLLLAASSDGKVSVVEFKENGTTSPIIIDAHSIGANTACWAPATLQQQSNQGTSGSASPQQVRRFVTGGADNLVKIWKYNSDAATYLLEHTLEGHSDWVRDVAWSPTVLSRSYLASVSQDRTCIIWTQDSKEDTWKKTLLKEDKFPDVLWRASWSLSGNILALSCGDNTVTLWKENLEGKWEPAGQVTE | Function: Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules. It also functions as a co... |
A5DXE2 | MVTIGNAHEDLIHDAVLDYYGKRLATCSSDKTIKIYDIEGTENYKLTATLTGHEGPIWQVAWAHPKFGSILASCSYDGKVLIWKEQQDTQQWSIIAEHTIHQASVNSVSWAPHELGAVLLCTSSDGKVSVVDFNDDGTTSHVIFDAHAIGVNSASWAPFTAASSTSSKDANTLKQHRRFVTCGSDNLVKIWKYDTALETYAEEAKLEGHTDWVRDVAWSPSNLVRPYIATASQDCTVLIWTQDKDGKWQSQPLTEEKFPDVCWRCSWSLSGNILAVSGGDNKVTLWKENLQGKWESAGEVELIK | Function: Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules. It also functions as a co... |
A6TLE7 | MKRLFEKVFGSESEREIKKIDKLADRVEALDEEYKKLSDQALQSKTAELKGRLSQGEALDDILPEAFATMREAAWRVLGMKHYRVQIYGAIILHQGRISEMKTGEGKTLMATLPVYLNALAGKGVHVVTVNDYLAQRDCEWMGKLYEFLGLSVGVIVHGITIEQRRAAYNADVTYGTNNEFGFDYLRDNMVIYQKDMVQREQNYAIVDEVDSILIDEARTPLIISGQGEKSTKLYHIVDQFVKTLKIEDDVSLDEKANSVTLTEDGGTKAEKAFGIENLADMNNMELSHHINQALKARNLMRLDKDYVVKDGEIIIVDDF... | Cofactor: May bind 1 zinc ion per subunit.
Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving ... |
Q9SYI0 | MVSPLCDSQLLYHRPSISPTASQFVIADGIILRQNRLLSSSSFWGTKFGNTVKLGVSGCSSCSRKRSTSVNASLGGLLSGIFKGSDNGESTRQQYASIVASVNRLETEISALSDSELRERTDALKQRAQKGESMDSLLPEAFAVVREASKRVLGLRPFDVQLIGGMVLHKGEIAEMRTGEGKTLVAILPAYLNALSGKGVHVVTVNDYLARRDCEWVGQVPRFLGLKVGLIQQNMTPEQRKENYLCDITYVTNSELGFDYLRDNLATSVEELVLRDFNYCVIDEVDSILIDEARTPLIISGPAEKPSDQYYKAAKIASAF... | Function: Has a central role in coupling the hydrolysis of ATP to the transfer of proteins across the thylakoid membrane. Involved in photosynthetic acclimation and required for chloroplast biogenesis.
Catalytic Activity: ATP + H2O + chloroplast-proteinSide 1 = ADP + phosphate + chloroplast-proteinSide 2.
Location Topo... |
Q4JTQ3 | MLGLSKILRMGEGRAVKRLAKIADQVMDLDEEYTKLTDEELQAKTDELKKRVQEDGESLDDILLEAFATAREASWRVLGQKHYKVQIMGGAGLHFGYVSEMKTGEGKTLTCVLPAYLNALSGKGVHVVTVNDYLAKRDAEWMGRVHRFLGLSTDVILSGKNPAERREAYNADITYGTNNEFGFDYLRDNMAHSLNDLVQRGHNYAIVDEVDSILIDEARTPLIISGPVEGSSKWFSAFAAIAPKLTRDIHYEVDERKKTVGVKEEGVEFVEDQLGIENLYAPEHSQLVSYLNNSIKAKELFTRDKDYIVRNGEVVIVDEF... | Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide c... |
P28366 | MLGILNKMFDPTKRTLNRYEKIANDIDAIRGDYENLSDDALKHKTIEFKERLEKGATTDDLLVEAFAVVREASRRVTGMFPFKVQLMGGVALHDGNIAEMKTGEGKTLTSTLPVYLNALTGKGVHVVTVNEYLASRDAEQMGKIFEFLGLTVGLNLNSMSKDEKREAYAADITYSTNNELGFDYLRDNMVLYKEQMVQRPLHFAVIDEVDSILIDEARTPLIISGQAAKSTKLYVQANAFVRTLKAEKDYTYDIKTKAVQLTEEGMTKAEKAFGIDNLFDVKHVALNHHINQALKAHVAMQKDVDYVVEDGQVVIVDSFT... | Cofactor: May bind 1 zinc ion per subunit.
Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving ... |
C5C1N8 | MPSILDKVLRMGEGRILKKLTGIVAQVNAHEDTVREFTDAELREETDVFKARLADGETLEAILPEAFATVREAARRTLGQRPHDVQVMGGAALHLGNIAEMKTGEGKTLAATLPAYLNALSGDGVHVVTVNDYLAQYQSDLMGRVYRFLGLTTGCILSGQKPEERRRHYAADITYGTNNELGFDYLRDNMAWSSGELVQRGHNFVIVDEVDSILIDEARTPLIISGPASGDANKWYAEFARVARRLTRESDYEVDEKKRNVGVLEPGIEKVEDYLGIDNLYESLNTPLIGFLNNAIKAKELFKRDKDYVVLKGEVLIVDE... | Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide c... |
Q8RI93 | MIGSLLKKIFGTKNDREIKALTKEVEKINALESEYEKLSDEDLKNKTNIFKERLKNGETLDDILVEAFATVREASKRVLGLRHYDVQLIGGMVLHQGKITEMKTGEGKTLVATCPVYLNALAGHGVHVITVNDYLAKRDRDQMSRLYGFLGLSSGVILNGLPTDQRKKSYNSDITYGTNSEFGFDYLRDNMVSSLDQKVQRELNFCIVDEVDSILIDEARTPLIISGAAEDKIKWYQISFQVVSMLNRSYETEKIKNIKEKKAMNIPDEKWGDYEVDEKSRVIVFTEKGVKRVEEILKIDNLYAPEYVELTHFLNQALKA... | Cofactor: May bind 1 zinc ion per subunit.
Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving ... |
Q6B8L3 | MFNFFKKNKLNKFQNTINEIHQIGNTVKNYSDAELKKQTHKLKKKIIQNSNLTEILPESFAIVKEAIKRSTGMILFDVQLVGSIVLHQGQIAEMKTGEGKTIVAITTGYLNALTSKGVHIITVNDYLAKRDSELAQKICSYIDLKVGLITQSMTYEEKKRAYDCDITYITNSELGFDYLRDNMAIEFNQIVQRGFNFAIIDEVDSILIDEARTPLIISGPFEIEINKYKKSTSIANTLQKDLDYEIDEKTKNITLTEKGISRCENMLNIDNLYDIHDSWIQYLLNSLKAKDLFLKNQHYIVKNNEIIIVDEFTGRVMQGR... | Function: Has a central role in coupling the hydrolysis of ATP to the transfer of proteins across the thylakoid membrane.
Catalytic Activity: ATP + H2O + cellular proteinSide 1 = ADP + phosphate + cellular proteinSide 2.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 103025
Sequence Length: 882
Subc... |
O78441 | MLNVLFGDPNERRINPYKQIVNKINYLEAKLKKLTDSELQEQTERFIKLLSNNSSNEELLPEIYATVREASLRVLGLRHFDVQLIGGLILNDGKIAEMKTGEGKTLVALLPTYLNALAGFGVHVVTVNDYLARRDSEWVGQVHKFLGLTVGLIQEGMSQFERRENYLKDVTYATNSELGFDYLRDNMAIDLEDIVQRPFYFCVIDEVDSILIDEARTPLIISGPGNSPVNKYIKANVISQDLIKDIDYEIDEKARNVILTDNGILKCENLLGNTDIFNLQDPWAPYIFNAIKAKELFLENIHYIIRNQEIVIVDEFTGRI... | Function: Has a central role in coupling the hydrolysis of ATP to the transfer of proteins across the thylakoid membrane.
