ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
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Q0CS61 | MTTDLNQNPYLVRAQQLLCRVPLIDGHNDFPFIIRGLYQNNLTRASLNDLPIGQTDISRLRQGSVGGQFWSAYVPNPVHSDKESDEAYLECLRQTLQQIDVIHRMVSEHPDVFGLAQSAADVWKIFRAGRIASLIGIEGLHQIAHSPSALRMMHKLGVRYATLCHTKNNRYCDSAVDRHTSSPWSEYGGQTHDPGDEPSRNVRTGFHSLTLKYLTAVHGRIVDLSHTSEATQRDAIAISKAPVIFSHSASSSLTPSPRNVTDEILHQLKRNGGLIMVCFLRDLVNSADDANTTGSRVVDHILYIAETIGYDHVGIGSDFD... | Function: Dipeptidase; part of the gene cluster that mediates the biosynthesis of acetylaranotin, a member of the epipolythiodioxopiperazine (ETP) class of toxins characterized by a disulfide-bridged cyclic dipeptide . The first step of acetylaranotin biosynthesis is performed by the NRPS ataP which produces diketopipe... |
Q0CXW9 | MAKQELMNLFLSKEFASGYKLAELVTGPFAQLLVDYSGVVQSTQRPLVILDNACGTGIISEALNRSLDSQTKGHWELTCGDISDSLVQYVNQRIQDEGWPRAKAQLVDAQDTKLPSSHFTHIFAAFECLRILQPGGTVAISNWQLPEWLVIAKSAVEAMPGDLPFPTVKEFLASLNEGWDSEEPTRVKLEQEGFDMVQVATVSQKLSLPKSTLVELIKPMLPVILGRFWTDEQRAKHEKHIPTALQQYLDDKYGASDDVPVEPRVIIATARKPC | Function: Acetylaranotin bis-thiomethyltransferase involved in the biosynthesis of acetylaranotin derivatives, members of the epipolythiodioxopiperazine (ETP) class of toxins characterized by a disulfide-bridged cyclic dipeptide . The first step of acetylaranotin biosynthesis is performed by the NRPS ataP which produce... |
O45100 | MQVDADLRPILGPQLVRLDPMRVKQLQDPIVYEAIDNLAKLSAHCLQLRTPLTTCEKLINSDSTLYLSWKYDEEEKVSRLMGFAKVGRKKLFLYDSQMQTYEGEILCLLDFYVHFSCQRQGVGQQILDYMFSQEHTEPYQLALDNPSVTLLGFMSQKYGLIKPVWQNTNFVVFEELFLALSAENGIEKPPPDGWRRPMTPRRLGTGMTDTRWLQHAVSGHQSKGNAMAAPVDADMTPQGALSNRAHQAKARKAHILSSKPLW | Function: Specifically acetylates 'Lys-40' in alpha-tubulin/mec-12 on the lumenal side of microtubules. Promotes microtubule destabilization and accelerates microtubule dynamics; this activity may be independent of acetylation activity. Acetylates alpha-tubulin with a slow enzymatic rate, due to a catalytic site that i... |
Q9VSY4 | MVEFRFDIKPLFAQPIIKVTSNLLPNTFRGDRRQCLDATSKMTEIIDQLGQLSATSQGLSKPVTTAQRLRMSDNQTIYLLADNEAGHNGAVLGLLKVGTKNLYLFDEAGKTRMVEQTPSILDFYVHESRQRAGLGKRLFQTMLNEEQWTARKCSVDRPSEKLLSFLSKHYGLKRIIPQANNFVLYEGFFNDGESGNGGGNGHANGTPNGLHITNSPNTHLFGATYLGEDSNQRRGSQQQTTPNARLQQITQISPSGRYGAKRPTCSMAEIIHAGNSKGGNGNGSAEANSGNGNHDIPEIAEQLQRQSLADLEANSYEPEP... | Function: Specifically acetylates 'Lys-40' in alpha-tubulin on the lumenal side of microtubules. Promotes microtubule destabilization and accelerates microtubule dynamics; this activity may be independent of acetylation activity. Acetylates alpha-tubulin with a slow enzymatic rate, due to a catalytic site that is not o... |
Q23192 | MEIAFDLSTIFTDNIQRLTRTDLLKYGPKRYWAVAQSIDCLGEMSSKFHGWKRVITMYDKIVDHDEEQTTYIMWEKVNGSKSILKGLLRVGYKTLYLTDNEQNQYMEKAMCILDFFVVPTEQRSGNGFKMFDEMLKAENVTVDQCAFDKPSAALQQFLEKYYDRKDLVWQSNKYALCSNFFIGRHPTVPFTPRQTKRASRASSAVSSHASSRNTSPIGRNRPRHDSVADLMRQDMLAGVRAEVDPNSPTGLKNARDFGHRRIW | Function: Specifically acetylates 'Lys-40' in alpha-tubulin/mec-12 on the lumenal side of microtubules. Promotes microtubule destabilization and accelerates microtubule dynamics; this activity may be independent of acetylation activity. Acetylates alpha-tubulin with a slow enzymatic rate, due to a catalytic site that i... |
Q9W5X9 | MVEFAFDIKHLFPQSIIRVQAHSLRPKVTQCRRYAQTERGKSTMTSCRLSEILNIMGKLSADAQGLCHAVTSADKLASDQVVYLMADKAAGHWEITGLLKVGTKDLFVFDQGGCYRRLNQTPAILDFYVHESRQRCGQGKLLFEWMLEKQGWSAHKCTVDRPSNKMLAFMAKHYGLVRTIPQGNNFVLYEGFFDDPITTCKSASGLQATGSGCRSRSQGHYVRQEQDQAQIKHGQANRNTVQNDANSGPFRQDQKIVVGTSIYRRRWKSPRTLARAGCREVSGGRRF | Function: Specifically acetylates 'Lys-40' in alpha-tubulin on the lumenal side of microtubules. Promotes microtubule destabilization and accelerates microtubule dynamics; this activity may be independent of acetylation activity. Acetylates alpha-tubulin with a slow enzymatic rate, due to a catalytic site that is not o... |
Q0CS60 | MYAHLAQMLNLLVTPSSGPATVFTDGPIPDNDAMKEALGKVDALKFNVETGKVIRLVPAVAPDIGVTVVVEGGKEYKLGYLGHKPYTVVAGKAMITRLGAEIEENPVMGEHVKTVDPLGSTNVKGVFVAGDAATPMKAVANAIGTGERYCRSWDRAAVDNGGHGEDLSLEEVHINTRPSSTATEFDKTHHIIEKMYPLESVRHLVVEQSQLCYILFGAVLAYAGWRWVLRLDILNEAITDLMSNLLNYYLTRRYPIHHSETGQQIPGRSYRWPNGQGDQGKFLDGIENRAQWAKEHGRIYRIWAGTTPEVVLQTPEHIKL... | Cofactor: Binds 1 FAD per subunit.
Function: Bimodular acetylaranotin synthesis protein; part of the gene cluster that mediates the biosynthesis of acetylaranotin, a member of the epipolythiodioxopiperazine (ETP) class of toxins characterized by a disulfide-bridged cyclic dipeptide . The first step of acetylaranotin bi... |
Q7PNM6 | MEFRFNMHPLFRARIVRINNSLLPTGFVAQSRRVALDATAQISEIINTIGSMSAQAQGLSVPVTTAQKLRNSDHHIYLMFESNDRNGLVVGILKVGRKSLYVFDPSGETVNVTAPCVLDFYVHESRQRGGLGRELFEHMLREENIQPDELAIDRPSEKLLGFLQKHYGLSKKIPQMNNFVVYEGFFASKAQNSTDIDGRRMHITASPNTNLFGPTFTTTEERRRSTSQTRTNVAPMPIIAQPPVGRYAAKRPTCSMAQVNHYSSMVGKISFPEENTGNGKRSVFEEQELDQRLADEMERCVELGAGGDEPDASRYTPHHG... | Function: Specifically acetylates 'Lys-40' in alpha-tubulin on the lumenal side of microtubules. Promotes microtubule destabilization and accelerates microtubule dynamics; this activity may be independent of acetylation activity. Acetylates alpha-tubulin with a slow enzymatic rate, due to a catalytic site that is not o... |
Q58CX6 | MEFPFDVDALLPERITVLDQHLRPPARRPGTTTPARVDLQQQIMTIVDELGKASAKAQHLPAPITSASRMQSNRHVMYILKDTSARPAGKGAIVGFLKVGYKKLFVLDDREAHNEVEPLCILDFYIHESLQRHGHGRELFQHMLQKERVEPHQLAIDRPSQKLLKFLNKHYNLETTVPQVNNFVIFEGFFAHQHPPARKLPPKRAEGDIKPYSSSDRESGLPQGW | Function: Specifically acetylates 'Lys-40' in alpha-tubulin on the lumenal side of microtubules. Promotes microtubule destabilization and accelerates microtubule dynamics; this activity may be independent of acetylation activity. Acetylates alpha-tubulin with a slow enzymatic rate, due to a catalytic site that is not o... |
Q9FM99 | MKISSLGWVLVLIFISITIVSSAPAPKPPKPKPAPAPTPPKPKPTPAPTPPKPKPKPAPTPPKPKPAPAPTPPKPKPAPAPTPPKPKPKPAPTPPNPKPTPAPTPPKPKPAPAPAPTPAPKPKPAPKPAPGGEVEDETEFSYETKGNKGPAKWGTLDAEWKMCGIGKMQSPIDLRDKNVVVSNKFGLLRSQYLPSNTTIKNRGHDIMLKFKGGNKGIGVTIRGTRYQLQQLHWHSPSEHTINGKRFALEEHLVHESKDKRYAVVAFLYNLGASDPFLFSLEKQLKKITDTHASEEHVGIIDPKKLSFESKHYYRYSGSLT... | Function: Reversible hydration of carbon dioxide.
