ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q4KFR2 | MTGLFITLEGPEGAGKSTNREYLAERLRAAGIEVLLTREPGGTPLAERIRDVLLTPVEEVMNADTELLLVFAARAQHLATVIRPALERGAVVLCDRFTDSTYAYQGAGRGLSLARIAALEDFVQGELRPDLTLVFDLPVDVGLARASARGRLDRFEQEGQAFFQKVREAFLARAAAAPQRYVLVDAAQPLAQVQQSLDSLLPQLLERARG | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Mass (Da): 22912
Sequence Length: 210
EC: 2.7.4.9
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Q83HB8 | MFVTFEGIDGSGKTAQLTAAGEFLKASGKQVVLTREPGTISCIRDYVLASDMDIRTEALLYSADRAENIAKNVIPALNAGKVVLQDRYLDSFLAYQLADNKLVETDIMRLFEFSSQGLRPDLTLLFDLTPACAQERLENRDRIERKPIDFHSKVRNIYLKLSADNTDRIRVIDASQSFSKIHQQVIYHIERKLGGTHSA | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Mass (Da): 22381
Sequence Length: 199
EC: 2.7.4.9
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B1AI06 | MILTKNSNEKKPLKKGLFIVFEGIDGAGKTSILKQLLEVLKEPKLVNKIFLTREPGGKNNNAAEMIREFFLKNLEVFDPLTLAYLYASSRAEHVKKTINPHLEKDHIVISDRFVHSSYIYQGIVQNQSLDVIYQINQQAIGELEIDYVFYFDVNVNNALNRMKNRFDNTNAFDSQNKQFYEKLLKQYPSVFKVYNQPKKIIFIDANKNENEVLCEVKEQLLKIFKEHKYI | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Mass (Da): 26900
Sequence Length: 230
EC: 2.7.4.9
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P0DSV5 | MSRGALIVFEGLDKSGKTTQCMNIMESIPTNTIKYLNFPQRSTVTGKMIDDYLTRKKTYNDHIVNLLFCANRWEFASFIQEQLEQGITLIVDRYAFSGVAYATAKGASMTLSKSYESGLPKPDLVIFLESGSKEINRNVGEEIYEDVAFQQKVLQEYKKMIEEGEDIHWQIISSEFEEDVKKELIKNIVIEAIHTVTGPVGQLWM | Function: Poxvirus TMP kinase is able to phosphorylate dTMP, dUMP and also dGMP from any purine and pyrimidine nucleoside triphosphate. The large substrate specificity is explained by the presence of a canal connecting the edge of the dimer interface to the TMP base binding pocket, canal not found in the human homolog.
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Mass (Da): 23378
Sequence Length: 205
Pathway: Pyrimidine metabolism; dTTP biosynthesis.
EC: 2.7.4.9
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A5CXH6 | MQRGKFITIDGVEGAGKSTQIDFICSYLAKKNINVVLTREPGGTKLGEKIRALLLSIDTQLMDNDTELLLIFAARNEHIKTKIIPALNRGDWVLSDRFTDASYAYQGGGRGLSIERIALLEQWVLQDFSPDVTLLLDVPVALGMLRIKSRSRKDRIELETNDFFNRVRDSYIKRSKQFPERIKLIDASQTLKETTQQIKVILQAL | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Mass (Da): 23267
Sequence Length: 205
EC: 2.7.4.9
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Q09JW6 | MRLLALFAFAVAVVSAQRNQMCQQPRTQGSCDASNQITKFFYTGSGCTSAPVCSDTDGGYGTEDECIQACTVQGGHHNEGAGEEGCSGDPPRGDCGGQVEERYYFDSTTRTCQTFEYRGCSSGNPDNSYETEIECEIACPSASS | Function: Tick salivary thrombin inhibitor that plays an important part in the anti-hemostatic strategy of ticks.
PTM: The N-terminus is blocked.
Sequence Mass (Da): 15352
Sequence Length: 144
Subcellular Location: Cytoplasmic vesicle
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P56409 | LNVLCNNPHTADCNNDAQVDRYFREGTTCLMSPACTSEGYASQHECQQACFVGGEDHSSEMHSSCLGDPPTSCAEGTDITYYDSDSKTCKVLAASCPSGENTFESEVECQVACGAPIEG | Function: Tick salivary thrombin inhibitor that plays an important part in the anti-hemostatic strategy of ticks (Probable). Is a potent and highly selective thrombin inhibitor (Ki=10 pM) .
Sequence Mass (Da): 12632
Sequence Length: 119
Domain: Has two domains of the BPTI family. The N-terminal domain bind to the active site of thrombin, the C-terminal domain binds at the fibrinogen recognition exosite.
Subcellular Location: Cytoplasmic vesicle
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Q09JW3 | MEGKVLLCFALLLPFTVAQAAKGDTRRCGYLMMQRCRGDTTETKAWGFNYEEKKCQKETVICGTGGAPRNAFETKKDCDALCKGYSGPQYSMQEMLQHIRDNAKKTG | Function: Tick salivary platelet aggregation inhibitor that plays an important part in the anti-hemostatic strategy of ticks. Inhibits platelet aggregation induced by ADP (IC(50)~150 nM), collagen, and platelet activating factor (PAF) . Acts by binding to platelet membrane glycoprotein IIb-IIIa (ITGA2B/ITGB3) in a metal ion dependent manner . Does not inhibit aggregation induced by ristocecin, an agonist that aggregates platelets independently from the glycoprotein IIb-IIIa (ITGA2B/ITGB3). In contrast to other tick platelet aggregation inhibitors, this protein does not protect ITGA2B/ITGB3 from dissociation under SDS condition, suggesting it may dissocate much faster than its orthologs .
PTM: The N-terminus is blocked.
Sequence Mass (Da): 11970
Sequence Length: 107
Subcellular Location: Cytoplasmic vesicle
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Q8G6U3 | MGCLDVRFCRIIFALYSLIRKYGAWLVIPAMLGGAAFLADSVLTPAVSISSAVEGLKTLPALEHLFTENKDLTMMITAVIIVILFAVQSRGTESIGKVFGSVVMVWFAFLAIVGVVAIGNDWSVLAALNPYYGIKFLFSPNNATGLALMGTVFLSTTGAEALYSDMGHVGRGNIYFTWPFIKVALVLNYFGQGAWMLHNQNNPELADAEGINPFFQMMDPNVRYVAVVLSVTAGIIASQALITGAFTMVSEATGLNWMPHLQVCYPARTRGQLYIPVVNVVLCVATLAVLLLFRDSEHISAAYGLALTITMITTTILLGIYLWHRSNKFGAVVFTIVFLAIQVLFFAASMAKFLHGGWFTLLLTLAILMIMYTWNEGTKLERSQRRHMMPKDFLPALDKLHGDSRIHRFADNIVYLTSDPDLKRLDTDIFFSIFADHPKRARAWWAVAVETTDEPFTREYSVESFGTDYLFRVRIRLGFKVSQSIPAYLHQIMHDLEKTGELPNQQSIYPKLDADPGIGTIRYVVIHKALMPESKVSGRGALSLQIKYAIRRVAGSPVKWFGLAPYNPLVEVQPLFVSTRRPPRLTRVASQAPKREG | Function: Transport of potassium into the cell. Likely operates as a K(+):H(+) symporter.
Catalytic Activity: H(+)(in) + K(+)(in) = H(+)(out) + K(+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 66382
Sequence Length: 597
Subcellular Location: Cell membrane
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Q89NN6 | MPIDRRAGSVKRRRIKFRDEAFSIHMTASITSTETQEGPVTSGFWALTLGSIGVVFGDIGTSPLYAFHEAVRGAAHGEPVTRVMVLGVLSLILWALLIVVTAKYVLLLLRADNNGEGGTLSLMALGQRALGRRSWFLLALGVVGASMFIGDSMITPAISVLSAVEGLKLATPALEHYVVPLTVLILVLLFAVQSKGTALVASAFGPVMVVWFTCIAVMGAVHIADDPSVLAAINPYYALQFLLSHGTIGLVTLGAVFLAVTGGEALYADLGHFGRKPIQAAWMFFVLPSLLINYFGQGALVLSDPSAIEHSFYRMVPEHLVLPLVGLATAATVIASQAVITGAYSLVYQAVQLGLLPRFEVRYTSESHAGQIYLPRVNRLLLIGVMLLVLLFHTPSNLASAYGIAVSTTMVADGIMGFVVIWKLWNWRAATAAAVILPFVVVDMSFFSANLLKLLEGAWVPLLFGAAMAGTIWTWRRGSGILIQKTRRIEVPLDDLIRSLEKRPPHIVKGTAVFLTSDPSFVPTALLHNLKHNKVLHEHNVVLTIETAHTPRVDLSERFRMEKISDKFSKVRLRFGFMEQPNVPKALAIARKQGWQFDIMSTSFFVSRRSLKASAQSGMPLWQDHLFIALSRSANDATDYFQIPTGRVVEVGTQVTI | Function: Transport of potassium into the cell. Likely operates as a K(+):H(+) symporter.
Catalytic Activity: H(+)(in) + K(+)(in) = H(+)(out) + K(+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 71563
Sequence Length: 657
Subcellular Location: Cell inner membrane
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A5EHA3 | MGLRPLMVGALGVVYGDIGTSPLYTMKTALEWAGGADAETALGMLSLIVWTLLITTSIKYVAVVMRADNDGEGGILALMSLLGIKHGERLGVIAMGLIGAALLYGDGAITPAISVLSALEGLKSPLPQISPYIVTLSAIILVGLFALQAQGTDRIGKLFGPVMIAWFIVIGILGLFGILRHPSVLAALDPRHGLSYLFSHGMTGFLVLGAVFLCATGAEALYADMGHFGARPIRFAWYGLVLPCLILNYAGQTAVVVDAALGQEPNPFFALCPAALQLPLVALATVATIIASQAIISGAFSMTRQAIQLGLCPRLNIAQTSATGYGQIYIGFVNWTLMALTLGLTLGFRSSDNLAAAFGIAVSLTMLLTSILMFLTMREIWKWNLAASLLTAGLFVVVDMSFVSANLMKVLEGGWFPLVVAAVIFFLMMTWHQGRDLLVKKLERDTLPLATFIAQVGAKTRVPGTAVYMTSRLDVVPVPLLHNLKHNKVLHDRIVLLRVVTASTPRVAPDLRIDVEHVGSNFHTMTVRYGFMEQPDVPEALDQCRQRGLIFNMMETSFFVGRVKIVAERRSRFAAFQAHLFEIMHRNAMAATEFFRIPPNRVIELGGQVEI | Function: Transport of potassium into the cell. Likely operates as a K(+):H(+) symporter.
Catalytic Activity: H(+)(in) + K(+)(in) = H(+)(out) + K(+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 65995
Sequence Length: 611
Subcellular Location: Cell inner membrane
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A4YN81 | MNANLAHQPPQGRLSLLALSALGIVFGDIGTSPLYTFKTILGTGGQPTGAAAVLGALSLVIWTLFIITTVKYVMFAMRVDNDGEGGILALMALLGVKRQRRPTIVALGLFGAALIYGDGAITPAISVLSALEGLNMAAPALQPYVVPAAVVILLALFAIQSRGTASIGRLFGPVMLLWFVTIAVLGLVGIARHPTVFAAINPSYGLSYLVSNGATGFLVLGSVFLCVTGAEALYADMGHFGAGPIKLAWFAVVFPSLIINYAGQAALVIDGAPTDGNIFFRLCPDGLLLPLIGLATLATIIASQSVITGAFSMTRQAIQLGWMPRLAIKQTSSEGYGQIYVGAVNWLLMLVTVSLTIGFGKSDNLASAYGIAVSLTMLMTSALLFIAMREIWQWSLLAAGAVAGVFLTIDSAFFLANLTKIAEGGYVPLLLATSVYGLMWIWHRGAAAVAERMRERLIPVAQFMADIAEKKVPRVPGTAVFLTRTERGAPPVMLWHVKHNRALHEHLLVLRVEVISIPWVAPDDRLKIEELAPNVWRAEATFGFMERPHIPELLKASKARGCRIDLDDITYYVGHETVTARDDGKGLPAWQEQLFAAMERNSLHVSDFFSLPRDSVVEIGRQVAI | Function: Transport of potassium into the cell. Likely operates as a K(+):H(+) symporter.
Catalytic Activity: H(+)(in) + K(+)(in) = H(+)(out) + K(+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 66988
Sequence Length: 625
Subcellular Location: Cell inner membrane
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Q7NUG7 | MSAGYRSMAISASDRERGQQSMAMLVLAALGVVYGDLGTSPLYALQEAFNGDHGVRPTPDNVVGVVSLFLWSLILMVSVKYVMVLMRADNKGEGGILALLAQITGGRSGDGRRVAVGWVLLGLAGAAMLYGDGVITPAVSVLSAMEGLQVATPALAAYVVPATVVILAMLFMIQPFGSGRVGAAFGPILAAWFVAIAALGLAQLWRNPAILQAVNPWHGIAYFQRNGFAGFVSLGAVVLCLTGAEALYADMGHFGARPIRLAWYGLALPALILSYLGQGALLLAHPQLSGRPFYSMVPEWGLLPMVALSTLATIVASQALITAVFSLTHQSAQLGFFPRVKVLHTSGSHKGQIYLPLLNWTLMLATIAVVLGFRESGKLAAAFGLAVSTTMAITTVLFAVLARRRWHWPWWAVALVAGSLFAIDLAFWLANALKFLDGGWLPLLLGLAVFCVMGCWFGGRRLQMRESRGRQLPLEALLSSLGMNPVARIPGVGVFLSERADGTPLVLLHHLKHNQALHETAILLTLQMLDVPRAAGERVSAQWLGQGMARVTARYGYMEEPDVPEAMARAAEALGLPPLEPLSTSYYLGRQTLVAAPGSGGLKRWLVGVFAFLRQNERSATLYFGLPPNRVVELGARIEL | Function: Transport of potassium into the cell. Likely operates as a K(+):H(+) symporter.
Catalytic Activity: H(+)(in) + K(+)(in) = H(+)(out) + K(+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 68440
Sequence Length: 640
Subcellular Location: Cell inner membrane
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B7JBL0 | MADQKKPLQGGATLPLMAMAALGVVFGDIGTSPLYTLSACLSAMSLQPTAVNLQGILSLIFWTLVLVVSVKYAWVIMRASNQGEGGAMALTALASHATGHSNRLRWWILSIGLLGAALFYGDGVITPAISVLSAIEGMEVASPAWKPLVIPLALGVIIGLFMVQRRGTAAISHLFGPSMLVWFLLLFGSGLTWIVADPQVLIALNPWYALQFFGIHGIGGLVILGAVVLAVTGAEALYADMGHFGARPIRMAWYFLVLPALALNYLGQGALLELDPSAIQNPFFMLFPAWATIPMVVISGIATVIASQSVISGAYSATRQALLLGYLPRQAIIHTSASERGQIYLPLLNWLLMVAVIVVILWFRSSNALSFAYGTAVTGTMLMTTILVFFVARHSWKWSLWKAGLFCGFFVLLDGVFFGANLLKFVEGGWFPLAIGLAVFTTMSTWRWGRGILASKLYPDTLSVEDFLSSVTPGDPIRVPGTAVYLTMREKAIPHALLHNLKHNKVLHERVVILTIKFEEEPRVLPANRVVVLDYGQGVRRLTARYGFMEHPDIPEILKSAENSDNLWNPLDTTYFVSRQRVIPTAKASLSLWREHLFAIMLRISANATDFFRLPPNLVMELGDVVEFSHKVPDAPKKEKTTQQ | Function: Transport of potassium into the cell. Likely operates as a K(+):H(+) symporter.