Catalytic Activity: ATP + H2O + cellular proteinSide 1 = ADP + phosphate + cellular proteinSide 2.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 100567
Sequence Length: 877
Subc... |
P0AG98 | MSANTEAQGSGRGLEAMKWVVVVALLLVAIVGNYLYRDIMLPLRALAVVILIAAAGGVALLTTKGKATVAFAREARTEVRKVIWPTRQETLHTTLIVAAVTAVMSLILWGLDGILVRLVSFITGLRF | Function: Essential subunit of the Sec protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13643
Sequence Length: 127
Subcellular Location: Cell inner membrane
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P43805 | MIFFAAAAIGNIYFQQIYSLPIRVIGMAIALVIAFILAAITNQGTKARAFFNDSRTEARKVVWPTRAEARQTTLIVIGVTMIASLFFWAVDSIIVTVINFLTDLRF | Function: Essential subunit of the Sec protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 11817
Sequence Length: 106
Subcellular Location: Cell inner membrane
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Q9KGE8 | MAGGVKGIGKFFGDVVAEMKRVSWPTRKELTRYTLVVLGTVAFITVFFAVVDYGISALVRGLIE | Function: Essential subunit of the Sec protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 6981
Sequence Length: 64
Subcellular Location: Cell membrane
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B9LV21 | MDVPYDLNSYIRVLKLASTPSTDEFLQVSKIAGAGILLIGFIGFLMFAIMSLLPGVGA | Function: Essential subunit of the Sec protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 6176
Sequence Length: 58
Subcellular Location: Cell membrane
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Q5V456 | MDVPYDLTSYIRVLKLASTPSWEEFSQIAKIAGAGIALVGLLGFIIFAVMTFVPGSKPV | Function: Essential subunit of the Sec protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 6331
Sequence Length: 59
Subcellular Location: Cell membrane
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Q8TI84 | MVESTFEPNITTKSVGQAIRAHLRVLKLTKKPSREEFLTIAKVAGAGILAVGAIGFIIYVLLTMLPQWVSQ | Function: Essential subunit of the Sec protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 7753
Sequence Length: 71
Subcellular Location: Cell membrane
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Q57817 | MKTDFNQKIEQLKEFIEECRRVWLVLKKPTKDEYLAVAKVTALGISLLGIIGYIIHVPATYIKGILKPPTTPRV | Function: Essential subunit of the protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 8438
Sequence Length: 74
Subcellular Location: Cell membrane
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Q8TX54 | MSTYEELISLLRDCKRVLRAARKPTWDEYIESAKIAGLGILIVGGVGFLIRVIVQLIELYT | Function: Essential subunit of the Sec protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 6895
Sequence Length: 61
Subcellular Location: Cell membrane
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Q6LXB7 | MQKSKLNTTLNGLKDFLHQCRRVLMISRKPTRQEYITISKVTGLGICLLGFVGFVIHVPITYLKALIKP | Function: Essential subunit of the Sec protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 7843
Sequence Length: 69
Subcellular Location: Cell membrane
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P58061 | MHPIQIVMFIMAVICLIIGLLLSNHGSTGGLASLSGQDLEIFRKTKDRGFVKILQIIMFILVVLFLILGLIFSFAPR | Function: Involved in protein export. Participates in an early event of protein translocation (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 8544
Sequence Length: 77
Subcellular Location: Cell membrane
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P38388 | MELALQITLVVTSILVVLLVLLHRAKGGGLSTLFGGGVQSSLSGSTVVEKNLDRLTLFVTGIWLVSIIGVALLTKYR | Function: Involved in protein export. Participates in an early event of protein translocation (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 8151
Sequence Length: 77
Subcellular Location: Cell membrane
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P51274 | MEQILKFLWYISTIILVFSILIHNPKSEGLGTIGSQNQFFSNTRSTENTLNKVTWLFLALFLLFTTILAIN | Function: Involved in protein export. Participates in an early event of protein translocation across the chloroplast thylakoid membrane (Potential).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 8166
Sequence Length: 71
Subcellular Location: Plastid
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Q9HV52 | MLEKVVIVVHLLMALGLVGLILVQHGKGADAGASFGAGASATVFGSQGSATFLSRITGILAAVFFLTSLGLAYFAKEKSDALQHIGLPDPAVLEQKQEKAPAADDVPVLQEQSKPAESAGDVPAAPEQK | Function: Involved in protein export. Participates in an early event of protein translocation (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13207
Sequence Length: 129
Subcellular Location: Cell inner membrane
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P95577 | MLETVVIVFHLLGALGVVALVLLQQGKGADAGASFGAGASNTVFGGQGTSTFLSKFTAILAACFFITSLGLGYFAKEKAQQLTQVGLPDPAVLEVKQKPAADDVPVLEGQKPAAVPADVPQAPEKK | Function: Involved in protein export. Participates in an early event of protein translocation (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 12866
Sequence Length: 126
Subcellular Location: Cell inner membrane
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P60462 | MAKEKTTLPPTGAGLMRFFDEDTRAIKITPKGAVALTLILIIFEIILHVVGPRIFG | Function: Involved in protein export. The function of the beta subunit is unknown, but it may be involved in stabilization of the trimeric complex (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 6122
Sequence Length: 56
Subcellular Location: Cell membrane
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A1RVP5 | MARRRKYEGLNPFVAAGLIKFSEEGELERIKLNPRTAILVSITVIIAILVLNILHPL | Function: Involved in protein export. The function of the beta subunit is unknown, but it may be involved in stabilization of the trimeric complex.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 6412
Sequence Length: 57
Subcellular Location: Cell membrane
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Q8E480 | MKLLYIFEKNIILRKILITFSLIIIFLLGRYVPIPGVLISAYKGQDNNFATLYSTVTGGNLSQVGVFSLGIGPMMTTMILLRLFTIGKYSSGVSQKVQQFRQNVVMLVIAIIQGLAIAISFQYHNGFSLTKLLLATMILVTGAYIISWIGNLNAEYGFGGMTILVVVGMLVGQFNNIPLIFELFQDGYQLAIILFLLWTLVAMYLMITFERSEYRIPVMRTSIHNRLVDDAYMPIKVNASGGMAFMYVYTLLMFPQYIIILLRSIFPTNPDITSYNDYFSLSSIQGVVIYMILMLVLSVAFTFVNIDPTKISEAMRESGD... | Function: Part of the accessory SecA2/SecY2 system specifically required for export of possible cell wall proteins. The central subunit of a protein translocation channel.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 46175
Sequence Length: 409
Subcellular Location: Cell membrane
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F8LR08 | MKKISQSIITKRVLWTLFFLFIYCLGNQLVLPFVDLKNANIFGGAIGSLAFSSAMMGGNLRSMSLFSVGLSPWMSAMILWQMFSFSKKMGLKNLPIEIQDRRRMYLALGIAIVQSLAVSLNLPIVSGVNASLAIFMNTILLIAGTFFLVWLSDLNSLFGIGGSIVILMASMMANLPYQIMDSIEKLGIGWNVLLPLILFSLVFLYVSGVVQRARYRISINKINIHNRFKQYSYLDIMLNPAGGMPFMYAMSLVSIPQYVFMLIQFIHPENKWTSGAIKALTVGQPLWLVVYLVMLFVLGLAFAFVNVSGEQISERMRKSG... | Function: Part of the accessory SecA2/SecY2 system specifically required for export of possible cell wall proteins. The central subunit of a protein translocation channel.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 45722
Sequence Length: 408
Subcellular Location: Cell membrane
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Q9AEU0 | MKSFFKPLILKKFLWTLLFVFIYVLGSKLTLPFVDVSSIAKLNGDSVTLNYAAALMGGNLRSMSFFSIGLAPWMSSILIWQMFTVSKRLGLNKLSMESQEKRRMLLTLAIALIQSLGLVLNLPLKTVAGVGQGTIVFLDTLILIAGTYFLIWLTDLNSSMGLGGSIMIVMVSMISYIPQDIWLSIQELKISPLILALIGFFSLCFLYLAVLVERAKYRIPINKINIHNRFKKYSYLDIRVNAAGGLPIMYAMTLVSIPQYFLMLLLFFQPNNRLLKEGILSLAMGGIPWFILYLLTIFILAWAFAFINVNSDQIAERMQR... | Function: The central subunit of a protein translocation channel (Potential). Part of the accessory SecA2/SecY2 system specifically required to export GspB, a serine-rich repeat cell wall protein encoded upstream in the same operon.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 46158
Sequence Lengt... |
A1C3L4 | MLRKLQKYWKKSIIFQRFTWMIGIVFIYMLGRQIPIPTVGVDKVVVGNASDSQLLENFGAITGIQFSNMTLFSLGIGPTMTMMILWRFLITFKLIGSWTSNKVNRLQFLLTLAIALLQSFGITNDSKFLLIFGYSHSTLRIITIILLTTGTFILNWLCKINSERGIGGMTVVILVNMILTFQSNIIRYFSVQQFKFSSLIQYGLVFFVALSILIWFNILLYKGEYRIPIQRVGLNTPYHASSYLPIRVTPAGAMPFMYGMTLMMLPPYIFVVLLHIFPGNQILEYLSVHIGLSQLPGVICYIFLLYFLSIGFAYYNYDPY... | Function: Part of the accessory SecA2/SecY2 system specifically required for correct glycosylation and export of Fap1, a serine-rich fimbrial adhesin. Potentially the central subunit of a protein translocation channel.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 47510
Sequence Length: 418
Subcell... |
Q97P79 | MTKIYSSIAVKKGLFTSFLLFIYVLGSRIILPFVDLNTKDFLGGSTAYLAFSAALTGGNLRSLSIFSVGLSPWMSAMILWQMFSFSKRLGLTSTSIEIQDRRKMYLTLLIAVIQSLAVSLRLPVQSSYSAILVVLMNTILLIAGTFFLVWLSDLNASMGIGGSIVILLSSMVLNIPQDVLETFQTVHIPTGIIVLLALLTLVFSYLLALMYRARYLVPVNKIGLHNRFKRYSYLEIMLNPAGGMPYMYVMSFLSVPAYLFILLGFIFPNHSGLAALSKEFMVGKPLWVYVYISVLFLFSIIFAFVTMNGEEIADRMKKSG... | Function: Part of the accessory SecA2/SecY2 system specifically required for export of possible cell wall proteins. The central subunit of a protein translocation channel.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 45367
Sequence Length: 405
Subcellular Location: Cell membrane
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Q0TNJ4 | MTKELLRALPKIDEILGIFNEDFLNENGRETVVSALRDIINENRKAILNEEVDYALTKEEAKSKCEHRLLKKRERNLKRVINGTGVVIHTNLGRSLLSKEATEAVALAASSYSNLEYDLEKGERGSRYSLIEGIIKDITGAEAALVVNNNAAAIMLVLNSLCENKEVIVSRGELVEIGGSFRIPEVMNFSRAKLVEVGTTNRTHLYDYEDAITEETGAFLKVHSSNFKIVGFTKSVSANEICNLAREKDIPVIEDIGSGVLIDLSKYGLEKEPTVIESLEDGVDVVTFSGDKMLGGAQAGIIVGKKKFIDKIKRNQLTRA... | Function: Converts seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis.