PTM: N-glycosylated.
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Mass (Da): 42567
Sequence Length: 389
Subcellular Location: Plastid
EC: 4.2.1.1
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Q86WG3 | MGTTEATLRMENVDVKEEWQDEDLPRPLPEETGVELLGSPVEDTSSPPNTLNFNGAHRKRKTLVAPEINISLDQSEGSLLSDDFLDTPDDLDINVDDIETPDETDSLEFLGNGNELEWEDDTPVATAKNMPGDSADLFGDGTTEDGSAANGRLWRTVIIGEQEHRIDLHMIRPYMKVVTHGGYYGEGLNAIIVFAACFLPDSSLPDYHYIMENLFLYVISSLELLVAEDYMIVYLNGATPRRRMPGIGWLKKCYQMIDRRLRKNLKSLIIVHPSWFIRTVLAISRPFISVKFINKIQYVHSLEDLEQLIPMEHVQIPDCV... | Function: Functions in the development of neural tissues, particularly the postnatal maturation of the cerebellar cortex. May play a role in neurotransmission through regulation of glutaminase/GLS, an enzyme responsible for the production in neurons of the glutamate neurotransmitter. Alternatively, may regulate the loc... |
Q1M168 | MGTTEATLRMENVDVRDEWQDEDLPRPLPEDTGEDHLGGTVEDSSSPPSTLNLSGAHRKRKTLVAPEINISLDQSEGSLLSDDFLDTPDDLDINVDDIETPDETDSLEFLGNGNELEWEDDTPVATAKNMPGDSADLFGDGSGEDGSAANGRLWRTVIIGEQEHRIDLHMIRPYMKVVTHGGYYGEGLNAIIVFAACFLPDSSSPDYHYIMENLFLYVISSLELLVAEDYMIVYLNGATPRRRMPGIGWLKKCYHMIDRRLRKNLKSLIIVHPSWFIRTVLAISRPFISVKFISKIQYVHSLEELEQLIPMEHVQLPACV... | Function: Functions in the development of neural tissues, particularly the postnatal maturation of the cerebellar cortex. May play a role in neurotransmission through regulation of glutaminase/GLS, an enzyme responsible for the production in neurons of the glutamate neurotransmitter. Alternatively, may regulate the loc... |
O34431 | MKFHEMGQTDLLEATNTSMKQGLTEKEVKKRLDKHGPNELQEGKKTSALLLFFAQFKDFMVLVLLAATLISGFLGEYVDAVAIIAIVFVNGILGFFQERRAEQSLQALKELSTPHVMALREGSWTKIPSKELVPGDIVKFTSGDRIGADVRIVEARSLEIEESALTGESIPVVKHADKLKKPDVSLGDITNMAFMGTIVTRGSGVGVVVGTGMNTAMGKIADMLESAGTLSTPLQRRLEQLGKILIVVALLLTVLVVAVGVIQGHDLYSMFLAGVSLAVAAIPEGLPAIVTVALSLGVQRMIKQKSIVRKLPAVETLGCA... | Function: This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of calcium.
PTM: Phosphorylated in a Ca(2+)-dependent manner starting 4 hours after shifting to sporulation medium.
Location Topology: Multi-pass membrane protein
Catalytic Activity: ATP + Ca(2+)(in) + H2O = ADP + Ca(2+... |
P47317 | MNSWTGLSEQAAIKSRQEHGANFLPEKKATPFWLLFLQQFKSLVVILLLLASLLSFVVAIVSGLRSNWNFNHDLIIEWVQPFIILLTVFANSLIGSIQEFKAQKSASALKSLTKSFTRVFRNGELISINVSEVVVGDIIFVDAGDIIPADGKLLQVNNLRCLESFLTGESTPVDKTIDSNEKATILEQTNLVFSGAQVVYGSGVFQVEAVGIKTQVGKIAKTVDDSVTKLSPLQQKLEKIGKWFSWFGLGLFAVVFLVQTALLGFDNFTNNWSIALIGAIALVVAIIPEGLVTFINVIFALSVQKLTKQKAIIKYLSVIE... | Function: Could mediate calcium influx.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 96318
Sequence Length: 874
Subcellular Location: Cell membrane
EC: 7.2.2.-
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P37278 | MKGAIVSASLTDVRQPIAHWHSLTVEECHQQLDAHRNGLTAEVAADRLALYGPNELVEQAGRSPLQILWDQFANIMLLMLLAVAVVSGALDLRDGQFPKDAIAILVIVVLNAVLGYLQESRAEKALAALKGMAAPLVRVRRDNRDQEIPVAGLVPGDLILLEAGDQVPADARLVESANLQVKESALTGEAEAVQKLADQQLPTDVVIGDRTNCLFQGTEVLQGRGQALVYATGMNTELGRIATLLQSVESEKTPLQQRLDKLGNVLVSGALILVAIVVGLGVLNGQSWEDLLSVGLSMAVAIVPEGLPAVITVALAIGTQ... | Function: This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of calcium. In vivo, probably exports the calcium from the cytoplasm to the periplasm and the extracellular medium.
Catalytic Activity: ATP + Ca(2+)(in) + H2O = ADP + Ca(2+)(out) + H(+) + phosphate
Location Topology: Mu... |
P37279 | MVNQQTLTLRGMGCAACAGRIEALIQALPGVQECSVNFGAEQAQVCYDPALTQVAAIQAAIEAAGYHAFPLQDPWDNEVEAQERHRRARSQRQLAQRVWVSGLIASLLVIGSLPMMLGISIPGIPMWLHHPGLQLGLTLPVLWAGRSFFINAWKAFRQNTATMDTLVAVGTGAAFLYSLAVTLFPQWLTRQGLPPDVYYEAIAVIIALLLLGRSLEERAKGQTSAAIRQLIGLQAKTARVLRQGQELTLPITEVQVEDWVRVRPGEKVPVDGEVIDGRSTVDESMVTGESLPVQKQVGDEVIGATLNKTGSLTIRATRVG... | Function: May play a role in the osmotic adaptation.
Catalytic Activity: ATP + Cu(+)(in) + H2O = ADP + Cu(+)(out) + H(+) + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 79700
Sequence Length: 747
Subcellular Location: Cell membrane
EC: 7.2.2.8
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P73241 | MAQTINLQLEGMRCAACASSIERAIAKVPGVQSCQVNFALEQAVVSYHGETTPQILTDAVERAGYHARVLKQQVLSSQQTEDRKPVFSAKLVTGLVISAVLFFGSLPMMLGVNIPHFPHIFHDPWLQWLLATPVQFWSGAEFYRGAWKSVRTRSATMDTLVALGTSAAYFYSVAITLFPQWLTSQGLAAHVYFEAAAVVITLILLGRSLEQRARRETSAAIRKLMGLQPQTALVKRGEHWETVAIAELAINDVVRVRPGEKIPVDGVVVAGNSTVDESLVTGESFPVDKTVGTEVIGATLNKSGSLDIQVSKLGQDSVLA... | Function: May play a role in the osmotic adaptation.
Catalytic Activity: ATP + Cu(+)(in) + H2O = ADP + Cu(+)(out) + H(+) + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 79950
Sequence Length: 745
Subcellular Location: Cell membrane
EC: 7.2.2.8
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Q9X5V3 | MNIKQEDDHHHSHAHGDNHCHCGHDQEKAADAIVRDPICGMTVDPQAGKPSLGHGGRIYHFCSEHCRTKFAAAPEDYLTAKDPVCGMSVDRSTARYFLKAEGEKFYFCSAACQAKFEADPAAYRDGQRPTAKPAPKGTLYTCPMHPEVVSDRPGDCPKCGMALEPMGIPPTDEGPNPELVDFVRRLWVSAILALPLLALGMGPMLGLPLREAIGEPQATFIELLLATPVVLWAALPFFRRAWASVVNRSPNMWTLIGLGVGTAYLYSVVATLAPGIFPMSFRGHGAAVPVYFEAAAVIVALVFVGQVLELKARERTGSAI... | Function: Involved in copper efflux.
Catalytic Activity: ATP + Cu(2+)(in) + H2O = ADP + Cu(2+)(out) + H(+) + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 88059
Sequence Length: 841
Subcellular Location: Cell membrane
EC: 7.2.2.9
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Q9X5X3 | MTALKQTEKSTSLPMSFDFDIEGMTCASCVRRVEKAIAAVPGVASANVNLATERATVQFNGVPETTSVLRAVEKAGYAPRIVTEEIQIEGMTCASCVSRVEKALKAVPGVADASVNLATEKATVRLVSGSAEISALAAAVKGAGYGIRKATPAEAMKEDVDHRTAELRSLKSAVTISSLMTLPLFLLEMGSHFIPGVHDFIMGTIGMRNNLYLQFALATLVLFGPGLRFFRKGVPNLLRWTPDMNSLVVLGTTAAWGYSVVTTFVPAILPSGTANVYYEAAAVIVTLILVGRYLESRAKGRTSQAIKRLVGLQPKTAFVL... | Function: Involved in copper efflux.
