ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
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F1RAX4 | MSAETVNNYDYSDWYENAAPTKAPVEVIPPCDPTADEGLFHICIAAISLVVMLVLAILARRQKLSDNQRGLTGLLSPVNFLDHTQHKGLAVAVYGVLFCKLVGMVLSHHPLPFTKEVANKEFWMILALLYYPALYYPLLACGTLHNKVGYVLGSLLSWTHFGILVWQKVDCPKTPQIYKYYALFGSLPQIACLAFLSFQYPLLLFKGLQNTETANASEDLSSSYYRDYVKKILKKKKPTKISSSTSKPKLFDRLRDAVKSYIYTPEDVFRFPLKLAISVVVAFIALYQMALLLISGVLPTLHIVRRGVDENIAFLLAGFNIILSNDRQEVVRIVVYYLWCVEICYVSAVTLSCLVNLLMLMRSMVLHRSNLKGLYRGDSLNVFNCHRSIRPSRPALVCWMGFTSYQAAFLCLGMAIQTLVFFICILFAVFLIIIPILWGTNLMLFHIIGNLWPFWLTLVLAALIQHVASRFLFIRKDGGTRDLNNRGSLFLLSYILFLVNVMIGVVLGIWRVVITALFNIVHLGRLDISLLNRNVEAFDPGYRCYSHYLKIEVSQSHPVMKAFCGLLLQSSGQDGLSAQRIRDAEEGIQLVQQEKKQNKVSNAKRARAHWQLLYTLVNNPSLVGSRKHFQCQSSESFINGALSRTSKEGSKKDGSVNEPSKEAESAAASN | 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
Sequence Mass (Da): 75397
Sequence Length: 670
Domain: Contrary to predictions, contains nine transmembrane helices, with an extracellular N-terminus and a cytoplasmic C-terminus. Besides, contains one long helix that dips into the membrane and then runs more or less parallel to the membrane surface.
Subcellular Location: Cell membrane
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Q9BX79 | MSSQPAGNQTSPGATEDYSYGSWYIDEPQGGEELQPEGEVPSCHTSIPPGLYHACLASLSILVLLLLAMLVRRRQLWPDCVRGRPGLPSPVDFLAGDRPRAVPAAVFMVLLSSLCLLLPDEDALPFLTLASAPSQDGKTEAPRGAWKILGLFYYAALYYPLAACATAGHTAAHLLGSTLSWAHLGVQVWQRAECPQVPKIYKYYSLLASLPLLLGLGFLSLWYPVQLVRSFSRRTGAGSKGLQSSYSEEYLRNLLCRKKLGSSYHTSKHGFLSWARVCLRHCIYTPQPGFHLPLKLVLSATLTGTAIYQVALLLLVGVVPTIQKVRAGVTTDVSYLLAGFGIVLSEDKQEVVELVKHHLWALEVCYISALVLSCLLTFLVLMRSLVTHRTNLRALHRGAALDLSPLHRSPHPSRQAIFCWMSFSAYQTAFICLGLLVQQIIFFLGTTALAFLVLMPVLHGRNLLLFRSLESSWPFWLTLALAVILQNMAAHWVFLETHDGHPQLTNRRVLYAATFLLFPLNVLVGAMVATWRVLLSALYNAIHLGQMDLSLLPPRAATLDPGYYTYRNFLKIEVSQSHPAMTAFCSLLLQAQSLLPRTMAAPQDSLRPGEEDEGMQLLQTKDSMAKGARPGASRGRARWGLAYTLLHNPTLQVFRKTALLGANGAQP | 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 retinol to all-trans retinyl esters, the storage forms of vitamin A . Contributes to the activation of a signaling cascade that depends on retinol transport and LRAT-dependent generation of retinol metabolites that then trigger activation of JAK2 and its target STAT5, and ultimately increase the expression of SOCS3 and inhibit cellular responses to insulin . Important for the homeostasis of vitamin A and its derivatives, such as retinoic acid . STRA6-mediated transport is particularly important in the eye, and under conditions of dietary vitamin A deficiency (Probable). Does not transport retinoic acid .
PTM: Phosphorylated on tyrosine residues in response to RBP4 binding . Phosphorylation requires the presence of LRAT, suggesting it may be triggered by the uptake of retinol that is then metabolized within the cell to retinoids that function as signaling molecules .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 73503
Sequence Length: 667
Domain: Contrary to predictions, contains nine transmembrane helices, with an extracellular N-terminus and a cytoplasmic C-terminus (By similarity). Besides, contains one long helix that dips into the membrane and then runs more or less parallel to the membrane surface (By similarity).
Subcellular Location: Cell membrane
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Q7Z7C7 | MGKIDVDKILFFNQEIRLWQLIMATPEENSNPHDRATPQLPAQLQELEHRVARRRLSQARHRATLAALFNNLRKTVYSQSDLIASKWQVLNKAKSHIPELEQTLDNLLKLKASFNLEDGHASSLEEVKKEYASMYSGNDSFPQNGSSPWYLNFYKQTMDLLTGSGIITPQEAALPIVSAAISHLWQNLSEERKASLRQAWAQKHRGPATLAEACREPACAEGSVKDSGVDSQGASCSLVSTPEEILFEDAFDVASFLDKSEVPSTSSSSSVLASCNPENPEEKFQLYMQIINFFKGLSCANTQVKQEASFPVDEEMIMLQCTETFDDEDL | 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 meiotic initiation, promotes (but is not required for) spermatogonial differentiation. In complex with MEIOSIN, directly activates the transcription of a subset of critical meiotic genes playing a central role in cell-cycle switching from mitosis to meiosis.
PTM: Phosphorylated.
Sequence Mass (Da): 36908
Sequence Length: 330
Subcellular Location: Cytoplasm
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P70278 | MATPGEGNQPSDDGAPQPLAQLQKLEPRVVRRRLSQARHRATLVGLFNNLRKAVYSQSDITASKWQVLNRTKIHIQEQEESLDKLLKLKASFNLQDGNPNSLEEVKEEYARMYSENDSVFLNSFLQDSPPEWFPSEAVGPDAEEEGEEEGEEEGEEGEEEEEGDEEGEEEEENGEEREVEEYQEEEEEEEEEEKKVDLSHSSSTLLPDLMEFERYLNFYKQTMDLLTMNSIISAHEVTLPIVSAAISHLWQTLSEEKKARLLQVWEQQHSAFADLTEACLELAGVEGSMKDSGVDSQGASCSLESTPEEILFEDAFDVASFLDKSEAQHMSNISAMFATCNSENPEEKFQLYIQIIEFFKSLGCVNTPLNQEPEPPDDDDAMLLKCLETFDDL | 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 meiotic initiation, promotes (but is not required for) spermatogonial differentiation . In complex with MEIOSIN, directly activates the transcription of a subset of critical meiotic genes playing a central role in cell-cycle switching from mitosis to meiosis .
PTM: Phosphorylated in P19 EC cells.
Sequence Mass (Da): 44555
Sequence Length: 393
Subcellular Location: Cytoplasm
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Q5ZK47 | MSNFLPDSSCYELLTIIGRGFEDLMVVNLARYKPSGEYVTVRRVNLEACTNEMVTFLQGELHVSKLFNHPNIVPYKATFIADNELWVVTSFMAYGSAKDLICTHFMDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLSGLRSNLSMINHGQRLKVVHDFPKYSIKVLPWLSPEVLQQNLQGYDAKSDIYSIGITACELANGHVPFKDMPSTQMLLEKLNGTVPCLLDTTTIPADELTMKTSRSSANYGLGESTAVSNVRAANGESTLHPYLRTFSSCFHNFVGQCLQRNPDFRPSAGALLNHPFFKQIKRRASEALPELLRPVTPITNFEGTRPQDPSGILGWCQTWSSWMWMTGNSRKTKTALGSGGAFWTL | 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 similarity).
Sequence Mass (Da): 43397
Sequence Length: 389
Domain: The protein kinase domain is predicted to be catalytically inactive.
Subcellular Location: Nucleus
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Q7RTN6 | MSFLVSKPERIRRWVSEKFIVEGLRDLELFGEQPPGDTRRKTNDASSESIASFSKQEVMSSFLPEGGCYELLTVIGKGFEDLMTVNLARYKPTGEYVTVRRINLEACSNEMVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVTSFMAYGSAKDLICTHFMDGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLSGLRSNLSMISHGQRQRVVHDFPKYSVKVLPWLSPEVLQQNLQGYDAKSDIYSVGITACELANGHVPFKDMPATQMLLEKLNGTVPCLLDTSTIPAEELTMSPSRSVANSGLSDSLTTSTPRPSNGDSPSHPYHRTFSPHFHHFVEQCLQRNPDARPSASTLLNHSFFKQIKRRASEALPELLRPVTPITNFEGSQSQDHSGIFGLVTNLEELEVDDWEF | 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 Mass (Da): 48369
Sequence Length: 431
Domain: The protein kinase domain is predicted to be catalytically inactive.
Subcellular Location: Nucleus
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Q9P2W9 | MAVDITLLFRASVKTVKTRNKALGVAVGGGVDGSRDELFRRSPRPKGDFSSRAREVISHIGKLRDFLLEHRKDYINAYSHTMSEYGRMTDTERDQIDQDAQIFMRTCSEAIQQLRTEAHKEIHSQQVKEHRTAVLDFIEDYLKRVCKLYSEQRAIRVKRVVDKKRLSKLEPEPNTKTRESTSSEKVSQSPSKDSEENPATEERPEKILAETQPELGTWGDGKGEDELSPEEIQMFEQENQRLIGEMNSLFDEVRQIEGRVVEISRLQEIFTEKVLQQEAEIDSIHQLVVGATENIKEGNEDIREAIKNNAGFRVWILFFLVMCSFSLLFLDWYDS | 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 | MAVDITLLFRASVKTVKTRNKALGVAVGGGADGSRDELFRRSPRPKGDFSSRAREVISHIGKLRDFLLEHRKEYINAYSHTMSDYGRMTDTERDQIDQDAQIFIRTCSEAIHQLRTEAHKEIHSQQVKEHRTAVLDFVDDYLKRVCKLYSEQRAIRVKRVVDKKRLSKLEPEPHTKRKDSTSEKAPQNASQDSEGKPAAEELPEKPLAESQPELGTWGDGKGEDELSPEEIQMFEQENQRLIGEMNSLFDEVRQIEGKVVEISRLQEIFTEKVLQQETEIDSIHQLVVGATENIKEGNEDIREAIKNNAGFRVWILFFLVMCSFSLLFLDWYDS | 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 localized on the plasma membrane while VAMP2 resides in synaptic vesicles. The pairing of the three SNAREs from the N-terminal SNARE motifs to the C-terminal anchors leads to the formation of the SNARE complex, which brings membranes into close proximity and results in final fusion (By similarity). Participates in the calcium-dependent regulation of acrosomal exocytosis in sperm. Also plays an important role in the exocytosis of hormones such as insulin or glucagon-like peptide 1 (GLP-1) (By similarity).
PTM: Phosphorylated by CK2. Phosphorylation at Ser-188 by DAPK1 significantly decreases its interaction with STXBP1 (By similarity).
Location Topology: Single-pass type IV membrane protein
Sequence Mass (Da): 33091
Sequence Length: 288
Subcellular Location: Cytoplasmic vesicle
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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 . Through binding to unc-18 mediates the release of the neurotransmitter acetylcholine from cholinergic motor neurons, and thereby promotes locomotory behaviors . Essential for embryonic viability and development. Has a role in dauer formation and adult life span . Required for locomotion . Probably by regulating neuronal transmission downstream of lin-3 and receptor lin-23 and phospholipase plc-3 and upstream of innexin unc-7 and egl-4/PKG in ALA neurons, involved in the decrease in pharyngeal pumping during the quiescent state that precedes each larval molt .
Location Topology: Single-pass type IV membrane protein
Sequence Mass (Da): 33253
Sequence Length: 291
Subcellular Location: Cell membrane
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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 contractions . Recruited by Unc-13-4B to secretory lysosome-related organelles (SLs) that are essential for tracheal lumen fusion between previously separate tracheal branches (anastomosis). Possibly promotes the intracellular fusion of the extending tracheal stalk cell lumens in tracheal fusion cells (Fcs) by interacting with complementary SNAREs (such as Syb) present in the apical membrane of the FC-FC interface and the membranes of the separate tracheal stalk cells .
Location Topology: Single-pass type IV membrane protein
Sequence Mass (Da): 33648
Sequence Length: 291
Subcellular Location: Cytoplasmic vesicle
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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 localized on the plasma membrane while VAMP2 resides in synaptic vesicles. The pairing of the three SNAREs from the N-terminal SNARE motifs to the C-terminal anchors leads to the formation of the SNARE complex, which brings membranes into close proximity and results in final fusion. Participates in the calcium-dependent regulation of acrosomal exocytosis in sperm . Also plays an important role in the exocytosis of hormones such as insulin or glucagon-like peptide 1 (GLP-1) (By similarity).
PTM: Phosphorylated by CK2 (By similarity). Phosphorylation at Ser-188 by DAPK1 significantly decreases its interaction with STXBP1.
Location Topology: Single-pass type IV membrane protein
Sequence Mass (Da): 33023
Sequence Length: 288
Subcellular Location: Cytoplasmic vesicle
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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 localized on the plasma membrane while VAMP2 resides in synaptic vesicles. The pairing of the three SNAREs from the N-terminal SNARE motifs to the C-terminal anchors leads to the formation of the SNARE complex, which brings membranes into close proximity and results in final fusion. Participates in the calcium-dependent regulation of acrosomal exocytosis in sperm . Also plays an important role in the exocytosis of hormones such as insulin or glucagon-like peptide 1 (GLP-1) .
PTM: Phosphorylated by CK2. Phosphorylation at Ser-188 by DAPK1 significantly decreases its interaction with STXBP1 (By similarity).
