ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
P43188 | ALADPLKVMISGAPASGKGTQCELIKTKYQLAHISAGDLLRAEIAAGSENGKRAKEFMEKGQLVPDEIVVNMVKERLRQPDAQENGWLLDGYPRSYSQAMALETLEIRPDTFILLDVPDELLVERVVGRRLDPVTGKIYHLKYSPPENEEIASRLTQRFDDTEEKVKLRLETYYQNIESLLSTYENIIVKVQGDATVDAVFAKIDELLGSILEKKNEMVSST | Function: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism. The maize enzyme also works with CMP, albeit with 10% of the activity with AMP.
Catalytic Activity: AMP + ATP = 2 ADP
Sequence Mas... |
P49983 | MLSTLAKRFASGKKDRMVVFFGPPGVGKGTQAKLLEKEFNLYQISTGDALRAEIRGQTPLGKRVKGIIESGGLVDDDTIMDILQACMQKNTDNNGYIFDGIPRTIGQVEKLDALLAKMGTPLTHVLYLSVNIDELRERVCGRLFHPGSGRVYHKVTNPPKKPMTDDITGEPLIIRKDDTPEVFNQRMNQYFGTFQPCIDYYSKKGILQTFPVDGQPIDVVHKKLHAALQ | Function: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Catalytic Activity: AMP + ATP = 2 ADP
Sequence Mass (Da): 25550
Sequence Length: 229
Subcellular Location: Hydrogenosome
EC: 2.7.4... |
Q493A3 | MIRIIFLGPPGSGKGTQAHLIANKYNIPNISTGTMLRQALTRSTHKSYELHKNIMHTGDLVNDEFMVQLISTRINQNDCRNGFLLDGFPRTILQAKSMKQCKIFVNYIIEFFASDSVIIDRIAGRRIHVGSGRTYHIKFNPPRNYGLDDITGEILTTRKDDHEEAIRKRLSNYYQHTEPVLDYYREESKYKKMKYFSVDGNRDISKIYKELINIISS | Function: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Catalytic Activity: AMP + ATP = 2 ADP
Sequence Mass (Da): 25153
Sequence Length: 217
Domain: Consists of three domains, a large ce... |
O51378 | MGLVFLGPPGSGKGTISKIISNEFKYQHISTGDLFRENILNSTALGQEIKKIVERGELVPDLITIKIVEDKIKAIKKNKDFILDGFPRNICQAEALDKFLPNVKIINFLIDEELVIKRLSGRRICKSCNNIFNIYTLTTKKNGICDVCGGDLYQREDDKEECLKTRLKEYKLQTKPLIEFYSKCSRLNNVDASVKIDEIKKKIIKIMLKKN | Function: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Catalytic Activity: AMP + ATP = 2 ADP
Sequence Mass (Da): 24099
Sequence Length: 211
Domain: Consists of three domains, a large ce... |
C0R000 | MLNIIFIGAPGVGKGTQSALIEKDYSISHIATGDMLRENIANGTELGKTAKSYMDKGELVPDSLVIDMLKDRIKKDDCKNGFMLDGFPRTIEQAKELSNILESLNYKISAVIDIFASEEIIIDRLLKRGRADDNEETIKNRLKVFENQSKPVLDYYSDKAKIIKIESIGTPEEVYAKIKKELDVL | Function: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Catalytic Activity: AMP + ATP = 2 ADP
Sequence Mass (Da): 20757
Sequence Length: 185
Domain: Consists of three domains, a large ce... |
P49982 | MQSLIKYQPKSPLKYLSSYFGDRKKNLFKLVLLGAPGAGKGTQAKHLVSKYSLKHISPGNLLREEMNRNSPITAQIKDYVSKGQLVPDSIVIKLIENHIATIGDSNWLLDGFPRSESQAAALRASPDLFPTHIVELKVDQEAVVQRLGGRRFDPITGNTYHIIYDPPPPDIADRVVVRTDDREDVIRERFRVYAENKDLVDKVFNHSVVSINCEGQTIDEVSLQLDRVLSMPSTIHPSIIMPERNKKQ | Function: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Catalytic Activity: AMP + ATP = 2 ADP