Catalytic Activity: ATP + Cu(2+)(in) + H2O = ADP + Cu(2+)(out) + H(+) + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 86239
Sequence Length: 827
Subcellular Location: Cell membrane
EC: 7.2.2.9
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Q6BZZ1 | MIESDSDTSDDAPQEYVSASANIPAQFELATAHMKATPEPQPTQQPDAEALHDDDPLTTTQDHPTGPSATASDTIDSTPQPMAPATLSASAVLPSLPSDTAALLETFSQQLQQSNVKCQLKFRPIGGATPSLKQSVYKIAETQQFGVVVKFLRKQLKIKNSQSSQIFCYISSFAPGLDETVGSLYNRYAIRGELTISYCLNQAFG | Function: Ubiquitin-like protein involved in cytoplasm to vacuole transport (Cvt), autophagy vesicles formation, mitophagy, and nucleophagy. Conjugation with ATG5 through a ubiquitin-like conjugating system involving also ATG7 as an E1-like activating enzyme and ATG10 as an E2-like conjugating enzyme, is essential for ... |
A6ZLF7 | MSRILESENETESDESSIISTNNGTAMERSRNNQELRSSPHTVQNRLELFSRRLSQLGLASDISVDQQVEDSSSGTYEQEETIKTNAQTSKQKSHKDEKNIQKIQIKFQPIGSIGQLKPSVCKISMSQSFAMVILFLKRRLKMDHVYCYINNSFAPSPQQNIGELWMQFKTNDELIVSYCASVAFG | Function: Ubiquitin-like protein involved in cytoplasm to vacuole transport (Cvt), autophagy vesicles formation, mitophagy, and nucleophagy. Conjugation with ATG5 through a ubiquitin-like conjugating system involving also ATG7 as an E1-like activating enzyme and ATG10 as an E2-like conjugating enzyme, is essential for ... |
Q08DY8 | METDLNSQDRKDLDKFIKFFALKTVQVIVQARLGEKICTRSSSSPTGSDWFNLAIKDIPEVTHEAKKALAGQLPAVGRSMCVEISLKTSEGDSMELEIWCLEMNEKCDKEIKVSYAVYNRLSLLLKSLLAITRVTPAYRLSRKQGHEYVILYRIYFGDVQLNGLGEGFQTVRVGTVGTPVGTITLSCAYRINLAFMSTRHFERTPPIMGIIIDHFVDRPYPSSSPMHPCNYRTAGEDTGVACPSVEDSQEVCATSFSTSPPSQLMVPGKEGGVPLGPSQPAHAAQADQERLATYTPSDGAHCAATPSSSEDAETVSNSSE... | Function: Autophagy factor required for autophagosome formation and mitophagy. Target of the TOR kinase signaling pathway that regulates autophagy through the control of the phosphorylation status of ATG13 and ULK1, and the regulation of the ATG13-ULK1-RB1CC1 complex. Through its regulation of ULK1 activity, plays a ro... |
Q9VHR6 | MSAQRLNAAERDLEKFIKFLVLKSTQVVVQSRLGEKMQTQCNPLAGSDWFNIAVQDHPEVLDETKRALNLKTGESILQRLPLCVEISLKTTEGDQMVLEVWSLDLLQPQNGASPATNDLNPEGQTLKAAHAIYNRMGIMLKSLISLTRTTPAYKLSRRQCPDSYGIFYRIYVDRPQVHTLGEGHKHVKIGQLSTIVGSLVMSVAYRTKLTISPTAAQSESNTIMLKSDHFRPATDANTPGNQQQTQNGTVVAKKLGLGALNPAQGTADRRFIDIEKPLRPGAFTDMGKLKQYTEDDFVLPETPPFEWLLRGRGSVESLNR... | Function: Autophagy factor required for autophagosome formation. Target of the TOR kinase signaling pathway that regulates autophagy through the control of the phosphorylation status of Atg13 and Atg1. The Atg1-Atg13 complex functions at multiple levels to mediate and adjust nutrient-dependent autophagic signaling. Inv... |
O75143 | METDLNSQDRKDLDKFIKFFALKTVQVIVQARLGEKICTRSSSSPTGSDWFNLAIKDIPEVTHEAKKALAGQLPAVGRSMCVEISLKTSEGDSMELEIWCLEMNEKCDKEIKVSYTVYNRLSLLLKSLLAITRVTPAYRLSRKQGHEYVILYRIYFGEVQLSGLGEGFQTVRVGTVGTPVGTITLSCAYRINLAFMSTRQFERTPPIMGIIIDHFVDRPYPSSSPMHPCNYRTAGEDTGVIYPSVEDSQEVCTTSFSTSPPSQLSSSRLSYQPAALGVGSADLAYPVVFAAGLNATHPHQLMVPGKEGGVPLAPNQPVHG... | Function: Autophagy factor required for autophagosome formation and mitophagy. Target of the TOR kinase signaling pathway that regulates autophagy through the control of the phosphorylation status of ATG13 and ULK1, and the regulation of the ATG13-ULK1-RB1CC1 complex. Through its regulation of ULK1 activity, plays a ro... |
W0TA43 | MSDSDREIIGLINNFFLKAALLLEQCKVVARGGGFDGEEPLRDGNHLFNIETRGDPTLEAQIQPWTTFDGEKSMPPLVLETFLDLRGLHSNQTVYLHDSDGNPWMVCKGGKKSEIVLERWLIELDRQFSSTTGSTDAAEDDEYNEFNDPENLHKQLVLLFRYLYTLTQLLPANDIITKLQASQQGTAQATTTTGTLKPLHIHTRLLDGSKPILSKGRVGLSKPIIASYSNTMNETNIASHLEQRKITPIKTKFGSLRITVSYRKDVDFYVIDQEDPYKRTTNVSALQDTVTATDRRISSNSNISISVSPKTTNMLNANHI... | Function: Activates the ATG1 kinase in a nutritional condition dependent manner through the TOR pathway, leading to autophagy . Involved in ATG9 and ATG23 cycling through the pre-autophagosomal structure (By similarity). Also involved in cytoplasm to vacuole transport (Cvt) and more specifically in Cvt vesicle formatio... |
Q59TN9 | MSSVLRNQDNPPTISEVSSTTKENTDNSNSKQEEKEKEKEISSTIENPTFVDDEEDNNPFSHHGEGLTSFMTANSFNEGPNTKSDKRTTKENNNSSSNNNRGDNNDDDDDDSLLLYNTSNNNKSNNVSRVNPMLKSTGEVFKTVNMNFESRVTKLLKPNTKIRIQITEAGNSNEGMSNSSKKYTVYTIKLINLEDPNNDILTRRRYSDFESLRDVLTKIFPLIVIPPIPPKNYFDFSMLNGLVGSNHENSSLSVAGSNGNSGGSGGGGASGGAGSGSGNGSIITSPKTYSYINSTHLTKGKLIEHRKRLLTNFLNNCLEI... | Function: Required for cytoplasm to vacuole transport (Cvt), pexophagy and mitophagy. Also involved in endoplasmic reticulum-specific autophagic process and is essential for the survival of cells subjected to severe ER stress. Functions in protein retrieval from the endocytic pathway (By similarity).
Location Topology:... |
Q6FR93 | MGRSKRSKKKSLAHLQSDGKDKLSSEENISRGSEVEESPENFEEAQDYGDSLKDTDEQSDSITAIRSVTGGTASTITDLNNKFKSQELVDNEKVEINTKSTEEVGCKPSTDHSTEALDEGHDTGISSTNKDDSDVRIIGDDNEDSEAIESVDIKGKVSSGISDADVLKPQEELVHTAILENDNPFYDANKEISGSKKLDEKVNSVDSMAETTKVNSGDSKQRMGDLVVRRSENLHNPNLDYEEEDEILVSNTDTNKHSKESSSALNNANMKSFGNAVKSYTKKSGKHVRILEAKKVSEGQSRTFVAYFIKYNGHMVRRRY... | Function: Required for cytoplasm to vacuole transport (Cvt), pexophagy and mitophagy. Also involved in endoplasmic reticulum-specific autophagic process and is essential for the survival of cells subjected to severe ER stress. Functions in protein retrieval from the endocytic pathway (By similarity).
Location Topology:... |
Q6BZE1 | MNPNDNNLFGDIEQDNNPSFYGNQSFLRDPYGKSKQTCPPSVTSNGDPSITNDDNNSAHNNDLVSNSIVLSKKIEQMVNDPNLQINVISSERMINSSVVAYSIELSSFDDNRMIVKRRYSEFKSLRDNLQILFPTLVIPPIPEKHTLFTYLINSIDNSKELNIIETRKRCFANFLKDIIFDSNVALKSCVLVHKFLDPNYELCWNNAVNEPPVSLIPNNLLLANPVNPTDQNGLYSLLPIVNGFELNSNIDNISSLHKLNEDLHKLNEQVHVFELRKEQNERRHPSEPTTSLFTEIPISLIDFEKNFHQNIKVLTELNKL... | Function: Required for cytoplasm to vacuole transport (Cvt), pexophagy and mitophagy. Also involved in endoplasmic reticulum-specific autophagic process and is essential for the survival of cells subjected to severe ER stress. Functions in protein retrieval from the endocytic pathway (By similarity).
