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stringlengths 6
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stringlengths 11
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Q0DGG8 | MLVVVARKSSSSARVAAHQTRSHRAAMPAGQPHAHEPDGGGASHRRPQSPPSLPAEVVPAFAPPESEDEESWVWSQIKAEARRDADAEPALASFLYATVLSHPSLPRSISFHLANKLCSSTLLSTLLYDLFLASFTAHPSLRAAVVADLLAARSRDPACVGFSQCLLNFKGFLAIQAHRVSHVLWAQQRRPLALALQSRVADVFAVDIHPAAVVGKGILLDHATGVVIGETAVVGDNVSILHHVTLGGTGKAVGDRHPKIGDGVLIGAGATILGNVKIGAGAKIGAGSVVLIDVPARNTAVGNPARLIGRKNGEVEKDEDMPGESMDHTSFIRQWSDYTI | Catalytic Activity: acetyl-CoA + L-serine = CoA + O-acetyl-L-serine
Sequence Mass (Da): 35852
Sequence Length: 340
Pathway: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine from L-serine: step 1/2.
EC: 2.3.1.30
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A0A084B9Z3 | MSTMAKSPEANNLHQDVIAQFPILNGYTHTVGAFSQPLNVSRLFIIDEIQTAYDELRVQIPWLAHQVVVVDAGPGKSGYITTAPWPSSAPPNDVTYEEKDDAFPSLNTLIKSGGSFLATKDLVGYPGLPEPHGLHPTPVATIRLVFITGGVLVVLSTHHNIVDGIGLMQMWDYLDILMGGGAISRQDARSANADRARVLPLIAPGEPVKDYSHLIRPNPWPLPPPPKTEWRLFKMHPWALAEIRSRARDGTDQRASARPASSDDALTAFCWQRVSAMRLASGRVTGDQVSKFGRAVNGRSAMGLDSSYLFHMMLHTETRLPIEQIARSTLAELSTQLRKDLDAARTEWSVRSYATFLAGVADKTRLLYGGITNPQTDLGGTSTMHWASRRPIRLGLLGDCHLIRKPEGMPLPGCLYFMPSGGTSGVVQLLLCLPKEELDALQEDAEWKHYTESGGRRVDGPRL | Function: O-acetyltransferase; part of the satratoxin SC1 cluster involved in the biosynthesis of satratoxins, trichothecene mycotoxins that are associated with human food poisonings . Satratoxins are suggested to be made by products of multiple gene clusters (SC1, SC2 and SC3) that encode 21 proteins in all, including polyketide synthases, acetyltransferases, and other enzymes expected to modify the trichothecene skeleton . SC1 encodes 10 proteins, SAT1 to SAT10 . The largest are SAT8, which encodes a putative polyketide synthase (PKS) with a conventional non-reducing architecture, and SAT10, a putative protein containing four ankyrin repeats and thus may be involved in protein scaffolding . The putative short-chain reductase SAT3 may assist the PKS in some capacity . SAT6 contains a secretory lipase domain and acts probably as a trichothecene esterase . SAT5 encodes a putative acetyltransferase, and so, with SAT6, may affect endogenous protection from toxicity . The probable transcription factor SAT9 may regulate the expression of the SC1 cluster . SC2 encodes proteins SAT11 to SAT16, the largest of which encodes the putative reducing PKS SAT13 . SAT11 is a cytochrome P450 monooxygenase, while SAT14 and SAT16 are probable acetyltransferases . The SC2 cluster may be regulated by the transcription factor SAT15 . SC3 is a small cluster that encodes 5 proteins, SAT17 to SAT21 . SAT21 is a putative MFS-type transporter which may have a role in exporting secondary metabolites . The four other proteins putatively encoded in SC3 include the taurine hydroxylase-like protein SAT17, the O-methyltransferase SAT18, the acetyltransferase SAT19, and the Cys6-type zinc finger SAT20, the latter being probably involved in regulation of SC3 expression .
Sequence Mass (Da): 50824
Sequence Length: 463
Pathway: Mycotoxin biosynthesis.
EC: 2.3.1.-
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A0A084B9Z4 | MPQDPNTTLQMSSSKPSLSDLSVSADPVLGKADNQVRDSLALPSIEGGEEGVMRPLAWLFGLCAIQQASGATLLRNDVSTVEPLPPTQDPWYRAPPGFEKKQPGDVLRIRQAPGNLTTVVSNSSAAFHILFRTTNARSEPAWAVTTLFLPKKLYRAPSRNAALLSFQLADNSANPDSAPSLGLYWRLAQDNPMLGLRSDTSFISNLLSEGWLVNIPDQSGPEAAFGASRQAGHATIDAIRAIQHLCSLTGATGINAAIWGYSGGTFATGAAAELMPTYAPNINIVGAVLGGMVTDVSGGFDSLNRSPIAATIIATLLGVTAQFPEERAYLESRLVPETRDEFMSVLDINVFDALVHFAGRDIYAFFIDGAADIEAPILQNLFEAQSRIGFGDIPPMPMFIYKAIADEVVPIGPTDVTVQRWCDGGADITYERNTVGGHIAEIENGKPRAIQWLWSIFDESYSAQSPECRIRDVTVEVPVQVVGRV | Function: Probable trichothecene esterase; part of the satratoxin SC1 cluster involved in the biosynthesis of satratoxins, trichothecene mycotoxins that are associated with human food poisonings . Satratoxins are suggested to be made by products of multiple gene clusters (SC1, SC2 and SC3) that encode 21 proteins in all, including polyketide synthases, acetyltransferases, and other enzymes expected to modify the trichothecene skeleton . SC1 encodes 10 proteins, SAT1 to SAT10 . The largest are SAT8, which encodes a putative polyketide synthase (PKS) with a conventional non-reducing architecture, and SAT10, a putative protein containing four ankyrin repeats and thus may be involved in protein scaffolding . The putative short-chain reductase SAT3 may assist the PKS in some capacity . SAT6 contains a secretory lipase domain and acts probably as a trichothecene esterase . SAT5 encodes a putative acetyltransferase, and so, with SAT6, may affect endogenous protection from toxicity . The probable transcription factor SAT9 may regulate the expression of the SC1 cluster . SC2 encodes proteins SAT11 to SAT16, the largest of which encodes the putative reducing PKS SAT13 . SAT11 is a cytochrome P450 monooxygenase, while SAT14 and SAT16 are probable acetyltransferases . The SC2 cluster may be regulated by the transcription factor SAT15 . SC3 is a small cluster that encodes 5 proteins, SAT17 to SAT21 . SAT21 is a putative MFS-type transporter which may have a role in exporting secondary metabolites . The four other proteins putatively encoded in SC3 include the taurine hydroxylase-like protein SAT17, the O-methyltransferase SAT18, the acetyltransferase SAT19, and the Cys6-type zinc finger SAT20, the latter being probably involved in regulation of SC3 expression .
Sequence Mass (Da): 52159
Sequence Length: 485
Pathway: Mycotoxin biosynthesis.
EC: 3.1.1.-
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A0A084B9Z5 | MSTSTSEPGAIAGLPLGAEVRTDGDATGLSVAIVGGGIVGIALALGLVERGVRVSVYERAQELPEIGVGFAFNGAARKSMARLSPLVMAAVERVANENEQAYDNYWDGYTSTAEDDESSTASKRGKLLFRMPNSNMAWWSCLRSQFLNEMLQALPPGTVTFGKELDSYDDPFDTSDPVRLRFTDGTTAAANVLIGSDGLRSRVRQQLFATSHPEVCNPTYTHKTCYRAVIPMAAAESAMGLSKPHNHCMHTGPRAHVLSYPIAQHKLVNVVLFVTHDEPWVDGTGDEAISVPRMTRPGDKKVLQNRLADWRPEVRNLVAQLPDAPTAWGIFDTAEHPVPFYAAGRVGLVGDAAHASSPHHGAGAGFGVEDALALAVALGMATEKKQSVAAALQAFNDVRYDRTQWLIRSSKETGDIYEWKHFGVGGDPVKIRAELEGRQKTIWDYDVDAMAEEVKTRYEARVTSETTAHQ | Function: FAD-dependent monooxygenase; part of the satratoxin SC1 cluster involved in the biosynthesis of satratoxins, trichothecene mycotoxins that are associated with human food poisonings . Satratoxins are suggested to be made by products of multiple gene clusters (SC1, SC2 and SC3) that encode 21 proteins in all, including polyketide synthases, acetyltransferases, and other enzymes expected to modify the trichothecene skeleton . SC1 encodes 10 proteins, SAT1 to SAT10 . The largest are SAT8, which encodes a putative polyketide synthase (PKS) with a conventional non-reducing architecture, and SAT10, a putative protein containing four ankyrin repeats and thus may be involved in protein scaffolding . The putative short-chain reductase SAT3 may assist the PKS in some capacity . SAT6 contains a secretory lipase domain and acts probably as a trichothecene esterase . SAT5 encodes a putative acetyltransferase, and so, with SAT6, may affect endogenous protection from toxicity . The probable transcription factor SAT9 may regulate the expression of the SC1 cluster . SC2 encodes proteins SAT11 to SAT16, the largest of which encodes the putative reducing PKS SAT13 . SAT11 is a cytochrome P450 monooxygenase, while SAT14 and SAT16 are probable acetyltransferases . The SC2 cluster may be regulated by the transcription factor SAT15 . SC3 is a small cluster that encodes 5 proteins, SAT17 to SAT21 . SAT21 is a putative MFS-type transporter which may have a role in exporting secondary metabolites . The four other proteins putatively encoded in SC3 include the taurine hydroxylase-like protein SAT17, the O-methyltransferase SAT18, the acetyltransferase SAT19, and the Cys6-type zinc finger SAT20, the latter being probably involved in regulation of SC3 expression .
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 50994
Sequence Length: 470
Pathway: Mycotoxin biosynthesis.
Subcellular Location: Membrane
EC: 1.-.-.-
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Q01826 | MDHLNEATQGKEHSEMSNNVSDPKGPPAKIARLEQNGSPLGRGRLGSTGAKMQGVPLKHSGHLMKTNLRKGTMLPVFCVVEHYENAIEYDCKEEHAEFVLVRKDMLFNQLIEMALLSLGYSHSSAAQAKGLIQVGKWNPVPLSYVTDAPDATVADMLQDVYHVVTLKIQLHSCPKLEDLPPEQWSHTTVRNALKDLLKDMNQSSLAKECPLSQSMISSIVNSTYYANVSAAKCQEFGRWYKHFKKTKDMMVEMDSLSELSQQGANHVNFGQQPVPGNTAEQPPSPAQLSHGSQPSVRTPLPNLHPGLVSTPISPQLVNQQLVMAQLLNQQYAVNRLLAQQSLNQQYLNHPPPVSRSMNKPLEQQVSTNTEVSSEIYQWVRDELKRAGISQAVFARVAFNRTQGLLSEILRKEEDPKTASQSLLVNLRAMQNFLQLPEAERDRIYQDERERSLNAASAMGPAPLISTPPSRPPQVKTATIATERNGKPENNTMNINASIYDEIQQEMKRAKVSQALFAKVAATKSQGWLCELLRWKEDPSPENRTLWENLSMIRRFLSLPQPERDAIYEQESNAVHHHGDRPPHIIHVPAEQIQQQQQQQQQQQQQQQAPPPPQPQQQPQTGPRLPPRQPTVASPAESDEENRQKTRPRTKISVEALGILQSFIQDVGLYPDEEAIQTLSAQLDLPKYTIIKFFQNQRYYLKHHGKLKDNSGLEVDVAEYKEEELLKDLEESVQDKNTNTLFSVKLEEELSVEGNTDINTDLKD | Function: Crucial silencing factor contributing to the initiation of X inactivation mediated by Xist RNA that occurs during embryogenesis and in lymphoma (By similarity). Binds to DNA at special AT-rich sequences, the consensus SATB1-binding sequence (CSBS), at nuclear matrix- or scaffold-associated regions. Thought to recognize the sugar-phosphate structure of double-stranded DNA. Transcriptional repressor controlling nuclear and viral gene expression in a phosphorylated and acetylated status-dependent manner, by binding to matrix attachment regions (MARs) of DNA and inducing a local chromatin-loop remodeling. Acts as a docking site for several chromatin remodeling enzymes (e.g. PML at the MHC-I locus) and also by recruiting corepressors (HDACs) or coactivators (HATs) directly to promoters and enhancers. Modulates genes that are essential in the maturation of the immune T-cell CD8SP from thymocytes. Required for the switching of fetal globin species, and beta- and gamma-globin genes regulation during erythroid differentiation. Plays a role in chromatin organization and nuclear architecture during apoptosis. Interacts with the unique region (UR) of cytomegalovirus (CMV). Alu-like motifs and SATB1-binding sites provide a unique chromatin context which seems preferentially targeted by the HIV-1 integration machinery. Moreover, HIV-1 Tat may overcome SATB1-mediated repression of IL2 and IL2RA (interleukin) in T-cells by binding to the same domain than HDAC1. Delineates specific epigenetic modifications at target gene loci, directly up-regulating metastasis-associated genes while down-regulating tumor-suppressor genes. Reprograms chromatin organization and the transcription profiles of breast tumors to promote growth and metastasis. Promotes neuronal differentiation of neural stem/progenitor cells in the adult subventricular zone, possibly by positively regulating the expression of NEUROD1 (By similarity).
PTM: Sumoylated. Sumoylation promotes cleavage by caspases.
Sequence Mass (Da): 85957
Sequence Length: 763
Subcellular Location: Nucleus matrix
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Q8VI24 | MERRSESPCLRDSPDRRSGSPDVKGPPPVKVARLEQNGSPMGARGRPNGAVAKAVGGLMIPVFCVVEQLDGSLEYDNREEHAEFVLVRKDVLFSQLVETALLALGYSHSSAAQAQGIIKLGRWNPLPLSYVTDAPDATVADMLQDVYHVVTLKIQLQSCSKLEDLPAEQWNHATVRNALKELLKEMNQSTLAKECPLSQSMISSIVNSTYYANVSATKCQEFGRWYKKYKKIKVERVERENLSDYCVLGQRPMHLPNMNQLASLGKTNEQSPHSQIHHSTPIRNQVPALQPIMSPGLLSPQLSPQLVRQQIAMAHLINQQIAVSRLLAHQHPQAINQQFLNHPPIPRAVKPEPTNSSVEVSPDIYQQVRDELKRASVSQAVFARVAFNRTQGLLSEILRKEEDPRTASQSLLVNLRAMQNFLNLPEVERDRIYQDERERSMNPNVSMVSSASSSPSSSRTPQAKTSTPTTDLPIKVDGANVNITAAIYDEIQQEMKRAKVSQALFAKVAANKSQGWLCELLRWKENPSPENRTLWENLCTIRRFLNLPQHERDVIYEEESRHHHSERMQHVVQLPPEPVQVLHRQQSQPTKESSPPREEAPPPPPPTEDSCAKKPRSRTKISLEALGILQSFIHDVGLYPDQEAIHTLSAQLDLPKHTIIKFFQNQRYHVKHHGKLKEHLGSAVDVAEYKDEELLTESEENDSEEGSEEMYKVEAEEENADKSKAAPAETDQR | Function: Binds to DNA, at nuclear matrix- or scaffold-associated regions. Thought to recognize the sugar-phosphate structure of double-stranded DNA. Transcription factor controlling nuclear gene expression, by binding to matrix attachment regions (MARs) of DNA and inducing a local chromatin-loop remodeling. Acts as a docking site for several chromatin remodeling enzymes and also by recruiting corepressors (HDACs) or coactivators (HATs) directly to promoters and enhancers. Required for the initiation of the upper-layer neurons (UL1) specific genetic program and for the inactivation of deep-layer neurons (DL) and UL2 specific genes, probably by modulating Bcl11b expression. Repressor of Ctip2 and regulatory determinant of corticocortical connections in the developing cerebral cortex. May play an important role in palate formation. Acts as a molecular node in a transcriptional network regulating skeletal development and osteoblast differentiation.
PTM: Sumoylated by PIAS1. Sumoylation promotes nuclear localization, but represses transcription factor activity (By similarity).
Sequence Mass (Da): 82559
Sequence Length: 733
Subcellular Location: Nucleus matrix
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P0AFY7 | MFKSFFPKPGTFFLSAFVWALIAVIFWQAGGGDWVARITGASGQIPISAARFWSLDFLIFYAYYIVCVGLFALFWFIYSPHRWQYWSILGTALIIFVTWFLVEVGVAVNAWYAPFYDLIQTALSSPHKVTIEQFYREVGVFLGIALIAVVISVLNNFFVSHYVFRWRTAMNEYYMANWQQLRHIEGAAQRVQEDTMRFASTLENMGVSFINAIMTLIAFLPVLVTLSAHVPELPIIGHIPYGLVIAAIVWSLMGTGLLAVVGIKLPGLEFKNQRVEAAYRKELVYGEDDATRATPPTVRELFSAVRKNYFRLYFHYMYFNIARILYLQVDNVFGLFLLFPSIVAGTITLGLMTQITNVFGQVRGAFQYLINSWTTLVELMSIYKRLRSFEHELDGDKIQEVTHTLS | Function: Uptake of antimicrobial peptides.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 46459
Sequence Length: 406
Subcellular Location: Cell inner membrane
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Q6AW68 | MEPWDPPQLPPVRHSHAAGSGRAEGRHGTPPPWRPIISGPLPRPGSWDPGRDLHRPASQAESYESGHAFRAYSRQGYEDPHWQYPGAAYRDNHAYQSHQWQPTAWQGNRDVTQVKPHGKSTTYRDQHYYRGYHPNLAASPLGQDRSQTYDAYKEGSRRSWAGVSNLGEASGQPQQPSLLQQYRESGLSSSGYELSQYIRDGAEPNDTAFLGGWSPVQGGGPLESAVMAPHKFLQPHVPVCLGAGGQLVLVCPHRPTEGQLPLVELHSLEVILQGTTDQEELQAFPGPLAREDLHKVDVMTFCQQKIASSCDLSTQRGRDSALLWKLLVLLCRQNGSMVGSDVAELLMQDCRQQERYKRQEPAVGPVSLADEEWRQLGTLDLITGEVPPVVETQAQIVEKFTKLLYYGRKKDALVWAMRNQLWGHALFLSSKMDPRTYSWVLSGFTSTLATNDPLQTFFQLMSGRIPQAAQSCGDAKWGDWRPHLAVLLSNKVGDMELNHRAIVTMGDTLAGKGAVEAAHFCYLMADIPFGYFGVKADRMALLGSSHRQAFTQFATKEAIQRMEIFEYCQQLRHPTSFLLPFQVYKLLYASRLADHGLPAQALLYCEQIATVLLQQDPTSHPVLAQQLTKLAERLKLCDPLLLLEMPEQDPVLEPQWLLQLRTYCQHCQVQDDLAPEVALTQPEPWDTTATPGREMVHEQPHSDGPHDEQWHQPPVPLQGPDPHQDVSIPPLEVAVLGVGPISQEELCTEPSLQAVPTAGDAEEPQDAHGVQQPVLAELQELSTRARSASESSTASLEEDSQTSSDSPAEELEGTSEDKSFGFRWFGWFRSKPQKETSPKATTSGSPTPGLQDRRSPSPPGAVPSAQPPASPSPYRNPVSIDMKGPWDADGHEPLPGMVPLFNPAQVSQLAAARPTQPRLLSQRRYPNPL | Function: Plays a role in the organization of the endoplasmic reticulum exit sites (ERES), also known as transitional endoplasmic reticulum (tER). Required for secretory cargo traffic from the endoplasmic reticulum to the Golgi apparatus. Involved in peroxisome biogenesis. Regulates the transport of peroxisomal biogenesis factors PEX3 and PEX16 from the ER to peroxisomes.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 102956
Sequence Length: 929
Subcellular Location: Endoplasmic reticulum membrane
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P58570 | VRDAYIAEDYDCVYHCARDA | Function: Binds to sodium channels (Nav) and inhibits the inactivation of the activated channels, thereby blocking neuronal transmission.