Sequence Mass (Da): 27965
Sequence Length: 248
Subcellular Location: Cytoplasm
EC: 2.7.4.3
|
Q7NKT5 | MATRRLMLLGAPGAGKGTQAQLLMQELGLPQVSTGDILRAAVKEGTPLGLEAQSYMNRGALVPDAVVVGLIEDRLARPDAGGGWILDGFPRTPAQAEALDGLLAHLAQSLEAVVLIDVPEAQLIERLTGRRTCPLCKRIFHVRFNPPPAAPPFCTDHTDCPSELVQRPDDTLEVVSKRLNVYRESTEPLIRYYQEQQKLTSVDGDRSPEVVYSELRELLG | Function: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Catalytic Activity: AMP + ATP = 2 ADP
Sequence Mass (Da): 24031
Sequence Length: 220
Domain: Consists of three domains, a large ce... |
A9H3J9 | MNVIFLGPPGAGKGTQSKRLEARYGIAQISTGDMLRAEVAAESAIGKQARALMDAGQLVPDDVIVAMLESRIAQPDCAKGFILDGFPRTQGQAVALDSMLKRRGARIDVVLFLEVDEEALADRIAGRFTCATCGAGYNDLFKKPKVEGTCDVCGGHSFVRREDDRRETVAARLVAYRKQTAPILPYYEAEGLLRRIDGMADIDTVTAKVFEIMDAITKK | Function: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Catalytic Activity: AMP + ATP = 2 ADP
Sequence Mass (Da): 23799
Sequence Length: 219
Domain: Consists of three domains, a large ce... |
P38372 | MNLILMGLPGAGKGTQAEKIIEKYGIPHISTGDMFRAAMKNETELGLKAKSYMDAGELVPDEVTIGIVRDRLSQDDCQNGFLLDGFPRTVAQAEALEDILASLDKKLDYVINIDVPEQLLMDRLTGRRVSPTSGRTYHVIFNPPKVEGICDVDGSELIQRDDDKPETVKKRLEVNQKQAQPLIDFYSEKGYLQNINGDQDISRVFEDINELLKGLSS | Function: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Catalytic Activity: AMP + ATP = 2 ADP
Sequence Mass (Da): 24170
Sequence Length: 217
Domain: Consists of three domains, a large ce... |
B0R683 | MSHPNVLLLGAPGAGKGTQSRRLVDEFGVEHVTTGDALRANKTKDITHLDVEYDTPGAYMDAGELVPDAVVNEIVKTALDDADGYVLDGYPRNESQTEYLDSITDLDVVLYLDVDEDELVGRLTGRRVCEDCGATFHVSFNQPETEGVCDACGGSLYQREDDTEETARERITVYEENTAPVVEYFREQGVLAEVDGERTPDEVWTDVAAAVDERTA | Function: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Catalytic Activity: AMP + ATP = 2 ADP
Sequence Mass (Da): 23711
Sequence Length: 216
Domain: Consists of three domains, a large ce... |
A1B049 | MAINIILLGPPGAGKGTQARRLIDERGLVQLSTGDMLREARSSGTEMGKRVAEVMDRGELVTDEIVIGLIREKLGQGGKGFIFDGFPRTLAQADALQALMAEMDQRIDAVIEMRVDDAALVSRISGRFTCGNCGEVYHDVTKPTKEPGKCDVCGSTDLRRRADDNEESLKTRLMEYYKKTSPLIGYYYVKGNLNPVDGLAEIDEVAAQVAKVMDKIPA | Function: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Catalytic Activity: AMP + ATP = 2 ADP
Sequence Mass (Da): 23811
Sequence Length: 218
Domain: Consists of three domains, a large ce... |
