ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q0DGG8 | MLVVVARKSSSSARVAAHQTRSHRAAMPAGQPHAHEPDGGGASHRRPQSPPSLPAEVVPAFAPPESEDEESWVWSQIKAEARRDADAEPALASFLYATVLSHPSLPRSISFHLANKLCSSTLLSTLLYDLFLASFTAHPSLRAAVVADLLAARSRDPACVGFSQCLLNFKGFLAIQAHRVSHVLWAQQRRPLALALQSRVADVFAVDIHPAAVVGKGILLDHATGVVIGETAVVGDNVSILHHVTLGGTGKAVGDRHPKIGDGVLIGAGATILGNVKIGAGAKIGAGSVVLIDVPARNTAVGNPARLIGRKNGEVEKDED... | 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 | MSTMAKSPEANNLHQDVIAQFPILNGYTHTVGAFSQPLNVSRLFIIDEIQTAYDELRVQIPWLAHQVVVVDAGPGKSGYITTAPWPSSAPPNDVTYEEKDDAFPSLNTLIKSGGSFLATKDLVGYPGLPEPHGLHPTPVATIRLVFITGGVLVVLSTHHNIVDGIGLMQMWDYLDILMGGGAISRQDARSANADRARVLPLIAPGEPVKDYSHLIRPNPWPLPPPPKTEWRLFKMHPWALAEIRSRARDGTDQRASARPASSDDALTAFCWQRVSAMRLASGRVTGDQVSKFGRAVNGRSAMGLDSSYLFHMMLHTETRL... | 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... |
A0A084B9Z4 | MPQDPNTTLQMSSSKPSLSDLSVSADPVLGKADNQVRDSLALPSIEGGEEGVMRPLAWLFGLCAIQQASGATLLRNDVSTVEPLPPTQDPWYRAPPGFEKKQPGDVLRIRQAPGNLTTVVSNSSAAFHILFRTTNARSEPAWAVTTLFLPKKLYRAPSRNAALLSFQLADNSANPDSAPSLGLYWRLAQDNPMLGLRSDTSFISNLLSEGWLVNIPDQSGPEAAFGASRQAGHATIDAIRAIQHLCSLTGATGINAAIWGYSGGTFATGAAAELMPTYAPNINIVGAVLGGMVTDVSGGFDSLNRSPIAATIIATLLGVT... | 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 al... |
A0A084B9Z5 | MSTSTSEPGAIAGLPLGAEVRTDGDATGLSVAIVGGGIVGIALALGLVERGVRVSVYERAQELPEIGVGFAFNGAARKSMARLSPLVMAAVERVANENEQAYDNYWDGYTSTAEDDESSTASKRGKLLFRMPNSNMAWWSCLRSQFLNEMLQALPPGTVTFGKELDSYDDPFDTSDPVRLRFTDGTTAAANVLIGSDGLRSRVRQQLFATSHPEVCNPTYTHKTCYRAVIPMAAAESAMGLSKPHNHCMHTGPRAHVLSYPIAQHKLVNVVLFVTHDEPWVDGTGDEAISVPRMTRPGDKKVLQNRLADWRPEVRNLVAQ... | 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, i... |
Q01826 | MDHLNEATQGKEHSEMSNNVSDPKGPPAKIARLEQNGSPLGRGRLGSTGAKMQGVPLKHSGHLMKTNLRKGTMLPVFCVVEHYENAIEYDCKEEHAEFVLVRKDMLFNQLIEMALLSLGYSHSSAAQAKGLIQVGKWNPVPLSYVTDAPDATVADMLQDVYHVVTLKIQLHSCPKLEDLPPEQWSHTTVRNALKDLLKDMNQSSLAKECPLSQSMISSIVNSTYYANVSAAKCQEFGRWYKHFKKTKDMMVEMDSLSELSQQGANHVNFGQQPVPGNTAEQPPSPAQLSHGSQPSVRTPLPNLHPGLVSTPISPQLVNQQ... | 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... |
Q8VI24 | MERRSESPCLRDSPDRRSGSPDVKGPPPVKVARLEQNGSPMGARGRPNGAVAKAVGGLMIPVFCVVEQLDGSLEYDNREEHAEFVLVRKDVLFSQLVETALLALGYSHSSAAQAQGIIKLGRWNPLPLSYVTDAPDATVADMLQDVYHVVTLKIQLQSCSKLEDLPAEQWNHATVRNALKELLKEMNQSTLAKECPLSQSMISSIVNSTYYANVSATKCQEFGRWYKKYKKIKVERVERENLSDYCVLGQRPMHLPNMNQLASLGKTNEQSPHSQIHHSTPIRNQVPALQPIMSPGLLSPQLSPQLVRQQIAMAHLINQQ... | 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 ... |
P0AFY7 | MFKSFFPKPGTFFLSAFVWALIAVIFWQAGGGDWVARITGASGQIPISAARFWSLDFLIFYAYYIVCVGLFALFWFIYSPHRWQYWSILGTALIIFVTWFLVEVGVAVNAWYAPFYDLIQTALSSPHKVTIEQFYREVGVFLGIALIAVVISVLNNFFVSHYVFRWRTAMNEYYMANWQQLRHIEGAAQRVQEDTMRFASTLENMGVSFINAIMTLIAFLPVLVTLSAHVPELPIIGHIPYGLVIAAIVWSLMGTGLLAVVGIKLPGLEFKNQRVEAAYRKELVYGEDDATRATPPTVRELFSAVRKNYFRLYFHYMYFN... | 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 | MEPWDPPQLPPVRHSHAAGSGRAEGRHGTPPPWRPIISGPLPRPGSWDPGRDLHRPASQAESYESGHAFRAYSRQGYEDPHWQYPGAAYRDNHAYQSHQWQPTAWQGNRDVTQVKPHGKSTTYRDQHYYRGYHPNLAASPLGQDRSQTYDAYKEGSRRSWAGVSNLGEASGQPQQPSLLQQYRESGLSSSGYELSQYIRDGAEPNDTAFLGGWSPVQGGGPLESAVMAPHKFLQPHVPVCLGAGGQLVLVCPHRPTEGQLPLVELHSLEVILQGTTDQEELQAFPGPLAREDLHKVDVMTFCQQKIASSCDLSTQRGRDS... | 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 biogene... |
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).