Location Topology: Single-pass type IV membrane protein
Sequence Mass (Da): 33054
Sequence Length: 288
Subcellular Location: Cytoplasmic vesicle
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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 localized on the plasma membrane while VAMP2 resides in synaptic vesicles. The pairing of the three SNAREs from the N-terminal SNARE motifs to the C-terminal anchors leads to the formation of the SNARE complex, which brings membranes into close proximity and results in final fusion . Participates in the calcium-dependent regulation of acrosomal exocytosis in sperm (By similarity). Also plays an important role in the exocytosis of hormones such as insulin or glucagon-like peptide 1 (GLP-1) (By similarity).
PTM: Phosphorylated by CK2. Phosphorylation at Ser-188 by DAPK1 significantly decreases its interaction with STXBP1.
Location Topology: Single-pass type IV membrane protein
Sequence Mass (Da): 33067
Sequence Length: 288
Subcellular Location: Cytoplasmic vesicle
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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
Subcellular Location: Membrane
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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
Subcellular Location: Membrane
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L8FSM5 | MKFSQSLIALAACFLPLIAAAPEEAQHAKIRSPGAQDIILDSYIVVFNKGVNDADIESEFASVSHILSKRRPAHKGVGHKYNITGFKGYQIETDTGSIGEIAASPLVAWIERDGKVQANALETRSGATWGLGRISHKATGSNSYVYDSSAGSGSTVYVVDSGIYIEHSEFEGRAKWGANYISGSPDTDENGHGTHCAGTIAGATYGVASKANLVAVKVLDGDGSGSNSGVIAGINFVGQNGKDGKSVLSMSLGGSYSAALNSAVESTISNGVTVVVAAGNDGADASNYSPASAKNAITVGAVDSTDTRADFSNYGSVLDVFAPGVDVKSAWIGSKSASNTISGTSMATPHVAGLAAYLIGLGGLSSPAAVASKIASIGIQGSVKDPKGSVNLIAYNGNGA | 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 mammalian host. Degrades the nonhelical regions of collagen that function in the cross-linking of the helical components . May function as virulence factor involved in epidermal wing necrosis observed in white nose syndrome (WNS) in bats (By similarity).
Sequence Mass (Da): 40489
Sequence Length: 400
Subcellular Location: Secreted
EC: 3.4.21.-
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O13792 | MASAQEDLIDYEEEEELVQDQPAQEITPAADTAENGEKSDKKGSYVGIHSTGFRDFLLKPELLRAITDSGFEHPSEVQQVCIPQSILGTDVLCQAKSGMGKTAVFVLSTLQQIEPVDGEVSVLVLCHTRELAFQIKNEYARFSKYLPDVRTAVFYGGINIKQDMEAFKDKSKSPHIVVATPGRLNALVREKILKVNSVKHFVLDECDKLLESVDMRRDIQEVFRATPPQKQVMMFSATLSNEIRPICKKFMQNPLEIYVDDETKLTLHGLQQHYVKLEEKAKNRKINDLLDSLEFNQVVIFVKSVSRANELDRLLRECNFPSICIHGGLPQEERIKRYKAFKDFDKRICVATDVFGRGIDIERVNIVINYDMPDSPDSYLHRVGRAGRFGTKGLAITFSSSEEDSQILDKIQERFEVNITELPDEIDVGSYMNA | 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 for targeting mRNA-protein complex to the proteins of the nucleoporin complex (NPC).
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 49231
Sequence Length: 434
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Subcellular Location: Nucleus
EC: 3.6.4.13
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Q6CH90 | MSHEGEEELLDYSDSEEIALPSTTVESGSNGDAKAETTTVKEENTEQKGSYVGIHSTGFRDFLLKPELLRAIVDCGFEHPSEVQQVCIPQSILGTDVLCQAKAGVGKTAVFVLSTLQQLEPVPGECSVVVLCHTRELAYQIMNEYARFSKYLPDVKTAVFYGGSPIQKDIELIQNKETSPHVIVATPGRLHALVRDKHLRLGNVKTFVIDECDKVLDQIDMRRDVQEIFRVTPRQKQVMMFSATLSQEIRPICKKFMSSPLEILVDDEGKLTLHGLQQYYVDVEEKSKNRKLGDLLDNLEFNQVIIFVKSTSRANGLSQVLNANGFPCTAVHSGIPQEERIARYKEFKEFKKRICVSTDVFGRGIDIERINLAINYDLPAEADQYLHRVGRAGRFGTKGLAISFVSTPEDKEVLAKIQERFEVNIAPYPAEGVDPSTYMNS | 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: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 49381
Sequence Length: 441
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Subcellular Location: Nucleus
EC: 3.6.4.13
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Q07478 | MSHEGEEDLLEYSDNEQEIQIDASKAAEAGETGAATSATEGDNNNNTAAGDKKGSYVGIHSTGFKDFLLKPELSRAIIDCGFEHPSEVQQHTIPQSIHGTDVLCQAKSGLGKTAVFVLSTLQQLDPVPGEVAVVVICNARELAYQIRNEYLRFSKYMPDVKTAVFYGGTPISKDAELLKNKDTAPHIVVATPGRLKALVREKYIDLSHVKNFVIDECDKVLEELDMRRDVQEIFRATPRDKQVMMFSATLSQEIRPICRRFLQNPLEIFVDDEAKLTLHGLQQYYIKLEEREKNRKLAQLLDDLEFNQVIIFVKSTTRANELTKLLNASNFPAITVHGHMKQEERIARYKAFKDFEKRICVSTDVFGRGIDIERINLAINYDLTNEADQYLHRVGRAGRFGTKGLAISFVSSKEDEEVLAKIQERFDVKIAEFPEEGIDPSTYLNN | 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.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 50309
Sequence Length: 446
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Subcellular Location: Nucleus
EC: 3.6.4.13
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Q8I430 | MINRQYFIWYIFIFNIINKIYFENIRYVKNYEVVIRKKKNIERGIGNDFAFIRRYYKSRLLSDVSYKNNSIKGKNRVDKEGDIKKYDNNDDNKMDNSYDYKNKSIKENETKIRKEQVISLDKRYNRNINEKEEIKKKIKDIQRKRLIIYFKQDNTILSSRNYKHIFMKVLSSCGHIEKLTFINFYLYEFPKSINNEDMLLKICLRLLESRRINVENDNQISHTVQMKSYNNNNNKWDNINSKNNCIYQIKDKIKDLPNVSPSASTFTSISTSPYTLKLRDRNKYANDKNHIFKINHSNKHKNNNNNNNNNDYHNNNKSNYHSHSSAKCQTQRLNKKMIGTNILDGYDIIQMEEGLNLSHNYELNDVNVCIIDTGIDENHIDLKDNIIEKKTFMKHSYKKYNIDGINNIESDNIDGINNIESDNIDGINNIESDNIDGINNIESDNIDGINNIESDNIDGINNIKSSDNIKSSDNIKSSDNINSSDNIKSSDNNNVHTMLRNKLYLKKKKECSNYNTSNDGHGHGTFIAGIIAGNSPKGKKGIKGISKKAKLIICKALNNNNAGYISDILECFNFCAKKKARIINASFASTTHYPSLFQALKELQDKDILVISSSGNCSSNSKCKQAFQECNLNIQKLYPAAYSADLNNIISVSNIIQQSNGNIVLSPDSCYSPNYVHLAAPGGNIISTFPNNKYAISSGTSFSASVITGLASLVLSINSNLTSQQVIELFKKSIVQTKSLENKVKWGGFINVYDLVRFTIDSLPKDKDE | 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 | MLFSKSLVALVACFLPLIVSATELKLRNAAATNVAADSYIVVYKDIDDSTFESEMFNVHSFLSKRDSTFRGLGHKYKMPKFKGYQIESDMDTVNRISQSPHVAYVDKDVKVSAYDLSVRIGAPWGLDRISHRNGTSPGLEEYTYDSSAGGGTTIYIIDTGVYIEHVEFEGRATFGANFIPGSPDTDEDGHGTHVAGIAAGANFGVASKAKIIAVRVLDANGDGKGSNVLAGMQWAADDAGKKNQTAKSVINMSLGADYSEAFNKATEAIIAKGIVVVAAAGNEDANASGVSPASTVDAITVGATDRNDSRAAFSNWGVALDVFAPGVDILSAWIGGKDANKTISGTSMACPHVAGLAAYFIGLEKNGTSTPSKIATKIKGVATKNVVLHPKNSRDNLAYNDDGY | 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 epidermal wing necrosis observed in white nose syndrome (WNS) in bats (By similarity).
Sequence Mass (Da): 42540
Sequence Length: 404
Subcellular Location: Secreted
EC: 3.4.21.-
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B3FHP0 | MLRMAPKTVGAVRNLNIHEWQSKQLIQKYGGRAQSGEVAFSPERSRDIAKKLWNQFPGCKFVVKAQVLAGGRGKGHWEHGMQGGVKLAKTPEEVYEIANEMIGHKLITKQTGAKGINCNKVMVCGAVKILKEFYLSILLDRAMGCPVIIATSQGGMGIEEVAQKCPECLFKVPISVKNGPTNEQLVKLAKDLGLEGDLVQDCVDNVKALYQVFDKCDSTMVEINPLGVIETPTDEKVICCLDAKIAFDKDAAFRQKEIFALRDKSREDPRDVRASLADLNYVGLDGDIGCMVNGAGLAMATMDTINYFGGSAANFLDVGGNAKKEQITEALRILNSDKHVKSILINIFGGIMRCDVVAQGIMDAVREMKLDLPLVVRLEGTNVAKGKEILKSSGLNIIPANDLGDAAKKAVASLKH | 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 enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit.
Catalytic Activity: ATP + CoA + succinate = ADP + phosphate + succinyl-CoA
Sequence Mass (Da): 45145
Sequence Length: 416
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle; succinate from succinyl-CoA (ligase route): step 1/1.
Subcellular Location: Hydrogenosome
EC: 6.2.1.5
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Q9P567 | MFKLGRNRALASAFAATSRAPLASRLPSVSQQQRRALSIHEYLSADLLRQYGIGVPKGDVARTGAEAEAIAKQIGGEDMVIKAQVLAGGRGKGTFDNGLKGGVRVIYSPTEAKMFAEQMIGHKLITKQTGAQGRLCSAVYICERKFARREFYLAVLMDRASQGPVIVSSSQGGMDIEGVAKENPEAIHTTYIDINVGVTDEMARDIATKLGFSEQCVEEAKDTIQKLYKIFCEKDATQIEINPLSETSDHKVMAMDAKFGFDDNADFRQPDIFKLRDTTQEDPDEVRAAQAGLNFIKLDGDIGCLVNGAGLAMATMDIIKLNGGQPANFLDVGGGATPAAIREAFELITSDPKVTAIFVNIFGGIVRCDAIAHGLINTVKSLDLKIPIIARLQGTNMEAARQLINDSGMKIFSIDDLQSAAEKSVQLSKVVKMARDIDVGVEFTLGI | 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 enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit.
Catalytic Activity: ATP + CoA + succinate = ADP + phosphate + succinyl-CoA
Sequence Mass (Da): 48210
Sequence Length: 447
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle; succinate from succinyl-CoA (ligase route): step 1/1.
Subcellular Location: Mitochondrion
EC: 6.2.1.5
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Q6K9N6 | MVRGSLGKLASRALSVAGKWQHQQLRRLNIHEYQGAELMGKYGINVPRGAAAGSVEEVKNTLKNVFPSEKEIVVKSQILAGGRGLGTFKSGLQGGVHIVKAEEAESLAAKMLGQILVTKQTGPQGKIVSKVYLCEKLSLVNEMYFAITLDRNTAGPLIIACSKGGTSIEDLAEKYPDMIIKVPIDVFKGITDDDAAKVVDGLAPKTADRQSSIEQIKKLYELFCKSDCTLLEINPLAETADNKLVAADAKLNFDDNAAFRQKEIFAMRDTTQEDPREVAAAKADLNYIGLDGEIGCMVNGAGLAMATMDIIKLHGGTPANFLDVGGSASEGQVVEAFKILTSDDRVKAILVNIFGGIMKCDVIASGIVNAAKQVDLKVPVVVRLEGTNVDQGKRILKESGMTLITAEDLDDAAEKAVKASVK | 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 enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit.
Catalytic Activity: ATP + CoA + succinate = ADP + phosphate + succinyl-CoA
Sequence Mass (Da): 45091
Sequence Length: 422
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle; succinate from succinyl-CoA (ligase route): step 1/1.
Subcellular Location: Mitochondrion
EC: 6.2.1.5
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Q84LB6 | MLRKLANQSLSVAGKWQQQQLRRLNIHEYQGAELMSKYGINVPKGVAVASLDEVKKAIQDVFPNQSEVVVKSQVLAGGRGLGTFKNGFQGGVHIVKADQAEDIASKMLGQILVTKQTGAQGKVVSKVYLCEKMSLVNEMYFSIILDRATAGPLIIACRKGGTSIEDLAEKFPDMIIKVPIDVFKGISDADAAKVVDGLAPKVADRNDSIEQVKKLYKLFCETDCTMLEINPLAETSDNKLVAADAKLNFDDNAAYRQKEIFSLRDSSQEDPREVAAAKADLNYIGLDGEIGCMVNGAGLAMATMDIIKLHGGTPANFLDVGGNATEGQVVEAFKILTADEKVKAILVNIFGGIMKCDVIASGIVNAAKQVQLKVPVIVRLEGTNVEQGKRILKESGMKLITAEDLDDAAEKAVKALA | 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 enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit.
Catalytic Activity: ATP + CoA + succinate = ADP + phosphate + succinyl-CoA
Sequence Mass (Da): 44840
Sequence Length: 417
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle; succinate from succinyl-CoA (ligase route): step 1/1.