Location Topology:... |
A0A098DRQ4 | MWNDEDNNPYGTSFDRRDSQSSSINPTSPSTREYQRFEPPQTPTSDSDNEHNHGVIHDDSDDDDEDLTQDAGPKRKPGGYDSRIEQILYENPKLSILITDAGKSIESGGRYIVYTIKTGDLEVRRRYSEFASLRDALTRLHPTLIVPPIPEKHTMADYAANPTNAKQDQQIIDLRKRMLAVFLNRCRRMEEIRTDGVWWRFFDPNASWSEVLHSHPVASIPKSILKAPPLNPANPTPAHNYLPIPAASAKLKTVAGTNHDNSSGHIQAGPHAFGRFPPEGHNLGEQELDPYFISYESSIKDLEQLLTGPMEKVNRRTLSH... | Function: Required for cytoplasm to vacuole transport (Cvt), pexophagy and mitophagy (By similarity). Also involved in endoplasmic reticulum-specific autophagic process and is essential for the survival of cells subjected to severe ER stress (By similarity). Functions in protein retrieval from the endocytic pathway. Re... |
Q6CNX6 | MQINFEPMPNSVTHLENNSPSRLKNNKTVEEHKEHEPDLQTQSEMRRESNGSPKDTAVTNQNGDQPHENVIHTQIIKKDNPFFNYMQDNVDGSDENGKNDDDDENAKNAGSDDNEDQLLQPNRRKNSKERRRSSVATSKDSSPDVPYNTLNHNASGMTKEGKKRAQILEASKVSEGQGRTYIAYAIKYGDSIVKRRYSDFESLRKVLVKLFPISLIPPIPEKQSLKSYGKAMTYSKSSYLLPTESGDSVDLSLSVINGPVTTNDEKLIRHRIRMLTSFLNRLLKNQEITKTSIVYDFLDPNNKNWNDLITSSLTISSLPK... | Function: Required for cytoplasm to vacuole transport (Cvt), pexophagy and mitophagy. Also involved in endoplasmic reticulum-specific autophagic process and is essential for the survival of cells subjected to severe ER stress. Functions in protein retrieval from the endocytic pathway (By similarity).
Location Topology:... |
Q9USM8 | MAQDDSYEEKPEVISSDSGGSGYSTEIQIVGTVTSSDGSYVEYEIVHQKRSVWRRYSDFESLVKLMRRQYPAAIVPPIPGKQSLLSYAKHPRKAKSDAEFLNFRSRMLELFLRQCLLHPCIRSNPIFDKFIHSTVSWHVTLSSLDLPKDSNTDPLRLPPIATEHDPFAHLRSSMPLVMANSLSPPSSRALKPIHSLSNPSTASSLEPSSPLGSEDECHPPTSDMQPTHELNESPSTPTAPDFPHYNSSPSELSPTQRRSSISNGKDAPSPVLKDLTSYTQEVIVCRKFLHHSLSPSIHSTLSSISKMESCLSKLGSAFHS... | Function: Required for cytoplasm to vacuole transport (Cvt), pexophagy and mitophagy. Also involved in endoplasmic reticulum-specific autophagic process and is essential for the survival of cells subjected to severe ER stress. Functions in protein retrieval from the endocytic pathway (By similarity).
Location Topology:... |
A7TIP6 | MKQKKNRFGSGKRITDQSSVDGDLIAPGNSSMDKRRNSSSSRSSSTQESKELTESLASVHTSDMHQSNIHERIDGDDNPFLDQDDESFKSTRANTSATKLTDVVNPNAEYKDNDSDNDEEILTATAPDTSITEGIVSTEADGGNDVVTASVEDKEGTVTDTAVGLDNANNTVDQKVKESIIPDIKLINDRVQILEANKVSEGQGRAYVAYTIKWGDQSVRRRYSDFESLRSVLMKLFPTSLLPPIPEKQTLKNYSKSIAGSKSNYLLPSEGTGSVDLVLSVINGTVTNNDEKLIRHRIRMLTSFLNKLLQDEEILKTPII... | Function: Required for cytoplasm to vacuole transport (Cvt), pexophagy and mitophagy. Also involved in endoplasmic reticulum-specific autophagic process and is essential for the survival of cells subjected to severe ER stress. Functions in protein retrieval from the endocytic pathway (By similarity).
Location Topology:... |
Q07528 | MSDLNDVQENAKLNSETRNTGKAEPPHGTTEYVAEAEISKNGVGSPKKSPKKGKVGKGDNNKVETELVHTALLEKDNPFMEEGPTGFTKSALLEIPGMRSHNLKNPNEDYEDDSEGLLPLNQESNAETCRTSLSGSINSMNGETSASEEPSVSNRKKSARIHILEAKRVSEGQGRAYIAYVIQFENSTVQRRYSDFESLRSILIRLFPMTLIPPIPEKQSIKNYGKSITGSSSKYLLPSEGSGSVDLSLSVIHASVNNSDEKLIRHRIRMLTEFLNKLLTNEEITKTSIITDFLDPNNHNWHEFVNSSSTFSSLPKSILQ... | Function: Required for cytoplasm to vacuole transport (Cvt), pexophagy and mitophagy. Also involved in endoplasmic reticulum-specific autophagic process and is essential for the survival of cells subjected to severe ER stress. Functions in protein retrieval from the endocytic pathway. Required for proper sorting of the... |
Q5AI22 | MVTINDLSFNPDYSSISVSTSDGFKIFNCEPFGEFYSSQESPLRKSISNSLEDSAGCQNPTHSKTDSQDTPARFPTAFLKMLFSTSLTIVVPQTQDNLGNRLLKIYNLKQNLKICELNFPSSIIDIKLNRKRLLVVLDTGQLYIYDLSCVRLLKILQLSFNEHDGDQKFIGDLSADDSSWLIIPVQSTNNQTDLLNAETGSQPSTPKLTPSDSVINTGSYSQYLEFTRNSSLSNLKKKNKLITLEDIKNDSEGWVVVYDTINLAPVVIFEAHHSTIARICISHRDNKVATASIKGTIIRIFDLKEFEGKVKVHKVKNLRR... | Function: Required for cytoplasm to vacuole transport (Cvt) vesicles formation and mitophagy. Involved in binding of phosphatidylethanolamine to ATG8 and in recruitment of ATG8 and ATG5 to the pre-autophagosomal structure. Protects ATG8 from ARG4-mediated cleavage (By similarity).
Location Topology: Peripheral membrane... |
Q6CLZ2 | MALKLLGFNQDATCFSVISSNKGVTIYNCDPFGKCFELEKSTSNDEELDFLVEMLFSTSLIAVVDKTIGASKRKKLKIVNTKRKATICELTFPHEIMDVIMNRKIICVVLKSDQIFVYDISCMKLLRTIDVRGEKLKSTSKFRNSEAVGDIGVRVSLSTDNNSILCYSSYSKSDKENAPLNDIVVFDALKCIQINVLPAVHQSNIVCIACSPDGMLMATASEKGTIIRVFKTIDTENDEPILVNEFRRGSRPSRISEMKFNHDNTLLACVGESDTIHIFALPVTTTEADANEDDTLQQSSHSLSSSINGLQYISKGLANR... | Function: Required for cytoplasm to vacuole transport (Cvt) vesicles formation and mitophagy. Involved in binding of phosphatidylethanolamine to ATG8 and in recruitment of ATG8 and ATG5 to the pre-autophagosomal structure. Protects ATG8 from ARG4-mediated cleavage (By similarity).
Location Topology: Peripheral membrane... |
Q5QJC0 | MALRSISFNQDYTCLAAGFDAAYKVYNCDPFGECFQKADDGGANLVEMLFSTSLIAVVGIGDKPANTMRKLKIINTKRKAVICELTFPTAILYVKMNRKRLVVVLVDQIFVYDVSCMKLLHSIEASAGLDDRIICDLCADDESVLVFQQSGSSDELAANAGTVVVFDALQIQPINVIECHRSPLQRIAVSKDGRLLATASVKGTIVRVFRVADGRKVHEFRRGSYTAQISCLSFNVDATVLCCSSNTGTVHFFRLDDVDRRRSTGSIDANIDGSETLPRESSITEEESSEINRLINSQLGGHNGFAKKKSAESLKNFIWS... | Function: Involved in peroxisome sequestration to the vacuole during macropexophagy. Also required for microautophagy.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 42854
Sequence Length: 388
Domain: Contains a beta-propeller domain involved in specific binding to phosphatidylinositol 3,5-bisphosph... |
Q8S929 | MKALCDRFVPQQCSSSSKSDTHDKSPLVSDSGPSDNKSKFTLWSNVFTSSSSVSQPYRESSTSGHKQVCTTRNGWTAFVKRVSMASGAIRRFQERVLGPNRTGLPSTTSDVWLLGVCYKISADENSGETDTGTVLAALQLDFSSKILMTYRKGFEPFRDTTYTSDVNWGCMIRSSQMLFAQALLFHRLGRAWTKKSELPEQEYLETLEPFGDSEPSAFSIHNLIIAGASYGLAAGSWVGPYAICRAWESLACKKRKQTDSKNQTLPMAVHIVSGSEDGERGGAPILCIEDATKSCLEFSKGQSEWTPIILLVPLVLGLDS... | Function: Cysteine protease that plays a key role in autophagy by mediating both proteolytic activation and delipidation of ATG8 family proteins. The protease activity is required for proteolytic activation of ATG8 family proteins: cleaves the C-terminal amino acid of ATG8 proteins to reveal a C-terminal glycine (By si... |
Q8WYN0 | MESVLSKYEDQITIFTDYLEEYPDTDELVWILGKQHLLKTEKSKLLSDISARLWFTYRRKFSPIGGTGPSSDAGWGCMLRCGQMMLAQALICRHLGRDWSWEKQKEQPKEYQRILQCFLDRKDCCYSIHQMAQMGVGEGKSIGEWFGPNTVAQVLKKLALFDEWNSLAVYVSMDNTVVIEDIKKMCRVLPLSADTAGDRPPDSLTASNQSKGTSAYCSAWKPLLLIVPLRLGINQINPVYVDAFKECFKMPQSLGALGGKPNNAYYFIGFLGDELIFLDPHTTQTFVDTEENGTVNDQTFHCLQSPQRMNILNLDPSVAL... | Function: Cysteine protease that plays a key role in autophagy by mediating both proteolytic activation and delipidation of ATG8 family proteins . The protease activity is required for proteolytic activation of ATG8 family proteins: cleaves the C-terminal amino acid of ATG8 proteins to reveal a C-terminal glycine . Exp... |