Sequence Mass (Da): 2349
Sequence Length: 20
Domain: Has the structural arrangement of an alpha-helix connected to antiparallel beta-sheets by disulfide bonds (CS-alpha/beta).
Subcellular Location: Secreted
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C0HK98 | MVSKVALLLAVLVCSQYMAQGVYVVSKAEWGGRGAKWTVGLGNYLSYAIIHHTAGSYCETRAQCNAVLQSVQNYHMDSLGWPDIGYNFLIGGDGNVYEGRGWNNMGAHAAEWNPYSIGISFLGNYNWDTLEPNMISAAQQLLNDAVNRGQLSSGYILYGHRQVSATECPGTHIWNEIRGWSHWSG | Function: N-acetylmuramyl-L-alanine amidase involved in innate immunity by degrading bacterial peptidoglycans (PGN). Plays a scavenger role by digesting biologically active PGN into biologically inactive fragments. Has no direct bacteriolytic activity.
Catalytic Activity: Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides.
Sequence Mass (Da): 20395
Sequence Length: 185
Subcellular Location: Secreted
EC: 3.5.1.28
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P30531 | MATNGSKVADGQISTEVSEAPVANDKPKTLVVKVQKKAADLPDRDTWKGRFDFLMSCVGYAIGLGNVWRFPYLCGKNGGGAFLIPYFLTLIFAGVPLFLLECSLGQYTSIGGLGVWKLAPMFKGVGLAAAVLSFWLNIYYIVIISWAIYYLYNSFTTTLPWKQCDNPWNTDRCFSNYSMVNTTNMTSAVVEFWERNMHQMTDGLDKPGQIRWPLAITLAIAWILVYFCIWKGVGWTGKVVYFSATYPYIMLIILFFRGVTLPGAKEGILFYITPNFRKLSDSEVWLDAATQIFFSYGLGLGSLIALGSYNSFHNNVYRDSIIVCCINSCTSMFAGFVIFSIVGFMAHVTKRSIADVAASGPGLAFLAYPEAVTQLPISPLWAILFFSMLLMLGIDSQFCTVEGFITALVDEYPRLLRNRRELFIAAVCIISYLIGLSNITQGGIYVFKLFDYYSASGMSLLFLVFFECVSISWFYGVNRFYDNIQEMVGSRPCIWWKLCWSFFTPIIVAGVFIFSAVQMTPLTMGNYVFPKWGQGVGWLMALSSMVLIPGYMAYMFLTLKGSLKQRIQVMVQPSEDIVRPENGPEQPQAGSSTSKEAYI | Function: Mediates transport of gamma-aminobutyric acid (GABA) together with sodium and chloride and is responsible for the reuptake of GABA from the synapse . The translocation of GABA, however, may also occur in the reverse direction leading to the release of GABA (By similarity). The direction and magnitude of GABA transport is a consequence of the prevailing thermodynamic conditions, determined by membrane potential and the intracellular and extracellular concentrations of Na(+), Cl(-) and GABA (By similarity). Can also mediate sodium- and chloride-dependent transport of hypotaurine but to a much lower extent as compared to GABA (By similarity).
Catalytic Activity: 4-aminobutanoate(out) + chloride(out) + 2 Na(+)(out) = 4-aminobutanoate(in) + chloride(in) + 2 Na(+)(in)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 67074
Sequence Length: 599
Subcellular Location: Cell membrane
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P31648 | MATDNSKVADGQISTEVSEAPVASDKPKTLVVKVQKKAGDLPDRDTWKGRFDFLMSCVGYAIGLGNVWRFPYLCGKNGGGAFLIPYFLTLIFAGVPLFLLECSLGQYTSIGGLGVWKLAPMFKGVGLAAAVLSFWLNIYYIVIISWAIYYLYNSFTTTLPWKQCDNPWNTDRCFSNYSLVNTTNMTSAVVEFWERNMHQMTDGLDKPGQIRWPLAITLAIAWVLVYFCIWKGVGWTGKVVYFSATYPYIMLIILFFRGVTLPGAKEGILFYITPNFRKLSDSEVWLDAATQIFFSYGLGLGSLIALGSYNSFHNNVYRDSIIVCCINSCTSMFAGFVIFSIVGFMAHVTKRSIADVAASGPGLAFLAYPEAVTQLPISPLWAILFFSMLLMLGIDSQFCTVEGFITALVDEYPRLLRNRRELFIAAVCIVSYLIGLSNITQGGIYVFKLFDYYSASGMSLLFLVFFECVSISWFYGVNRFYDNIQEMVGSRPCIWWKLCWSFFTPIIVAGVFLFSAVQMTPLTMGSYVFPKWGQGVGWLMALSSMVLIPGYMAYMFLTLKGSLKQRLQVMIQPSEDIVRPENGPEQPQAGSSASKEAYI | Function: Mediates transport of gamma-aminobutyric acid (GABA) together with sodium and chloride and is responsible for the reuptake of GABA from the synapse . The translocation of GABA, however, may also occur in the reverse direction leading to the release of GABA (By similarity). The direction and magnitude of GABA transport is a consequence of the prevailing thermodynamic conditions, determined by membrane potential and the intracellular and extracellular concentrations of Na(+), Cl(-) and GABA (By similarity). Can also mediate sodium- and chloride-dependent transport of hypotaurine but to a much lower extent as compared to GABA .
Catalytic Activity: 4-aminobutanoate(out) + chloride(out) + 2 Na(+)(out) = 4-aminobutanoate(in) + chloride(in) + 2 Na(+)(in)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 67001
Sequence Length: 599
Subcellular Location: Cell membrane
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P23975 | MLLARMNPQVQPENNGADTGPEQPLRARKTAELLVVKERNGVQCLLAPRDGDAQPRETWGKKIDFLLSVVGFAVDLANVWRFPYLCYKNGGGAFLIPYTLFLIIAGMPLFYMELALGQYNREGAATVWKICPFFKGVGYAVILIALYVGFYYNVIIAWSLYYLFSSFTLNLPWTDCGHTWNSPNCTDPKLLNGSVLGNHTKYSKYKFTPAAEFYERGVLHLHESSGIHDIGLPQWQLLLCLMVVVIVLYFSLWKGVKTSGKVVWITATLPYFVLFVLLVHGVTLPGASNGINAYLHIDFYRLKEATVWIDAATQIFFSLGAGFGVLIAFASYNKFDNNCYRDALLTSSINCITSFVSGFAIFSILGYMAHEHKVNIEDVATEGAGLVFILYPEAISTLSGSTFWAVVFFVMLLALGLDSSMGGMEAVITGLADDFQVLKRHRKLFTFGVTFSTFLLALFCITKGGIYVLTLLDTFAAGTSILFAVLMEAIGVSWFYGVDRFSNDIQQMMGFRPGLYWRLCWKFVSPAFLLFVVVVSIINFKPLTYDDYIFPPWANWVGWGIALSSMVLVPIYVIYKFLSTQGSLWERLAYGITPENEHHLVAQRDIRQFQLQHWLAI | Function: Mediates sodium- and chloride-dependent transport of norepinephrine (also known as noradrenaline) . Can also mediate sodium- and chloride-dependent transport of dopamine .
Catalytic Activity: (R)-noradrenaline(out) + chloride(out) + Na(+)(out) = (R)-noradrenaline(in) + chloride(in) + Na(+)(in)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 69332
Sequence Length: 617
Subcellular Location: Cell membrane
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P27922 | MSEGRCSVAHMSSVVAPAKEANAMGPKAVELVLVKEQNGVQLTNSTLLNPPQSPTEAQDRETWSKKADFLLSVIGFAVDLANVWRFPYLCYKNGGGAFLVPYLFFMVVAGVPLFYMELALGQFNREGAAGVWKICPILRGVGYTAILISLYIGFFYNVIIAWALHYLLSSFTTELPWTHCNHSWNSPRCSDARAPNASSGPNGTSRTTPAAEYFERGVLHLHESQGIDDLGPPRWQLTSCLVLVIVLLYFSLWKGVKTSGKVVWITATMPYVVLFALLLRGITLPGAVDAIRAYLSVDFHRLCEASVWIDAAIQICFSLGVGLGVLIAFSSYNKFTNNCYRDAIITTSVNSLTSFSSGFVVFSFLGYMAQKHSVPIGDVAKDGPGLIFIIYPEALATLPLSSVWAVVFFVMLLTLGIDSAMGGMESVITGLADEFQLLHRHRELFTLLVVLATFLLSLFCVTNGGIYVFTLLDHFAAGTSILFGVLMEVIGVAWFYGVWQFSDDIKQMTGRRPSLYWRLCWKFVSPCFLLFVVVVSIATFRPPHYGAYVFPEWATALGWAIAASSMSVVPIYAAYKLCSLPGSSREKLAYAITPETEHGRVDSGGGAPVHAPPLARGVGRWRKRKSCWVPSRGPGRGGPPTPSPRLAGHTRAFPWTGAPPVPRELTPPSTCRCVPPLVCAHPAVESTGLCSVY | Function: Mediates sodium- and chloride-dependent transport of dopamine . Also mediates sodium- and chloride-dependent transport of norepinephrine (also known as noradrenaline) (By similarity). Regulator of light-dependent retinal hyaloid vessel regression, downstream of OPN5 signaling (By similarity).
Catalytic Activity: chloride(out) + dopamine(out) + Na(+)(out) = chloride(in) + dopamine(in) + Na(+)(in)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 75691
Sequence Length: 693
Subcellular Location: Cell membrane
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Q01959 | MSKSKCSVGLMSSVVAPAKEPNAVGPKEVELILVKEQNGVQLTSSTLTNPRQSPVEAQDRETWGKKIDFLLSVIGFAVDLANVWRFPYLCYKNGGGAFLVPYLLFMVIAGMPLFYMELALGQFNREGAAGVWKICPILKGVGFTVILISLYVGFFYNVIIAWALHYLFSSFTTELPWIHCNNSWNSPNCSDAHPGDSSGDSSGLNDTFGTTPAAEYFERGVLHLHQSHGIDDLGPPRWQLTACLVLVIVLLYFSLWKGVKTSGKVVWITATMPYVVLTALLLRGVTLPGAIDGIRAYLSVDFYRLCEASVWIDAATQVCFSLGVGFGVLIAFSSYNKFTNNCYRDAIVTTSINSLTSFSSGFVVFSFLGYMAQKHSVPIGDVAKDGPGLIFIIYPEAIATLPLSSAWAVVFFIMLLTLGIDSAMGGMESVITGLIDEFQLLHRHRELFTLFIVLATFLLSLFCVTNGGIYVFTLLDHFAAGTSILFGVLIEAIGVAWFYGVGQFSDDIQQMTGQRPSLYWRLCWKLVSPCFLLFVVVVSIVTFRPPHYGAYIFPDWANALGWVIATSSMAMVPIYAAYKFCSLPGSFREKLAYAIAPEKDRELVDRGEVRQFTLRHWLKV | Function: Mediates sodium- and chloride-dependent transport of dopamine . Also mediates sodium- and chloride-dependent transport of norepinephrine (also known as noradrenaline) (By similarity). Regulator of light-dependent retinal hyaloid vessel regression, downstream of OPN5 signaling (By similarity).
Catalytic Activity: chloride(out) + dopamine(out) + Na(+)(out) = chloride(in) + dopamine(in) + Na(+)(in)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 68495
Sequence Length: 620
Subcellular Location: Cell membrane
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Q9GJT6 | MSKSKCSVGLMSSVVAPAKEPNAMGPKEVELILVKEQNGVQLTSSTLTNPRQSPVEAQDRETWGKKIDFLLSVIGFAVDLANVWRFPYLCYKNGGGAFLVPYLLFMVIAGMPLFYMELALGQFNREGAAGVWKICPVLKGVGFTVILISLYVGFFYNVIIAWALHYLFSSFTTELPWIHCNNSWNSPNCSDAHSGDSGGNGPGLNDTFGTTPAAEYFERGVLHLHQSHGIDDLGPPRWQLTACLVLVIVLLYFSLWKGVKTSGKVVWITATMPYVVLTALLLRGVTLPGAIDGIRAYLSVDFYRLCEASVWIDAATQVCFSLGVGFGVLIAFSSYNKFTNNCYRDAIVTTSINSLTSFSSGFVVFSFLGYMAQKHSVPIGDVAKDGPGLIFIIYPEAIATLPLSSAWAVVFFIMLLTLGIDSAMGGMESVITGLIDEFQLLHRHRELFTLFIVLATFLLSLFCVTNGGIYVFTLLDHFAAGTSILFGVLIEAIGVAWFYGVGQFSDDIQQMTGQRPSLYWRLCWKLVSPCFLLFVVVVSIVTFRPPHYGAYIFPDWANALGWVIATSSMAMVPIYAAYKFCSLPGSFREKLAYAIAPEKDRELVDRGEVRQFTLRHWLKV | Function: Mediates sodium- and chloride-dependent transport of dopamine (By similarity). Also mediates sodium- and chloride-dependent transport of norepinephrine (also known as noradrenaline) (By similarity). Regulator of light-dependent retinal hyaloid vessel regression, downstream of OPN5 signaling (By similarity).
Catalytic Activity: chloride(out) + dopamine(out) + Na(+)(out) = chloride(in) + dopamine(in) + Na(+)(in)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 68452
Sequence Length: 620
Subcellular Location: Cell membrane
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O35899 | METTALNSQKAPSVCKDREDCQENSILQKSGPTSAGGVESGQIFNGYSSVPSTGMGDDAEHSVPTATTTLVAEVHHGERETWGKKVDFLLSVIGYAVDLGNIWRFPYVCYQNGGGAFLLPYIIMAIFGGIPLFYMELALGQYHRNGCISIWRKICPIFKGIGYTICIIAFYIASYYNTIIAWALYYLISSFTDRLPWTSCRNSWNTANCTNYFSEDNITWTLHSTSPAEEFYIRHILQIHRSKGLQDVGGVSWQLTLCIMLIFTIIYFSIWKGVKTSGKVVWVTATFPYIVLSVLLVRGATLPGAWKGVLFYLKPNWQKLLETGVWIDAAAQIFFSLGPGFGVLLAFASYNKFNNNCYQDALVTSAVNCMTSFVSGFVIFTVLGYMAEMRSEDVSEVAKDAGPSLLFITYAEAIANMPASTFFAIIFFLMLITLGLDSTFAGLEGVITAVLDEFPHIWAKHREWFVLAVVITCFFGSLTTLTFGGAYVVKLLEEYATGPAVLTVVFIEAIAVSWFYGVTQFCSDVKEMLGFSPGWFWRICWVAVSPVFLLFIICSFLMSPPQLRLFQYSYPHWSVILGYCIGTSSVICIPTYITYRLVTTPGTLKERIIKSITPETPTEIPCGDICLNAV | Function: Serotonin transporter that cotransports serotonin with one Na(+) ion in exchange for one K(+) ion and possibly one proton in an overall electroneutral transport cycle. Transports serotonin across the plasma membrane from the extracellular compartment to the cytosol thus limiting serotonin intercellular signaling (By similarity). Essential for serotonin homeostasis in the central nervous system. In the developing somatosensory cortex, acts in glutamatergic neurons to control serotonin uptake and its trophic functions accounting for proper spatial organization of cortical neurons and elaboration of sensory circuits. In the mature cortex, acts primarily in brainstem raphe neurons to mediate serotonin uptake from the synaptic cleft back into the pre-synaptic terminal thus terminating serotonin signaling at the synapse (By similarity). Modulates mucosal serotonin levels in the gastrointestinal tract through uptake and clearance of serotonin in enterocytes. Required for enteric neurogenesis and gastrointestinal reflexes (By similarity). Regulates blood serotonin levels by ensuring rapid high affinity uptake of serotonin from plasma to platelets, where it is further stored in dense granules via vesicular monoamine transporters and then released upon stimulation. Mechanistically, the transport cycle starts with an outward-open conformation having Na1(+) and Cl(-) sites occupied. The binding of a second extracellular Na2(+) ion and serotonin substrate leads to structural changes to outward-occluded to inward-occluded to inward-open, where the Na2(+) ion and serotonin are released into the cytosol. Binding of intracellular K(+) ion induces conformational transitions to inward-occluded to outward-open and completes the cycle by releasing K(+) possibly together with a proton bound to Asp-98 into the extracellular compartment. Na1(+) and Cl(-) ions remain bound throughout the transport cycle (By similarity). Additionally, displays serotonin-induced channel-like conductance for monovalent cations, mainly Na(+) ions. The channel activity is uncoupled from the transport cycle and may contribute to the membrane resting potential or excitability (By similarity).
PTM: Phosphorylation at Thr-276 increases 5-HT uptake and is required for cGMP-mediated SERT regulation.