Subcellular Location: Mitochondrion
EC: 6.2.1.5
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Q03184 | MLSSSFARNFNILEWQSKEICAKYNVAAGINLVARSPEEAAEAFRKMNLPAAVIKAQVYCGGRGKGHWLETGFKSGVHFVKSADEAAKIAKEMLGHHLVTKQTGKDGLLCQAVMLSDPVEVKRELYFAILLDRQTQSPVVIASTEGGVEIEEVAAHHPEKIHKFVLDGVEGITEEVAKNISTKLGLTGKAYDNGVVEMQKLWKLFVGSDATQVEVNPLAETTDGRIITVDSKFNFDDSAHYRQKQIFGYRDLKQVNPFEIRAEKYGLNYVPLDGNVACLVNGAGLAMATMDVIKLAGGDPANFLDLGGAASEAAVTEGFTIISQQSHVKAILVNIFGGIVRCDMVAAGVIAAFKKVGLKVPLVVRLEGTNVEAGKKLIRESGLPIISADNLTDAGEKAVKAAKGEKF | 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 enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit.
Catalytic Activity: ATP + CoA + succinate = ADP + phosphate + succinyl-CoA
Sequence Mass (Da): 43829
Sequence Length: 407
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle; succinate from succinyl-CoA (ligase route): step 1/1.
Subcellular Location: Hydrogenosome
EC: 6.2.1.5
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P53312 | MYSRKSLSLISKCGQLSRLNAQAALQARRHLSIHEYRSAQLLREYGIGTPEGFPAFTPEEAFEAAKKLNTNKLVIKAQALTGGRGKGHFDTGYKSGVHMIESPQQAEDVAKEMLNHNLITKQTGIAGKPVSAVYIVKRVDTKHEAYLSILMDRQTKKPMIIASSQGGMNIEEVAERTPDAIKKFSIETSKGLSPQMAKDVAKSLGFSPDAQDEAAKAVSNLYKIFMERDATQVEINPLSEIEHDPTHKIMCTDAKFGFDDNASFRQEKIYSWRDLSQEDPDEVKAKKYDLNFVKLKGNIGCLVNGAGLAMATMDVIKLNGGDPANFLDCGGGATPETIKQGFELILSNKNVDAIFVNIFGGIVRCDYVALGLVEAARELEVRVPIVARLQGTKVEEGRDIINKSGVKIYSFDELDPAAKKVVELTQN | 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 enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit (By similarity).
Catalytic Activity: ATP + CoA + succinate = ADP + phosphate + succinyl-CoA
Sequence Mass (Da): 46901
Sequence Length: 427
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle; succinate from succinyl-CoA (ligase route): step 1/1.
Subcellular Location: Mitochondrion
EC: 6.2.1.5
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O28732 | MRLHEHQAKQIFAKHGIRVPRGEVATSPEEAEKIAEKLGGRVVVKAQILVGGRGKAGGVKKANSPEEAKEVAKKILGMTIKGHRVEKVLVEEQLNMRKEYYVGYVVDKSSRLPTVIFSRMGGMDVEEIAAKHPDAIHRIYFDPLWGLKDYEVRKALFRAGFEGEEFKQMFDIIKKLVDIAFAYEAELTEINPLAVTDEGFLAADARLNTDDNALYRHPELAELREATEEDPLEREARLKGINYVHLGGNVGVIANGAGLAMATMDIINLMGGKPANFLDTGGGLADPVKMKNCLLHVLKDPNVRVVFINIYAEITRCEKVAEGIILALDEAPRKVPLVVKLAGTNEEIGREMLERYSSEKGAEIHFVESIEEGARKAVELAG | 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 specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit.
Catalytic Activity: ATP + CoA + succinate = ADP + phosphate + succinyl-CoA
Sequence Mass (Da): 42205
Sequence Length: 382
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle; succinate from succinyl-CoA (ligase route): step 1/1.
EC: 6.2.1.5
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Q9KY56 | MDLFEYQARDLFAKHDVPVLAGEVIDTPEAAREITERLGGKSVVKAQVKVGGRGKAGGVKLAASADEAVARATDILGMDIKGHTVHKVMIAETAPEIVEEYYVSFLLDRANRTFLSIASVEGGVEIEEVAATRPEAVAKTPIDAIDGVTPEKAREIVEAAKFPAEVADKVADILVKLWDTFIKEDALLVEVNPLAKVVSGDVIALDGKVSLDDNAEFRHPDFEALHDKAAANPLEAAAKEKNLNYVKLDGEVGIIGNGAGLVMSTLDVVAYAGEAHGNVKPANFLDIGGGASAQVMANGLEIILGDPDVRSVFVNVFGGITACDEVANGIVQALKLLEDRGEKVEKPLVVRLDGNNAELGRKILTDANHPLVQRVDTMDGAADKAAELAHAAAK | 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 specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit.
Catalytic Activity: ATP + CoA + succinate = ADP + phosphate + succinyl-CoA
Sequence Mass (Da): 41602
Sequence Length: 394
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle; succinate from succinyl-CoA (ligase route): step 1/1.
EC: 6.2.1.5
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O87840 | MDLYEHQARELFKEHGIVVPRAEVTDSPERAREIARALGGRAVVKAQVKTGGRGKAGGVRLAADPAEAEEAARHILGMDIRGHTVDTVMLAEPCEIEREFYVSYVLDRASGGFLAIASAEGGTEIEEVAARRPEAVARIPVDPATGVHTATAVRIADAAGLPPQTVDTLVRLWKVLVREDALLVEVNPLVRTAEGRIVALDGKVTLDDNARFRQSRWGETRQEDADSLEARAGAKGLNYVKLDGEVGVIGNGAGLVMSTLDVVAGCGARPANFLDIGGGASARVMADGLSVVLSDPDVRSVLVNVFGGITACDAVADGIVRALDEVRLTKPLVVRLDGNNAARGRALLDARAHPLVEQATTMDGAARRAARLATAASTAGQAG | 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 specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit.
Catalytic Activity: ATP + CoA + succinate = ADP + phosphate + succinyl-CoA
Sequence Mass (Da): 40162
Sequence Length: 383
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle; succinate from succinyl-CoA (ligase route): step 1/1.
EC: 6.2.1.5
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Q6F8L4 | MNLHEYQAKALLKKYGVSVQEGILARSAEEAVAAFEQLGGKFAVIKAQVHAGGRGKAGGVKVVKSKEEAADYANQLIGTNLVTYQTDANGQPVNSVLVCEDVYPVERELYLGAVVDRSSRRVTFMASTEGGVEIEKVAEETPEKIIKVEVDPLVGLQPFQAREVAFALGLKDKQIGQFVKLMAGAYQAFVENDFALFEINPLSVRENGDILAVDAKIGIDSNALYRLPEIAASRDKSQENERELKASEFELNYVALEGNIGCMVNGAGLAMATMDIIKLYGGQPANFLDVGGGATKERVIEAFKLILADTSVQGVLINIFGGIVRCDMIAEAIIAAVQEVNVTVPVVVRLEGNNAELGAKILDESGLKLTSANGLSDAAEKIVAAVKG | 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 specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit.
Catalytic Activity: ATP + CoA + succinate = ADP + phosphate + succinyl-CoA
Sequence Mass (Da): 41375
Sequence Length: 388
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle; succinate from succinyl-CoA (ligase route): step 1/1.
EC: 6.2.1.5
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Q2N695 | MNLHEYQAKELLAKYGIGIPAGHAALTVEEAVAGAKQLPGPLYVVKAQIHAGGRGKGKFKELGPDAKGGVRLAKSIEDVEASAREMLGNTLVTVQTGEEGKQVNRLYVTDGVDIASEYYLSMVVDRASGRVGMIVSTEGGMDIEEVAHSTPEKITTITIDPAQGFMPHHGRAVAFALKLSGDLNKQAQKLAKQLYTAFMDLDCEMLEINPLVETEDGQLLVLDTKMSIDGNALYRHKDVEEMRDETEEDPAEVEASEYDLAYIKLDGNIGCMVNGAGLAMATMDIIKLNGAFPANFLDVGGGATTEKVTAAFKIILKDPAVEGILVNIFGGIMRCDTIAEGIVVAAKEVELDVPLVVRLEGTNVEKGKDILANSGLPIVPADDLGDAARKIVAEVKQAA | 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 specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit.
Catalytic Activity: ATP + CoA + succinate = ADP + phosphate + succinyl-CoA
Sequence Mass (Da): 42505
Sequence Length: 399
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle; succinate from succinyl-CoA (ligase route): step 1/1.
EC: 6.2.1.5
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A6GY30 | MNIHEYQGKEILASYGVRIQRGIVANNPVEAVAAAKQLTTETGTSWYVVKAQVHAGGRGKGGGVKLAKNLQQVEEISEQIIGMQLITPQTSAEGKKVHKVLIAEDVYYPGESETSEFYISVLLNRSTGRNMIVYSTEGGMDIEEVAAHTPHLIHNEEIDPSVGLQAFQARRIAFNLGLSGNAFKEMVKFIDSLYNAYIGSDASMFEINPVLKTSDDKIMAVDAKVNIDDNALYRQPKYADMRDIREENPIEVEAKEVGLNYVDLDGTVGCMVNGAGLAMATMDLIKYAGFEPANFLDVGGTADAKRVETAFRIILKDENVKAILINIFGGIVRCDRVAQGVVDAYKNMGDAIKVPIIVRLQGTNAEIAKELIDNSGMPILSAVQFQEAADQVKAALSK | 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 specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit.
Catalytic Activity: ATP + CoA + succinate = ADP + phosphate + succinyl-CoA
Sequence Mass (Da): 43319
Sequence Length: 398
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle; succinate from succinyl-CoA (ligase route): step 1/1.
EC: 6.2.1.5
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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 direct transfer of the sulfur atom from the S-sulfanylcysteine of SufS, an intermediate product of cysteine desulfuration process.
Sequence Mass (Da): 16883
Sequence Length: 144
Pathway: Cofactor biosynthesis; iron-sulfur cluster biosynthesis.
Subcellular Location: Cytoplasm
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O32164 | MNITDIREQFPILHQQVNGHDLVYLDSAATSQKPRAVIETLDKYYNQYNSNVHRGVHTLGTRATDGYEGAREKVRKFINAKSMAEIIFTKGTTTSLNMVALSYARANLKPGDEVVITYMEHHANIIPWQQAVKATGATLKYIPLQEDGTISLEDVRETVTSNTKIVAVSHVSNVLGTVNPIKEMAKIAHDNGAVIVVDGAQSTPHMKIDVQDLDCDFFALSSHKMCGPTGVGVLYGKKALLENMEPAEFGGEMIDFVGLYESTWKELPWKFEAGTPIIAGAIGLGAAIDFLEEIGLDEISRHEHKLAAYALERFRQLDGVTVYGPEERAGLVTFNLDDVHPHDVATVLDAEGIAVRAGHHCAQPLMKWLDVTATARASFYLYNTEEEIDKLVEALQKTKEYFTNVF | 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, which acts as a sulfurtransferase that receives sulfur from SufS via a zinc-ligand swapping mechanism and transfers it to SufB .
Catalytic Activity: [sulfur carrier]-H + L-cysteine = [sulfur carrier]-SH + L-alanine
Sequence Mass (Da): 44922
Sequence Length: 406
EC: 2.8.1.7
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Q9EXP2 | MNYPVEHYPIDRVRADFPILQQSVNGQPLAYLDSAASAQKPLAVIDRERDFYLHEYAAVHRGIHTLSARATSAMEEVRAKVATFIHAASAEDIVFVRGTTEAINLVANSYGRTAFQPGDNLVISEMEHHANIVPWQMLAQARGLTLRVLPITDDGELDMAQLPALLDERTRLVAVTQVSNVLGTVNPLAEIIRQAHACGAKVLVDGAQAVMHQAVDVQALDCDFYAFSGHKLYGPSGIGVLYGKSELLQAMPPWEGGGAMIREVSLTQGTTYADPPWRFEAGSPHVAGIIGLGAALDYVSALGVDAIQAHEGLLMRYALASLAEVPTLRLYGPVHRQGVIAFNLGRHHAFDVGSFLDQYGIAIRTGHHCAMPLMSRYGVPSMCRASLALYSCQDEIDRLVAGLHRIHRLLGE | 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 limitation. Acts as a potent selenocysteine lyase in vitro, that mobilizes selenium from L-selenocysteine. Selenocysteine lyase activity is however unsure in vivo.