Q9M1Y0 | MKAICDRFVPSKCSSSSTSEKRDISSPTSLVSDSASSDNKSNLTLCSDVVASSSPVSQLCREASTSGHNPVCTTHSSWTVILKTASMASGAIRRFQDRVLGPSRTGISSSTSEIWLLGVCYKISEGESSEEADAGRVLAAFRQDFSSLILMTYRRGFEPIGDTTYTSDVNWGCMLRSGQMLFAQALLFQRLGRSWRKKDSEPADEKYLEILELFGDTEASAFSIHNLILAGESYGLAAGSWVGPYAVCRSWESLARKNKEETDDKHKSFSMAVHIVSGSEDGERGGAPILCIEDVTKTCLEFSEGETEWPPILLLVPLVL... | Function: Cysteine protease that plays a key role in autophagy by mediating both proteolytic activation and delipidation of ATG8 family proteins. The protease activity is required for proteolytic activation of ATG8 family proteins: cleaves the C-terminal amino acid of ATG8 proteins to reveal a C-terminal glycine (By si... |
Q6PZ03 | MDAATLTYDTLRFAEFEDFPETSEPVWILGRKYSVLTEKDEILADVASRLWFTYRKNFPAIGGTGPTSDTGWGCMLRCGQMIFAQALVCRHLGRDWRWTQRKRQPDSYCSVLQAFLDRKDSCYSIHQIAQMGVGEGKSIGQWYGPNTVAQVLKKLAVFDTWSALAVHVAMDNTVVMADIRRLCRSSLPCAGAEAFPADSERHCNGFPAGAEGGGRAAPWRPLVLLIPLRLGLADVNAAYAGTLKHCFRMPQSLGVIGGKPNSAHYFIGYVGEELIYLDPHTTQPAVAAADRCPVPDESFHCQHPPGRMSIAELDPSIAVG... | Function: Cysteine protease that plays a key role in autophagy by mediating both proteolytic activation and delipidation of ATG8 family proteins. Required for canonical autophagy (macroautophagy), non-canonical autophagy as well as for mitophagy. The protease activity is required for proteolytic activation of ATG8 fami... |
Q9Y4P1 | MDAATLTYDTLRFAEFEDFPETSEPVWILGRKYSIFTEKDEILSDVASRLWFTYRKNFPAIGGTGPTSDTGWGCMLRCGQMIFAQALVCRHLGRDWRWTQRKRQPDSYFSVLNAFIDRKDSYYSIHQIAQMGVGEGKSIGQWYGPNTVAQVLKKLAVFDTWSSLAVHIAMDNTVVMEEIRRLCRTSVPCAGATAFPADSDRHCNGFPAGAEVTNRPSPWRPLVLLIPLRLGLTDINEAYVETLKHCFMMPQSLGVIGGKPNSAHYFIGYVGEELIYLDPHTTQPAVEPTDGCFIPDESFHCQHPPCRMSIAELDPSIAVG... | Function: Cysteine protease that plays a key role in autophagy by mediating both proteolytic activation and delipidation of ATG8 family proteins . Required for canonical autophagy (macroautophagy), non-canonical autophagy as well as for mitophagy . The protease activity is required for proteolytic activation of ATG8 fa... |
Q2XPP4 | MTSLPDRGVSSSSSDPLCEGNIAPCSSSSEQKEDCSLKQSKTSILSCVFNSPFNIFEAHQDSSANKSPKSSSGSYDWLRVLRRIVCSGSMWRFLGTSKVLTSSDVWFLGKCYKLSSEESSSDSDSESGHATFLEDFSSRIWITYRRGFDAISDSKYTSDVNWGCMVRSSQMLVAQALIFHHLGRSWRRPSEKPYNPEYIGILHMFGDSEACAFSIHNLLQAGNSYGLAAGSWVGPYAMCRAWQTLVRTNREQHEVVDGNESFPMALYVVSGDEDGERGGAPVVCIDVAAQLCCDFNKGQSTWSPILLLVPLVLGLDKINP... | Function: Cysteine protease that plays a key role in autophagy by mediating both proteolytic activation and delipidation of ATG8 family proteins . The protease activity is required for proteolytic activation of ATG8 family proteins: cleaves the C-terminal amino acid of ATG8 proteins to reveal a C-terminal glycine . Exp... |
Q96DT6 | MEATGTDEVDKLKTKFISAWNNMKYSWVLKTKTYFSRNSPVLLLGKCYHFKYEDEDKTLPAESGCTIEDHVIAGNVEEFRKDFISRIWLTYREEFPQIEGSALTTDCGWGCTLRTGQMLLAQGLILHFLGRAWTWPDALNIENSDSESWTSHTVKKFTASFEASLSGEREFKTPTISLKETIGKYSDDHEMRNEVYHRKIISWFGDSPLALFGLHQLIEYGKKSGKKAGDWYGPAVVAHILRKAVEEARHPDLQGITIYVAQDCTVYNSDVIDKQSASMTSDNADDKAVIILVPVRLGGERTNTDYLEFVKGILSLEYCV... | Function: Cysteine protease that plays a key role in autophagy by mediating both proteolytic activation and delipidation of ATG8 family proteins . The protease activity is required for proteolytic activation of ATG8 family proteins: cleaves the C-terminal amino acid of ATG8 proteins MAP1LC3 and GABARAPL2, to reveal a C... |
O74312 | MFYQPAQNKKQYDDLADIEAQNNVPNTQEVLEAWQESLDSDEDESSPLEESNGFTISEHDDFVKSVPRKNNPTDLLYSGKLLDSDEPPSVHGNSSKVPSKHPSPSFPETTSLRNLQNGSKQKPALPNFNDPHFYNEDVTRSGHPNRSIYTQLPRNEFSNARVLWNRLSARDRVLWRWANVENLDSFLQQVYTYYTGKGLSCIIVHRLFQILTVSFVIGFTTFITSCIDWPAVTPHGSLAGVTKSQCIAQMSPITYLVLWLFLSFLLALWIYYLTDIPRLWQMREFYIHALKIATADMPTVSWQRVLYRLLKLKNVNALTA... | Function: Phospholipid scramblase involved in autophagy and cytoplasm to vacuole transport (Cvt) vesicle formation . Cycles between the preautophagosomal structure/phagophore assembly site (PAS) and the cytoplasmic vesicle pool and supplies membrane for the growing autophagosome (By similarity). Lipid scramblase activi... |
Q4P683 | MDRDSPFADPDRSDPLPAPSNTLKASIFAQSRIVHPSTSVYNQFGRHRHDDIGQESFHEGIQPSVASLANLQGSYTAKSIHPHHSAIGLRNSSYDDHGDDADEQDPEDLLSDEELGLIAGDARNPSASLSYASNRSRKRRTNPSDPRSRASAVGGLSAKQKALWMWANVDNLDAFLQEVYAYYVGRGAICIALSRSLNLLTVAFVICFSTFLFGCIDYSSIRHDGQLSDVIVGHCVAGFSPFATLVVVLLLAAFGWQAVQFVLGLSRLRAMHRFYEQLLGIPDADVQSIPWHEVVNRLSALRDQHPTTSLSSADEMELGQ... | Function: Phospholipid scramblase involved in autophagy and cytoplasm to vacuole transport (Cvt) vesicle formation. Cycles between the preautophagosomal structure/phagophore assembly site (PAS) and the cytoplasmic vesicle pool and supplies membrane for the growing autophagosome. Lipid scramblase activity plays a key ro... |
Q6C2F5 | MTDKSTFLSVLFGGGSVYQDLDGDGEVEDAEILRRVEEEHAQTSDNSNSDNDSGNDSDVPTSLMVEGVQDPKPGSKRRQPHRMATLSNLQSSAGPGARSVSFAQGTKTQTPIRLTKPTGVANGGLPRHKQDLGASIRTMVDPKELALWKWANVQNLDNFFAEAYMYYTGKGLVSIILSRVLNMSTIMFVVVFSTYLGSCIDYSKIKGSRTLDEVHVKQCYAKLGSFHVFVLWTFFVLWFMKLFQYVKDIRRLVDMKSFYQELLEIDENELQTISWPQVAKRMATLSEANAATQVGNSTKQRIEPHDIANRVMRKENYLVA... | Function: Phospholipid scramblase involved in autophagy and cytoplasm to vacuole transport (Cvt) vesicle formation. Cycles between the preautophagosomal structure/phagophore assembly site (PAS) and the cytoplasmic vesicle pool and supplies membrane for the growing autophagosome. Lipid scramblase activity plays a key ro... |
Q12142 | MERDEYQLPNSHGKNTFLSRIFGLQSDEVNPSLNSQEMSNFPLPDIERGSSLLHSTNDSREDVDENDLRVPESDQGTSTEEEDEVDEEQVQAYAPQISDGLDGDHQLNSVTSKENVLETEKSNLERLVEGSTDDSVPKVGQLSSEEEEDNEFINNDGFDDDTPLFQKSKIHEFSSKKSNTIEDGKRPLFFRHILQNNRPQRDTQKLFTSSNAIHHDKDKSANNGPRNINGNQKHGTKYFGSATQPRFTGSPLNNTNRFTKLFPLRKPNLLSNISVLNNTPEDRINTLSVKERALWKWANVENLDIFLQDVYNYYLGNGFY... | Function: Phospholipid scramblase involved in autophagy and cytoplasm to vacuole transport (Cvt) vesicle formation . Cycles between the preautophagosomal structure/phagophore assembly site (PAS) and the cytoplasmic vesicle pool and supplies membrane for the growing autophagosome . Lipid scramblase activity plays a key ... |
O25711 | MIQSVRIKNFKNFKNTKIDGFTKLNIITGQNNAGKSNLLEALYYLVGKSMHPCTNVLEIYDNIRKEPLTSESKSLMFYGLDTKEEIQIVTTLDNNQTLDLQIKFIASENQKVIESQIIPTAEQTQMSSQLNFTLKKNNEEIYNDHLNIAKVPNFPPIPNQSGYNRQFKNFDSNQLQKLLPFESAVIIPSDVVYRQAHMIQAVSKICSNNQLEEELNKHLNQFDNNIQAISFNTNNQLKLKVKDIKEKVPLSVFGDGLKKYLHIVSAFMADNAKTIYIDEVENGLHFSRMRLLLKNTIDFINNNKDGNLQVFMTTHSQEFI... | Function: Has nucleotide phosphatase activity toward ATP and GTP, but not toward CTP, TTP and ADP.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 42920
Sequence Length: 370
EC: 3.6.1.-
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Q9YAC2 | MFEIRDVDLAGRIGRIYTQHGVVETPAFFPVIDVYRQEVSVDEVRAAGFGQVITNAYLLWKRFGWEAAEKGVHRILGFPGVVMTDSGAYQILEYGGVELSQGEVVEYQKRLGSDIAVILDIPTGDVGRREAEESVRETIRRALEARVMIEGDERIWVYPVQGGRYFDLVEESARVGGRLGFYRMYGIGSPTVFLERYMYHVVVEAVYRAKKHLPWGRPVHLFGAGHPLIFPYAVALGVDTFDSASYILYAREGRYITEYGVYRIEDLDYLPCSCPVCSRYTPQELREMDRVERTRLLALHNLYVISASMRRVKQAIREGR... | Cofactor: Binds 1 zinc ion per subunit.