Subcel... |
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 re... |
P30531 | MATNGSKVADGQISTEVSEAPVANDKPKTLVVKVQKKAADLPDRDTWKGRFDFLMSCVGYAIGLGNVWRFPYLCGKNGGGAFLIPYFLTLIFAGVPLFLLECSLGQYTSIGGLGVWKLAPMFKGVGLAAAVLSFWLNIYYIVIISWAIYYLYNSFTTTLPWKQCDNPWNTDRCFSNYSMVNTTNMTSAVVEFWERNMHQMTDGLDKPGQIRWPLAITLAIAWILVYFCIWKGVGWTGKVVYFSATYPYIMLIILFFRGVTLPGAKEGILFYITPNFRKLSDSEVWLDAATQIFFSYGLGLGSLIALGSYNSFHNNVYRDS... | 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 ... |
P31648 | MATDNSKVADGQISTEVSEAPVASDKPKTLVVKVQKKAGDLPDRDTWKGRFDFLMSCVGYAIGLGNVWRFPYLCGKNGGGAFLIPYFLTLIFAGVPLFLLECSLGQYTSIGGLGVWKLAPMFKGVGLAAAVLSFWLNIYYIVIISWAIYYLYNSFTTTLPWKQCDNPWNTDRCFSNYSLVNTTNMTSAVVEFWERNMHQMTDGLDKPGQIRWPLAITLAIAWVLVYFCIWKGVGWTGKVVYFSATYPYIMLIILFFRGVTLPGAKEGILFYITPNFRKLSDSEVWLDAATQIFFSYGLGLGSLIALGSYNSFHNNVYRDS... | 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 ... |
P23975 | MLLARMNPQVQPENNGADTGPEQPLRARKTAELLVVKERNGVQCLLAPRDGDAQPRETWGKKIDFLLSVVGFAVDLANVWRFPYLCYKNGGGAFLIPYTLFLIIAGMPLFYMELALGQYNREGAATVWKICPFFKGVGYAVILIALYVGFYYNVIIAWSLYYLFSSFTLNLPWTDCGHTWNSPNCTDPKLLNGSVLGNHTKYSKYKFTPAAEFYERGVLHLHESSGIHDIGLPQWQLLLCLMVVVIVLYFSLWKGVKTSGKVVWITATLPYFVLFVLLVHGVTLPGASNGINAYLHIDFYRLKEATVWIDAATQIFFSLG... | 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 Topolo... |
P27922 | MSEGRCSVAHMSSVVAPAKEANAMGPKAVELVLVKEQNGVQLTNSTLLNPPQSPTEAQDRETWSKKADFLLSVIGFAVDLANVWRFPYLCYKNGGGAFLVPYLFFMVVAGVPLFYMELALGQFNREGAAGVWKICPILRGVGYTAILISLYIGFFYNVIIAWALHYLLSSFTTELPWTHCNHSWNSPRCSDARAPNASSGPNGTSRTTPAAEYFERGVLHLHESQGIDDLGPPRWQLTSCLVLVIVLLYFSLWKGVKTSGKVVWITATMPYVVLFALLLRGITLPGAVDAIRAYLSVDFHRLCEASVWIDAAIQICFSLG... | 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 Activi... |
Q01959 | MSKSKCSVGLMSSVVAPAKEPNAVGPKEVELILVKEQNGVQLTSSTLTNPRQSPVEAQDRETWGKKIDFLLSVIGFAVDLANVWRFPYLCYKNGGGAFLVPYLLFMVIAGMPLFYMELALGQFNREGAAGVWKICPILKGVGFTVILISLYVGFFYNVIIAWALHYLFSSFTTELPWIHCNNSWNSPNCSDAHPGDSSGDSSGLNDTFGTTPAAEYFERGVLHLHQSHGIDDLGPPRWQLTACLVLVIVLLYFSLWKGVKTSGKVVWITATMPYVVLTALLLRGVTLPGAIDGIRAYLSVDFYRLCEASVWIDAATQVCF... | 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 Activi... |
Q9GJT6 | MSKSKCSVGLMSSVVAPAKEPNAMGPKEVELILVKEQNGVQLTSSTLTNPRQSPVEAQDRETWGKKIDFLLSVIGFAVDLANVWRFPYLCYKNGGGAFLVPYLLFMVIAGMPLFYMELALGQFNREGAAGVWKICPVLKGVGFTVILISLYVGFFYNVIIAWALHYLFSSFTTELPWIHCNNSWNSPNCSDAHSGDSGGNGPGLNDTFGTTPAAEYFERGVLHLHQSHGIDDLGPPRWQLTACLVLVIVLLYFSLWKGVKTSGKVVWITATMPYVVLTALLLRGVTLPGAIDGIRAYLSVDFYRLCEASVWIDAATQVCF... | 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).