A7HWT2 | MKLILLGPPGAGKGTQAKRLEEAHGLVQLSTGDMLRAAVAQGSEVGKVAEGIMARGELVPDDVVVGIIADRIEQPDAVNGYILDGFPRNVAQAEALDKMLAGKGTTLDAVVELGVDDSILLKRIETRAAETAGGPRADDNAEALAKRLKVYHEQTAPLIAYYKAKGKLRTVDGMKSMDEVTGQIETVLGISKRKGSWLSRLTGKK | Function: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Catalytic Activity: AMP + ATP = 2 ADP
Sequence Mass (Da): 21744
Sequence Length: 205
Domain: Consists of three domains, a large ce... |
Q6D7Z5 | MRIILLGAPGAGKGTQAQFIMGKYGIPQISTGDMLRAAVKAGTELGKQAKEIMDAGKLVTDELVIALVKERIAQDDCRNGFLLDGFPRTIPQADAMKDAGIDVDYVIEFAVPDELIIDRIIGRRVHAASGRVYHVKFNPPKVEDKDDVTGEDLSVRKDDQEDTVRKRLVEYHQQTAPLVSYYQKEADAGNTRYFKVEGTRKVEEVRAELETILG | Function: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Catalytic Activity: AMP + ATP = 2 ADP
Sequence Mass (Da): 23733
Sequence Length: 214
Domain: Consists of three domains, a large ce... |
Q4FLN8 | MNIILFGPPGAGKGTQAQSIVKKHNYFQLSTGNLLRDEVKSKTDLGVDIEKLISNGKFVSDEIVNTLLRQSLTNLKYRDRIIFDGYPRNVEQAINLEVLLNEFNQTIGHTIFLNVSRDIIEKRIMGRMTCEKCNMTLNEYFNKEQIELHPCGVEHLKKRKDDNLEIVISRYDTYMSSTKPVLEFYSKNSNFTEIDGAGEIDQITNKINEILKV | Function: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Catalytic Activity: AMP + ATP = 2 ADP
Sequence Mass (Da): 24450
Sequence Length: 213
Domain: Consists of three domains, a large ce... |
A9BFZ7 | MRLLFFGPPGAGKGTQAKKVAQEFQIVHISTGDILRDAVSKGTELGKMAKAIMDRGELVSDEIMNSLVKERLEELDSFILDGYPRTLDQAKFLDQATKELQKEIDAAVLIDVSEEEIVKRISNRRVCPNCGKVYNLITLQPKEDEKCDVCGTKLIQRDDDKEEVVRERYKVYKKNTEPVIEYYRKNNKIITIDGAQNVEDVTKELFNILRSFNKQ | Function: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Catalytic Activity: AMP + ATP = 2 ADP
Sequence Mass (Da): 24573
Sequence Length: 215
Domain: Consists of three domains, a large ce... |
B4R8N8 | MNLILFGPPAAGKGTQAKRLVEQRRMVQLSTGDMLRAAIASGSELGQRVSGIMERGELVSDAIVIELIEQRLPEAEAAGGAIFDGFPRTLAQAEALDAMLAGRGRRIDLVVRLKVDDAALMQRIAGRFAESGRADDNPESFKVRLDAYNRQTAPLLPYYEGQGKLVEVDGMGSIDQVAAAIDAALTGAAA | Function: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Catalytic Activity: AMP + ATP = 2 ADP
Sequence Mass (Da): 20180
Sequence Length: 190
Domain: Consists of three domains, a large ce... |
Q9X1I8 | MMAYLVFLGPPGAGKGTYAKRLQEITGIPHISTGDIFRDIVKKENDELGKKIKEIMERGELVPDELVNEVVKRRLSEKDCERGFILDGYPRTVAQAEFLDGFLKTQNKELTAAVLFEVPEEVVVQRLTARRICPKCGRIYNLISLPPKEDELCDDCKVKLVQREDDKEETVRHRYKVYLEKTQPVIDYYDKKGILKRVDGTIGIDNVIAEVLKIIGWSDK | Function: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Catalytic Activity: AMP + ATP = 2 ADP
Sequence Mass (Da): 25169
Sequence Length: 220