Location Topology: Multi-pass membrane protein
Catalytic Activity: H(+)(in) + K(+)(in) + Na(+)(out) + serotonin(out) = H(+)(out) + K(+)(out) + Na(+)(in) + serotonin(in)
Sequence Mass (Da): 70114
Sequence Length: 630
Subcellular Location: Cell membrane
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P51905 | MDRSGSSDFAGAAATTGRSNPAPWSDDKESPNNEDDSNEDDGDHTTPAKVTDPLAPKLANNERILVVSVTERTRETWGQKAEFLLAVIGFAVDLGNVWRFPYICYQNGGGAFLVPYCLFLIFGGLPLFYMELALGQFHRCGCLSIWKRICPALKGVGYAICLIDIYMGMYYNTIIGWAVYYLFASFTSKLPWTSCDNPWNTENCMQVTSENFTELATSPAKEFFERKVLESYKGNGLDFMGPVKPTLALCVFGVFVLVYFSLWKGVRSAGKVVWVTALAPYVVLIILLVRGVSLPGADEGIKYYLTPEWHKLKNSKVWIDAASQIFFSLGPGFGTLLALSSYNKFNNNCYRDALITSSINCLTSFLAGFVIFSVLGYMAYVQKTSIDKVGLEGPGLVFIVYPEAIATMSGSVFWSIIFFLMLITLGLDSTFGGLEAMITALCDEYPRVIGRRRELFVLLLLAFIFLCALPTMTYGGVVLVNFLNVYGPGLAILFVVFVEAAGVFWFYGVDRFSSDVEQMLGSKPGLFWRICWTYISPVFLLTIFIFSIMGYKEMLGEEYYYPDWSYQVGWAVTCSSVLCIPMYIIYKFFFASKGGCRQRLQESFQPEDNCGSVVPGQQGTSV | Function: Terminates the action of serotonin by its high affinity sodium-dependent reuptake into presynaptic terminals.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 69326
Sequence Length: 622
Subcellular Location: Cell membrane
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P31645 | METTPLNSQKQLSACEDGEDCQENGVLQKVVPTPGDKVESGQISNGYSAVPSPGAGDDTRHSIPATTTTLVAELHQGERETWGKKVDFLLSVIGYAVDLGNVWRFPYICYQNGGGAFLLPYTIMAIFGGIPLFYMELALGQYHRNGCISIWRKICPIFKGIGYAICIIAFYIASYYNTIMAWALYYLISSFTDQLPWTSCKNSWNTGNCTNYFSEDNITWTLHSTSPAEEFYTRHVLQIHRSKGLQDLGGISWQLALCIMLIFTVIYFSIWKGVKTSGKVVWVTATFPYIILSVLLVRGATLPGAWRGVLFYLKPNWQKLLETGVWIDAAAQIFFSLGPGFGVLLAFASYNKFNNNCYQDALVTSVVNCMTSFVSGFVIFTVLGYMAEMRNEDVSEVAKDAGPSLLFITYAEAIANMPASTFFAIIFFLMLITLGLDSTFAGLEGVITAVLDEFPHVWAKRRERFVLAVVITCFFGSLVTLTFGGAYVVKLLEEYATGPAVLTVALIEAVAVSWFYGITQFCRDVKEMLGFSPGWFWRICWVAISPLFLLFIICSFLMSPPQLRLFQYNYPYWSIILGYCIGTSSFICIPTYIAYRLIITPGTFKERIIKSITPETPTEIPCGDIRLNAV | Function: Serotonin transporter that cotransports serotonin with one Na(+) ion in exchange for one K(+) ion and possibly one proton in an overall electroneutral transport cycle. Transports serotonin across the plasma membrane from the extracellular compartment to the cytosol thus limiting serotonin intercellular signaling . Essential for serotonin homeostasis in the central nervous system. In the developing somatosensory cortex, acts in glutamatergic neurons to control serotonin uptake and its trophic functions accounting for proper spatial organization of cortical neurons and elaboration of sensory circuits. In the mature cortex, acts primarily in brainstem raphe neurons to mediate serotonin uptake from the synaptic cleft back into the pre-synaptic terminal thus terminating serotonin signaling at the synapse (By similarity). Modulates mucosal serotonin levels in the gastrointestinal tract through uptake and clearance of serotonin in enterocytes. Required for enteric neurogenesis and gastrointestinal reflexes (By similarity). Regulates blood serotonin levels by ensuring rapid high affinity uptake of serotonin from plasma to platelets, where it is further stored in dense granules via vesicular monoamine transporters and then released upon stimulation . Mechanistically, the transport cycle starts with an outward-open conformation having Na1(+) and Cl(-) sites occupied. The binding of a second extracellular Na2(+) ion and serotonin substrate leads to structural changes to outward-occluded to inward-occluded to inward-open, where the Na2(+) ion and serotonin are released into the cytosol. Binding of intracellular K(+) ion induces conformational transitions to inward-occluded to outward-open and completes the cycle by releasing K(+) possibly together with a proton bound to Asp-98 into the extracellular compartment. Na1(+) and Cl(-) ions remain bound throughout the transport cycle . Additionally, displays serotonin-induced channel-like conductance for monovalent cations, mainly Na(+) ions. The channel activity is uncoupled from the transport cycle and may contribute to the membrane resting potential or excitability (By similarity).
PTM: Phosphorylation at Thr-276 increases 5-HT uptake and is required for cGMP-mediated SERT regulation.
Location Topology: Multi-pass membrane protein
Catalytic Activity: H(+)(in) + K(+)(in) + Na(+)(out) + serotonin(out) = H(+)(out) + K(+)(out) + Na(+)(in) + serotonin(in)
Sequence Mass (Da): 70325
Sequence Length: 630
Subcellular Location: Cell membrane
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Q9Y345 | MDCSAPKEMNKLPANSPEAAAAQGHPDGPCAPRTSPEQELPAAAAPPPPRVPRSASTGAQTFQSADARACEAERPGVGSCKLSSPRAQAASAALRDLREAQGAQASPPPGSSGPGNALHCKIPFLRGPEGDANVSVGKGTLERNNTPVVGWVNMSQSTVVLATDGITSVLPGSVATVATQEDEQGDENKARGNWSSKLDFILSMVGYAVGLGNVWRFPYLAFQNGGGAFLIPYLMMLALAGLPIFFLEVSLGQFASQGPVSVWKAIPALQGCGIAMLIISVLIAIYYNVIICYTLFYLFASFVSVLPWGSCNNPWNTPECKDKTKLLLDSCVISDHPKIQIKNSTFCMTAYPNVTMVNFTSQANKTFVSGSEEYFKYFVLKISAGIEYPGEIRWPLALCLFLAWVIVYASLAKGIKTSGKVVYFTATFPYVVLVILLIRGVTLPGAGAGIWYFITPKWEKLTDATVWKDAATQIFFSLSAAWGGLITLSSYNKFHNNCYRDTLIVTCTNSATSIFAGFVIFSVIGFMANERKVNIENVADQGPGIAFVVYPEALTRLPLSPFWAIIFFLMLLTLGLDTMFATIETIVTSISDEFPKYLRTHKPVFTLGCCICFFIMGFPMITQGGIYMFQLVDTYAASYALVIIAIFELVGISYVYGLQRFCEDIEMMIGFQPNIFWKVCWAFVTPTILTFILCFSFYQWEPMTYGSYRYPNWSMVLGWLMLACSVIWIPIMFVIKMHLAPGRFIERLKLVCSPQPDWGPFLAQHRGERYKNMIDPLGTSSLGLKLPVKDLELGTQC | Function: Sodium- and chloride-dependent glycine transporter . Terminates the action of glycine by its high affinity sodium-dependent reuptake into presynaptic terminals . May be responsible for the termination of neurotransmission at strychnine-sensitive glycinergic synapses .
PTM: N-glycosylated.
Location Topology: Multi-pass membrane protein
Catalytic Activity: chloride(out) + glycine(out) + 3 Na(+)(out) = chloride(in) + glycine(in) + 3 Na(+)(in)
Sequence Mass (Da): 87434
Sequence Length: 797
Subcellular Location: Cell membrane
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P54951 | MKPRYRLAVERDAEQLLELTLRAYEPIRKLGIRFAAAHADLDLVLKNIRENACYVMEEDGRIIATITLRMPWGKQPGPYGVPHIWWFAVDPDTGKKGIGTKLLQWLEETILRDTLKVPFVSLGTADKHPWLIEMYERKGYVRSGEQDLGKGHITVYMKKQLRHDL | Function: Catalyzes the N-acetylation of S-(2-succino)cysteine. Is involved in a S-(2-succino)cysteine (2SC) degradation pathway that allows B.subtilis to grow on 2SC as a sole sulfur source, via its metabolization to cysteine. Moreover, 2SC is a toxic compound in B.subtilis at high exogenous concentrations, and this enzyme relieves 2SC toxicity via N-acetylation.
Catalytic Activity: acetyl-CoA + S-(2-succino)-L-cysteine = CoA + H(+) + N-acetyl-S-(2-succino)-L-cysteine
Sequence Mass (Da): 19125
Sequence Length: 165
Pathway: Amino-acid biosynthesis; L-cysteine biosynthesis.
EC: 2.3.1.-
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P54955 | MADKAFHTRLINMRRDLHEHPELSFQEVETTKKIRRWLEEEQIEILDVPQLKTGVIAEIKGREDGPVIAIRADIDALPIQEQTNLPFASKVDGTMHACGHDFHTASIIGTAMLLNQRRAELKGTVRFIFQPAEEIAAGARKVLEAGVLNGVSAIFGMHNKPDLPVGTIGVKEGPLMASVDRFEIVIKGKGGHAGIPNNSIDPIAAAGQIISGLQSVVSRNISSLQNAVVSITRVQAGTSWNVIPDQAEMEGTVRTFQKEARQAVPEHMRRVAEGIAAGYGAQAEFKWFPYLPSVQNDGTFLNAASEAAARLGYQTVHAEQSPGGEDFALYQEKIPGFFVWMGTNGTEEWHHPAFTLDEEALTVASQYFAELAVIVLETIK | Cofactor: Binds 2 divalent metal cations per subunit.
Function: Probably catalyzes the deacetylation of N-acetylcysteine (NAC) to acetate and cysteine. Is involved in a S-(2-succino)cysteine (2SC) degradation pathway that allows B.subtilis to grow on 2SC as a sole sulfur source, via its metabolization to cysteine.
Catalytic Activity: H2O + N-acetyl-L-cysteine = acetate + L-cysteine
Sequence Mass (Da): 41552
Sequence Length: 380
Pathway: Amino-acid biosynthesis; L-cysteine biosynthesis.
EC: 3.5.1.-
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A0QU81 | MLASVALAALAGVGTPHATADDASPLVPLVDAAAQRLQTADPVAASKFRSGGAIDDPDREQQVIAAVTGDATRHNIDPGYVHDVFRNQIDATSSVEHTRFAQWKLDPAAAPSSAPDLSESRQKIDTLNRTMVDEIARQWPVLHSPVCRPDLDRALDAVATARGFDPVYRHALEYATHSYCR | Function: Catalyzes the Claisen rearrangement of chorismate to prephenate. May play some role in the pathogenicity.
Catalytic Activity: chorismate = prephenate
Sequence Mass (Da): 19491
Sequence Length: 181
Pathway: Metabolic intermediate biosynthesis; prephenate biosynthesis; prephenate from chorismate: step 1/1.
Subcellular Location: Secreted
EC: 5.4.99.5
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P9WIB8 | MLTRPREIYLATAVSIGILLSLIAPLGPPLARADGTSQLAELVDAAAERLEVADPVAAFKWRAQLPIEDSGRVEQQLAKLGEDARSQHIDPDYVTRVFDDQIRATEAIEYSRFSDWKLNPASAPPEPPDLSASRSAIDSLNNRMLSQIWSHWSLLSAPSCAAQLDRAKRDIVRSRHLDSLYQRALTTATQSYCQALPPA | Function: Catalyzes the Claisen rearrangement of chorismate to prephenate. May play some role in the pathogenicity.
Catalytic Activity: chorismate = prephenate
Sequence Mass (Da): 21945
Sequence Length: 199
Pathway: Metabolic intermediate biosynthesis; prephenate biosynthesis; prephenate from chorismate: step 1/1.
Subcellular Location: Secreted
EC: 5.4.99.5
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Q7CHH5 | MQPTHTLTRLTVIGKLIIASSFFLSLAVQAQQCGQTAPLINERLSYMKDVAGYKAENHLPIEDRIQEEKVINSAMAQAESLGLNGESIKPLMVAQINAAKAIQYRYRADWLSQPEPGWQPKPLDDVRANIGELSTKILEQIAEELKTCKPAEMGDKAHFINTIRQHNLTSADVEAIFSTFNQVKLK | Function: Catalyzes the Claisen rearrangement of chorismate to prephenate. May play some role in the pathogenicity.
Catalytic Activity: chorismate = prephenate
Sequence Mass (Da): 20745
Sequence Length: 186
Pathway: Metabolic intermediate biosynthesis; prephenate biosynthesis; prephenate from chorismate: step 1/1.
Subcellular Location: Periplasm
EC: 5.4.99.5
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Q9VHA0 | MSGGRDSSTSSGSNSAAPGASTNATSSASASASSTSTSASPGSTTSPASTQRQRGRPAKRATCTWCGEGKLPLQYVLPTQTGKKEFCSETCIAEFRKAYSKGACTQCDNVIRDGAPNKEFCSIMCMNKHQKKNCSTRHSGGSASGKGLAESERKLLASGAPAPTGPFQYESFHVFDWDAYLEETGSEAAPAKCFKQAQNPPNNDFKIGMKLEALDPRNVTSTCIATVVGVLGSRLRLRLDGSDSQNDFWRLVDSTEIHAIGHCEKNGGMLQPPLGFRMNASSWPGYLCKILNNAMVAPEEIFQPEPPEPEENLFKVGQKLEAVDKKNPQLICCATVDAIKDDQIHVTFDGWRGAFDYWCNYRSRDIFPAGWCARSCHPMQPPGHKSRMDSSSSKQRCPRPRYTVVAESEAMVPASPATAHFHPNCKGGPFINNSKLPCMVTGPTYQTLAKLCLQEVLAASTDTQQLSKLLFALEGDVHIVTAAGKNFTVKIPSPMRMKDDESLAQFIETLCTTCRACANLISLVHETEECKKCANSRKRQLTQSATPPSSPVLADKRNRQSNSATTSPSEKIIKQELAVKSPVESKSKTSTNNGKEPASQQNSNHSLNNNNNSASKSSNKVVIKSEPNGANAQTSSTTQALRKVRFQHHANTNTNSSATNGNQDTSQTTHVSTSHCSSSSTSSSTSLAGGSANTSTIGKYLAPLVAEVHPEQANVKPSNSYYKSPTTLSSSASLPTSVSTPFTGCQSASSTALAAGGVTAAKAATAPAGAAATAGASPSYTAITSPVSTPTSALANSHLRSQPIDWTIEEVIQYIESNDNSLAVHGDLFRKHEIDGKALLLLNSEMMMKYMGLKLGPALKICNLVNKVNGRRNNLAL | Function: Polycomb group (PcG) protein. PcG proteins act by forming multiprotein complexes, which are required to maintain the transcriptionally repressive state of homeotic genes throughout development. PcG proteins are not required to initiate repression, but to maintain it during later stages of development. They probably act via the methylation of histones, rendering chromatin heritably changed in its expressibility.
Sequence Mass (Da): 93551
Sequence Length: 877
Domain: The SAM domain is essential for function.
Subcellular Location: Nucleus
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Q17QN4 | MGTLLAFVVGAALVSSAWGGCVEVDSETEAVYGMTFKILCISCKRRSETNAETFTEWTFRQKGTEEFVKILRYENEVLQLEEDERFEGRVVWNGSRGTKDLQDLSIFITNVTYNHSGDYECHVYRLLFFDNYEHNTSVVKKIHLEVVDKANRDMASIVSEIMMYVLIVVLTIWLVAEMVYCYKKIAAATEAAAQENASEYLAITSESKENCTGVQVAE | Function: Regulatory subunit of multiple voltage-gated sodium channel complexes that play important roles in excitable membranes in brain, heart and skeletal muscle. Enhances the presence of the pore-forming alpha subunit at the cell surface and modulates channel gating characteristics and the rate of channel inactivation. Modulates the activity of a variety of pore-forming alpha subunits, such as SCN1A, SCN2A, SCN3A, SCN4A, SCN5A and SCN10A.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 24711
Sequence Length: 218
Subcellular Location: Cell membrane
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Q07699 | MGRLLALVVGAALVSSACGGCVEVDSETEAVYGMTFKILCISCKRRSETNAETFTEWTFRQKGTEEFVKILRYENEVLQLEEDERFEGRVVWNGSRGTKDLQDLSIFITNVTYNHSGDYECHVYRLLFFENYEHNTSVVKKIHIEVVDKANRDMASIVSEIMMYVLIVVLTIWLVAEMIYCYKKIAAATETAAQENASEYLAITSESKENCTGVQVAE | Function: Regulatory subunit of multiple voltage-gated sodium channel complexes that play important roles in excitable membranes in brain, heart and skeletal muscle. Enhances the presence of the pore-forming alpha subunit at the cell surface and modulates channel gating characteristics and the rate of channel inactivation. Modulates the activity of multiple pore-forming alpha subunits, such as SCN1A, SCN2A, SCN3A, SCN4A, SCN5A and SCN10A.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 24707
Sequence Length: 218
Subcellular Location: Cell membrane
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P97952 | MGTLLALVVGAALVSSAWGGCVEVDSDTEAVYGMTFKILCISCKRRSETTAETFTEWTFRQKGTEEFVKILRYENEVLQLEEDERFEGRVVWNGSRGTKDLQDLSIFITNVTYNHSGDYECHVYRLLFFDNYEHNTSVVKKIHLEVVDKANRDMASIVSEIMMYVLIVVLTIWLVAEMVYCYKKIAAATEAAAQENASEYLAITSESKENCTGVQVAE | Function: Regulatory subunit of multiple voltage-gated sodium channel complexes that play important roles in excitable membranes in brain, heart and skeletal muscle. Enhances the presence of the pore-forming alpha subunit at the cell surface and modulates channel gating characteristics and the rate of channel inactivation. Modulates the activity of a variety of pore-forming alpha subunits, such as SCN1A, SCN2A, SCN3A, SCN4A, SCN5A and SCN10A.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 24650
Sequence Length: 218
Subcellular Location: Cell membrane
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D4B0Q6 | MRFTQIVAAALCLGATEAAVAPIDRARKVLGNQHAFDKRDASGDTAKAPKHLTSKNKKFYVDPNSIPGVPFDIGESYAGNLANTPAGNSSLFFWYFPSENPEAKNEITIWLNGGPGCSSMIGLLQENGPFLWQPGTDGPVKNPYAWSKLTNMVWVDQPAGTGFSPGPPTVKDEIDVANQFSDFWKNFMDTFDLHHSDVYLAGESYAGQYIPYIASGMLDRKDSEYFNVQGITIIDPSIGATEVIIDAPSVPALHRFNNIIDLNETFVNDITKKWESCGYKKFMDDALKFPPAGPMTVPGKSAGCDVWDEIIAAVKEVNPCFNIYHLRDNCPSPSNVMNGPKNFFNNKQIQEAIHAHPTDYRLCGESQIFGPHRNDRSVPSSYGPLASVIERTNNTIIAHGDLDFLLFTEGSLASIQNMTWGGLQGFQKEPSDKFYVPYKDGSEVGGAGFVGKTHRERGLTWVTVDLAGHEIPQYAPTAAYRMLEYMLGRVQSLTETH | Function: Involved in degradation of small peptides.
Catalytic Activity: Release of a C-terminal amino acid with broad specificity.