C... |
O35899 | METTALNSQKAPSVCKDREDCQENSILQKSGPTSAGGVESGQIFNGYSSVPSTGMGDDAEHSVPTATTTLVAEVHHGERETWGKKVDFLLSVIGYAVDLGNIWRFPYVCYQNGGGAFLLPYIIMAIFGGIPLFYMELALGQYHRNGCISIWRKICPIFKGIGYTICIIAFYIASYYNTIIAWALYYLISSFTDRLPWTSCRNSWNTANCTNYFSEDNITWTLHSTSPAEEFYIRHILQIHRSKGLQDVGGVSWQLTLCIMLIFTIIYFSIWKGVKTSGKVVWVTATFPYIVLSVLLVRGATLPGAWKGVLFYLKPNWQKL... | 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 signal... |
P51905 | MDRSGSSDFAGAAATTGRSNPAPWSDDKESPNNEDDSNEDDGDHTTPAKVTDPLAPKLANNERILVVSVTERTRETWGQKAEFLLAVIGFAVDLGNVWRFPYICYQNGGGAFLVPYCLFLIFGGLPLFYMELALGQFHRCGCLSIWKRICPALKGVGYAICLIDIYMGMYYNTIIGWAVYYLFASFTSKLPWTSCDNPWNTENCMQVTSENFTELATSPAKEFFERKVLESYKGNGLDFMGPVKPTLALCVFGVFVLVYFSLWKGVRSAGKVVWVTALAPYVVLIILLVRGVSLPGADEGIKYYLTPEWHKLKNSKVWID... | 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 | METTPLNSQKQLSACEDGEDCQENGVLQKVVPTPGDKVESGQISNGYSAVPSPGAGDDTRHSIPATTTTLVAELHQGERETWGKKVDFLLSVIGYAVDLGNVWRFPYICYQNGGGAFLLPYTIMAIFGGIPLFYMELALGQYHRNGCISIWRKICPIFKGIGYAICIIAFYIASYYNTIMAWALYYLISSFTDQLPWTSCKNSWNTGNCTNYFSEDNITWTLHSTSPAEEFYTRHVLQIHRSKGLQDLGGISWQLALCIMLIFTVIYFSIWKGVKTSGKVVWVTATFPYIILSVLLVRGATLPGAWRGVLFYLKPNWQKL... | 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 signal... |
Q9Y345 | MDCSAPKEMNKLPANSPEAAAAQGHPDGPCAPRTSPEQELPAAAAPPPPRVPRSASTGAQTFQSADARACEAERPGVGSCKLSSPRAQAASAALRDLREAQGAQASPPPGSSGPGNALHCKIPFLRGPEGDANVSVGKGTLERNNTPVVGWVNMSQSTVVLATDGITSVLPGSVATVATQEDEQGDENKARGNWSSKLDFILSMVGYAVGLGNVWRFPYLAFQNGGGAFLIPYLMMLALAGLPIFFLEVSLGQFASQGPVSVWKAIPALQGCGIAMLIISVLIAIYYNVIICYTLFYLFASFVSVLPWGSCNNPWNTPEC... | 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: M... |
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 e... |
P54955 | MADKAFHTRLINMRRDLHEHPELSFQEVETTKKIRRWLEEEQIEILDVPQLKTGVIAEIKGREDGPVIAIRADIDALPIQEQTNLPFASKVDGTMHACGHDFHTASIIGTAMLLNQRRAELKGTVRFIFQPAEEIAAGARKVLEAGVLNGVSAIFGMHNKPDLPVGTIGVKEGPLMASVDRFEIVIKGKGGHAGIPNNSIDPIAAAGQIISGLQSVVSRNISSLQNAVVSITRVQAGTSWNVIPDQAEMEGTVRTFQKEARQAVPEHMRRVAEGIAAGYGAQAEFKWFPYLPSVQNDGTFLNAASEAAARLGYQTVHAEQ... | 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.
Cata... |
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.
Subc... |
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.
Subc... |
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.
Subc... |
Q9VHA0 | MSGGRDSSTSSGSNSAAPGASTNATSSASASASSTSTSASPGSTTSPASTQRQRGRPAKRATCTWCGEGKLPLQYVLPTQTGKKEFCSETCIAEFRKAYSKGACTQCDNVIRDGAPNKEFCSIMCMNKHQKKNCSTRHSGGSASGKGLAESERKLLASGAPAPTGPFQYESFHVFDWDAYLEETGSEAAPAKCFKQAQNPPNNDFKIGMKLEALDPRNVTSTCIATVVGVLGSRLRLRLDGSDSQNDFWRLVDSTEIHAIGHCEKNGGMLQPPLGFRMNASSWPGYLCKILNNAMVAPEEIFQPEPPEPEENLFKVGQKL... | 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 pr... |
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 inactivat... |
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 inactivat... |
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 inactivat... |
D4B0Q6 | MRFTQIVAAALCLGATEAAVAPIDRARKVLGNQHAFDKRDASGDTAKAPKHLTSKNKKFYVDPNSIPGVPFDIGESYAGNLANTPAGNSSLFFWYFPSENPEAKNEITIWLNGGPGCSSMIGLLQENGPFLWQPGTDGPVKNPYAWSKLTNMVWVDQPAGTGFSPGPPTVKDEIDVANQFSDFWKNFMDTFDLHHSDVYLAGESYAGQYIPYIASGMLDRKDSEYFNVQGITIIDPSIGATEVIIDAPSVPALHRFNNIIDLNETFVNDITKKWESCGYKKFMDDALKFPPAGPMTVPGKSAGCDVWDEIIAAVKEVNPC... | 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 | MHVAILLAIISLARAAPSTKGYTVATSLPGKSAFETRRLPDAPEILKNWAGRLDIPGTTIGNSLFFWLFSAEDKAYDDNLIIWLNGGPGCSSLVGAFLENGPLRFMGNSTMPERNPYSWAKLGHVLYIDQPVGTGFASEKVPVTSNKEVISNLYSWLMSFDAIFDHILRTKKVHIVGESYAGIYIPYIASEIVKRKSELPVNLVSIAIGDGTIGPNTGMSSLGMVGFLEEYASKLRIPRDIMNAISFGDHACGFDIIRQRAKVYPPRGPFHLPGRSGSANNTEISNMLQKGVADESLGSCNIHPDTPEKIRSSIVNSTCY... | 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 | MKGLLSLLLVGAANALAASYEPRSLTEDMLQGKEKEVWDAIKGEIPGAQLDDYFNPPTAHQREPDEKWDGKLEGKSVNTLWVEEGKDKPSGIEEYGMRFKTVDPSSLGVDNVTQYSGYLDNKKNGQHLFFWFFESRRDPQYDPVILWLNGGPGCSSMTSLFMELGPARVGQDLKLTRNPNSWNNRASIIFLDQPVNVGFSYGKSGAFNTPSASKDVFAFLTLFFKKFPQYALQDFHIAGESYAGHYIPFASYPPMACGKGGYSAVLDQPTCKAMEAAVPQCQKEIKRCYDKPTDVATCVKGAKFCKDALVRPYSRTGQSI... | 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 | MTYAESTRSAVVYSSIVPPPRTPVGPPMLKDGVRKGSASQPLQPKNGANSLDYWSKSEDEKSGITCYYSRHNIQFPPPQRKMKPVKPNPVGRSTINGFTPSTSSPQNGLRYPPFPQNTPESVMSPPVGIYRNIPAMPRAKLTKDEKNGGKMNRDGGGENPKNVVWGGTSRKDDDTASTPLNSFSANASIEKKRSTARRKPRWARCFQTLFCCVTPPREIEKIQSSQRTNSTNNNHQNGRPSTPTNTGPPIQLITQVHRDGTVTGLPTTGQACQQNGSGDGVTPYDKIANDSVGTINEKPLLPPLLPQDSNKKCLVIDLDE... | 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 | MMKLLFIIISIIFVINVSNSTPTLQLSGYFNVNETTNANLFYLFYESQNSPSTDPLILWLTGGPGCSSLMAAFYENGPYFVNDNLTLSENPNSWNMVANVLYVDSPLGAGFSYVVDSDGYSTTETEISENLYSFLTQFLSKYPKYSKLPLYIFGESYAGHYVPSFSYYIYQKNLGLATINLKGLAIGNGMVDPYIQYGSLGPFAYAHGMLDINALKETEGLYESCQQAIDSGDYNMTTQICNNIMDIVQEYAGNFNVYDVSKTCYPNEPLCYNFTAIIDYLNLASTKQSFGVLPNSTWNVCSTQPYSAIIRDWFNTPINY... | Function: Probable carboxypeptidase.