Domain: Consists of three domains, a large ce... |
Q59WU8 | MNIVLLIYCLAMVVAHDLQLFGDFKFELSDNWRNDCAKKALEPIINQCAEGIETISPFQQKSIAIQLSICEFENAEISYPSECRSQNLDTCILLLEKSPQYWTTFSGYYREIRNICHQVSLPFAKDQILQVYGNITEFYRTLMDEMTNSSKYTENMQNELKAKFDKLIGVIDLILADREKNREDLKSSFNMFKNNFEKSLNNALVVMKHSYEDANSNVKELESHLNYFINDMSQVYILINEKALEVKSQQDRIKEHNADILNQIEEIKKNLDNAYEEASEVQISNNQLVHDIQSSLDYSLFTVSNLNSHLQLSINDFIEK... | Function: Required for nuclear membrane fusion during karyogamy.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 56008
Sequence Length: 485
Subcellular Location: Endoplasmic reticulum membrane
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Q6FU40 | MSMSITQPIKDLLSSQFQSYNISEQVKLYDIFPLLKPSCIKEAITDVVEVCTGYGPESLDPSIRAKAAVKLSLCEFEAVGLSIIPQGCYSNSIEEMMDCMLEIEHSSHWWTTYSGNYQRLSDVCSTYREYYQEKAIIETFLNITDFMADFHNQFKSSVVSETQEFQSNMKDKFAGVYNQFTHFESLLSQMIQKHSGIINDSIVAIKNKLSTEFVDELQMLKNDRYILINQILESDTEIKKTIDSMLVELTEDMKNQISAKSEFLINHMNITRLNESTALHDIIEENLQERFKDIAIFLDKFMVEIQTETNKVLLEVNEKL... | Function: Required for nuclear membrane fusion during karyogamy.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 53659
Sequence Length: 469
Subcellular Location: Endoplasmic reticulum membrane
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Q6BNJ4 | MDCVNISWFLITLFAAIATSTMHDGENNNVGKMLQEPTYLQSEMIESIMSRHLESFSLTESDFEDIIFMKPRSKCVKDALKDIIPECMRLGVDSIEPGLQKKAAIQLSICEFENSKVTYPSSCYNMINDNDFDSCIFDIERAPQYWTTFSGYYREITKICYEESLPFEKEQIISLYSNITKLYSKMFQDLNDSYKDSTHIQQMMKNEFKELQRMMKVILDQNEKTSEEVKEKYEEFSEQYSSMLSTSLEISKKFSLGTENLVEDMANNIKYLDFELSRISIAIEDLDFETKLTDMKNSVLDDVRNLSDESISLLDSILTN... | Function: Required for nuclear membrane fusion during karyogamy.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 65792
Sequence Length: 574
Subcellular Location: Endoplasmic reticulum membrane
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Q6CIJ3 | MWFLVFSIWIASGQLLPHISNVIEKELDQLEITELSREYINNKFPITQSSCVKNALGEFLEICMRKGFEFVDADLRVITAVRLSVCEFESSGLTNYPSECHEKRLGGIDTISCVNALESSPQWWTTYSGNYQNLPHICMENSLPFEKEQILELFLNITDMYSEFQRNIENYWKSFSSDLEINGKENIDMIQNLFNSLVNDLIQNHKMKDEELITEFDKMKAEFDIRFFNFTESFDNLNDEVNEDLSLIKSHLIETFRQVDSEYMAQLQKNKNSTDKAFNELESMSTYILDHQKTSMELIDSFFSDLIDLTRDKNLVISDE... | Function: Required for nuclear membrane fusion during karyogamy.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 56279
Sequence Length: 487
Subcellular Location: Endoplasmic reticulum membrane