Catalytic Activity: H(+) + L-seryl-tRNA(Sec) + selenophosphate = L-selenocysteinyl-tRNA(Sec) + phosphate
Sequence Mass (Da): 51913
Sequence Length: 462
Pathway: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec)... |
B1I3P6 | MELNTGDVMRRLPAVDELLREPELEMLLAEHPRALVVAAVREVLQQWRETVRAEPERVPGSREELAAAIVQEVTITVRAKARPALRRVINATGVVLHTNLGRAVLSDKALRAVHEAAAHYSNLEFNLETGRRGSRYALVEDLLKLLTGTESCLVVNNNAAAVLLALSTLAAGREVIVSRGQLVEIGGSFRIPEVMKQSGARLVEVGATNKTHLRDYRDAITSETALLLHVHASNYRIVGFTHEVGLEELVALGREHGLPVMSDLGSGFLVDLSRFGYPYEPTVQETAGAGVDVVTFSGDKLLGGPQAGIIVGRREVVDRM... | Function: Converts seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis.
Catalytic Activity: H(+) + L-seryl-tRNA(Sec) + selenophosphate = L-selenocysteinyl-tRNA(Sec) + phosphate
Sequence Mass (Da): 51152
Sequence Length: 473
Pathway: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec)... |
P56372 | MSSLFRHIPSVDRFLQDLEQDRALADLPRQMLKDLVAEFLDLCREEIRAGVVTDESALAFTTLAARAGAYVRTRSRPHFRRVVNATGVVIHTNLGRSILAEEAVLAVAEGCRHYSNLEMDLDTGQRGSRYSHVEKLLCRLTGAEAGLVVNNNAAAVLLVLDTLAKGREVVVSRGQLVEIGGSFRIPEVMKKSGAVLREVGATNRTHLRDYAEAIGPDTAMLMKVHTSNYRIIGFHKEVDLPDLVALGRERGLSTFEDLGSGNLFDFSPYGFMPEPTVQQVLRSGVDVVTFSGDKLLGGPQAGVIVGRREFIERIKKNQLN... | Function: Converts seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis.
Catalytic Activity: H(+) + L-seryl-tRNA(Sec) + selenophosphate = L-selenocysteinyl-tRNA(Sec) + phosphate
Sequence Mass (Da): 50688
Sequence Length: 465
Pathway: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec)... |
B8J1N0 | MNNLFRSIPAVDLCLTALGQADPSLVEAPRGLMRDLITEFWDKKRHEIREGHCKKNEQLTLDACLPGLMTHVRAGLRSRFRAALNATGVVVHTNMGRSVLAKEAREAVITAATGYCNLELDMQSGGRGSRHALVEDLLCRLTGAEAALVVNNNAAAVLLVLDTFCKGGEVVVSRGELVEIGGSFRIPEVMEKSGATLREVGATNRTHLHDYSAAINENTRALMRVHTSNYRIVGFHSAVPLPELAALARRHDLPLIEDLGSGSLTDFSSCGLPDEPTVPSVLAQGADIATFSGDKVLGGPQAGIITGRKDMVDTLKRNPL... | Function: Converts seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis.
Catalytic Activity: H(+) + L-seryl-tRNA(Sec) + selenophosphate = L-selenocysteinyl-tRNA(Sec) + phosphate
Sequence Mass (Da): 51084
Sequence Length: 475
Pathway: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec)... |
Q30SC1 | MFLLKSIPQVDKFIKNEKFASLPLTLLVQITAEVLQDLRERILKNEIESFSEDELVKKVLQKYKDITKPSLQKIINATGVIVHTNLGRSLIDANAFERVKGIVTSYNNLEYDLEKGKRGERYSHISDAICRLLGCEDVLIVNNNASAVFLILNTFAKQKEVVVSRGELVEIGGSFRVPDVMKQSGAKLVEVGATNKTHLYDYENAISKKTSMLMKVHKSNYSIEGFSSEVEFKELVKLAREKNLIDYYDMGSGHLVNLPYGLDQHEPSVLKYMQENPSLLSFSGDKLLGSVQAGIIVGKKEYIAKLKKNQLLRMLRVDKL... | Function: Converts seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis.
Catalytic Activity: H(+) + L-seryl-tRNA(Sec) + selenophosphate = L-selenocysteinyl-tRNA(Sec) + phosphate
Sequence Mass (Da): 50610
Sequence Length: 449
Pathway: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec)... |
Q7M9L1 | MSHPLRSLPKIDKILQESRFADHSKELLTTLARDYLEEIRAQFLQDATPIPPSESILQEVERRYEASLAPSLVPLVNATGIIVHTNLGRSVFAPELIEEIKPLLTSYNNLEYDLKAGRRGERYSHLHGILKAILGCEEVLVVNNNAAAVFLILHTFAQNQEAIISRGELIEIGGSFRIPEVMKNAGAILKEVGTTNKTHRRDYEEAITPQSALLMKVHKSNYDIVGFTQEVDLQELIELSQKHNLIDYYDLGSGFLESVPFTNEPTLKKIASLSPSLVSFSGDKLLGGAQAGIIFGKKSLIDRLKKNQLLRMLRVDKFTL... | Function: Converts seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis.
Catalytic Activity: H(+) + L-seryl-tRNA(Sec) + selenophosphate = L-selenocysteinyl-tRNA(Sec) + phosphate
Sequence Mass (Da): 49749
Sequence Length: 444
Pathway: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec)... |
A1JT25 | MSAEPHHLYSQLPAIDSLLRAPEMAPLLDEYGAALLTENLRLMQAEAREYIRQFHTLADWCADWPAALRHRLNQRQPALKPVFNLSGTVLHTNLGRAPLAESAIAAVTDAMRGAVTLEYSLSGAGRGHRDRAVADLLCELTGAEDACIVNNNAAAVFLMLTVMAAGKQVVVSRGELVEIGGAFRIPDVMRQAGCELVEVGTTNRTHLKDYRQAISEHTGLLMKVHTSNYSIEGFTASVAEQQLAALGHEFAIPTATDLGSGSLVDMTRYGLPAEPMPQQLIAAGVDLVTFSGDKLLGGPQAGIILGKKQWIDQLQQHPLK... | Function: Converts seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis.
Catalytic Activity: H(+) + L-seryl-tRNA(Sec) + selenophosphate = L-selenocysteinyl-tRNA(Sec) + phosphate
Sequence Mass (Da): 50072
Sequence Length: 462
Pathway: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec)... |
Q06373 | MDNKNFQSKTGFNLENTYLTLPNIFFSEQNPKGSKNPKLIKFNTSLAEELGLNEEVLNSDFGLNIFAGNETFPGIVPIAQAYAGHQFGHFTMLGDGRALLLGEHVTKDCKRYDVQLKGSGRTIYSRGGDGKAALAPMLREYIISEGMHGLGIPTTRSLAVVSTGEEVLRERFEQGAILTRIASSHIRVGTFAYAAQWGTLEDLKSLADYTIKRHFPNIADNENKYILFLEEVINRQAELIVKWQSVGFIHGVMNTDNMVISGETIDYGPCAFMDTYDTNTVFSSIDYAGRYAYGNQPNMALWNLARFSEALLPLLNPNLD... | Function: Catalyzes the transfer of adenosine 5'-monophosphate (AMP) to Ser, Thr or Tyr residues of target proteins (AMPylation).
Catalytic Activity: ATP + L-tyrosyl-[protein] = diphosphate + O-(5'-adenylyl)-L-tyrosyl-[protein]
Sequence Mass (Da): 55805
Sequence Length: 490
EC: 2.7.7.108
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Q8FP92 | MSTPTNPEQPTDHPSAPFTLEARFAEEFPEMTTPWRGEDQPDPELAVLNEDLARLLGIDPDWLRSPAGVEFLLGLNPEPTTEMVAQGYAGHQFGQFVPSLGDGRALLLGEIRGTDGVLRDIHLKGSGRTRYSRGADGRAALGPALREYLVSEAMHALGVPTTRALAVVTTGRKIQRDRVLPGAVVVRVATSHIRVGSFQYANITGGIDLSRRLADHAITRHYPRLVERFPESGPERYAWFFRQVMDAQAQTVARWMRLGFVHGVLNTDNTLVSGETIDYGPCAFMDRYREDAVFSSIDTHGRYKFSNQPLILGWNLARLA... | Function: Catalyzes the transfer of adenosine 5'-monophosphate (AMP) to Ser, Thr or Tyr residues of target proteins (AMPylation).