Catalytic Activity: H(+)(in) + K(+)(in) = H(+)(out) + K(+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 70429
Sequence Length: 644
Subcellular Location: Cell inner membrane
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Q9F5A5 | MSAESHPTESQMTPKKLFYLTLGSIGVVYGDIGTSPLYAFREALKPVAHDGLTRFEVISLISLMIWALTIIVTIKYVLFLLRADNEGEGGTLSLLALLMKTANGHTAILMLLGLLGAALFLGDAMITPALSVLSAVEGLKLVTPRLSEYIVPISVVILALLFVVQSRGTGAVAKFFGPITAVWFLVMAAAGISHISDDFGILAAFNPYYAVSFLLHEGFYGVVVLGAVFLTVTGAEALYADLGHFGRRPIQWAWFLLVFPSLTLNYLGQGALVLGKPETMSDPFYLMYPQWALLPVVILATAATIIASQAVITGAFSMVRQGINLGFLPRREILFTSETNTGQIFVPSVNAVLFIGVIFLVLSFKTSDALATAYGISVTGAMVVTSIMAFEFVRARWNWSLPVAVIALAPLVILELIFLGANLLKIHDGGYIPILIATAFTVIMWTWRRGTAILMEKTRHTDIPLASFVSSIERKSEHSPAQVPGTAIFLTSDPESAPAALLHNLKHNHVLHDRNVILTIRTVNKPRVPSQDRYKVEQISERFSRVELLFGFMESQNVSQALATLRKAGLKFDIMSTSFYLGRRKLVPDANSGMPYWQDRFYILLANAASLPSDYFHLPANRVVELGSQIIV | Function: Transport of potassium into the cell. Likely operates as a K(+):H(+) symporter.
Catalytic Activity: H(+)(in) + K(+)(in) = H(+)(out) + K(+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 69112
Sequence Length: 632
Subcellular Location: Cell inner membrane
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Q2IPI8 | MSQIPSPNDPPPAGAVPTSGAPAGPSATPAPSPTAGFSLPEHRPAPTGKALAALAVGALGVVYGDIGTSPLYSLKECFGGPHGVHPTDANVLGVLSLVFWAMTFVVTFKYMSFVMRADNRGEGGILALMALVGKTETTRLGRRVLLMLGLFGAALLYGDGIITPAISVLGAVEGVAVAAPAMERVVVPATVVILVFLFLFQKQGTAKVGAVFGPIMLVWFATIAVLGVRGILHDPSILRALLPTHALSFFARNGWHGFLVLGGVVLVITGGEALYADMGHFGKRPIRVAWLGLAMPALLLNYLGQGALLLHDPGAARNPFYLLAPEWALYPTIAIATAAAIVASQALISGAYSLTQQAIQLGYSPRVTIRHTSQREIGQIYLPEVNWMLGTACVALVLGFQTSSRLASAYGIAVTGTMIVTTLLFHRVMRDRWGWARWKAWPLTVLFLTVDASFFLANVVKFRDGGWFPIAAAALVFTLMSTWKRGRDALALMLKDAGLPLDLFMADVARRKVQRVAGTAVFMTSNPGGVPPVLLHHLKHNKVLHERVILVSILAHEIPFVAEAERVNARELGSGFFQVIAHYGFMETPDVPALLDSLPRRALAGPRLTIVPMETTYFLGRETLLANGPSTIPTWRKRLFIVMARNAQTASAFFGLPPNRVVEMGAQIQL | Function: Transport of potassium into the cell. Likely operates as a K(+):H(+) symporter.
Catalytic Activity: H(+)(in) + K(+)(in) = H(+)(out) + K(+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 71715
Sequence Length: 670
Subcellular Location: Cell inner membrane
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A7H902 | MSDNPSSRAGPEVVPTPPPSPAAEAAVTALPAHGHRPPATGSALAKLALGALGVVYGDIGTSPLYALKECFTGHHGVQATPANVLGVLSLVFWAMTFVVTFKYLSFVMRADNRGEGGILALLALVGKHEVRRSGKQLLIILGLFGAALLYGDGVITPAISVLGAVEGLSVAAPALEHWVVPVTVGILALLFFIQRRGTAAVGAVFGPVMLVWFLCIAILGVRGILFDATILQAVLPTHAVAFFARNSWHGFLVLGGVVLVITGGEALYADMGHFGKRPIRFAWLLVAMPALMLNYMGQGAILLHDPQAARNPFYLLVPGWALYPMIAVATAAAIVASQALISGAFSLTRQAVQLGYSPRVTIRHTSSTEIGQIYVPEVNALLGAATIALVLGFKSSSNLAAAYGIAVTGTMAITTLLFHRVARDLWRWPRWRAWPLTLLFLLVDLAFFGANIVKVEEGGWFPLAAAAFVFTLLSTWKRGREGLADLMRGAGLPLDVFLEDIARRKPQRVPGTAVFMTGNTGTVPPVLLHHLKHNKVLHERVVLTSIMSEEIPSVRDAERVTVKELGSGFIQVIARYGFMETPDVPAMFASLPHRKLDGPRIELKPMETTYYLGRETLLPTGPSKMARWRKRLFIIMSRNAQTASAFFGLPPNRVVEMGAQLQL | Function: Transport of potassium into the cell. Likely operates as a K(+):H(+) symporter.
Catalytic Activity: H(+)(in) + K(+)(in) = H(+)(out) + K(+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 71322
Sequence Length: 663
Subcellular Location: Cell inner membrane
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A7IBQ1 | MALSFSRDRTRPLPFAAEIGALGVVFGDIGTSPLYALKQGVLAVGGTNFLGGDVLGLLSLITWSIILSVTVKYVMLVLRADNDGEGGILALVTLLDLHRSALGMRWYLLAAGLLGAAMLIGDGVLTPAMSVLSAIEGLQVISPELEHWVVTLTVLVLLAVFLSQRLGTERIASFFGPIMLMWFGSLGALGVYGILQAPQVLAGLDPRYGIMLMVNHPGLAGVILGACFLAVTGGEALYADLGHFGRPVIARAWLFVAMPALLLNYFGQGAILLVDPNAVRNPFYDLCPDVFDIPLLFLATAATVIASQSIITGVFSLAKQAIELGYLPPMRIRYTSEHNEQHIYVGRLNWLLMIACIAVVLGFEASDRLASAYGIAVAFAMVTTSILFIAQVHRSWGWPAPAVWAMATGLLTIDFAFASANMTKIHDGGWLPLSIAAAIIFVMVSWRRGLEGVVAQQVRFTEPLDSFVARKDRVNDVEAPRTAIFLSRAGAMTPVALSRMADLLKVRFEKAVIVSVWIAARPRVSVEDRVKVTTLNEGFVRVDLRFGYMQQIDVPSVLGPALSARGIDPDAAIYVIGHERIIPPDEVTKIKDVVAHVFAFLARNAERSVDRFGLPRARTVEIGYPVKL | Function: Transport of potassium into the cell. Likely operates as a K(+):H(+) symporter.
Catalytic Activity: H(+)(in) + K(+)(in) = H(+)(out) + K(+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 67859
Sequence Length: 628
Subcellular Location: Cell inner membrane
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A1JHR6 | MSTEHKKQSLSAVTLAAIGVVYGDIGTSPLYTLRECFSGHYGFDVRPDVVFGFLSLIFWMLILIVSVKYLTYVMRADNAGEGGILTLMSLAGRNTSSRATSILVILGLIGGSFFYGEVVITPAISVMSAIEGLEIAAPALDPYIVPCSIAVLTLLFVIQKHGTGSVGKLFAPVMLVWFLTLALLGLRSIIANPEVLAALNPKWAISFFTEYKSVSFFALGAVVLAITGVEALYADMGHFGKFPIRLAWFTVVLPSLVLNYFGQGALLLKNPEAIKNPFFLLAPDWALIPLLILATLATVIASQAVISGVFSLTRQAVRLGYLPPMRIIHTSEMESGQIYIPVINWTLYLAVVLVIVGFERSSNLAAAYGIAVTGTMVITSVLFCTVALKNWHWNRFFVYFLLVALLVIDVPMFSANALKLFSGGWLPLSLGLVMFIIMTTWKSERFSLLRRMHEHGNSLEAMIASLEKSPPVRVPGTAVYMSRAMNVIPFALLHNLKHNKVLHDRVVLLTLRTEDAPYVHNVNRVTIEQLSPTFWRVVASYGWRETPNVEEIFHRCGLEGLPCQMMETSFFMSHESLILTKRPWYLFLRGKLFIALSRNALRAADQFEIPPNRVIELGTQVEI | Function: Responsible for the low-affinity transport of potassium into the cell. Likely operates as a K(+):H(+) symporter.
Catalytic Activity: H(+)(in) + K(+)(in) = H(+)(out) + K(+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 68987
Sequence Length: 623
Subcellular Location: Cell inner membrane
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Q5NN77 | MSNDTSPGTSSVDSKSSDPSYGVPGHSHSDKDLLKLSLGAIGIVFGDIGTSPLYALKECFKGHHQLPVDDFHIYGLVSLIFWTMGLVVTVKYVMFIMKADNKGEGGSMSLLSLIIRGANPKLSRWLIVLGVFATALFYGDSMITPAMSVLSAVEGLTVIEPSFDSWVPPVSVVILIGLFCIQARGTESVGRLFGPIMLVYFATLAILGAFNIITRSPAILLALNPYYAIHFFASDPLQGFWALGSVVLSVTGAEALYADMGHFGRQPISLGWYWVVFPALTLNYLGQCALLSADHEAIANPFYFLAPDFLRVPLIILATFAAVIASQAVITGAFSVTQQAIQLGYIPRLRVNHTSASTVGQIYIPSVNWVLMFMVMVLIAMFKNSTNLANAYGIAVTGTMFITSCMMGVLVHRVWHWKAWQSIPLVSFFLLIDGAFFLSNVTKIPEGGWFPLLVGFVVFTMLMTWSRGRHLMAERMRQVAMPIQLFIRSAAASAVRIPGTAIFLTPEDDGVPHALLHNLKHNKILHERVILLTVKIEDVPYVDPHYRASMSSLEDGFYRLIVRYGFMEEPDVPLALNKIEQSGPMLRMDDTSFFISRQTLIPSTHTSMAIWREKLFAWMLRNSESATEFFKLPSNRVVELGSQIELVGSNGK | Function: Transport of potassium into the cell. Likely operates as a K(+):H(+) symporter.
Catalytic Activity: H(+)(in) + K(+)(in) = H(+)(out) + K(+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 71915
Sequence Length: 652
Subcellular Location: Cell inner membrane
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Q9I234 | MTSLRYWDISPALDPNTPTWPGDTPFQQEWAARLDEQCPVNVGRITLSPHTGAHVDGPLHYRADGLPIGQVPLDIYMGPCRVIHCIGANPLVTPEHLAGQLDDLPSRVLLRTFERVPANWPEGFCAIAPATIECLAERGVRLVGIDTPSLDPQHSKTLDAHHAVGRHGMAILEGVVLDDVPAGDYELLALPLKFTHLDASPVRAVLRALPTAE | Cofactor: Binds 2 zinc ions per subunit.
Function: Catalyzes the hydrolysis of N-formyl-L-kynurenine to L-kynurenine, the second step in the kynurenine pathway of tryptophan degradation.
Catalytic Activity: H2O + N-formyl-L-kynurenine = formate + H(+) + L-kynurenine
Sequence Mass (Da): 23152
Sequence Length: 213
Pathway: Amino-acid degradation; L-tryptophan degradation via kynurenine pathway; L-kynurenine from L-tryptophan: step 2/2.
EC: 3.5.1.9
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Q8Y1D0 | MERTLWDISPALSTATPTWPGDTPFSQEIAWKLEGDCPVNVGRITLSPHTGAHADAPLHYHADGAPIGAVPLDAYLGPCRVIHCVGVARVEPEHVRDALDGAPPRVLLRTYARMPQNAWDDHFAAVAPETIGLLAAHGVRLIGTDTASLDPQTSKTMDAHHAVGRHGLAILEGLVLDDVPAGDYELIALPLKFATLDASPVRAVLRRLP | Cofactor: Binds 2 zinc ions per subunit.
Function: Catalyzes the hydrolysis of N-formyl-L-kynurenine to L-kynurenine, the second step in the kynurenine pathway of tryptophan degradation.
Catalytic Activity: H2O + N-formyl-L-kynurenine = formate + H(+) + L-kynurenine
Sequence Mass (Da): 22347
Sequence Length: 209
Pathway: Amino-acid degradation; L-tryptophan degradation via kynurenine pathway; L-kynurenine from L-tryptophan: step 2/2.
EC: 3.5.1.9
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Q2S2F5 | MALIDISRSVSPATAVWPGDQEVQWTWTARRNEDESSVNLGSLRLSTHTGTHVDAPLHVKRQGQATDDLPLDSFVGPARVVDVNANAPSVRPEHIGQLDGASAERVLFKTSSGVSPDDEWPDAVVPIQPDTIHALADAGVSLVGTDAPSVDPLDSTDLPAHHALLDTGIVNLEGLVLTNVPPGRYELIALPLKIVGGDAAPVRAVLRDAPDP | Cofactor: Binds 2 zinc ions per subunit.
Function: Catalyzes the hydrolysis of N-formyl-L-kynurenine to L-kynurenine, the second step in the kynurenine pathway of tryptophan degradation.
Catalytic Activity: H2O + N-formyl-L-kynurenine = formate + H(+) + L-kynurenine
Sequence Mass (Da): 22347
Sequence Length: 212
Pathway: Amino-acid degradation; L-tryptophan degradation via kynurenine pathway; L-kynurenine from L-tryptophan: step 2/2.
EC: 3.5.1.9
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A1C688 | MGSRLHTREIQNGPPLPYNDDIRAFSKEYAESLDAQDPLHRFRNEFVIPSKEDLKRTTLDPNQEPEHSPTPSLYLCGNSLGLQPQSTRKYIEYYLRAWATKGVTGHFVQHDDQLLPPFVDVDAAGARLMAPIVGAMESEVAVMGTLTTNLHILMASFYQPTQERYKIIIEGKAFPSDHYAVESQIKHHNFDPKDGMVLIEPEDHTRPVLDTEHIIRTIDEHASSTAVILLSAIQYYTGQYFDIKRITAHAQSKGILVGWDCAHAAGNVDLQLHDWNVDFAAWCTYKYLNSGPGGTAALFVHERHGRVNLEQVNSESEPFRPRLSGWWGGDKKTRFLMDNNFIPQPGAAGFQLSNPSVLDMNAVVASLELFKQASMAEIRKKSLHITGYLEHLLLNYPLDTPSEKKPFTIITPSNPAERGAQLSVRLQPGLLDHVLETLEDNAVVIDERKPDVIRVAPAPLYNTYTDVWEFCRIFHEACQKALKARG | Function: Catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3-hydroxykynurenine (L-3OHKyn) into anthranilic acid (AA) and 3-hydroxyanthranilic acid (3-OHAA), respectively.
Catalytic Activity: H2O + L-kynurenine = anthranilate + H(+) + L-alanine
Sequence Mass (Da): 54747
Sequence Length: 486
Pathway: Amino-acid degradation; L-kynurenine degradation; L-alanine and anthranilate from L-kynurenine: step 1/1.
Subcellular Location: Cytoplasm
EC: 3.7.1.3
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Q2U038 | MGSRLHVQEIKKGPPLPFKDDIRAFTREYAESLDAQDPLRHFRDEFIIPSKKDLKRKTLNANENIEDSSDPRSIYLCGNSLGLQPRNTRKYLEHYLRTWAIKGVTGHFTPHDDQLLPPFVDVDDAGAKLMAPIVGALESEVAVMGTLTANLHFLMASFYQPTKEKYKIILEGKAFPSDHYAVESQIQHHNLDPKDAMVLIELENLDRPILDTEKILRVIDEHASSTALILLSGIQFYTGQYFDIEKITAYAHSKGIIIGWDCAHAAGNVELKLHDWNVDFAAWCNYKYLNSGPGGMAGLFVHENHGRVDMTKVGSKDEPFRPRLSGWWGDDKKTRFRMENRFVPQPGAAGFQLSNPSVLDMNAVAASLEIFNRTSMAEIRKKSLDLTGYLEHLLLKYPLDAAPEDKPFSIITPSNPAERGAQLSLRLGPGLLDNVLEVLEENGVVIDERKPDVIRVAPAPLYNTYADVWQFCQIFFDACQKAVRARK | Function: Catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3-hydroxykynurenine (L-3OHKyn) into anthranilic acid (AA) and 3-hydroxyanthranilic acid (3-OHAA), respectively.
Catalytic Activity: H2O + L-kynurenine = anthranilate + H(+) + L-alanine
Sequence Mass (Da): 54916
Sequence Length: 487
Pathway: Amino-acid degradation; L-kynurenine degradation; L-alanine and anthranilate from L-kynurenine: step 1/1.