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A5E4Z8 | MVGASAISGVVIIANVVAAIAAAAGDGDGGIASTTDTILTLDGIKILNNALLQWKDDCNQRALAEVMPQCIHGVENITPSQQKHTAMELSICEFENNGLDYPLECHASVRNLNTNTCIQALEKSPQYWTTFSGNYRAVKDICHQISLPYEKDQIIEVYENMTLLYRSVMEDLKSSHHKYTVELEMKIQNKFNKLFSVVDDLMRSRAEENNKVNQTFNKFYENFQVSISNALVVMQNSYDGANTNFELMQRHVSYFATELQRILLLVQEQGEKLQVQQEQLVTGNVKLSIQQERLFDNMQLFGNELDKLHNAEVSRVSSVN... | Function: Required for nuclear membrane fusion during karyogamy.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 58786
Sequence Length: 523
Subcellular Location: Endoplasmic reticulum membrane
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A5DJU3 | MKKILRLVFILVYTNISTFVSAHELEDAASFTADELDRLLEDPPGCIQLAMRPIFEKCVLNGIHAVDPKDRRSSAIEMSVCEFESAGVEYPAECSTTDYDTCIWKLGLVPQYWTTFSGNYRDIGLFCEGVSRNNEKEQLVLLYSNITKVFAGFRHAFYESYSKSQEMKDEMEEGFSRWSADFDIAKDQHKEFYEFVAKQQEHIKIELMKNQKVIFDFHDEQEVRFNSYSNHIVDVIDSMAVDLDIILAKLADDGIIEDMENQKSKSLDIMKSYSEDAELTLSRIVSELERVGIIQKNDVSIVENLNSGLADTSNKVSKLN... | Function: Required for nuclear membrane fusion during karyogamy.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 56885
Sequence Length: 493
Subcellular Location: Endoplasmic reticulum membrane
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Q09684 | MKFHPTRPFGLYFEFFIIISFFFTSESTGDVESFMKYSNVAFSEGLAGFDSLAHVYQALLKKSTCYQEVAATLISKCSLLNTELTIDNRIHSAIQMTLCDFERSQILAPSECVRGSQSECVSKLESTSTWWLSFTSHFHDVNHLCRLANLEMQKELSIEVNMNVTLVQKQFLEMVILHLRNFESVTDKMNQRIDKFDGKFNSVIENSFKDINFRVNQEIMGLVELQNHQQEGMVQQKEILSTIKQLKSEIFDINSFFANFIEESAGYSNSLIEKLNEKFTSENAIALSAIGKYTSEFSAFMEKRIKNLITTTEDSLQQSV... | Function: Required for nuclear membrane fusion during karyogamy.
PTM: N-glycosylated.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 66973
Sequence Length: 577
Subcellular Location: Endoplasmic reticulum membrane
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Q6C994 | MSLSYSFNTTIFTENRDLVAALQPQTNCARTALTLIVSDCGKLSSFNEDQQLRVSLAVGLAVCEFKAAQVTYPDACNNIEDWMSTSACTQQLVSSPQWWTTYHGCYNSVKQICHMHEASRECDRALKTHSQIVDMQEKLHTKMDQYWELVETMSDHRDAVLDYWNDTFDFMSETLAHMKETSVSLNAVYRDNFAQAQEHFQMLSENLQEARVQMENLGWAAQDAVVSLSKSTLAEQSLVSERLKNDASSLHKLLVLAHQDTTESFETQLQQSLTILVESSDNVLLNHVQQVSSRLSALMSDLEESQKKNMDMQHQLQQKV... | Function: Required for nuclear membrane fusion during karyogamy.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 45815
Sequence Length: 407
Subcellular Location: Endoplasmic reticulum membrane