Catalytic Activity: [sulfur carrier]-H + L-cysteine = [sulfur carrier]-SH + L-alanine
Sequence Mass (Da): 44785
Sequence Length: 412
Pathway: Cofactor biosynthesis; iron-sulfur cluster biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.8.1.7
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P38359 | MSRKSSTEYVHNQEDADIEVFESEYRTYRESEAAENRDGLHNGDEENWKVNSSKQKFGVTKNELSDVLYDSIPAYEESTVTLKEYYDHSIKNNLTAKSAGSYLVSLFPIIKWFPHYNFTWGYADLVAGITVGCVLVPQSMSYAQIASLSPEYGLYSSFIGAFIYSLFATSKDVCIGPVAVMSLQTAKVIAEVLKKYPEDQTEVTAPIIATTLCLLCGIVATGLGILRLGFLVELISLNAVAGFMTGSAFNIIWGQIPALMGYNSLVNTREATYKVVINTLKHLPNTKLDAVFGLIPLVILYVWKWWCGTFGITLADRYYRNQPKVANRLKSFYFYAQAMRNAVVIVVFTAISWSITRNKSSKDRPISILGTVPSGLNEVGVMKIPDGLLSNMSSEIPASIIVLVLEHIAISKSFGRINDYKVVPDQELIAIGVTNLIGTFFHSYPATGSFSRSALKAKCNVRTPFSGVFTGGCVLLALYCLTDAFFFIPKATLSAVIIHAVSDLLTSYKTTWTFWKTNPLDCISFIVTVFITVFSSIENGIYFAMCWSCAMLLLKQAFPAGKFLGRVEVAEVLNPTVQEDIDAVISSNELPNELNKQVKSTVEVLPAPEYKFSVKWVPFDHGYSRELNINTTVRPPPPGVIVYRLGDSFTYVNCSRHYDIIFDRIKEETRRGQLITLRKKSDRPWNDPGEWKMPDSLKSLFKFKRHSATTNSDLPISNGSSNGETYEKPLLKVVCLDFSQVAQVDSTAVQSLVDLRKAVNRYADRQVEFHFAGIISPWIKRSLLSVKFGTTNEEYSDDSIIAGHSSFHVAKVLKDDVDYTDEDSRISTSYSNYETLCAATGTNLPFFHIDIPDFSKWDV | 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 | MVRDLVTLPSSLPLITAGFATDQVHLLIGTGSTDSVSVCKNRIHSILNAGGNPIVVNPSSPSHTKQLQLEFGKFAKFEIVEREFRLSDLTTLGRVLVCKVVDRVFVDLPITQSRLCEEIFWQCQKLRIPINTFHKPEFSTFNMIPTWVDPKGSGLQISVTTNGNGYILANRIKRDIISHLPPNISEVVINMGYLKDRIINEDHKALLEEKYYQTDMSLPGFGYGLDEDGWESHKFNKLIREFEMTSREQRLKRTRWLSQIMEYYPMNKLSDIKLEDFETSSSPNKKTKQETVTEGVVPPTDENIENGTKQLQLSEVKKEEGPKKLGKISLVGSGPGSVSMLTIGALQEIKSADIILADKLVPQAILDLIPPKTETFIAKKFPGNAERAQQELLAKGLESLDNGLKVVRLKQGDPYIFGRGGEEFNFFKDHGYIPVVLPGISSSLACTVLAQIPATQRDIADQVLICTGTGRKGALPIIPEFVESRTTVFLMALHRANVLITGLLKHGWDGDVPAAIVERGSCPDQRVTRTLLKWVPEVVEEIGSRPPGVLVVGKAVNALVEKDLINFDESRKFVIDEGFREFEVDVDSLFKLY | 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 | MSASTVSITANTAAATRRTPILAGEKKSNFDYPQSESLANGGVGEAGGTSRDLSRGEATLDRSQGQDLGPVTRRSVSAATGTNTTATQRRTRKVATPKSEKARWKTVVRIFAKQLGALLIIVGLIQLTRKMILKASSPSSPISSYETEMAFSGLESRIAEVDGLVKATTNSMQVQVELLDKKMEREAKVLRQEIERKASAFQSELKKIESRTESLEKSVDEVNAKPWVTKDELERIYEELKKGNVDDSAFSEISIDELRAYARDIMEKEIEKHAADGLGRVDYALASGGAFVMEHSDPYLVGKGSSWFATTMRRAHTNAVKMLSPSFGEPGQCFPLKGSEGYVQIRLRGPIIPEAFTLEHVAKSVAYDRSSAPKDCRVSGSLQGPESSAETENMQLLTEFTYDLDRSNAQTFNILESSSSGLIDTVRLDFTSNHGSDSHTCIYRFRVHGRAPDPVPVVGTNLDQDSSPESE | 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 hairs . Modulates the anchoring and mobility of WIP proteins and RANGAP1 in the nuclear envelope (NE) . In association with SUN2, may be involved in telomere attachment to nuclear envelope in the prophase of meiosis . As component of the SUN-WIP-WIT2-KAKU1 complex, mediates the transfer of cytoplasmic forces to the nuclear envelope (NE), leading to nuclear shape changes .
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 51502
Sequence Length: 471
Domain: The SUN domain may play a role in nuclear anchoring and/or migration (By similarity). The SUN domain is required for interactions with WIP proteins .
Subcellular Location: Nucleus inner membrane
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Q4WGL5 | MKFNTVALTLATAGSLVTAQHHHQHRHHQHKREDVVESSATVVQYELDGKPISLKQVCAGLADNTLKFANNDHPTGICDNLSSAAAPASTPEVTSAFAPAQFIELSSVVTSATPTSASSSETVQTPAASSSSASSSSTATGLDADFPDGELDCSTFPSEYGAIPLDYLKLGGWSGIQYVSYAGNFINDIVTAVAGDTCKDGAMCSYACPPGYQKSQWPSTQGATGQSVGGIECRNGKLHLTNPSLSKKLCIPGVGGVHVQNTLGETVAVCRTDYPGTESETIPIGLGGNDLQPLTCPDGETYYKWQGKTTSAQYYVNPKGVTPEKGCQWGDGTQPIGNWAPVNLGVGLNKGKWLSIFQNSPTTSEKLDFNIKIKGDNLSGSCKYENGVFYSETGSSSSGCTVQVMSGDATFVFY | 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: Highly glycosylated.
Sequence Mass (Da): 43504
Sequence Length: 414
Subcellular Location: Secreted
EC: 3.2.1.-
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Q20924 | MALRHTISPQFSNRHSPPVTRSVSRTGVHQPLDTSTPVTRRDSQPGTITGTIQRFHESADDSEIDLNSSKFIYKEHFSYKEITSMKKEMWYDWLEYRIRMVRRRFVPTWAQFKRTLMAVVLFAMLYKYARDCLFDGTHHNSEGSYADKDANWASEKQKFHQTISNLRAEFSAHDKQLDFKTDHLEKLLENVLEHSKGWKESAIEELKQIKLWQAEISDALQQMKKEIDDAKSTKIIHSTPEKAPETAPTASLPPSSQLQPMHITRRALLGVNVANSLIGASIDHSCSSRPVSAKDGFFYDFMSYFGTFQEGYALLDRDVLSPGEAWCTYDKRATLTVKLARFVIPKSVSYQHVRWSGIVPNHAPKLYDVVACTDSCCTKWQPLVANCEYKERDGSYDEQEQFCSVPTIQNHSPINHVQFRFRENHGDMPKTCAYLIRVYGEPVDPPKETQPMTDNGTESKLESAIVNSVSETA | 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 SUN domain may play a role in nuclear anchoring.
Subcellular Location: Nucleus membrane
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Q558Z2 | MSGDYKPNYQSSPSRKRLPLQSKDQASIYKYQTPSTLNLYNNTVNNNSSNNSNNHLLHNSNPNSSYLYDSSKQYSNQINIRNNSNSNSNTNNITSKKASSSYSINNKVDHNSHNNNDDDDIEDDVDINYSTNNASSNILHNRFSNSNKDDSYIDYSTDENPKILKQPQPLYNHLNNQIQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQRNNNNNSNSSNNNNTSTTIKRNNQQIDNNSNKNIISKFIGDPWKNFYYGSNKSLWPFERNNNSNNSSNNNNKVNFKQAIWIFIFSVLFIGCLLGLFSTNFYGIHIYFPSFSTTKTNSPFNSTNNNIQFSNLITKEQLYPIIDEYFKKNEILKSYNKLFEKIENDIKYLSEREQYKDIINEIKEELKLVKLSNMDEDRVNQLISKMINHYNNNENNKQELKELLSKSIEELTKLKSDSKEQLIQISTESMNQLGQLKSESINQLGQVKSESIDKFQSTLKSLSKEEQSKIEREFNHQFNQLNKDADQLLSQHSLKIEKLREEINENQQSSLLKLTQEYKQLEERLKEFSSKLQQSISSSSMDQFESWKLVFIKDIEERINKESSKLTNQYIQLTQQFTKIQSFIKDNPSIDSLTNTIESLEGIKLLIEDILEVYSADKIAKVDYALGLAGASIEYNALHYRVSETYPPIKGSGSGSGSGGANGNSLGLYYYNLATNWIFPQPKPNPPETILDPMVNTGSCWGFYTGNGTIVIRLAKKIAITEVTMEHISSNISHHIDSAPKEFQVFGLINSSDIGQSLGVFTYDTTINRHLQTFKVNKIQSTTTTTTNQDQNDDDNIQEFSHVALRILSNHGYRYTCIYRFRVHGYQIPHPEQEQIQIIQEEQSFKQEEINQQQIEQIEQIEQIEKQQQSDEL | 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 binding for inner nuclear membrane targeting.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 104743
Sequence Length: 905
Subcellular Location: Nucleus membrane
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Q9D666 | MDFSRLHTYTPPQCVPENTGYTYALSSSYSSDALDFETEHKLEPVFDSPRMSRRSLRLVTTASYSSGDSQAIDSHISTSRATPAKGRETRTVKQRRSASKPAFSINHLSGKGLSSSTSHDSSCSLRSATVLRHPVLDESLIREQTKVDHFWGLDDDGDLKGGNKAATQGNGELAAEVASSNGYTCRDCRMLSARTDALTAHSAIHGTTSRVYSRDRTLKPRGVSFYLDRTLWLAKSTSSSFASFIVQLFQVVLMKLNFETYKLKGYESRAYESQSYETKSHESEAHLGHCGRMTAGELSRVDGESLCDDCKGKKHLEIHTATHSQLPQPHRVAGAMGRLCIYTGDLLVQALRRTRAAGWSVAEAVWSVLWLAVSAPGKAASGTFWWLGSGWYQFVTLISWLNVFLLTRCLRNICKVFVLLLPLLLLLGAGVSLWGQGNFFSLLPVLNWTAMQPTQRVDDSKGMHRPGPLPPSPPPKVDHKASQWPQESDMGQKVASLSAQCHNHDERLAELTVLLQKLQIRVDQVDDGREGLSLWVKNVVGQHLQEMGTIEPPDAKTDFMTFHHDHEVRLSNLEDVLRKLTEKSEAIQKELEETKLKAGSRDEEQPLLDRVQHLELELNLLKSQLSDWQHLKTSCEQAGARIQETVQLMFSEDQQGGSLEWLLEKLSSRFVSKDELQVLLHDLELKLLQNITHHITVTGQAPTSEAIVSAVNQAGISGITEAQAHIIVNNALKLYSQDKTGMVDFALESGGGSILSTRCSETYETKTALLSLFGVPLWYFSQSPRVVIQPDIYPGNCWAFKGSQGYLVVRLSMKIYPTTFTMEHIPKTLSPTGNISSAPKDFAVYGLETEYQEEGQPLGRFTYDQEGDSLQMFHTLERPDQAFQIVELRVLSNWGHPEYTCLYRFRVHGEPIQ | 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 envelope and in nuclear movement and positioning . Required for interkinetic nuclear migration (INM) and essential for nucleokinesis and centrosome-nucleus coupling during radial neuronal migration in the cerebral cortex and during glial migration . Involved in telomere attachment to nuclear envelope in the prophase of meiosis implicating a SUN1/2:KASH5 LINC complex in which SUN1 and SUN2 seem to act at least partial redundantly . Required for gametogenesis and involved in selective gene expression of coding and non-coding RNAs needed for gametogenesis . Helps to define the distribution of nuclear pore complexes (NPCs) . Required for efficient localization of SYNE4 in the nuclear envelope . May be involved in nuclear remodeling during sperm head formation in spermatogenesis . May play a role in DNA repair by suppressing non-homologous end joining repair to facilitate the repair of DNA cross-links (By similarity).
PTM: The disulfide bond with KASH domain-containing nesprins is required for stability of the respective LINC complexes under tensile forces.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 101976
Sequence Length: 913
Domain: The coiled coil domains differentially mediate trimerization required for binding to nesprins and are proposed to dynamically regulate the oligomeric state by locking the SUN domain in an inactive confirmation. The coiled coil domains are proposed to be involved in load-bearing and force transmission from the cytoskeleton.
Subcellular Location: Nucleus inner membrane
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Q9SG79 | MSASTVSITASPRTIRRTPVLSGEKKSNFDFPPSESHANAAIGESSAGTNKDLIRAEAAGERSNTYDVGPVTRKSGSTATGTNTTTTQRRTRKSQGNKIDRGKWKTVVRVFAKQFGALLLLVGLIQLIRKLTLKDSSLSSSNFPIETEMVLSELESRISAVDGLVKTTTKMMQVQVEFLDKKMDSESRALRQTIDSTSSVLHSELKKVESKTERLQVSVDELNAKPLVSREELERVYEELKKGKVGDSDVNIDKLRAYARDIVEKEIGKHVADGLGRVDYALASGGAFVMGHSDPFLVGNGRNWFGTSRRRVHSKAVKMLTPSFGEPGQCFPLKGSNGYVLVRLRAPIIPEAVTLEHVSKAVAYDRSSAPKDCRVSGWLGDIDMETETMPLLTEFSYDLDRSNAQTFDIADSAHSGLVNTVRLDFNSNHGSSSHTCIYRFRVHGRELDSVSVAHA | 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 hairs . Modulates the anchoring and mobility of WIP proteins in the nuclear envelope (NE) . In association with SUN1, may be involved in telomere attachment to nuclear envelope in the prophase of meiosis . As component of the SUN-WIP-WIT2-KAKU1 complex, mediates the transfer of cytoplasmic forces to the nuclear envelope (NE), leading to nuclear shape changes .
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 49940
Sequence Length: 455
Domain: The SUN domain may play a role in nuclear anchoring and/or migration (By similarity). The SUN domain is required for interactions with WIP proteins .