Subcellular Location: Cytoplasm
EC: 3.7.1.3
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Q2H9P7 | MSEILKSPIQSPLLRGFVTSRRCDASEIEDLGSNVTKGLRVAGGRRVLRSHFFSYCLTYPAVNVAATTETGSGDGATEKCVYLCGNSLGLQPKRTQTRVNQYLSTWGTQGVQGHFKPLEESPLPTWLDADDRAAQLIAPIVGASKAEVAVMQTLTANLHLLMSAFYKPDINGKHKIILESKAFPSDHFAVETQLRHHNLDPATSMITLTSPSSPEDNILTTAEILSAITTHAATTALILLPGIQYYTGQLLDIPTITAHARTHSVFLIWDLAHAVGNAPLHLHDWGVDAAAWCSYKYLNGGPGCIGGLFVHERNSAVPPPVGELEVQQKEGEWEREGYANRLAGWWGNDKRTRFAMVNRFRPVPGAAGFQLSNPSILDITSLTASLEVFAEAGGVGALRGKSLRLTAFLEELLVGEGSSIVGVEERALFRVITPSDPGQRGAQLSLMLRGGLLEAVMRELEKRAVIVDERKPDVIRVAPAPLYNSFEDCVRFVVAFGEALAVARKEVAV | Function: Catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3-hydroxykynurenine (L-3OHKyn) into anthranilic acid (AA) and 3-hydroxyanthranilic acid (3-OHAA), respectively.
Catalytic Activity: H2O + L-kynurenine = anthranilate + H(+) + L-alanine
Sequence Mass (Da): 55240
Sequence Length: 509
Pathway: Amino-acid degradation; L-kynurenine degradation; L-alanine and anthranilate from L-kynurenine: step 1/1.
Subcellular Location: Cytoplasm
EC: 3.7.1.3
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Q95XZ6 | MKTGGLSDFADFGEEDANCTQGIQWIKDVFTDCVDTDLKLLGFIIGLISLALWLIPLFPQLWQNYKTKKCEGLSLAFLFFWLVGDTCNMLGAILTNQQPIQKIIGVYYIIQDLVLWTQYGYYLKIYNRPTTSSARSNTIVVPVLALASVGSFFVFESALPPVGDHRVKRSFLESLNHQEGLPLEGILKMWPIFTSYTDMLGYIIGSMAAVCYFGGRIPQIIKNYRHSSCEGLSLTMFYIIVAANFTYGISVLLATTSWLYLLRHLPWLAGSLGCCCFDAVIISQYYLYRPKTPLAEDTERAGLLNSQDDSD | Function: Amino acid transporter that specifically mediates the pH-dependent export of the cationic amino acids arginine, histidine and lysine from lysosomes . May play a role in the degradation of autophagic substrates in autolysosomes by regulating lysosome function .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34960
Sequence Length: 311
Domain: The di-leucine motif mediates lysosomal localization.
Subcellular Location: Lysosome membrane
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Q5ZJX0 | MAEGLRAPPPPGNGSECPDGARWVLRLLGECARDGRDVGSALLGLLSIGCFAAAALPQFYQACKTGIMDRALSIYFLLGWLGGDLLNLIGSFLANQLPLQVYTAVYYVLADLVMLSLYGYYKAKNWGTGATASINAACLFCLLGTATTLTVLSHDTGPAPNPAAFGGRSLLSLGLEGPGPEPISKTEIIGFAIGSISSVLYLCSRLPQIYTNYRRKSTAGVSFLLFALVMLGNLLYGTSVLLKNPEPGQSEGDYILHHLPWLIGSLGVLSLDVIISFQFLAYRTGQPSAGEEREALLAEHGDS | Function: Amino acid transporter that specifically mediates the pH-dependent export of the cationic amino acids arginine, histidine and lysine from lysosomes.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32167
Sequence Length: 303
Domain: The di-leucine motif mediates lysosomal localization.
Subcellular Location: Lysosome membrane
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Q6ZP29 | MVWKKLGSRNFSSCPSGSIQWIWDVLGECAQDGWDEASVGLGLISILCFAASTFPQFIKAYKTGNMDQALSLWFLLGWIGGDSCNLIGSFLADQLPLQTYTAVYYVLADLVMLTLYFYYKFRTRPSLLSAPINSVLLFLMGMACATPLLSAAGPVAAPREAFRGRALLSVESGSKPFTRQEVIGFVIGSISSVLYLLSRLPQIRTNFLRKSTQGISYSLFALVMLGNTLYGLSVLLKNPEEGQSEGSYLLHHLPWLVGSLGVLLLDTIISIQFLVYRRSTAASELEPLLPS | Function: Amino acid transporter that specifically mediates the pH-dependent export of the cationic amino acids arginine, histidine and lysine from lysosomes.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 31947
Sequence Length: 291
Domain: The di-leucine motif mediates lysosomal localization.
Subcellular Location: Lysosome membrane
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B0BMY1 | MVWRTLVASNFSTCPNGSIQWIWDVFGECAQDGWDEASVALGLVSIFCFAASTFPQYIKACKTGNMDQALSLWFLLGWIGGDSCNLIGSFLADQLPLQTYTAVYYVLADLLMLTLYFHYKFKKQPSLLSAPINSVLLFILGTVCITPLLSSTDPVAVPREGFRGRTLLSVEPGNKPFTKKEVVGFVIGSASSVLYLLSRLPQIRTNFVRQSTQGISYSLFALVMLGNTLYGLSVLLKNPEVGQSEGSYLLHHLPWLVGSLGVLLLDTIISIQFLVYRSHDADAASEREPLLPS | Function: Amino acid transporter that specifically mediates the pH-dependent export of the cationic amino acids arginine, histidine and lysine from lysosomes.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32232
Sequence Length: 293
Domain: The di-leucine motif mediates lysosomal localization.
Subcellular Location: Lysosome membrane
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P28048 | MAENGDKEQKLDSDTKICEQIEYYFGDHNLPRDKFLKQQILLDDGWVPLETMIKFNRLSKLTTDFNTILQALKKSKTELLEINEEKCKIRRSPAKPLPELNDEYKNSLKHKSVYIKGFPTSAILDDVKEWLKDKGPIENIQMRRTLQREFKGSIFIIFNTDDDAKKFLENRNLKYKDNDMTVLSREEYHAKKNEERKLNKSEEKAKSKQVKKEAQKQAEDAERKLVEERVGSLLKFSGDLDNMTSREDLHALFQTHGDIEWIDFSRGAKEGIVLFKMNAKEALDKAKAANSDNLKLKGKDVKWELIEGDTEKEALKKILEGKQESFNKRKGRDGRKFKGKGRGGKGNDSSSRKRTQFQGKKKTFDSSDDEDDMEESESPQKASVKAEESAGTKNGAAAAPGSPKKRSLDDKAEDGPAVKQSKTEVGDQ | Function: La protein plays a role in the transcription of RNA polymerase III. It is most probably a transcription termination factor. Binds to the 3' termini of virtually all nascent polymerase III transcripts (By similarity).
PTM: Phosphorylated.
Sequence Mass (Da): 48864
Sequence Length: 428
Subcellular Location: Nucleus
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Q2XSC4 | MEARRSGNFESSIWDDDYIQSLTSSYTGKMYVDKSEKLKIEVKMMMDEATDELEQLELINDLQRLGISYHFKDGIAKMLNNIYKSDSKYMEKDLHLTALKFRLLRQHGYRVPQDVFSSFMDDEGNFEAWVVEDVSVLVSLYEASHISVEGESILDMAKDFSSHHLTEMVEQIGEACLAEQVKRTLELPLHWRVGRLEARWFVQAYETRPNSNPTLVELAKLDFNMVQAKYQDELKRCSRWYEETGLPEKMSFARHRLAECFLWSLGFIPDPHHGYSREIMTKIAVLITITDDIYDIYGALEELQEFTEAFERWDINSLDLLPEYMQICFLAIFNSANELGYQILRDQGLNIIPNLKRSWAELSRAYYLEARWFHNGFVPTTDQYLNTAWISISGPLLLSYGYLTTTNPINNKELKSLEKHPSIIRWPSMVLRLADDLGTSSEEIKRGDVSKSIQCYMNETGCCEGDARHHVKSLIEVALKRMNDEILMEKPFKSFDTNAMNLARISLCFYQYGDGFGKPHSDTIKNLVSLIVLPFHMP | Cofactor: Binds 3 Mg(2+) or Mn(2+) ions per subunit.
Function: Catalyzes a mixture of sesquiterpenoids from (2E,6E)-farnesyl diphosphate. Catalyzes the formation of exo-alpha-bergamotene, as well as (E)-nerolidol, (Z)-alpha-bisabolene, (E)-beta-farnesene and beta-sesquiphellandrene. Also has activity towards geranyl diphosphate, but to a much lesser extent.
Catalytic Activity: (2E,6E)-farnesyl diphosphate = (1S,5S,6R)-alpha-bergamotene + diphosphate
Sequence Mass (Da): 62405
Sequence Length: 538
EC: 4.2.3.81
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Q8VZA1 | MKMGFLFLFCYLLAFLGYSPVDAAVKKYQFDVQVKNISRICNAKPIVTVNGMFPGPTVYAREGDRVIINVTNHVQYNMSIHWHGLKQYRNGWADGPAYITQCPIQTGQSYLYDFNVTGQRGTLWWHAHILWLRATVYGAIVILPAPGKPYPFPQPYQESNIILGEWWNKDVETAVNQANQLGAPPPMSDAHTINGKPGPLFPCSEKHTFVIEAEAGKTYLLRIINAALNDELFFGIAGHNMTVVEIDAVYTKPFTTKAILLGPGQTTNVLVKTDRSPNRYFMAASPFMDAPVSVDNKTVTAILQYKGVPNTVLPILPKLPLPNDTSFALDYNGKLKSLNTPNFPALVPLKVDRRLFYTIGLGINACPTCVNGTNLAASINNITFIMPKTALLKAHYSNISGVFRTDFPDRPPKAFNYTGVPLTANLGTSTGTRLSRVKFNTTIELVLQDTNLLTVESHPFHLHGYNFFVVGTGVGNFDPKKDPAKFNLVDPPERNTVGVPTGGWAAIRFRADNPGVWFMHCHLEVHTMWGLKMAFVVENGETPELSVLPPPKDYPSC | Cofactor: Binds 4 Cu cations per monomer.
Function: Lignin degradation and detoxification of lignin-derived products.
Catalytic Activity: 4 hydroquinone + O2 = 4 benzosemiquinone + 2 H2O
Sequence Mass (Da): 61748
Sequence Length: 557
Subcellular Location: Secreted
EC: 1.10.3.2
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Q9FLB5 | MTTVHTFSILLFFCSLFSASLIIAKVQHHDFVIQETPVKRLCKTRNAITVNGMFPGPTLEVNNGDTLEVKVHNRARYNITIHWHGVRQIRTGWADGPEFVTQCPIRPGKSYTYRFTIQGQEGTLWWHAHSSWLRATVYGALIIHPTPGSSFPFPKPDRQTALMLGEWWNANPVDVINQATRTGAAPNISDAYTINGQPGDLYNCSTKETVVVPINSGETSLLRVINAALNQPLFFTVANHKLTVVGADASYLKPFTTKVLMLGPGQTTDVLLTADQPPKRYYIAARAYQSAQNAPFDNTTTTAILQYKKTTTTSKPIMPVLPAFNDTNTVTSFSRKFKSLRNVVVPKTIDDNLFFTIGLGLDNCPKKFPKSRCQGLNGTRFTASMNNVSFVLPSNFSLLQAHSNGIPGVFTTDFPSKPPVKFDYTGNNISRALFQPVKGTKLYKLKYGSRVQVVLQDTNIVTSENHPIHLHGYDFYIVGEGFGNFNPKKDTSKFNLVDPPLRNTVAVPVNGWAVIRFVADNPGVWLMHCHLDVHIKWGLAMAFLVDNGVGELETLEAPPHDLPIC | Cofactor: Binds 4 Cu cations per monomer.
Function: Lignin degradation and detoxification of lignin-derived products.
Catalytic Activity: 4 hydroquinone + O2 = 4 benzosemiquinone + 2 H2O
Sequence Mass (Da): 62734
Sequence Length: 565
Subcellular Location: Secreted
EC: 1.10.3.2
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Q8Y9I9 | MVQITKGKFDGLQRLSNDKGVIAALAIDQRGSLKKMIQQAKGTENKKDVEDFKQLVSEELTPYASAILLDLEYGTPAIKARHEGSGLLTSYEKTGYDATTPGKLPDLIEDLSALRIKENGGDAVKILVYYDPDEPAEINEIKYAFLERIGAECRAVDIPFFLEPITYDATVTDSGSLEYAKLKPAKVKASIKEFSKPRYGVDVLKLEVPVNFKYVEGFAEGEVAYTQDEAARHFEECSDLSPLPFIYLSAGVTSEMFHKTIQFANQHNVQYSGVLCGRATWADGIEVYGKQGDDALREWLRTQGKENITSLDKLLDEGAVPWWTKYGSFEDVHVVEKQ | Catalytic Activity: D-tagatofuranose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate
Sequence Mass (Da): 37684
Sequence Length: 338
Pathway: Carbohydrate metabolism; D-tagatose 6-phosphate degradation; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-tagatose 6-phosphate: step 2/2.
EC: 4.1.2.40
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P37154 | KQFTKCELSQVLKDMDGYGGIALP | Function: Regulatory subunit of lactose synthase, changes the substrate specificity of galactosyltransferase in the mammary gland making glucose a good acceptor substrate for this enzyme. This enables LS to synthesize lactose, the major carbohydrate component of milk. In other tissues, galactosyltransferase transfers galactose onto the N-acetylglucosamine of the oligosaccharide chains in glycoproteins.
PTM: Glycosylated (50% of the proteins).
Sequence Mass (Da): 2642
Sequence Length: 24
Subcellular Location: Secreted
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Q7TV59 | MSEEQLKAFIAKVQADTSLQEQLKVEGADVVAIAKASGFAITTEDLKAHQANSQKNLSDAELEGVAGGTIGGTIVSITCETCDLLVGKMC | Function: Lanthionine-containing peptide (lantipeptide) with unknown function (Probable). Does not show antibiotic activity against Lactococcus lactis 117 and Bacillus subtilis 6633 bacteria (By similarity). Organisms that produce this peptide live in oligotrophic environments at very dilute concentrations, suggesting this peptide is not secreted to influence other bacteria (Probable).
PTM: Cross-links are proved in vitro, when coepressed in E.coli with the ProcM lanthionine synthetase.
Sequence Mass (Da): 9342
Sequence Length: 90
Subcellular Location: Secreted
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P0DQM1 | MNKNPIYRSEEEAKDIACGNVAAELDENSQALDAINGAGWKQTIVCTIAQGTVGCLVSYGLGNGGYCCTYTVECSKTCNK | Function: Lanthionine-containing peptide antibiotic (lantibiotic) only active on Gram-positive bacteria in synergy with Flvbeta peptides, which are encoded by the same operon than Flvalpha.a . Shows antibacterial activity in synergy with Flvbeta.b, Flvbeta.c, Flvbeta.e and Flvbeta.g . Does not show antibacterial activity when tested with Flvbeta.a, Flvbeta.d, Flvbeta.f and Flvbeta.h . The bactericidal activity of lantibiotics is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores (By similarity).
PTM: The lanthionine formed by Ser-58 and Cys-68 forms a putative lipid II binding motif.
Sequence Mass (Da): 8458
Sequence Length: 80
Subcellular Location: Secreted
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P0DQL3 | MSEKNMEKAGVVKADELDEMIDETTGGASTVNTVGIHTTYLISKGLQNCPLKPTTILPILPRK | Function: Lanthionine-containing peptide that does probably not show antibacterial activity, since its analog [+3]Flvbeta.a does not show antibacterial activity against M.luteus . Also does not show antibiotic activity when tested with [Del2]Flvalpha.a, an analog of Flvalpha.a, which is encoded by the same operon than Flvbeta.a . The bactericidal activity of lantibiotics is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores (By similarity).
PTM: Maturation of FlvA2 peptides involves the enzymatic conversion of Thr, and Ser into dehydrated AA and the formation of thioether bonds with cysteines . Modifications are processed by the flavecin synthetase FlvM2 . This is followed by membrane translocation and cleavage of the modified precursor (By similarity).
Sequence Mass (Da): 6800
Sequence Length: 63
Subcellular Location: Secreted
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P0DQL6 | MDNNTEKFNELAAIADESELNEMLDENITGAGSTIQCVNTTIGTILSVVFDCCPTSACTPPCRF | Function: Lanthionine-containing peptide that does probably not show antibacterial activity, since its analog [+2]Flvbeta.d does not show antibacterial activity against M.luteus . Also does not show antibiotic activity when tested with [Del2]Flvalpha.a, an analog of Flvalpha.a, which is encoded by the same operon than Flvbeta.d . The bactericidal activity of lantibiotics is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores (By similarity).