Function: Exchanges the guanine residue with 7-cyano-7-deazaguanine (preQ0) at position 15 in the dihydrouridine loop (D-loop) of archaeal tRNAs.
Catalytic Activity: 7-cyano-7-deazaguanine + guanosine(15) in tRNA = 7-cyano-7-carbaguanosine(15) in tRNA + guanine
Sequence Mass (Da)... |
Q1IS49 | MPHQLWFTAFLNQYLAGPVSAMMSVLHVPNPHPRAPISNYVAMEILVFLLLVLFFIATRISLSWDKPGVLQHIAEGMNNFVSNQGEEMIGHGYETYTSYIVTLGVFILSMNLIGLIPGFEAPTAFPSVPLGCALVTWFFYHVHGLRENGVIGYLKHFLGPVWWISPLLFVIEICSHFARIMSLTIRLYANMFAGDMVTLAFFSLVPLGFPVVFMGLHIFVSLIQTYIFITLAAVYLAEATAHGHD | Function: Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 27397
Sequence Length: 245
Subcellular Location: Cell inner membrane
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Q5ZWN4 | MGEEGFLAHFAFSIGGLPITQSVLTTWFIMISLFIMAWSTTYKCSLLQPSTYQLIWEGVLSTMYDAIKEVLPEHVELIFPFVATLWIFILVSNLIGVIPGFYSPTADLSVTASLAIMTFLSVHWFGIRAEGWREYLKHYIKPTPFLLPFHLISEISRTLALAVRLFGNIMSLQLTALIVLMIAGFLVPIPILILHIIEAIIQAYIFGMLALIYIAGGIQAHELKSQGESL | Function: Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 25723
Sequence Length: 230
Subcellular Location: Cell inner membrane
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A5VIQ5 | MGGDALTFKLFGLTFNTTNIVSGLIIYAIVFFTLYGMSRKIQMKPTGAQNVFEWLVDFTNGIVRSQMPASEQGHYSFFAFVLFVFIFFANQFGLIFQFHWNGAEVLRSPTADPVVTLTLSLMVMVLAFAAGVAHNGLGGYLKGYTKPFTLMLPVNIIEDFANFLTLGLRIFGNIFAGELLMSLIANMAFSHGILTIIPGLFLELAWQGFSVFIGSIQAYVFVTLTTVYISRKISE | Function: Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 26045
Sequence Length: 235
Subcellular Location: Cell membrane
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Q37601 | MFNSPLEQFEILPLLSFGANLFDFSITNAMLTTCVSLSFFLFLFYCLFSYGLNSFPTRWQLVLEGLYTSTAGLVWDSVGPRRPKVFPFLFVIFSFILISNVQGLVPYSFTITSHLIQTMVLALTVFIGVIIIVLAHGFHMLSLFLPGGTSIVLAFLLVPIEIVSYVFKPLSLAVRLFANMMAGHTLLKVIAAVAWAMMGSGGLLLIAHIVPLGVLVILFGLELAVALIQAYVFTILSCIYINDAIVLH | Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramemb... |
O05330 | MFDGEAIRWFEFFVPTNSTLWMAIGVLMIALLMVVGTLRRAIVPGRIQSLAELTYGFIHKMVEDVAGKDGLVYFPYIFTLFLFILFSNFLGLIPMAFTPTSHIAVTGVMAMGVFIGVTALGFMKHGSHFLNLFWVSAAPLPLRPILAVIEVISYFVRPVSHSIRLAGNMMAGHAVMEVFAAFAPLILFSFVGVIVTPLSVLAIVAMYALEILVAFVQAYVFTILTCVYLKDALHPGH | Function: Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 26096
Sequence Length: 237
Subcellular Location: Cellular chromatophore membrane
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C1A1Y4 | MMAADRLRERTLSVTTLAADEFHAPSLDDFFPPSVLIHAGPFELDRLMLIRLLMSVLVAAFFVIAMRSPRLVPRGMQNAAELALDFVRINIAEEILGKEQGKRFLPVITTIFFIVVASNMASIIPFLNISPNARIGMPLVLAALAYIVFNYVGIKKYGFFKYVKSSIVVPGVPLPLHFLLVPIEFISTFILRPFTLMVRLMANMLAGHILLVLFFSATNYFFFVSGGFQAIFGVPSIIAGIAFTFFELLVIFLQAYVFALLTAVYIELALHADEH | Function: Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 30671
Sequence Length: 275
Subcellular Location: Cell membrane
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Q9B6H6 | MTTNLFNIFDPSTTIFNLEMNWISTLLIILFMPNFLWILPNRMNWLLFKMFNMLNNEMLMLYKMKKTKSPAFLFISLFMFILLNNFFSLFPYIFSSSSHMVFSVTLAIPFWMFFIILSTCKNTKNMIAHLIPLNTPIYLAPLMTIIETMSIIIRPMSLSIRLTANLIAGHLLMTLLNFNSLMIIIIFIQMFMMIFELCVALIQSYVFSILSSLYSSE | Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramemb... |
P24499 | MFLFFFCDLFWLRLLLCMYYCVSRLCFIVYFNCLMLIFDFLLFCLFDLYLFVGLCLFLLLWFMLFNLYSLILYYCITYLNLYLLFCIVFLLYIAFLFLFCFLCDFFLFNNLLVGDSFMDVFFIRFLLCFLECFSLLCRCLSTFLRLFCNLLSSHFLLLMFFDFFYFIFVFFFYGVFCYFILFIFVFCFCLLFYVFLYLLDLFAAILQLFIFCNMILQLIMDFLLFLLFV | Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramemb... |
Q0H8Y6 | MAFLIHSPLEQFEVTSLISLNLPVLGYINLSLTNLGLYTILTVYLVLALHIMGSNNKQLIPSRWSIALESSFASVHGLVKSQIGAANEMYLPFIYSLFFFILIANLSGNVPYGFTVATSIMVSIGLSMTIFIGVTILGLRLHKVHFFSFFVPSGTPLGLVPLLVPIELISYLARAFSLGVRLFANVTAGHVLMKILAGFLAPLFTSTFIISVLTVLPFIIFTGIIGLEIAVSFIQAYVFCVLTCSYLKDAIDLH | Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramemb... |
P12984 | MAAPGEALTSSGYIAHHLSNLSLYKLGLVGSETSFWNVHIDSLFFSWFTGLIFLGIFYKVAKRTTAGVPGKLQCAVEMIVEFVADNVKDTFHGRNPLIAPLALTIFCWVFLMNVMDLVPIDFLPYPAEHWLGIPYLKVVPSADVNITMAMALGVFALMIYYSIKVKGLGGFAKELALHPFNHPLMIPFNLLIEVVSLLAKPLSLGMRLFGNMFAGEVVFILCAAMLPWYLQWMGSLPWAIFHILVITIQAFVFMMLTIVYLSMAHEDPDH | Function: Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 30134
Sequence Length: 270
Subcellular Location: Cell inner membrane
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A5F473 | MAAPGEALTPSSYITHHLTNLSTYKLGLVAEESSFWNVHIDSLFFSVLTGLIFLGVFRAVARKATAGVPGKLQCAVEMVVEFVDKNVKDTFHGRNPLIAPLALTIFCWVFLMNLMDLVPIDFLPYPAQHWLGIPYLKVVPSADVNITMAMALGVFALMIYYSIKVKGLGGFAKELALHPFNHWIMIPFNLLIEVVSLLAKPLSLGMRLFGNMFAGEVVFILCAAMLPWYLQWMGSLPWAIFHILVILIQSFVFMMLTIVYMSMAHEDNDH | Function: Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 30227
Sequence Length: 270
Subcellular Location: Cell inner membrane
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Q04654 | MNLYLQLDLYLYNDNLYLYLYLESGVVPIPSPLEQFEIIPFLPMKIGDLYFSFTNPSLFMLLTLSLVLLLVHFVTKKGGGKSVPNAWQSLVELIYDFVPNLVNEQIGGLSGNVKQQFFPCIFVTFTFLLFCNLQGMIPYSFTVTSHFLITLGLSFSIFIGITIVGFQRNGLHFLSFLLPAGVPLPLAPFLVLLELISYCFRALSLGIRLFANMMAGHSLVKILSGFAWTMLCMNDLLYFIGDLGPLFIVLALTGPELGVAISQAHVSTISICIYLNDATNLHQTCLLFIYN | Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramemb... |
Q3T4E5 | MVAAAKILGAGLATIGLAGAGVGVGLVFAALINSTSRNPSLRPQLFSYTILGFALTEAIGLFALMMAFLLLYAA | Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramemb... |
P21537 | MIQAAKYIGAGLATIGVSGAGVGIGLIFSNLISGTSRNPSVRPHLFSMAILGFALTEATGLFCLMLAFLIIYAA | Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramemb... |
P60117 | MLEGAKLMGAGAATIALAGAAIGIGNVFSSLIHSVARNPSLAKQLFGYAILGFALTEAIALFALMMAFLISFVF | Function: This protein is one of the chains of the nonenzymatic membrane component (F0) of mitochondrial ATPase.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 7563
Sequence Length: 74
Subcellular Location: Mitochondrion membrane
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P60114 | MLEGAKLMGAGAATIALAGAAIGIGNVFSSLIHSVARNPSLAKQLFGYAILGFALTEAIALFALMMAFLILFVF | Function: This protein is one of the chains of the nonenzymatic membrane component (F0) of mitochondrial ATPase.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 7589
Sequence Length: 74
Subcellular Location: Mitochondrion membrane
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Q01554 | MIQAAKIIGTGLATTGLIGAGVGIGVVFGALILGVARNPSLRGLLFSYAILGFAFSEATGLFALMMAFLLLYVA | Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramemb... |
P61829 | MQLVLAAKYIGAGISTIGLLGAGIGIAIVFAALINGVSRNPSIKDTVFPMAILGFALSEATGLFCLMVSFLLLFGV | Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramemb... |
Q2GIG2 | MSGVSSGEVLKILRERIENFGGPVKAGSVGEVLSVKDGIAVVYGLHGAGFGETVAFASGVRGVISGLESDIASVVIFGEDREVKEGDSVECTGELMKVPVGFSLLGRVVSPLGMPLDGEGAISGCDGENPVEVKAPGIMARQPVSEPLQTGIKTIDMLIPIGRGQRELIIGDRKTGKTAIALDTIINQKRYNDRAASEKDKVYCIYVAIGQKNSSIARVVSKLCEAGAADYTIVVATGASDSVPLQYLAPYAACAMGEFFRDNGMHCLIVYDDLSKHAVAYRQMSLLLRRPPGREAYPGDVFYIHSRLLERAAKLSDALG... | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.