Catalytic Activity: ATP + L-tyrosyl-[protein] = diphosphate + O-(5'-adenylyl)-L-tyrosyl-[protein]
Sequence Mass (Da): 54555
Sequence Length: 492
EC: 2.7.7.108
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Q8NP26 | MNTAPFKLEADFASALPTMAAPWQGEEAPNPELVILNDDLAYSLGLDPTWLRTPEGVQFLLGLNPEPLTKAVAQAYSGHQFGQFVASLGDGRALLLGEARSADGVLHDIHLKGSGRTQFSRGADGRAVLGPVLREYIISEAMHALGVPTTRSLAVISTGRKIQRGSVAPGAVLVRVATSLIRVGSFQYSNISGGIELSQHLANYTITRHFPSLVAELSAPTPATYVSLFKAILQRQADTVGKWTRLGFVHGALNTDNTLISGETVDYGPCAFMERYRGDAKFSSIDTYGRYKFENQPMILGWNMARLVETLLPLLGATPD... | Function: Catalyzes the transfer of adenosine 5'-monophosphate (AMP) to Ser, Thr or Tyr residues of target proteins (AMPylation).
Catalytic Activity: ATP + L-tyrosyl-[protein] = diphosphate + O-(5'-adenylyl)-L-tyrosyl-[protein]
Sequence Mass (Da): 51595
Sequence Length: 474
EC: 2.7.7.108
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Q1LM83 | MCTHTGHSAAPSLSGLIDAEPCHFWLPLMPNEPTDVLPPTSFNVPFGTRPGIAALGERFFTRLSPTPLPSPYLVSVAPAAAALLGWNETDLQDAVKDPAFIDSFVGNAVPDWADPLATVYSGHQFGVWAGQLGDGRAIRLAEAQTPGGPWEIQLKGGGLTPYSRMADGRAVLRSSIREYLCSEAMYALGVPTTRALSIIGSDAPVRRETIETSAVVTRLAPSFIRFGHFEHFAAREDHASLRQLADFVIDNFYPACRNAANPYQALLRDVSLLTADMVAHWQAVGFCHGVMNTDNMSILGLTIDYGPFGFLDAFDANHIC... | Function: Catalyzes the transfer of adenosine 5'-monophosphate (AMP) to Ser, Thr or Tyr residues of target proteins (AMPylation).
Catalytic Activity: ATP + L-tyrosyl-[protein] = diphosphate + O-(5'-adenylyl)-L-tyrosyl-[protein]
Sequence Mass (Da): 60199
Sequence Length: 544
EC: 2.7.7.108
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Q11T54 | MEHLHRKQITNTFTETFPGDLSMNNTTRQTPGVLYCSVLPTPVHHPQLLAWSADVAEMLGLESPVPEDVLILGGNTVNPTMKPYASCYAGHQFGNWAGQLGDGRAISLGFCSGKDSMEYELQLKGAGPTPYSRNSDGRAVLRSSLREYLMSEAMHYLGVPTTRALSLVSTGDAVLRDMFYNGHAAYEPGAVVLRVAPSFIRFGNFEILAERNNRDLSQQLCDWVITRYYPEIRGEDRVVQLFQAVAERTADMVVQWLRVGFVHGVMNTDNMSILGVTIDYGPYSFVDEYDARFTPNTTDLPGRRYAFGNQAAVAYWNLGR... | Function: Catalyzes the transfer of adenosine 5'-monophosphate (AMP) to Ser, Thr or Tyr residues of target proteins (AMPylation).
Catalytic Activity: ATP + L-tyrosyl-[protein] = diphosphate + O-(5'-adenylyl)-L-tyrosyl-[protein]
Sequence Mass (Da): 57994
Sequence Length: 515
EC: 2.7.7.108
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Q6PBD1 | MARSSGPLCLLLLGGLVAGILSGASADGNGLPSKKLKMQYTAGPLLKFQICVSUGYRRVFEDYMRVISQRYPDIRIEGENYLPHPIYRNIASFLSVFKLVLIGLIIAGKDPFAFFGMQAPSVWQWGQENKVYACMMVFFVSNMIENQCMSTGAFEITLNDVPVWSKLESGHLPSVQQLVQIIDNEMKLNVHMDAIPHHHRS | Function: Selenoprotein with thioredoxin reductase-like oxidoreductase activity.
PTM: May contain a selenide-sulfide bond between Cys-51 and Sec-54. This bond is speculated to serve as redox-active pair (By similarity).
Location Topology: Single-pass membrane protein
Catalytic Activity: [thioredoxin]-dithiol + NADP(+) ... |
A0KKE6 | MSALPLATDYARIFLDDVPLIDLRAPIEFKEGAFPCSTNLPLMTDDERAQVGTCFKQQGQAAAIALGHQLVGGAVRAERLEGWLAQLRRQPDAVLYCFRGGLRSQTVQQWLHEAGVTRPRIAGGYKDLRRFLIDTLDGAAAECQWTVLTGMTGSGKTHMLAEVAQALDLEGHAHHRGSSFGQLPGGQPSNINFENNLAIELLKRRHQGEQAFVVEDESRLIGRCCLPNPLFDAMSQAPLVVVEVPQEERAEQIRQDYVHDLWLRYQAMFGAEEGWPLFAAYLTDALARLKRRLGDQAHRELDTLMQSALAEQASSGDTSL... | Function: Involved in the post-transcriptional modification of the uridine at the wobble position (U34) of tRNA(Lys), tRNA(Glu) and tRNA(Gln). Catalyzes the conversion of 2-thiouridine (S2U-RNA) to 2-selenouridine (Se2U-RNA). Acts in a two-step process involving geranylation of 2-thiouridine (S2U) to S-geranyl-2-thiour... |
C1DNN5 | MRADTADYPQLFLEDVPMMDTRAPVEFAGGAFPNVLNLPLMTDSERQKVGTCYKQHGQRAAIELGHRLVSGRTKELRIQAWADFARAHPEGYLYCFRGGLRSQIVQQWLRDEAGIDYPRVTGGYKAMRNFLLDTTRQATAQCAFVLVGGLTGTGKTEVIAALGNALDLEGHANHRGSSFGKRATPQPAQIDFENRLAIDILRKRAAGVGRFVLEDESRLVGSCSLPLELHQGMQRYPLVWLEDSFEGRVERILRDYVVDLCAEFVAVEGPQAGFAAFAARLTQSLANIVKRLGGERYQRLSTLMARALAEQEAGRGVALH... | Function: Involved in the post-transcriptional modification of the uridine at the wobble position (U34) of tRNA(Lys), tRNA(Glu) and tRNA(Gln). Catalyzes the conversion of 2-thiouridine (S2U-RNA) to 2-selenouridine (Se2U-RNA). Acts in a two-step process involving geranylation of 2-thiouridine (S2U) to S-geranyl-2-thiour... |
Q6MK43 | MSLKNIKPDQLKNLFQQNIPLMDVRAPVEFSQGSIPGAVNLPVMNDDERAQVGTVYKNQGNEAAVKLGHELVSGLVKEQRVAAWKSFVQAHPEAVFYCFRGGQRSRISQAWLKEAGVERPLLVGGFKAARNYLIKQIEEFSVRQELISVSGPTGSGKTHFLRGLKGCPVIDLEALARHRGSAFGNWEVPQPTQVDYENNLAREILLLEDKIHGKIKPLVEDESRLIGRISQPATFFIRLRSSPVIWIDEPLPVRVDNVFDDYILNSSIGKSLEAAPRCAEENDILRAQALQLFARYRQSLLAIQRKLGGLRAQEVMADLE... | Function: Involved in the post-transcriptional modification of the uridine at the wobble position (U34) of tRNA(Lys), tRNA(Glu) and tRNA(Gln). Catalyzes the conversion of 2-thiouridine (S2U-RNA) to 2-selenouridine (Se2U-RNA). Acts in a two-step process involving geranylation of 2-thiouridine (S2U) to S-geranyl-2-thiour... |
Q1R084 | MSLPHLAPEMALLERPLIDVRAPVEFARGALPGAVNLPLMDDAERHAVGIRYKEAGQGAAIALGERLVDGDLKARRVAAWRAFAERHPDAVIYCFRGGLRSRIAQQWLQEAGITLPRIQGGWKAMRQCVNAEIEAAAARPVLVVAGLTGCAKTELVQSLDVGIDLEGHARHKGSAFGRHPLQGPSQIDFEHALGAALSHATHGCVVEDESRMIGQLDIPLSFWQTMETAPRIRVEMPLDWRLEQIRKDYIDTLWRTYRDHYGEWLGWSLMRKQLSSALKRVRKRLGSARFQRLQRLQALAFREHQRGNTQAHEAWLAPLM... | Function: Involved in the post-transcriptional modification of the uridine at the wobble position (U34) of tRNA(Lys), tRNA(Glu) and tRNA(Gln). Catalyzes the conversion of 2-thiouridine (S2U-RNA) to 2-selenouridine (Se2U-RNA). Acts in a two-step process involving geranylation of 2-thiouridine (S2U) to S-geranyl-2-thiour... |
Q488J6 | MSINTSGKITSATERADSADFRTIIRNKIPLMDVRAPVEFGKGAFDLSINYPLMNNDERADVGICYKQNGQEAAIKLGNALVSGQSKARRLTQWQTFARENPQGYLYCFRGGLRSQTVQRWLKESGINYPLITGGYKALRQFLLNELEQLALHPLTILAGNTGSGKTPFLAHCANSLDLEGAAGHRGSSFGSFVTPQSNQINFENKLAEQYIRGDFSLEQRLVLEDEGRLIGSVHLPESLRNAMTLAPLVVIEESLEYRLEQIYQEYIIKMTAQYQAAYGVEQGFTAFSEYLEHGLFKVRKRLGTQRYGQLKEIQSTALT... | Function: Involved in the post-transcriptional modification of the uridine at the wobble position (U34) of tRNA(Lys), tRNA(Glu) and tRNA(Gln). Catalyzes the conversion of 2-thiouridine (S2U-RNA) to 2-selenouridine (Se2U-RNA). Acts in a two-step process involving geranylation of 2-thiouridine (S2U) to S-geranyl-2-thiour... |
Q04675 | MATTDIISLVKNNLLYFQMWTEVEILQDDLSWKGNSLRLLRGRPPHKLSNDVDTEHENSLSSPRPLEFILPINMSQYKENFLTLECLSQTFTHLCSPSTERILLAIINDDGTIVYYFVYKGVRKPKRN | Function: Non-catalytic subunit of the tRNA-splicing endonuclease complex, a complex responsible for identification and cleavage of the splice sites in pre-tRNA. It cleaves pre-tRNA at the 5' and 3' splice sites to release the intron. The products are an intron and two tRNA half-molecules bearing 2',3' cyclic phosphate... |