Subcellular Location: Nucleus inner membrane
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Q9UH99 | MSRRSQRLTRYSQGDDDGSSSSGGSSVAGSQSTLFKDSPLRTLKRKSSNMKRLSPAPQLGPSSDAHTSYYSESLVHESWFPPRSSLEELHGDANWGEDLRVRRRRGTGGSESSRASGLVGRKATEDFLGSSSGYSSEDDYVGYSDVDQQSSSSRLRSAVSRAGSLLWMVATSPGRLFRLLYWWAGTTWYRLTTAASLLDVFVLTRRFSSLKTFLWFLLPLLLLTCLTYGAWYFYPYGLQTFHPALVSWWAAKDSRRPDEGWEARDSSPHFQAEQRVMSRVHSLERRLEALAAEFSSNWQKEAMRLERLELRQGAPGQGGGGGLSHEDTLALLEGLVSRREAALKEDFRRETAARIQEELSALRAEHQQDSEDLFKKIVRASQESEARIQQLKSEWQSMTQESFQESSVKELRRLEDQLAGLQQELAALALKQSSVAEEVGLLPQQIQAVRDDVESQFPAWISQFLARGGGGRVGLLQREEMQAQLRELESKILTHVAEMQGKSAREAAASLSLTLQKEGVIGVTEEQVHHIVKQALQRYSEDRIGLADYALESGGASVISTRCSETYETKTALLSLFGIPLWYHSQSPRVILQPDVHPGNCWAFQGPQGFAVVRLSARIRPTAVTLEHVPKALSPNSTISSAPKDFAIFGFDEDLQQEGTLLGKFTYDQDGEPIQTFHFQAPTMATYQVVELRILTNWGHPEYTCIYRFRVHGEPAH | 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 envelope and in nuclear movement and positioning. Specifically, SYNE2 and SUN2 assemble in arrays of transmembrane actin-associated nuclear (TAN) lines which are bound to F-actin cables and couple the nucleus to retrograde actin flow during actin-dependent nuclear movement. Required for interkinetic nuclear migration (INM) and essential for nucleokinesis and centrosome-nucleus coupling during radial neuronal migration in the cerebral cortex and during glial migration. Required for nuclear migration in retinal photoreceptor progenitors implicating association with cytoplasmic dynein-dynactin and kinesin motor complexes, and probably B-type lamins; SUN1 and SUN2 seem to act redundantly. The SUN1/2:KASH5 LINC complex couples telomeres to microtubules during meiosis; SUN1 and SUN2 seem to act at least partial redundantly. Anchors chromosome movement in the prophase of meiosis and is involved in selective gene expression of coding and non-coding RNAs needed for gametogenesis. Required for telomere attachment to nuclear envelope and gametogenesis. May also function on endocytic vesicles as a receptor for RAB5-GDP and participate in the activation of RAB5.
PTM: The disulfide bond with SYNE2 is required for stability of the SUN2:SYNE2/KASH2 LINC complex under tensile forces though not required for the interaction. The disulfide bond is proposed to be conserved in LINC complexes involved in force transmission.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 80311
Sequence Length: 717
Domain: The coiled coil domains differentially mediate trimerization required for binding to nesprins and are proposed to dynamically regulate the oligomeric state by locking the SUN domain in an inactive confirmation (By similarity). The coiled coil domains are proposed to be involved in load-bearing and force transmission from the cytoskeleton.
Subcellular Location: Nucleus inner membrane
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Q8BJS4 | MSRRSQRLTRYSQDDNDGGSSSSGASSVAGSQGTVFKDSPLRTLKRKSSNMKHLSPAPQLGPSSDSHTSYYSESVVRESYIGSPRAVSLARSALLDDHLHSEPYWSGDLRGRRRRGTGGSESSKANGLTAESKASEDFFGSSSGYSSEDDLAGYTDSDQHSSGSRLRSAASRAGSFVWTLVTFPGRLFGLLYWWIGTTWYRLTTAASLLDVFVLTRSRHFSLNLKSFLWFLLLLLLLTGLTYGAWHFYPLGLQTLQPAVVSWWAAKESRKQPEVWESRDASQHFQAEQRVLSRVHSLERRLEALAADFSSNWQKEAIRLERLELRQGAAGHGGGSSLSHEDALSLLEGLVSRREATLKEDLRRDTVAHIQEELATLRAEHHQDSEDLFKKIVQASQESEARVQQLKTEWKSMTQEAFQESSVKELGRLEAQLASLRQELAALTLKQNSVADEVGLLPQKIQAARADVESQFPDWIRQFLLGDRGARSGLLQRDEMHAQLQELENKILTKMAEMQGKSAREAAASLGQILQKEGIVGVTEEQVHRIVKQALQRYSEDRIGMVDYALESGGASVISTRCSETYETKTALLSLFGIPLWYHSQSPRVILQPDVHPGNCWAFQGPQGFAVVRLSARIRPTAVTLEHVPKALSPNSTISSAPKDFAIFGFDEDLQQEGTLLGTFAYDQDGEPIQTFYFQASKMATYQVVELRILTNWGHPEYTCIYRFRVHGEPAH | 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 envelope and in nuclear movement and positioning. Specifically, SYNE2 and SUN2 assemble in arrays of transmembrane actin-associated nuclear (TAN) lines which are bound to F-actin cables and couple the nucleus to retrograde actin flow during actin-dependent nuclear movement. Required for interkinetic nuclear migration (INM) and essential for nucleokinesis and centrosome-nucleus coupling during radial neuronal migration in the cerebral cortex and during glial migration. Required for nuclear migration in retinal photoreceptor progenitors implicating association with cytoplasmic dynein-dynactin and kinesin motor complexes, and probably B-type lamins; SUN1 and SUN2 seem to act redundantly. The SUN1/2:KASH5 LINC complex couples telomeres to microtubules during meiosis; SUN1 and SUN2 seem to act at least partial redundantly. Anchors chromosome movement in the prophase of meiosis and is involved in selective gene expression of coding and non-coding RNAs needed for gametogenesis. Required for telomere attachment to nuclear envelope and gametogenesis. May also function on endocytic vesicles as a receptor for Rab5-GDP and participate in the activation of Rab5.
PTM: The disulfide bond with SYNE2 is required for stability of the SUN2:SYNE2/KASH2 LINC complex under tensile forces though not required for the interaction. The disulfide bond is proposed to be conserved in LINC complexes involved in force transmission.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 81605
Sequence Length: 731
Domain: The proximal coiled coil domain mediates trimerization required for binding to nesprins. The distal coiled coil domain is proposed to dynamically regulate the oligomeric state by locking the SUN domain in an inactive confirmation . The coiled coil domains are proposed to be involved in load-bearing and force transmission from the cytoskeleton (By similarity).
Subcellular Location: Nucleus inner membrane
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F4I316 | MQRSCRTRRRVSVNKFNGRNSFYKVSLSLVFLLWVLLFFSTLLISHGDGAKDEPLNDSMGMADPDDGQSDEKVVPFDGPLSLASASVDVTSDLSRNDDVNLSEESEDKEQEAEISSTVSGNDIESKDTYLLKQSEINKKDTGIDAGSKYDDFPKKSEINNTGTWNDTEGKDDNNFLKQSQLNKTGTGNDTESSDNEFLEQNQMNKTVLGNGTEINVSKVDQPSRAVPLGLDEFKSRASNSRNKSLSDQVSGVIHRMEPGGKEYNYASASKGAKVLSSNKEAKGAASILSRDNDKYLRNPCSTEGKFVVVELSEETLVNTIKIANFEHYSSNLKEFELQGTLVYPTDTWVHMGNFTASNVKHEQNFTLLEPKWVRYLKLNFISHYGSEFYCTLSLIEVYGVDAVERMLEDLISVQDNKNAYKPREGDSEHKEKPMQQIESLEGDDGADKSTHREKEKEAPPENMLAKTEASMAKSSNKLSEPVEEMRHHQPGSRMPGDTVLKILMQKLRSLDLNLSILERYLEELNLRYGNIFKEMDREAGVREKAIVALRLDLEGMKERQEGMVSEAEEMKEWRKRVEAEMEKAEKEKENIRQSLEQVSKRLEWMEKKCLTVFTVCLGFGIIAVIAVVIGMGTGLAEKTGSGAWLLLLISSTFIMFVLSL | 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 Location: Nucleus membrane
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Q95LV7 | MSGKAKARRAAMFFRGCSEDASGSTSGSTLLSEDENPDTNGVTRSWKIILSTMFTLTFLLVGLLSHQWLKETEVPQKSRQLYAIIAEYGSRLYKYQARLRMPKEQLELLKKESQTLENNFHKILLLIEQIDVLKALLRDMKDGTDNNHSWNTHGDPVEDPDHTEVLDEEMSNLVNYVLKKLREDQVQMADYALKSAGASIIEAGTSESYKNNKAKLYWHGISFLNHEMPPDIILQPDVYPGNCWAFPGSQGHTLIKLATKIIPTAVTMEHISEKVSPSGNISSAPKEFSVYGITKKCEGEEIFLGQFIYNKTGTTVQTFELQHAVSEYLLCVKLNIFSNWGHPKYTCLYRFRVHGTPGKHI | 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 nuclear envelope and in nuclear movement and positioning. May be involved in nuclear remodeling during sperm head formation in spermatogenesis. A probable SUN3:SYNE1 LINC complex may tether spermatid nuclei to posterior cytoskeletal structures such as the manchette.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 40839
Sequence Length: 361
Domain: The short coiled coil domain is proposed to be not involved in load-bearing and force transmission from the cytoskeleton but in mere nucleus anchorage instead.
Subcellular Location: Membrane
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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 nuclear envelope and in nuclear movement and positioning. May be involved in nuclear remodeling during sperm head formation in spermatogenesis. A probable SUN3:SYNE1 LINC complex may tether spermatid nuclei to posterior cytoskeletal structures such as the manchette.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 36758
Sequence Length: 320
Subcellular Location: Membrane
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D4AM57 | MKFSSGILSLAVAASVQSVQASYHAHGHAHHHRVLNKRADPDVVTIPGPKVYAFILNGSEMSKEQVCAGIRDGRLDWSGQNHDELCGFPVGMQKGSPPACPAPSYVPSPPAAPSSPPAAPQPPSKSPETPEEPKKPEEPKKPEGPKKPEGPKTPSPKKPDGPQHPQTPTGGEGVNRPFPDGEIDCGDFPSKYGAVPVDYLGLGGYTGIQHTTLVGEVFGTIRTAIAGESCTDGAMCSYACPPGYQKSQWPEQQGSTGESVGGLACRNGKLYLTNRKLSTRLCISGVGGVHIKSTISVEISICRTDYPGTESETVPVPLPPHGHLPLTCPQAETYYFWQGKSTSAQYYVNPPGYGPAKACQWGHAGLPIGNWAPVNIGVGEKGGVKWLSMFPNRPTTTAILHMTIEIVGEGLSGKCKHKDGKYYTDTGVNEDGCTVSVLHGEATFVFSYD | 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
Sequence Length: 449
Subcellular Location: Secreted
EC: 3.2.1.-
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Q59NP5 | MRFSQATVLAFAALSLAAPAFEADNKNIKREDCDKTSFHGHHKHKRAVAYDYAYVTVTVDGNGNPITTVSPVLSIETIAKSEETSSTSTSISSTTTIVQNDSLTSDEPKTLSLPSGTIKPSSFATESQSQSQSSSTGGSGSGSTNGIEGDLAAFEDPTEEFEDGVLSCSDFPSGQGVIPLDHLGFGGWSGIENSDGSTGGNCKEGSYCSYACQSGMSKTQWPEDQPSNGVSIGGLLCKNGKLYKSSTRSNYLCEWGVKKANVVNKLSETVAICRTDYPGTENMVIPTVVGGGSTSVITVVDQSTYYTWRGGATSAQYYVNNAGVSWEDGCVWGTPGSGVGNWAPLNFGAGYANGIAYLSLIPNPNNRDSLNFKVKIVGESGSTVSGSCSYANGKFNGNSDDGCTVGVTSGEADFVLYN | 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: Predicted to be a substrate for cleavage by KEX2.
Sequence Mass (Da): 43693
Sequence Length: 418
Subcellular Location: Secreted
EC: 3.2.1.-
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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
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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
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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
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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 activity) with the preference for short-chain-length substrates (P20-25). Might be involved in the regulation of dNTP and NTP pools, and in the turnover of 3'-mononucleotides produced by numerous intracellular RNases (T1, T2, and F) during the degradation of various RNAs.