Sequence Mass (Da): 46858
Sequence Length: 416
Subcellular Location: Secreted
EC: 3.4.16.-
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Q54VW1 | MNIKIILLSIILIIQLLLLNNNGGIVESKINFSKRKQTDRKPNPSPKTYTKEYYDNKYLKSLKNVKQTPNDFLVTDLPGLDNGILTSFSGLLTTNETSDGNLFFWFFPANETVINPMDAPLLVWLNGGPGCSSMDSVFIETGPLRFIGDSDNSDKFYINPWSWHNSANMLYIDQPFGTGLSFVSDNDGLVTNDLEINQNFYQFIQEFFQIFSNYSTLPFFISGESYAGHYIPHMASYILNMNENLSKDSIKINLQGVAIGNGYTHPTTQINSYREFGYYATGIIGQRQYNNYENLNNLCQEQLSQGNYNSDECANVFNTL... | 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: 1.1... |
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 | MSALITHDRSTPVTGSLLPYVETPAPAPLQTQQVAGELKDKNGGVSSQGVQLPAPLAVVASQVTEGQQQEVTKLLESVTRGAAGSQLISNYVSVLTKFTLASPDTFEIELGKLVSNLEEVRKDIKIADIQRLHEQNMKKIEENQEKIKETEENAKQVKKSGIASKIFGWLSAIASVIVGAIMVASGVGAVAGAMMVASGVIGMANMAVKQAAEDGLISQEAMKILGPILTAIEVALTVVSTVMTFGGSALKCLANIGAKLGANTASLAAKGAEFSAKVAQISTGISNTVGSAVTKLGGSFAGLTMSHAIRTGSQATQVAV... | 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 t... |
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 signa... |
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.
Seq... |
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... |
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 s... |
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)... |
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/Sc... |
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 ... |
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 arr... |
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 permeab... |
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 ant... |
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 Lengt... |
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 arr... |
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 arr... |
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 conta... |
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 p... |
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 even... |
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 ce... |
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 cel... |
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 plasm... |
C8VPE5 | MATVSELCCAALNTSIGNRIAFPGSTAYNESLSSYFGVNAQLPPSCFVLPLSAQDVSVAVQTLTSQPDPCFFAIRSGGHTTSLGASAIEAGVTMDLSGMNTTTYDSSTNTAFIQPGARWGSVYETLLRDNVLVPGGRTASVGVGGYLTGGRNSFHAARVGLACLSIKGYEIVLADGEVAKVDQDSHPNLFRALKGGSNNFGIVTLFDMEAFSTEGTIWGGTVLYDISTKDQYIAAGTAFTDNIPNDPYASWVGMFAYNSTTDQTAIFTSLAYTRPVQSWPQAFSEFYAIPNITHTLRSATVLDLAVENSFPYGYRNVLQT... | 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 methylatio... |
Q2FWY4 | MAYFNQHQSMISKRYLTFFSKSKKKKPFSAGQLIGLILGPLLFLLTLLFFHPQDLPWKGVYVLAITLWIATWWITEAIPIAATSLLPIVLLPLGHILTPEQVSSEYGNDIIFLFLGGFILAIAMERWNLHTRVALTIINLIGASTSKILLGFMVATGFLSMFVSNTAAVMIMIPIGLAIIKEAHDLQEANTNQTSIQKFEKSLVLAIGYAGTIGGLGTLIGTPPLIILKGQYMQHFGHEISFAKWMIVGIPTVIVLLGITWLYLRYVAFRHDLKYLPGGQTLIKQKLDELGKMKYEEKVVQTIFVLASLLWITREFLLKK... | 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 | MIKKNNLLTKKKPIANKSNKYAIRKFTVGTASIVIGAALLFGLGHNEAKAEENTVQDVKDSNMDDELSDSNDQSSNEEKNDVINNSQSINTDDDNQIKKEETNSNDAIENRSKDITQSTTNVDENEATFLQKTPQDNTQLKEEVVKEPSSVESSNSSMDTAQQPSHTTINSEASIQTSDNEENSRVSDFANSKIIESNTESNKEENTIEQPNKVREDSITSQPSSYKNIDEKISNQDELLNLPINEYENKVRPLSTTSAQPSSKRVTVNQLAAEQGSNVNHLIKVTDQSITEGYDDSDGIIKAHDAENLIYDVTFEVDDK... | 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): 102... |