Sequence Mass (Da): 54755
Sequence Length: 497
Subcellular Location: Secreted
EC: 3.4.16.5
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D4AZG9 | MHVAILLAIISLARAAPSTKGYTVATSLPGKSAFETRRLPDAPEILKNWAGRLDIPGTTIGNSLFFWLFSAEDKAYDDNLIIWLNGGPGCSSLVGAFLENGPLRFMGNSTMPERNPYSWAKLGHVLYIDQPVGTGFASEKVPVTSNKEVISNLYSWLMSFDAIFDHILRTKKVHIVGESYAGIYIPYIASEIVKRKSELPVNLVSIAIGDGTIGPNTGMSSLGMVGFLEEYASKLRIPRDIMNAISFGDHACGFDIIRQRAKVYPPRGPFHLPGRSGSANNTEISNMLQKGVADESLGSCNIHPDTPEKIRSSIVNSTCYGHCAVFETTADYMSSQQCFSIYNINYGCNFTNPTSTLEAYFSRSDVQIALNLMHPTDPLRPFQSCNPKILETLMAPANRPVPPSFEILPDLLTTHKLPVHIYQGRLDMLINHVGIEVTIQNMTWNGAQGFQDSLHFEFGRQKDKAVGLWNEERGLSYHLFFEGGHFLPADLPMEVLSYVKEVVLRQ | Function: Involved in degradation of small peptides.
Catalytic Activity: Release of a C-terminal amino acid with broad specificity.
Sequence Mass (Da): 56016
Sequence Length: 506
Subcellular Location: Secreted
EC: 3.4.16.5
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D4ASE6 | MKGLLSLLLVGAANALAASYEPRSLTEDMLQGKEKEVWDAIKGEIPGAQLDDYFNPPTAHQREPDEKWDGKLEGKSVNTLWVEEGKDKPSGIEEYGMRFKTVDPSSLGVDNVTQYSGYLDNKKNGQHLFFWFFESRRDPQYDPVILWLNGGPGCSSMTSLFMELGPARVGQDLKLTRNPNSWNNRASIIFLDQPVNVGFSYGKSGAFNTPSASKDVFAFLTLFFKKFPQYALQDFHIAGESYAGHYIPFASYPPMACGKGGYSAVLDQPTCKAMEAAVPQCQKEIKRCYDKPTDVATCVKGAKFCKDALVRPYSRTGQSIYDIRGRCEDPKDLCYPILGWIAKYLNQRHVQKAIGAEVSHFKGCSNHISSQFFAHGDYNQPFHRKIPGILKDVNVLVYAGDADYICNWLGVKEWTEALQWPGRHIFRRKNLSVVYHSVNKWPLGRVKYHNGLAFLQVFKAGHRVPYDQPENALDFFNRWLAGEWTP | Function: Involved in degradation of small peptides.
Catalytic Activity: Release of a C-terminal amino acid with broad specificity.
Sequence Mass (Da): 54906
Sequence Length: 486
Subcellular Location: Secreted
EC: 3.4.16.5
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Q8T3G2 | MTYAESTRSAVVYSSIVPPPRTPVGPPMLKDGVRKGSASQPLQPKNGANSLDYWSKSEDEKSGITCYYSRHNIQFPPPQRKMKPVKPNPVGRSTINGFTPSTSSPQNGLRYPPFPQNTPESVMSPPVGIYRNIPAMPRAKLTKDEKNGGKMNRDGGGENPKNVVWGGTSRKDDDTASTPLNSFSANASIEKKRSTARRKPRWARCFQTLFCCVTPPREIEKIQSSQRTNSTNNNHQNGRPSTPTNTGPPIQLITQVHRDGTVTGLPTTGQACQQNGSGDGVTPYDKIANDSVGTINEKPLLPPLLPQDSNKKCLVIDLDETLVHSSFKPVKNPDFVIPVEIDGVEHQVYVLKRPYVDEFLAKVGEHFECILFTASLAKYADPVADLLDKKRVFRGRLFREACVFHKGNYVKDLSRLGRNLNQTLIIDNSPASYAFHPENAVPVTTWFDDPSDTELLDILPSLEHLNGFSSIYDLYRPEEGPQSELLNHCSC | Cofactor: May also use Mn(2+).
Function: Phosphatase which may play a role in the egg laying muscles.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 54372
Sequence Length: 491
Subcellular Location: Cytoplasm
EC: 3.1.3.16
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Q54DY7 | MMKLLFIIISIIFVINVSNSTPTLQLSGYFNVNETTNANLFYLFYESQNSPSTDPLILWLTGGPGCSSLMAAFYENGPYFVNDNLTLSENPNSWNMVANVLYVDSPLGAGFSYVVDSDGYSTTETEISENLYSFLTQFLSKYPKYSKLPLYIFGESYAGHYVPSFSYYIYQKNLGLATINLKGLAIGNGMVDPYIQYGSLGPFAYAHGMLDINALKETEGLYESCQQAIDSGDYNMTTQICNNIMDIVQEYAGNFNVYDVSKTCYPNEPLCYNFTAIIDYLNLASTKQSFGVLPNSTWNVCSTQPYSAIIRDWFNTPINYIPTLLENYKVLVYNGNYDWICNFLGSTEWTSQLKWKYNQEFNNSPRKILYINGNTISGYSQSYDNLTMQVLLGASHMAPREAPVAALAMVESFIQN | Function: Probable carboxypeptidase.
Sequence Mass (Da): 46858
Sequence Length: 416
Subcellular Location: Secreted
EC: 3.4.16.-
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Q54VW1 | MNIKIILLSIILIIQLLLLNNNGGIVESKINFSKRKQTDRKPNPSPKTYTKEYYDNKYLKSLKNVKQTPNDFLVTDLPGLDNGILTSFSGLLTTNETSDGNLFFWFFPANETVINPMDAPLLVWLNGGPGCSSMDSVFIETGPLRFIGDSDNSDKFYINPWSWHNSANMLYIDQPFGTGLSFVSDNDGLVTNDLEINQNFYQFIQEFFQIFSNYSTLPFFISGESYAGHYIPHMASYILNMNENLSKDSIKINLQGVAIGNGYTHPTTQINSYREFGYYATGIIGQRQYNNYENLNNLCQEQLSQGNYNSDECANVFNTLLDDSGSSNTSQVNMYDYRLNDPTAGNNWPLPGINQEFVYLNRDDVRSAIHATVTPHQWNECNDTVNGLLTNQDESSLYLFPELLSNIRVLIYNGQFDVICNHVGTTEYLNQIEWDYTQEWSDAPRFTWTSVGTDGSLQSGGYGKTAANLTFVLALGGSHMYPMNMPSTSFDMITRFLKNKSFNDLPQSIGIDAPSTPKPVPLTLGAWIGITVGGCAFGFLVGGLIIYIIMKKSSKNGYYKVIQ | Function: Probable carboxypeptidase.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 63223
Sequence Length: 563
Subcellular Location: Membrane
EC: 3.4.16.-
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A0A194XJW1 | MATLIRLLRLLPVASSSAVLMFALDEHLIFGTWVQPSIRERANANLPAWWTRGGLRWRWVLIIFYPVNYILGILNLFISQDQLQDTGASKWYTLGLLFSIAHMFYLFRALKLIAAIENDEPKGNVTYSMGRWLKMNWTRALLTDLPAWLCFIAAALKAL | Function: Probable epoxidase; part of the gene scp cluster that mediates the biosynthesis of a hirsutellone-like compound that has still to be identified.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 18272
Sequence Length: 159
Pathway: Mycotoxin biosynthesis.
Subcellular Location: Membrane
EC: 1.14.-.-
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P09892 | METSVSRVTVSLTLLVLIICSADAMNYLAFPRMGRARPGYLAFPRMGRSQMKTETGTDCCGLGMKSEFVIGQEGKEELRHGACSSSVACCAGLREIVDQKQDGVFFSMCVPDFVASRSSEESSSEVLSKLKSLLQK | Function: Involved in the stimulation of contractile activity in the gut, the increase of the amplitude of the heart beat, and enhancement of the contractile response of the radula closer muscle.
PTM: Contains three disulfide bonds.
Sequence Mass (Da): 14773
Sequence Length: 136
Subcellular Location: Secreted
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Q06114 | MSALITHDRSTPVTGSLLPYVETPAPAPLQTQQVAGELKDKNGGVSSQGVQLPAPLAVVASQVTEGQQQEVTKLLESVTRGAAGSQLISNYVSVLTKFTLASPDTFEIELGKLVSNLEEVRKDIKIADIQRLHEQNMKKIEENQEKIKETEENAKQVKKSGIASKIFGWLSAIASVIVGAIMVASGVGAVAGAMMVASGVIGMANMAVKQAAEDGLISQEAMKILGPILTAIEVALTVVSTVMTFGGSALKCLANIGAKLGANTASLAAKGAEFSAKVAQISTGISNTVGSAVTKLGGSFAGLTMSHAIRTGSQATQVAVGVGSGITQTINNKKQADLQHNNADLALNKADMAALQSIIDRLKEELSHLSESHQQVMELIFQMINAKGDMLHNLAGRPHTV | Function: Component of the type III secretion system (T3SS), also called injectisome, which is used to inject bacterial effector proteins into eukaryotic host cells . YopB/SctE and YopD/SctB are inserted into the host membrane where they form a pore and allow the translocation of effector proteins into the cytosol of target cells . Is an essential virulence determinant . Required for YopE and YopH translocation . Shows membrane disruptive activity in vitro .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 41795
Sequence Length: 401
Subcellular Location: Secreted
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P41784 | MATPWSGYLDDVSAKFDTGVDNLQTQVTEALDKLAAKPSDPALLAAYQSKLSEYNLYRNAQSNTVKVFKDIDAAIIQNFR | Function: Component of the type III secretion system (T3SS), also called injectisome, which is used to inject bacterial effector proteins into eukaryotic host cells . PrgI/SctF1 forms the external needle filament that protrudes from the bacterial surface . Is probably involved in the transduction of an activating signal, thought to be mediated by the distal tip of the needle filament, to the secretion machine . Required for invasion of epithelial cells . Required for the secretion of the effector protein SptP .
Sequence Mass (Da): 8857
Sequence Length: 80
Domain: Deletion of the last five residues prevents self-association and yields monomeric proteins that allow biophysical studies . Forms a right-handed helical assembly with roughly 11 subunits per two turns . The location of the negatively charged surfaces are radically different among the needle filament proteins PrgI, BsaL and MxiH . In PrgI, the major negatively charged surface is not on the 'face' but instead is on the 'side' of the two-helix bundle, and only residues from helix alpha1 contribute to this negative region . The insertion of the needle tip complex on the distal end of the filament results in significant conformational changes in PrgI/SctF .
Subcellular Location: Secreted
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P95434 | MAQIFNPNPGNTLDTVANALKEQANAANKDVNDAIKALQGTDNADNPALLAELQHKINKWSVIYNINSTVTRALRDLMQGILQKI | Function: Component of the type III secretion system (T3SS), also called injectisome, which is used to inject bacterial effector proteins into eukaryotic host cells, facilitating the establishment and dissemination of infection. PscF/SctF forms the external needle filament that protrudes from the bacterial surface.
Sequence Mass (Da): 9285
Sequence Length: 85
Domain: The N-terminal part (1-11) is species-specific and essential for export/assembly and the function of needle.
Subcellular Location: Secreted
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P0A223 | MSVTVPNDDWTLSSLSETFDDGTQTLQGELTLALDKLAKNPSNPQLLAEYQSKLSEYTLYRNAQSNTVKVIKDVDAAIIQNFR | Function: Component of the type III secretion system (T3SS), also called injectisome, which is used to inject bacterial effector proteins into eukaryotic host cells . MxiH/SctF forms the external needle filament that protrudes from the bacterial surface .
Sequence Mass (Da): 9265
Sequence Length: 83
Domain: The helical filament defines an inner channel with about 20 Angstroms diameter and has an outer diameter of approximately 70 Angstroms . Deletion of the last five residues prevents self-association and yields monomeric proteins that allow biophysical studies .
Subcellular Location: Secreted
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O68691 | MSNFSGFTKGTDIADLDAVAQTLKKPADDANKAVNDSIAALKDKPDNPALLADLQHSINKWSVIYNINSTIVRSMKDLMQGILQKFP | Function: Component of the type III secretion system (T3SS), also called injectisome, which is used to inject bacterial effector proteins into eukaryotic host cells . YscF/SctF forms the external needle filament that protrudes from the bacterial surface . Essential for the calcium-dependent regulation of T3SS and Yop secretion . Required to block Yop secretion in the presence of extracellular calcium . May be the extracellular T3SS component that senses extracellular calcium and/or participates in transmitting the calcium signal to the cytoplasmic compartment where the block in secretion is initiated .
Sequence Mass (Da): 9490
Sequence Length: 87
Domain: Contains an N-terminal secretion signal that is required for secretion.
Subcellular Location: Secreted
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E1WAE4 | MKKFYSCLPVFLLIGCAQVPLPSSVSKPVQQPGAQKEQLANANSIDECQSLPYVPSDLAKNKSLSNHNADNSASKNSAISSSIFCEKYKQTKEQALTFFQEHPQYMRSKEDEEQLMTEFKKVLLEPGSKNLSIYQTLLAAHERLQAL | Function: Involved in the synthesis of the type III secretion system (T3SS), also called injectisome, which is used to inject bacterial effector proteins into eukaryotic host cells (By similarity). Pilot protein that is required for the proper localization of the secretin InvG/SctC in the outer membrane (By similarity). Necessary for efficient adherence and entry of these organisms into cultured epithelial cells .
Location Topology: Lipid-anchor
Sequence Mass (Da): 16455
Sequence Length: 147
Subcellular Location: Cell outer membrane
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P0A1X2 | MIRHGSNKLKIFILSILLLTLSGCALKSSSNSEKEWHIVPVSKDYFSIPNDLLWSFNTTNKSINVYSKCISGKAVYSFNAGKFMGNFNVKEVDGCFMDAQKIAIDKLFSMLKDGVVLKGNKINDTILIEKDGEVKLKLIRGI | Function: Involved in the synthesis of the type III secretion system (T3SS), also called injectisome, which is used to inject bacterial effector proteins into eukaryotic host cells . Pilot protein that is required for the proper localization of the secretin MxiD/SctC in the outer membrane . Also influences both MxiD/SctC multimerization and stability . Required for both Ipa translocation and tissue culture cell invasion . Binds lipids .
Location Topology: Lipid-anchor
Sequence Mass (Da): 15853
Sequence Length: 142
Subcellular Location: Cell outer membrane
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Q56851 | MSRIIALIISFLLVGCATPPMPAQRIVGEVRMSRPLSRTAHIDVSIFGLYEGKVREVQRTRFETGNLPLFFSIKLNPAQRGEGELYLRSTLSFPERGVQAVAQQKLIGKNKVVLQMIPKTCYPNCQSPNTR | Function: Involved in the synthesis of the type III secretion system (T3SS), also called injectisome, which is used to inject bacterial effector proteins into eukaryotic host cells . Pilot protein that is required for the proper localization of the secretin YscC/SctC in the outer membrane . Also required for efficient oligomerization of YscC/SctC and stabilization of the oligomers .
Location Topology: Lipid-anchor
Sequence Mass (Da): 14687
Sequence Length: 131
Subcellular Location: Cell outer membrane
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P84693 | MKAIIFFIGCLMLIDLVAGSRSGYPVTQKGCVYSCFWGSNWWCNAECTALGGSSGYCAWPSCWCYSLPDNRNIWGSYPNNCGKK | Function: Beta toxins bind voltage-independently at site-4 of sodium channels (Nav) and shift the voltage of activation toward more negative potentials thereby affecting sodium channel activation and promoting spontaneous and repetitive firing.
Sequence Mass (Da): 9310
Sequence Length: 84
Domain: Has the structural arrangement of an alpha-helix connected to antiparallel beta-sheets by disulfide bonds (CS-alpha/beta).
Subcellular Location: Secreted
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P46115 | KKDGYPVEGDNCAFACFGYDNAYCDKLCKDKKADDGYCVWSPDCYCYGLPEHILKEPTKTSGRC | Function: Alpha toxins bind voltage-independently at site-3 of sodium channels (Nav) and inhibit the inactivation of the activated channels, thereby blocking neuronal transmission. By extending the depolarized period it indirectly affects beta-cell voltage-dependent potassium channels, thus increasing potassium permeability.
Sequence Mass (Da): 7200
Sequence Length: 64
Domain: Has the structural arrangement of an alpha-helix connected to antiparallel beta-sheets by disulfide bonds (CS-alpha/beta).
Subcellular Location: Secreted
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P56743 | GRDGYVVKNGTNCKYSCEIGSEYEYCGPLCKRKNAKTGYCYAFACWCIDVPDDVKLYGDDGTYCSS | Function: Beta toxins bind voltage-independently at site-4 of sodium channels and shift the voltage of activation toward more negative potentials thereby affecting sodium channel activation and promoting spontaneous and repetitive firing. This toxin is active only on insects (By similarity). This toxin has very low anti-insect activity.
PTM: N-glycans are core-fucosylated, heterogeneous and short which could be the result of extensive trimming.
Sequence Mass (Da): 7348
Sequence Length: 66
Domain: Has the structural arrangement of an alpha-helix connected to antiparallel beta-sheets by disulfide bonds (CS-alpha/beta).
Subcellular Location: Secreted
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M1INJ1 | VRDGYIRRKDEFKFKCYVDGKDCDDVCKSEGGSAGYCTALGFLCYCAGLPDDKAWKPTSS | Function: Depressant insect toxins cause a transient contraction paralysis followed by a slow flaccid paralysis. They bind voltage-independently to sodium channels (Nav) and block action potentials, primarily by depolarizing the axonal membrane and suppressing the sodium current.
Sequence Mass (Da): 6640
Sequence Length: 60
Domain: Has the structural arrangement of an alpha-helix connected to antiparallel beta-sheets by disulfide bonds (CS-alpha/beta).
Subcellular Location: Secreted
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P0DUH8 | MKTFVLALCLVLIGMVYAKDGYLVSKHTGCKLGCSPKIGDRYCHIECTSMNHKGDEGYCYWLACYCKGMPENAEVYPLPNKSCGK | Function: Beta toxins bind voltage-independently at site-4 of sodium channels (Nav) and shift the voltage of activation toward more negative potentials thereby affecting sodium channel activation and promoting spontaneous and repetitive firing.
Sequence Mass (Da): 9450
Sequence Length: 85
Domain: Has the structural arrangement of an alpha-helix connected to antiparallel beta-sheets by disulfide bonds (CS-alpha/beta).
Subcellular Location: Secreted
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P84685 | MSIFPIILALLLIGLDEGEALDGYPLSKNNYCKIYCPDEKVCKWSCKHRAGATNGKGDCINKGCYCYDVAPGTEMYPGRLPCNPY | Function: Beta toxins bind voltage-independently at site-4 of sodium channels (Nav) and shift the voltage of activation toward more negative potentials thereby affecting sodium channel activation and promoting spontaneous and repetitive firing.
Sequence Mass (Da): 9385
Sequence Length: 85
Domain: Has the structural arrangement of an alpha-helix connected to antiparallel beta-sheets by disulfide bonds (CS-alpha/beta).