Catalytic Activity: a ribonucleoside 5'-phosphate + H2O = a ribonucleoside + phosphate
Sequence Mass (Da): 26980
Sequence Length: 253
Subcellular Location: Cytoplasm
EC: 3.1.3.5
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Q9SE51 | MATSLSKILTRSNTKRYWCSTTTSISASPSLPKQFWSRHFSAVADSSSSSSAALGSQSSSSAPPQENKRGSKWSQLLLFLPGAITFGLGSWQIVRREEKFKTLEYQQQRLNMEPIKLNIDHPLDKNLNALEFRRVSCKGVFDEQRSIYLGPRSRSISGITENGFFVITPLMPIPGDLDSMQSPILVNRGWVPRSWREKSQESAEAEFIANQSTKAKSPSNEPKSWWKFWSKTPVITKEHISAVKPVEVVGVIRGGENPSIFVPSNDPSTGQWFYVDVPAMARAVGLPENTIYVEDVHEHVDRSRPYPVPKDINTLIRSKVMPQDHLNYSITWYSLSAAVTFMAYKRLKAKPVRR | 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 | MPLPAAAFARILVVSRQRLFNTRIIHTSGSGYSITQCRFYKTTPCLTHKQSQILDLDAPKSRENREKDGGKSKKSKKSIKWSTGSVLMLTIPVFAFSLGIWQTFRLKWKLDLIEHLKGRLNQTAQELPEDLSCESLEPLEYCRVTVTGEFLHEKEFIISPRGRFDPGKKTSAAAGSMLSENEMSSHGGHLITPFRLKNSGKIILINRGWLPSFYFDPETRQKTNPRGTLTLPAIVRKTEKRPQFVGQNVPEQGVWYYRDLNQMAKHYGTEPVLLDAAYETTVPGGPIGGQTNINVRNEHLNYLTTWFTLTLVTMLMWIHKFRK | 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 membrane
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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: Mitochondrion membrane
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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 membrane
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P12297 | MLPYNVRNAGGGSVGGILRRTGQGSGTGSTILGNGNSPGALGAGKVSSSLENHRQPPLELLVFGYACKIFRDDEKAREMDHGKQLIPWMGDVNLKIDRYDVRGALCELAPHEAPPGGYGNRLEYLSAEEQRAEQLCEEERYLFLYNNEEELRLRQEEDLKRLQQETSGGCFSQVGFQYDGQSAASTSIGGSSTATSQLSPNSEESELPFVLPYTLMMAPPLDMQLPETMKQHAIIEKTARFIATQGAQMEILIKAKQANNTQFDFLTQGGHLQPYYRHLLAAIKAAKFPPAPQTPLDQQNTDKEAPSADDHSEEVAGGRRNPNQVVITVPTIKYKPSANCAYTQLISKIKGVPLQAVLQEDESSNPGNSQHSGGTASPALSCRSEGHNSQGGEFTPVLLQYNGSTFTHEEESSNREQQDDNDVNGGEPPQVELLKNTSALALAQNYSSESEEEEDQVQPEKEEEKKPEPVLTFPVPKDSLRHIIDKTATYVIKNGRQFEETLRTKSVDRFSFLLPANEYYPYYLYKVTGDVDAASKEEKTRKAAAVAAALMSKKGLSFGGAAAAVSGSNLDKAPVSFSIRARDDQCPLQHTLPQEASDEETSSNAAGVEHVRPGMPDSVQRAIKQVETQLLARTAGQKGNITASPSCSSPQKEQRQAEERVKDKLAQIAREKLNGMISREKQLQLERKRKALAFLNQIKGEGAIVGSAVPVVGPNPPESAAGAATADSGDESGDSVRSIPITYFGPDDDDEVGEQRPEMRLIGSTQKDEEDDDEEDGGDLEKYNLLNDDSTNTFTSKPVLPPTAAPPPAAVLLSDDDDVQLVATTSTRSSSSRHLKTHRRSRSRSKNVRSSDSSPSSRESSRRRRQKSSRLSREPSSNPPRKSQHSSTQRKKTPKKRRRSKSRSRSKSIRRSRSISILRNNRRSRSRSPSCRNAEQRRQQDRRRTPTKKSHKRHKRRRRSSSP | 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 localization is to allow colocalization and co-concentration of components of the splicing and splicing regulatory machinery to permit relatively high rates and/or efficiencies of reaction and interaction.
Subcellular Location: Nucleus speckle
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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 | MALDFSNATVKAWRRENGRVGVRNHVLILPVDDISNAACEAVANNVKGTLAIPHAYGRLQFGEDLELHFRTIIGTGANPNVAAVVVIGIEPEWTQVIVDGIAKTGKPVTGFSIEQKGDFETIRQAGWKAKEYVHWASELQKEDCPISDLWISTKCGESDTTTGLSSCPTVGNMYDKLLPQGIYGCFGETSEITGAEHICEKRAANPETARKFKEIWQAYSDDVIFAHQTDDLSDSQPTKGNILGGLTTIEEKALGNLEKIGRTSTYIDAMGPAETPSKGPGLYFMDSSSAAAECVTLMAAGGYVIHTFPTGQGNVVGNPIVPVIKISGNPRTLRTMSEHIDVDVTGVLTREMTIDQAGDALIEMIIRTANGRMTAAEALGHREFSMTKLYRSA | 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 | MAPQKHGGGGGGGSGPSAGSGGGGFGGSAAVAAATASGGKSGGGSCGGGGSYSASSSSSAAAAAGAAVLPVKKPKMEHVQADHELFLQAFEKPTQIYRFLRTRNLIAPIFLHRTLTYMSHRNSRTNIKRKTFKVDDMLSKVEKMKGEQESHSLSAHLQLTFTGFFHKNDKPSPNSENEQNSVTLEVLLVKVCHKKRKDVSCPIRQVPTGKKQVPLNPDLNQTKPGNFPSLAVSSNEFEPSNSHMVKSYSLLFRVTRPGRREFNGMINGETNENIDVNEELPARRKRNREDGEKTFVAQMTVFDKNRRLQLLDGEYEVAMQEMEECPISKKRATWETILDGKRLPPFETFSQGPTLQFTLRWTGETNDKSTAPIAKPLATRNSESLHQENKPGSVKPTQTIAVKESLTTDLQTRKEKDTPNENRQKLRIFYQFLYNNNTRQQTEARDDLHCPWCTLNCRKLYSLLKHLKLCHSRFIFNYVYHPKGARIDVSINECYDGSYAGNPQDIHRQPGFAFSRNGPVKRTPITHILVCRPKRTKASMSEFLESEDGEVEQQRTYSSGHNRLYFHSDTCLPLRPQEMEVDSEDEKDPEWLREKTITQIEEFSDVNEGEKEVMKLWNLHVMKHGFIADNQMNHACMLFVENYGQKIIKKNLCRNFMLHLVSMHDFNLISIMSIDKAVTKLREMQQKLEKGESASPANEEITEEQNGTANGFSEINSKEKALETDSVSGVSKQSKKQKL | 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 epigenetic repression systems . Genes repressed by the PRC2 complex include HOXC8, HOXA9, MYT1 and CDKN2A .
PTM: Sumoylated, probably by PIAS2.
Sequence Mass (Da): 83055
Sequence Length: 739
Subcellular Location: Nucleus
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Q02563 | MEEGFRDRAAFIRGAKDIAKEVKKHAAKKVVKGLDRVQDEYSRRSYSRFEEEEDDDDFPAPADGYYRGEGAQDEEEGGASSDATEGHDEDDEIYEGEYQGIPRAESGGKGERMADGAPLAGVRGGLSDGEGPPGGRGEAQRRKDREELAQQYETILRECGHGRFQWTLYFVLGLALMADGVEVFVVGFVLPSAEKDMCLSDSNKGMLGLIVYLGMMVGAFLWGGLADRLGRRQCLLISLSVNSVFAFFSSFVQGYGTFLFCRLLSGVGIGGSIPIVFSYFSEFLAQEKRGEHLSWLCMFWMIGGVYAAAMAWAIIPHYGWSFQMGSAYQFHSWRVFVLVCAFPSVFAIGALTTQPESPRFFLENGKHDEAWMVLKQVHDTNMRAKGHPERVFSVTHIKTIHQEDELIEIQSDTGTWYQRWGVRALSLGGQVWGNFLSCFSPEYRRITLMMMGVWFTMSFSYYGLTVWFPDMIRHLQAVDYAARTKVFPGERVEHVTFNFTLENQIHRGGQYFNDKFIGLRLKSVSFEDSLFEECYFEDVTSSNTFFRNCTFINTVFYNTDLFEYKFVNSRLVNSTFLHNKEGCPLDVTGTGEGAYMVYFVSFLGTLAVLPGNIVSALLMDKIGRLRMLAGSSVLSCVSCFFLSFGNSESAMIALLCLFGGVSIASWNALDVLTVELYPSDKRTTAFGFLNALCKLAAVLGISIFTSFVGITKAAPILFASAALALGSSLALKLPETRGQVLQ | 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 regulates interaction with SYT1.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 82661
Sequence Length: 742
Subcellular Location: Presynapse
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Q7L1I2 | MDDYKYQDNYGGYAPSDGYYRGNESNPEEDAQSDVTEGHDEEDEIYEGEYQGIPHPDDVKAKQAKMAPSRMDSLRGQTDLMAERLEDEEQLAHQYETIMDECGHGRFQWILFFVLGLALMADGVEVFVVSFALPSAEKDMCLSSSKKGMLGMIVYLGMMAGAFILGGLADKLGRKRVLSMSLAVNASFASLSSFVQGYGAFLFCRLISGIGIGGALPIVFAYFSEFLSREKRGEHLSWLGIFWMTGGLYASAMAWSIIPHYGWGFSMGTNYHFHSWRVFVIVCALPCTVSMVALKFMPESPRFLLEMGKHDEAWMILKQVHDTNMRAKGTPEKVFTVSNIKTPKQMDEFIEIQSSTGTWYQRWLVRFKTIFKQVWDNALYCVMGPYRMNTLILAVVWFAMAFSYYGLTVWFPDMIRYFQDEEYKSKMKVFFGEHVYGATINFTMENQIHQHGKLVNDKFTRMYFKHVLFEDTFFDECYFEDVTSTDTYFKNCTIESTIFYNTDLYEHKFINCRFINSTFLEQKEGCHMDLEQDNDFLIYLVSFLGSLSVLPGNIISALLMDRIGRLKMIGGSMLISAVCCFFLFFGNSESAMIGWQCLFCGTSIAAWNALDVITVELYPTNQRATAFGILNGLCKFGAILGNTIFASFVGITKVVPILLAAASLVGGGLIALRLPETREQVLM | 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 | MDDYRYRDNYEGYAPNDGYYRGNEQNPEEDAQSDVTEGHDEEDEIYEGEYQGIPHPDDVKSKQTKMAPSRADGLRGQADLMAERMEDEEQLAHQYETIIDECGHGRFQWTLFFVLVLALMADGVEVFVVSFALPSAEKDMCLSSSKKGMLGLIVYLGMMAGAFILGGLADKLGRKKVLSMSLAINASFASLSSFVQGYGAFLFCRLISGIGIGGSLPIVFAYFSEFLSREKRGEHLSWLGIFWMTGGIYASAMAWSIIPHYGWGFSMGTNYHFHSWRVFVIVCALPATVSMVALKFMPESPRFLLEMGKHDEAWMILKQVHDTNMRAKGTPEKVFTVSHIKTPKQMDEFIEIQSSTGTWYQRWLVRFMTIFKQVWDNALYCVMGPYRMNTLILAVVWFTMALSYYGLTVWFPDMIRYFQDEEYKSKMKVFFGEHVHGATINFTMENQIHQHGKLVNDKFIKMYFKHVLFEDTFFDKCYFEDVTSTDTYFKNCTIESTTFYNTDLYKHKFIDCRFINSTFLEQKEGCHMDFEEDNDFLIYLVSFLGSLSVLPGNIISALLMDRIGRLKMIGGSMLISAVCCFFLFFGNSESAMIGWQCLFCGTSIAAWNALDVITVELYPTNQRATAFGILNGLCKLGAILGNTIFASFVGITKVVPILLAAASLVGGGLVALRLPETREQVLM | 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 | MEDSYKDRTSLMKGAKDIAREVKKQTVKKVNQAVDRAQDEYTQRSYSRFQDEEDDDDYYPAGETYNGEANDDEGSSEATEGHDEDDEIYEGEYQGIPSMNQAKDSIVSVGQPKGDEYKDRRELESERRADEEELAQQYELIIQECGHGRFQWALFFVLGMALMADGVEVFVVGFVLPSAETDLCIPNSGSGWLGSIVYLGMMVGAFFWGGLADKVGRKQSLLICMSVNGFFAFLSSFVQGYGFFLFCRLLSGFGIGGAIPTVFSYFAEVLAREKRGEHLSWLCMFWMIGGIYASAMAWAIIPHYGWSFSMGSAYQFHSWRVFVIVCALPCVSSVVALTFMPESPRFLLEVGKHDEAWMILKLIHDTNMRARGQPEKVFTVNKIKTPKQIDELIEIESDTGTWYRRCFVRIRTELYGIWLTFMRCFNYPVRDNTIKLTIVWFTLSFGYYGLSVWFPDVIKPLQSDEYALLTRNVERDKYANFTINFTMENQIHTGMEYDNGRFIGVKFKSVTFKDSVFKSCTFEDVTSVNTYFKNCTFIDTVFDNTDFEPYKFIDSEFKNCSFFHNKTGCQITFDDDYSAYWIYFVNFLGTLAVLPGNIVSALLMDRIGRLTMLGGSMVLSGISCFFLWFGTSESMMIGMLCLYNGLTISAWNSLDVVTVELYPTDRRATGFGFLNALCKAAAVLGNLIFGSLVSITKSIPILLASTVLVCGGLVGLCLPDTRTQVLM | 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 abundant glycan on Asn-534 is GlcNAc(3)Hex(5), while on Asn-559 and Asn-565 the most abundant glycan is GlcNAc2Fuc1Man3GlcNAc3Gal3. Both Asn-559 and Asn-565 have a high degree of glycan heterogeneity .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 82342
Sequence Length: 727
Subcellular Location: Cytoplasmic vesicle
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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 Topology: Multi-pass membrane protein
Sequence Mass (Da): 32936
Sequence Length: 292
Subcellular Location: Cell membrane
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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) .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 25744
Sequence Length: 230
Subcellular Location: Vacuole membrane
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Q10LN5 | MADPSFFVGIVGNVISILVFASPIATFRRIVRSKSTEEFRWLPYVTTLLSTSLWTFYGLHKPGGLLIVTVNGSGAALEAIYVTLYLAYAPRETKAKMVKVVLAVNVGALAAVVAVALVALHGGVRLFVVGVLCAALTIGMYAAPMAAMRTVVKTRSVEYMPFSLSFFLFLNGGVWSVYSLLVKDYFIGIPNAIGFALGTAQLALYMAYRRTKKPAGKGGDDDEDDEEAQGVARLMGHQVEMAQQRRDQQLRKGLSLSLPKPAAPLHGGLDRIIKSFSTTPIELHSILHQHHGGHHHHHRFDTVPDDDDEAVAAGGTTPATTAGPGDRH | 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 | MSGVNEIRSTFLNFFAENGHEIVPSSPLVPRNDPTLMFTNAGMVQFKNVFTGVEKRPYQRATTSQKCVRAGGKHNDLDNVGYTARHLTFFEMLGNFSFGDYFKERAIELAWKLITKDFGLNKDKLLVTVYHTDDEAHGLWKKIAGFSDDRIIRIPTSDNFWAMGDTGPCGPCSEIFIDRGDHIWGGPPGSPEEDGDRFLEFWNLVFMQYEQVTKEERVDLPRPSIDTGMGLERMACIMQGVDSVFETDLFRHLIDATASALGSGPNEQTVASFRVIADHLRSSAFLVSDGVLPSNEGRGYVLRRIMRRAMRHAQLLGAKEPLMHRLVWALVREMGQAYPELMRAEKLIEETLRLEETRFRKTLTRGLAILDEKSASLKKGDMFDGDVAFTLYDTYGFPLDLTQDALKSRGIGVDQSAFTDAMERQKAKARESWKGSGEAASEAIWFPLREKLGATEFLGYETESAEGVVSALVKDGQEAASLKAGETGALVLNQTPFYAESGGQVGDTGVLLGEGGVKFRVTDTQKKLGDLFVHVGTVESGELKLGTALQLEVDHSRRSSIRAHHSATHLIHEALRQVLGDHIAQRGSMVAPDRLRFDFVHPKPITAEELARVEDIANDVVLENDEVTTRVMGVDEAREAGARALFGEKYGDEVRVVSMGRTARERGANALGWSVELCGGTHVRRTGDIGLITLTGESAVASGVRRIEALTGNYARKHANDTMALAKTAANELRTSIDDVPARITALMEERKKLERELSDARKKLAMGGGAAASNGAASGVREVGDVKLMARAVEGIEMKDLKSLADDGKKQIGSGVVAIVGVTGDGKAGIVVGVTADLTARFNAVNLVRVASEALGGKGGGGRPDMAQAGGPDGAKAPEALAAIEKAMAGA | 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.