Catalytic Activity: ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 54102
Sequence Length: 506
Subcellular Location... |
P56757 | MVTIRADEISNIIRERIEQYNREVTIVNTGTVLQVGDGIARIYGLDEVMAGELVEFEEGTIGIALNLESNNVGVVLMGDGLMIQEGSSVKATGKIAQIPVSEAYLGRVINALANPIDGRGKISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATDTILNQQGQNVICVYVAIGQKASSVAQVVTSLQERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYREQHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSSQLGEGSMTALPIV... | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.
Catalytic Activity: ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 55328
Sequence Length: 507
Subcellular Location... |
B8DYT2 | MKEEVLGLPIDKIEKKIKEYDFSPRISNIGYVKHVGDGVAEVSLLNSAFIGEMVVFESGIQGMVLSLKEDSVGVILFGKDEYVKEGDVVYSTSKILQVPTGNGFLGRVIDPLGNPIDGGGLIFPEAYVPIDNEAPSIFDREPVKEPLYTGIRTIDALIPIGHGQRELILGDRQTGKTTIALDTIISQKNYGTICIYVAIAQKRTNIARIVQTLREYGALSNTIVIATFPDEPPALRYIAPMAGCAMGEYFMRQGERVLIVYDDLTKHANTYREVALLLRRVPGREAYPGDIFYLHAHLLERAAKLNKRLGGGALTALPIA... | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.
Catalytic Activity: ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 56466
Sequence Length: 508
Subcellular Location... |
B1NWD5 | MVTIRADEISNIIRERIEQYNREVKIVNTGTVLQVGDGIARIYGLDEVMAGELVEFEEGTIGIALNLESNNVGVVLMGDGLMIQEGSSVKATGRIAQIPVSEAYLGRVINALAKPIDGRGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATDTILNQQGQNVICVYVAIGQKASSVAQVVTTLQERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRERHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSSRLGEGSMTALPIV... | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.
Catalytic Activity: ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 55599
Sequence Length: 507
Subcellular Location... |
Q0AUD1 | MSIRPEEISAILKEQIERYQSEVEVSNVGSVIYVGDGIARVYGLQGAMAGELLEFTGGTFGMVLNLEEDNVGAVLLGEYNHIKEGDVVKATGRIMEVPAGSAMLGRVVNALGQPIDGKGPINTTAFRPLEKVAHGVVTRQPVTTPMQTGLKAIDSMVPIGRGQRELIIGDRQIGKTAIALDSIINQREKKDLICIYVAVGQKQASIAGIAAKFEEMGAMDYTIIVAATASEPAPLLYMAPYAGVAMAEEFMEAEGKDVLIIYDDLSKHAVAYREMSLLLRRPPGREAYPGDVFYLHSRLLERACRLNPDHGGGSITALPI... | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.
Catalytic Activity: ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 54508
Sequence Length: 504
Subcellular Location... |
Q9X1U7 | MRINPGEITKVLEEKIKSFEEKIDLEDTGKVIQVGDGIARAYGLNKVMVSELVEFVETGVKGVAFNLEEDNVGIIILGEYKDIKEGHTVRRLKRIIEVPVGEELLGRVVNPLGEPLDGKGPINAKNFRPIEIKAPGVIYRKPVDTPLQTGIKAIDSMIPIGRGQRELIIGDRQTGKTAIAIDTIINQKGQGVYCIYVAIGQKKSAIARIIDKLRQYGAMEYTTVVVASASDPASLQYIAPYAGCAMGEYFAYSGRDALVVYDDLSKHAVAYRQLSLLMRRPPGREAYPGDIFYLHSRLLERAVRLNDKLGGGSLTALPIV... | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.
Catalytic Activity: ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 56062
Sequence Length: 503
Subcellular Location... |
Q2IHQ2 | MPTATNVENGRITQVIGPVVDVEFPPGTLPDIYTALKVTNPGVDERQDNLVIEVAQHLGENTARCIAMDSTEGLVRGMPVKNTGAPISVPVGQEVLGRILNVVGEPVDERGPVAATKTLPIHRSAPLLTDLNVKVESFETGIKVIDLLAPYLRGGKIGLFGGAGVGKTVLLMELVNNVAKKRGGFSVFGGVGERTREGNDLYHEMIEAGVINKDDLSKSQCVLVYGQMNEPPGARARVALSALTVAEYFRDVENRDMLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLSTEMGELQERITSTQKGAITSVQAIYVPA... | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits.
Catalytic Activity: ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 52132
Sequence Length: 48... |
Q31794 | MKTNYLILGVSTLISKNVGHISQIIGPVLDVTFPPGKMPNIYNSLIVRGQNPAGQEINVTCEVQQLLGNNKVRAVAMSATDGLTRGMKVTDTGAPLSVPVGEVTLGRIFNVLGEPVDNLGAIDVSTTFPIHRSAPAFTQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESKVINEQDISESKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSIT... | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits.
Catalytic Activity: ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 53161
Sequence Length: 49... |
P31476 | MKSSLRLNTGIILQIIGPVMDISFPSGKMPNIYNSLLIEGKTESGDRLKVVCEVQQLLGDNVVRAIAMSATDGLQRGIKVIDTGAPLSVPVGVTTLGRIFNVLGESVDKMGLIDYSITLPIHRAAPSFVELDTQLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYQEMKESGVINDRNFKESKVALIYGQMNEPPGARMRVGLTALTMAEYFRDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLATEMGGLQERITSTKVGSITSIQAVYVPA... | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits.
Catalytic Activity: ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 52078
Sequence Length: 48... |
P85446 | KVHQVIGAVVDVKFRVPVGAGTLGRIINVTGDPIDERGKIGLFGGAGVGKTKVALVFGQMNEPPGARARFTQAGSEVSALLGRMRGISELGIYPAVDPLDSKSRVQQMLQEYKS | Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramemb... |
Q9BA86 | MRTNPTTSSPVVSTLEEKNLGRIAQIIGPVLDVVFPPGKMPNIYNALVVKSRDTVGQQINVTCEVQQLLGNNRVRAVAMSATDGLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINEKNIAESKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGS... | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits.
Catalytic Activity: ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 53834
Sequence Length: 49... |
A6L4L7 | MSQIIGHISQVIGPVVDVYFEGKGIDTDLLLPSIHDALTIKRNDGRILVVEVQQHIGEDTVRTVAMDSTDGLQRGMEVIPTGHPITMPVGNQIKGRLMNVVGEAVDGMRPLSKEGAFPIHREPPKFDELSTVQEVLFTGIKVIDLLEPYSKGGKIGLFGGAGVGKTVLIMELINNIAKKHNGFSVFAGVGERTREGNDLLREMIESGVIRYGEEFKKSMEEGHWDLSKVDYNEVEKSQATLVYGQMNEPPGARSSIALSGLTVAESFRDRKNGDSNGPRDILFFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMG... | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits.