Q9M1E8 | MAPRWKWKGAEAKALAEPVSKTVSELRSSLTQTEALGFLSSCNVLLSVESEEAELLDRCCFGRLVVGAEKDKRWIQLSFEEAFFLFYKLKCIKICLHGRSLENEVDLWRSMSSFKQDFAILYKAYSHLRSKNWIVRSGLQYGVDFVVYRHHPSLVHSEYAVLVQSIGGNDRLKVWSDIHCSVRLTGSVAKSLLVLYVNRKVNTEKMNLPLCLEDYTVEEQTIRRWSPELSREDETRT | Function: Constitutes one of the two catalytic subunit of the tRNA-splicing endonuclease complex, a complex responsible for identification and cleavage of the splice sites in pre-tRNA. It cleaves pre-tRNA at the 5'- and 3'-splice sites to release the intron. The products are an intron and two tRNA half-molecules bearin... |
Q5ZIN2 | MAEAAFHPPRRKRRVFECYQAPFPVGPGAGDFRMCRADMVNNCVVVRSPEDMDQLYNKGYFGKGILSRSRPVYSISDPSLVSKWQGANLNVPIITSKKYQQRVQWAKSALQEQGFDGCSVTKILENYTRPLEFPFLEKGGAEQTGDSCDTVCPNTENTELSGQSSTDTGNIATSSPECQKEVCQKAYAEGDPASDSMVGSKEQEPADVKETAQTSCQMHGSCMHCGCKAKGAPDRESCNMAKSRERAPEYVLVQEEEESSLCPEEGSAREQENFVKKEKLVCRRNPFRIFEYLQLSLEEAFFLVYALGCLTVYYGEEPLT... | Function: Constitutes one of the two catalytic subunit of the tRNA-splicing endonuclease complex, a complex responsible for identification and cleavage of the splice sites in pre-tRNA. It cleaves pre-tRNA at the 5'- and 3'-splice sites to release the intron. The products are an intron and two tRNA half-molecules bearin... |
Q8NCE0 | MAEAVFHAPKRKRRVYETYESPLPIPFGQDHGPLKEFKIFRAEMINNNVIVRNAEDIEQLYGKGYFGKGILSRSRPSFTISDPKLVAKWKDMKTNMPIITSKRYQHSVEWAAELMRRQGQDESTVRRILKDYTKPLEHPPVKRNEEAQVHDKLNSGMVSNMEGTAGGERPSVVNGDSGKSGGVGDPREPLGCLQEGSGCHPTTESFEKSVREDASPLPHVCCCKQDALILQRGLHHEDGSQHIGLLHPGDRGPDHEYVLVEEAECAMSEREAAPNEELVQRNRLICRRNPYRIFEYLQLSLEEAFFLVYALGCLSIYYEK... | Function: Constitutes one of the two catalytic subunit of the tRNA-splicing endonuclease complex, a complex responsible for identification and cleavage of the splice sites in pre-tRNA. It cleaves pre-tRNA at the 5'- and 3'-splice sites to release the intron. The products are an intron and two tRNA half-molecules bearin... |
Q9P6Y2 | MAENMTIATMAQPSESPSKSGEEAPASTNPAATSAPPRPPRVPYHQIYKLPAPIRTFPLPTFYPSNPLSLFHLAVAWLRQVLLPPPAEPSVIHEGIWDPDTRSVHVKDPKSIRALWEQGFYGKGSLSRSEPNWFKRELSRRGLDGTTVSEERTASRREERRQVKWERAKAELEAIEKQKHEEAKLNSETVNAAIPEPPAAEIEPEPEVLLSSLPDHVLSATSTIPLSRAAPTNEFVPKTVAHGHVEPKPPVGPLELLALPNSYALVRGEELALSQPEPAPTEENVRKELKAPVGPIELLALPNSLVDLVALSVVSVLSED... | Function: Constitutes one of the two catalytic subunit of the tRNA-splicing endonuclease complex, a complex responsible for identification and cleavage of the splice sites in pre-tRNA. It cleaves pre-tRNA at the 5'- and 3'-splice sites to release the intron. The products are an intron and two tRNA half-molecules bearin... |
Q5Z6B1 | MDLPGPRWKKGKDGKDFASLAAANPMSAIVSELKASFISSKPVAILSGPGGSAVLGVGPEQAVILNRAAFGHAIENATAQKHWFQLSPEEVFYLCHALNCIRVDSLDNKQMSEIELWDYFRSGSESFPEMYKAYAHLRLKNWVVRSGLQYGADFVAYRHHPALVHSEFAVVVVPEGAEFGNRCGRLEVWSDLLCALRASGSVAKTLLVLTISSSSKCELSSPDCLEQLVVHERTITRWILQQCREQRCEPSRDEVNREELIIEKESVVFNHWGVILGFTVLSGLLVYRLKFRQ | Function: Constitutes one of the two catalytic subunit of the tRNA-splicing endonuclease complex, a complex responsible for identification and cleavage of the splice sites in pre-tRNA. It cleaves pre-tRNA at the 5'- and 3'-splice sites to release the intron. The products are an intron and two tRNA half-molecules bearin... |
Q8TFH7 | MSKNHEVYKDALPISLAYPLPPIILTNPLTWIPYIYRYLFRKTPRQVQWQCQLHESDLSCVVTDSEAIKKFWTSGFFGKGNLSRSEPTWHTRTKRSLGLLGFDEDLVAEEVTARRRFQRKQFKAQRAYRENRARERQLLLENGKPIPASLEEDAELPEYLTKSLKDFSRVSENPYHITSVPNVEHLQLTFPEAFFLASLGVLRINYENPNFELLPILKLFANIVANSVALTHDYSLQQSHEDPIIEPDNKFLTELAAYFYFRQQGWVVKNGTKFSVDFLLYKKGPVFSHAEFAILLIPCVGNKQKYNMQWHEVHCLNRVI... | Function: Constitutes one of the two catalytic subunit of the tRNA-splicing endonuclease complex, a complex responsible for identification and cleavage of the splice sites in pre-tRNA. It cleaves pre-tRNA at the 5'- and 3'-splice sites to release the intron. The products are an intron and two tRNA half-molecules bearin... |
P16658 | MSKGRVNQKRYKYPLPIHPVDDLPELILHNPLSWLYWAYRYYKSTNALNDKVHVDFIGDTTLHITVQDDKQMLYLWNNGFFGTGQFSRSEPTWKARTEARLGLNDTPLHNRGGTKSNTETEMTLEKVTQQRRLQRLEFKKERAKLERELLELRKKGGHIDEENILLEKQRESLRKFKLKQTEDVGIVAQQQDISESNLRDEDNNLLDENGDLLPLESLELMPVEAMFLTFALPVLDISPACLAGKLFQFDAKYKDIHSFVRSYVIYHHYRSHGWCVRSGIKFGCDYLLYKRGPPFQHAEFCVMGLDHDVSKDYTWYSSIA... | Function: Constitutes one of the two catalytic subunit of the tRNA-splicing endonuclease complex, a complex responsible for identification and cleavage of the splice sites in pre-tRNA. It cleaves pre-tRNA at the 5'- and 3'-splice sites to release the intron. The products are an intron and two tRNA half-molecules bearin... |
Q754T3 | MPHTKVAISLNSKTGVPLVFDLDDVRRIRGLGVLGTLCGSLPTAAQQNLFLTVPLRLMLEDAVWLVLSGHAYFSFDDKLLVQAAGSLTAAEVCRWRQDTERGLEQQRELRRREQQLKLAALHRTADETDTQRRLLEQSLFLETENCSKMIAAAEPAGLQLAILREMVAQHLDLGNYLIYRYLREEQYFLSAGGRFGARYVAYPGDPLRYHSHMAVQPAMDYYNESLDLLHVVGGGRLGTGVKKLWVVGGVRYREAEAAATAEEQIPPPDTLDRLLATSPPVSVFSIEWSGFG | Function: Constitutes one of the two catalytic subunit of the tRNA-splicing endonuclease complex, a complex responsible for identification and cleavage of the splice sites in pre-tRNA. It cleaves pre-tRNA at the 5'- and 3'-splice sites to release the intron. The products are an intron and two tRNA half-molecules bearin... |
Q9BSV6 | MLVVEVANGRSLVWGAEAVQALRERLGVGGRTVGALPRGPRQNSRLGLPLLLMPEEARLLAEIGAVTLVSAPRPDSRHHSLALTSFKRQQEESFQEQSALAAEARETRRQELLEKITEGQAAKKQKLEQASGASSSQEAGSSQAAKEDETSDGQASGEQEEAGPSSSQAGPSNGVAPLPRSALLVQLATARPRPVKARPLDWRVQSKDWPHAGRPAHELRYSIYRDLWERGFFLSAAGKFGGDFLVYPGDPLRFHAHYIAQCWAPEDTIPLQDLVAAGRLGTSVRKTLLLCSPQPDGKVVYTSLQWASLQ | Function: Constitutes one of the two catalytic subunit of the tRNA-splicing endonuclease complex, a complex responsible for identification and cleavage of the splice sites in pre-tRNA. It cleaves pre-tRNA at the 5'- and 3'-splice sites to release the intron. The products are an intron and two tRNA half-molecules bearin... |
P42207 | MADTKGFSSIETPGYVGFANLPNQVHRKSVKKGFEFTLMVVGESGLGKSTLVNSLFLTDLYPERIIPDAIEKQKQTVKLEASTVEIEERGVKLRLTVVDTPGFGDAIDNSNSFGAILEYIDEQYERFLRDESGLNRRNIVDNRIHCCFYFISPFGHGLKPLDVEFMKKLHSKVNIVPVIAKADCLTKKEILRLKCRIMQEIESHGIKIYPLPDCDSDEDEDYKEQVKQLKEAVPFAVCGANTLLEVKGKKVRGRLYPWGVVEVENPDHCDFIKLRTMLITHMQDLQEVTQEVHYENYRSDRLAKGIKGKENGVKAERDSS... | Function: Involved in cytokinesis (Probable). May be involved in p53-dependent apoptosis .