PTM: Contains LL-lanthionine, DL-lanthionine, and DL-beta-methyllanthionine, when coepressed in E.coli with the flavecin synthetase FlvM2.
Sequence Mass (Da): 6861
Sequence Length: 64
Subcellular Location: Secreted
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P0DQL8 | MEKMNNIAGITPENELDEMFDDSVVGAVGYTTYWGILPLVTKNPQICPVSENTVKCRLL | Function: Lanthionine-containing peptide that does probably not show antibacterial activity, since its analog [+7]Flvbeta.f does not show antibacterial activity against M.luteus . Also does not show antibiotic activity when tested with [Del2]Flvalpha.a, an analog of Flvalpha.a, which is encoded by the same operon than Flvbeta.f . The bactericidal activity of lantibiotics is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores (By similarity).
PTM: Contains DL-beta-methyllanthionine, when coepressed in E.coli with the flavecin synthetase FlvM2.
Sequence Mass (Da): 6560
Sequence Length: 59
Subcellular Location: Secreted
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P0DQL9 | MNNNNFDMEKFKKLAAIVSEGEIDEMLDETTVGAASTLPCAEVVVTVTGIIVKATTGFDWCPTGACTHSCRF | Function: Lanthionine-containing peptide antibiotic (lantibiotic) that is probably weakly active on Gram-positive bacteria, since its analog [Del1]Flvbeta.g shows weak antibacterial activity against M.luteus . This activity is synergistically enhanced by [Del2]Flvalpha.a, an analog of Flvalpha.a, which is encoded by the same operon than Flvbeta.g . The bactericidal activity of lantibiotics is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores (By similarity).
PTM: Contains LL-lanthionine and DL-beta-methyllanthionine, when coepressed in E.coli with the flavecin synthetase FlvM2.
Sequence Mass (Da): 7731
Sequence Length: 72
Subcellular Location: Secreted
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P0DQM0 | MERYGHLAGVIPVDEIDDMFESNVIGGTSSIDCVRLASNTPEGTVNLTVRIEFCPSAACTYSCRL | Function: Lanthionine-containing peptide that does probably not show antibacterial activity, since its analog [+2]Flvbeta.h does not show antibacterial activity against M.luteus . Also does not show antibiotic activity when tested with [Del2]Flvalpha.a, an analog of Flvalpha.a, which is encoded by the same operon than Flvbeta.h . The bactericidal activity of lantibiotics is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores (By similarity).
PTM: Contains LL-lanthionine, DL-lanthionine, and DL-beta-methyllanthionine, when coepressed in E.coli with the flavecin synthetase FlvM2.
Sequence Mass (Da): 7026
Sequence Length: 65
Subcellular Location: Secreted
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O87236 | MNKNEIETQPVTWLEEVSDQNFDEDVFGACSTNTFSLSDYWGNNGAWCTLTHECMAWCK | Function: Lanthionine-containing peptide antibiotic (lantibiotic) active on Gram-positive bacteria. The bactericidal activity of lantibiotics is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores. When present individually lacticin 3147 A1 exhibits strong activity towards L.lactis strain AM2, weak activity towards L.lactis strain HP and no activity towards L.lactis strain IFPL359, but when combined with lacticin 3147 A2 it displays strong activity towards all three strains.
PTM: Maturation of lantibiotics involves the enzymatic conversion of Thr, and Ser into dehydrated AA and the formation of thioether bonds with cysteine. This is followed by membrane translocation and cleavage of the modified precursor.
Sequence Mass (Da): 6798
Sequence Length: 59
Subcellular Location: Secreted
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O61967 | MPAFFCLPMACQRQVDSIDRSQSNLQAIPSDIFRFRKLEDLNLTMNNIKELDHRLFSLRHLRILDVSDNELAVLPAEIGNLTQLIELNLNRNSIAKLPDTMQNCKLLTTLNLSSNPFTRLPETICECSSITILSLNETSLTLLPSNIGSLTNLRVLEARDNLLRTIPLSIVELRKLEELDLGQNELEALPAEIGKLTSLREFYVDINSLTSLPDSISGCRMLDQLDVSENQIIRLPENLGRMPNLTDLNISINEIIELPSSFGELKRLQMLKADRNSLHNLTSEIGKCQSLTELYLGQNFLTDLPDTIGDLRQLTTLNVDCNNLSDIPDTIGNCKSLTVLSLRQNILTELPMTIGKCENLTVLDVASNKLPHLPFTVKVLYKLQALWLSENQTQSILKLSETRDDRKGIKVVTCYLLPQVDAIDGEGRSGSAQHNTDRGAFLGGPKVHFHDQADTTFEENKEAEIHLGNFERHNTPHPKTPKHKKGSIDGHMLPHEIDQPRQLSLVSNHRTSTSSFGESSNSINRDLADIRAQNGVREATLSPEREERMATSLSSLSNLAAGTQNMHTIRIQKDDTGKLGLSFAGGTSNDPAPNSNGDSGLFVTKVTPGSAAYRCGLREGDKLIRANDVNMINASQDNAMEAIKKRETVELVVLRRSPSPVSRTSEPSLNGSSHQLNHFDAGSPDSTMFVTSSTPVYAS | Function: Critical role in assembling adherens junctions; adapter protein involved in polarizing protein trafficking in epithelial cells. Necessary to maintain, not establish, the entire terminal web (organelle-depleted, intermediate filament-rich layer of cytoplasm that underlies the apical microvilli of polarized epithelial cells) or brush border assembly at the apical surface gut cells. Required for correct localization of ifb-2 intermediate filaments in the terminal web. Required for dlg-1 lateral localization . With dlg-1, cooperatively regulates ajm-1 localization to apical junctions .
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 77350
Sequence Length: 699
Subcellular Location: Basolateral cell membrane
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E3QQU9 | MKVAKASLLTILAHSVSARFLAEDEINRVQLYPAGSEPEKYLIELAPGDTRWVTEEEKWELRRNGNRFFDITDHKDLGATRLRTKTKSVFPEKCSLQDKVKPLLKDLDKSEIQKNLEKFTSFHTRYYKSDYGRQSSEWLLAKIDSIIKDAGADKNVYAQPFPHTWQQSSIIVTIPGKSNSTVIIGAHQDSINLWLPSILAAPGADDDGSGSMTILEAFRTLLKSKDIVSGKADNTIEFHWYSAEEGGLLGSQAIFSSYEKEGRDIKAMLQQDMTGFVQRTLDAGQPESVGVITDFVDPGLTGFIKKVIVEYCKVPYVETKCGYACSDHASASKAGYPSAFVIESAFEYSDNHIHSVDDTIKYLSFDHMLEHAKMTLGLVYELGFTDFTALEKKGESVSEEL | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Extracellular aminopeptidase that allows assimilation of proteinaceous substrates.
Sequence Mass (Da): 44812
Sequence Length: 401
Subcellular Location: Secreted
EC: 3.4.11.-
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F0X8C8 | MKVSSAIALLLPVVAARFVDSAFEQDHVQLHPEQAAAEQFLIELSPGETRWVTEDEKWELRRNGQRFMDITDNRDLGLASAQSATTGPARVFPPNVTLDEEVFPLLANLSKGELQTHLEKLTSFHTRYYRSEHGRASSNWLLGQVKKTVGEAGGFKHGITVKPFKHPWGQNSVIARIPGQTNRTIVVGAHQDSINLFLPSVLSAPGADDDGSGTVTILEALRVLLQSEAVLAGKAANTIEFHWYSAEEGGLLGSQAIFNTYEKASRDVRAMLQQDMTGFVQRTLDAGEVESVGVIVDYVDPGLTAFIKKVITAYCDIPFIETKCGYACSDHASASKAGYPSAFVIESAFERSDDHIHTSDDLIKYLSFDHMLQHARLTLAFVYELAFADFDKLDKAAAVSVAPEMGDL | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Extracellular aminopeptidase that allows assimilation of proteinaceous substrates.
Sequence Mass (Da): 44744
Sequence Length: 408
Subcellular Location: Secreted
EC: 3.4.11.-
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A4R640 | MKPTTSILALLLPAISARFVQETDGDHVQLHPEVAEAEKFHIELAPGETRWVTEEEKWELRRNGQRFFDITSTPELGKTLRSQSRPAAVFPSKLSQQDAVKPLLKKLAKEPMQKHLEKFTSFHTRYYKSEYGRQSSQWLLSEVNKTIADADAHKHGVHVQHFEHSWGQNSVIATIPGKSKSTIVVGAHQDSINLFLPSILAAPGADDDGSGIVTTLEALRVLLTSDELAGGKLENTVEFHWYSAEEGGLLGSQAIFSTYEKQKRDIKAMLQQDMTGFIQRTIDAGKPESVGVIVDYVDPALTEFIKTVIDEYCDIPYVETECGYACSDHASASKAGYPSAFVIESSFDLSDNHIHTTDDKIKFLSFDHMLQHAKMTTAFVYELASTDFKKLENESQGMSEL | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Extracellular aminopeptidase that allows assimilation of proteinaceous substrates.
Sequence Mass (Da): 44754
Sequence Length: 401
Subcellular Location: Secreted
EC: 3.4.11.-
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Q7RYC8 | MKISNASLLALLLPAASARFVEQAEQNRVMLFPDGIPEEPKSTTKYHIELSPGDTRWVTEDEKWELRRNGQRFFDITDHAELGTFNKRPYKKSVFPKKPTQKKDLEPLLKNLSKTEMEDHLTTFTSFHTRYYKSESGRQSSEWLLKQVRDTIKAAGADDTVTARHFEHAWGQNSIIATIPGKTNATVVIGAHQDSINLWLPSVLAAPGADDDGSGTVTILEAFRVLLQSEDIIKGNHENTIEFHWYSAEEGGLLGSQAIFTTYEKARRDVKAMLQQDMTGFVSRTLQAGEVESVGVIVDYVDPNLTDFIKKIIVEYCDIPYVETKCGYACSDHASASKAGYPSAFVIESAFEYSDNHIHTTDDLIKYLSFDHMLQHARMTLAFAYELAFADFAKLEKGHGDL | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Extracellular aminopeptidase that allows assimilation of proteinaceous substrates.
Sequence Mass (Da): 45198
Sequence Length: 402
Subcellular Location: Secreted
EC: 3.4.11.-
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Q0U6L1 | MKSSVLLSLCTAALVAGAAHPLEPQVVLKDGQSTFTEPDEYLIELSPGETRWVTEEGKWELRRQNINFFDITHHEDLGTINANRLIEKSVKFPSKPAFNKTVVPLLKKLKKDNMRKHLETFTSFHTRYYKSQYGAQSSAWLLEQVSKTLSDAGAVNASVKAFPHPWGQSSIIATLPGKSNKTVVIGAHQDSINLFLPSILAAPGADDDGSGTVTILEALRVLLKSEGILDGSAPNTVEFHWYSAEEGGLLGSQAIFQSYEKEGRDVKAMLQQDMTGYVQKTLDAGEPESVGVITDFVDPGLTEFIKQIITVYCDIPFILTKCGYACSDHASASKAGYPSAFVIESDFKYSDSKIHTTEDKIEYLSFDHMLQHAKLTLALAYELAFAEFK | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Extracellular aminopeptidase that allows assimilation of proteinaceous substrates.
Sequence Mass (Da): 42895
Sequence Length: 389
Subcellular Location: Secreted
EC: 3.4.11.-
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Q9GSF8 | MEMDIDLDDIENLLPNTFNKYSSSCSDKKGCKTLKSGSKSPSLTIPKLQKQLEFYFSDANLYNDSFLRKLVLKSGEQRVEIETLLMFKKIRSLLKEHYGENYLILKANNDEYIKFICECVKGSRYIRLTKDKLAIKRKKKFDNRTAEELIAFTIRIDGELPSLETIEKAVYNCRNRSSESSDVNKPNKPCKFNGIYVKSFGTNAHCIYIGFLKHRYTECFRDCFSLQQITCFDYSCSSLISLKEAGEMKRRLKKEISKFVDSSVTGINNKNISNEKEEELSQSCFLKISKIPAGSKKYQIREALDCDRPSYIQYDDKETAVIRFKNSAMRTKFLESRNGAEILIKKNCVDIAKESNSKSFVNKYYQSCLIEEIDEATAQKIIKEIKDQRSSIDEIKAELKLDNKKYKPWSKYCGRKRRPVSKRKNKAINKMSTEVKK | Function: RNA-binding protein required for assembly of the holoenzyme telomerase ribonucleoprotein (RNP) complex . Specifically binds telomerase RNA and promotes its assembly with catalytic subunit p123, thereby stimulating enzymatic activity and processivity of p123 . Telomerase is a ribonucleoprotein enzyme essential that copies new telomeric repeats onto chromosome ends and functions to maintain cell division .
PTM: The mature form of the protein is a protein of 43 kDa, which is derived from a 51 kDa precursor by proteolytic cleavage.
Sequence Mass (Da): 50722
Sequence Length: 437
Subcellular Location: Nucleus
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Q4G0J3 | METESGNQEKVMEEESTEKKKEVEKKKRSRVKQVLADIAKQVDFWFGDANLHKDRFLREQIEKSRDGYVDISLLVSFNKMKKLTTDGKLIARALRSSAVVELDLEGTRIRRKKPLGERPKDEDERTVYVELLPKNVNHSWIERVFGKCGNVVYISIPHYKSTGDPKGFAFVEFETKEQAAKAIEFLNNPPEEAPRKPGIFPKTVKNKPIPALRVVEEKKKKKKKKGRMKKEDNIQAKEENMDTSNTSISKMKRSRPTSEGSDIESTEPQKQCSKKKKKRDRVEASSLPEVRTGKRKRSSSEDAESLAPRSKVKKIIQKDIIKEASEASKENRDIEISTEEEKDTGDLKDSSLLKTKRKHKKKHKERHKMGEEVIPLRVLSKSEWMDLKKEYLALQKASMASLKKTISQIKSESEMETDSGVPQNTGMKNEKTANREECRTQEKVNATGPQFVSGVIVKIISTEPLPGRKQVRDTLAAISEVLYVDLLEGDTECHARFKTPEDAQAVINAYTEINKKHCWKLEILSGDHEQRYWQKILVDRQAKLNQPREKKRGTEKLITKAEKIRLAKTQQASKHIRFSEYD | Function: RNA-binding protein that specifically binds distinct small nuclear RNA (snRNAs) and regulates their processing and function . Specifically binds the 7SK snRNA (7SK RNA) and acts as a core component of the 7SK ribonucleoprotein (RNP) complex, thereby acting as a negative regulator of transcription elongation by RNA polymerase II . The 7SK RNP complex sequesters the positive transcription elongation factor b (P-TEFb) in a large inactive 7SK RNP complex preventing RNA polymerase II phosphorylation and subsequent transcriptional elongation . The 7SK RNP complex also promotes snRNA gene transcription by RNA polymerase II via interaction with the little elongation complex (LEC) . LARP7 specifically binds to the highly conserved 3'-terminal U-rich stretch of 7SK RNA; on stimulation, remains associated with 7SK RNA, whereas P-TEFb is released from the complex . LARP7 also acts as a regulator of mRNA splicing fidelity by promoting U6 snRNA processing . Specifically binds U6 snRNAs and associates with a subset of box C/D RNP complexes: promotes U6 snRNA 2'-O-methylation by facilitating U6 snRNA loading into box C/D RNP complexes . U6 snRNA 2'-O-methylation is required for mRNA splicing fidelity . Binds U6 snRNAs with a 5'-CAGGG-3' sequence motif . U6 snRNA processing is required for spermatogenesis (By similarity).
Sequence Mass (Da): 66899
Sequence Length: 582
Domain: The xRRM domain binds the 3' end of 7SK snRNA (7SK RNA) at the top of stem-loop 4.