Catalytic Activity: ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 56120
Sequence Length: 51... |
Q2PMV0 | MRINPTTSGPEVSALEKKNLGRIAQIIGPVLDVAFPPGKMPNIYNALIVKGRDTVGQQINVTCEVQQLLGNNRIRAVAMSATEGLMRGMEVIDTGAALSVPVGGATLGRIFNVLGEPIDNLGPVDTRTTSPIHRSAPAFIQLDTKLAIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINEQNIAESKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGS... | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits.
Catalytic Activity: ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 53755
Sequence Length: 49... |
Q7CWL8 | MPVAETSQGTSGVAERYASSLFELALEAGTVEAVQVELDKFGALLDESDDLKRLVASPVFSAEDQFKAISAICEKAGIAGLAVNFLKVVANNRRLFAVPGMIRAYRTIAAAHRGEITAEVTSAHALDEAQETELKAALKSVTGKDVAISVTVDPSILGGLIVKVGSRQIDTSLRTKLSTLKLALKEVG | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During c... |
Q0VKX1 | MAELTTIARPYAKAAFVFAKEHDALEQWEKMLGLAAAVAGDASMRAYLDQPELDDATKVSAFAEVCGDELDESGRNFVAQLTQNKRLPLLPIILQLFHELLAEQQQFTDVEMISAFELDDAATDKLVAALKKRLGTEVNVTTSVDQSLIGGVLVRAGDTVIDGSVRGRLNRLAEQLNS | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During c... |
A8EV73 | MKDLVAKRYVKALIDGRNSESINTISNKLNQVASAFADERFNSIISSPEISDKSKVDLIISFVDGTDNSLNNFIKLLGEKRRLDLLPFIAKDLNIQLAKMNNNYIGVVYTNQELSSDYISSIEKQFSKKFDVKLSLSQNVCDYDGIKVDIDGLGVEISFSKDRLKSQLIDHILKAV | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During c... |
Q5WB75 | MSNKAVANRYAVALFELAEEKGQTDVFERELELVQEVFETTPQLETVLAQPGLAADKKQALLRDAFQAHLSPAVMNTINLLMERGRYSEIVGLAGEYKQLNDDKKGIAEATVFSVKALSDSEKNQIAAVFAPKAGKRELRVVNVVDSALIGGLKVRVGDRVFDGSIQGQLKRLEKQLVAGQ | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During c... |
Q0A4M5 | MAEQTTLARPYAKAVFELTKDAKTRNTWSKRLQALGTVAADDQVAALVGNPRVSREQLIGLLLDAVGEDTLGQEGKNLVQLLADNGRLGLLPEIAALYEHLRAEAEGVVDVQVTSASKLTKEQQDQIAGALKKRLGRKVRLHCRTDEALIGGALIQAGDLTIDGSVRGKLARLSSAMAH | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During c... |
A6TK62 | MAELVAKRYAKALFQVAFEMNRYEDVTEELAFVAENLKQHSDLNELLKSPVITLGEKKEILSTIFKEQISPEVFNFLRILLDKSRQGDFQEIYEEYKILADAGKNKIEAVAITALPMDNNDLLKLQVNLSMSSGKNVKLKNEIDPTVIGGVLVKMGDKIIDGTVKARLNQMQDQLLQIIV | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During c... |
A8MJW2 | MAELVSKRYASALFELAFEEQKHHKVQEELAFIRSCIEDEPSFFELLKSPLITADEKKDIISNIFRDRVCMEVLNFLYIIIDKGREAYIKDIVNEYILLVDSVQNKVDAVAITAVPMEKQDLLMLQANLSKSSGKNIQLQNQVDPTIIGGVLVKIGDKVIDGTIKNRLATMQEQLSKILV | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During c... |
Q24MN8 | MLKGAIAQRYAQALFELAVQENLDGIEAELQELVQCVEQNAEVAHVLYHPHISLSEKKDLMNKIFAGELSVTVRNFLNLLIDRRRQNYLMEIARVFAHLADEARNIVEAKVASAIPLSETQEQRLHQELARMTGKNVRMVKEVRPELIGGVMIQIGDRVMDGTVAFKLQRIRQSLSHA | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During c... |
A8ZU98 | MKNYVIQRRYAKALLLIGKEDNNAEQYKEELNGFVSVLDMEKAFESAITNPLYPVEARRKVLDMVIEKLGVSVMMRSFLALLFEKRRIQHVRGINEVYQNLVDELKGIVRADVVSAGELSDDVVEKIRASLSKMTGKQVIVDIAQDPTLIGGIVTKVGDMVLDGSIKTQLSNMKESLKKGERV | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During c... |
Q6AQ13 | MKQTILARRYAKAVFSIGADSGKYGEYNDALQAVANLYMTNPDVVDALTNPLYPLELREKVMVGIVKSMDIDAVMSNFLNLLVEKKRAEILPEIAEEFQAMVDDAQNLSHGSVISAVELSEELQGKIQQTLEKLTGKKVELTTSVDPSIIGGIVAKVGDLVLDGSIKTQLAGLKESIKGRE | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During c... |
A4J9A2 | MLRGAVARRYAQALYEIAQEKNALEAMEQELKGVAEAIEGTRELQKVLYHPQVLPGEKKNLLKALFTDKVSDETLNFLGLVVDKRRENYIAGIAAEFSVLANEARGKVAAEVTTAIEIDEKQKQELVKVASRMAGKEVEPTFGVDPSLIGGVVVRIGSKVIDGSIKTRLATIKSRLMSKTS | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During c... |
Q72E01 | MTGNIVARRYARALFALGKKSGLSDLETFGNDLAALAGTLETAPELVRMFRNPVFTPDEKRNVIAKLLDKLKVCPTVRNFCLLLADRERLAFIQDIQAYYGILLDAEKGVIRGELVTAIELANAKRDKVKAQLEAQAGRKLELGFSVDKNILGGVVLKVGDRILDASLRAQLGILKDNIKRGE | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During c... |
A5EXJ8 | MSQTETIARPYAKAVFEQAVETESVANWIDFLEIASTFVSNEAVKEHLASASFMENFLVWFEQFLVESRGEALSEQERNFLNVLNQQGRMAIVPEIATQFKQLYYSAQNVCKATVYTALALDEKQKKELQATIERNVHREVVLDVREEPALIAGVRIEYDGMVIDQSARGRLERFARMLDESRN | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During c... |
A7ZTU7 | MSEFITVARPYAKAAFDFAVEHQSVERWQDMLAFAAEVTKNEQMAELLSGALAPETLAESFIAVCGEQLDENGQNLIRVMAENGRLNALPDVLEQFIHLRAVSEATAEVDVISAAALSEQQLAKISAAMEKRLSRKVKLNCKIDKSVMAGVIIRAGDMVIDGSVRGRLERLADVLQS | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During c... |
Q82XQ1 | MAEAITIARPYAEAVFKLARESGSLFSWSETLDAVNSIVRESQIRELISNPLISSVKLREIIFSVCGKKLNEDGKRLVSLLIDNQRLLVMPQIHELFEQLKAQHESILEAEVVSAFPLDSGQLEKLVSILEAKFQRKVKAEVSVDSELIGGVRIKIGDQVVDSSVHGKLEAMATALKS | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During c... |
Q3J6M8 | MAEKITIARPYANAVFELAQAQKNYDQWSRVLNVFADLARDSEMQILIDDPRYTSEQLIGLFVEIGGDTVTESAKNFIKILADNRRLSVLPEVAALFEQLRAEIEGTLEVEIISAKPLAEEQLNEIASALKRRLGREVTFSRKTDESLLGGVIIRAGDLVIDGSAIGKLNQLAASLLH | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During c... |
A6Q4C3 | MEELIAKRYAKALMESCSEKELQAIEDALVAIAALFRDWKVKEFIISPEVEKSAKEEILLAPFKDAGKKFVHLIKLLAEKDRLEIIPALANELKIQRALKERKFDGVVYSEFKLSDNELKKIAEALSKKVNGEVVLHQGKEPYDGIKVEVNTVGIEIEFSKSKIKKQLIENILKAI | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During c... |
Q5Z0Y4 | MYAASREASSRSREALRAALTGSDSVAATTGSELFAVVAVLDDQRSLRVALADVSVPGSARAELSERVFGGKVSVATQAVLTTAVAQNWSRTSDMVDTLVLLGQEALLESAANAGRLDAVEDELFRLGRIIADNADLEQALSDRAKPAAAKRELIARLLAGKAEPVTISLAEQVVGRNTTRIGAAFDELSDLAAARRDQIVAHVRAAIALTSQQRERLAASLQRIYGKPVTVHVQVDPSLLSGLVVRIGDDVIDGSAVGRLERLRRELA | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During c... |
A1SHI8 | MVQQLSSLRGSSAEALQVLGEQVDGDRYTLEEFAALADDLFRAAALLRSEPALRRAVTDVSTPAEAKSSLVHGLLDGKLGAPAVDLLAQAVGLRWVAARDLADAVEHLGVVAAVRSAGRRESVRLSDELFVVAQVVEENAELRIALSDPVRSTDDKRELLRGLLAQRALPATVALVEQALAGSFRSFHAAVSEYQKVAAATQGEGVALVRVARELTEAERTRLEQALSTQYGRPVHLNIEVDPSLLGGMRVEIGDDVIDGTVVSRLDDARRRLAG | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During c... |
Q8EM80 | MSNSVVAKRYADALFQLGREKNSLDQLVADFLEVRQIFTNDQKLNVFLKHPKIDNEKKKQFLADVFKGADPVVINTLKLLVDRHRTSTIPSIVDHLVALVNDTKGIADATVYSIRELNTDEKEQLQTSFAKRLGKRSVQITNVVDPKILGGMKIRVGNTIYDGTVSNKLNRISRSIVSANK | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During c... |
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