PTM: Ubiquitinated by park, leading to its degradation by the proteasome.
Sequence Mass (Da): 41131
Sequence Length: 361
Subcellular Location: Cytoplasm
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Q08DM7 | MSKGLPETRTDAAMSELVPEPRPKPAVPMKPIGINPNLLGYIGIDTIIEQMRKKTMKTGFDFNIMVVGQSGLGKSTLVNTLFKSQVSRKASSWNREEKIPKTVEIKAIGHVIEEGGVKMKLTVIDTPGFGDQINNENCWEPIEKYINEQYEKFLKEEVNIARKKRIPDTRVHCCLYFISPTGHSLRPLDLEFMKHLSKVVNIIPVIAKADTMTLEEKSEFKQRVRKELEVNGIEFYPQKEFDEDLEDKTENDKIRESMPFAVVGSDKEYQVNGKRVLGRKTPWGIIEVENLNHCEFALLRDFVIRTHLQDLKEVTHNIHY... | Function: Filament-forming cytoskeletal GTPase (By similarity). May play a role in cytokinesis (Potential).
PTM: Phosphorylated by PKG on serine residues. Phosphorylated by PKG on Ser-91 (By similarity).
Sequence Mass (Da): 40538
Sequence Length: 357
Subcellular Location: Cytoplasm
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Q9UH03 | MSKGLPETRTDAAMSELVPEPRPKPAVPMKPMSINSNLLGYIGIDTIIEQMRKKTMKTGFDFNIMVVGQSGLGKSTLVNTLFKSQVSRKASSWNREEKIPKTVEIKAIGHVIEEGGVKMKLTVIDTPGFGDQINNENCWEPIEKYINEQYEKFLKEEVNIARKKRIPDTRVHCCLYFISPTGHSLRPLDLEFMKHLSKVVNIIPVIAKADTMTLEEKSEFKQRVRKELEVNGIEFYPQKEFDEDLEDKTENDKIRQESMPFAVVGSDKEYQVNGKRVLGRKTPWGIIEVENLNHCEFALLRDFVIRTHLQDLKEVTHNIH... | Function: Filament-forming cytoskeletal GTPase (By similarity). May play a role in cytokinesis (Potential).
PTM: Phosphorylated by PKG on serine residues. Phosphorylated by PKG on Ser-91 (By similarity).
Sequence Mass (Da): 40704
Sequence Length: 358
Subcellular Location: Cytoplasm
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Q9Z1S5 | MSKGLPEARTDAAMSELVPEPRPKPAVPMKPVSINSNLLGYIGIDTIIEQMRKKTMKTGFDFNIMVVGQSGLGKSTLVNTLFKSQVSRKASSWNREEKIPKTVEIKAIGHVIEEGGVKMKLTVIDTPGFGDQINNENCWEPIEKYINEQYEKFLKEEVNIARKKRIPDTRVHCCLYFISPTGHSLRPLDLEFMKHLSKVVNIIPVIAKADTMTLEEKSEFKQRVRKELEVNGIEFYPQKEFDEDLEDKTENDKIRQESMPFAVVGSDKEYQVNGKRVLGRKTPWGIIEVENLNHCEFALLRDFVIRTHLQDLKEVTHNIH... | Function: Filament-forming cytoskeletal GTPase (By similarity). May play a role in cytokinesis (Potential).
PTM: Phosphorylated by PKG on serine residues. Phosphorylated by PKG on Ser-91 (By similarity).
Sequence Mass (Da): 40038
Sequence Length: 350
Subcellular Location: Cytoplasm
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B4EB45 | MRVFNFSAGPAAMPEEVLRQAADEMLDWHGSGMSVMEMSHRGKEFMSIHEAALTDLRDLLGVPASHRILFLQGGGIAENAIVPMNLLGARNTADFVVTGSWSQKSFGEAKKFCTPHLAASGKTENGFTRAPTRAEWQLSDDPAYVHLCTNETIDGVETFEIPDLGDVPLVADVSSHILSRPMDVAKYGVLFGGAQKNIGMAGVTVVIVREDLLDRALSICPSAFEWKTIAANNSLYNTPPTYAIYIAGLVFQWLKRQGGLEAIEARNIEKSKLLYDTIDASSFYLNKVEPAARSRMNVPFFLADETRNEDFLAGAKARGL... | Cofactor: Binds 1 pyridoxal phosphate per subunit.
Function: Catalyzes the reversible conversion of 3-phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-phosphonooxybutanoate to phosphohydroxythreonine.
Catalytic Activity: 2-oxoglutarate + O-phospho-L-serine = 3-phosphooxypyruvate + L-glutamate
Sequence M... |
P91856 | MAAPGRKINFAAGPAKLPEEVLLKMQEEQLNFNNLGVSVIEMSHRSKEFGALLNETISLIRELMNVPDNFEILFMQGGGTGQFAAIPLNLKGDHEHADYIVTGAWSSKAADEAGKYINVKKVFQPSKPYVTVPDQENWVHDEKAAYLYYCANETVHGIEFTPTAPESHNVPLVADVSSNFMARPFDFKDHGVVFGGAQKNLGAAGLTIVIVRKDLIGKQQAITPSVFSYKEMIANNSLYNTPPTGGIYTTNLVLKWIKSKGGLQAIYELNLQKSGMIYDIIDNSNGFYHCAVDKRYRSIMNVCFRIGGPSGNDELEEKFL... | Cofactor: Binds 1 pyridoxal phosphate per subunit.
Function: Catalyzes the reversible conversion of 3-phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-phosphonooxybutanoate to phosphohydroxythreonine.
Catalytic Activity: 2-oxoglutarate + O-phospho-L-serine = 3-phosphooxypyruvate + L-glutamate
Sequence M... |
Q9PIH3 | MRKINFSAGPSTLPLEILEQAQKELCDYQGRGYSIMEISHRTKVFEEVHFGAQEKAKKLYELNDDYEVLFLQGGASLQFAMIPMNLALNGVCEYANTGVWTKKAIKEAQILGVNVKTVASSEESNFDHIPRVEFSDNADYAYICSNNTIYGTQYQNYPKTKTPLIVDASSDFFSRKVDFSNIALFYGGVQKNAGISGLSCIFIRKDMLERSKNKQIPSMLNYLTHAENQSLFNTPPTFAIYMFNLEMDWLLNQGGLDKVHEKNSQKATMLYECIDLSNGFYKGHADKKDRSLMNVSFNIAKNKDLEPLFVKEAEEAGMIG... | Cofactor: Binds 1 pyridoxal phosphate per subunit.
Function: Catalyzes the reversible conversion of 3-phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-phosphonooxybutanoate to phosphohydroxythreonine.
Catalytic Activity: 2-oxoglutarate + O-phospho-L-serine = 3-phosphooxypyruvate + L-glutamate
Sequence M... |
A8FVN8 | MSTTYNFCAGPAMLPQAVMKKAQSELLDWNGLGTSVMEISHRSKEFIALTDKAETDLRELMSIPENYHVLFMHGGGRGQFSAVVNNFLGENGKALYLVSGSWSKSAVDEARKLTSDAQIDTLDLVVNDNGIGAVSIPELTGEAADYRYLHYCPNETVDGIEIFEDINSPWPIVADMSSNIMSREIDVSKFGLIYAGAQKNIGPSGLSIVIVRDDMLELPSLPQSSIMDYRLAVKHGSMYNTPPTFAWYLAAEVFKWLKSSGGVATMAEVNAKKAQLLYDFIDGSNFYNNTVSAQNRSLMNVIFYLANEDNNADFLAEASR... | Cofactor: Binds 1 pyridoxal phosphate per subunit.