Catalytic Activity: ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala)
Sequence Mass (Da): 96773
Sequence Length: 892
Domain: Consists of three domains; the N-terminal catalytic domain, the editing domain and the C-terminal C-Ala domain. The editing domain removes incorrectly charged amino acids, while the C-Ala domain, along with tRNA(Ala), serves as a bridge to cooperatively bring together the editing and aminoacylation centers thus stimulating deacylation of misacylated tRNAs.
Subcellular Location: Cytoplasm
EC: 6.1.1.7
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Q8K9E7 | MKKTTNEIRQSFLNFFKEKEHVIVPSSSLIPENDSTLLFTNAGMNQFKEYFLGQKKKFYPRVTTVQNCLRTGGKHNDLENVGYTKRHHTFFEMLGNFSFNDYFKKEAITYAWELLTSRKWFNIDKNKLWISVYEDDEETYKIWRDIIRIPCHHIVKIGSKNNSQYDSENFWQMGETGPCGPCTEIFYNYDDSNKSNDFLKDKNESFIEIWNIVFIEFNRISKTKIVPLINKSIDTGMGLERISAVLQNVHSNYKIDIFQKLIQKISNFTEIKDLNNISLKIIADHIRSCAFLIAENILPSNEHRGYVLRRIIRRALRHGHKIGIKNNFFYKLVPSLIEIMGDSAKILRKKEKIIEETLKIEEIQFSQTLDKGLKILNAEIKKSTNKTISGKTAFYLYDTFGFPIDLTSDICSEKNIKIDFKGFNIAKEEQKKRSSIKNKFYKDYNKDIIINDTCIFEGYKKNKTKSLVKYIFIKNESVFLIYKGQTATIFLDKTSFYPESGGQIGDIGELYHKKSRFIVENTKKYGDTIGHYGKLISGKIIVNDSIYSKINHVYRNAIQLNHSATHLLHAALQKVLGKNAIQKGSLVSNTHLRFDFSYSGNINLSQIQNIENIINKKIRSNDLIKIKNLSLEEAKKKKAIALFDYKYQSSVRVVFIKDFSIELCGGTHTKRTGNIGLFKIIEQSSVSSGIKRIEAVTGQQAIDYLHIKDNDMQNISFLLKCQNSKITEKIKKIIIQVEKLEKKTDQLQKRENIYQIKKLSKKINNIKGINLLINTFTNYDQKSMKMIIDQLKKELKISIIIFINKNKNDFTVIIRVTKNLINYITALKIINIFIKKANGKGGGKKEIAEGGGMNIKKLPMILNYIKSWITIQLENIKTKNFNN | 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.
Catalytic Activity: ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala)
Sequence Mass (Da): 102345
Sequence Length: 883
Domain: Consists of three domains; the N-terminal catalytic domain, the editing domain and the C-terminal C-Ala domain. The editing domain removes incorrectly charged amino acids, while the C-Ala domain, along with tRNA(Ala), serves as a bridge to cooperatively bring together the editing and aminoacylation centers thus stimulating deacylation of misacylated tRNAs.
Subcellular Location: Cytoplasm
EC: 6.1.1.7
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P59420 | MIYTSNEICQMFLNFFYKKGHTILPGSTLIPNNDPSLLFTNSGMNQFKDIFIQKNYNFKYNRVTTLQNCLRTGGKHNDFENVGYTPQHHTFFQMLGNFSFRDYFKLDAILYAWKFLTSKEQLNLSKEKLWITVYQDDLESYNIWKNIIKIDKHKIIKIGNKYNSSDSDNFWQMGEIGPCGPCTEIFYDYGNTLPGTIPGNNGCNVPRFVEIWNIVFIQFNKLSNGKLIKLTESYVDTGMGLERISAVINNVTSNYEIDLFKPLIKHILELSTVNTPKNKSIYVIADHIRACSFIISENIIPSNEKHGYVLRRIIRRAIRHGHNLGIKSLFLHKLIPTLINTMGKFNPVLKKQQNKIENVLKLEEQKFIETLEKGLKLLHKELKQIQPKHVLSGKLAFNLYDTFGFPIDLTIDICKEHNISINIMEFKRYLNQHKQNSINKNFLNTRNAYYIEDNNINIKTHFVGYQFNKTQSIINNIIIKNNKKTLQINDYQNSILFLNETPFYGESGGQIGDSGIIHNKTGKFIVNCTKMFGNIIGHVGTLASGYLNIHDTVCAEINLPKRKSIQINHTATHLLHASLRKILGKHVFQKGSFISDQSLKFDFSHNAPMNLREIQEVENIINKKIQKNISVSTTLTTLQEIQNKKVMALFQDKYKDKVRMISINDFSVELCGGTHTKYTGDIGLFKITSEISISSGIRRIEAVTGKHAISIIHHQEKTINNIANMLNSKTNNIEQTITKLLNNNIHLKKQIYTLYNQNIYNIVNSLSKHNILIKDVNIIIKNLKNENLLSLRNIVDKLKNRFKCSVIIISSIINNKSIIIVGVTRNVTDRISALDILNKLTKKLGGRGGGKNNIAEGGIKNLISLPIELKKIKTWISSRL | 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.
Catalytic Activity: ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala)
Sequence Mass (Da): 100873
Sequence Length: 880
Domain: Consists of three domains; the N-terminal catalytic domain, the editing domain and the C-terminal C-Ala domain. The editing domain removes incorrectly charged amino acids, while the C-Ala domain, along with tRNA(Ala), serves as a bridge to cooperatively bring together the editing and aminoacylation centers thus stimulating deacylation of misacylated tRNAs.
Subcellular Location: Cytoplasm
EC: 6.1.1.7
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Q057H8 | MKTDKIRAMFLQFFKEKNHKIFKSSSLIPKDDNSLLFTNAGMNQFKKIYLKNKKKNQLSIATSQYCIRTGGKHDDLKKVGHTPYHHTLFEMLGNFSFGEYFKENAIKYAWEFLTHKKWLNLSKKKIWITYYYNDNETKKIWLNIIKIKNTHLIKIYDKKNIKYNSDNFWKMGDLGPCGPSTEIFYYQKKNRKEKKSIKSYKELEKYCLEIWNLVFMEFNQITKKKIIKLPIPSIDTGMGLERISVILQNVKSIFHTNNFIQLIEAIKKKIKIKIKKKNNVSLKIISDHIRTSTCLIAENILPGNEGRNYVLRKIIRRALCHGYFIGLQKPFFYKLSELIIYNMKKMNYDFHIQEKIHKIKKILFYEEKQFYYILENGLQKLKKIIKNIKKNKICEQKIFTLYDTYGLPIQITQKFCKKKNISFNINKLNLIIKNNKKKQKNKEKKKKNFSFITFKKKSIFDGYHIYEKKSKIIQIIYKNKNVLKLSKSQLGIIILDITPFFSKSSGQIGDSGKILNDKGIFIVQKTKKFDNYILHIGYIKHGCINIKDIVHAKINKKKRKTIQSNHSATHLLNAALCKIFSEKIIQKGSFINDKYLRFDFFCNKTLTEEKINYLENIINKKIQKNIPINFVITSFKKAKKKKIKFLLEKKYKKTVRIIYIKNFSIELCNGTHHDNTGKIGCFKIIAYNNIGNEIKRITAITGMEVIQYFNDKDKINKKLENLFSTNIHNIYLIAKNIVNKNKKLLEENIKLKNKNIIEISKILISKAYLSNKKFLIIEKTSYIEYKLLRKLSDILKEKLKSLIVILINDNNKKINFLISITKNLKHIINLNNIKNIIFSVIPGTGGGKKTIIEGKFNIDKIHLYKIDKIKKKIIKYINKYK | 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.
Catalytic Activity: ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala)
Sequence Mass (Da): 104147
Sequence Length: 881
Domain: Consists of three domains; the N-terminal catalytic domain, the editing domain and the C-terminal C-Ala domain. The editing domain removes incorrectly charged amino acids, while the C-Ala domain, along with tRNA(Ala), serves as a bridge to cooperatively bring together the editing and aminoacylation centers thus stimulating deacylation of misacylated tRNAs.
Subcellular Location: Cytoplasm
EC: 6.1.1.7
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Q39HB7 | MKAAEIREKFLKFFESKGHTIVRSSSLVPGNDPTLMFTNSGMVQFKDVFLGTDPRPYSRATTAQRSVRAGGKHNDLENVGYTARHHTFFEMLGNFSFGDYFKHDAIKFAWELLTTVYQLPKDKLWVTVYQEDDEAYDIWAKEVGVPTERIIRIGDNKGARYASDNFWTMGDTGPCGPCTEIFYDHGPDVWGGPPGSPEEDGDRYIEIWNLVFMQFNRDAQGNMTRLPKQSVDTGMGLERLAAVLQHVHSNYEIDLFQNLIKAAARVTEISDLTNNSLKVIADHIRACSFLIVDGVIPGNEGRGYVLRRIVRRAIRHGYKLGRKGSFFHKLVADLVAEMGVAYPELKEAEQRVTDVLRQEEERFFETIEHGMSILEGALADVEAKGGKVLDGELAFKLHDTYGFPLDLTADVCRERGMTVDEPAFDDAMARQREQARAAGKFKAAQGLEYTGAKTTFHGYEEIAFDDAKIVALYVDGSSVNEVKTGQDAVVVLDHTPFYAESGGQVGDQGVLANAATRFAVADTLKVQADVIGHHGTLEQGTLKVGDVLRAEIDAHRRARTQRNHSATHLMHKALREVLGAHVQQKGSLVDAEKTRFDFAHNAPMTDDEIRRVEQIVNNEILANAPGIVRVMPYDEAVKGGAMALFGEKYGDEVRVLDLGFSRELCGGTHVSRSGDIGFFKIVVEGGVAAGIRRVEAITGDNAVRYVQELDARVNEAAAALKAQPSELTQRIAQVQDQVKSLEKELGALKSKLASSQGDELAQQAVEIGGVFVLAATLDGADAKTLRETVDKLKDKLKSAAIVLAAVESGKVSLIAGVTPDASKKVKAGELVNFVAQQVGGKGGGRPDMAQAGGTEPANLPGALAGVKGWVEERL | 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.
Catalytic Activity: ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala)
Sequence Mass (Da): 95520
Sequence Length: 874
Domain: Consists of three domains; the N-terminal catalytic domain, the editing domain and the C-terminal C-Ala domain. The editing domain removes incorrectly charged amino acids, while the C-Ala domain, along with tRNA(Ala), serves as a bridge to cooperatively bring together the editing and aminoacylation centers thus stimulating deacylation of misacylated tRNAs.
Subcellular Location: Cytoplasm
EC: 6.1.1.7
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B0TFY7 | MEFTGNRVRQLFLEYFEQKGHTIVASSSLVPHNDPTLLFSNAGMNQFKDVFLGFEKRPYLRATTSQKCVRAGGKHNDLDTVGRTARHHTFFEMLGNFSFGDYFKKDAIRYAWEFLTDVCGLPKDKLYATVYLDDDEAFALWRDMIGLPEARILRLGEKDNFWAMGDTGPCGPCSEILIDRGEHLRCKAEECAIGKCDCDRWLEIWNLVFMQYNRDENGTMTPLPRPSIDTGMGLERVTSVLQKVGSNYDTDLLRPLIAFVEQLCGQVYHRDDRGFPFRVIADHIRSCTFLITDGVLPSNEGRGYVLRRILRRAVRFGKVLGIDKPFMYEIVPVVVELMGEAYPDIREKQDFVCKVIKIEEERFHETLHDGMRIAADMVAKVKQEGGNVLPGKQAFTLYDTYGFPLDLAEDIAEENGLTVDKDGFQQAMEAQRERARAARQDTAYGAGMELWAELLQQLGPTVFTGYGRTSGESVVKAIVAGATRVTEAGAGTAVQVVLAETPFYAESGGQIGDSGLLRAGDAVVRVEDTKKMAGGLHVHFGVVAEGVFKEGDQVVAEVESARRLAIARHHSATHLMHKALKEVLGEHVNQAGSLVTPDRLRFDFSHFSPLTRDEWNRIEAAVNRAVFQALPVEVFETSIDEAKAMGATALFGEKYGDRVRVVRMGNYSMELCGGTHLDNTSQVGLCKLLSESGIGAGLRRIEAVTGEAALAYLNEQEETVRMLAEKLKVPAAEVTNRVDSLQAQLREKEREMEQLLSRLAKYQIDDLLAGKEEINGVTVLAAKVQAPDMDALRSMSDLLKEKLGSGVLILGAVAGDKVNLVAAATKDIVGRGVHAGNLVKEAAKVCGGGGGGRPDMAQAGGKDPSRLSDALEAAKKLLKSQIK | 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.