Subcellular Location: Nucleus
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Q05CL8 | METENQKTMEESTKRKEEKKKRSRVKQVLADIAKQVDFWFGDANLHKDKFLREQIEKSRDGYVDISLLVSFNKMKKLTTDGKLIARALKSSSVVELDLEGTRIRRKKPLGERPKDEEERTVYVELLPKNVTHSWIERVFGKCGNVVYISIPHYKSTGDPKGFAFVEFETKEQAAKAIEFLNNPPEEAPRKPGIFPKTVKNKPIPSLRVAEEKKKKKKKKGRIKKEESVQAKESAVDSSSSGVCKATKRPRTASEGSEAETPEAPKQPAKKKKKRDKVEASSLPEARAGKRERCSAEDEDCLPPRPKAKKRAQKDGVGQAASEVSKESRDLEFCSTEEEKETDRKGDSLSKVKRKHKKKHKERHKMGEEVIPLRVLSKTEWMDLKKEYLALQKASMASLKKTISQIKLESEMETDCKAPTAGSGQECSTQEKVSAQGPQFVTGVIVKIVSGEPLPGRKQVKDILATISEVVYIDLLEGDTECHARFKTPEDAQAVMNAQTEIRKKHSWNLEVLSGDHEQRYWQKILVDRQAKLNQPREKKRGTEKLITKAEKIRLAKTQQASQHIRFSEYD | Function: RNA-binding protein that specifically binds distinct small nuclear RNA (snRNAs) and regulates their processing and function . Specifically binds the 7SK snRNA (7SK RNA) and acts as a core component of the 7SK ribonucleoprotein (RNP) complex, thereby acting as a negative regulator of transcription elongation by RNA polymerase II (By similarity). The 7SK RNP complex sequesters the positive transcription elongation factor b (P-TEFb) in a large inactive 7SK RNP complex preventing RNA polymerase II phosphorylation and subsequent transcriptional elongation (By similarity). The 7SK RNP complex also promotes snRNA gene transcription by RNA polymerase II via interaction with the little elongation complex (LEC) (By similarity). LARP7 specifically binds to the highly conserved 3'-terminal U-rich stretch of 7SK RNA; on stimulation, remains associated with 7SK RNA, whereas P-TEFb is released from the complex (By similarity). LARP7 also acts as a regulator of mRNA splicing fidelity by promoting U6 snRNA processing . Specifically binds U6 snRNAs and associates with a subset of box C/D RNP complexes: promotes U6 snRNA 2'-O-methylation by facilitating U6 snRNA loading into box C/D RNP complexes . U6 snRNA 2'-O-methylation is required for mRNA splicing fidelity . Binds U6 snRNAs with a 5'-CAGGG-3' sequence motif (By similarity). U6 snRNA processing is required for spermatogenesis .
Sequence Mass (Da): 64802
Sequence Length: 570
Domain: The xRRM domain binds the 3' end of 7SK snRNA (7SK RNA) at the top of stem-loop 4.
Subcellular Location: Nucleus
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W7X6T2 | MDEYLENTNLEELEQECFMEDYQHEDVVEQENHQVDANDIYENQQMNDESQLNQDVKISQQKEQAVEMIEEQQQNNQDKFKQFQDCMAHITELNFKRNYQNLTEQSSSNNVVAEELDIKESLKLQMEYYFCDTNLTHDSYLRGIISKSPKNCVDIKVFLKFNKIQQILKQIQDKQIVSTYGIENQSQKKNHKNYKNQNATFSKKDLIHLIRDSLKESKILKVKMDSLKVKRRFPFNLEQALKNSKQRTLYIDFLPPKCSKQTLVSIFGNFRIININLPLQKNSQLCQGFAFIEFFSEEEANQALITKNSSIPKELILLTEKKIGQGSIRIITYKKWQEEKQSFKELSKNQNEQKNKNMNQSRKASDEFVSIDVEIKQNCLIKIINIPQGTLKAEVVLAVRHLGYEFYCDYIDENSNQINSNKISLSTQQQNTAQCSNIQIENNLIQQDQHPQLNDLLKEGQAMIRFQNSDEQRLAIQKLLNHNNNKLQIEIRGQICDVISTIPEDEEKNYWNYIKFKKNEFRKFFFMKKQQKKQNITQNYNK | Function: RNA-binding protein required for assembly of the holoenzyme telomerase ribonucleoprotein (RNP) complex . Telomerase is an essential ribonucleoprotein enzyme that copies new telomeric repeats onto chromosome ends by repetitively synthesizing the short telomere-repeat sequence 5'-TTGGGG-3' using an RNA template component TER . TAP65/p65 specifically binds telomerase RNA template TER and is required for biogenesis and placement of the TER stem-terminus element: TAP65/p65 first protects the 3'-end of TER from degradation and acts as a chaperone to correctly fold TER for protein binding; it then bends TER stem-loop IV to position it for interaction of stem-loop IV with catalytic TERT RNA-binding domain .
Sequence Mass (Da): 64125
Sequence Length: 542
Domain: The HTH La-type RNA-binding and RRM domains cooperatively bind to TER RNA UUU-3'OH sequence after it is transcribed by Polymerase III . UUU-3'OH-binding by the HTH La-type RNA-binding and RRM domains positions the xRRM domain to bind to the adjacent proximal stem-loop IV and central dinucleotide GA bulge .
Subcellular Location: Chromosome
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Q28G87 | MTAIETDTPSNKVKEDESTDLRKDREKKKRSRVKQLLADIAKQVDFWFGDVNLHKDRFLREQIEKTRDGYIDISLLASFNKMKKITTDSKLIARAVKNSSVVEINLSGTKIRRRFPLGEKPQDVDSRTVYVELLPKNVTHSWIERVFGKYGMVVYVSIPRYKSTGDPKGFAFIEFETQEQAAKAIEVLNNPPEEAPRKAGMFPKTVKNKHLPPVEVTEHSITEGCGTEEKKKKKKKKSKARKDSVEKAEEDTKEQDMDIISEGVPKRRKTVSESSVPDVQEADKQTAKKEKKKKERAESFDQSEKVRQGKRKCSSSEEHDCSSAKQKKSDTKDLPQDEKPMVTQEVLQECKELSTEEEKDAVDKKEISVPKVKRKRKKKHKERHRVGEEVIPLRVLSKTEWLVLKAEYLTLQRASMASLKKSMSEMNHISEEEMQTQPSMQSFDIKNGKVETVKNEPLGPQFVCGVIGKITSSDPLQGRKYVKDAFSGVCEVVYVDMLEGDTECHVRFKSPEDAQTAVKTRSDLQGKHNWKLQILAGDNEQRYWQKILVDRQAKLNRPREKKRGTEKLIAKAEKMRLAKTQEASKHIRFSDGF | Function: RNA-binding protein that specifically binds distinct small nuclear RNA (snRNAs) and regulates their processing and function. Specifically binds the 7SK snRNA (7SK RNA) and acts as a core component of the 7SK ribonucleoprotein (RNP) complex, thereby acting as a negative regulator of transcription elongation by RNA polymerase II. The 7SK RNP complex sequesters the positive transcription elongation factor b (P-TEFb) in a large inactive 7SK RNP complex preventing RNA polymerase II phosphorylation and subsequent transcriptional elongation (By similarity). The 7SK RNP complex also promotes snRNA gene transcription by RNA polymerase II via interaction with the little elongation complex (LEC). LARP7 specifically binds to the highly conserved 3'-terminal U-rich stretch of 7SK RNA; on stimulation, remains associated with 7SK RNA, whereas P-TEFb is released from the complex. LARP7 also acts as a regulator of mRNA splicing fidelity by promoting U6 snRNA processing. Specifically binds U6 snRNAs and associates with a subset of box C/D RNP complexes: promotes U6 snRNA 2'-O-methylation by facilitating U6 snRNA loading into box C/D RNP complexes. U6 snRNA 2'-O-methylation is required for mRNA splicing fidelity (By similarity).
Sequence Mass (Da): 68069
Sequence Length: 593
Domain: The xRRM domain binds the 3' end of 7SK snRNA (7SK RNA) at the top of stem-loop 4.
Subcellular Location: Nucleus
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F9USS6 | MKPTRPNTDIPAWLQTTTTTPTPAIKAKFWQRNQRHLRQLLSRLAQPAPVTATSHWRVAPQFKLIQLLLLVILIALSNNLILLWSLALLVGCQLLWLPPRQLRRFMGSWLISVGMAMLFVLPSYWLAGPTTLLFFGLKTSLMLANAQYYRLTTPFQDLLAGLKALHCPDLLIMTLAIAITYLRMLGQHLLLTMEALELRTVAPTAHPYRLIGALFGNLYLKSYTYALELYAAMEARGFNGHYVRSTGRRTHWRDYLALSPAIIVWILFIFWRH | Function: Probable transmembrane component of the energy-coupling factor (ECF) transporter complex LarMNQO involved in nickel import.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 31307
Sequence Length: 273
Subcellular Location: Cell membrane
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Q5ZZ30 | MYSKYPAFFLNKNIKSSSGVQFSNVVKIPSAIESLYRGDNNLTGIIFLLPTLITGVFCQNFPEVVDIEQIRLHKLTNLSNDFHMVSMSEDPQIALDWGNGCFITIDPVSFSDYIVDVHATFSENQLNLPGRMEREKEHVALAVPFCSIKKITIHNKELANPFYLSIPQENHEAKMELNTLYGELISLLRKKYTQEVDEKEEQIALRTYAIRYLDFYAKFCGCDNPFDKTIAQLSELYPEFMSNFLQSSHFSSKTGLMKEIVVNSLDNLFKEHPYTKSIDASYIYRVKESTTCYEDDWAKPVYD | Function: ADP-ribosyltransferase that targets a specific class of NAD(+)-dependent glutamate dehydrogenase (GDH) enzymes found in fungi and protists, including many natural hosts of Legionella. Acts by targeting a conserved arginine residue in the NAD(+)-binding pocket of GDH, thereby blocking oxidative deamination of glutamate. Lart1 may target amoeba GDH to prevent a conserved stress response. In vitro, acts on Glud2 from the amoeba Dictyostelium discoideum (DdGluD2) and yeast Gdh2p but does not act on human or Legionella GDH homologs.
Catalytic Activity: L-arginyl-[protein] + NAD(+) = H(+) + N(omega)-(ADP-D-ribosyl)-L-arginyl-[protein] + nicotinamide
Sequence Mass (Da): 34911
Sequence Length: 303
Subcellular Location: Secreted
EC: 2.4.2.31
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Q84V83 | MTVSGAIPSMTKNRTLVVGGTGFIGQFITKASLGFGYPTFLLVRPGPVSPSKAVIIKTFQDKGAKVIYGVINDKECMEKILKEYEIDVVISLVGGARLLDQLTLLEAIKSVKTIKRFLPSEFGHDVDRTDPVEPGLTMYKEKRLVRRAVEEYGIPFTNICCNSIASWPYYDNCHPSQVPPPMDQFQIYGDGNTKAYFIDGNDIGKFTMKTIDDIRTLNKNVHFRPSSNCYSINELASLWEKKIGRTLPRFTVTADKLLAHAAENIIPESIVSSFTHDIFINGCQVNFSIDEHSDVEIDTLYPDEKFRSLDDCYEDFVPMVHDKIHAGKSGEIKIKDGKPLVQTGTIEEINKDIKTLVETQPNEEIKKDMKALVEAVPISAMG | Function: Catalyzes the synthesis of catechin from 3,4-cis-leucocyanidin. Also synthesizes afzelechin and gallocatechin.
Catalytic Activity: (2R,3S)-catechin + H2O + NADP(+) = (2R,3S,4S)-leucocyanidin + H(+) + NADPH
Sequence Mass (Da): 42665
Sequence Length: 382
Pathway: Flavonoid metabolism; proanthocyanidin biosynthesis.
EC: 1.17.1.3
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Q1G1A4 | MWRLKLSEGDEESVNQHVGRQFWEYDNQFGTSEERHHINHLRSNFTLNRFSSKHSSDLLYRFQCWKEKGKGMERLPQVKVKEGEERLINEEVVNVTLRRSLRFYSILQSQDGFWPGDYGGPLFLLPALVIGLYVTEVLDGTLTAQHQIEIRRYLYNHQNKDGGWGLHVEGNSTMFCTVLSYVALRLMGEELDGGDGAMESARSWIHHHGGATFIPSWGKFWLSVLGAYEWSGNNPLPPELWLLPYSLPFHPGRMWCHCRMVYLPMSYLYGRRFVCRTNGTILSLRRELYTIPYHHIDWDTARNQCAKEDLYYPHPKIQDVLWSCLNKFGEPLLERWPLNNLRNHALQTVMQHIHYEDQNSHYICIGPVNKVLNMLCCWVESSNSEAFKSHLSRIKDYLWVAEDGMKMQGYNGSQLWDVTLAVQAILATNLVDDYGLMLKKAHNYIKNTQIRKDTSGDPGLWYRHPCKGGWGFSTGDNPWPVSDCTAEALKAALLLSQMPVNLVGEPMPEEHLVDAVNFILSLQNKNGGFASYELTRSYPELEVINPSETFGDIIIDYQYVECTSAAIQGLVLFTTLNSSYKRKEIVGSINKAVEFIEKTQLPDGSWYGSWGVCFTYATWFGIKGMLASGKTYESSLCIRKACGFLLSKQLCCGGWGESYLSCQNKVYTNLPGNKSHIVNTSWALLALIEAGQASRDPMPLHRGAKSLINSQMEDGDYPQQEILGVFNRNCMISYSAYRNIFPIWALGEYRKLMLSL | Function: Converts oxidosqualene to lanosterol.
Catalytic Activity: (S)-2,3-epoxysqualene = lanosterol
Sequence Mass (Da): 86518
Sequence Length: 756
EC: 5.4.99.7
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O95232 | MISAAQLLDELMGRDRNLAPDEKRSNVRWDHESVCKYYLCGFCPAELFTNTRSDLGPCEKIHDENLRKQYEKSSRFMKVGYERDFLRYLQSLLAEVERRIRRGHARLALSQNQQSSGAAGPTGKNEEKIQVLTDKIDVLLQQIEELGSEGKVEEAQGMMKLVEQLKEERELLRSTTSTIESFAAQEKQMEVCEVCGAFLIVGDAQSRVDDHLMGKQHMGYAKIKATVEELKEKLRKRTEEPDRDERLKKEKQEREEREKEREREREERERKRRREEEEREKERARDRERRKRSRSRSRHSSRTSDRRCSRSRDHKRSRSRERRRSRSRDRRRSRSHDRSERKHRSRSRDRRRSKSRDRKSYKHRSKSRDREQDRKSKEKEKRGSDDKKSSVKSGSREKQSEDTNTESKESDTKNEVNGTSEDIKSEGDTQSN | Function: Binds cAMP regulatory element DNA sequence. May play a role in RNA splicing.
PTM: Phosphorylated in vitro by SRPK1, SRPK2 and CLK1.
Sequence Mass (Da): 51466
Sequence Length: 432
Subcellular Location: Nucleus speckle
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Q6BQD2 | MISPQEKQDKVIRATDLDALSCRYSANNKSYFSKPDPFIDSLISSYKMHLPLCTGYTNMSANRTLRSVFNEQKLPLINRGTYLRTESIDVITQEFIKEFKKCQVISLGGGSDTRCFRILEEHGEDVRYCEIDFHESVKIKKLAIINDKKLADIVKYDEESQSITSKEEFARLESNIHTENYHLIGYDLRELTGALDSGAILEYVDTSLPTLILSECVLCYLNPKENERIIEFWKNAFASKALLALLIYEPMSLNDAFGTTMTHNLSNRGINLLTFNEYPNLEARYKFLSEKCQSSNVKLTDMSNVGGYDSDNTTKAWINSKDLARINRLELVDEIEEIRLLLKHYCLCYCEFSHSPSLKTINKWKWILE | Function: Methylates the carboxyl group of the C-terminal leucine residue of protein phosphatase 2A catalytic subunits to form alpha-leucine ester residues.
Catalytic Activity: [phosphatase 2A protein]-C-terminal L-leucine + S-adenosyl-L-methionine = [phosphatase 2A protein]-C-terminal L-leucine methyl ester + S-adenosyl-L-homocysteine
Sequence Mass (Da): 42526
Sequence Length: 369
EC: 2.1.1.233
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Q5AQJ2 | MSAPQIPNLNTLRRGGGRGRFRARGGPDSSSSSGNKDRVVQGTDNDASVSRLSAVELGYLEDPFARALTPMGQEMRRLPIINRGTYVRTTAIDQLVASFLGLKADSDPTWKLKKKQIISLGAGSDTRVFRLLSLRPALDIIYHEIDFAVNNTAKIKAIQGTPLLQRVLGQSQVSISNEGDELHSPAYHIHAVDLRTLAQKGEGDKSTGQDPGRRLQDFVDTTLPTLLLSECCLIYLSPNDAAGVVRYFTHTLFPASQETETLALVLYEPIRPDDAFGRTMVANLATRGIQLQTLHQYASLGAQRQRLREHGFNGGQAAADVDFLWERWVAEEEKERVAALEMLDEVEEWKLLAQHYCVAWGWRKGSTRFTGWGDLDGQSAEE | Function: Methylates the carboxyl group of the C-terminal leucine residue of protein phosphatase 2A catalytic subunits to form alpha-leucine ester residues.