Q99S97 | MRLKSIITVIALILIMFMSAIESSIISLALPTIKQDLNAGNLISLIFTAYFIALVIANPIVGELLSRFKIIYVAIAGLLLFSIGSFMCGLSTNFTMLIISRVIQGFGSGVLMSLSQIVPKLAFEIPLRYKIMGIVGSVWGISSIIGPLLGGGILEFATWHWLFYINIPIAIIAIILVIWTFHFPEEETVAKSKFDTKGLTLFYVFIGLIMFALLNQQLLLLNFLSFILAIVVAMCLFKVEKHVSSPFLPVVEFNRSITLVFITDLLTAICLMGFNLYIPVYLQEQLGLSPLQSGLVIFPLSVAWITLNFNLHRIEAKLSR... | 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 ... |
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-hel... |
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-hel... |
Q6FIY2 | MKFHTKLYKVGYPLYGAKFVCDDQFVVTGGGGEGNNGVDNKLTVLKVGSSEGNGLRVDEVCDATLPANDDSPTALDAVGDTILIGCNENSAKVKSGAGNSHVRKFRYDGKSLKFESAADIDKSTNPEDYTKVIRLSKDGSEAAIASSKNPPSMAIIDPRNYSVKYEIETGRDVKDLHFSPNGKLIGYITESSLEIISTVTGSCVVRKTDFDRKIILSKMKFLDDNNVLIAATWASSKGILLTKISIKSGKTTVFWSRQISSKFKGITAMDVNDQMNLVMLATNDNSVLLVKLRNLSVGKTFTQVHGFAITRVIFSPDSRY... | 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: Singl... |
P11655 | MKFVTASYNVGYPAYGAKFLNNDTLLVAGGGGEGNNGIPNKLTVLRVDPTKDTEKEQFHILSEFALEDNDDSPTAIDASKGIILVGCNENSTKITQGKGNKHLRKFKYDKVNDQLEFLTSVDFDASTNADDYTKLVYISREGTVAAIASSKVPAIMRIIDPSDLTEKFEIETRGEVKDLHFSTDGKVVAYITGSSLEVISTVTGSCIARKTDFDKNWSLSKINFIADDTVLIAASLKKGKGIVLTKISIKSGNTSVLRSKQVTNRFKGITSMDVDMKGELAVLASNDNSIALVKLKDLSMSKIFKQAHSFAITEVTISPD... | 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 m... |
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 co... |
Q4P9K4 | MAQPPPQLPPGWVAQWDPNAARQVFVETATGRTSWQPPTAGPAGVAPPQQHQQRPTHPQGQARMSMPQIQPPPGMRGPSLSPISQHGPGAPVSPPSAGSPAPASIGPGASRRRAYPTAHLAANSISYAGGYDASTATGAGVAYPGAQDAQPQLFTPGAPDLTPSPYGAAAQPALGAPGLAPAPGAHGAPGVGPAPGYAAGGVQGITNQFQAMGVGGGVAGGMGQKFSTLQTVNISGVQPNVNDLERPPPEIRLPPNACVSTNPKANADPSYQRCTLNAVPTTSSLLQKSKIPLGLILSPYRSVREADGDEPVPVVTDTVI... | 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 ... |
Q6C2T4 | MSQEHPEQGSSSKRRVYPQQQYDFAAAQPAGYSMPDPTQPYGASASPSAAMYGGAHAIPSPAAFQPHTANVQSGAFAPPPGTPGSAVDPPVAPGVAGGMAYGAPQAAGAAYGYQGLTNQMGNLNIGGGGAYQGGAPPGAAGGAHMAAPTQLNQIYNTDLLQNFPPPISDLTLPPPPVILPPGSSVTGNPDPNADSEFMRCTLNTVPTSSSLLKKSKLPFALVIRPYTALRDADENVPTVADTTIARCRRCRSYINPYVVFLEGGARWRCNMCNLTNDVPSGFDYDAVANKPRDRWSRAELNHSVVEFVAPAEYMVRPPQP... | 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 ... |
P40482 | MSHHKKRVYPQAQLQYGQNATPLQQPAQFMPPQDPAAAGMSYGQMGMPPQGAVPSMGQQQFLTPAQEQLHQQIDQATTSMNDMHLHNVPLVDPNAYMQPQVPVQMGTPLQQQQQPMAAPAYGQPSAAMGQNMRPMNQLYPIDLLTELPPPITDLTLPPPPLVIPPERMLVPSELSNASPDYIRSTLNAVPKNSSLLKKSKLPFGLVIRPYQHLYDDIDPPPLNEDGLIVRCRRCRSYMNPFVTFIEQGRRWRCNFCRLANDVPMQMDQSDPNDPKSRYDRNEIKCAVMEYMAPKEYTLRQPPPATYCFLIDVSQSSIKSG... | 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 recrui... |
Q5AL49 | MSSQADYDKRLAEEVGSLSTRLVTAVNKQVELEETILELRKQVSALKLKNEQLNQSDIKLKTILPKYIKLQDDYRETLTKKKEAESQNTKLQGEVEDLTASLFDEANTMVSNASRETHNFKIKNRKLYEELDEKNIIINDLQEQLQDLKQMFIKMEEQSKIQSYSQSNTPKIESSTDFNETNSIHTNTNFSESKLSKYNTRSTLGDEESQNYNLQQLQRIIYSPLITSIRFDLNNYNIDFKGFVYQLIKPDFQFDLSHLKTIPFFKSIWQSEIENCIHYIPSLPATTTLLNRWQKGKTFWGSLIEGKVSIEPIKGSNETF... | 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-... |
P17065 | MDASEEAKRVSIQVTSLSTQLIESVDKQSHLEEQLNKSLKTIASQKAAIENYNQLKEDYNTLKRELSDRDDEVKRLREDIAKENELRTKAEEEADKLNKEVEDLTASLFDEANNMVADARKEKYAIEILNKRLTEQLREKDTLLDTLTLQLKNLKKVMHSLDNESTVTNNSNRYSTILSDSATSSSTSLNKVPTSYSLASQDIYSGIVYSPSISSIRYDISLYNEFLKFVAALPRCENIKATSTESKLIRRLVNDEIQPILKIDNASGIGWLVKKTLLSLIIDGLVVVEPLSGVNATYQIGYNSSSPAKQATSNMPKMFK... | 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.
Se... |
Q2YAJ4 | MSKALLAAWRINSLAPAPYPERLDTNDNALDRFLGSSLGQARLWASHLRLKRLRSFADKVVHRSNALSALSEAELAACVDDLRVKLARQGLTEDLTIEVFSLVREVCGRKLGLRHFPVQLIGGRVILAGKLAEMQTGEGKSLTAVLPAIAVALSGLPVHVITVNEYLVRRDARFMRPVYEFFGLDVGMVVPDQDPETRRNAYGCDVTYCVNKDLVFDYLRDRIDSNRDVSDARRAVARLFRGDENSRAYLRGLFFGIVDEADSVLIDEARTPLIISSSVSDKQGVDDYRRALDFCRQLRDGLHFRIFAADKLIQLTPAGR... | 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 mo... |
Q03HZ9 | MEFNLDNFRLRKYSKITKKILALGKKYQTLTDDQLRIKTETLRNKLVKGASLDSILIEAYATIREADFRVLGLKPFENQVLGAVVLHYGNVAQMNTGEGKTLTATMPLYLNGLTGPGNFLVTVNSYLANRDAEEIGKVYKWMGLTCASGVSLDDEELDKKAIYQNDIVYTTNSELGFDYLTDNLVDNINKKKLNDLNFALVDEVDSVLLDLAQTPLVISGAPRVQSNLFVSTDRIVKSLKPNVDFEFSEDLKDVWFTQTGIEQLEEYLGIQGLISDKWSDFYRHLVLALKANYVMKRNQDYIVTNREVLLLDSENGRALT... | Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide c... |
Q7UWI5 | MRRSSDPSANKKKWTKASNWRPRMVRWQRQLARVNALESTLQAEDDQTIRKRSLALRYRAMAGEKLSELLPEAYALCREAGRRSLSMRHYDVQILGGIALFEGHITEMQTGEGKTLTATLPLYLHSLVGKGAHLATVNDYLAKRDAEWMMPLFEMLGVSVGIIQTEDDQGGRRKSYGAAITYGTAKEFGFDFLRDRLLLRAQNRMQTEMLGSGDGGFSNSGDQVVMRGMHFCLVDEADSILIDEARTPLIIGSIEDTVRDQIIETYKWAAENAPLFELDEHFEIDDETKRYELTARGRSKVRALPKSDLVRTMGLVDMYE... | Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide c... |
Q5LPY3 | MSDTFPGQAPGAFYPRAPAEPAKSKLDRWIEKYTTLPRRRRRARPSRFFAWRVLRRGKAFAQMSDDRLQGEVRAAAYGMRAARAHPGEALLVRSFALIRECAGRELGQRHYATQILGARAVLNGAVAEMQTGEGKTLAITLAAGTAALAGRRVHVITANDYLAGRDADTMRGLYARLGLTCAAVEPGCTPEERRAAFAADIVYASGKEVAFTFLRDRVAMGGRAGDIGLRTRAFFDGTGLLLPGLQFAIVDEIDSVMIDEARTPLILSVPPADAEVEAEAARAAHAIAAELKEGRDYRLDRLRHAVELSRNGCDRLADLA... | 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 mo... |
Q8CMU9 | MAKGVNQIINNIRLRKLRKILNQINALSEEFSNFSDEALQAKTKEFKVYLNDNKASLNHILPQAYATVREASKRVLGMYPKDVQILGAIAMHQGNIAEMQTGEGKTLTATMPLYLNALTGKGAYLITTNDYLAKRDFLEMKPLYEWLGLSVSLGFVDIPEYEYAENEKYELYHHDIVYTTNGRLGFDYLIDNLADDIRAKFLPKLNFAIIDEVDSIILDAAQTPLVISGAPRVQSNLFHIVKKFVETLEKDKDFIVNFNKKEVWLTDEGSEKASHYFKVNSIYQQQYFDLVRMIHLSLRAKYLFKYNLDYFIFDGEIVLI... | Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide c... |
Q83F06 | MLGNIIKKAFGTRNERLLKGYSKIVSRINALEPEIQALSDADLRAKTDEFKKRLVDGEGLDALLPEAFAVVRETSVRTLGLRHFDVQIIGGLALHGGKIAEMRTGEGKTLGATMPAYLNALTGKGVHIVTVNDYLAKRDAEWMKPIYEFLGLTVGVNVPGMEPVEKQAAYAADITYGTNNEFGFDYLRDNMVFDLDQRVQRPLHYAIIDEVDSILIDEARTPLIISGQAEESSDLYVKINKFIPQLKLQKMEEGQKEEEVPPENRGDYTLDEKNRQAYLTEQGHRTIEALMIKQGLMQAGESLYDVSNISLMHYVYAALR... | 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-Sec... |
Q85G35 | MKNKLRQIKENREKYRKLKEEELREKTKQLKERAKQESLEELMVEAYSNVWEGAARVLKLEAYDVQLIGAMVLNKGQIAEMKTGEGKSLVAAFASYLNALSGKGVHIVTVNDYLAKRDERWIGEVLRYLGLKTAVITNESSREERKKGYEADVTYITNSELGFDYLRDHMAWSKEEIVQREFNYCIIDEVDSILIDEARTPLIISGPTKGSEKPYKVAWEIGKRMKEGEDYELEEKSKQVILKEKGIKRCEEALEVKDIFSMETPWAHYVMNAIKAKHFYIKDVNYIIKEGEVVIVDEFTGRIMGGRRWADGLHQAIEAK... | 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
Subce... |
Q3Z9C1 | MFKFFSGFGDSNEKEIRALEPLVDKINQLESSFSALSDEALKAKTAEFKERLKETFETTASAILKDIAGTTAELEEAQKTADNSKQSRLKAKLESLNKDLSVKENAALNAILPEAFAAVREASRRTIGLRHYDVQLIGGMVLHHGKIAEMRTGEGKTLVATLPLYLNSLLGKGVHLVTVNDYLARRDAYWMGPVYHALGVSVSSIYPMQTPTEELPSRLFDPTYTSETPNDPWMHFRPISRQEAYKADITYGTSTEFGFDYLRDNLRPDLAQCVQREMNYAIVDEIDNLLIDEARTPLIISAPDTEAGKLYEVFARLAPR... | 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 ... |
Q9RWU0 | MFRVLNKVFDNNKRDVERIIQTVVKPVNALEEETMRVENLAEAFMDLRRRVQDGGESLDSLIVPAFALIREAGRRSIGKRHYDTQLIGGAALHQGRIAEMRTGEGKTLVATLALAFNALEGKGCHLVTVNDYLARVGMEEMGLLYRTLGLTVGLANRELSPAEKQAAYACDITYVTNSELGFDYLRDNMAQSKEALVLRADTPLHYAIVDEVDSILIDEARTPLIISGAAEKATDLYYVFAKLIRRLQKGEPAEPGVRTEPTGDYTIEEKSKAVHLTEQGITKIERLLSLKDLYSPENMDKAHMITQAIRARELYHREKD... | Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide c... |