Function: Catalyzes the reversible conversion of 3-phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-phosphonooxybutanoate to phosphohydroxythreonine.
Catalytic Activity: 2-oxoglutarate + O-phospho-L-serine = 3-phosphooxypyruvate + L-glutamate
Sequence M... |
B2FKF0 | MTRAFNFSAGPATLPESVLRQAQAEMLDWHGSGASIVEMSHRGAEFMSVAAEAEADLRRLLDIPDDYAVLFLSGGATTQQALIPLNFAAPGQRADYVVSGHWGKTAVKQAGVYVDVNIAASSEANGYRELPARADWQLSRDAAYVHITANETIHGVEFRDVPDTGNVPLIADFSSSIASEPLDVRRYGVIYAGAQKNLGPVGVAVMIIRRDLLERSGQPRADIFDYRSHVARDSMLNTPPTWNWYLAGLVFKWMLAEGGVTEFAKRNAAKAALVYGAIDGSGGFYRNEVAYAARSRMNIPFFLPDAELDARFVAEAKAAG... | Cofactor: Binds 1 pyridoxal phosphate per subunit.
Function: Catalyzes the reversible conversion of 3-phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-phosphonooxybutanoate to phosphohydroxythreonine.
Catalytic Activity: 2-oxoglutarate + O-phospho-L-serine = 3-phosphooxypyruvate + L-glutamate
Sequence M... |
Q5AZY3 | MPSSKARSSPSVDRRERLTLAKLASYDDVATDALVDCAYFWTKTRKNRTKYIPVRGLAEDTVAHILLHDVIVAKDVSAAERKILDLIGMKRYLAKLPNDREKDWFRKHLRKYIQMYLPDCPFEVTTTNRYTITEHEAAICARKFIPQGQEIKYLSGTLVPMTKEEERDLDLKRKDFSIVMSSRRKTPSFFLGPARFANHDCSANGRLVTRGSEGMQVVATRDIYIGEEITVSYGEDYFGIDNCECLCLSCERVPRNGWSQNLAPGPQSKPSTPEPKASEDHLTPRKRKAQSDIDSDSSPSSTPRKRGKFTPRGSKLRSQL... | Function: Histone methyltransferase that trimethylates 'Lys-20' of histone H4 to form H4K20me3.
Catalytic Activity: L-lysyl(20)-[histone H4] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl(20)-[histone H4] + 3 S-adenosyl-L-homocysteine
Sequence Mass (Da): 71748
Sequence Length: 641
Subcellular L... |
Q4I8C9 | MAPSQTANKKPRMTLAQVSAYDDILTDALVDHVFYWTTVPKNRTSYHPSRGVKEEEISKILQEEVVLKKDLDSAEKRLLTTNGLKRFHNGLKTDKEKDDFRKHLRRYVQIYLPDCPWEVSSTNRYTIVSHEAAVTARRAIRRNEAIKYLSGVQVVITPEEEMAISSQKKDFSIVVSSRSKCTSLFMGPARFANHDCDANAKLMRTSHAGIEIVATRPIDAGEEITVTYGDNYFGENNCECLCKTCEDLLRNAWEPEEGTVPVQTGIGQSLSDGYSLRRRRRDDSISGSSRTPSVTPDMRPRITKANSRGSLLARDTSSVR... | Function: Histone methyltransferase that trimethylates 'Lys-20' of histone H4 to form H4K20me3.
Catalytic Activity: L-lysyl(20)-[histone H4] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl(20)-[histone H4] + 3 S-adenosyl-L-homocysteine
Sequence Mass (Da): 74100
Sequence Length: 662
Subcellular L... |
Q7SBJ9 | MTKPQGTGGKKKNQLTLAQLAAYDDILTDALVDHAYYWTTIPKNRTSYHPSRGIKEEEITKIIQNHLIVDPDIATAEEKLLATDGLKRFCNTLKTPREQNDFKAHLRRYMSIYLPDCPFEVNATNRYTIVTYEASITARRFIQRNETIKYLAGIQVVITPEEELEMSLRKKDFSLIVSSRSKSTSLFMGPARFANHDCNANARLITRGQAGIEIIACRNIEVGEEITVTYSESYFGENNCDCLCATCESNLRNGWRPVDGEAAVQKSIEDEQPTESSTPYSFRRKRRYGSTALQASRTPSVTPDMRPRVLRKSQSQMMLG... | Function: Histone methyltransferase that trimethylates 'Lys-20' of histone H4 to form H4K20me3.
Catalytic Activity: L-lysyl(20)-[histone H4] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl(20)-[histone H4] + 3 S-adenosyl-L-homocysteine
Sequence Mass (Da): 86094
Sequence Length: 777
Subcellular L... |
Q0U3A4 | MPPSKAEKRGLTLEKLASYDDVITDALVDKIYYWATIRKNRGTRFTASRGLQEEDIAGVIREQVIWDKDPVEAVQQLLDLPGLRKYMKGLRDEKDQDQFKRHLRRYVNIYMPDCPFEVTTTNRYTITDHEASITARRDINPREEIKYLTGVQVAMTEEQEKTLELARKDFSLVISSRKKTRSLFLGPARFANHDCDANARLSTKGYDGMQIVAVKPINEGDEITVSYGDDYFGDNNEECLCHTCEDRQQNGWAPMKRVEDSDDEDMEEAESPVENPSEATSSGTATSGGKRARDITEEDAGADLPPTSKRARIEKKPSPT... | Function: Histone methyltransferase that trimethylates 'Lys-20' of histone H4 to form H4K20me3.
Catalytic Activity: L-lysyl(20)-[histone H4] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl(20)-[histone H4] + 3 S-adenosyl-L-homocysteine
Sequence Mass (Da): 75177
Sequence Length: 662
Subcellular L... |
Q9USK2 | MRQTNTHLETFSLFDDVCTCLLVDKVFYWSQIHKVRKLVDRSIERMESCSIINIITKYIIEQTDLDQAAKNILQFRELDPLLRRLSSTSLLAFTRHLKYYLSLYLPSCKFEICSTNQYFSSSKPEACVIARESINAGEDITDLCGTIIKLSPKEERNIGIGKDFSILHSSRLDSMCLFLGPARFVNHDCNANCRFNTSGKRIWLRCVRDIKPGEEITTFYSSNYFGLENCECLCVSCERMGINGFKKLFHTSATSTSCSSKSSSDVSDLSSLPQSNRYVISEEDRSFLNIWDSGGELSDASSSDLDEEFSLFIPRHKKRV... | Function: Histone methyltransferase that specifically trimethylates 'Lys-20' of histone H4 to form H4K20me3. H4 'Lys-20' methylation is apparently not involved in the regulation of gene expression or heterochromatin function but participates in DNA damage response by giving a 'histone mark' required for the recruitment... |
Q6C519 | MITVTPGELATIDDALTDLLLERVFYWAEVRKASVHYKPLRGISDRHIHDLVRSIAACETGAAANLAVKKATNAFLELKEVRGYRGRLSPLAYEEFQRHTVRYLTIYKASCGFEINVSMRYKCRSNRGESCVISRVRYNRGDEIVGLSGCLAKMTKDEELALANDFSVLHSSRRGGNCLMLGPARFVNHDCSANARFVPVPSGMVIQAVKPINVGDEITVKYAENYFGRRNKECLCQTCEENSRGLYGSPQESSEEESDDDMDELTKIELQRRKKRQEQREGGTPELREGGRGSSESSRETSEEAIEISTSKNWPLIPKI... | Function: Histone methyltransferase that trimethylates 'Lys-20' of histone H4 to form H4K20me3.
Catalytic Activity: L-lysyl(20)-[histone H4] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl(20)-[histone H4] + 3 S-adenosyl-L-homocysteine
Sequence Mass (Da): 96798
Sequence Length: 866
Subcellular L... |
P31675 | MIWIMTMARRMNGVYAAFMLVAFMMGVAGALQAPTLSLFLSREVGAQPFWIGLFYTVNAIAGIGVSLWLAKRSDSQGDRRKLIIFCCLMAIGNALLFAFNRHYLTLITCGVLLASLANTAMPQLFALAREYADNSAREVVMFSSVMRAQLSLAWVIGPPLAFMLALNYGFTVMFSIAAGIFTLSLVLIAFMLPSVARVELPSENALSMQGGWQDSNVRMLFVASTLMWTCNTMYIIDMPLWISSELGLPDKLAGFLMGTAAGLEIPAMILAGYYVKRYGKRRMMVIAVAAGVLFYTGLIFFNSRMALMTLQLFNAVFIGI... | Function: Involved in the efflux of sugars. The physiological role may be the detoxification of non-metabolizable sugar analogs. Can transport IPTG, lactose and glucose. Has broad substrate specificity, with preferences for glucosides or galactosides with alkyl or aryl substituents.
Location Topology: Multi-pass membra... |
Q5ZU30 | MYKIYSYLGWRIDMKTENLPQAGQEAQIDKKIHFIWVGHIMPQKNIQVVSEWAEKNPGYETIIWVDKKIAPAKELDLFILDMKSKGITVKDINEEGVCRDSIRHELDQESPNYGMVSDMLRLNILAAEGGIYLDSDILCSAPFPDEIYAPFGFLLSPWSQGANNTLCNDIILCSKGNQIIQQLADAIEQSYIARDSFEFTHEYASMKETKGERIAKTLGVTGPGFLFHQLKKMGILNDKSEMEAIHWELQDQRYLIDGSVKEPDYFYVPQNNTNDASWVPSIKRPGIENMSFQERLENAVQLIAFDIQKTGLFNLDHYAN... | Function: Secreted effector that interferes with vesicular trafficking of host cells. Possesses glucohydrolase and mono-O-glucosyltransferase activity by using UDP-glucose as a sugar donor substrate. Is able to glucosylate histones H4 and H3.1 in vitro, but it is unlikely that histones are the natural substrates for Se... |
Q06ZW3 | METEADTAKTFWSEVDVDGVFDELMEVLRRLRHTLRHNTATDREYVQAMRIVQESKLIRTETEDVLLDEDILTVTVSEPQCSPESLQNGIEPEDPQHSTARLYSDVGVVCSHMSSSRPDPAAPLVFQPHVCSSACVPHLPAHTHHLLGHNPLRAPLLCHFQRVCDDAGVVYKAPCGRSLSCMQEVLHFLLQTQSVCVLQTDRFSFSTQVCVERQVCAAPLLERDLSRGLEPVPVALVNTVDGARPREFRYRRERWPHGCFLSAEPLYSVCCDCTDGCTDAHSCACVRRTAGAAYTHQRLTHTLRTGLFECGPWCGCERSR... | Function: Histone methyltransferase involved in left-right axis specification in early development and mitosis. Specifically trimethylates 'Lys-9' of histone H3 (H3K9me3). H3K9me3 represents a specific tag for epigenetic transcriptional repression by recruiting HP1 (CBX1, CBX3 and/or CBX5) proteins to methylated histon... |
Q96T68 | MGEKNGDAKTFWMELEDDGKVDFIFEQVQNVLQSLKQKIKDGSATNKEYIQAMILVNEATIINSSTSIKGASQKEVNAQSSDPMPVTQKEQENKSNAFPSTSCENSFPEDCTFLTTENKEILSLEDKVVDFREKDSSSNLSYQSHDCSGACLMKMPLNLKGENPLQLPIKCHFQRRHAKTNSHSSALHVSYKTPCGRSLRNVEEVFRYLLETECNFLFTDNFSFNTYVQLARNYPKQKEVVSDVDISNGVESVPISFCNEIDSRKLPQFKYRKTVWPRAYNLTNFSSMFTDSCDCSEGCIDITKCACLQLTARNAKTSPL... | Function: Histone methyltransferase involved in left-right axis specification in early development and mitosis. Specifically trimethylates 'Lys-9' of histone H3 (H3K9me3). H3K9me3 is a specific tag for epigenetic transcriptional repression that recruits HP1 (CBX1, CBX3 and/or CBX5) proteins to methylated histones. Cont... |
Q6YI93 | MEQSANARQSTLRSRTQELNTLSVLSKDVSLEDAKKYWKDRQADGKVDWIFEKVLNKLKILWQKIKDGSATNLEYVRAVILVNEAGNLEEDLEEDLKEDTDTIHIDIHKENEVQENTDCSPERKEDTCLNLNTDCGTDVSGSEPECNSTVSPPAAERVYFGNHSCGPSCLSGINSFLFTKGNPLQLPISCDFQRCHLKINSPDDLSHILYKAPCGRSLRDYDEVHSYLTETGCHFLAVDNFSFNNHVRLDSNSSFNQGIVQDCDISNDVESVPVAFSNEIDNTRPSNFIYRKTSWPPGYSLNNFTDIFVKCCNCTDGCLD... | Function: Histone methyltransferase involved in left-right axis specification in early development and mitosis. Specifically trimethylates 'Lys-9' of histone H3 (H3K9me3). H3K9me3 is a specific tag for epigenetic transcriptional repression that recruits HP1 (CBX1, CBX3 and/or CBX5) proteins to methylated histones. Cont... |
D0NXM3 | MRAYFVLLVAATAILTYGGATATYSTSKGEMNLTGTVENNRPTRSLRVAPSGGNGEERSWSTIYGISRSKAETVRDWLMPRLNQGMDVQALAREMGITSRQAATQHQNWDALVKYLKMYNYAVRGEKMSKSMAESVLLHNVLTAKNNF | Function: Effector that suppresses flg22-induced post-translational MAP kinase activation in tomato but not in Arabidopsis. The perception of highly conserved pathogen- or microbe-associated molecular patterns (PAMPs/MAMPs), such as flg22, triggers converging signaling pathways recruiting MAP kinase cascades and induci... |
P61094 | AECMVDETVCYIHNHNNC | Function: Insecticidal toxin. Causes flaccid paralysis followed by death when injected into Heliothis virescens larvae. Does not induce any toxic effects when injected intravenously into adult mice at a dose of 1.1 mg/kg body weight.
PTM: Contains 4 disulfide bonds.
Sequence Mass (Da): 2095
Sequence Length: 18
Domain: ... |
Q9Y7U1 | MDNDYTTSTTTSRRPRFWGFFFILFPLVSFLMWTIGLIVLLGLWSTQDKWHTPSEPDPVYLSDMGAYTKGFFIPMCVITGVFYFLTFIMIRLARQWGWIYPTGRKVETYLGWFAALTGAAAASCLISLSIRDDVHHDNVHWKFTAAFVVLAFVSAASNIFEWLSATRYYPQSSLLRVSFIFKFVIIVVGIICAIAFGGLHHNYRGRSARFEWVVCFLWSIYICLLCLDLAPALFYDSLASAPDLEKGAYATSVPESYVAPMEPPAAVLPDGEERYATPDLVPDTTAQYPYASATEPGVSNIPETRPERPVVYNMDVSQTT... | Function: May control the production of phosphatidylinositol 4-phosphate (PI4P).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 36917
Sequence Length: 328
Subcellular Location: Cell membrane
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P35735 | MIQFKSPGNWLFIVPWIAFIPWYGMLIAMLICWASQGHPIYWFMHSEQFPVYISDIGATNLRPLFISCAGWQGLGYVITVALEFFQRSGYLPFQLKKKDPSISDSTSYAEKLHSGKYLMPPYYTKDERNLIFAAFVLGSIGELALLFSSIFSTALYHRVHIAMVSVFVVFMFLSTCCLIAEYFLMGRHYASVHPLASPHFNPQSSEKSFNQDYNTVDELPWYKWKGHVWNKFTISATLKVIWLTLAVVWAICFGAINDRSKSACFEWLLAFWFGIIFMILSADFYLGGRYRQSRYFNHVESFSGYYKYDKALGLYHSEDV... | Function: May control the production of phosphatidylinositol 4-phosphate (PI4P) by the STT4 PI 4-kinase. Mediates proper localization of STT4 to the plasma membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 40463
Sequence Length: 353
Subcellular Location: Cell membrane
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Q12314 | MKYIIEHMEEGFSEWVILEYSQILREVGAENLILSSLPESTTEKDIPQRLLKLGLRWTTKDLKGINEDFKDLELLKDGRVCLLDPRATIDLQPEDATKFDYFVFGGILGDHPPRDRTKELKTAYPNLLISRRLGDKQMTTDTAIRTTQLIIKDRIAFEDIKFIDYPEFRFNKNEATEMPFRYVLDKEGKPILPEGMLDLIKKDSAQSLDDLLM | Function: S-adenosyl-L-methionine-dependent protein-arginine N-methyltransferase that monomethylates ribosomal protein S3 (RPS3) at 'Arg-146'.
Sequence Mass (Da): 24744
Sequence Length: 213
Subcellular Location: Cytoplasm
EC: 2.1.1.-
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A0LNN5 | MADQQTTMPRWVPLLLGLLGSTTCGMLLYAWSVFIKPLNAEFGWSRAEIAMAFAICCLIFGLMTFPAGRLSDKMGPRKVVMTGGVLLAIGFILSGFIQSKYQLYITYGVIAGFGGGMIYLPPIATAPKWWPDRRALATGFAVVGLGLGSFLMGPLATYIIEKPGMGWRYVFWYCGVAMGIMALIAGAFLEPPPAGWKPAGYTPPAPPAGAAAPKVTRDWTYEEAKGDTKFWLLYLAYFCGSFAGLMVIGHLAGFGRDAGLTAMAAAGAVSSLAFSNAATRILSGWFVDKIGIRVYFAALFALQTAAMIAIFQLGGSVVGL... | Function: Proton-coupled L-lactate specific transporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 43800
Sequence Length: 412
Subcellular Location: Cell inner membrane
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P77468 | MKIPTTTDIPQRYTWCLAGICYSSLAILPSFLSYAESYFNPAFLLENGTSVADLSRFERGNHQPAGVYRVDLWRNDEFIGSQDIVFESTTENTGDKSGGLMPCFNQVLLERIGLNSSAFPELAQQQNNKCINLLKAVPDATINFDFAAMRLNITIPQIALLSSAHGYIPPEEWDEGIPALLLNYNFTGNRGNGNDSYFFSELSGINIGPWRLRNNGSWNYFRGNGYHSEQWNNIGTWVQRAIIPLKSELVMGDGNTGSDIFDGVGFRGVRLYSSDNMYPDSQQGFAPTVRGIARTAAQLTIRQNGFIIYQSYVSPGAFEI... | Function: Part of the sfmACDHF fimbrial operon. Could contribute to adhesion to various surfaces in specific environmental niches. Increases adhesion to eukaryotic T24 bladder epithelial cells in the absence of fim genes. Probably involved in the export and assembly of fimbrial subunits across the outer membrane.
Locat... |
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