Catalytic Activity: [phosphatase 2A protein]-C-terminal L-leucine + S-adenosyl-L-methionine = [phosphatase 2A protein]-C-terminal L-leucine methyl ester + S-adenosyl-L-homocysteine
Sequence Mass (Da): 42319
Sequence Length: 382
EC: 2.1.1.233
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Q4ICG8 | MSGPEIPNLLSSLRSARGGRGRGRGRGGHASSSATHDSTIQGTDTDASVSRLSAVDLGYLDDPYAQYFVRSSAGPAARRLPIINRGTYARTISLDTLIESFLSADQSTGPDSTPKQIVSLGAGTDTRPFRLFASKARPGLVYHELDFEVVTSKKLRTVQAVPLLRNILTNVTQLTEHSWSSKPSGGEYYCHGQDLRNFSLSKASKEYHNTQDAPQEKPEITLPGLRTDIPTLLLSECCLCYLNGTEASDVLNFFTSRIPNLATIIYEPIRPDDAFGKMMVSNLAARRIEMPTLKMYPTPEDQRTRLRTAGFETVHHMTIEDIWQNWVSPEEKQRVDYLEGLDEVEEWKLLAAHYIVVWASRGSGFGNWGGVGVGA | Function: Methylates the carboxyl group of the C-terminal leucine residue of protein phosphatase 2A catalytic subunits to form alpha-leucine ester residues.
Catalytic Activity: [phosphatase 2A protein]-C-terminal L-leucine + S-adenosyl-L-methionine = [phosphatase 2A protein]-C-terminal L-leucine methyl ester + S-adenosyl-L-homocysteine
Sequence Mass (Da): 41396
Sequence Length: 375
EC: 2.1.1.233
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Q9UIC8 | MATRQRESSITSCCSTSSCDADDEGVRGTCEDASLCKRFAVSIGYWHDPYIQHFVRLSKERKAPEINRGYFARVHGVSQLIKAFLRKTECHCQIVNLGAGMDTTFWRLKDEDLLPSKYFEVDFPMIVTRKLHSIKCKPPLSSPILELHSEDTLQMDGHILDSKRYAVIGADLRDLSELEEKLKKCNMNTQLPTLLIAECVLVYMTPEQSANLLKWAANSFERAMFINYEQVNMGDRFGQIMIENLRRRQCDLAGVETCKSLESQKERLLSNGWETASAVDMMELYNRLPRAEVSRIESLEFLDEMELLEQLMRHYCLCWATKGGNELGLKEITY | Function: Methylates the carboxyl group of the C-terminal leucine residue of protein phosphatase 2A catalytic subunits to form alpha-leucine ester residues.
Catalytic Activity: [phosphatase 2A protein]-C-terminal L-leucine + S-adenosyl-L-methionine = [phosphatase 2A protein]-C-terminal L-leucine methyl ester + S-adenosyl-L-homocysteine
Sequence Mass (Da): 38379
Sequence Length: 334
EC: 2.1.1.233
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Q6CWW0 | MERVIQETDNDAFSCKISAITKRYLPSSEQKKIGNYEHYEDIHLEFCKEIKSRSRRKYANITKACRHSLPVMNYGTYLRTVSIDLKLTQWLKNNLENPADKVQVINLGCGSDLRMMTFLASFPGVQWLDLDYKDVVTFKSTILRSNAKFRASLQIEGDLPEEPSSIENVITDRYQLLPCNVTDDEQLIPILKKYTDFSVPAVILTECVLCYLHESKASQLISTVTGLYKQGYWISYDPIGGSQTNDRFGSIMQDNLMESRQLSMPTLMVFNSEDKYKERFPGKSEIQTMWDYYQNHLEDSERQRLKTLQFLDEIEELQVIFSHYVICTTNWRI | Function: Methylates the carboxyl group of the C-terminal leucine residue of protein phosphatase 2A catalytic subunits to form alpha-leucine ester residues.
Catalytic Activity: [phosphatase 2A protein]-C-terminal L-leucine + S-adenosyl-L-methionine = [phosphatase 2A protein]-C-terminal L-leucine methyl ester + S-adenosyl-L-homocysteine
Sequence Mass (Da): 38811
Sequence Length: 333
EC: 2.1.1.233
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Q7SAP7 | MSGSAPSIPNLLTLRGRIGGGGVTRGRYRGVIHRGGRGHGPGAPSASAAHDATIQGTDTDAAVSRLSAVQIGYIDDPYAELFAQSGPGAARRLPIINRGTYARTTAIDKLVDKFLDDTESSPEGRQIVSLGAGTDTRSLRLFSPSAPTPRKRVIYHEIDFPAMCEKKQRIVCSAPQLRSILSDPDSVEELSQHGGGNSWHSKAVAEKHKGSELWVHGLDLRAIAASQQPQQPLPPGVPIGSRGLHASPFTPGSTTQHEEQTEETSLPQQREPLTLTSLNPNLPTLIISECCLCYLPPSTASSIVSFFTTTIQSSLSIVIYEPIKPDDAFGKMMVSNLAAREIRMPTLEVYKEAEDQERRLREAGFSGGEGKGIGGARSKTIEQIWEEWTSQEEKERVDALEGLDEVEEWKLLAGHYIVVWGWRGVGVDLEI | Function: Methylates the carboxyl group of the C-terminal leucine residue of protein phosphatase 2A catalytic subunits to form alpha-leucine ester residues.
Catalytic Activity: [phosphatase 2A protein]-C-terminal L-leucine + S-adenosyl-L-methionine = [phosphatase 2A protein]-C-terminal L-leucine methyl ester + S-adenosyl-L-homocysteine
Sequence Mass (Da): 46747
Sequence Length: 431
EC: 2.1.1.233
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Q6P4Z6 | MATGSRESSFSSCASSCDFDDEGVRGTCEDASLCKRFAVSIGHWHDPYIEHLVRQSKERKAPEINRGYFARVHGVSQLIKAFLRKTECRCQILNLGAGMDTTFWKLKDEGLLPNKYFEVDFPMIVTRKLHTIKNKPLLFRPIMELHPEDTLQIDSHMLDSKRYAIIGADLRDLSELEEKLKKCNMNTQLPTLLITECVLVYMTPEQSANLLKWAARSFETAMFINYEQVNMDDRFGQIMIENLRRRQCDLAGVETCKSLESQKERLLLNGWETASAVNMMELYSGLPRAEVNRIESLEFLDEMELLEQLMRHYCLCWATRGGQELGLKEITY | Function: Methylates the carboxyl group of the C-terminal leucine residue of protein phosphatase 2A catalytic subunits to form alpha-leucine ester residues.
Catalytic Activity: [phosphatase 2A protein]-C-terminal L-leucine + S-adenosyl-L-methionine = [phosphatase 2A protein]-C-terminal L-leucine methyl ester + S-adenosyl-L-homocysteine
Sequence Mass (Da): 38330
Sequence Length: 332
EC: 2.1.1.233
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O94257 | MDITETDLDALKCRSSATKSGYIHDPFIKFFSPSRNSHKPPIINRGTYVRTWSIDHILQKFIESFDGKKQIISLGAGTDTRVFRYISEYGPENLKFIEFDFYPNCIRKIRTIEKHEALKQNIGDYVVDISGGSLVSGSLDIYSYDIREIVHKGFPGFVDFSLPTIVLSECCLCYLEPEEASSLCRWFQNMFATSGIVVYEPIQGMDNFGKMMKANLSARGVILKTLDCYETTEQQRMRFLDYGYSEVIAEDFLTIEETWIPIEEKKRTMSIEMLDELEEWQLLAKHYCLTFAATENLWNQIILQLPHLKT | Function: Methylates the carboxyl group of the C-terminal leucine residue of protein phosphatase 2A catalytic subunits to form alpha-leucine ester residues.
Catalytic Activity: [phosphatase 2A protein]-C-terminal L-leucine + S-adenosyl-L-methionine = [phosphatase 2A protein]-C-terminal L-leucine methyl ester + S-adenosyl-L-homocysteine
Sequence Mass (Da): 35855
Sequence Length: 310
EC: 2.1.1.233
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Q4P4G2 | MQRDTSLRDPFATEDESSASEIGRAPERRLRIPQNQLRNADERCEIRSPQPVPGPGLPRSIAVRTETAATSKDAPAPAPSLRLSLGLPRSRTKAHSGQTSDATNITSTARQADDAVRNTDSDALLSRLSALKLGYLPSEPFTQEFSSTLPSNGGHPTGRSGFPQPHHPGSSIRRSPLINIGTYLRCSTIDAEVESFLRQGCEQKQIISVGAGSDSRYWRIMADTDLSRRLHHYVEIDFEENTSQKLSRILKSPILRASLDTNSSVYGVPLSHLSQFSLGVPCHTGSESRQFDVIRSSKYSLLAADVRSLHPDTPSAERIDLEHLLGPASTGLDSTLPTLILFECVLAYIAPDRADWLIRHLGQRFAAVQALSYDIALAGDAHPSAKAVACVSSESESSECGQTVGTADSAISTSTTVASPAPPSRFGRVMLQNLEMRKLSLPGARAYPTIHAQSQRFAQAWSDSQALQIETSGRSLFSIWSDLGAEQRSRLSRLEGLDEVEEIDMLLQHYCIVQARRQRP | Function: Methylates the carboxyl group of the C-terminal leucine residue of protein phosphatase 2A catalytic subunits to form alpha-leucine ester residues.
Catalytic Activity: [phosphatase 2A protein]-C-terminal L-leucine + S-adenosyl-L-methionine = [phosphatase 2A protein]-C-terminal L-leucine methyl ester + S-adenosyl-L-homocysteine
Sequence Mass (Da): 56802
Sequence Length: 520
EC: 2.1.1.233
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Q6C997 | MNLRKDKVVQSTDGDALSSKYSAVQKGYLQDEFIDLFVAGSKQAAAQQGPGSARKVVAQFQPKLPLINRGTFVRHHAIDVLVDRFLAAKKPGQRVQIISLGAGSDTRPFSLWSSKPENRDEILYHEIDFAVSVERKRDIIMQDSTLRELVGAQEYDKTTGMHTQRYHLHGIDLRSIGPGFVLPGSDPSLATLIISECCLCYLEPDQAKQVIFWITSEFTNSTIVMYEPLSGQDQFGQVMIENLASRGISIPSMTKFPSLESQIERFKAAGYTEVLATSMDVIHDEWLSPEEQQRIHGLEFLDEREELLLLLKHYCVVWASNLTK | Function: Methylates the carboxyl group of the C-terminal leucine residue of protein phosphatase 2A catalytic subunits to form alpha-leucine ester residues.
Catalytic Activity: [phosphatase 2A protein]-C-terminal L-leucine + S-adenosyl-L-methionine = [phosphatase 2A protein]-C-terminal L-leucine methyl ester + S-adenosyl-L-homocysteine
Sequence Mass (Da): 36463
Sequence Length: 324
EC: 2.1.1.233
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Q04081 | MERIIQQTDYDALSCKLAAISVGYLPSSGLQRLSVDLSKKYTEWHRSYLITLKKFSRRAFGKVDKAMRSSFPVMNYGTYLRTVGIDAAILEFLVANEKVQVVNLGCGSDLRMLPLLQMFPHLAYVDIDYNESVELKNSILRESEILRISLGLSKEDTAKSPFLIDQGRYKLAACDLNDITETTRLLDVCTKREIPTIVISECLLCYMHNNESQLLINTIMSKFSHGLWISYDPIGGSQPNDRFGAIMQSNLKESRNLEMPTLMTYNSKEKYASRWSAAPNVIVNDMWEIFNAQIPESERKRLRSLQFLDELEELKVMQTHYILMKAQW | Function: Methylates the carboxyl group of the C-terminal leucine residue of protein phosphatase 2A catalytic subunits to form alpha-leucine ester residues. Acts on the two major protein phosphatase 2A catalytic subunits, PPH21 and PPH22.
Catalytic Activity: [phosphatase 2A protein]-C-terminal L-leucine + S-adenosyl-L-methionine = [phosphatase 2A protein]-C-terminal L-leucine methyl ester + S-adenosyl-L-homocysteine
Sequence Mass (Da): 37695
Sequence Length: 328
EC: 2.1.1.233
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Q9CII4 | MKITSRKVVVIGTGFVGTSIAYSMINQGLVNELVLIDVNQDKAEGEALDLLDGVSWGQENVIVRAGDYKDCKNADIVVVTAGVNQKPGQSRLDLVNTNAKIMRSIVTQVMDSGFDGIFVIASNPVDILTYVAWETSGLDQSRIVGTGTTLDTTRFRKELATKLEIDPRSVHGYIIGEHGDSEVAVWSHTTVGGKPILEFIVKNKKIGVEDLSNLSNKVKNAAYEIIDKKQATYYGIGMSTARIVKAILNNEQAILPVSAYLRGEYGQEGVFTGVPSIVNQNGVREIIELNIDAYEKKQFEKSVSQLKEVIESIK | Function: Catalyzes the conversion of lactate to pyruvate.
Catalytic Activity: (S)-lactate + NAD(+) = H(+) + NADH + pyruvate
Sequence Mass (Da): 34311
Sequence Length: 314
Pathway: Fermentation; pyruvate fermentation to lactate; (S)-lactate from pyruvate: step 1/1.
Subcellular Location: Cytoplasm
EC: 1.1.1.27
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Q8Y6Z6 | MKPRKVMIIGAGNVGTAAAHAFVNQKFVEELILVDLNKERVEGNRKDLADAAAFMPGKMDITVRDASDCADVDIAVITVTAGPLKEGQTRLDELRSTSRIVSGIVPEMMKGGFNGIFLIATNPCDIITYQVWKLSGLPRERVLGTGVWLDTTRLRRLLAEKLDIAAQSIDAFILGEHGDSQFPVWSHSSIYGKPVNEYSLEKLGESLDLKQIGETARDTGFEIYHQKGCTEYGIGGTIVEICRHIFSGSQRALTVSCVLDGEYGESGLAIGVPAVLSQNGVKEIISLKLDEQEQQAFANSVSVIKKSIASI | Function: Catalyzes the conversion of lactate to pyruvate.
Catalytic Activity: (S)-lactate + NAD(+) = H(+) + NADH + pyruvate
Sequence Mass (Da): 33741
Sequence Length: 311
Pathway: Fermentation; pyruvate fermentation to lactate; (S)-lactate from pyruvate: step 1/1.
Subcellular Location: Cytoplasm
EC: 1.1.1.27
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P20619 | MIQRNINRVALIGAGSVGSSYAFALLNQSITEELVIIDVNEDKAMGDAMDLNHGKIFAPNPTKTWYGNYDDCKEADIVCICAGANQKPGETRLDLVEKNLKIFKSLVDQVMASGFDGIFLIATNPVDILTYATWKFSGLPKERVIGSGTILDSGRFRFLLGEYFDIAPANVHAHIIGEHGDTELPVWSHADIGGVPVEELITRNPEYKMEDLDQLFVNVRDAAYHIIKKKGATYYGIAMGLARITKAILNNENSVLTVSTYLDGEYGEKDVYIGVPAVVNRTGIREILELTLSETEQKQFTHSSTVLKEILNPHFKEAR | Function: Catalyzes the conversion of lactate to pyruvate.
Catalytic Activity: (S)-lactate + NAD(+) = H(+) + NADH + pyruvate
Sequence Mass (Da): 35312
Sequence Length: 319
Pathway: Fermentation; pyruvate fermentation to lactate; (S)-lactate from pyruvate: step 1/1.
Subcellular Location: Cytoplasm
EC: 1.1.1.27
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P50933 | MKVGVVGTGFVGSTAAFALVLRGSCSELVLVDRDEDRAQAEAEDIAHAAPVSHGTRVWHGGHSELADAQVVILTAGANQKPGESRLDLLEKNADIFRELVPQITRAAPDAVLLVTSNPVDLLTDLATQLAPGQPVIGSGTVLDSARFRHLMAQHAGVDGTHAHGYVLGEHGDSEVLAWSSAMVAGMPVADFMQAQNLPWNEQVRAKIDEGTRNAAASIIEGKRATYYGIGAALARITEAVLRDRRAVLTVSAPTPEYGVSLSLPRVVGRQGVLSTLHPKLTGDEQQKLEQSAGVLRGFKQQLGL | Function: Catalyzes the conversion of lactate to pyruvate.