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Q04746 | MFEMRYVYLFAICIKFVSSSELGKINNLLQGRLIYTDNSVATNVLESKFPFLKSTCVKDALKLFLPQCIANGLESIDAETRVETAIKLSICEFQASGLGEIPENCMVDDLGSMMDCMFELESSSQWWTTYSGNYQRLSSICYENLLPFEKEQILKLFLNITELYDSFGDDVDTKLNHLMFQMEQDSQNFLDDLARMFRNYDNELRNATESNRIILENDLSFFRNKVNDVLYETSEQLEVQIIEKNSQLMNEVDTVHHIMSDLADELAKNDIKSKINDLKDDSLNNLQDLVEMSNDVKEYYSRNNKLVNTELENFSMGLKK... | Function: Required for nuclear membrane fusion during karyogamy.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 58440
Sequence Length: 504
Subcellular Location: Endoplasmic reticulum membrane
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Q004B5 | MADAAVIEKLEAGFKKLEAATDCKSLLKKYLTKEVFDKLKDKRTSLGATLLDVIQSGVENLDSGVGIYAPDAEAYTLFAPLFDPIIEDYHVGFKQTDKHPNKDFGDVNSFVNVDPEGKFVISTRVRCGRSLQGYPFNPCLTESQYKEMEAKVSSTLSSLEGELKGTYYPLTGMSKEVQQKLIDDHFLFKEGDRFLQAANACRYWPAGRGIYHNDNKTFLVWVNEEDHLRIISMQMGGDLGQVFRRLTSAVNEIEKRIPFSHHDRLGFLTFCPTNLGTTVRASVHIKLPKLAANREKLEEVAGKYNLQVRGTRGEHTEAEG... | Function: Catalyzes the reversible transfer of high energy ATP gamma-phosphate group to L-arginine . Has nucleoside diphosphate kinase-like activity toward dTDP. Binds and phosphorylates dTDP using ATP as a phosphate donor. Does not phosphorylate dADP, dCDP, dGDP, dTMP or thymidine .
Catalytic Activity: ATP + L-arginin... |
G1ESZ9 | MAEELFKTLQNAKECHSLLKKHLTKERFDKLKGLKTKFGGTLADCIRSGCKNPDSGVGIYASDPDAYTVFAEVLDAVIMDYHKIDKVHHPIPDFGDVNNLNIGDLDPSGNMIVSTRVRVGRSHDSFGFPPVLKKDDRIKMEQVSVEALKSLDGELAGSYFPLANMSADVQKQLTEDHFLFNDSDRFLKAASGYDDWPIGRGIYFSENKTFLCWVNEEDHLRLISMQKGGNLGEVYKRLVSAINKMEKKLNFAKKDNMGYLTFCPSNLGTTMRASVHIKIPKLSQRSDFKSICDKYNLQARGIHGEHTESVCGVYDISNKR... | Function: Catalyzes the reversible transfer of high energy ATP gamma-phosphate group to L-arginine.
Catalytic Activity: ATP + L-arginine = ADP + H(+) + N(omega)-phospho-L-arginine
Sequence Mass (Da): 39239
Sequence Length: 348
EC: 2.7.3.3
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O61367 | MVDQAVLDKLETGFSKLSSSDSKSLLKKYLSKDVFDQLKTKKTSFDSTLLDCIQSGIENLDSGVGIYAPDAEAYTLFADLFDPIIEDYHGGFKKTDKHPPKDFGDVDSLGNLDPANEFIVSTRVRCGRSLEGYPFNPCLTEAQYKEMEEKVSSTLSGLEGELKGTFYPLTGMSKETQQKLIDDHFLFKEGDRFLQAANACRFWPTGRGIYHNDDKTFLVWCNEEDHLRIISMQMGGDLGQVYRRLVHAVNEIEKRLLFSHNDRLGFLTFCPTNLGTTVRASVHIKLPKLAANRAKLEEIAGKFNLQVRGTRGEHTEAEGG... | Function: May play an important role in the energy releasing mechanism in the visual system. By acting as an energy shuttle and/or as an energy reservoir, ARGK can provide both spatial and temporal buffering in delivering energy in sensory cells.