Subcellular Location: Secreted
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P49416 | MPLPRAAFLLGLLLAAAAAESVRETETMDARWLDNVGSGDLPDDEDIGEFTPHLTSDEFDIDDTSGSGDYSDYDDAIYLTTVDTPAISDNYIPGDTERKMEGEKKNTMLDNEIIPDKASPVEANLSNKISMASTANSSIFERTEVLTALIAGGAVGLLFAVFLILLLVYRMKKKDEGSYDLGKKPIYKKAPTNEFYA | Function: Cell surface proteoglycan which regulates exosome biogenesis in concert with SDCBP and PDCD6IP.
PTM: O-glycosylated; contains both chondroitin sulfate and heparan sulfate. Ser-38, Ser-65 and Ser-67 can all be modified by either chondroitin sulfate or heparan sulfate, and the protein exists in forms that contain only chondroitin sulfate, only heparan sulfate and both chondroitin sulfate and heparan sulfate.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 21502
Sequence Length: 197
Subcellular Location: Membrane
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P31431 | MAPARLFALLLFFVGGVAESIRETEVIDPQDLLEGRYFSGALPDDEDVVGPGQESDDFELSGSGDLDDLEDSMIGPEVVHPLVPLDNHIPERAGSGSQVPTEPKKLEENEVIPKRISPVEESEDVSNKVSMSSTVQGSNIFERTEVLAALIVGGIVGILFAVFLILLLMYRMKKKDEGSYDLGKKPIYKKAPTNEFYA | Function: Cell surface proteoglycan which regulates exosome biogenesis in concert with SDCBP and PDCD6IP .
PTM: Shedding is enhanced by a number of factors such as heparanase, thrombin or EGF. Also by stress and wound healing. PMA-mediated shedding is inhibited by TIMP3.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 21642
Sequence Length: 198
Subcellular Location: Membrane
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Q8HZJ6 | MASPRLLALLLLLVGAFNAAAAESIRETEVINPQDLLEGRYFSGDLPDDEDVGGPGQEPDDFEWSGSGDLEGPEDKHMLPEVTHPLVPLDNHIPERTGPGGRVPTEPKELEENEVIPKRMSPFDGDEDVSNKVSMSSTAQGSNIFERTEVLSALIVGGIVGILFAVFLVLLLVYRMKKKDEGSYDLGKKPIYKKAPTNEFYA | Function: Cell surface proteoglycan which regulates exosome biogenesis in concert with SDCBP and PDCD6IP.
PTM: Shedding, cleavage of the extracellular domain to release a soluble form, is enhanced by a number of factors such as heparanase, growth factor receptor action for example by thrombin or EGF. Physiological events such as stress or wound healing can activate the shedding. PMA-mediated shedding is inhibited by TIMP3 (By similarity).
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 22081
Sequence Length: 202
Subcellular Location: Membrane
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O00560 | MSLYPSLEDLKVDKVIQAQTAFSANPANPAILSEASAPIPHDGNLYPRLYPELSQYMGLSLNEEEIRANVAVVSGAPLQGQLVARPSSINYMVAPVTGNDVGIRRAEIKQGIREVILCKDQDGKIGLRLKSIDNGIFVQLVQANSPASLVGLRFGDQVLQINGENCAGWSSDKAHKVLKQAFGEKITMTIRDRPFERTITMHKDSTGHVGFIFKNGKITSIVKDSSAARNGLLTEHNICEINGQNVIGLKDSQIADILSTSGTVVTITIMPAFIFEHIIKRMAPSIMKSLMDHTIPEV | Function: Multifunctional adapter protein involved in diverse array of functions including trafficking of transmembrane proteins, neuro and immunomodulation, exosome biogenesis, and tumorigenesis . Positively regulates TGFB1-mediated SMAD2/3 activation and TGFB1-induced epithelial-to-mesenchymal transition (EMT) and cell migration in various cell types. May increase TGFB1 signaling by enhancing cell-surface expression of TGFR1 by preventing the interaction between TGFR1 and CAV1 and subsequent CAV1-dependent internalization and degradation of TGFR1 . In concert with SDC1/4 and PDCD6IP, regulates exosome biogenesis . Regulates migration, growth, proliferation, and cell cycle progression in a variety of cancer types . In adherens junctions may function to couple syndecans to cytoskeletal proteins or signaling components. Seems to couple transcription factor SOX4 to the IL-5 receptor (IL5RA) . May also play a role in vesicular trafficking . Seems to be required for the targeting of TGFA to the cell surface in the early secretory pathway .
PTM: Phosphorylated on tyrosine residues.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 32444
Sequence Length: 298
Subcellular Location: Cell junction
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O08992 | MSLYPSLEDLKVDKVIQAQTAYSANPASQAFVLVDASAALPPDGNLYPKLYPELSQYMGLSLNEAEICESMPMVSGAPAQGQLVARPSSVNYMVAPVTGNDAGIRRAEIKQGIREVILCKDQDGKIGLRLKSIDNGIFVQLVQANSPASLVGLRFGDQVLQINGENCAGWSSDKAHKVLKQAFGEKITMTIRDRPFERTVTMHKDSSGHVGFIFKSGKITSIVKDSSAARNGLLTDHHICEINGQNVIGLKDAQIADILSTAGTVVTITIMPTFIFEHIIKRMAPSIMKSLMDHTIPEV | Function: Multifunctional adapter protein involved in diverse array of functions including trafficking of transmembrane proteins, neuro and immunomodulation, exosome biogenesis, and tumorigenesis. Positively regulates TGFB1-mediated SMAD2/3 activation and TGFB1-induced epithelial-to-mesenchymal transition (EMT) and cell migration in various cell types. May increase TGFB1 signaling by enhancing cell-surface expression of TGFR1 by preventing the interaction between TGFR1 and CAV1 and subsequent CAV1-dependent internalization and degradation of TGFR1. In concert with SDC1/4 and PDCD6IP, regulates exosome biogenesis (By similarity). Regulates migration, growth, proliferation, and cell cycle progression in a variety of cancer types . In adherens junctions may function to couple syndecans to cytoskeletal proteins or signaling components. Seems to couple transcription factor SOX4 to the IL-5 receptor (IL5RA). May also play a role in vesicular trafficking. Seems to be required for the targeting of TGFA to the cell surface in the early secretory pathway (By similarity).
PTM: Phosphorylated on tyrosine residues.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 32379
Sequence Length: 299
Subcellular Location: Cell junction
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Q9H190 | MSSLYPSLEDLKVDQAIQAQVRASPKMPALPVQATAISPPPVLYPNLAELENYMGLSLSSQEVQESLLQIPEGDSTAVSGPGPGQMVAPVTGYSLGVRRAEIKPGVREIHLCKDERGKTGLRLRKVDQGLFVQLVQANTPASLVGLRFGDQLLQIDGRDCAGWSSHKAHQVVKKASGDKIVVVVRDRPFQRTVTMHKDSMGHVGFVIKKGKIVSLVKGSSAARNGLLTNHYVCEVDGQNVIGLKDKKIMEILATAGNVVTLTIIPSVIYEHMVKKLPPVLLHHTMDHSIPDA | Function: Binds phosphatidylinositol 4,5-bisphosphate (PIP2). May play a role in the organization of nuclear PIP2, cell division and cell survival .
Sequence Mass (Da): 31594
Sequence Length: 292
Domain: Binds phosphatidylinositol 4,5-bisphosphate (PIP2) via its two PDZ domains. These domains target SDCBP2 to the plasma membranes and nucleoli, two PIP2-rich regions.
Subcellular Location: Cytoplasm
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C8VPE5 | MATVSELCCAALNTSIGNRIAFPGSTAYNESLSSYFGVNAQLPPSCFVLPLSAQDVSVAVQTLTSQPDPCFFAIRSGGHTTSLGASAIEAGVTMDLSGMNTTTYDSSTNTAFIQPGARWGSVYETLLRDNVLVPGGRTASVGVGGYLTGGRNSFHAARVGLACLSIKGYEIVLADGEVAKVDQDSHPNLFRALKGGSNNFGIVTLFDMEAFSTEGTIWGGTVLYDISTKDQYIAAGTAFTDNIPNDPYASWVGMFAYNSTTDQTAIFTSLAYTRPVQSWPQAFSEFYAIPNITHTLRSATVLDLAVENSFPYGYRNVLQTGTYSNNAEIIQKAVIILNNQVKMAKLRARGKDYALFAIVQPWVPLFWEHSEARGGDVLGLERFETNLLNIAWDYSWDNSADDELLYELAQSAREQLDEYARSTGAYNEYIYLNYAGRTQDPLRGYGLENLEFLRRVSEKFDPDGVFQRLVRGGFKIDRA | Function: FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of the polyenes aspernidgulenes . The carbon backbone of aspernidgulenes is synthesized by the HR-PKS sdgA, which accepts acetyl-CoA as the starter unit and performs malonyl-CoA extensions as well as regioselective methylation and reduction . The resulting nonaketide offloads the HR-PKS by intramolecular lactonization to yield the 5,6-dihydro-alpha-pyrone-containing hexaenoic acids preaspernidgulene A1 and A2 . The FAD-dependent monooxygenase sdgC then installs the first epoxide on the penultimate double bond . Subsequently, the FAD-dependent monooxygenase sdgF presumably generates a ketone intermediate through Meinwald rearrangement involving a hydride shift . Next, sdgC introduces another epoxide on the last olefin of the ketone intermediate after E/Z isomerization . The epoxide hydrolase sdgD then catalyzes stereospecific cyclization of the 5,6-dihydro-alpha-pyrone and opening of the epoxide ring to form an oxygenated trimethylcyclopentanone and an oxabicyclo[2.2.1]heptane unit . Finally, the bicyclic unit undergoes hydrolytic cleavage, either spontaneously or catalyzed by sdgD, to assemble the dimethyl-gamma-lactone moiety in aspernidgulene A1 .
Sequence Mass (Da): 52411
Sequence Length: 479
Pathway: Secondary metabolite biosynthesis.
EC: 1.-.-.-
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Q2FWY4 | MAYFNQHQSMISKRYLTFFSKSKKKKPFSAGQLIGLILGPLLFLLTLLFFHPQDLPWKGVYVLAITLWIATWWITEAIPIAATSLLPIVLLPLGHILTPEQVSSEYGNDIIFLFLGGFILAIAMERWNLHTRVALTIINLIGASTSKILLGFMVATGFLSMFVSNTAAVMIMIPIGLAIIKEAHDLQEANTNQTSIQKFEKSLVLAIGYAGTIGGLGTLIGTPPLIILKGQYMQHFGHEISFAKWMIVGIPTVIVLLGITWLYLRYVAFRHDLKYLPGGQTLIKQKLDELGKMKYEEKVVQTIFVLASLLWITREFLLKKWEVTSSVADGTIAIFISILLFIIPAKNTEKHRRIIDWEVAKELPWGVLILFGGGLALAKGISESGLAKWLGEQLKSLNGVSPILIVIVITIFVLFLTEVTSNTATATMILPILATLSVAVGVHPLLLMAPAAMAANCAYMLPVGTPPNAIIFGSGKISIKQMASVGFWVNLISAIIIILVVYYVMPIVLGIDINQPLPLK | Function: Mediates the transport of the dicarboxylates fumarate, malate, and succinate across the cytoplasmic membrane via a Na(+)-electrochemical gradient.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 57172
Sequence Length: 520
Subcellular Location: Cell membrane
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Q9KI13 | MIKKNNLLTKKKPIANKSNKYAIRKFTVGTASIVIGAALLFGLGHNEAKAEENTVQDVKDSNMDDELSDSNDQSSNEEKNDVINNSQSINTDDDNQIKKEETNSNDAIENRSKDITQSTTNVDENEATFLQKTPQDNTQLKEEVVKEPSSVESSNSSMDTAQQPSHTTINSEASIQTSDNEENSRVSDFANSKIIESNTESNKEENTIEQPNKVREDSITSQPSSYKNIDEKISNQDELLNLPINEYENKVRPLSTTSAQPSSKRVTVNQLAAEQGSNVNHLIKVTDQSITEGYDDSDGIIKAHDAENLIYDVTFEVDDKVKSGDTMTVNIDKNTVPSDLTDSFAIPKIKDNSGEIIATGTYDNTNKQITYTFTDYVDKYENIKAHLKLTSYIDKSKVPNNNTKLDVEYKTALSSVNKTITVEYQKPNENRTANLQSMFTNIDTKNHTVEQTIYINPLRYSAKETNVNISGNGDEGSTIIDDSTIIKVYKVGDNQNLPDSNRIYDYSEYEDVTNDDYAQLGNNNDVNINFGNIDSPYIIKVISKYDPNKDDYTTIQQTVTMQTTINEYTGEFRTASYDNTIAFSTSSGQGQGDLPPEKTYKIGDYVWEDVDKDGIQNTNDNEKPLSNVLVTLTYPDGTSKSVRTDEEGKYQFDGLKNGLTYKITFETPEGYTPTLKHSGTNPALDSEGNSVWVTINGQDDMTIDSGFYQTPKYSLGNYVWYDTNKDGIQGDDEKGISGVKVTLKDENGNIISTTTTDENGKYQFDNLNSGNYIVHFDKPSGMTQTTTDSGDDDEQDADGEEVHVTITDHDDFSIDNGYYDDDSDSDSDSDSDSDDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSGLDNSSDKNTKDKLPDTGANEDHDSKGTLLGALFAGLGALLLGKRRKNRKNKN | Function: Binds to the N-terminus of the B beta-chain of human fibrinogen and thereby interferes with thrombin cleavage and release of fibrinopeptide B, thus interfering with fibrin clot formation. This may hinder host defense against microbial infections.
Location Topology: Peptidoglycan-anchor
Sequence Mass (Da): 102956
Sequence Length: 931
Subcellular Location: Secreted
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Q99S97 | MRLKSIITVIALILIMFMSAIESSIISLALPTIKQDLNAGNLISLIFTAYFIALVIANPIVGELLSRFKIIYVAIAGLLLFSIGSFMCGLSTNFTMLIISRVIQGFGSGVLMSLSQIVPKLAFEIPLRYKIMGIVGSVWGISSIIGPLLGGGILEFATWHWLFYINIPIAIIAIILVIWTFHFPEEETVAKSKFDTKGLTLFYVFIGLIMFALLNQQLLLLNFLSFILAIVVAMCLFKVEKHVSSPFLPVVEFNRSITLVFITDLLTAICLMGFNLYIPVYLQEQLGLSPLQSGLVIFPLSVAWITLNFNLHRIEAKLSRKVIYLLSFTLLLVSSIIISFGIKLPVLIAFVLILAGLSFGYIYTKDSVIVQEETSPLQMKKMMSFYGLTKNLGASIGSTIMGYLYAIQSGIFGPNLHNVLSAVAVISIGLIVLWVVFFKEQSSQSKE | Function: Energy-dependent drug efflux pump that increases resistance to antimicrobial agents such as norfloxacin, acriflavine and ethidium bromide.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 49410
Sequence Length: 447
Subcellular Location: Cell membrane
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Q6CEE9 | MPAPATYATGLTPLPTPVPKVSKNIMERFSLKGKVASITGSSSGIGFAVAEAFAQAGADVAIWYNSKPSDEKAEYLSKTYGVRSKAYKCAVTNAKQVETTIQTIEKDFGKIDIFIANAGIPWTAGPMIDVPNNEEWDKVVDLDLNGAYYCAKYAGQIFKKQGYGSFIFTASMSGHIVNIPQMQACYNAAKCAVLHLSRSLAVEWAGFARCNTVSPGYMATEISDFIPRDTKEKWWQLIPMGREGDPSELAGAYIYLASDASTYTTGADILVDGGYCCP | Function: Versatile oxidoreductase that catalyzes the oxidation and reduction of polar as well as non-polar substrates at a very broad pH range. Preferentially oxidizes secondary alcohols. Has highest activity for racemic 2-heptanol and racemic octanol. Is also an efficient reductase for selected substrates. Substrate selectivity was found for medium chain length ketones with the carbonyl function at position C-2. Has highest activities for ribulose and fructose. The enzyme is (R)-selective in the reduction direction and produces exclusively the (R)-enantiomer.
Catalytic Activity: D-mannitol + NADP(+) = D-fructose + H(+) + NADPH
Sequence Mass (Da): 30033
Sequence Length: 278
EC: 1.1.1.138
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D5GNC3 | MDALGLSKLRHLKPRQLLSQVLNFALILSTAFMLWKGLSVATDSPSPIVVVLSGSMEPAFQRGDLLFLWNRNLELDSPPTPGTRVGEIVVYNVIGKDIPIVHRVVRKHQGPKTPLHLLTKGDNNHADDTELYARGRWYLDREKEVIGSVVGYVPFVGYVTIMLSEHPWMKTALLGIMGLLVIVQRE | Function: Catalytic component of the signal peptidase complex (SPC) which catalyzes the cleavage of N-terminal signal sequences from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum (By similarity). Specifically cleaves N-terminal signal peptides that contain a hydrophobic alpha-helix (h-region) shorter than 18-20 amino acids (By similarity).
Catalytic Activity: Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 20817
Sequence Length: 186
Domain: The C-terminal short (CTS) helix is essential for catalytic activity. It may be accommodated as a transmembrane helix in the thinned membrane environment of the complex, similarly to the signal peptide in the complex substrates.
Subcellular Location: Endoplasmic reticulum membrane
EC: 3.4.21.89
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C5E3W1 | MNLRLELTRFLKLCFVLSSAFMFWKGLSIATNSHSPIVVVLSGSMEPAFQRGDVLFLWNRNERSKVGDVVIYEVQDKSIPIVHRVLREHHNDKNKQLLLTKGDNNAGDDIPLYGRKKIYLQKERDIVGTVKGYVPQLGYVTIWISENKYAKLALMGFLGISALLSNE | Function: Catalytic component of the signal peptidase complex (SPC) which catalyzes the cleavage of N-terminal signal sequences from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum (By similarity). Specifically cleaves N-terminal signal peptides that contain a hydrophobic alpha-helix (h-region) shorter than 18-20 amino acids (By similarity).
Catalytic Activity: Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 19009
Sequence Length: 167
Domain: The C-terminal short (CTS) helix is essential for catalytic activity. It may be accommodated as a transmembrane helix in the thinned membrane environment of the complex, similarly to the signal peptide in the complex substrates.
Subcellular Location: Endoplasmic reticulum membrane
EC: 3.4.21.89
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Q6FIY2 | MKFHTKLYKVGYPLYGAKFVCDDQFVVTGGGGEGNNGVDNKLTVLKVGSSEGNGLRVDEVCDATLPANDDSPTALDAVGDTILIGCNENSAKVKSGAGNSHVRKFRYDGKSLKFESAADIDKSTNPEDYTKVIRLSKDGSEAAIASSKNPPSMAIIDPRNYSVKYEIETGRDVKDLHFSPNGKLIGYITESSLEIISTVTGSCVVRKTDFDRKIILSKMKFLDDNNVLIAATWASSKGILLTKISIKSGKTTVFWSRQISSKFKGITAMDVNDQMNLVMLATNDNSVLLVKLRNLSVGKTFTQVHGFAITRVIFSPDSRYAVSISAAETVHVIEIPSDFADSRSLSESTTQWLMNTIMVLFLAFVLNSMYKEDMHKNVLNYFRSVKSIDSSSILSMEDMEQVTLVGTISTSVRSTTQRFESSKSVSSTSVVARTNVSEKERSQQDPVKKSPEQHQQNQQ | Function: Guanine nucleotide-exchange factor (GEF) required for the formation or budding of transport vesicles from the ER. This function involves the cytoplasmic domain of the protein, which is thought to interact with the small GTP-binding protein SAR1. Required for autophagy (By similarity).