Catalytic Activity: (S)-lactate + NAD(+) = H(+) + NADH + pyruvate
Sequence Mass (Da): 32164
Sequence Length: 304
Pathway: Fermentation; pyruvate fermentation to lactate; (S)-lactate from pyruvate: step 1/1.
Subcellular Location: Cytoplasm
EC: 1.1.1.27
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P62051 | MNRIAVIGVGNVGMAFAYAAAIKRLANDIVLIDANAARAEGESMDLADAMALVGPVQIRSGGYEQCEGARIVVVTAGAKQMPGQSRLDLVRVNAGITRDILTAVMQYADDPLYIMATNPVDVLTHVARTVTGVAPGRVIGSGTVLDSARFRGHVAEILGVDVRGVHAHIVGEHGDSEVALWSRANVSGIPVAEMCARRGIAYDAAFREKALGHVRHAAYEIIGRKGATGYGIGMSLCRIVEAILHDEHSVLTVSCPVAGHYGLGDVSLSLPCVIGSDGIEEVLDAPIAEDEQAALAASARVLGEHLAAL | Function: Catalyzes the conversion of lactate to pyruvate.
Catalytic Activity: (S)-lactate + NAD(+) = H(+) + NADH + pyruvate
Sequence Mass (Da): 32213
Sequence Length: 309
Pathway: Fermentation; pyruvate fermentation to lactate; (S)-lactate from pyruvate: step 1/1.
Subcellular Location: Cytoplasm
EC: 1.1.1.27
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Q8RED8 | MLQTRKVGIVGIGHVGSHCALSMLLQGVCDEMVLMDIIPEKAKAHAIDCMDTISFLPHRAIIRDGGIQELSKMDVIVISVGSLTKNEQRLEELKGSLEAIKSFVPDVVKAGFNGIFVTITNPVDIVTYFVRELSGFPKNRVIGTGTGLDSARLKRILSEVTNIDSQVIQAYMLGEHGDTQIANFSSATIQGVPFLDYMKTHPEQFKGVELSVLEKQVVRTAWDIISGKNCTEFGIGCTCSNLVKAIFHNERRVLPCSAYLNGEYGHSGFYTGVPAIIGSNGVEEILELPLDERERKGFEDACAVMKKYIEVGKSYKIV | Function: Catalyzes the conversion of lactate to pyruvate.
Catalytic Activity: (S)-lactate + NAD(+) = H(+) + NADH + pyruvate
Sequence Mass (Da): 34887
Sequence Length: 318
Pathway: Fermentation; pyruvate fermentation to lactate; (S)-lactate from pyruvate: step 1/1.
Subcellular Location: Cytoplasm
EC: 1.1.1.27
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Q7NG49 | MQDRLFVSMEHPRALPETDLIKGAIVGAGAVGMAIAYSMLIQNTFDELVLVDIDRRKVEGEVMDLVHGIPFVEPSVVRAGTLADCRGVDVVVITAGARQREGETRLSLVQRNVEIFRGLIGEIMEHCPNAILLVVSNPVDVMTYVAMKLAGLPPSRVIGSGTVLDTARFRYLLAERLRVDPRSLHAYIIGEHGDSEVPVWSRANVAGAFLSEIEPAVGTPDDPAKMFEVFEHVKNAAYEIIERKGATSWAIGLATTQIVRAITRNQNRVLPVSVLMSGLHGIEEVCLAYPAVLNRQGIDRLVKFSLSPGEEEQLQRSARVMRQTLDGIQF | Function: Catalyzes the conversion of lactate to pyruvate.
Catalytic Activity: (S)-lactate + NAD(+) = H(+) + NADH + pyruvate
Sequence Mass (Da): 36216
Sequence Length: 330
Pathway: Fermentation; pyruvate fermentation to lactate; (S)-lactate from pyruvate: step 1/1.
Subcellular Location: Cytoplasm
EC: 1.1.1.27
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C5CGP2 | MKVSIIGAGMVGSSIAYATMIKGVAREISIVDINGDLAEGQALDLSHGAPYVHPVRIKGGNDYSLTKNSDVVVITAGRAQKPGETRLQLLKSNAKIISSIVESCLKYSENPIILMVSNPVDVLTWVAWKKSGLPRERIIGSGTTLDTARLRQNIADHCKLDPRSVHAYIIGEHGDSEIASWSTANVGGVPIKEFCNGCLAKGCERDKVFERIFENTRDAAYKIIEKKGATYYGIGLAVARILETIAGDHHSVLTVSSVHEEFRGMRDVPFSVPSVLGKKGIERILPLKLSDDELKGLENSAKVIKAAIESILENREPRAENPR | Function: Catalyzes the conversion of lactate to pyruvate.
Catalytic Activity: (S)-lactate + NAD(+) = H(+) + NADH + pyruvate
Sequence Mass (Da): 35081
Sequence Length: 323
Pathway: Fermentation; pyruvate fermentation to lactate; (S)-lactate from pyruvate: step 1/1.
Subcellular Location: Cytoplasm
EC: 1.1.1.27
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P00343 | MASITDKDHQKVILVGDGAVGSSYAYAMVLQGIAQEIGIVDIFKDKTKGDAIDLSNALPFTSPKKIYSAEYSDAKDADLVVITAGAPQKPGETRLDLVNKNLKILKSIVDPIVDSGFNGIFLVAANPVDILTYATWKLSGFPKNRVVGSGTSLDTARFRQSIAEMVNVDARSVHAYIMGEHGDTEFPVWSHANIGGVTIAEWVKAHPEIKEDKLVKMFEDVRDAAYEIIKLKGATFYGIATALARISKAILNDENAVLPLSVYMDGQYGLNDIYIGTPAVINRNGIQNILEIPLTDHEEESMQKSASQLKKVLTDAFAKNDIETRQ | Function: Catalyzes the conversion of lactate to pyruvate.
Catalytic Activity: (S)-lactate + NAD(+) = H(+) + NADH + pyruvate
Sequence Mass (Da): 35531
Sequence Length: 326
Pathway: Fermentation; pyruvate fermentation to lactate; (S)-lactate from pyruvate: step 1/1.
Subcellular Location: Cytoplasm
EC: 1.1.1.27
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P84821 | DASNAQKQHDVNFLL | Cofactor: Binds Ca(2+). Mn(2+) or Mg(2+) can also be used to a lesser extent.
Function: Sialic acid-specific lectin. Has hemagglutinating activity towards erythrocytes from several species, with high activity towards, rabbit, mouse and guinea pig erythrocytes, and low activity towards human erythrocytes. Hemagglutinating activity is blocked by treatment of erythrocytes with V.cholerae sialidase.
Sequence Mass (Da): 1700
Sequence Length: 15
Subcellular Location: Secreted
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P0DQV9 | NYLSKNDELRKGDSLVSNNGEFKAVFQDDANFVIYGWQPLWASDTYGSDAIRLCMQADCNLVMYNGSGQARWHTNTSKGDCNMCRLFLTNEGKLVLNKESTEIWNSDKNKGSK | Function: May contribute to some of the local and systemic effects of envenomation by the scorpionfish. Preferentially recognizes mannose-containing carbohydrate structures, but its interaction with single mannose residues is weak. Potently inhibits alpha-1-beta-1 integrin (ITGA1/ITGB1) binding to basement membrane collagen IV in a divalent cation-independent manner. In addition, moderately inhibits both laminin binding integrins alpha-3-beta-1 (ITGA3/ITGB1) and alpha-7-beta-1 (ITGA7/ITGB1). Weakens the cell-collagen contacts, reduces cell spreading, and alters the actin cytoskeleton, after the compensating alpha-2-beta-1 integrin is blocked. On the cellular level, fails to completely detach hepatocarcinoma HepG2 cells and primary arterial smooth muscle cells from the collagen IV fragment CB3.
PTM: Not glycosylated. Not N-glycosylated and not O-glycosylated with the mostcommon O-linked glycoconjugates.
Sequence Mass (Da): 12783
Sequence Length: 113
Subcellular Location: Secreted
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P72660 | MQNSPIPSPWQFIKENIPLLMVALVLALLLRFFVAEPRYIPSDSMLPTLEQGDRLVVEKVSYHFHPPQVGDIIVFHPPELLQVQGYDLGQAFIKRVIALPGQTVEVNNGIVYRDGQPLQEEYILEPPQYNLPAVRVPDGQVFVMGDNRNNSNDSHVWGFLPQQNIIGHALFRFFPASRWGQLGSFTFVPARTIINT | 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): 22230
Sequence Length: 196
Subcellular Location: Cell membrane
EC: 3.4.21.89
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P73157 | MTENIVRETSKKKESPPENTWLELGKTMVTAVILAIGIRTFVAEARYIPSSSMEPTLQINDRLIIEKISYRLRDPERGEIVVFNPTDALKAKNFHDAFIKRIIGLPGDEVRVSQGNVYVNGKMLDENYIAAPPAYEYGPVKVPDDQYLVLGDNRNNSYDSHYWGFVPREKLLGRAFVRFWPVPRVGLLTDDAEREAVEISPQAWESPAISPQTVPESR | 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): 24733
Sequence Length: 218
Subcellular Location: Cell membrane
EC: 3.4.21.89
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P15378 | MLSILFIFGLILGSFYYTAGCRIPLHLSIIAPRSSCPFCRRTLTPAELIPILSFLFQKGKCKSCGHRISFMYPAAELVTACLFAAAGIRFGISLELFPAVVFISLLIIVAVTDIHFMLIPNRILIFFLPFLAAARLISPLDSWYAGLLGAAAGFLFLAVIAAITHGGVGGGDIKLFAVIGFVLGVKMLAAAFFFSVLIGALYGAAAVLTGRLAKRQPLPFAPAIAAGSILAYLYGDSIISFYIKMALG | Cofactor: Zinc is required for the N-terminal methylation of the mature pilin, but not for signal peptide cleavage.
Function: Plays a role in type II pseudopili formation by proteolytically removing the leader sequence from substrate proteins and subsequently monomethylating the alpha-amino group of the newly exposed N-terminal phenylalanine. Substrates include proteins required for biogenesis of the type II general secretory apparatus.
Catalytic Activity: Typically cleaves a -Gly-|-Phe- bond to release an N-terminal, basic peptide of 5-8 residues from type IV prepilin, and then N-methylates the new N-terminal amino group, the methyl donor being S-adenosyl-L-methionine.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 26435
Sequence Length: 248
Subcellular Location: Cell membrane
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I1WFC0 | MPTASMTPNPFLSGSPEHAAAAGPLAAFAALPTGMQLAFAIVLGLVVGSFLNVVVHRLPIMMKRAWLAEIAEATGAPCADDSLPARYNLCVPRSACPHCGHALRAWENVPVLSYIALRGRCRHCRTPIGARYPLIELASGALAAGALALFGPSGAALAAFGLCAALLAMSAIDMQTGFLPDSLTLPLLWAGLCVNLWGTFASLRAAVIGAIAGYLFLWCILWLFKLLRGIEGIGYGDLKLLAALGAWLGWEALPQVVLIAAVAGAAVGLVATWRGRMRFEEPLPFGPFLAAGGAATLFFGTPFYLLLGG | Cofactor: Zinc is required for the N-terminal methylation of the mature pilin, but not for signal peptide cleavage.
Function: Plays an essential role in type IV pili and type II pseudopili formation by proteolytically removing the leader sequence from substrate proteins and subsequently monomethylating the alpha-amino group of the newly exposed N-terminal phenylalanine.
Catalytic Activity: Typically cleaves a -Gly-|-Phe- bond to release an N-terminal, basic peptide of 5-8 residues from type IV prepilin, and then N-methylates the new N-terminal amino group, the methyl donor being S-adenosyl-L-methionine.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32224
Sequence Length: 309
Subcellular Location: Cell inner membrane
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Q46525 | MLISELLQTPLGIFFVGLFSLMVGSFLNVVIYRVPVMMDREEKQYAWQVFHGEDSVCPEIPKQRFNLLVPASRCPHCGHRIRAIENIPVISWLFLKGKCSGCGAAISARYLLVELLTAALSVIVAFHYHDPLSLGFALVFTWTLIALCFIDAEHQLLPDRLTLPLLWLGILAALFNVFINLESSVIGAMIGYLSLWSVYWLFKLITGREGMGYGDFKLLACLCAWQGAWMLPIILFSAAILGMIYALGIGLRMGKPMPFGPFLAIAGWLTFLYGAQIGQLFGYFPA | Cofactor: Zinc is required for the N-terminal methylation of the mature pilin, but not for signal peptide cleavage.
Function: Plays an essential role in type IV pili and type II pseudopili formation by proteolytically removing the leader sequence from substrate proteins and subsequently monomethylating the alpha-amino group of the newly exposed N-terminal phenylalanine.
Catalytic Activity: Typically cleaves a -Gly-|-Phe- bond to release an N-terminal, basic peptide of 5-8 residues from type IV prepilin, and then N-methylates the new N-terminal amino group, the methyl donor being S-adenosyl-L-methionine.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 31863
Sequence Length: 286
Subcellular Location: Cell inner membrane
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P25960 | MTMLLPLFILVGFIADYFVNAIAYHLSPLEDKTALTFRQVLVHFRQKKYAWHDTVPLILCVAAAIACALAPFTPIVTGALFLYFCFVLTLSVIDFRTQLLPDKLTLPLLWLGLVFNAQYGLIDLHDAVYGAVAGYGVLWCVYWGVWLVCHKEGLGYGDFKLLAAAGAWCGWQTLPMILLIASLGGIGYAIVSQLLQRRTITTIAFGPWLALGSMINLGYLAWISY | Function: Plays a role in type II pseudopili formation by proteolytically removing the leader sequence from substrate proteins and subsequently monomethylating the alpha-amino group of the newly exposed N-terminal phenylalanine. Substrates include proteins required for biogenesis of the type II general secretory apparatus.
Catalytic Activity: Typically cleaves a -Gly-|-Phe- bond to release an N-terminal, basic peptide of 5-8 residues from type IV prepilin, and then N-methylates the new N-terminal amino group, the methyl donor being S-adenosyl-L-methionine.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 24957
Sequence Length: 225
Subcellular Location: Cell inner membrane
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B2RKK1 | MKNIRNFCIIAHIDHGKSTLADRLLEYTNTVSGKDLQDQVLDNMDLERERGITIKSHAIQMDYEMDGEKYVLNLIDTPGHVDFSYEVSRSIAACEGALLIVDAAQGIQAQTISNLYMAIENDLTIIPIVNKVDLPSAMPEEVEDQIIELLGCDRSEIIRASGKTGQGVDQILRAIVEQVPAPAGDPDAPLQCLIFDSVFNPFRGIIAYFKVVNGSIRKGDHVKFIATEKEYDADEVGVLRLDMEPRSEVKTGDVGYIISGIKTSREVKVGDTITHVAKPAKEAIAGFEEVKPMVFAGVYPIEAEDFENLRTSLEKLQLNDASLTFQPESSVALGFGFRCGFLGLLHMEIVQERLDREFNMNVITTVPNVSYKVYDKKGGCKEVHNPSGLPEPTLIDHIEEPFIRASVITNTAYIGPIMTLCLGKRGVLVKQEYISGDRVEIFYDLPLGEIVIDFYDKLKSISKGYASFDYHLHDFRESKLVKLDILLNGEPVDALSTLTHVDNSVTFGQRMCEKLKELIPRQQFEIAIQAAIGAKIIARETIKPVRKDVTAKCYGGDISRKRKLLEKQKEGKKRMKQIGTVEVPQKAFLAVLKLD | Function: Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre-translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP-dependent manner.