Q9JYK8 | MLTNIAKKIFGSRNDRLLKQYRKSVARINALEEQMQALSDADLQAKTAEFKQRLADGQTLDGILPEAFAVCREASRRTLGMRHFDVQLIGGMVLHDGKIAEMRTGEGKTLVATLAVYLNALAGKGVHVVTVNDYLASRDAGIMEPLYNFLGLTVGVIISDMQPFDRQNAYAADITYGTNNEFGFDYLRDNMVTDQYDKVQRELNFAVVDEVDSILIDEARTPLIISGQADDNIQLYQIMNTVPPHLVRQETEEGEGDYWVDEKAHQVILSEAGHEHAEQILTQMGLLAENDSLYSAANIALMHHLMAALRAHSLFHKDQH... | 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-Sec... |
A1SGL9 | MPAILDKILRIGEGKILRQLEAIAQAVNAIEDDFVAMSDAELQGMTAEFKERLANGESLDDIMPEAFATVREAARRVIGLRPFDVQVMGAGALHMGNIAEMKTGEGKTLVAVLPSYLNALSGKGVHIVTVNDYLAKFQSEMMGRVHHFLGLTVGVILPEMRPDERRVAYNCDITYGTNNELGFDYLRDNMAGSIEECVQRGHNFAIVDEVDSILIDEARTPLIISGPTQDEVHWYAEFAKVARNLVRDEDYEVDEKKRTISVLEPGITKVEDHLGIENLYESANTPLISFLHNSIKAKELFHNDKEYVVLNGEVLIVDEH... | 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 ... |
Q313L3 | MLGSIVKKVFGSKNDRYLKSLNHYLKEINALEENIATMPDEAISARMAELRAEVQQGTSLDSILPEVFAMVREAGKRVLGMRHYDVQMVGGIALHSGKIAEMRTGEGKTLVATLPAALNALTGKGVHLITVNDYLARRDAEWMGKIYNFLGLSVGVIVHGLNDEERRAAYASDITYGTNNEFGFDYLRDNMKFYKEQLVQRPHHFAIVDEVDSILIDEARTPLIISGPSDESTGLYRRVNDIIPRLKRDTHYTVDEKARAAALTDEGVQEAEKLLGLDNLYDPQNISFQHHILQALKAHSIFTRDVDYIVKDDQVVIVDE... | 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 ... |
Q32743 | MFNFLENEKYKLKEYQPLVNQINLLETSVKNYTDIELKEQFDKLRKEYFLSQNFSNDIIARSFSLTREAAFRTIGLRPFDQQLLGGLVLNSGKITEMKTGEGKTLVATLPAALNAISGRGVHIVTVNDYLAKRDSTWMGQIYDYLGLTVGLVQSQMESQERKDNYFQDITYITNSELGFDYLRDNQVKTFQEMVQRKFNYCIIDEVDAILIDEARTPLVLSIPDTIHNPKIYLDANTTAKSLIRDVDFKADEKTKNITFTDIGIDKIEYFRKIPNIYGTNAGFLFYLQNAISANIFFRKNSEYIIENNKIAIVDEFTGRV... | 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
Subc... |
P47994 | MGFLTKIVDGNKREIKRLSKQADKVISLEEEMSILTDEEIRNKTKAFQERLQAEEDVSKQDKILEEILPEAFALVREGAKRVFNMTPYPVQIMGGIAIHNGDISEMRTGEGKTLTATMPTYLNALAGRGVHVITVNEYLASSQSEEMAELYNFLGLSVGLNLNSLSTEQKREAYNADITYSTNNELGFDYLRDNMVNYSEERVMRPLHFAIIDEVDSILIDEARTPLIISGEAEKSTSLYTQANVFAKMLKAEDDYNYDEKTKSVQLTDQGADKAERMFKLDNLYDLKNVDIITHINTALRANYTLQRDVDYMVVDGEVL... | 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 ... |
P0AG95 | MAQEYTVEQLNHGRKVYDFMRWDYWAFGISGLLLIAAIVIMGVRGFNWGLDFTGGTVIEITLEKPAEIDVMRDALQKAGFEEPMLQNFGSSHDIMVRMPPAEGETGGQVLGSQVLKVINESTNQNAAVKRIEFVGPSVGADLAQTGAMALMAALLSILVYVGFRFEWRLAAGVVIALAHDVIITLGILSLFHIEIDLTIVASLMSVIGYSLNDSIVVSDRIRENFRKIRRGTPYEIFNVSLTQTLHRTLITSGTTLMVILMLYLFGGPVLEGFSLTMLIGVSIGTASSIYVASALALKLGMKREHMLQQKVEKEGADQPS... | 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: 3... |
B2KBZ0 | MMNLIPKTNFDFLKIRKYFYAVSAIILIAGLICILTRGLNMGIDFKGGTMVQVQFTESITIDQVRSAVEKYNPEIQSYVGKNTYMIKIKGSQENVNEVRSDVETSLTAAKLKFTVVATDFVGPTVGKDLGERALWALALSLVFMVLYIAFRFQNIIWGTAGVIALIHDAFFMVAAFAFLQKEFDLVIVAALLTAVGYSINDNIVIFDRMRENIKENPKESFYNIVNRSLNETLSRTVITGSTVLIVLVIIYFFGGEVLKNFSLIMLIGVIVGTYSTLFIATPIVYDWAKDSDNFAKTVGNQDVALAAEIKTAKKHNKKKH... | 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: 3... |
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: 3... |
C1A8P3 | MLRIFHNTKYEFVRWWRVAAGLTLAFIAAGFVSFAVTGGVNYSIEFTGGTLMQLQFKTPPDVAEVRSALDAAGIQGAEIQQFGANTDFTIRARDEKQVEAQDAGAEGISRQITAALDAKFGAGTVTIVRTEAVGPKVGAELRTGAAMAMLIASIFTLIYLAIRFDWRFGLAAVLSTTHDILITLAFIKIFHIEVSLTVVAAILTLVGYSANDTIIIFDRVRENLKKPHKGETLSHILDRSINETLPRSIMTHTTTFSATLALLLLAGEVIRPFAWVMAFGVVMATFSSIYVAGPLLLWIEGRWPRLDDAATARAVRAGEA... | 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: 3... |
D4GTK4 | MVEFTVPEVDYTRYTNRQLAAVPLAVLAVALLVIGGWYVATGAPVNPGVDFTGGTELRIATDAPQSEVAAAFDSQPESIRSVAADGTYVVTFQSGSATSTELQTQAEDAGFEVRSIDAVSANFGGETQLLALGGLAVAFAGMSVLVFAMFRSFVPSIAVVLSAFSDIVIPVALMNLFGIELSLGTVAALLMLIGYSVDSDILLNNHVLRRSGDFYESTARAMRTGVTMTLTSIAAMIVMTIMATLFGIQLLAAIGTVLVFGLTADLMNTYMLNVTLLRWYKFEGVTR | Function: Involved in protein export.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 30425
Sequence Length: 287
Subcellular Location: Cell membrane
|
O26073 | MELFKRTRILSFMRYSNYGVIVSAILALLALGLLFFKGFSLGIDFAGGSLVQVRYTQNAPIKEVRDLFEKEARFKGVQVSEFGSKEEILIKFPFVETAENEDLNAIVANILKPSGDFEIRKFDTVGPRVGSELKEKGILSLILALIAIMVYVSFRYEWRFALASVIALVHDVILVASSVIVFKIDMNLEVIAALLTLIGYSINDTIIIFDRIREEMLSQKTKNATQAIDEAISSTLTRTLLTSLTVFFVVLILCVFGSKIIIGFSLPMLIGTIVGTYSSIFIAPKVALLLGFDMDKYYENETRKIKKAQEKEKMRRLYES... | 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: 3... |
E3F0U0 | MAFRLKLVPDKTSVNFFKWGGIPTHATFALALASLIAVMTIGLNYGIDFLGGTTIRAESSENVAVSEYRSALDQIELGDVTITEVFDPGFRADQFVKQVRIQAANETEVSNALIGQVEAALQVVDPQVVFTAVETVGPKVSGELIQTAVLAAVLAVAASLLGIMAYVWLRFEWQFGFGAVVGLFTDAMITVGLFSVFQVRFDLTIVAAVLTIVGFSINDKVVVFDRVREILRRDSTTPLPELMVVALNETLSRTVMTTVTTILALVALYIWGGDVIRGFAFAMLFGSVIAVYSTIFVSAQVVLWLGVKRDWEKKTDTGPS... | 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
Se... |
Q1IVE8 | MELFRNTNIDFLGKKWYFLAFSLVFSVAGLISMGARYAKTGTAVPLGVDFKGGTLVYVKFAQTPNLGDIRAAMDRSGLKDPKIQTYGGPANNEVLIALEQKETSEQALDAGKNTIIKALETNPASGKNDLNNVGSTTIRDYLMSKDPLHEVVDPGAKYQQIASQIVDYRDKERGGVLSSVDELQGHVPADVVNALKTDYFTSGFGVRNVEIVGPQVGKQLSNQALLATLYSLGGMLVYLWFRFELIYGIGAVVACFHDTIITVGAFSLLNRDISLTVVAAILTLIGYSMNDTIVVYDRIRENIKLLRRESLADIVNKSIN... | 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: 4... |
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: 3... |
Q58650 | MIKDYKVSIAIPIALLILSILLIGFKGIPKSIDITGGTEITIKVNENMDITPLKESLNGIAEVKKLESADGYYIVIRCKNEDVDIVKQKIKEFFHVDSLDKLNYSEKTIGATLSSKFFEEGFKAVGFAFMFMAIVVYLYFRNPVPSGAIILSALSDIIMALGAMSLLGIELSSATIAALLMVIGYSVDSDILLTTRVLKRLTKSFDETVKEAMKTGLTMTLTTITAMLILLIVVKLFIPVADILANIATVLILALIADIINTWLLNAGILKYYITEYRAKKI | Function: Involved in protein export.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 31029
Sequence Length: 282
Subcellular Location: Cell membrane
|
Q8TWM5 | MGLFEKYVSNLNRLLILTMVFAVICAGSTLALGVKKGIDLKGGTMVILKTEKDPDTVTSEASRILGVSDVEAIRSSQGDVIVQVPKYLSADDVNKLARAVGGEVESVQTIGPALGRVFWESVKVAVPLALVAVSIVVFAIFRKPLLSAAVLGALALDLVDALGLMALTGVPLTLASFAGLLMIIGYAVDSNILLSMYTVKRRRVRRVDRAIADSFKTGITMVATTTAAACALFLLSMSEAMFEIAAVVIFGLIADVLNTWIFNAWVIREKIAGR | Function: Involved in protein export.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 29148
Sequence Length: 274
Subcellular Location: Cell membrane
|
E1RHR2 | MGKFTYDINRYEPKQMVALPLCLLILSVIFLAFNTVSTGMPVEPGIDFAGGVAVTLSTSDSVDVIEDYFADYPLKISESDVAAGYLVFNYLEGDSFKDLTEHITARYPDATIYQMGETFGKTLQSQAIWALLFAFVLMAIVVFVAFRIFIPSVAVVLSAFSDIVITAAFMDVFGLTLSLGTTAALLMLIGYSVDSDVLLTTRLLKRQGKVDEKFRGAFRTGIIMTTTTLAAVVVMFIVFSLGQVTLIRDISAVLIIGLIIDMMNTWMLNAGLLKWYVKKGGK | Function: Involved in protein export.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 30925
Sequence Length: 282
Subcellular Location: Cell membrane
|
O26936 | MGETLKVIVLIDRILKSYRPLIAIPAAITVIALLLVVFNGLNESVDLKGGALAELTLEKSVTQAELESLLREKLGTGDIKVLSIRGERVTVQFGTDMDVVKVSEALRGTATINSYKAVGPVLSKQAMNQIYWAIGFAFLFMSVTVFIIFRDPVPSLAVILAAASDIIIAVGGMSLFGIPLSLASVGAILMLIGYSVDTDILLTTRVLKRRKGTINERALGAMKTGVTMSIAAIASMAALYLVTVFVMPEARVLSDIAAVLIIGLLADILTTWLMNLGILRWYLEVRS | Function: Involved in protein export.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 30839
Sequence Length: 287
Subcellular Location: Cell membrane
|
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 ... |
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