Catalytic Activity: ATP + L-arginine = ADP + H(+) + N(omega)-phospho-L-ar... |
Q08415 | MTKRLQARRLDGIDQNLWVEFGKLTKEYDVVNLGQGFPDFSPPDFATQAFQQATSGNFMLNQYTRAFGYPPLTNVLASFFGKLLGQEMDPLTNVLVTVGAYGALFTRFQALVDEGDEVIIMEPAFDCYEPMTMMAGGCPVFVTLKPSPAPKGKLGASNDWQLDPAELASKFTPRTKILVLNTPNNPLGKVFSRMELELVANLCQQHDVVCISDEVYQWLVYDGHQHVSIASLPGMWDRTLTIGSAGKSFSATGWKVGWVMGPDNIMKHLRTVHQNSIFHCPTQAQAAVAQCFEREQQHFGQPSSYFLQLPQAMELNRDHM... | Function: Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA), an intermediate in the tryptophan catabolic pathway which is also a broad spectrum antagonist of the three ionotropic excitatory amino acid receptors among others . Metabolizes the cysteine conju... |
A0A0R4IXF6 | MADPAAQSSAQPRLQQAQSSGPTGSNSNPGAGSSDPARPGLSQQQWSSQKKAQVRSFPRAKKLEKLGVFSSCKANDACKCNGWKNPNPPTAARMELQQQAASLTETCRSCGHSLAEHVSHLENVSEEEINRLLGMVVDVENLFMSVHKEEDTDTKQVYFYLFKLLRKCILQMGKPVVEGSLGSPPFEKPNIEQGVLNFVQYKFSHLAPKERQTMYELSKMFLLCLNYWKLETPSQFRQRAQKEDAAAYKVDYTRWLCYCHVPQSNDSLPRYETCQVFGRSLLKSIFTVTRRQLLEKFRVEKDKLPPEKRTLILTHFPKFL... | Function: Protein lysine acyltransferase that can act as a acetyltransferase, glutaryltransferasesucc, succinyltransferase or malonyltransferase, depending on the context (By similarity). Acts as a histone lysine succinyltransferase: catalyzes succinylation of histone H3 on 'Lys-79' (H3K79succ), with a maximum frequenc... |
Q92830 | MAEPSQAPTPAPAAQPRPLQSPAPAPTPTPAPSPASAPIPTPTPAPAPAPAAAPAGSTGTGGPGVGSGGAGSGGDPARPGLSQQQRASQRKAQVRGLPRAKKLEKLGVFSACKANETCKCNGWKNPKPPTAPRMDLQQPAANLSELCRSCEHPLADHVSHLENVSEDEINRLLGMVVDVENLFMSVHKEEDTDTKQVYFYLFKLLRKCILQMTRPVVEGSLGSPPFEKPNIEQGVLNFVQYKFSHLAPRERQTMFELSKMFLLCLNYWKLETPAQFRQRSQAEDVATYKVNYTRWLCYCHVPQSCDSLPRYETTHVFGRS... | Function: Protein lysine acyltransferase that can act as a acetyltransferase, glutaryltransferase, succinyltransferase or malonyltransferase, depending on the context . Acts as a histone lysine succinyltransferase: catalyzes succinylation of histone H3 on 'Lys-79' (H3K79succ), with a maximum frequency around the transc... |
Q1LUC3 | MSESTGIPQGSPAVGAAGSAPAAPGVGGTECSGAAVGSARIAVKKAQLRSSPRPKKLEKLGVYSSCKAEGACKCNGWKSQNPPPTPPPPTPPRAEQPTAVSLMEPCRSCSHALGDHVTHLENVSEEEMNRLLGIVLDVEYLYTCVHKEEDPDTKQVYFSLFKLLRKCILQMGRPVVEALESPPFEKPSIEQGVNNFVQYKFSHLPSKERQTIVELAKMFLNQINYWQLETPSQKRQRAPDDDVAGYKVNYTRWLCYCNVPQFCDSLPRYEATQIFGRIFLRSVFTIMRKQLLEQARQEKDKLPPEKRTLILTHFPKFLSM... | Function: Functions as a histone acetyltransferase (HAT) to promote transcriptional activation (By similarity). Has significant histone acetyltransferase activity with core histones (H3 and H4), and also with nucleosome core particles (By similarity). