ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
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F1RAX4 | MSAETVNNYDYSDWYENAAPTKAPVEVIPPCDPTADEGLFHICIAAISLVVMLVLAILARRQKLSDNQRGLTGLLSPVNFLDHTQHKGLAVAVYGVLFCKLVGMVLSHHPLPFTKEVANKEFWMILALLYYPALYYPLLACGTLHNKVGYVLGSLLSWTHFGILVWQKVDCPKTPQIYKYYALFGSLPQIACLAFLSFQYPLLLFKGLQNTETANASEDLSSSYYRDYVKKILKKKKPTKISSSTSKPKLFDRLRDAVKSYIYTPEDVFRFPLKLAISVVVAFIALYQMALLLISGVLPTLHIVRRGVDENIAFLLAGFN... | Function: Retinol transporter. Accepts retinol from the extracellular retinol-binding protein rbp4, mediates retinol transport across the cell membrane, and then transmits retinol to the cytoplasmic retinol-binding protein rbp1 . Required for normal vitamin A homeostasis .
Location Topology: Multi-pass membrane protein... |
Q9BX79 | MSSQPAGNQTSPGATEDYSYGSWYIDEPQGGEELQPEGEVPSCHTSIPPGLYHACLASLSILVLLLLAMLVRRRQLWPDCVRGRPGLPSPVDFLAGDRPRAVPAAVFMVLLSSLCLLLPDEDALPFLTLASAPSQDGKTEAPRGAWKILGLFYYAALYYPLAACATAGHTAAHLLGSTLSWAHLGVQVWQRAECPQVPKIYKYYSLLASLPLLLGLGFLSLWYPVQLVRSFSRRTGAGSKGLQSSYSEEYLRNLLCRKKLGSSYHTSKHGFLSWARVCLRHCIYTPQPGFHLPLKLVLSATLTGTAIYQVALLLLVGVVP... | Function: Functions as retinol transporter. Accepts all-trans retinol from the extracellular retinol-binding protein RBP4, facilitates retinol transport across the cell membrane, and then transfers retinol to the cytoplasmic retinol-binding protein RBP1 . Retinol uptake is enhanced by LRAT, an enzyme that converts reti... |
Q7Z7C7 | MGKIDVDKILFFNQEIRLWQLIMATPEENSNPHDRATPQLPAQLQELEHRVARRRLSQARHRATLAALFNNLRKTVYSQSDLIASKWQVLNKAKSHIPELEQTLDNLLKLKASFNLEDGHASSLEEVKKEYASMYSGNDSFPQNGSSPWYLNFYKQTMDLLTGSGIITPQEAALPIVSAAISHLWQNLSEERKASLRQAWAQKHRGPATLAEACREPACAEGSVKDSGVDSQGASCSLVSTPEEILFEDAFDVASFLDKSEVPSTSSSSSVLASCNPENPEEKFQLYMQIINFFKGLSCANTQVKQEASFPVDEEMIMLQ... | Function: Meiosis-inducer required for the transition into meiosis for both female and male germ cells. In female germ cells, acts downstream of ZGLP1 as a key effector of the meiotic program: required for premeiotic DNA replication and subsequent events in meiotic prophase. During spermatogenesis, next to its role in ... |
P70278 | MATPGEGNQPSDDGAPQPLAQLQKLEPRVVRRRLSQARHRATLVGLFNNLRKAVYSQSDITASKWQVLNRTKIHIQEQEESLDKLLKLKASFNLQDGNPNSLEEVKEEYARMYSENDSVFLNSFLQDSPPEWFPSEAVGPDAEEEGEEEGEEEGEEGEEEEEGDEEGEEEEENGEEREVEEYQEEEEEEEEEEKKVDLSHSSSTLLPDLMEFERYLNFYKQTMDLLTMNSIISAHEVTLPIVSAAISHLWQTLSEEKKARLLQVWEQQHSAFADLTEACLELAGVEGSMKDSGVDSQGASCSLESTPEEILFEDAFDVAS... | Function: Meiosis-inducer required for the transition into meiosis for both female and male germ cells . In female germ cells, acts downstream of ZGLP1 as a key effector of the meiotic program: required for premeiotic DNA replication and subsequent events in meiotic prophase . During spermatogenesis, next to its role i... |
Q5ZK47 | MSNFLPDSSCYELLTIIGRGFEDLMVVNLARYKPSGEYVTVRRVNLEACTNEMVTFLQGELHVSKLFNHPNIVPYKATFIADNELWVVTSFMAYGSAKDLICTHFMDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLSGLRSNLSMINHGQRLKVVHDFPKYSIKVLPWLSPEVLQQNLQGYDAKSDIYSIGITACELANGHVPFKDMPSTQMLLEKLNGTVPCLLDTTTIPADELTMKTSRSSANYGLGESTAVSNVRAANGESTLHPYLRTFSSCFHNFVGQCLQRNPDFRPSAGALLNHPF... | Function: Pseudokinase which, in complex with CAB39/MO25 (CAB39/MO25alpha or CAB39L/MO25beta), binds to and activates STK11/LKB1. Adopts a closed conformation typical of active protein kinases and binds STK11/LKB1 as a pseudosubstrate, promoting conformational change of STK11/LKB1 in an active conformation (By similari... |
Q7RTN6 | MSFLVSKPERIRRWVSEKFIVEGLRDLELFGEQPPGDTRRKTNDASSESIASFSKQEVMSSFLPEGGCYELLTVIGKGFEDLMTVNLARYKPTGEYVTVRRINLEACSNEMVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVTSFMAYGSAKDLICTHFMDGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLSGLRSNLSMISHGQRQRVVHDFPKYSVKVLPWLSPEVLQQNLQGYDAKSDIYSVGITACELANGHVPFKDMPATQMLLEKLNGTVPCLLDTSTIPAEELTMSPSRSVAN... | Function: Pseudokinase which, in complex with CAB39/MO25 (CAB39/MO25alpha or CAB39L/MO25beta), binds to and activates STK11/LKB1. Adopts a closed conformation typical of active protein kinases and binds STK11/LKB1 as a pseudosubstrate, promoting conformational change of STK11/LKB1 in an active conformation.
Sequence Ma... |
Q9P2W9 | MAVDITLLFRASVKTVKTRNKALGVAVGGGVDGSRDELFRRSPRPKGDFSSRAREVISHIGKLRDFLLEHRKDYINAYSHTMSEYGRMTDTERDQIDQDAQIFMRTCSEAIQQLRTEAHKEIHSQQVKEHRTAVLDFIEDYLKRVCKLYSEQRAIRVKRVVDKKRLSKLEPEPNTKTRESTSSEKVSQSPSKDSEENPATEERPEKILAETQPELGTWGDGKGEDELSPEEIQMFEQENQRLIGEMNSLFDEVRQIEGRVVEISRLQEIFTEKVLQQEAEIDSIHQLVVGATENIKEGNEDIREAIKNNAGFRVWILFFL... | Function: Syntaxin that may be involved in targeting and fusion of Golgi-derived retrograde transport vesicles with the ER.
Location Topology: Single-pass type IV membrane protein
Sequence Mass (Da): 38674
Sequence Length: 335
Subcellular Location: Endoplasmic reticulum membrane
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Q8VDS8 | MAVDITLLFRASVKTVKTRNKALGVAVGGGADGSRDELFRRSPRPKGDFSSRAREVISHIGKLRDFLLEHRKEYINAYSHTMSDYGRMTDTERDQIDQDAQIFIRTCSEAIHQLRTEAHKEIHSQQVKEHRTAVLDFVDDYLKRVCKLYSEQRAIRVKRVVDKKRLSKLEPEPHTKRKDSTSEKAPQNASQDSEGKPAAEELPEKPLAESQPELGTWGDGKGEDELSPEEIQMFEQENQRLIGEMNSLFDEVRQIEGKVVEISRLQEIFTEKVLQQETEIDSIHQLVVGATENIKEGNEDIREAIKNNAGFRVWILFFLV... | Function: Syntaxin that may be involved in targeting and fusion of Golgi-derived retrograde transport vesicles with the ER.
Location Topology: Single-pass type IV membrane protein
Sequence Mass (Da): 38381
Sequence Length: 334
Subcellular Location: Endoplasmic reticulum membrane
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Q0VCI2 | MKDRLPELKQRTKETELSKDKDVPTTEAEEQGVFLQQAVIYEREPVAERHLHEIQKLQESINNLTDNVQKFGQQQKSLVASMRRFSLLKKESSIAKEIKIQAEHINRGLDDLVKEVKKSEDESGPSSVVTRILKFQHAAMFRHFQQTMFTYNDTIAAKQEKCRTFIFRQLEVAGKELPEEEVNDMLHQGKWEVFNESLLTEISITKAQLSEIEQRHKELVNLENQIKDLRDLFIQISLLVEEQGESVNSIEMIVNGTKEYVNTTKEKFGLAVKYKKRNPCKILCCWCCPCCG | Function: Plays a role in endosomal trafficking of the epidermal growth factor receptor (EGFR).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 33890
Sequence Length: 292
Subcellular Location: Cell membrane
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Q8N4C7 | MKDRLQELKQRTKEIELSRDSHVSTTETEEQGVFLQQAVIYEREPVAERHLHEIQKLQESINNLADNVQKFGQQQKSLVASMRRFSLLKRESTITKEIKIQAEYINRSLNDLVKEVKKSEVENGPSSVVTRILKSQHAAMFRHFQQIMFIYNDTIAAKQEKCKTFILRQLEVAGKEMSEEDVNDMLHQGKWEVFNESLLTEINITKAQLSEIEQRHKELVNLENQIKDLRDLFIQISLLVEEQGESINNIEMTVNSTKEYVNNTKEKFGLAVKYKKRNPCRVLCCWCCPCCSSK | Function: Plays a role in endosomal trafficking of the epidermal growth factor receptor (EGFR).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 34324
Sequence Length: 294
Subcellular Location: Cell membrane
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P32850 | MKDRTQELRTAKDSDDDDDVTVTVDRDRFMDEFFEQVEEIRGFIDKISENVEEVKRKHSAILASPNPDEKTKEELEELMSDIKKTANKVRSKLKSIEQSIEQEEGLNRSSADLRIRKTQHSTLSRKFVEVMSEYNATQSDYRERCKGRIQRQLEITGRTTTSEELEDMLESGNPAIFASGIIMDSSISKQALSEIETRHSEIIKLENSIRELHDMFMDMAMLVESQGEMIDRIEYNVEHSVDYVERAVSDTKKAVKYQSKARRKKIMIVICCVVLGIVIASTFGGIFG | Function: Plays an essential role in hormone and neurotransmitter calcium-dependent exocytosis and endocytosis. Part of the SNARE (Soluble NSF Attachment Receptor) complex composed of SNAP25, STX1A and VAMP2 which mediates the fusion of synaptic vesicles with the presynaptic plasma membrane. STX1A and SNAP25 are locali... |
O16000 | MTKDRLSALKAAQSEDEQDDDMHMDTGNAQYMEEFFEQVEEIRGSVDIIANNVEEVKKKHSAILSNPVNDQKTKEELDELMAVIKRAANKVRGKLKLIENAIDHDEQGAGNADLRIRKTQHSTLSRRFVEVMTDYNKTQTDYRERCKGRIQRQLDIAGKQVGDEDLEEMIESGNPGVFTQGIITDTQQAKQTLADIEARHNDIMKLESSIRELHDMFMDMAMLVESQGEMVDRIEYNVEHAKEFVDRAVADTKKAVQYQSKARRKKICILVTGVILITGLIIFILFYAKVL | Function: Plays a critical role in several secretory processes, including cuticle secretion and neurotransmitter release, and probably assists in neuronal membrane maturation or the final stages of neuronal differentiation . Plays a role in synaptic vesicle docking and tethering through its association with unc-18 . Th... |
Q24547 | MTKDRLAALHAAQSDDEEETEVAVNVDGHDSYMDDFFAQVEEIRGMIDKVQDNVEEVKKKHSAILSAPQTDEKTKQELEDLMADIKKNANRVRGKLKGIEQNIEQEEQQNKSSADLRIRKTQHSTLSRKFVEVMTEYNRTQTDYRERCKGRIQRQLEITGRPTNDDELEKMLEEGNSSVFTQGIIMETQQAKQTLADIEARHQDIMKLETSIKELHDMFMDMAMLVESQGEMIDRIEYHVEHAMDYVQTATQDTKKALKYQSKARRKKIMILICLTVLGILAASYVSSYFM | Function: Plays a critical role in several secretory processes, including cuticle secretion and neurotransmitter release, and probably assists in neuronal membrane maturation or the final stages of neuronal differentiation . Essential for embryonic viability and development . Required for coordinated peristaltic contra... |
Q16623 | MKDRTQELRTAKDSDDDDDVAVTVDRDRFMDEFFEQVEEIRGFIDKIAENVEEVKRKHSAILASPNPDEKTKEELEELMSDIKKTANKVRSKLKSIEQSIEQEEGLNRSSADLRIRKTQHSTLSRKFVEVMSEYNATQSDYRERCKGRIQRQLEITGRTTTSEELEDMLESGNPAIFASGIIMDSSISKQALSEIETRHSEIIKLENSIRELHDMFMDMAMLVESQGEMIDRIEYNVEHAVDYVERAVSDTKKAVKYQSKARRKKIMIIICCVILGIVIASTVGGIFA | Function: Plays an essential role in hormone and neurotransmitter calcium-dependent exocytosis and endocytosis . Part of the SNARE (Soluble NSF Attachment Receptor) complex composed of SNAP25, STX1A and VAMP2 which mediates the fusion of synaptic vesicles with the presynaptic plasma membrane. STX1A and SNAP25 are local... |
O35526 | MKDRTQELRTAKDSDDDDDVTVTVDRDRFMDEFFEQVEEIRGFIDKIAENVEEVKRKHSAILASPNPDEKTKEELEELMSDIKKTANKVRSKLKSIEQSIEQEEGLNRSSADLRIRKTQHSTLSRKFVEVMSEYNATQSDYRERCKGRIQRQLEITGRTTTSEELEDMLESGNPAIFASGIIMDSSISKQALSEIETRHSEIIKLETSIRELHDMFMDMAMLVESQGEMIDRIEYNVEHAVDYVERAVSDTKKAVKYQSKARRKKIMIIICCVILGIIIASTIGGIFG | Function: Plays an essential role in hormone and neurotransmitter calcium-dependent exocytosis and endocytosis . Part of the SNARE (Soluble NSF Attachment Receptor) complex composed of SNAP25, STX1A and VAMP2 which mediates the fusion of synaptic vesicles with the presynaptic plasma membrane. STX1A and SNAP25 are local... |
P32851 | MKDRTQELRTAKDSDDDDDVTVTVDRDRFMDEFFEQVEEIRGFIDKIAENVEEVKRKHSAILASPNPDEKTKEELEELMSDIKKTANKVRSKLKSIEQSIEQEEGLNRSSADLRIRKTQHSTLSRKFVEVMSEYNATQSDYRERCKGRIQRQLEITGRTTTSEELEDMLESGNPAIFASGIIMDSSISKQALSEIETRHSEIIKLENSIRELHDMFMDMAMLVESQGEMIDRIEYNVEHAVDYVERAVSDTKKAVKYQSKARRKKIMIIICCVILGIIIASTIGGIFG | Function: Plays an essential role in hormone and neurotransmitter calcium-dependent exocytosis and endocytosis . Part of the SNARE (Soluble NSF Attachment Receptor) complex composed of SNAP25, STX1A and VAMP2 which mediates the fusion of synaptic vesicles with the presynaptic plasma membrane . STX1A and SNAP25 are loca... |
P61267 | MKDRTQELRSAKDSDDEEEVVHVDRDHFMDEFFEQVEEIRGCIEKLSEDVEQVKKQHSAILAAPNPDEKTKQELEDLTTDIKKTANKVRSKLKAIEQSIEQEEGLNRSSADLRIRKTQHSTLSRKFVEVMTEYNATQSKYRDRCKDRIQRQLEITGRTTTNEELEDMLESGKLAIFTDDIKMDSQMTKQALNEIETRHNEIIKLETSIRELHDMFVDMAMLVESQGEMIDRIEYNVEHSVDYVERAVSDTKKAVKYQSKARRKKIMIIICCVVLGVVLASSIGGTLGL | Function: Potentially involved in docking of synaptic vesicles at presynaptic active zones. May mediate Ca(2+)-regulation of exocytosis acrosomal reaction in sperm (By similarity).
PTM: Phosphorylated by CK2.
Location Topology: Single-pass type IV membrane protein
Sequence Mass (Da): 33275
Sequence Length: 288
Subcellu... |
P61266 | MKDRTQELRSAKDSDDEEEVVHVDRDHFMDEFFEQVEEIRGCIEKLSEDVEQVKKQHSAILAAPNPDEKTKQELEDLTADIKKTANKVRSKLKAIEQSIEQEEGLNRSSADLRIRKTQHSTLSRKFVEVMTEYNATQSKYRDRCKDRIQRQLEITGRTTTNEELEDMLESGKLAIFTDDIKMDSQMTKQALNEIETRHNEIIKLETSIRELHDMFVDMAMLVESQGEMIDRIEYNVEHSVDYVERAVSDTKKAVKYQSKARRKKIMIIICCVVLGVVLASSIGGTLGL | Function: Potentially involved in docking of synaptic vesicles at presynaptic active zones. May mediate Ca(2+)-regulation of exocytosis acrosomal reaction in sperm (By similarity).
PTM: Phosphorylated by CK2.
Location Topology: Single-pass type IV membrane protein
Sequence Mass (Da): 33245
Sequence Length: 288
Subcellu... |
L8FSM5 | MKFSQSLIALAACFLPLIAAAPEEAQHAKIRSPGAQDIILDSYIVVFNKGVNDADIESEFASVSHILSKRRPAHKGVGHKYNITGFKGYQIETDTGSIGEIAASPLVAWIERDGKVQANALETRSGATWGLGRISHKATGSNSYVYDSSAGSGSTVYVVDSGIYIEHSEFEGRAKWGANYISGSPDTDENGHGTHCAGTIAGATYGVASKANLVAVKVLDGDGSGSNSGVIAGINFVGQNGKDGKSVLSMSLGGSYSAALNSAVESTISNGVTVVVAAGNDGADASNYSPASAKNAITVGAVDSTDTRADFSNYGSVLDV... | Function: Major secreted subtilisin-like serine endopeptidase. Preferentially cleaves substrates containing hydrophobic residues at P4, positively charged residues at P3, small or flexible residues at P2, and large, bulky residues at P1. Mediates the degradation of collagen, the major structural protein in the mammalia... |
O13792 | MASAQEDLIDYEEEEELVQDQPAQEITPAADTAENGEKSDKKGSYVGIHSTGFRDFLLKPELLRAITDSGFEHPSEVQQVCIPQSILGTDVLCQAKSGMGKTAVFVLSTLQQIEPVDGEVSVLVLCHTRELAFQIKNEYARFSKYLPDVRTAVFYGGINIKQDMEAFKDKSKSPHIVVATPGRLNALVREKILKVNSVKHFVLDECDKLLESVDMRRDIQEVFRATPPQKQVMMFSATLSNEIRPICKKFMQNPLEIYVDDETKLTLHGLQQHYVKLEEKAKNRKINDLLDSLEFNQVVIFVKSVSRANELDRLLRECNF... | Function: ATP-binding RNA helicase involved in transcription elongation and required for the export of mRNA out of the nucleus. SUB2 also plays a role in pre-mRNA splicing and spliceosome assembly. May be involved in rDNA and telomeric silencing, and maintenance of genome integrity. Links the mRNA adapter mlo3 to rae1 ... |
Q6CH90 | MSHEGEEELLDYSDSEEIALPSTTVESGSNGDAKAETTTVKEENTEQKGSYVGIHSTGFRDFLLKPELLRAIVDCGFEHPSEVQQVCIPQSILGTDVLCQAKAGVGKTAVFVLSTLQQLEPVPGECSVVVLCHTRELAYQIMNEYARFSKYLPDVKTAVFYGGSPIQKDIELIQNKETSPHVIVATPGRLHALVRDKHLRLGNVKTFVIDECDKVLDQIDMRRDVQEIFRVTPRQKQVMMFSATLSQEIRPICKKFMSSPLEILVDDEGKLTLHGLQQYYVDVEEKSKNRKLGDLLDNLEFNQVIIFVKSTSRANGLSQV... | Function: ATP-binding RNA helicase involved in transcription elongation and required for the export of mRNA out of the nucleus. SUB2 also plays a role in pre-mRNA splicing and spliceosome assembly. May be involved in rDNA and telomeric silencing, and maintenance of genome integrity (By similarity).
Catalytic Activity: ... |
Q07478 | MSHEGEEDLLEYSDNEQEIQIDASKAAEAGETGAATSATEGDNNNNTAAGDKKGSYVGIHSTGFKDFLLKPELSRAIIDCGFEHPSEVQQHTIPQSIHGTDVLCQAKSGLGKTAVFVLSTLQQLDPVPGEVAVVVICNARELAYQIRNEYLRFSKYMPDVKTAVFYGGTPISKDAELLKNKDTAPHIVVATPGRLKALVREKYIDLSHVKNFVIDECDKVLEELDMRRDVQEIFRATPRDKQVMMFSATLSQEIRPICRRFLQNPLEIFVDDEAKLTLHGLQQYYIKLEEREKNRKLAQLLDDLEFNQVIIFVKSTTRAN... | Function: ATP-binding RNA helicase component of the TREX complex involved in transcription elongation and required for the export of mRNA out of the nucleus. SUB2 also plays a role in pre-mRNA splicing and spliceosome assembly. May be involved in rDNA and telomeric silencing, and maintenance of genome integrity.
Cataly... |
Q8I430 | MINRQYFIWYIFIFNIINKIYFENIRYVKNYEVVIRKKKNIERGIGNDFAFIRRYYKSRLLSDVSYKNNSIKGKNRVDKEGDIKKYDNNDDNKMDNSYDYKNKSIKENETKIRKEQVISLDKRYNRNINEKEEIKKKIKDIQRKRLIIYFKQDNTILSSRNYKHIFMKVLSSCGHIEKLTFINFYLYEFPKSINNEDMLLKICLRLLESRRINVENDNQISHTVQMKSYNNNNNKWDNINSKNNCIYQIKDKIKDLPNVSPSASTFTSISTSPYTLKLRDRNKYANDKNHIFKINHSNKHKNNNNNNNNNDYHNNNKSNY... | Function: Serine protease which may cleave PFN/profilin.
Catalytic Activity: Hydrolysis of proteins with broad specificity for peptide bonds, and a preference for a large uncharged residue in P1. Hydrolyzes peptide amides.
Sequence Mass (Da): 88047
Sequence Length: 769
Subcellular Location: Secreted
EC: 3.4.21.62
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L8GD75 | MLFSKSLVALVACFLPLIVSATELKLRNAAATNVAADSYIVVYKDIDDSTFESEMFNVHSFLSKRDSTFRGLGHKYKMPKFKGYQIESDMDTVNRISQSPHVAYVDKDVKVSAYDLSVRIGAPWGLDRISHRNGTSPGLEEYTYDSSAGGGTTIYIIDTGVYIEHVEFEGRATFGANFIPGSPDTDEDGHGTHVAGIAAGANFGVASKAKIIAVRVLDANGDGKGSNVLAGMQWAADDAGKKNQTAKSVINMSLGADYSEAFNKATEAIIAKGIVVVAAAGNEDANASGVSPASTVDAITVGATDRNDSRAAFSNWGVAL... | Function: Secreted subtilisin-like serine endopeptidase . Mediates the degradation of collagen, the major structural protein in the mammalian host. Degrades the nonhelical regions of collagen that function in the cross-linking of the helical components (By similarity). May function as virulence factor involved in epide... |
B3FHP0 | MLRMAPKTVGAVRNLNIHEWQSKQLIQKYGGRAQSGEVAFSPERSRDIAKKLWNQFPGCKFVVKAQVLAGGRGKGHWEHGMQGGVKLAKTPEEVYEIANEMIGHKLITKQTGAKGINCNKVMVCGAVKILKEFYLSILLDRAMGCPVIIATSQGGMGIEEVAQKCPECLFKVPISVKNGPTNEQLVKLAKDLGLEGDLVQDCVDNVKALYQVFDKCDSTMVEINPLGVIETPTDEKVICCLDAKIAFDKDAAFRQKEIFALRDKSREDPRDVRASLADLNYVGLDGDIGCMVNGAGLAMATMDTINYFGGSAANFLDVGG... | 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 ATP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the e... |
Q9P567 | MFKLGRNRALASAFAATSRAPLASRLPSVSQQQRRALSIHEYLSADLLRQYGIGVPKGDVARTGAEAEAIAKQIGGEDMVIKAQVLAGGRGKGTFDNGLKGGVRVIYSPTEAKMFAEQMIGHKLITKQTGAQGRLCSAVYICERKFARREFYLAVLMDRASQGPVIVSSSQGGMDIEGVAKENPEAIHTTYIDINVGVTDEMARDIATKLGFSEQCVEEAKDTIQKLYKIFCEKDATQIEINPLSETSDHKVMAMDAKFGFDDNADFRQPDIFKLRDTTQEDPDEVRAAQAGLNFIKLDGDIGCLVNGAGLAMATMDIIK... | 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 ATP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the e... |
Q6K9N6 | MVRGSLGKLASRALSVAGKWQHQQLRRLNIHEYQGAELMGKYGINVPRGAAAGSVEEVKNTLKNVFPSEKEIVVKSQILAGGRGLGTFKSGLQGGVHIVKAEEAESLAAKMLGQILVTKQTGPQGKIVSKVYLCEKLSLVNEMYFAITLDRNTAGPLIIACSKGGTSIEDLAEKYPDMIIKVPIDVFKGITDDDAAKVVDGLAPKTADRQSSIEQIKKLYELFCKSDCTLLEINPLAETADNKLVAADAKLNFDDNAAFRQKEIFAMRDTTQEDPREVAAAKADLNYIGLDGEIGCMVNGAGLAMATMDIIKLHGGTPAN... | 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 ATP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the e... |
Q84LB6 | MLRKLANQSLSVAGKWQQQQLRRLNIHEYQGAELMSKYGINVPKGVAVASLDEVKKAIQDVFPNQSEVVVKSQVLAGGRGLGTFKNGFQGGVHIVKADQAEDIASKMLGQILVTKQTGAQGKVVSKVYLCEKMSLVNEMYFSIILDRATAGPLIIACRKGGTSIEDLAEKFPDMIIKVPIDVFKGISDADAAKVVDGLAPKVADRNDSIEQVKKLYKLFCETDCTMLEINPLAETSDNKLVAADAKLNFDDNAAYRQKEIFSLRDSSQEDPREVAAAKADLNYIGLDGEIGCMVNGAGLAMATMDIIKLHGGTPANFLDV... | 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 ATP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the e... |
Q03184 | MLSSSFARNFNILEWQSKEICAKYNVAAGINLVARSPEEAAEAFRKMNLPAAVIKAQVYCGGRGKGHWLETGFKSGVHFVKSADEAAKIAKEMLGHHLVTKQTGKDGLLCQAVMLSDPVEVKRELYFAILLDRQTQSPVVIASTEGGVEIEEVAAHHPEKIHKFVLDGVEGITEEVAKNISTKLGLTGKAYDNGVVEMQKLWKLFVGSDATQVEVNPLAETTDGRIITVDSKFNFDDSAHYRQKQIFGYRDLKQVNPFEIRAEKYGLNYVPLDGNVACLVNGAGLAMATMDVIKLAGGDPANFLDLGGAASEAAVTEGFT... | 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 ATP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the e... |
P53312 | MYSRKSLSLISKCGQLSRLNAQAALQARRHLSIHEYRSAQLLREYGIGTPEGFPAFTPEEAFEAAKKLNTNKLVIKAQALTGGRGKGHFDTGYKSGVHMIESPQQAEDVAKEMLNHNLITKQTGIAGKPVSAVYIVKRVDTKHEAYLSILMDRQTKKPMIIASSQGGMNIEEVAERTPDAIKKFSIETSKGLSPQMAKDVAKSLGFSPDAQDEAAKAVSNLYKIFMERDATQVEINPLSEIEHDPTHKIMCTDAKFGFDDNASFRQEKIYSWRDLSQEDPDEVKAKKYDLNFVKLKGNIGCLVNGAGLAMATMDVIKLNG... | 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 ATP and thus represents the only step of substrate-level phosphorylation in the TCA . The beta subunit provides nucleotide specificity of the ... |
O28732 | MRLHEHQAKQIFAKHGIRVPRGEVATSPEEAEKIAEKLGGRVVVKAQILVGGRGKAGGVKKANSPEEAKEVAKKILGMTIKGHRVEKVLVEEQLNMRKEYYVGYVVDKSSRLPTVIFSRMGGMDVEEIAAKHPDAIHRIYFDPLWGLKDYEVRKALFRAGFEGEEFKQMFDIIKKLVDIAFAYEAELTEINPLAVTDEGFLAADARLNTDDNALYRHPELAELREATEEDPLEREARLKGINYVHLGGNVGVIANGAGLAMATMDIINLMGGKPANFLDTGGGLADPVKMKNCLLHVLKDPNVRVVFINIYAEITRCEKV... | 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... |
Q9KY56 | MDLFEYQARDLFAKHDVPVLAGEVIDTPEAAREITERLGGKSVVKAQVKVGGRGKAGGVKLAASADEAVARATDILGMDIKGHTVHKVMIAETAPEIVEEYYVSFLLDRANRTFLSIASVEGGVEIEEVAATRPEAVAKTPIDAIDGVTPEKAREIVEAAKFPAEVADKVADILVKLWDTFIKEDALLVEVNPLAKVVSGDVIALDGKVSLDDNAEFRHPDFEALHDKAAANPLEAAAKEKNLNYVKLDGEVGIIGNGAGLVMSTLDVVAYAGEAHGNVKPANFLDIGGGASAQVMANGLEIILGDPDVRSVFVNVFGGI... | 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... |
O87840 | MDLYEHQARELFKEHGIVVPRAEVTDSPERAREIARALGGRAVVKAQVKTGGRGKAGGVRLAADPAEAEEAARHILGMDIRGHTVDTVMLAEPCEIEREFYVSYVLDRASGGFLAIASAEGGTEIEEVAARRPEAVARIPVDPATGVHTATAVRIADAAGLPPQTVDTLVRLWKVLVREDALLVEVNPLVRTAEGRIVALDGKVTLDDNARFRQSRWGETRQEDADSLEARAGAKGLNYVKLDGEVGVIGNGAGLVMSTLDVVAGCGARPANFLDIGGGASARVMADGLSVVLSDPDVRSVLVNVFGGITACDAVADGIV... | 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... |
Q6F8L4 | MNLHEYQAKALLKKYGVSVQEGILARSAEEAVAAFEQLGGKFAVIKAQVHAGGRGKAGGVKVVKSKEEAADYANQLIGTNLVTYQTDANGQPVNSVLVCEDVYPVERELYLGAVVDRSSRRVTFMASTEGGVEIEKVAEETPEKIIKVEVDPLVGLQPFQAREVAFALGLKDKQIGQFVKLMAGAYQAFVENDFALFEINPLSVRENGDILAVDAKIGIDSNALYRLPEIAASRDKSQENERELKASEFELNYVALEGNIGCMVNGAGLAMATMDIIKLYGGQPANFLDVGGGATKERVIEAFKLILADTSVQGVLINIF... | 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... |
Q2N695 | MNLHEYQAKELLAKYGIGIPAGHAALTVEEAVAGAKQLPGPLYVVKAQIHAGGRGKGKFKELGPDAKGGVRLAKSIEDVEASAREMLGNTLVTVQTGEEGKQVNRLYVTDGVDIASEYYLSMVVDRASGRVGMIVSTEGGMDIEEVAHSTPEKITTITIDPAQGFMPHHGRAVAFALKLSGDLNKQAQKLAKQLYTAFMDLDCEMLEINPLVETEDGQLLVLDTKMSIDGNALYRHKDVEEMRDETEEDPAEVEASEYDLAYIKLDGNIGCMVNGAGLAMATMDIIKLNGAFPANFLDVGGGATTEKVTAAFKIILKDPA... | 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... |
A6GY30 | MNIHEYQGKEILASYGVRIQRGIVANNPVEAVAAAKQLTTETGTSWYVVKAQVHAGGRGKGGGVKLAKNLQQVEEISEQIIGMQLITPQTSAEGKKVHKVLIAEDVYYPGESETSEFYISVLLNRSTGRNMIVYSTEGGMDIEEVAAHTPHLIHNEEIDPSVGLQAFQARRIAFNLGLSGNAFKEMVKFIDSLYNAYIGSDASMFEINPVLKTSDDKIMAVDAKVNIDDNALYRQPKYADMRDIREENPIEVEAKEVGLNYVDLDGTVGCMVNGAGLAMATMDLIKYAGFEPANFLDVGGTADAKRVETAFRIILKDENV... | 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... |
Q8D2J8 | MNKFIKKINFIKNFSSCENWEEKYLYIIELGNKLSPFPEKFRKNSNLIPGCQNDSWIYLIYENTKKIKFYGDSNSLIVKGLIAIIFILHEDLKLSEILTFDVKPYFNKLSLTNYLTPSRVQGLSSISKFIKKSARCLLIKEKIL | 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 ... |
O32164 | MNITDIREQFPILHQQVNGHDLVYLDSAATSQKPRAVIETLDKYYNQYNSNVHRGVHTLGTRATDGYEGAREKVRKFINAKSMAEIIFTKGTTTSLNMVALSYARANLKPGDEVVITYMEHHANIIPWQQAVKATGATLKYIPLQEDGTISLEDVRETVTSNTKIVAVSHVSNVLGTVNPIKEMAKIAHDNGAVIVVDGAQSTPHMKIDVQDLDCDFFALSSHKMCGPTGVGVLYGKKALLENMEPAEFGGEMIDFVGLYESTWKELPWKFEAGTPIIAGAIGLGAAIDFLEEIGLDEISRHEHKLAAYALERFRQLDGV... | Function: Type II cysteine desulfurase that acts as the initial step in the SUF-like Fe-S cluster assembly pathway. Catalyzes the removal of elemental sulfur atoms from L-cysteine by using the cofactor pyridoxal 5'-phosphate (PLP), resulting in the production of L-alanine and persulfide . Activity is stimulated by SufU... |
Q9EXP2 | MNYPVEHYPIDRVRADFPILQQSVNGQPLAYLDSAASAQKPLAVIDRERDFYLHEYAAVHRGIHTLSARATSAMEEVRAKVATFIHAASAEDIVFVRGTTEAINLVANSYGRTAFQPGDNLVISEMEHHANIVPWQMLAQARGLTLRVLPITDDGELDMAQLPALLDERTRLVAVTQVSNVLGTVNPLAEIIRQAHACGAKVLVDGAQAVMHQAVDVQALDCDFYAFSGHKLYGPSGIGVLYGKSELLQAMPPWEGGGAMIREVSLTQGTTYADPPWRFEAGSPHVAGIIGLGAALDYVSALGVDAIQAHEGLLMRYALA... | Function: Cysteine desulfurases mobilize the sulfur from L-cysteine to yield L-alanine, an essential step in sulfur metabolism for biosynthesis of a variety of sulfur-containing biomolecules. Component of the suf operon, which is activated and required under specific conditions such as oxidative stress and iron limitat... |
P38359 | MSRKSSTEYVHNQEDADIEVFESEYRTYRESEAAENRDGLHNGDEENWKVNSSKQKFGVTKNELSDVLYDSIPAYEESTVTLKEYYDHSIKNNLTAKSAGSYLVSLFPIIKWFPHYNFTWGYADLVAGITVGCVLVPQSMSYAQIASLSPEYGLYSSFIGAFIYSLFATSKDVCIGPVAVMSLQTAKVIAEVLKKYPEDQTEVTAPIIATTLCLLCGIVATGLGILRLGFLVELISLNAVAGFMTGSAFNIIWGQIPALMGYNSLVNTREATYKVVINTLKHLPNTKLDAVFGLIPLVILYVWKWWCGTFGITLADRYYR... | Function: High affinity uptake of sulfate into the cell.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 95951
Sequence Length: 859
Subcellular Location: Membrane
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P36150 | MVRDLVTLPSSLPLITAGFATDQVHLLIGTGSTDSVSVCKNRIHSILNAGGNPIVVNPSSPSHTKQLQLEFGKFAKFEIVEREFRLSDLTTLGRVLVCKVVDRVFVDLPITQSRLCEEIFWQCQKLRIPINTFHKPEFSTFNMIPTWVDPKGSGLQISVTTNGNGYILANRIKRDIISHLPPNISEVVINMGYLKDRIINEDHKALLEEKYYQTDMSLPGFGYGLDEDGWESHKFNKLIREFEMTSREQRLKRTRWLSQIMEYYPMNKLSDIKLEDFETSSSPNKKTKQETVTEGVVPPTDENIENGTKQLQLSEVKKEE... | Function: Siroheme synthase involved in methionine biosynthesis.
Catalytic Activity: 2 S-adenosyl-L-methionine + uroporphyrinogen III = H(+) + precorrin-2 + 2 S-adenosyl-L-homocysteine
Sequence Mass (Da): 66125
Sequence Length: 593
EC: 2.1.1.107
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Q9FF75 | MSASTVSITANTAAATRRTPILAGEKKSNFDYPQSESLANGGVGEAGGTSRDLSRGEATLDRSQGQDLGPVTRRSVSAATGTNTTATQRRTRKVATPKSEKARWKTVVRIFAKQLGALLIIVGLIQLTRKMILKASSPSSPISSYETEMAFSGLESRIAEVDGLVKATTNSMQVQVELLDKKMEREAKVLRQEIERKASAFQSELKKIESRTESLEKSVDEVNAKPWVTKDELERIYEELKKGNVDDSAFSEISIDELRAYARDIMEKEIEKHAADGLGRVDYALASGGAFVMEHSDPYLVGKGSSWFATTMRRAHTNAV... | Function: Component of SUN-protein-containing multivariate complexes also called LINC complexes which link the nucleoskeleton and cytoskeleton by providing versatile outer nuclear membrane attachment sites for cytoskeletal filaments . Required for the maintenance and/or formation of polarized nuclear shape in root hair... |
Q4WGL5 | MKFNTVALTLATAGSLVTAQHHHQHRHHQHKREDVVESSATVVQYELDGKPISLKQVCAGLADNTLKFANNDHPTGICDNLSSAAAPASTPEVTSAFAPAQFIELSSVVTSATPTSASSSETVQTPAASSSSASSSSTATGLDADFPDGELDCSTFPSEYGAIPLDYLKLGGWSGIQYVSYAGNFINDIVTAVAGDTCKDGAMCSYACPPGYQKSQWPSTQGATGQSVGGIECRNGKLHLTNPSLSKKLCIPGVGGVHVQNTLGETVAVCRTDYPGTESETIPIGLGGNDLQPLTCPDGETYYKWQGKTTSAQYYVNPKG... | Function: Cell surface beta-glucosidase involved in cell wall biosynthesis and septation, and thus required for normal growth and correct hyphal morphogenesis. Has hydrolytic activity on linear (1->3)-beta-D-glucans such as laminaribiose and other laminarioligosaccharides. Has also a minor transferase activity.
PTM: Hi... |
Q20924 | MALRHTISPQFSNRHSPPVTRSVSRTGVHQPLDTSTPVTRRDSQPGTITGTIQRFHESADDSEIDLNSSKFIYKEHFSYKEITSMKKEMWYDWLEYRIRMVRRRFVPTWAQFKRTLMAVVLFAMLYKYARDCLFDGTHHNSEGSYADKDANWASEKQKFHQTISNLRAEFSAHDKQLDFKTDHLEKLLENVLEHSKGWKESAIEELKQIKLWQAEISDALQQMKKEIDDAKSTKIIHSTPEKAPETAPTASLPPSSQLQPMHITRRALLGVNVANSLIGASIDHSCSSRPVSAKDGFFYDFMSYFGTFQEGYALLDRDVL... | Function: Involved in centrosome attachment to the nucleus. Required for zyg-12 localization to the nuclear envelope. Together with pot-1, it is required to anchor telomeres to the nuclear envelope in embryos .
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 54132
Sequence Length: 473
Domain: The SU... |
Q558Z2 | MSGDYKPNYQSSPSRKRLPLQSKDQASIYKYQTPSTLNLYNNTVNNNSSNNSNNHLLHNSNPNSSYLYDSSKQYSNQINIRNNSNSNSNTNNITSKKASSSYSINNKVDHNSHNNNDDDDIEDDVDINYSTNNASSNILHNRFSNSNKDDSYIDYSTDENPKILKQPQPLYNHLNNQIQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQRNNNNNSNSSNNNNTSTTIKRNNQQIDNNSNKNIISKFIGDPWKNFYYGSNKSLWPFERNNNSNNSSNNNNKVNFKQAIWIFIFSVLFIGCLLGLFSTNFYGIHIYF... | Function: May have an important role in defining the spacing of the nuclear envelope lumen. Essential for centrosome attachment to the nucleus, maintenance of correct ploidy, proper mitosis, association of the centromere cluster with the centrosome and the maintenance of genome stability. Requires direct chromatin bind... |
Q9D666 | MDFSRLHTYTPPQCVPENTGYTYALSSSYSSDALDFETEHKLEPVFDSPRMSRRSLRLVTTASYSSGDSQAIDSHISTSRATPAKGRETRTVKQRRSASKPAFSINHLSGKGLSSSTSHDSSCSLRSATVLRHPVLDESLIREQTKVDHFWGLDDDGDLKGGNKAATQGNGELAAEVASSNGYTCRDCRMLSARTDALTAHSAIHGTTSRVYSRDRTLKPRGVSFYLDRTLWLAKSTSSSFASFIVQLFQVVLMKLNFETYKLKGYESRAYESQSYETKSHESEAHLGHCGRMTAGELSRVDGESLCDDCKGKKHLEIHT... | Function: As a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex involved in the connection between the nuclear lamina and the cytoskeleton . The nucleocytoplasmic interactions established by the LINC complex play an important role in the transmission of mechanical forces across the nuclear enve... |
Q9SG79 | MSASTVSITASPRTIRRTPVLSGEKKSNFDFPPSESHANAAIGESSAGTNKDLIRAEAAGERSNTYDVGPVTRKSGSTATGTNTTTTQRRTRKSQGNKIDRGKWKTVVRVFAKQFGALLLLVGLIQLIRKLTLKDSSLSSSNFPIETEMVLSELESRISAVDGLVKTTTKMMQVQVEFLDKKMDSESRALRQTIDSTSSVLHSELKKVESKTERLQVSVDELNAKPLVSREELERVYEELKKGKVGDSDVNIDKLRAYARDIVEKEIGKHVADGLGRVDYALASGGAFVMGHSDPFLVGNGRNWFGTSRRRVHSKAVKML... | Function: Component of SUN-protein-containing multivariate complexes also called LINC complexes which link the nucleoskeleton and cytoskeleton by providing versatile outer nuclear membrane attachment sites for cytoskeletal filaments . Required for the maintenance and/or formation of polarized nuclear shape in root hair... |
Q9UH99 | MSRRSQRLTRYSQGDDDGSSSSGGSSVAGSQSTLFKDSPLRTLKRKSSNMKRLSPAPQLGPSSDAHTSYYSESLVHESWFPPRSSLEELHGDANWGEDLRVRRRRGTGGSESSRASGLVGRKATEDFLGSSSGYSSEDDYVGYSDVDQQSSSSRLRSAVSRAGSLLWMVATSPGRLFRLLYWWAGTTWYRLTTAASLLDVFVLTRRFSSLKTFLWFLLPLLLLTCLTYGAWYFYPYGLQTFHPALVSWWAAKDSRRPDEGWEARDSSPHFQAEQRVMSRVHSLERRLEALAAEFSSNWQKEAMRLERLELRQGAPGQGGG... | Function: As a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, involved in the connection between the nuclear lamina and the cytoskeleton. The nucleocytoplasmic interactions established by the LINC complex play an important role in the transmission of mechanical forces across the nuclear enve... |
Q8BJS4 | MSRRSQRLTRYSQDDNDGGSSSSGASSVAGSQGTVFKDSPLRTLKRKSSNMKHLSPAPQLGPSSDSHTSYYSESVVRESYIGSPRAVSLARSALLDDHLHSEPYWSGDLRGRRRRGTGGSESSKANGLTAESKASEDFFGSSSGYSSEDDLAGYTDSDQHSSGSRLRSAASRAGSFVWTLVTFPGRLFGLLYWWIGTTWYRLTTAASLLDVFVLTRSRHFSLNLKSFLWFLLLLLLLTGLTYGAWHFYPLGLQTLQPAVVSWWAAKESRKQPEVWESRDASQHFQAEQRVLSRVHSLERRLEALAADFSSNWQKEAIRLE... | Function: As a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, involved in the connection between the nuclear lamina and the cytoskeleton. The nucleocytoplasmic interactions established by the LINC complex play an important role in the transmission of mechanical forces across the nuclear enve... |
F4I316 | MQRSCRTRRRVSVNKFNGRNSFYKVSLSLVFLLWVLLFFSTLLISHGDGAKDEPLNDSMGMADPDDGQSDEKVVPFDGPLSLASASVDVTSDLSRNDDVNLSEESEDKEQEAEISSTVSGNDIESKDTYLLKQSEINKKDTGIDAGSKYDDFPKKSEINNTGTWNDTEGKDDNNFLKQSQLNKTGTGNDTESSDNEFLEQNQMNKTVLGNGTEINVSKVDQPSRAVPLGLDEFKSRASNSRNKSLSDQVSGVIHRMEPGGKEYNYASASKGAKVLSSNKEAKGAASILSRDNDKYLRNPCSTEGKFVVVELSEETLVNTI... | Function: Encodes a member of the mid-SUN subfamily of SUN-domain proteins that is localized to both the nuclear envelope and the ER. It is involved in early seed development and nuclear morphology. [TAIR].
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 74184
Sequence Length: 660
Subcellular Locatio... |
Q95LV7 | MSGKAKARRAAMFFRGCSEDASGSTSGSTLLSEDENPDTNGVTRSWKIILSTMFTLTFLLVGLLSHQWLKETEVPQKSRQLYAIIAEYGSRLYKYQARLRMPKEQLELLKKESQTLENNFHKILLLIEQIDVLKALLRDMKDGTDNNHSWNTHGDPVEDPDHTEVLDEEMSNLVNYVLKKLREDQVQMADYALKSAGASIIEAGTSESYKNNKAKLYWHGISFLNHEMPPDIILQPDVYPGNCWAFPGSQGHTLIKLATKIIPTAVTMEHISEKVSPSGNISSAPKEFSVYGITKKCEGEEIFLGQFIYNKTGTTVQTFE... | Function: As a probable component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, involved in the connection between the nuclear lamina and the cytoskeleton. The nucleocytoplasmic interactions established by the LINC complex play an important role in the transmission of mechanical forces across the nuc... |
Q5SS91 | MLTRSWKIILSTVFISTFLLVGLLNHQWLKETEFPQKPRQLYTVIAEYGSRLYNYQARLRMPKEQQELLKKESQTLENNFREILFLIEQIDVLKALLKDMKDGVHNHSLPVHRDAVQDQATTDVLDEEMSNLVHYVLKKFRGDQIQLADYALKSAGASVIEAGTSESYKNNKAKLYWHGIGFLNYEMPPDMILQPDVHPGKCWAFPGSQGHILIKLARKIIPTAVTMEHISEKVSPSGNISSAPKEFSVYGVMKKCEGEEIFLGQFIYNKMEATIQTFELQNEASESLLCVKLQILSNWGHPKYTCLYRFRVHGIPSDYT | Function: As a probable component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, involved in the connection between the nuclear lamina and the cytoskeleton. The nucleocytoplasmic interactions established by the LINC complex play an important role in the transmission of mechanical forces across the nuc... |
D4AM57 | MKFSSGILSLAVAASVQSVQASYHAHGHAHHHRVLNKRADPDVVTIPGPKVYAFILNGSEMSKEQVCAGIRDGRLDWSGQNHDELCGFPVGMQKGSPPACPAPSYVPSPPAAPSSPPAAPQPPSKSPETPEEPKKPEEPKKPEGPKKPEGPKTPSPKKPDGPQHPQTPTGGEGVNRPFPDGEIDCGDFPSKYGAVPVDYLGLGGYTGIQHTTLVGEVFGTIRTAIAGESCTDGAMCSYACPPGYQKSQWPEQQGSTGESVGGLACRNGKLYLTNRKLSTRLCISGVGGVHIKSTISVEISICRTDYPGTESETVPVPLPP... | Function: Cell surface beta-glucosidase involved in cytokinesis, cell wall biogenesis, adhesion to host tissue; thus playing an important role in the host-pathogen interaction. Has hydrolytic activity on linear (1->3)-beta-D-glucans such as laminaribiose and other laminarioligosaccharides.
Sequence Mass (Da): 47606
Seq... |
Q59NP5 | MRFSQATVLAFAALSLAAPAFEADNKNIKREDCDKTSFHGHHKHKRAVAYDYAYVTVTVDGNGNPITTVSPVLSIETIAKSEETSSTSTSISSTTTIVQNDSLTSDEPKTLSLPSGTIKPSSFATESQSQSQSSSTGGSGSGSTNGIEGDLAAFEDPTEEFEDGVLSCSDFPSGQGVIPLDHLGFGGWSGIENSDGSTGGNCKEGSYCSYACQSGMSKTQWPEDQPSNGVSIGGLLCKNGKLYKSSTRSNYLCEWGVKKANVVNKLSETVAICRTDYPGTENMVIPTVVGGGSTSVITVVDQSTYYTWRGGATSAQYYVN... | Function: Cell surface beta-glucosidase involved in cytokinesis, cell wall biogenesis, adhesion to host tissue, and biofilm formation; thus playing an important role in the host-pathogen interaction. Has hydrolytic activity on linear (1->3)-beta-D-glucans such as laminaribiose and other laminarioligosaccharides.
PTM: P... |
Q5HBM5 | MRVLLSNDDGFHANGIKALKEIVIKSGIASEIWVVAPLNNCSGSGRSVGLNVKVQVSKVSDTEFIVDSTPSTSVFLALRKIMNYKPDLILSGINHGVNIGNDVWYSGTVAAAAEGAAINIPSIAISQEYDNKSGEINWVNPQRFLKQIIEMLMNVSFWNKSTVMNVNFPLMPAKGIKFTDQGKYVPCNEIEKNESSDDSNVSYTITRITPNKKNRAQCDGSIKAIDEGYITITPLKFDMTDFDVLTSLNSLK | 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): 27644
Sequence Length: 252
Subcellular Location: Cytoplasm
EC: 3.1.3.5
|
Q2NDM8 | MRILLTNDDGIHAPGFEVLEDIARELSDEIWVCAPAEEQSGAGHSLTLHHPVRLRQLGERRYSVTGTPTDSVMLALRTVLEDKQPDLILSGVNRGANLGDDITYSGTASAAMEGALGGIKSIALSQVYKRDAEHELFDAARTYGADVIRKLIDAPFGDRTLININFPPLPADKVRGIRAVRQGFHDYSRGSVVKGRDPRGLEYYWFGLYAIEHTLDHGTDLEAIDEGFVSVTPLQLDLTQHSLLSVIGERFE | 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: 252
Subcellular Location: Cytoplasm
EC: 3.1.3.5
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A6H213 | MSKPLILVTNDDGISAPGIRSLIAVMQEIGTVVVVAPDSPQSAMGHAITINSTLHLNKISAENAAVTEYSCSGTPVDCVKLAVNEILKQKPDLCVSGVNHGSNSSINVIYSGTMSAAVEAGIEGIPAIGFSLLDYDWNADFETFKPYIKKIALEVLQKGLPDSVVLNVNFPKRKEEDLKGIKICRQAKAMWEEKFDKRKTPQGKDYYWLTGEFVNHDKGEDTDEWALQNGYISVVPVQFDMTAHHAIQALNNWDLNK | 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): 28207
Sequence Length: 257
Subcellular Location: Cytoplasm
EC: 3.1.3.5
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C1A8T7 | MRILLSNDDGILAKGLGVLERAAESLGELHVVAPDREQSATSHSLTLHHPLRPVRLGERRWQVDGTPTDCVMLACEALLEARPDFVLSGINHGPNMGEDVLYSGTVAAAMEGLALGIPAIALSFAGNVLRADALLDTQVGAIRSLLHHLTGLPAFPADTLLNVNLPAVPGDEIRGIRLTRLGRRVFSDSIARMKDPWGRDILWIGGGSVEWSGAPDSDFRAVHDGYISVTPLHLDLTHRDVLNTSTEWWQEP | 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): 27287
Sequence Length: 252
Subcellular Location: Cytoplasm
EC: 3.1.3.5
|
Q39VS1 | MKILVTNDDGVRAPGIRSLAEALRNIGDVVVVAPDRERSAVGHALTLHHPLRASEIRPAVFAVDGTPTDCVNLGIHTLLGSRPDIVVSGVNCGGNMGDDITYSGTVSAAMEATLMGIPALAVSLATSGRGDNYAVASAFAARLVRIVSERGLPPDTLLNVNVPDLPLEKLGGAVVTIQGKRDYEGKIVTKTDPRGRNYYWIGNGSLQFRDLEGTDYYAVKRGLVSITPLHLDLTNYASLTTLKTWDFAEMTL | 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): 26884
Sequence Length: 252
Subcellular Location: Cytoplasm
EC: 3.1.3.5
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Q74CZ6 | MNILVTNDDGVHAPGIVALAEALRLVGTVTVVAPDRERSAVGHALTLHHPLRVTEIMAGIFAVDGTPTDCVNLGIHTLLAEAPDIVVSGVNRGGNLGDDITYSGTVSAALEATLMGIPAIAVSLATNGHGSNYRAAAAFAAQLAREVLDRGLPRDTFLNVNVPDLPAEELGGPVITSQGKRDYGGDIVTKVDPRGRNYYWIGGNEPVFRDIEGTDFHAVKRGRISVTPLHLDLTNYASLSILQSWDLSACRPEAGQPSGALL | 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): 27542
Sequence Length: 262
Subcellular Location: Cytoplasm
EC: 3.1.3.5
|
B7KB74 | MTTEKPLNLLISNDDGIFALGVRTLANTLAKAGHQVTVVCPDRERSATGHGLTLHQPIRAQIVEGIFDPQVTAWSCSGTPSDCIKFALSAVLFTRPDFVLSGINHGSNLGTDILYSGTVSAAMEGLIDGITSIALSLTSFSSQDFQPAANFAVDLIAKLARHPLPQPTLLNVNVPPVKSEDMAGVKLTRQGLRRYRENFEKRLDPRGKSYYWLVGEVIEEIEQPDHLHLPGHIPTDVQAIGDNYITITPLQYNLTDVQGFSDLNQTQWFDP | 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): 29676
Sequence Length: 271
Subcellular Location: Cytoplasm
EC: 3.1.3.5
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Q7NNG7 | MRILVSNDDGILAQGIRTLANTLHRAGHTVTVVCPDRERSATGHALTMHKPLRAEAVENLFEPGLAAWAINGTPSDSVKLGLDALLGERPDLVVSGINCGANLGSDVLYSGTVSAAMEGTIEGLPSIAVSLASRVRCDFQPAADFLVRFVRALEVQPLPEAFLLNVNVPALPESEILGARVCRLGMRRYRDQFVKRVDPRGVNYYWLAGEVIESEEAPDSDVVAVGEGCIAITPLKYDLTYEPGIGLLGARQWEKIFDPLAGG | 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): 28260
Sequence Length: 263
Subcellular Location: Cytoplasm
EC: 3.1.3.5
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Q8EBR5 | MMRILVSNDDGVNAPGIKALTEALAEIATVMTVAPDRNCSGASNSLTLTNPLRINRLDNGYISVHGTPTDCVHLAIRELCDGEPDMVVSGINAGANMGDDTLYSGTVAAAMEGRFLGFPAVAISLNGKAFKHYHTAAVYARRIVQGLLAHPIASDQILNINVPDLPLDEIKGISVTRLGARHKAEGIVRTQDPAGREIFWLGPPGLEQDASEGTDFHAIAHGYVSITPLTVDLTAYRQLSILQNWVDKI | 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): 26619
Sequence Length: 249
Subcellular Location: Cytoplasm
EC: 3.1.3.5
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Q83JY2 | MRILLSNYDGVHAPGIQTLAKALREFADVQVVAPDRNRSGASNSLTLESSLRTFTFENGDIAVQMGTPTDCVYLGVNALMRPRPDIVVSGINAGPNLGDDVIYSGTVAAAMEGRHLGFPALAVSLDGHKHYDTAAAVTCSILRALCKEPLRTGRILNINVQDLPLDQIKGIRVTRCGTRHPADQVIPQQDPRGNTLYWIGPPGGKCDAGPGTDFAAVDEGYVSITPLHVDLTAHSAQDVVSDWLNSVGVGTQW | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Nucleotidase with a broad substrate specificity as it can dephosphorylate various ribo- and deoxyribonucleoside 5'-monophosphates and ribonucleoside 3'-monophosphates with highest affinity to 3'-AMP. Also hydrolyzes polyphosphate (exopolyphosphatase activit... |
Q9SE51 | MATSLSKILTRSNTKRYWCSTTTSISASPSLPKQFWSRHFSAVADSSSSSSAALGSQSSSSAPPQENKRGSKWSQLLLFLPGAITFGLGSWQIVRREEKFKTLEYQQQRLNMEPIKLNIDHPLDKNLNALEFRRVSCKGVFDEQRSIYLGPRSRSISGITENGFFVITPLMPIPGDLDSMQSPILVNRGWVPRSWREKSQESAEAEFIANQSTKAKSPSNEPKSWWKFWSKTPVITKEHISAVKPVEVVGVIRGGENPSIFVPSNDPSTGQWFYVDVPAMARAVGLPENTIYVEDVHEHVDRSRPYPVPKDINTLIRSKV... | Function: Probably involved in the biogenesis of the COX complex.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 39921
Sequence Length: 354
Subcellular Location: Mitochondrion inner membrane
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Q9N5N8 | MPLPAAAFARILVVSRQRLFNTRIIHTSGSGYSITQCRFYKTTPCLTHKQSQILDLDAPKSRENREKDGGKSKKSKKSIKWSTGSVLMLTIPVFAFSLGIWQTFRLKWKLDLIEHLKGRLNQTAQELPEDLSCESLEPLEYCRVTVTGEFLHEKEFIISPRGRFDPGKKTSAAAGSMLSENEMSSHGGHLITPFRLKNSGKIILINRGWLPSFYFDPETRQKTNPRGTLTLPAIVRKTEKRPQFVGQNVPEQGVWYYRDLNQMAKHYGTEPVLLDAAYETTVPGGPIGGQTNINVRNEHLNYLTTWFTLTLVTMLMWIHK... | Function: Probably involved in the biogenesis of the COX complex.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 36842
Sequence Length: 323
Subcellular Location: Mitochondrion inner membrane
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Q556J9 | MNKNKKGFKLFFIFPVIAFGLGTWQVYRYDWKKRLIQRAKDRMEEDPIELSNSFIKNFKGSSFGDLNKYEFRRVYLNGKVIDNQYVLLGPRSIDGTLGYYVISPLQLSDGTRILLNRGWSASTPKSNYKIPYAIEELKLIHQKEKEQGQQQGNQESILYRYFNILGVISKTKERGSAFTPTNQPEKGQWYSLDVDAMADQLNTEPLMINTMDETEINSKPSSLPNPQFKRFDNDVESSFHNKHMSYIGTWYTLSASLFFIYFRYMRKLPK | Function: Probably involved in the biogenesis of the COX complex.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 31623
Sequence Length: 270
Subcellular Location: Mitochondrion inner membrane
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Q9U4F3 | MIRLGNQMCRQVAFNIQTVFRNPGTANNPRLITRKMTQQRPPVNWTTSIPNQAAKDKEKIAPLGWFLLLIPATTFGLGCWQVKRKIWKEQLIKDLNKQLSTAPVALPDDLTDLAQMEYRLVKIRGRFLHDKEMRLGPRSLIRPDGVETQGGLFSQRDSGNGYLIVTPFQLADRDDIVLVNRGWVSRKQVEPETRPLGQQQAEVELTAVVRKGEARPQFTPDHKGNVYLYRDLARMCAATGAAPVFLDAVYDPQTAAHAPIGGQTRVTLRNDHLSYLVTWFSLSAATSFLWYRQIVKRIPF | Function: Probably involved in the biogenesis of the COX complex.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34064
Sequence Length: 300
Subcellular Location: Mitochondrion inner membrane
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Q15526 | MAAVAALQLGLRAAGLGRAPASAAWRSVLRVSPRPGVAWRPSRCGSSAAEASATKAEDDSFLQWVLLLIPVTAFGLGTWQVQRRKWKLNLIAELESRVLAEPVPLPADPMELKNLEYRPVKVRGCFDHSKELYMMPRTMVDPVREAREGGLISSSTQSGAYVVTPFHCTDLGVTILVNRGFVPRKKVNPETRQKGQIEGEVDLIGMVRLTETRQPFVPENNPERNHWHYRDLEAMARITGAEPIFIDANFQSTVPGGPIGGQTRVTLRNEHLQYIVTWYGLSAATSYLWFKKFLRGTPGV | Function: Component of the MITRAC (mitochondrial translation regulation assembly intermediate of cytochrome c oxidase complex) complex, that regulates cytochrome c oxidase assembly.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 33331
Sequence Length: 300
Subcellular Location: Mitochondrion inner me... |
A9UWF0 | MATSSSVAAASKRGGGLYWALLSVPVVTFGLGTWQIFRKQQKEELIATLEAKLSKEPAALPTNPADLAHMEYERVAVTGTFLHDQEMLVGPRTVTREVFSGMADLPEAGVQVITPFRLADTGEVILVNRGFVPEAQAPPHKRAAGQVEGTVRLEGIVRHGESQTAFVPDNHPEQNTWYWIDVFTMASNRSALPVLIDATAECTPPGGFPLGGQTNITVRNEHLSYIITWYSISAITLAMWVFLRRKGGNRSGLRAPPPRRT | Function: Probably involved in the biogenesis of the COX complex.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28531
Sequence Length: 261
Subcellular Location: Mitochondrion inner membrane
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P09925 | MAAVMALAVLPRRMTRWSQWAYAGRAQFCAVRRSVFGFSVRSGMVCRPRRCCSSTAETAAAKAEDDSFLQWFLLLIPATAFGLGTWQVQRRKWKLKLIAELESRVMAEPIPLPADPMELKNLEYRPVKVRGHFDHSKELYIMPRTMVDPVREARDAGRLSSTESGAHVVTPFHCSDLGVTILVNRGFVPRKKVNPETRQKGQVLGEVDLVGIVRLTENRKPFVPENSPERNHWYYRDLEAMAKITGADPIFIDADFHSTAPGGPIGGQTRVTLRNEHMQYILTWYGLCAATSYLWFQKFVRRTPIM | Function: Component of the MITRAC (mitochondrial translation regulation assembly intermediate of cytochrome c oxidase complex) complex (By similarity). Regulates cytochrome c oxidase assembly .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34798
Sequence Length: 306
Subcellular Location: Mitochondr... |
Q9QXU2 | MAAVMALTVLRSRITRWPQWACAGPAPFCAVRRSVFGFSVRSGMVCRPHRCCSSTAETAAAKAEDDSFLQWFLLFIPATAFGLGTWQVQRRKWKLKLIAELESRVMAEPIPLPADPMELKNLEYRPVKVRGHFDHSKELYIMPRTMVDPVREARDAGRLSSTESGAYVVTPFHCSDLGVTILVNRGFVPRKKVNPETRQQGQVLGEVDLVGIVRLTENRKPFVPENNPERSLWYYRDLDAMAKRTGTDPIFIDADFNSTTPGGPIGGQTRVTLRNEHMQYIITWYGLCAATSYLWFRKFVRRTPGV | Function: Component of the MITRAC (mitochondrial translation regulation assembly intermediate of cytochrome c oxidase complex) complex, that regulates cytochrome c oxidase assembly.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34683
Sequence Length: 306
Subcellular Location: Mitochondrion inner me... |
P12297 | MLPYNVRNAGGGSVGGILRRTGQGSGTGSTILGNGNSPGALGAGKVSSSLENHRQPPLELLVFGYACKIFRDDEKAREMDHGKQLIPWMGDVNLKIDRYDVRGALCELAPHEAPPGGYGNRLEYLSAEEQRAEQLCEEERYLFLYNNEEELRLRQEEDLKRLQQETSGGCFSQVGFQYDGQSAASTSIGGSSTATSQLSPNSEESELPFVLPYTLMMAPPLDMQLPETMKQHAIIEKTARFIATQGAQMEILIKAKQANNTQFDFLTQGGHLQPYYRHLLAAIKAAKFPPAPQTPLDQQNTDKEAPSADDHSEEVAGGRR... | Function: Regulator of pre-mRNA splicing (and, possibly, of other RNA processing events). Regulates its own expression at the level of RNA processing.
Sequence Mass (Da): 106141
Sequence Length: 963
Domain: RS domain directs localization of proteins to the speckled subnuclear compartment and the purpose of this localiz... |
Q1QWP1 | MSIDFVVHDADDAVGVVVVEGVEAGQMLTGWVMDQDRTLQFEVKDAIPIGHKLAIRDLAEDETVIKYSVDIGRVVQSIRQGEHVHVHNVKTKRW | Function: Together with SuyB, desulfonates sulfolactate to pyruvate and sulfite.
Catalytic Activity: (2R)-3-sulfolactate = H(+) + pyruvate + sulfite
Sequence Mass (Da): 10548
Sequence Length: 94
Subcellular Location: Cytoplasm
EC: 4.4.1.24
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Q58Y44 | MLCVVTSDNSDFRLTAKADIPIGHKVALKALKAGDTVIKYHEDIGKMVGDAEVGGHVHTHNCKTKRW | Function: Together with SuyB, desulfonates sulfolactate to pyruvate and sulfite.
Catalytic Activity: (2R)-3-sulfolactate = H(+) + pyruvate + sulfite
Sequence Mass (Da): 7328
Sequence Length: 67
Subcellular Location: Cytoplasm
EC: 4.4.1.24
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Q58Y43 | MALDFSNATVKAWRRENGRVGVRNHVLILPVDDISNAACEAVANNVKGTLAIPHAYGRLQFGEDLELHFRTIIGTGANPNVAAVVVIGIEPEWTQVIVDGIAKTGKPVTGFSIEQKGDFETIRQAGWKAKEYVHWASELQKEDCPISDLWISTKCGESDTTTGLSSCPTVGNMYDKLLPQGIYGCFGETSEITGAEHICEKRAANPETARKFKEIWQAYSDDVIFAHQTDDLSDSQPTKGNILGGLTTIEEKALGNLEKIGRTSTYIDAMGPAETPSKGPGLYFMDSSSAAAECVTLMAAGGYVIHTFPTGQGNVVGNPI... | Function: Together with SuyA, desulfonates sulfolactate to pyruvate and sulfite.
Catalytic Activity: (2R)-3-sulfolactate = H(+) + pyruvate + sulfite
Sequence Mass (Da): 42452
Sequence Length: 393
Subcellular Location: Cytoplasm
EC: 4.4.1.24
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Q15022 | MAPQKHGGGGGGGSGPSAGSGGGGFGGSAAVAAATASGGKSGGGSCGGGGSYSASSSSSAAAAAGAAVLPVKKPKMEHVQADHELFLQAFEKPTQIYRFLRTRNLIAPIFLHRTLTYMSHRNSRTNIKRKTFKVDDMLSKVEKMKGEQESHSLSAHLQLTFTGFFHKNDKPSPNSENEQNSVTLEVLLVKVCHKKRKDVSCPIRQVPTGKKQVPLNPDLNQTKPGNFPSLAVSSNEFEPSNSHMVKSYSLLFRVTRPGRREFNGMINGETNENIDVNEELPARRKRNREDGEKTFVAQMTVFDKNRRLQLLDGEYEVAMQ... | Function: Polycomb group (PcG) protein. Component of the PRC2 complex, which methylates 'Lys-9' (H3K9me) and 'Lys-27' (H3K27me) of histone H3, leading to transcriptional repression of the affected target gene . The PRC2 complex may also serve as a recruiting platform for DNA methyltransferases, thereby linking two epig... |
Q02563 | MEEGFRDRAAFIRGAKDIAKEVKKHAAKKVVKGLDRVQDEYSRRSYSRFEEEEDDDDFPAPADGYYRGEGAQDEEEGGASSDATEGHDEDDEIYEGEYQGIPRAESGGKGERMADGAPLAGVRGGLSDGEGPPGGRGEAQRRKDREELAQQYETILRECGHGRFQWTLYFVLGLALMADGVEVFVVGFVLPSAEKDMCLSDSNKGMLGLIVYLGMMVGAFLWGGLADRLGRRQCLLISLSVNSVFAFFSSFVQGYGTFLFCRLLSGVGIGGSIPIVFSYFSEFLAQEKRGEHLSWLCMFWMIGGVYAAAMAWAIIPHYGW... | Function: Plays a role in the control of regulated secretion in neural and endocrine cells, enhancing selectively low-frequency neurotransmission. Positively regulates vesicle fusion by maintaining the readily releasable pool of secretory vesicles.
PTM: Phosphorylation by CK1 of the N-terminal cytoplasmic domain regula... |
Q7L1I2 | MDDYKYQDNYGGYAPSDGYYRGNESNPEEDAQSDVTEGHDEEDEIYEGEYQGIPHPDDVKAKQAKMAPSRMDSLRGQTDLMAERLEDEEQLAHQYETIMDECGHGRFQWILFFVLGLALMADGVEVFVVSFALPSAEKDMCLSSSKKGMLGMIVYLGMMAGAFILGGLADKLGRKRVLSMSLAVNASFASLSSFVQGYGAFLFCRLISGIGIGGALPIVFAYFSEFLSREKRGEHLSWLGIFWMTGGLYASAMAWSIIPHYGWGFSMGTNYHFHSWRVFVIVCALPCTVSMVALKFMPESPRFLLEMGKHDEAWMILKQV... | Function: Probably plays a role in the control of regulated secretion in neural and endocrine cells.
PTM: N-glycosylated.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 77444
Sequence Length: 683
Subcellular Location: Cytoplasmic vesicle
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Q63564 | MDDYRYRDNYEGYAPNDGYYRGNEQNPEEDAQSDVTEGHDEEDEIYEGEYQGIPHPDDVKSKQTKMAPSRADGLRGQADLMAERMEDEEQLAHQYETIIDECGHGRFQWTLFFVLVLALMADGVEVFVVSFALPSAEKDMCLSSSKKGMLGLIVYLGMMAGAFILGGLADKLGRKKVLSMSLAINASFASLSSFVQGYGAFLFCRLISGIGIGGSLPIVFAYFSEFLSREKRGEHLSWLGIFWMTGGIYASAMAWSIIPHYGWGFSMGTNYHFHSWRVFVIVCALPATVSMVALKFMPESPRFLLEMGKHDEAWMILKQV... | Function: Probably plays a role in the control of regulated secretion in neural and endocrine cells.
PTM: N-glycosylated.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 77502
Sequence Length: 683
Subcellular Location: Cytoplasmic vesicle
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Q496J9 | MEDSYKDRTSLMKGAKDIAREVKKQTVKKVNQAVDRAQDEYTQRSYSRFQDEEDDDDYYPAGETYNGEANDDEGSSEATEGHDEDDEIYEGEYQGIPSMNQAKDSIVSVGQPKGDEYKDRRELESERRADEEELAQQYELIIQECGHGRFQWALFFVLGMALMADGVEVFVVGFVLPSAETDLCIPNSGSGWLGSIVYLGMMVGAFFWGGLADKVGRKQSLLICMSVNGFFAFLSSFVQGYGFFLFCRLLSGFGIGGAIPTVFSYFAEVLAREKRGEHLSWLCMFWMIGGIYASAMAWAIIPHYGWSFSMGSAYQFHSWR... | Function: Plays a role in the control of regulated secretion in neural and endocrine cells, enhancing selectively low-frequency neurotransmission. Positively regulates vesicle fusion by maintaining the readily releasable pool of secretory vesicles.
PTM: N-glycosylated. Upon expression in a kidney cell line the most abu... |
Q2R3P9 | MAGMSLQHPWAFAFGLLGNIISFMTYLAPLPTFYRIYKSKSTQGFQSVPYVVALFSAMLWIYYALLKSDECLLITINSAGCVIETIYIAVYLVYAPKKAKMFTAKLLLLVNVGVFGLILLLTLLLSAGDRRIVVLGWVCVGFSVSVFVAPLSIIRLVVRTKSVEFMPFSLSFSLTISAVVWFLYGLLIKDKYVALPNVLGFSFGVIQMGLYAMYRNSTPKAVLTKEVEAATATGDDDHSAAGVKEHVVNIAKLSAAVDVVKTREVHPVDVESPPAEAPPEEDDKAAAATAAAVAGAGEKKVAA | Function: Mediates both low-affinity uptake and efflux of sugar across the plasma membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32701
Sequence Length: 303
Subcellular Location: Cell membrane
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Q9FY94 | MGVMINHHFLAFIFGILGNVISFLVFLAPVPTFYRIYKRKSTESFQSLPYQVSLFSCMLWLYYALIKKDAFLLITINSFGCVVETLYIAMFFAYATREKRISAMKLFIAMNVAFFSLILMVTHFVVKTPPLQVSVLGWICVAISVSVFAAPLMIVARVIKTKSVEYMPFTLSFFLTISAVMWFAYGLFLNDICIAIPNVVGFVLGLLQMVLYLVYRNSNEKPEKINSSEQQLKSIVVMSPLGVSEVHPVVTESVDPLSEAVHHEDLSKVTKVEEPSIENGKCYVEATRPETV | Function: Mediates both low-affinity uptake and efflux of sugar across the plasma membrane. Regulates cell viability under high salinity. Promotes senescence and sensitivity to salt stress . Contributes to seed filling by triggering sucrose efflux involved in the transfer of sugars from seed coat to embryos .
Location ... |
Q6K602 | MAFMSMERSTWAFTFGILGNLISLMVFLSPLPTFYRVYRKKSTEGFQSTPYVVTLFSCMLWMYYAFVKSGAELLVTINGVGCVIETVYLAMYLAYAPKSARMLTAKMLLGLNIGLFGVIALVTLLLSRGELRVHVLGWICVAVSLSVFAAPLSIIRLVIRTKSVEFMPFSLSFFLVLSAVIWFLYGLLKKDVFVALPNVLGFVFGVAQMALYMAYRSKKPLVASSSSAVVAAGLEIKLPEHVKEVQAVAKGAVAAAPEGRISCGAEVHPIDDVMPSEVVEVKVDDEETNRTDEMAGDGDHAMVRTEQIIKPDMAIVVEV | Function: Mediates both low-affinity uptake and efflux of sugar across the plasma membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34965
Sequence Length: 319
Subcellular Location: Cell membrane
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P0DKJ5 | MAMAMANHHTLGLIFGILGNIISFLVYFAPAPTFYRIYKRKSAEGFHSLPYIVALFSAMLWLYYALLKKDAFLLITINSFGCAIESFYILLYFFYAPMQAKKQTLKVVISLNVGVFSILVVLIQFLLKGSNRINVFGWICASFSVAVFAAPLSIVAKVIRTKSVEFMPFSLSFFLTLSAIMWFAYGLLKNDPCVAIPNILGVILGLVQMVLYGFYRNAGKEKMEKKLPEHIIDMVMLSTLGTSDIHPIGAQQNGIKKSGSEDVKDDEETGNREKSTENSGELQPNGSTV | Function: Mediates both low-affinity uptake and efflux of sugar across the plasma membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32149
Sequence Length: 289
Subcellular Location: Cell membrane
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Q9LUR4 | MADLSFYVGVIGNVISVLVFLSPVETFWRIVQRRSTEEYECFPYICTLMSSSLWTYYGIVTPGEYLVSTVNGFGALAESIYVLIFLFFVPKSRFLKTVVVVLALNVCFPVIAIAGTRTLFGDANSRSSSMGFICATLNIIMYGSPLSAIKTVVTTRSVQFMPFWLSFFLFLNGAIWGVYALLLHDMFLLVPNGMGFFLGIMQLLIYAYYRNAEPIVEDEEGLIPNQPLLA | Function: Mediates both low-affinity uptake and efflux of sugar across the vacuolar membrane. Regulates sugars homeostasis in leaves and roots by exporting/importing them through the tonoplast regarding metabolic demand . Acts as a vacuolar hexose transporter, such as glucose (Glc), fructose (Fru), and sucrose (Suc) .
... |
Q10LN5 | MADPSFFVGIVGNVISILVFASPIATFRRIVRSKSTEEFRWLPYVTTLLSTSLWTFYGLHKPGGLLIVTVNGSGAALEAIYVTLYLAYAPRETKAKMVKVVLAVNVGALAAVVAVALVALHGGVRLFVVGVLCAALTIGMYAAPMAAMRTVVKTRSVEYMPFSLSFFLFLNGGVWSVYSLLVKDYFIGIPNAIGFALGTAQLALYMAYRRTKKPAGKGGDDDEDDEEAQGVARLMGHQVEMAQQRRDQQLRKGLSLSLPKPAAPLHGGLDRIIKSFSTTPIELHSILHQHHGGHHHHHRFDTVPDDDDEAVAAGGTTPAT... | Function: Mediates both low-affinity uptake and efflux of sugar across the plasma membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35391
Sequence Length: 328
Subcellular Location: Cell membrane
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Q8RZQ8 | MEHIARFFFGVSGNVIALFLFLSPVVTFWRIIKKRSTEDFSGVPYNMTLLNCLLSAWYGLPFVSPNNILVTTINGTGSVIEAIYVVIFLIFAERKARLKMMGLLGLVTSIFTMVVLVSLLALHGQGRKLFCGLAATIFSICMYASPLSIMRLVIKTKSVEFMPFLLSLSVFLCGTSWFIYGLLGRDPFIAIPNGCGSFLGLMQLILYAIYRNHKGATPAAAAGKGDAADEVEDAKKAAAAVEMADAKTNKVVADDADADADGKSADDKVASQV | Function: Mediates both low-affinity uptake and efflux of sugar across the plasma membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 29503
Sequence Length: 273
Subcellular Location: Cell membrane
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Q60EC2 | MEDLAKFLFGVSGNVIALFLFLSPVPTFWRIIRRKSTEDFSGVPYNMTLINCLLSAWYGLPFVSPNNILVSTINGAGAVIETAYVVVFLVFASTHKTRLRTLGLAAAVASVFAAVALVSLLALHGQHRKLLCGVAATVCSICMYASPLSIMRLVIKTKSVEYMPFLMSLAVFLCGTSWFIYGLLGRDPFVTIPNGCGSFLGAVQLVLYAIYRNNKGAGGGSGGKQAGDDDVEMAEGRNNKVADGGAADDDSTAGGKAGTEV | Function: Mediates both low-affinity uptake and efflux of sugar across the plasma membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 27622
Sequence Length: 261
Subcellular Location: Cell membrane
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Q89I89 | MSGVNEIRSTFLNFFAENGHEIVPSSPLVPRNDPTLMFTNAGMVQFKNVFTGVEKRPYQRATTSQKCVRAGGKHNDLDNVGYTARHLTFFEMLGNFSFGDYFKERAIELAWKLITKDFGLNKDKLLVTVYHTDDEAHGLWKKIAGFSDDRIIRIPTSDNFWAMGDTGPCGPCSEIFIDRGDHIWGGPPGSPEEDGDRFLEFWNLVFMQYEQVTKEERVDLPRPSIDTGMGLERMACIMQGVDSVFETDLFRHLIDATASALGSGPNEQTVASFRVIADHLRSSAFLVSDGVLPSNEGRGYVLRRIMRRAMRHAQLLGAKE... | 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... |
Q8K9E7 | MKKTTNEIRQSFLNFFKEKEHVIVPSSSLIPENDSTLLFTNAGMNQFKEYFLGQKKKFYPRVTTVQNCLRTGGKHNDLENVGYTKRHHTFFEMLGNFSFNDYFKKEAITYAWELLTSRKWFNIDKNKLWISVYEDDEETYKIWRDIIRIPCHHIVKIGSKNNSQYDSENFWQMGETGPCGPCTEIFYNYDDSNKSNDFLKDKNESFIEIWNIVFIEFNRISKTKIVPLINKSIDTGMGLERISAVLQNVHSNYKIDIFQKLIQKISNFTEIKDLNNISLKIIADHIRSCAFLIAENILPSNEHRGYVLRRIIRRALRHGH... | 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... |
P59420 | MIYTSNEICQMFLNFFYKKGHTILPGSTLIPNNDPSLLFTNSGMNQFKDIFIQKNYNFKYNRVTTLQNCLRTGGKHNDFENVGYTPQHHTFFQMLGNFSFRDYFKLDAILYAWKFLTSKEQLNLSKEKLWITVYQDDLESYNIWKNIIKIDKHKIIKIGNKYNSSDSDNFWQMGEIGPCGPCTEIFYDYGNTLPGTIPGNNGCNVPRFVEIWNIVFIQFNKLSNGKLIKLTESYVDTGMGLERISAVINNVTSNYEIDLFKPLIKHILELSTVNTPKNKSIYVIADHIRACSFIISENIIPSNEKHGYVLRRIIRRAIRH... | 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... |
Q057H8 | MKTDKIRAMFLQFFKEKNHKIFKSSSLIPKDDNSLLFTNAGMNQFKKIYLKNKKKNQLSIATSQYCIRTGGKHDDLKKVGHTPYHHTLFEMLGNFSFGEYFKENAIKYAWEFLTHKKWLNLSKKKIWITYYYNDNETKKIWLNIIKIKNTHLIKIYDKKNIKYNSDNFWKMGDLGPCGPSTEIFYYQKKNRKEKKSIKSYKELEKYCLEIWNLVFMEFNQITKKKIIKLPIPSIDTGMGLERISVILQNVKSIFHTNNFIQLIEAIKKKIKIKIKKKNNVSLKIISDHIRTSTCLIAENILPGNEGRNYVLRKIIRRALC... | 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... |
Q39HB7 | MKAAEIREKFLKFFESKGHTIVRSSSLVPGNDPTLMFTNSGMVQFKDVFLGTDPRPYSRATTAQRSVRAGGKHNDLENVGYTARHHTFFEMLGNFSFGDYFKHDAIKFAWELLTTVYQLPKDKLWVTVYQEDDEAYDIWAKEVGVPTERIIRIGDNKGARYASDNFWTMGDTGPCGPCTEIFYDHGPDVWGGPPGSPEEDGDRYIEIWNLVFMQFNRDAQGNMTRLPKQSVDTGMGLERLAAVLQHVHSNYEIDLFQNLIKAAARVTEISDLTNNSLKVIADHIRACSFLIVDGVIPGNEGRGYVLRRIVRRAIRHGYKL... | 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... |
B0TFY7 | MEFTGNRVRQLFLEYFEQKGHTIVASSSLVPHNDPTLLFSNAGMNQFKDVFLGFEKRPYLRATTSQKCVRAGGKHNDLDTVGRTARHHTFFEMLGNFSFGDYFKKDAIRYAWEFLTDVCGLPKDKLYATVYLDDDEAFALWRDMIGLPEARILRLGEKDNFWAMGDTGPCGPCSEILIDRGEHLRCKAEECAIGKCDCDRWLEIWNLVFMQYNRDENGTMTPLPRPSIDTGMGLERVTSVLQKVGSNYDTDLLRPLIAFVEQLCGQVYHRDDRGFPFRVIADHIRSCTFLITDGVLPSNEGRGYVLRRILRRAVRFGKVL... | 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... |
P56452 | MDIRNEFLQFFQNKGHAVYPSMPLVPNDATLLFTNAGMVQFKDIFTGIVPRPSIPRAASSQLCMRAGGKHNDLENVGYTARHHTLFEMLGNFSFGDYFKEEAILFAWEFVTKNLGFKPKDLYISVHEKDDEAVKLWEKFVPVDRIKKMGDKDNFWQMGDSGPCGPCSEIYIDQGEKHFKGSEDYFGGEGDRFLEIWNLVFMQYERSNDGVLSPLPKPSIDTGMGLERVQALLEHKLNNFDSSLFAPLMEEISELTSLDYASEFQPSFRVVADHARAVAFLLAQGVHFNKEGRGYVLRRILRRALRHGYLMGLKEAFLYKV... | 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... |
A9B660 | MKGSELRQRFLDYFARQGHAVVPSSSLIPADNPTLLFTVAGMVQFNDVFLGRESRPYSRAVSSQKCLRISGKQNDLENVGPSPRHHTFFEMLGNFSFGDYFKKDAIRFAWEFLTQEIGLDPKRMWVSIYEGDEQIPADEEAHDLWLAYMPAERILRFDAKDNLWSAGDVGPRGPCSEIHYYIGDDPDNQVPEGVNSEDDTYMEIWNLVFMQYNRDENGVLTLLPKPSIDTGMSLERLAIVKQGVFRSYETDLFTPIIHTVMELLGTGSDHYQANSSAYHVVADHSRSIAFMIADGLRPGNEGRSYVLRRLVRRAAYFGQT... | 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... |
Q6MB06 | MLTQSIRRQFLEYFKKHQHQIVSSSSVLPHDDPTLLFNNAGMNQFKDVFLGKSYRDYNRAATSQKCIRVGGKHNDLENVGHTSRHLTFFEMLGNFSFGDYFKTQAIRFAWEVSTQVFGFEPERIWPTVFREDDETFELWTQYVPAERITRFGEKDNFWAMGDTGPCGPCSELLYDRGSDYGNATKPSEDSSGERFLEFWNLVFMQFNRQTSGVQNPLPKPSIDTGAGLERVINLKMGVNSVFETDILRSIIAQIELLSGIAYHPQDQQSAAFRVIADHLRCLSFAIADGVQPSNVDRGYVLRKVLRRAVRYGRTLKLEKP... | 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... |
A5D3F4 | MTGNEIRESYLKFFEKKGHKILPSASLIPLNDPSILWTAAGMVPFKPFFTGAAKPEYTRVTTCQKCIRTPDIESVGKTARHHTFFEMLGNFSFGDYFKESAIPWAWEFVTEHLRLPADKLWISIFLDDDEAFEIWNKTVGVPAGRIVRMGKDTNFWEIGVGPCGPCSEIYVDLGAERGCGSPECKVGCDCDRFLEIWNLVFIQFFKDEEGNYTPLTSKGIDTGFGLERVASVMQGVPTNFDTDLFREIMDFTAGLFGLKYGVDGRVDVALKVIADHCRAITFAVADGALPSNEGRGYVIRRLLRRAVRFGRLLGIEDPFL... | 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... |
Q6L1Z4 | MEFDLEFFRENNFVRKQCSVCSSYFWTLDDKRSTCGDPACNGYSFINKSPVYKKYNVDEMRDEFIKFFENDSLPHKFVEPYPVVPRWRDDVLLVNASIYDFQPQVTSGLAKPPGNPIVMSQPSIRMLDIDLVGKTGRHLTSFEMLCHDSFNYDDNYIYWKDETVRYSFRFLTERLRVDPLLITYKEKPWFGGGNAGNALEVFVMGLEVATLVFMDLKEDKNGDIELEGTRYSRMPLRVVDTGYGLERLVWLSTGTPTVYESIYKRSLDYIIKNSNAEYVSPEIMARISEIAAEIDPYSDELVLSRINKTGDKKFMEMLDN... | 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... |
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