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 66340
Sequence Length: 595
Subcellular Location: Cell inner membrane
EC: 3.6.5.n1
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Q3SH47 | MSQTLTRNFSIIAHIDHGKSTLADRLIQFCGGLSEREMEAQVLDSMDLEKERGITIKAQTAALAYKAQDGQIYRLNLIDTPGHVDFSYEVSRSLSACEGALLVVDASQGVEAQTVANCYTAIDLGVEVIPVLNKIDLPAADPDRVAEEIEDIVGIDATDAVRASAKTGIGIAEILEVVVKQVPPPRGDENAPLKALIIDSWFDNYVGVVMLVRVVDGVLRPKDKIRFMASGTQYLTEHVGVFTPKSVDRPQLSAGDVGFVIAGIKELKSAQVGDTVTLVDNPAGEPLPGFKKVQSQVFAGLYPVESHDFEALRDALTKLQLNDAALQFEPEVSQALGFGFRCGFLGLLHMDIVQERLEREYDMDLITTAPTVVYEVVQKDGTTINVENPSKLPELSKIEEIREPIITATIFVPEEYVGNVITLCNQKRGVQLDMQYHGKQVMLRYDLPMNEVVMDFFDKLKSTSRGYASLDYEFKEFRAGDLVKLDILVNSEKVDALSLIVHRATSVYRGRELAAKMRELIPRQMFDVAVQAAIGANIIARENVKAMRKNVLAKCYGGDITRKKKLLEKQKAGKRRMKQVGNVEIPQEAFLAILQVSDK | Function: Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre-translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP-dependent manner.
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 66185
Sequence Length: 599
Subcellular Location: Cell inner membrane
EC: 3.6.5.n1
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A8FAK7 | MFNHKKYEKKYFLPPNLTYDWVKNETLESAPIWCSVDLRDGNQALPIPMNLEEKLEMFQLLVEIGFKEIEIAFPAASDTEFRLLRTLIDHHMIPDDVTIMVITQAREHIIRRTFEAIKGVPKAIVHLYNSTSEAQRRQVFKKTKDEVKQMAMDGAILVKELAEKTESDIYFQYSPESFPGTEVDYALDICNSVLDIWKPTPNHKAIINIPTTVEYSMPHIFASQIEYIHKNLSYRDSVTLSVHPHNDRGSGVSDAEFGVLAGAERVEGTLFGIGERTGNVDLITLAMNMYSQGYDPKLNFNNLEAIRKQYEKLTNITVHERQPYSGEMVFTAFSGSHQDAISKGMKYRKEHHVDKWDVPYIPVDPVDLGRNYQTDVIRINSQSGKGGIGYILETNYGIQLPYQMNEAMGYEAKKVSDQSNRELSVEEIYHVFEKQYVDFHPHFQLLDYQFHKGEKQEVTLTLLRDHQQIDIQGTGTGSLDAISNALKAYFHLEYDLEVYEQNSLGKDSQAKACAQIGISHQGKMHWGAGIDKDIIEATVKALVVAVNRLEVWM | Function: Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-ketoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate).
Catalytic Activity: 3-methyl-2-oxobutanoate + acetyl-CoA + H2O = (2S)-2-isopropylmalate + CoA + H(+)
Sequence Mass (Da): 63211
Sequence Length: 553
Pathway: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 1/4.
Subcellular Location: Cytoplasm
EC: 2.3.3.13
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Q8RCF9 | MAFKKDKPVYIVDTTLRDGEQTAGVVFANNEKIRIAQMLDEIGIDQLEVGIPTMGGDEKETVAKIAKLGLKASIMAWNRAVVKDVQESLECGVDAVAISISTSDIHIEHKLKKTRQWVLDSMTEAVRFAKKEGVYVSVNAEDASRTDMNFLIEFARCAKQAGADRLRFCDTVGFLDPFKTYEMVKAIKDAVDIEIEMHTHNDFGMATANALAGVKAGAKFVGVTVNGLGERAGNAALEEVVMALKYVYKMDLGIDTSRFREISEYVALASGRPLPPSKAIVGKNVFAHESGIHVDGALKNPYTYEVFDPQEVGLERQIVIGKHSGTAALINKFKEYGRVLTEEEANLLLPHVRKMAIQLKRPLFDKELMYLYEDVIVKGKAKAI | Function: Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-ketoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate).
Catalytic Activity: 3-methyl-2-oxobutanoate + acetyl-CoA + H2O = (2S)-2-isopropylmalate + CoA + H(+)
Sequence Mass (Da): 42404
Sequence Length: 384
Pathway: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 1/4.
Subcellular Location: Cytoplasm
EC: 2.3.3.13
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Q8F8T4 | MKQDSQSENESIVCDLSVSEDQRNVKFFSDLQTPIPKHLPFFMDVTLRDGNQALRRPWNLEQKETIFKQLLKLGVQGIEVGFASSNNQEFEACKYLSSIAPDNVVISSLSRAVEKEIEVSWKAIRFAPKPRIHIVYPVSAFTIQNVLKISPEKVLDRISQSVAYAKSLVGSKGEVQFSGEHFGDSLENLDFAAEAFQIALNNGADVVNLPNTVERYRPWLFVSMVKAVANLLPEDTRISIHTHNDLGMATATTVESYFAGAVQLETALNGLGERAGNTNTYEVAIALHNCGVEVPLNFSTIYETSRLVSYLSEIPIYEKAPLIGEDVISHRSGIHQDGVAKTRHLQKGAYRAFDAALIGRPEGDRIEFTNQSGKSAVYCILKDAGENITLEEAGRLQPILKKISEDLGRRELTLEEIRIEWNRLLRAI | Function: Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-ketoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate). Has high alpha-isopropylmalate synthase activity and low citramalate synthase activity .
Catalytic Activity: 3-methyl-2-oxobutanoate + acetyl-CoA + H2O = (2S)-2-isopropylmalate + CoA + H(+)
Sequence Mass (Da): 47721
Sequence Length: 428
Pathway: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 1/4.
Subcellular Location: Cytoplasm
EC: 2.3.3.13
|
Q8XSZ5 | MLKHPATKYRPFPPIALPDRTWPSKTLTRAPIWMSTDLRDGNQALFEPMNAERKMRMFKMLVQIGFKEIEAAFPAASQTDYDFVRELIEGGHIPDDVTIEVLTQAREDLIRRTMESLRGARRAIIHVYNATSPVFRRTVFNTDREGVKRIAVESAKLIREIAESMPETQWTYQYSPEVFSGTELDFALEVCNAVTEAWDPTPAHKIIFNLPATVEMATPNVYADQIEWMHRHLARRDSILLSVHPHNDRGTAVAAAELAVMAGADRVEGCLFGNGERTGNVDLVTLALNLYSQGIDPGLDFSHVNDVARTCEDCTQLPVHPRHPYVGDLVFTAFSGSHQDAIKKGFAVQKPDAIWEMPYLPIDPADVGRTYDSIIRVNSQSGKGGVAYLLESGYGIAMPRRLQVEFSSTVQQLTDASGREATAADIWALFQETYLRADGPIGYVSHRLAERDDGSQHIRLVVNIADREHVCEGVGNGPLDALVQALAAVLAAPVSIHHYEERALGQGANADAIAFAELAAPGVAGSVFGVGIDANLTTASIRAVVGGVNRLAARHAQAQPGQSLLRRGMAPSMELA | Function: Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-ketoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate).
Catalytic Activity: 3-methyl-2-oxobutanoate + acetyl-CoA + H2O = (2S)-2-isopropylmalate + CoA + H(+)
Sequence Mass (Da): 63150
Sequence Length: 576
Pathway: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 1/4.
Subcellular Location: Cytoplasm
EC: 2.3.3.13
|
O04973 | MFFFLQLLVPIISVFQSKKHYYSTFIRCSISNRRPEYVPSKISDPKYVRIFDTTLRDGEQSPGATMTTKEKLDVARQLAKLGVDIIEAGFPASSEADFESVKLIAEEIGNNTDENGFVPVICGLSRCNKSDIDKAWEAVKYAKKPRVHTFIATSEIHMKYKLKMSREQVVEKARSMVAYARSLGCEDVEFSPEDAGRSDREFLYDILGEVIKAGATTLNIPDTVGYTVPSEFGQLITDIKANTPGIENVIISTHCQNDLGLSTANTLAGACAGARQLEVTINGIGERAGNASLEEVVMALKCRGEQVLGGLYTGINTQHIVPSSKMVEEYSGLQVQPHKAIVGANAFAHESGIHQDGMLKHKDTYEIISPDDVGLSRSNEAGIVLGKLSGRHALKSKMLELGYDIDGKELEDLFWRFKSVAEKKKKITDDDLIALMSDEVLQPNVYWKLGDVQIMCGSLGLSTATVKLINTDGQEHIACSVGTGPVDAAYKAVDLIVKVPITLLEYSMNAVTEGIDAIASTRVSICSIDRHTIMNGSTGQTIHRTFSGTGADMDVVISSVRAYIGALNKMLSYEKLVSRYSKPEDSVVV | Function: Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate).
Catalytic Activity: 3-methyl-2-oxobutanoate + acetyl-CoA + H2O = (2S)-2-isopropylmalate + CoA + H(+)
Sequence Mass (Da): 64361
Sequence Length: 589
Pathway: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 1/4.
EC: 2.3.3.13
|
O04974 | MASITANHPISGKPLISFRPKNPLLQTQTLFNFKPSISKHSNSSFSIPVVRCSIRRIPEYTPSHIPDPNYVRIFDTTLRDGEQSPGATMTTKEKLDVARQSAKLGVDIIEAGFPASSEADLEAVKLIAKEVGNGVYEEEYVPVICGLARCNKKDIDKAWEAVKYAKKPRIHTFIATSEVHMNYKLKMSRDQVVEKARSMVAYARSIGCEDVEFSPEDAGRSDPEFLYHILGEVIKAGATTLNIPDTVGYTVPEEFGQLIAKIKANTPGVEDVIISTHCQNDLGLSTANTLAGACAGARQLEVTINGIGERAGNASLEEVVMALKCRGEQVLGGLYTGINTQHILMSSKMVEGISGLHVQPHKAIVGANAFVHESGIHQDGMLKHKDTYEIISPEDIGLNRANESGIVFGKLSGVMLCKPKMLELGYEIEGKELDDLFWRFKSVAEKKKKITDDDLVALMSDEVFQPQFVWQLQNVQVTCGSLGLSTATVKLIDADGREHISCSVGTGPVDAAYKAVDLIVKVPVTLLEYSMNAVTQGIDAIASTRVLIRGENGHTSTHALTGETVHRTFSGTGADMDIVISSVRAYVGALNKMMSFRKLMAKNNKPESSAVI | Function: Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate).
Catalytic Activity: 3-methyl-2-oxobutanoate + acetyl-CoA + H2O = (2S)-2-isopropylmalate + CoA + H(+)
Sequence Mass (Da): 66535
Sequence Length: 612
Pathway: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 1/4.
EC: 2.3.3.13
|
A3DF94 | MRRIRIFDTTLRDGEQTPGVNLNIQEKVDIAKQLARLGVDVIEPGFPLTSPGDFEAVQRIAREVEGPYICGFSRAIIRDIDETWKAIKDAQKKCFHIFISSSDIQIKHQLGKTEKDVLEIVKSTVYHAKQYTDEVEYSPMDASRTRLEFLYEVIEAAIDNGATVINIPDTVGYATPIEFGELIQKIRKNVRNIDKAIISVHCHNDLGMAVANSIVAAMNGAQQIECTINGVGERAGNAALEEVVTHIAARKDYLGFETGIDLSQLYKTSKIVSRYMGIPIPVNKPIVGKNVFTHESGIHQDGVLKERSTYEVIDPRLVGRDDSVILLGKHSGRHALKVEAEKLGYDLDEERLNKLFNDFKKLTDVKKNVTTADLESLIIESAAKAVEEAYVLEKIRVVSGNIETPSAKVVIKDSKGNLLEAEQTGNGPVDAVFKAINSVIKETENLTLYKYSVSAVTEEMESLGEVSVTLREKEKLYTGIGTHTDIITSSAIAYIDAINKAIAANARAQKN | Function: Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-ketoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate).
Catalytic Activity: 3-methyl-2-oxobutanoate + acetyl-CoA + H2O = (2S)-2-isopropylmalate + CoA + H(+)
Sequence Mass (Da): 56457
Sequence Length: 511
Pathway: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 1/4.
Subcellular Location: Cytoplasm
EC: 2.3.3.13
|
C7M0E4 | MDEVGTQERIRIFDTTLRDGEQAPGISLDPLEKLEIAEQLARLGVDIIEAGFPVASQGDFDAVRQIARQVHGPVICGLSRTHVADIERCYEAVRDAEHHRIHVFISTSPSHLEHMLRMSEDQVVEAVRRAIARARELVDDVEFSPQDATRTPLPFLYRVLQVAVDEGASTLNIPDTVGYGIPWDFARMVESVRREVAGSYVISCHCHNDLGLATANSLAAVAAGARQVECCINGIGERAGNAALEEVVMGLAIRSDVIGDVTTGIDTRELARTSRLVSRLTGYPVQYNKAVVGRNAFAHESGIHQHGVLTDRSTYEVIDAASVGQEAAQIVLGKHSGRHAFQEALARMGIALEGDALNATFQRFKELADRKVELSEADLEAIVAEELGTTLADRFELVSFRVEAGTGREAVASATVLVDGTPVEASASGNGMVDALGRVLAEATALEARLTGFSVTSVTGGADALGSVAVTVDVGGHEVSGRGVSTDIVEASARALLNALNRAARVREKASNRETP | Function: Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-ketoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate).
Catalytic Activity: 3-methyl-2-oxobutanoate + acetyl-CoA + H2O = (2S)-2-isopropylmalate + CoA + H(+)
Sequence Mass (Da): 55125
Sequence Length: 516
Pathway: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 1/4.
Subcellular Location: Cytoplasm
EC: 2.3.3.13
|
Q8UD63 | MTDASVKYRPYPTINIPDRTWPGKTIDKAPIWCSVDLRDGNQSLVNPMGHDRKARMFKLLLEMGFKEIEIGFPSASQTDFDFARWCVEEGNVPDDVSLQVLVQCRPELITRTFEALEGANKPIIHFYNSTSELQRRVVFGKDVHGIKQIAVDAAKMITDMAAKAGGGFRFEYSPESFTGTELEVALEICNAVVEVVKPTADNKLILNLPSTVEMATPNIYADQIEWMCRNIDNRENVIISLHPHNDRGTGIAATELALMAGADRVEGTLFGNGERTGNVDVVTLALNMYTQGVDPELDCRDIERIKAVYEYSNEMTIPERHPYVGELVYTAFSGSHQDAINKGMKAIKVANHPVWEVPYLPIDPKDVGRSYEAIIRINSQSGKGGIAYILQQDYGINLPRNLQVEFREDIQRITDEEGVELPAKRIYERFIERYVTQPNARIKFVDHHTYPAGDFKGVRIVAAEITDNGEVKRIEGKGTGPIDGFINALSVYLGVDLSVNDYSEHSLQHGSNASAIAYVEMEHPGGKLFGAGVNTNIVAASLEAIVSAANRVLEERAK | Function: Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-ketoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate).
Catalytic Activity: 3-methyl-2-oxobutanoate + acetyl-CoA + H2O = (2S)-2-isopropylmalate + CoA + H(+)
Sequence Mass (Da): 61978
Sequence Length: 558
Pathway: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 1/4.
Subcellular Location: Cytoplasm
EC: 2.3.3.13
|
Q0VLR3 | MSFDHRKYRPVAVIDKPDRRWPNQRIEKAPLWAAVDLRDGNQALIKPMSVAQKRRFFQMLVELGFKEIEVGFPSASQIDFDFCRALIEEDLVPDDVHIQVLTQAREDLIARTFDSLKGAKNAIVHIYNATSPTFREQVFNVDKAGCKAIAVRAAEWVKENAAKQPDTHWSFQYSPETFSATETDFAIEVIDAVNAVWRPDQGQRVIINLPATVEVSTPNVFADQVEMVHDNIQYRDDVIISVHTHDDRGCGVAAAEMAVMAGADRVEGTLLGNGERTGNMDLVTAGMNLYSQGIDPGIDFSRMKEIVALVEEITDIQTHPRHPYAGDLVFSAFSGSHQDAIRKCLARYQEGDIWTAAYLPIDPADVGRRYEEVVRINSQSGKGGVAHVLERDFGIDLPRWLQQELAGVVQGDAEEDGGEITSERVHRRFNSDYLNVPMGWVLRSYDLNRSNEQVQAQISIGDDRQPVTLLSGRGDGAMSALVDALNRRIGGEVKVVSFDEYSLGDNTEANAMACVRVQVGDSTQSAVAMAVDTTAAALQAILSAVGRMQETSEQLIANS | Function: Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-ketoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate).
Catalytic Activity: 3-methyl-2-oxobutanoate + acetyl-CoA + H2O = (2S)-2-isopropylmalate + CoA + H(+)
Sequence Mass (Da): 61822
Sequence Length: 559
Pathway: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 1/4.
Subcellular Location: Cytoplasm
EC: 2.3.3.13
|
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