Catalytic Activity: ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala)
Sequence Mass (Da): 97267
Sequence Length: 883
Domain: Consists of three domains; the N-terminal catalytic domain, the editing domain and the C-terminal C-Ala domain. The editing domain removes incorrectly charged amino acids, while the C-Ala domain, along with tRNA(Ala), serves as a bridge to cooperatively bring together the editing and aminoacylation centers thus stimulating deacylation of misacylated tRNAs.
Subcellular Location: Cytoplasm
EC: 6.1.1.7
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P56452 | MDIRNEFLQFFQNKGHAVYPSMPLVPNDATLLFTNAGMVQFKDIFTGIVPRPSIPRAASSQLCMRAGGKHNDLENVGYTARHHTLFEMLGNFSFGDYFKEEAILFAWEFVTKNLGFKPKDLYISVHEKDDEAVKLWEKFVPVDRIKKMGDKDNFWQMGDSGPCGPCSEIYIDQGEKHFKGSEDYFGGEGDRFLEIWNLVFMQYERSNDGVLSPLPKPSIDTGMGLERVQALLEHKLNNFDSSLFAPLMEEISELTSLDYASEFQPSFRVVADHARAVAFLLAQGVHFNKEGRGYVLRRILRRALRHGYLMGLKEAFLYKVVGVVCEQFANTHAYLKESKEMVVKECFEEEEHFLETLESGMELFNLSLKHLNENKIFDGKIAFKLYDTFGFPLDLTNDMLRSHGACADMQGFELCMQEQVKRSKASWKGKQNNADFSAILNAYAPNVFVGYETTECSAKVLGFFDSDFKEITDANPNQEVWVLLEKTPFYAEGGGAIGDRGALFKDNGEVAIVLDTKNFFGLNFSLLEIKKALKKGDQVIAQVSDERFEIAKHHSATHLLQSALREVLGSHVSQAGSLVESKRLRFDFSHAKALNDEELEKVEDLVNAQIFKHLNSQVEHMPLNQAKDKGALALFSEKYAENVRVVSFKEASIELCGGIHVENTGLIGGFRIVKESGVSSGVRRIEAVCGKAFYQLAKEENKELKNAKTLLKNNDVIAGINKLKESVKNSQKAPVSMDLPVEKIHGVNLVVGVVEQGDIKEMIDRLKSKHERLLAMVFKKENERITLACGVKNAPIKANVWANEVAQILGGKGGGRGDFASAGGKDIENLQAALNLAKNTALKALEG | 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.
Catalytic Activity: ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala)
Sequence Mass (Da): 94700
Sequence Length: 847
Domain: Consists of three domains; the N-terminal catalytic domain, the editing domain and the C-terminal C-Ala domain. The editing domain removes incorrectly charged amino acids, while the C-Ala domain, along with tRNA(Ala), serves as a bridge to cooperatively bring together the editing and aminoacylation centers thus stimulating deacylation of misacylated tRNAs.
Subcellular Location: Cytoplasm
EC: 6.1.1.7
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A9B660 | MKGSELRQRFLDYFARQGHAVVPSSSLIPADNPTLLFTVAGMVQFNDVFLGRESRPYSRAVSSQKCLRISGKQNDLENVGPSPRHHTFFEMLGNFSFGDYFKKDAIRFAWEFLTQEIGLDPKRMWVSIYEGDEQIPADEEAHDLWLAYMPAERILRFDAKDNLWSAGDVGPRGPCSEIHYYIGDDPDNQVPEGVNSEDDTYMEIWNLVFMQYNRDENGVLTLLPKPSIDTGMSLERLAIVKQGVFRSYETDLFTPIIHTVMELLGTGSDHYQANSSAYHVVADHSRSIAFMIADGLRPGNEGRSYVLRRLVRRAAYFGQTIGFKAPFLAETIATVIDMMGAAYPELRSKQAYIAEVVTGEEERFNKTLAGGLRQLEAMLPNQADKAVFSGADAFKLYDTYGFPLDLTERIVAERGLTVDLAGYEAELEAQRARGRGAAQFKKGAVTERWAERNLAPTSFTGYNELESWGHVLALEFDGEELGTVQRGQEVAFVLDRTPCYAESGGQMGDSGVLVGPHGTIVIDDVQKPVPGVFVHRGKVSKGSVSLGEQVTVTVDAARRRDIVRNHTATHLLHRALRDTLGDHAEQKGSLVAPERLRFDFNNQKGLSSEQLQQIEDQVNAWIRADSKVEAAEMALPQARELGAMALFGEKYGDVVRVVTVGCGNASDHIHTNSEAPVCSRELCGGVHVARTGEIGFFKIVSEGSVASGVRRIEAVTGRAAAEWVSQQAQLIRTLGDKLGAQPGKVEEKLDALLLDQKARRDEIERLRGEIAAGQVDSLLAQKIEQAGTPLVVARVEASDADSFRRLGEQLRDKIGSGVVILGTVIDGKPLLLAAATADQVKAGRHAGNLVKALAAKVGGGGGGRADFAQAGGRDAAALDQALAEANGLL | 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.
Catalytic Activity: ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala)
Sequence Mass (Da): 97075
Sequence Length: 889
Domain: Consists of three domains; the N-terminal catalytic domain, the editing domain and the C-terminal C-Ala domain. The editing domain removes incorrectly charged amino acids, while the C-Ala domain, along with tRNA(Ala), serves as a bridge to cooperatively bring together the editing and aminoacylation centers thus stimulating deacylation of misacylated tRNAs.
Subcellular Location: Cytoplasm
EC: 6.1.1.7
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Q6MB06 | MLTQSIRRQFLEYFKKHQHQIVSSSSVLPHDDPTLLFNNAGMNQFKDVFLGKSYRDYNRAATSQKCIRVGGKHNDLENVGHTSRHLTFFEMLGNFSFGDYFKTQAIRFAWEVSTQVFGFEPERIWPTVFREDDETFELWTQYVPAERITRFGEKDNFWAMGDTGPCGPCSELLYDRGSDYGNATKPSEDSSGERFLEFWNLVFMQFNRQTSGVQNPLPKPSIDTGAGLERVINLKMGVNSVFETDILRSIIAQIELLSGIAYHPQDQQSAAFRVIADHLRCLSFAIADGVQPSNVDRGYVLRKVLRRAVRYGRTLKLEKPFLAEVLPQLVSTMGSDYPELVKGQDRIAEILTIEEEAFIRTLKRGGNILNQVIEKSRASHQIISGDDAFKLKDTYGLPIEEILLIAKDSGLKVDEPRYQQLEEEAKQRSRHVHKTVHQIAGENIFADFVKVRGETKFAGFTQNSLKSSVVGLFVNGEFVEEMQSGQEGLVFLSETPFYAEMGGQVGDTGTLENSNSKFSVEDCVVPYKGLIAHKGKLNTGSLKNGEMITASIDKKRRQKIANNHTATHLLHWALHQILGEHIKQAGSVVDPQRLRFDFSHHKALSLEESRQIEDLVNQKIRENLPVKCYEIKYEEAQKKEDIKQFFGEKYGSTVRVIDIDYSKELCGGTHTSALGNIGLFRILKESGIAAGIRRIEAVTGAEAELLQRQDEDLLRTLAQQLKVPIHQVLEKLEKLQEENKQFIAELKEIKKKELNVLINGFIKKIEQLGNTSVLILETALSVEELRLCVDLISDQIPSAVIILGAAFPDKCQILVKISDDLVKQGINANEIIKILMPIVEGSGGGKQHTAQGGGKKPAMLGEAFKQIRIYLKEKMNVK | 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.
Catalytic Activity: ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala)
Sequence Mass (Da): 98968
Sequence Length: 878
Domain: Consists of three domains; the N-terminal catalytic domain, the editing domain and the C-terminal C-Ala domain. The editing domain removes incorrectly charged amino acids, while the C-Ala domain, along with tRNA(Ala), serves as a bridge to cooperatively bring together the editing and aminoacylation centers thus stimulating deacylation of misacylated tRNAs.
Subcellular Location: Cytoplasm
EC: 6.1.1.7
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A5D3F4 | MTGNEIRESYLKFFEKKGHKILPSASLIPLNDPSILWTAAGMVPFKPFFTGAAKPEYTRVTTCQKCIRTPDIESVGKTARHHTFFEMLGNFSFGDYFKESAIPWAWEFVTEHLRLPADKLWISIFLDDDEAFEIWNKTVGVPAGRIVRMGKDTNFWEIGVGPCGPCSEIYVDLGAERGCGSPECKVGCDCDRFLEIWNLVFIQFFKDEEGNYTPLTSKGIDTGFGLERVASVMQGVPTNFDTDLFREIMDFTAGLFGLKYGVDGRVDVALKVIADHCRAITFAVADGALPSNEGRGYVIRRLLRRAVRFGRLLGIEDPFLHEVSGAVVRQMGRVYPELVTQREHVFRVIRREEERFGETLAQGTEMLNRLIAEARQAGSAVVSGEDAFRLYDTYGFPLELTQEMAGEQGLTVDTDGFGRAMEEQRQRARSARQETDYISGRDAMFKKMREEVGETVFVGYDALEATGRVLRIVQGGKRLESAQAGEEVEFILDVTPFYAESGGQVSDRGKVTAADLEVEIHEVTKPVENLFVHRGKVVAGILKEHDTVTARVDPARRAATCRNHSATHLLHKALKEVLGGHVNQAGSLVEPERLRFDFTHYAAATPEELQKVEELVNRMVLSALPVEAFETSLAEARKMGAAALFGEKYGERVRVVKMGDFSLELCGGTHLRNTAEVGLFKLLGESSVGAGLRRIEAVTGEGALSYVKAKEEQLAEIARLVKAAPHEAVRRVEGLLQTVRDLEAENEALQARLARYQVQDLMDRLREVKGVKVLAGQAAAPDMDSLRGMVDLLRDRVGSGVIVLGSAGENRVNLVAAVTKDLVEKGLHAGKLVKELAPVVGGGGGGRPEMAQAGGKDPSRLKEALEKTYKAVESQLK | 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.
Catalytic Activity: ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala)
Sequence Mass (Da): 96721
Sequence Length: 877
Domain: Consists of three domains; the N-terminal catalytic domain, the editing domain and the C-terminal C-Ala domain. The editing domain removes incorrectly charged amino acids, while the C-Ala domain, along with tRNA(Ala), serves as a bridge to cooperatively bring together the editing and aminoacylation centers thus stimulating deacylation of misacylated tRNAs.
Subcellular Location: Cytoplasm
EC: 6.1.1.7
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Q6L1Z4 | MEFDLEFFRENNFVRKQCSVCSSYFWTLDDKRSTCGDPACNGYSFINKSPVYKKYNVDEMRDEFIKFFENDSLPHKFVEPYPVVPRWRDDVLLVNASIYDFQPQVTSGLAKPPGNPIVMSQPSIRMLDIDLVGKTGRHLTSFEMLCHDSFNYDDNYIYWKDETVRYSFRFLTERLRVDPLLITYKEKPWFGGGNAGNALEVFVMGLEVATLVFMDLKEDKNGDIELEGTRYSRMPLRVVDTGYGLERLVWLSTGTPTVYESIYKRSLDYIIKNSNAEYVSPEIMARISEIAAEIDPYSDELVLSRINKTGDKKFMEMLDNIRSAYGLVDHARTLLLMFSDYVIPSNVKVGYLARMLLRRSFRFMEKIKFNGSINDIFDAVYDEFNKIIKNYDKDFINNIIKIETEKYKEMLRSAPEIIRKHINKNTISNENIAKIYDTYGIPLEIISKVFKDLTNKELDIPENFQEYLVKLHENVKKPEKTVKDYPDINTRPLYYNDTGIMEFTGIVMYSNGNEIILNQTAFYPEGGGQPADHGYFLYNGKKIEVLDVQKYGNSIVHIINGSIPGHSRIKGFVDKERRTQLMIHHSATHLLLGICRAYFGEHVWQNSVKKDIDESRLDITHYKKITEDDIKNIENMCLDAIMASKNIHVKNIEWNRAISEYGFRLFEGGFPLSDTIRVVTIDDIDSEGCGGTHLKNTKDILMLKIVSTETVQEGIQRIVFTAGPAALRYSQKLYSIINDEQEYLKVPPEKIPEQSIKLVRENIENKKMINSLERELAEIYIKNALRIDDESFYIKSNEILSRVILKYTGARNGRFIINTGSRIYISSSYNDADVIASMLSNNYSGSKRVAICDCNANENLIKEILVKIKR | 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.
Catalytic Activity: ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala)
Sequence Mass (Da): 100575
Sequence Length: 870
Domain: Consists of three domains; the N-terminal catalytic domain, the editing domain and the C-terminal C-Ala domain. The editing domain removes incorrectly charged amino acids, while the C-Ala domain, along with tRNA(Ala), serves as a bridge to cooperatively bring together the editing and aminoacylation centers thus stimulating deacylation of misacylated tRNAs.
Subcellular Location: Cytoplasm
EC: 6.1.1.7
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