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 50383
Sequence Length: 459
Subcellular Location: Endoplasmic reticulum membrane
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P11655 | MKFVTASYNVGYPAYGAKFLNNDTLLVAGGGGEGNNGIPNKLTVLRVDPTKDTEKEQFHILSEFALEDNDDSPTAIDASKGIILVGCNENSTKITQGKGNKHLRKFKYDKVNDQLEFLTSVDFDASTNADDYTKLVYISREGTVAAIASSKVPAIMRIIDPSDLTEKFEIETRGEVKDLHFSTDGKVVAYITGSSLEVISTVTGSCIARKTDFDKNWSLSKINFIADDTVLIAASLKKGKGIVLTKISIKSGNTSVLRSKQVTNRFKGITSMDVDMKGELAVLASNDNSIALVKLKDLSMSKIFKQAHSFAITEVTISPDSTYVASVSAANTIHIIKLPLNYANYTSMKQKISKFFTNFILIVLLSYILQFSYKHNLHSMLFNYAKDNFLTKRDTISSPYVVDEDLHQTTLFGNHGTKTSVPSVDSIKVHGVHETSSVNGTEVLCTESNIINTGGAEFEITNATFREIDDA | Function: Guanine nucleotide-exchange factor (GEF) required for the formation or budding of transport vesicles from the ER. This function involves the cytoplasmic domain of the protein, which is thought to interact with the small GTP-binding protein SAR1. Required for autophagy.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 51608
Sequence Length: 471
Subcellular Location: Endoplasmic reticulum membrane
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Q75BS2 | MVTITNAHTELIHDAVLDYYGKRLATCSSDKTIQIFEVDGDSHKLVDSLHGHEGPVWQVDWAHPKFGVILASCSYDGKVLIWKEENGRWSQIAAYEVHSASVNSVKWAPHEYGPLLLCSSSDGKFSVVEFKENGTTSPIIIDAHAIGVNAACWAPATIEDDGQQSQHLRRIATGGADNLVKIWKYNPEANTYLLEDTLAAHADWVRDVAWSPSVLPRAYLATVSQDRTCIIWTQENNQGPWTKTLLKEDKFPDVLWRASWSLSGNILALSGGDNKVTLWKENLEGKWESAAEIEQ | Function: Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules. It also functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. SEC13 is required for efficient mRNA export from the nucleus to the cytoplasm and for correct nuclear pore biogenesis and distribution (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 32855
Sequence Length: 295
Subcellular Location: Cytoplasmic vesicle
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Q4P9K4 | MAQPPPQLPPGWVAQWDPNAARQVFVETATGRTSWQPPTAGPAGVAPPQQHQQRPTHPQGQARMSMPQIQPPPGMRGPSLSPISQHGPGAPVSPPSAGSPAPASIGPGASRRRAYPTAHLAANSISYAGGYDASTATGAGVAYPGAQDAQPQLFTPGAPDLTPSPYGAAAQPALGAPGLAPAPGAHGAPGVGPAPGYAAGGVQGITNQFQAMGVGGGVAGGMGQKFSTLQTVNISGVQPNVNDLERPPPEIRLPPNACVSTNPKANADPSYQRCTLNAVPTTSSLLQKSKIPLGLILSPYRSVREADGDEPVPVVTDTVIARCRRCRTYINPYVTFIENGNRWKCCMCNISNEVPQLFDWNSETNQPADRWQRPELNHSVVEFIAPREYMVRPPQPPVYTFLIDVSYQAVNSGMVATAARTILETLDRLPNSDNRAKICIIGVDTSLHFFSITPEGTEPDMLVVSDLDDVFLPKPNDLLVNLTECRAGVEALLQRLGDMYKDSLVTGSALGAALQAAYKLISPIGGKIMVLTASLPSVGPGALKNREDPKLLGTAKESTLLGAASSFYKTFPIDCSRSQVSVDMFLFAPSYTDVATLSCLPRYTGGQTFFYPAFHAGRAEDAVKFSHEFSEVLASPISYEAVLRLRATKGIRATAFHGNFFVRSTDLLALPSVPLDQNYAIECEIEETINAPFVVFQSVVLHSTSSGERRIRVINLALPTTSSMSEVYANADQIAIATLLADKAVERSIHSRLEDARDALFNKLVDVFSTYKSTMTSAGSGASPQLAIAQNLAQLPLLVLALLKHVGIRQSSSIPSDLRAYAQALLTTLPAQQLIPYLHASFYCLHNMAPEAGTTVAEKGFVMPAKLNLTSERFERHGLYLIEDGQNIFLWVGREAVPQLCLDVFDVANYGTLRGGKTTLPKLDNSMNQRVNAIVQRIRDSRRGPYRPHLYIVKEDGEPSLRLWALSLLIEDRFEQSPSYMQFIGQLRDKVNGGS | Function: Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 106974
Sequence Length: 995
Subcellular Location: Cytoplasm
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Q6C2T4 | MSQEHPEQGSSSKRRVYPQQQYDFAAAQPAGYSMPDPTQPYGASASPSAAMYGGAHAIPSPAAFQPHTANVQSGAFAPPPGTPGSAVDPPVAPGVAGGMAYGAPQAAGAAYGYQGLTNQMGNLNIGGGGAYQGGAPPGAAGGAHMAAPTQLNQIYNTDLLQNFPPPISDLTLPPPPVILPPGSSVTGNPDPNADSEFMRCTLNTVPTSSSLLKKSKLPFALVIRPYTALRDADENVPTVADTTIARCRRCRSYINPYVVFLEGGARWRCNMCNLTNDVPSGFDYDAVANKPRDRWSRAELNHSVVEFVAPAEYMVRPPQPLVYVFVLDVSVHSVKNGLLATAARTIKESLSRIPNVDNRTRVGFLAVDSSLHYFAIPRKEDVAEGEGEEGEENEWPEPRMMVVSDIDDPFLPMPTDLLVNLSQCKGGIEKLLDSLQSMFAHTVNPASALGSAVVAAHKLIANIGGKIVCLTSTLPNVGQGKLEVRDDKKALGTSREGQMLQTASTFYKSFAVECSKTQVTVDMFLFSSHYQDVASLSNLPRFSAGQTYFYPGWIASNPEDANKFALEFSEYLSQELATEAVLRVRSCDGIRMSAFYGNFFSRSSDLCSFSTFPRDQSYVIEVNIEETIVKPWVTFQAAILHSTASGERRIRVITRAFPTSALLQDIYASADQIAITTYLANKAVEKALQKGPQDARDLLMNRLNEMFTCYKKDLMTTNVGASAPLQFCTNLRMLPLLVNALIKHIGFRKTSQIPSDLRSAALCLLSTLPDKYLIQYIYPNFYNLIFMPDEAGLPDAETGQIVMPPCTNLSGEHLISHGLFLIDDGQVMFLWVGRDAQPALLQDVFGVSSITEVPTGKTELPVLDNQFNERIRNIISKAREKTDAITYQHLYVVREDGEPALRLWATTHLVEDRVEQSGVTYHQFLTSIREKLNS | Function: Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 101900
Sequence Length: 934
Subcellular Location: Cytoplasm
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P40482 | MSHHKKRVYPQAQLQYGQNATPLQQPAQFMPPQDPAAAGMSYGQMGMPPQGAVPSMGQQQFLTPAQEQLHQQIDQATTSMNDMHLHNVPLVDPNAYMQPQVPVQMGTPLQQQQQPMAAPAYGQPSAAMGQNMRPMNQLYPIDLLTELPPPITDLTLPPPPLVIPPERMLVPSELSNASPDYIRSTLNAVPKNSSLLKKSKLPFGLVIRPYQHLYDDIDPPPLNEDGLIVRCRRCRSYMNPFVTFIEQGRRWRCNFCRLANDVPMQMDQSDPNDPKSRYDRNEIKCAVMEYMAPKEYTLRQPPPATYCFLIDVSQSSIKSGLLATTINTLLQNLDSIPNHDERTRISILCVDNAIHYFKIPLDSENNEESADQINMMDIADLEEPFLPRPNSMVVSLKACRQNIETLLTKIPQIFQSNLITNFALGPALKSAYHLIGGVGGKIIVVSGTLPNLGIGKLQRRNESGVVNTSKETAQLLSCQDSFYKNFTIDCSKVQITVDLFLASEDYMDVASLSNLSRFTAGQTHFYPGFSGKNPNDIVKFSTEFAKHISMDFCMETVMRARGSTGLRMSRFYGHFFNRSSDLCAFSTMPRDQSYLFEVNVDESIMADYCYVQVAVLLSLNNSQRRIRIITLAMPTTESLAEVYASADQLAIASFYNSKAVEKALNSSLDDARVLINKSVQDILATYKKEIVVSNTAGGAPLRLCANLRMFPLLMHSLTKHMAFRSGIVPSDHRASALNNLESLPLKYLIKNIYPDVYSLHDMADEAGLPVQTEDGEATGTIVLPQPINATSSLFERYGLYLIDNGNELFLWMGGDAVPALVFDVFGTQDIFDIPIGKQEIPVVENSEFNQRVRNIINQLRNHDDVITYQSLYIVRGASLSEPVNHASAREVATLRLWASSTLVEDKILNNESYREFLQIMKARISK | Function: Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules. SEC24 specifically recruits cargo proteins like BET1 or SYS1 to the COPII vesicles. The SEC23/24 complex is also involved in internalization of plasma membrane proteins like the maltose transporter.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 103636
Sequence Length: 926
Subcellular Location: Cytoplasm
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Q5AL49 | MSSQADYDKRLAEEVGSLSTRLVTAVNKQVELEETILELRKQVSALKLKNEQLNQSDIKLKTILPKYIKLQDDYRETLTKKKEAESQNTKLQGEVEDLTASLFDEANTMVSNASRETHNFKIKNRKLYEELDEKNIIINDLQEQLQDLKQMFIKMEEQSKIQSYSQSNTPKIESSTDFNETNSIHTNTNFSESKLSKYNTRSTLGDEESQNYNLQQLQRIIYSPLITSIRFDLNNYNIDFKGFVYQLIKPDFQFDLSHLKTIPFFKSIWQSEIENCIHYIPSLPATTTLLNRWQKGKTFWGSLIEGKVSIEPIKGSNETFKLTYKGNNASGNSSNENTESISNRSSATGSVVPVAIKDPCTFCGEARNDSLEHCRLYHLKLFESNTANNSGNNSTNQDQQGNNDNTHVIASYPLCNYCLIKLRNLCDFFAKIRLIRSNIFKLKQNDSFDEFIVVPGSFGQFKRSNTISNRNGTYSSSSTSSSSTSSVSSSSATTANGESLNSTTHNIQLERTEESKLIKLYIMMLLIRSKIFWSKLGFWDTIDQINEINLDEIHYEAFSYLIPKPTQQQQQQQGDIRSQSNFNSPRQSVDGRSVLSGSISSPRQPNLDKQQKDSIVDETVAQLQRDGVVRSETASAEEKFEDAISDETNGQEQLRSEKLQTGKTVTEPNSVSESEPVQEPEQVRSKSNNNTNNKNKDTKIEDSDAEHTFSLKRSHSKQFKDQLNKELDQTLEMLAENIDFDESSNGNGNGN | Function: Guanine nucleotide exchange factor for SEC4, catalyzing the dissociation of GDP from SEC4 and also potently promoting binding of GTP. Activation of SEC4 by SEC2 is needed for the directed transport of vesicles to sites of exocytosis (By similarity). Required for filamentous growth.
PTM: Phosphorylated at Ser-584 and Ser-598. Phosphorylation at Ser-584 by the CDC28-CCN1 and CDC28-HGC1 complexes is required to support hyphal growth. In stationary phase and growing yeast cells, is constitutively phosphorylated, probably on more than one residue, but the pattern of phosphorylation rapidly changes upon hyphal induction and precedes the appearance of hyphal germ tubes.
Sequence Mass (Da): 85334
Sequence Length: 751
Subcellular Location: Bud neck
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P17065 | MDASEEAKRVSIQVTSLSTQLIESVDKQSHLEEQLNKSLKTIASQKAAIENYNQLKEDYNTLKRELSDRDDEVKRLREDIAKENELRTKAEEEADKLNKEVEDLTASLFDEANNMVADARKEKYAIEILNKRLTEQLREKDTLLDTLTLQLKNLKKVMHSLDNESTVTNNSNRYSTILSDSATSSSTSLNKVPTSYSLASQDIYSGIVYSPSISSIRYDISLYNEFLKFVAALPRCENIKATSTESKLIRRLVNDEIQPILKIDNASGIGWLVKKTLLSLIIDGLVVVEPLSGVNATYQIGYNSSSPAKQATSNMPKMFKFPLDSPPVAVHAACSFCGESRDDIIEHARMYILKTLHKTDDGKEQVTNTYPLCHWCLLKLRQTCEIFAFLRSLKVGAWHLEKLTTQNITKEDLEKFSEVTKHTKRDGRVSSQDKKTKRLSFMAGLGINSSTKNKPKMEIFSSETNAKPGQPTTNIQRAWLQLCKLRCILHWTHIGIWAVDDSISSKIGPLVEDDSDEDQNDAISVRLQDKALWKQDAKRPFSSSSAEESQKSDAFDFESGDMENEITGESSSDESSSDGSSTDNSTADSSSEDESSLADSTTSSADSSSPESIDNGEGDDTVTKDDKSSIKSANNNEENSDCGDKKGRSIIKKKAPQRKIQKKKLLQDLDDLEEQFREESAIDQTEFENAESNVKQNISSKRASSGDENSKKDNNEKTLKTNLTIGDKTQEQIGENSPSSGLHASSSNDDNFDDAQEQQ | Function: Guanine nucleotide exchange factor for SEC4, catalyzing the dissociation of GDP from SEC4 and also potently promoting binding of GTP. Activation of SEC4 by SEC2 is needed for the directed transport of vesicles to sites of exocytosis. Binds the Rab GTPase YPT32, but does not have exchange activity on YPT32.
Sequence Mass (Da): 84652
Sequence Length: 759
Domain: The N-terminal domain (1-374) is sufficient for the exchange factor activity.
Subcellular Location: Bud neck
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Q2YAJ4 | MSKALLAAWRINSLAPAPYPERLDTNDNALDRFLGSSLGQARLWASHLRLKRLRSFADKVVHRSNALSALSEAELAACVDDLRVKLARQGLTEDLTIEVFSLVREVCGRKLGLRHFPVQLIGGRVILAGKLAEMQTGEGKSLTAVLPAIAVALSGLPVHVITVNEYLVRRDARFMRPVYEFFGLDVGMVVPDQDPETRRNAYGCDVTYCVNKDLVFDYLRDRIDSNRDVSDARRAVARLFRGDENSRAYLRGLFFGIVDEADSVLIDEARTPLIISSSVSDKQGVDDYRRALDFCRQLRDGLHFRIFAADKLIQLTPAGRDHITNICGNLPGVWQVARARFELIEQALAAQLLYMRDKHYIVKDEKVQIVDEYTGRVMSDRTWESGLHQMIEVKEGCALTDRRKTISRITYQRFFRRYLRLGGMTGTAAEVVGELSAIFGLDVLRIPTNRAVQRKNLGTRIFLDTASRWDAVLKSIRRVRDEGRPVLIGTRSVAASEHLSSLLKTEGIEHSVINARQDEDEATVVEQAGRVGRVTVATNMAGRGTDIKLESGVSDRGGLHVILSEFHESPRIDRQLYGRAGRQGDKGSYESIVSLEDELFVLFSGEMARRVMSNSSFSNVITGMKAKLLRGSAQRSSERYYSRIRRQTVLEDQRLAKMLAFAGRGE | Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving both as a receptor for the preprotein-SecB complex and as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane.
Catalytic Activity: ATP + H2O + cellular proteinSide 1 = ADP + phosphate + cellular proteinSide 2.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 74707
Sequence Length: 666
Subcellular Location: Cell inner membrane
EC: 7.4.2.8
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Q03HZ9 | MEFNLDNFRLRKYSKITKKILALGKKYQTLTDDQLRIKTETLRNKLVKGASLDSILIEAYATIREADFRVLGLKPFENQVLGAVVLHYGNVAQMNTGEGKTLTATMPLYLNGLTGPGNFLVTVNSYLANRDAEEIGKVYKWMGLTCASGVSLDDEELDKKAIYQNDIVYTTNSELGFDYLTDNLVDNINKKKLNDLNFALVDEVDSVLLDLAQTPLVISGAPRVQSNLFVSTDRIVKSLKPNVDFEFSEDLKDVWFTQTGIEQLEEYLGIQGLISDKWSDFYRHLVLALKANYVMKRNQDYIVTNREVLLLDSENGRALTGMKLEAGIHQAIEAKEEVELSDQTRSMASITLQNFFKMFRKLSGMTGTAKSSAREFLEVYNLPVLKIPTHKPNIRIDHADVVFATMDEKIEATVRMVKAAYQIKRPVLLKTGSLSLSRLYSRVLLEHGIVHNVLNAQSESKEAMIVASAGKSGAITVATSMAGRGTDIKLGKGVKEKGGLLVIGTERMDSRRVDDQLRGRAGRQGDPGESIFLVSLDDKVVIENAPDWVEKYRLKLEQAVEQGKRKYGAPLKGRRARKIVEKAQQAADSAAEESRKNAVKMDDILRIQRELIYDFRDYIMKSTDLTTMVQQIKNDYFNAIARENKKDAGKLLDFIINNVDYNYMDNDFNPEILESTADIKQYLEEIARNRWSQQQMIVNNKFKQNYLERLAVLKALDVAWIEQVDNLQQLKTVVTSRSSGQHNPVFEYEKEAMHSFEQMKKLFWKNTVKYMLLSELIPGKNGSVRVEFP | Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane.
Catalytic Activity: ATP + H2O + cellular proteinSide 1 = ADP + phosphate + cellular proteinSide 2.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 89472
Sequence Length: 789
Subcellular Location: Cell membrane
EC: 7.4.2.8
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Q7UWI5 | MRRSSDPSANKKKWTKASNWRPRMVRWQRQLARVNALESTLQAEDDQTIRKRSLALRYRAMAGEKLSELLPEAYALCREAGRRSLSMRHYDVQILGGIALFEGHITEMQTGEGKTLTATLPLYLHSLVGKGAHLATVNDYLAKRDAEWMMPLFEMLGVSVGIIQTEDDQGGRRKSYGAAITYGTAKEFGFDFLRDRLLLRAQNRMQTEMLGSGDGGFSNSGDQVVMRGMHFCLVDEADSILIDEARTPLIIGSIEDTVRDQIIETYKWAAENAPLFELDEHFEIDDETKRYELTARGRSKVRALPKSDLVRTMGLVDMYEYIERSIKTHREFLLDRQYVIRPSEKDPNVDEIVIVDEFTGRLAEGRKWRDGIHQSIEAKEGVEISVPTGQAARITVQDLFLRYPHLAGMTGTAATSAGELRKIYRTPVVRVPTNRPPQRIQLPSRVFGTLTSKFEAIAKEVEEIHATGRPVLVGTRSIDKSVLLSKLLDDLGIEHEVLNANNVEREAEIVAEAGGRGKVTVATNMAGRGTDIKLSNDVEQIGGMHVICTELHDAARIDRQLIGRCGRQGDRGSYRQYLSLDDDILKGGYGAIKYEKLKKRGEATSGSVDRLAAMFHKAQRKVERRHFRDRMVLMHHEKERKKMQREIGQDPYLDTPD | Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane.
Catalytic Activity: ATP + H2O + cellular proteinSide 1 = ADP + phosphate + cellular proteinSide 2.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 74268
Sequence Length: 657
Subcellular Location: Cell inner membrane
EC: 7.4.2.8
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Q5LPY3 | MSDTFPGQAPGAFYPRAPAEPAKSKLDRWIEKYTTLPRRRRRARPSRFFAWRVLRRGKAFAQMSDDRLQGEVRAAAYGMRAARAHPGEALLVRSFALIRECAGRELGQRHYATQILGARAVLNGAVAEMQTGEGKTLAITLAAGTAALAGRRVHVITANDYLAGRDADTMRGLYARLGLTCAAVEPGCTPEERRAAFAADIVYASGKEVAFTFLRDRVAMGGRAGDIGLRTRAFFDGTGLLLPGLQFAIVDEIDSVMIDEARTPLILSVPPADAEVEAEAARAAHAIAAELKEGRDYRLDRLRHAVELSRNGCDRLADLAERMPPAWRPAPIREDAVRTAISAIRLHQRDEHYILRDGKVEIVDEFTGRIMPDRSWSAGLHQAVEAKEGVEITSRRVTLAQITFQRFFRRYIHLGGMTGTATEAADEFWSVYDLPVVRIPTHKRSRRRTWKTQVSTRAATKWARVAKRAKALSASGRPVLIGTRTVAASEAASAALHALGVPHRVLSAAQDADEAAVVAEAGRAGAVTVATNMAGRGTDIILDAEARKAGGLHVIMTEKHSSRRIDRQLAGRAGRQGDPGSTEAILSAEDSLLPEFGGRYSSFVTRFGGSAVLSALTDAQRRAERTHVAARRRLLELDEQMAENLAFTGTPE | Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving both as a receptor for the preprotein-SecB complex and as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane.
Catalytic Activity: ATP + H2O + cellular proteinSide 1 = ADP + phosphate + cellular proteinSide 2.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 71074
Sequence Length: 652
Subcellular Location: Cell inner membrane
EC: 7.4.2.8
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Q8CMU9 | MAKGVNQIINNIRLRKLRKILNQINALSEEFSNFSDEALQAKTKEFKVYLNDNKASLNHILPQAYATVREASKRVLGMYPKDVQILGAIAMHQGNIAEMQTGEGKTLTATMPLYLNALTGKGAYLITTNDYLAKRDFLEMKPLYEWLGLSVSLGFVDIPEYEYAENEKYELYHHDIVYTTNGRLGFDYLIDNLADDIRAKFLPKLNFAIIDEVDSIILDAAQTPLVISGAPRVQSNLFHIVKKFVETLEKDKDFIVNFNKKEVWLTDEGSEKASHYFKVNSIYQQQYFDLVRMIHLSLRAKYLFKYNLDYFIFDGEIVLIDRITGRMLPGTKLQSGLHQAIEALENVEISQDMSVMATITFQNLFKQFDEFSGMTGTGKLGEKEFFDLYSKVVIEIPTHSPIERDDRPDRVFANGDKKNDAILKTVIGIHETQQPVLLITRTAEAAEYFSAELFKRDIPNNLLIAQNVAKEAQMIAEAGQLSAVTVATSMAGRGTDIKLSKEVHDIGGLAVIINEHMDNSRVDRQLRGRSGRQGDPGYSQIFVSLDDDLVKRWSNSNLAENKNLQTMDASKLESSALFKKRVKSIVNKAQRVSEETAMKNREMANEFEKSISVQRDKIYAERNHILEASDFDDFNFEQLARDVFTKDVKNLDLSSERALVNYIYENLSFVFDEDVSNINMQNDEEIIQFLIQQFTQQFNNRLEVAADSYLKLRFIQKSILKAIDSEWIEQVDNLQQLKASVNNRQNGQRNVIFEYHKVALETYEYMSEDIKRKMVRNLCLSILAFDKDGDMVIHFP | Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane.
Catalytic Activity: ATP + H2O + cellular proteinSide 1 = ADP + phosphate + cellular proteinSide 2.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 91214
Sequence Length: 796
Subcellular Location: Cell membrane
EC: 7.4.2.8
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Q83F06 | MLGNIIKKAFGTRNERLLKGYSKIVSRINALEPEIQALSDADLRAKTDEFKKRLVDGEGLDALLPEAFAVVRETSVRTLGLRHFDVQIIGGLALHGGKIAEMRTGEGKTLGATMPAYLNALTGKGVHIVTVNDYLAKRDAEWMKPIYEFLGLTVGVNVPGMEPVEKQAAYAADITYGTNNEFGFDYLRDNMVFDLDQRVQRPLHYAIIDEVDSILIDEARTPLIISGQAEESSDLYVKINKFIPQLKLQKMEEGQKEEEVPPENRGDYTLDEKNRQAYLTEQGHRTIEALMIKQGLMQAGESLYDVSNISLMHYVYAALRAHTLFYRDVHYIVKNNEVIIVDEHTGRLMPGRRWSDGLHQAVEAKEGATIQLENQTLATITFQNYFRLYEKLSGMTATADTEAFELQKIYGLEVVVIPTNRPMIRRDESDQVYLTADAKFDAIVNEVKKRHEKGQPLLIGTASIEASELVARFLKKANIKHEILNAKNHEREAKIIAEAGRPGAVTIATNMAGRGTDIVLGGNLEAEMSELDNLAEEEIQKRKADWQKRHDAVIAAGGLHVLGTERHESRRIDNQLRGRSGRQGDPGSSQFYLSMEDNLLRIFAAERMSNMMRRLGVKEDDVIEHPWITRAIEKAQRRVEGMNFDIRKQLLEYDDVANDQRKVIYQQRFQLLQTDDISETIEAIREEAVSEMISSFVPPQSLEEEWDIPGLEKQIREDFGLALPIAQWLEKDETLHEETLHKRIIDEITKAYKAKEAKADPKAMREVEKTLMLQLLDHHWKEHLAAMDHLRQGIHLRGYAQKNPAQEYKRESFELFTQMLKRIKYELAATLSKLEIATEEQVAQQQRLYQQSAPELQYHHAEMTALQPEKEVAVAEQEEATQPFVRSQPKVGRNESCPCGSGKKYKQCHGKLS | Cofactor: May bind 1 zinc ion per subunit.
Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving both as a receptor for the preprotein-SecB complex and as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane.
Catalytic Activity: ATP + H2O + cellular proteinSide 1 = ADP + phosphate + cellular proteinSide 2.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 103879
Sequence Length: 913
Subcellular Location: Cell inner membrane
EC: 7.4.2.8
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Q85G35 | MKNKLRQIKENREKYRKLKEEELREKTKQLKERAKQESLEELMVEAYSNVWEGAARVLKLEAYDVQLIGAMVLNKGQIAEMKTGEGKSLVAAFASYLNALSGKGVHIVTVNDYLAKRDERWIGEVLRYLGLKTAVITNESSREERKKGYEADVTYITNSELGFDYLRDHMAWSKEEIVQREFNYCIIDEVDSILIDEARTPLIISGPTKGSEKPYKVAWEIGKRMKEGEDYELEEKSKQVILKEKGIKRCEEALEVKDIFSMETPWAHYVMNAIKAKHFYIKDVNYIIKEGEVVIVDEFTGRIMGGRRWADGLHQAIEAKEGVKIQEESETLASITYQNLFLLYPKLAGMTGTAKTEEEEFEQIYGLKVVSIPTHRKMKRKDYPDVVYRTSRSKWMAVAEECERMWTKGRPVLVGTTSIEKSELLARLLEEKGVKYKLLNARPSLAADEASIIAQAGKIGSITIATNMAGRGTDIILGGNIKEAFGEWIKERKKQVDIEEEWRKVLEGKADEESEKKYKQLKEEHEKEQKRVKQLGGLYVIGTERHESRRIDNQLRGRSGRQGDEGSSRFFISLEDDLLRIFGGGQMGEIMSRLGVEEPLESAFLSKSLDRAQKKVENYYYQMRKQLFEYDQVLNSQRKAIYKERTDILRSEEVGEWSKSYIRKEWPGGLLGIKRGMRNRSEVEISYDVKKMQMESVQAGLMNELERLLLLQQIDKSWSKHLKEMSLLREFIAWRGYAQRDPLVEYKNESYNLFIKMIEEIRQGYAYSLFRSQA | Function: Has a central role in coupling the hydrolysis of ATP to the transfer of proteins across the thylakoid membrane.
Catalytic Activity: ATP + H2O + cellular proteinSide 1 = ADP + phosphate + cellular proteinSide 2.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 89750
Sequence Length: 774
Subcellular Location: Plastid
EC: 7.4.2.8
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Q3Z9C1 | MFKFFSGFGDSNEKEIRALEPLVDKINQLESSFSALSDEALKAKTAEFKERLKETFETTASAILKDIAGTTAELEEAQKTADNSKQSRLKAKLESLNKDLSVKENAALNAILPEAFAAVREASRRTIGLRHYDVQLIGGMVLHHGKIAEMRTGEGKTLVATLPLYLNSLLGKGVHLVTVNDYLARRDAYWMGPVYHALGVSVSSIYPMQTPTEELPSRLFDPTYTSETPNDPWMHFRPISRQEAYKADITYGTSTEFGFDYLRDNLRPDLAQCVQREMNYAIVDEIDNLLIDEARTPLIISAPDTEAGKLYEVFARLAPRLAAGKDYEINEKDRNAELTEDGWANVEKLLSREGVMKGSSLYDPQNAPLIRHLRNALSAKEFYKKDHQYVVKENEVIIIDEFTGRMMLGRRYSEGLHQAIEAKEHVKIQQESKTYATVTIQNLFRMYRKLCGMTGTAATEAEEFSKIYKLEVVIIPTNKPAIREDYGDQIYKDQSAKFKAVVNEINEMRNLGRPVLVGTVSIENSEMLSNMLKRQGIEHKVLNAKQHEKEAQVVAEAGKPGAVTVATNMAGRGVDILLGGKEPPKDDDKAYSQWQVHHQQVLEAGGLHVIGTERHESRRIDNQLRGRSGRQGDPGSSRFYVALDDDIMRRFGSERIQGIMEWAGMDENTPIENGLVSRTLENAQKRVEGYHFDVRKHLVEYDDVVNKHREVIYAERRKILLGADLKSNILDMIREEIMTQTAEHTQGYDSSEWNLEGLVTHIGGIFALPAEINAEALAKLSQEEITELLTRTAEELYQKKEAEIGAGSMRLLERIIMLHTLDSLWVEHLTIMENLRREIGLQAFAQRDPLIAYKNEGHVRFQELLETIKHDVVHNIYRVNIQIQHQTESATAKAASRPVQQQKPLPAAPAAAIPGVSAKAATQPAAPAAKEVGRNDPCPCGSGKKYKKCCGK | Cofactor: May bind 1 zinc ion per subunit.
Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane.
Catalytic Activity: ATP + H2O + cellular proteinSide 1 = ADP + phosphate + cellular proteinSide 2.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 106951
Sequence Length: 952
Subcellular Location: Cell membrane
EC: 7.4.2.8
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Q9RWU0 | MFRVLNKVFDNNKRDVERIIQTVVKPVNALEEETMRVENLAEAFMDLRRRVQDGGESLDSLIVPAFALIREAGRRSIGKRHYDTQLIGGAALHQGRIAEMRTGEGKTLVATLALAFNALEGKGCHLVTVNDYLARVGMEEMGLLYRTLGLTVGLANRELSPAEKQAAYACDITYVTNSELGFDYLRDNMAQSKEALVLRADTPLHYAIVDEVDSILIDEARTPLIISGAAEKATDLYYVFAKLIRRLQKGEPAEPGVRTEPTGDYTIEEKSKAVHLTEQGITKIERLLSLKDLYSPENMDKAHMITQAIRARELYHREKDYIVNAEGEVVIVDEFTGRSMPGRRYGEGLHQAIEAKEGVKIENENQTLATITYQNFFRLYDKFAGMTGTAKTEEKEFLDIYGSDVLVIPTNKPVIRVDSDDLIYRTRMGKYAAVVGEVQEMHATGRPILIGTASIETSEQLSSLLQQAGVQHAVLNAKFEAQEASIIAQAGRSGTVTIATNMAGRGTDIMLGGNDEYIIGESIEQQLGVSRYAPEVEAFIKAISREDPAAEQLGMQIPGITLDFIRQAQELHRATVEDRQRVRDLGGLHIVGTERHESRRIDNQLRGRAGRQGDPGSSRFYVSFEDDLMRLFANDRVVGMMDRLGMDDSQPIEAKMVTGAIEKAQARVEDRNFGIRKQLLEFDNVMSKQRDEIYAQRREVLLGPDEDIEETTEGMIGDFVDSQLAAYAPIEVSHEQWDIEQLRSAMVEAVPALETFDFESLRVNSPAEAQDRLLSAVADAFDARKEELSPTMMNSLARYVLLQVVDQHWKEHLHGMDVLRQGIGLRGYGQRDPFTEYKFEATNMFNEMIDALKADVTKFIFRMQFGGA | Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane.
Catalytic Activity: ATP + H2O + cellular proteinSide 1 = ADP + phosphate + cellular proteinSide 2.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 97270
Sequence Length: 868
Subcellular Location: Cell membrane
EC: 7.4.2.8
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Q9JYK8 | MLTNIAKKIFGSRNDRLLKQYRKSVARINALEEQMQALSDADLQAKTAEFKQRLADGQTLDGILPEAFAVCREASRRTLGMRHFDVQLIGGMVLHDGKIAEMRTGEGKTLVATLAVYLNALAGKGVHVVTVNDYLASRDAGIMEPLYNFLGLTVGVIISDMQPFDRQNAYAADITYGTNNEFGFDYLRDNMVTDQYDKVQRELNFAVVDEVDSILIDEARTPLIISGQADDNIQLYQIMNTVPPHLVRQETEEGEGDYWVDEKAHQVILSEAGHEHAEQILTQMGLLAENDSLYSAANIALMHHLMAALRAHSLFHKDQHYVIQDGEIVIVDEFTGRLMSGRRWSEGLHQAVEAKEGVEIKRENQTLASITFQNYFRLYTKLSGMTGTADTEAFEFQSIYNLETVIIPTNRPVQRKDFNDQIFRSAEEKFEAVVKDIEECHKRGQPVLVGTTSIENSELVSKLLTQAGLPHNVLNAKEHEREALIVAQAGKVGAITVATNMAGRGTDIVLGGNLKHQTDAIRADETLSDEEKQAQIAALEDGWQAEHDKVMEAGGLHIIGTERHESRRIDNQLRGRSGRQGDPGSSRFYLSFEDPLLRLFALDRAAAILNRLAPERGVAIEHNLLTRQIEGAQRKVEGRNFDMRKQVLEYDDVANEQRKVIYSQRNEILTSKDISDLMQEIRSDVVSDLVDTYMPPDSMEEQWDIPTLENRLAAEFRLHEDIQSWLKADNAIDGQDIKERLIERIENEYAAKTELVGKQAMADFERNVMLQVIDNQWREHLAAMDYLRQGIHLRSYAQKNPKQEYKREAFTMFQDLWNGIKFHIASLLTSVQIEQNPVAVVEEQPIGNIQSIHSESPDMEELLGQSQTDLVTEAFNPDGTDFSPEALEARGQIVHRNDPCPCGSGLKYKQCHGKLA | Cofactor: May bind 1 zinc ion per subunit.
Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving both as a receptor for the preprotein-SecB complex and as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane.
Catalytic Activity: ATP + H2O + cellular proteinSide 1 = ADP + phosphate + cellular proteinSide 2.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 103294
Sequence Length: 916
Subcellular Location: Cell inner membrane
EC: 7.4.2.8
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A1SGL9 | MPAILDKILRIGEGKILRQLEAIAQAVNAIEDDFVAMSDAELQGMTAEFKERLANGESLDDIMPEAFATVREAARRVIGLRPFDVQVMGAGALHMGNIAEMKTGEGKTLVAVLPSYLNALSGKGVHIVTVNDYLAKFQSEMMGRVHHFLGLTVGVILPEMRPDERRVAYNCDITYGTNNELGFDYLRDNMAGSIEECVQRGHNFAIVDEVDSILIDEARTPLIISGPTQDEVHWYAEFAKVARNLVRDEDYEVDEKKRTISVLEPGITKVEDHLGIENLYESANTPLISFLHNSIKAKELFHNDKEYVVLNGEVLIVDEHTGRMLAGRRYNDGLHQAIEAKEDVQVREEYQTLATVTLQNYFRLYDKLSGMTGTAMTEASEFDKIYKLGVVPIPTNKPMARKDQADLVYRTEEAKYEAVVEDIAERHEKGQPILVGTVSVEKSEHLSAKLKKRGIPHSVLNAKVHADEAKIVALAGHKGAVTVATNMAGRGTDIMLGGSVEFLADAELRKRGLEPAGETADEYQAEWPGTVERIKSQVANEHDEVRALGGLYVVGTERHESRRIDNQLRGRSGRQGDPGESRFYLSLQDELMRLFKSDWVDRVLQVLKIPDDVPIENKRVTSAIANAQGQVESQNFESRKNVLKYDDVMDRQRKVIYAERREVLEGKDLQDQIRTFIDDTVTGYVTGATEEFAEEWDLEALWTALRQIYPVGVDYRVLEEEAGGRANMDRDELIAVLQKDAHEAYDRREAEVGETVMRELERRVVLSVLDRKWREHLYEMDYLREGIYLRAYSQRDPLVEYQREGFEMFAAMMDGIKEESVGFLFNLEVQVEIEEEDEEEEEVLEPMRQPVPSFDQQGAMPQIRAKGLERPSQPTKLAYSAPSEDGDAEVKGATVTNADDEFAGVGRNDRCPCGSGKKFKQCHGRPGGPTGLTARVS | Cofactor: May bind 1 zinc ion per subunit.
Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane.
Catalytic Activity: ATP + H2O + cellular proteinSide 1 = ADP + phosphate + cellular proteinSide 2.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 105321
Sequence Length: 937
Subcellular Location: Cell membrane
EC: 7.4.2.8
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Q313L3 | MLGSIVKKVFGSKNDRYLKSLNHYLKEINALEENIATMPDEAISARMAELRAEVQQGTSLDSILPEVFAMVREAGKRVLGMRHYDVQMVGGIALHSGKIAEMRTGEGKTLVATLPAALNALTGKGVHLITVNDYLARRDAEWMGKIYNFLGLSVGVIVHGLNDEERRAAYASDITYGTNNEFGFDYLRDNMKFYKEQLVQRPHHFAIVDEVDSILIDEARTPLIISGPSDESTGLYRRVNDIIPRLKRDTHYTVDEKARAAALTDEGVQEAEKLLGLDNLYDPQNISFQHHILQALKAHSIFTRDVDYIVKDDQVVIVDEFTGRLMPGRRFSDGLHQALEAKEGVKVEAENQTLASITFQNYFRMYEKLSGMTGTADTEAVEFQQIYDLEVVNIPTNKPMIRKDQPDSIYRTRPEKFNAIVEEIARLHHKGQPVLVGTISIETSELIAGMLKKKGVPHNVLNAKQHEKEAEIVAEAGQAGKVTIATNMAGRGTDIVLGEGVPQLGGLYILGTERHESRRIDNQLRGRSGRQGDPGETRFFLSLEDDLLRLFGSDRIAGLMERLGMQEGEPIENKMVSRAIENAQKRVEGHNFEIRKTLLDYDNVMNQQREVIYSLRRDTMMEDDLEPSVHEFLDDIIEDIYAPLEQTKGKALDEETHAAIAARLEETFFLSRVYPEFALKGSEQQEKLPELPSAADVKKAVESMLEKLKRDAGPVYGDILRYFLLEELDRNWKEHLLNMDHLRDGIGLRGYGQRDPKQEYKREGFSLFQNMLWSIKESVFRALTRLRLQRVEEAADPAEQPEAAGLQEAKATELRHKEQPAELSYSGGDEDGAKTPSRRNAPKVGRNDPCPCGSGKKYKKCCGA | Cofactor: May bind 1 zinc ion per subunit.
Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane.
Catalytic Activity: ATP + H2O + cellular proteinSide 1 = ADP + phosphate + cellular proteinSide 2.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 97327
Sequence Length: 864
Subcellular Location: Cell inner membrane
EC: 7.4.2.8
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Q32743 | MFNFLENEKYKLKEYQPLVNQINLLETSVKNYTDIELKEQFDKLRKEYFLSQNFSNDIIARSFSLTREAAFRTIGLRPFDQQLLGGLVLNSGKITEMKTGEGKTLVATLPAALNAISGRGVHIVTVNDYLAKRDSTWMGQIYDYLGLTVGLVQSQMESQERKDNYFQDITYITNSELGFDYLRDNQVKTFQEMVQRKFNYCIIDEVDAILIDEARTPLVLSIPDTIHNPKIYLDANTTAKSLIRDVDFKADEKTKNITFTDIGIDKIEYFRKIPNIYGTNAGFLFYLQNAISANIFFRKNSEYIIENNKIAIVDEFTGRVMPVRRWSNGLHEAIEAKESIDITQTSRISSSITYQNFFTLYPKLAGMTGTAKSAALELESIYNLEVVVIPTSKKFQRKDLPDKVYTNDFAKWKAIAKECFEIHKTGRPILVGTSSIEKSDFVSFLLENYKLQYNVLNARPENLKYESEIVGEAGCLNAITIATNMAGRGTDIILGGSPGFKIIRLLKILVLKVKLKEARTKKGLFLTHELYKELQKERLNYDAITQLVKFETEFGQKQIVRQKKLSTLFFYLKINYKSRFKKQKQYINQLGGLYVIGTERQDSKRIDNQLRGRAGRQGDAGSSRFFVSIEDKIFRLFGDNKFSNLFNQLNLTNEEISLESDLITKTLDNTQERVENYYYDIRKQVYDYDELITEQRKTFYLFRSKVLKTQVSGNLIIASTEDVIKKIVKSIKTPQLKFTNLTHKQENQIILEDFEQCRRIMRYALPPINLKQINASNHNVLFEFLMQEFWISYDIHKTKAFSSIGEEYYKEYERSCVLESIDHGWSTNLEKMETIRESIVWRVYAQKDPLAEYKKEGFSTFRKMDEEMKRFLVFAVFDTDFYVT | Function: Has a central role in coupling the hydrolysis of ATP to the transfer of proteins across the thylakoid membrane.
Catalytic Activity: ATP + H2O + cellular proteinSide 1 = ADP + phosphate + cellular proteinSide 2.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 102800
Sequence Length: 884
Subcellular Location: Plastid
EC: 7.4.2.8
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P47994 | MGFLTKIVDGNKREIKRLSKQADKVISLEEEMSILTDEEIRNKTKAFQERLQAEEDVSKQDKILEEILPEAFALVREGAKRVFNMTPYPVQIMGGIAIHNGDISEMRTGEGKTLTATMPTYLNALAGRGVHVITVNEYLASSQSEEMAELYNFLGLSVGLNLNSLSTEQKREAYNADITYSTNNELGFDYLRDNMVNYSEERVMRPLHFAIIDEVDSILIDEARTPLIISGEAEKSTSLYTQANVFAKMLKAEDDYNYDEKTKSVQLTDQGADKAERMFKLDNLYDLKNVDIITHINTALRANYTLQRDVDYMVVDGEVLIVDQFTGRTMPGRRFSEGLHQAIEAKEGVQIQNESKTMASITFQNYFRMYNKLAGMTGTAKTEEEEFRNIYNMTVTQIPTNRPVQREDRPDLIFISQKGKFDAVVEDVVEKHKKGQPILLGTVAVETSEYISQLLKKRGVRHDVLNAKNHEREAEIVSTAGQKGAVTIATNMAGRGTDIKLGEGVEELGGLAVIGTERHESRRIDDQLRGRSGRQGDRGESRFYLSLQDELMVRFGSERLQKMMGRLGMDDSTPIESKMVSRAVESAQKRVEGNNFDARKRILEYDEVLRKQREIIYGERNNIIDSESSSELVITMIRSTLDRAISYYVNEELEEIDYAPFINFVEDVFLHEGEVKEDEIKGKDREDIFDTVWAKIEKAYEAQKANIPDQFNEFERMILLRSIDGRWTDHIDTMDQLRQGIHLRSYGQQNPLRDYQNEGHQLFDTMMVNIEEDVSKYILKSIITVDDDIERDKAKEYQGQHVSAEDGKEKVKPQPVVKDNHIGRNDPCPCGSGKKYKNCCGK | Cofactor: May bind 1 zinc ion per subunit.
Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane.
Catalytic Activity: ATP + H2O + cellular proteinSide 1 = ADP + phosphate + cellular proteinSide 2.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 96056
Sequence Length: 842
Subcellular Location: Cell membrane
EC: 7.4.2.8
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P0AG95 | MAQEYTVEQLNHGRKVYDFMRWDYWAFGISGLLLIAAIVIMGVRGFNWGLDFTGGTVIEITLEKPAEIDVMRDALQKAGFEEPMLQNFGSSHDIMVRMPPAEGETGGQVLGSQVLKVINESTNQNAAVKRIEFVGPSVGADLAQTGAMALMAALLSILVYVGFRFEWRLAAGVVIALAHDVIITLGILSLFHIEIDLTIVASLMSVIGYSLNDSIVVSDRIRENFRKIRRGTPYEIFNVSLTQTLHRTLITSGTTLMVILMLYLFGGPVLEGFSLTMLIGVSIGTASSIYVASALALKLGMKREHMLQQKVEKEGADQPSILP | Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35382
Sequence Length: 323
Subcellular Location: Cell inner membrane
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B2KBZ0 | MMNLIPKTNFDFLKIRKYFYAVSAIILIAGLICILTRGLNMGIDFKGGTMVQVQFTESITIDQVRSAVEKYNPEIQSYVGKNTYMIKIKGSQENVNEVRSDVETSLTAAKLKFTVVATDFVGPTVGKDLGERALWALALSLVFMVLYIAFRFQNIIWGTAGVIALIHDAFFMVAAFAFLQKEFDLVIVAALLTAVGYSINDNIVIFDRMRENIKENPKESFYNIVNRSLNETLSRTVITGSTVLIVLVIIYFFGGEVLKNFSLIMLIGVIVGTYSTLFIATPIVYDWAKDSDNFAKTVGNQDVALAAEIKTAKKHNKKKHR | Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35877
Sequence Length: 321
Subcellular Location: Cell inner membrane
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B1H0M3 | MRFFRSVDIDFIGNRYKFFTISGLLLLLTVGAFIYRGGLNYGIDFTGGILMRISFQNEVGLQDVRIAVEESGINSFELQSSGNLVMIRIKKDLEAQEEFETLIKSSIQLRFPDNPVKIEGIEYIGPTVGEYLSKQAVYAFLFAFLVMIVYVAFRFKSSLWGIVSVVGIIHDIVISLGFVILANKEINITIVAALLTVVGYSINDTIVLFDRIKENLKLLVKEDFVAVINKSINEVLVRTIVTSLTVFIVACSLFFFGGEVMHTFAYIMIIGTVLGVFSTIFVCAPLICEWRIKTNKRLKIAIKQDGVRSK | Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34806
Sequence Length: 310
Subcellular Location: Cell inner membrane
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C1A8P3 | MLRIFHNTKYEFVRWWRVAAGLTLAFIAAGFVSFAVTGGVNYSIEFTGGTLMQLQFKTPPDVAEVRSALDAAGIQGAEIQQFGANTDFTIRARDEKQVEAQDAGAEGISRQITAALDAKFGAGTVTIVRTEAVGPKVGAELRTGAAMAMLIASIFTLIYLAIRFDWRFGLAAVLSTTHDILITLAFIKIFHIEVSLTVVAAILTLVGYSANDTIIIFDRVRENLKKPHKGETLSHILDRSINETLPRSIMTHTTTFSATLALLLLAGEVIRPFAWVMAFGVVMATFSSIYVAGPLLLWIEGRWPRLDDAATARAVRAGEAATTTARGTDRVSAR | Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 36252
Sequence Length: 334
Subcellular Location: Cell inner membrane
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D4GTK4 | MVEFTVPEVDYTRYTNRQLAAVPLAVLAVALLVIGGWYVATGAPVNPGVDFTGGTELRIATDAPQSEVAAAFDSQPESIRSVAADGTYVVTFQSGSATSTELQTQAEDAGFEVRSIDAVSANFGGETQLLALGGLAVAFAGMSVLVFAMFRSFVPSIAVVLSAFSDIVIPVALMNLFGIELSLGTVAALLMLIGYSVDSDILLNNHVLRRSGDFYESTARAMRTGVTMTLTSIAAMIVMTIMATLFGIQLLAAIGTVLVFGLTADLMNTYMLNVTLLRWYKFEGVTR | Function: Involved in protein export.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 30425
Sequence Length: 287
Subcellular Location: Cell membrane
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O26073 | MELFKRTRILSFMRYSNYGVIVSAILALLALGLLFFKGFSLGIDFAGGSLVQVRYTQNAPIKEVRDLFEKEARFKGVQVSEFGSKEEILIKFPFVETAENEDLNAIVANILKPSGDFEIRKFDTVGPRVGSELKEKGILSLILALIAIMVYVSFRYEWRFALASVIALVHDVILVASSVIVFKIDMNLEVIAALLTLIGYSINDTIIIFDRIREEMLSQKTKNATQAIDEAISSTLTRTLLTSLTVFFVVLILCVFGSKIIIGFSLPMLIGTIVGTYSSIFIAPKVALLLGFDMDKYYENETRKIKKAQEKEKMRRLYESGQV | Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 36277
Sequence Length: 323
Subcellular Location: Cell inner membrane
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E3F0U0 | MAFRLKLVPDKTSVNFFKWGGIPTHATFALALASLIAVMTIGLNYGIDFLGGTTIRAESSENVAVSEYRSALDQIELGDVTITEVFDPGFRADQFVKQVRIQAANETEVSNALIGQVEAALQVVDPQVVFTAVETVGPKVSGELIQTAVLAAVLAVAASLLGIMAYVWLRFEWQFGFGAVVGLFTDAMITVGLFSVFQVRFDLTIVAAVLTIVGFSINDKVVVFDRVREILRRDSTTPLPELMVVALNETLSRTVMTTVTTILALVALYIWGGDVIRGFAFAMLFGSVIAVYSTIFVSAQVVLWLGVKRDWEKKTDTGPSGTQFTTSAE | Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35652
Sequence Length: 329
Subcellular Location: Cell inner membrane
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Q1IVE8 | MELFRNTNIDFLGKKWYFLAFSLVFSVAGLISMGARYAKTGTAVPLGVDFKGGTLVYVKFAQTPNLGDIRAAMDRSGLKDPKIQTYGGPANNEVLIALEQKETSEQALDAGKNTIIKALETNPASGKNDLNNVGSTTIRDYLMSKDPLHEVVDPGAKYQQIASQIVDYRDKERGGVLSSVDELQGHVPADVVNALKTDYFTSGFGVRNVEIVGPQVGKQLSNQALLATLYSLGGMLVYLWFRFELIYGIGAVVACFHDTIITVGAFSLLNRDISLTVVAAILTLIGYSMNDTIVVYDRIRENIKLLRRESLADIVNKSINQTLSRTILTSGLTFLTVLSLYVFGGEVLRGFSLALVIGILIGTYSSIAVAAPMLVAYQEWRGHRGTAALPGPAPRKNDRVKVKA | Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 43937
Sequence Length: 404
Subcellular Location: Cell inner membrane
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A0LCK8 | MQVFLKATHFDFIGRRKPAIYASLFLIGVSLVSLFTQGLNFGIDFAGGTLIQVRFEKPMDLAPVRQAIAPLDLGDTVVQSFGTPEEVLIRVEKQGADNAAQQAIVSGVLDALKPIAGEHGVEMRRVEYVGPQVGEELTEKGMLAMLYAMVAILIYISFRFELRFALGAVLALVHDVVLTMGFFSVLQKEFTLVVVAALLTVVGYSLNDTIVVYDRIREEMKRMKRQPLATIINEAVNRTLSRTLITSLTTVLVLIALFVLGGAVIHDFALTLLFGVGIGTYSSIFVASPLVLLMDPGSRRKVAAETAEETP | Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 33934
Sequence Length: 311
Subcellular Location: Cell inner membrane
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Q58650 | MIKDYKVSIAIPIALLILSILLIGFKGIPKSIDITGGTEITIKVNENMDITPLKESLNGIAEVKKLESADGYYIVIRCKNEDVDIVKQKIKEFFHVDSLDKLNYSEKTIGATLSSKFFEEGFKAVGFAFMFMAIVVYLYFRNPVPSGAIILSALSDIIMALGAMSLLGIELSSATIAALLMVIGYSVDSDILLTTRVLKRLTKSFDETVKEAMKTGLTMTLTTITAMLILLIVVKLFIPVADILANIATVLILALIADIINTWLLNAGILKYYITEYRAKKI | Function: Involved in protein export.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 31029
Sequence Length: 282
Subcellular Location: Cell membrane
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Q8TWM5 | MGLFEKYVSNLNRLLILTMVFAVICAGSTLALGVKKGIDLKGGTMVILKTEKDPDTVTSEASRILGVSDVEAIRSSQGDVIVQVPKYLSADDVNKLARAVGGEVESVQTIGPALGRVFWESVKVAVPLALVAVSIVVFAIFRKPLLSAAVLGALALDLVDALGLMALTGVPLTLASFAGLLMIIGYAVDSNILLSMYTVKRRRVRRVDRAIADSFKTGITMVATTTAAACALFLLSMSEAMFEIAAVVIFGLIADVLNTWIFNAWVIREKIAGR | Function: Involved in protein export.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 29148
Sequence Length: 274
Subcellular Location: Cell membrane
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E1RHR2 | MGKFTYDINRYEPKQMVALPLCLLILSVIFLAFNTVSTGMPVEPGIDFAGGVAVTLSTSDSVDVIEDYFADYPLKISESDVAAGYLVFNYLEGDSFKDLTEHITARYPDATIYQMGETFGKTLQSQAIWALLFAFVLMAIVVFVAFRIFIPSVAVVLSAFSDIVITAAFMDVFGLTLSLGTTAALLMLIGYSVDSDVLLTTRLLKRQGKVDEKFRGAFRTGIIMTTTTLAAVVVMFIVFSLGQVTLIRDISAVLIIGLIIDMMNTWMLNAGLLKWYVKKGGK | Function: Involved in protein export.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 30925
Sequence Length: 282
Subcellular Location: Cell membrane
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O26936 | MGETLKVIVLIDRILKSYRPLIAIPAAITVIALLLVVFNGLNESVDLKGGALAELTLEKSVTQAELESLLREKLGTGDIKVLSIRGERVTVQFGTDMDVVKVSEALRGTATINSYKAVGPVLSKQAMNQIYWAIGFAFLFMSVTVFIIFRDPVPSLAVILAAASDIIIAVGGMSLFGIPLSLASVGAILMLIGYSVDTDILLTTRVLKRRKGTINERALGAMKTGVTMSIAAIASMAALYLVTVFVMPEARVLSDIAAVLIIGLLADILTTWLMNLGILRWYLEVRS | Function: Involved in protein export.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 30839
Sequence Length: 287
Subcellular Location: Cell membrane
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P21135 | MLPRTMFSYGKENAFPVTPISNRNGTKGAGSKRAPLGSTKQSNAPSSVTVPRTVLGGKSTNISKFISAPSTKKMSPMDISMDSPTILEPNSQGISRSAVQERSKRLSASPRRSSLTDTPLPNELEEDIEYMPPPVHLDPIQSLGFDDVAIDCETLDPWPSMQNKATSVTIRNTPASDFHVYKEFSDDDPIQFPLLSVDGDSPLTEKDTNLTTPATLKASDQQRKVLEKPSVSKQSSSRTRLSTVYRTKLASGKSIPRPLSHKLTRPRVTASGNSRRRPLSRSIHSLSSSRIDFSSLDTGLL | Function: Regulatory protein, which plays a central role in chromosome stability. Probably acts by blocking the action of key proteins. During the mitosis, it blocks separase/cut1 function, preventing the proteolysis of the cohesin complex and the subsequent segregation of the chromosomes. At the onset of anaphase, it is ubiquitinated, conducting to its destruction and to the liberation of cut1.
PTM: Ubiquitinated by the anaphase promoting complex (APC) at the onset of anaphase, conducting to its degradation.
Sequence Mass (Da): 32854
Sequence Length: 301
Domain: The N-terminal destruction boxes (D-box 1 and D-box 2) act as a recognition signal for degradation via the ubiquitin-proteasome pathway.
Subcellular Location: Cytoplasm
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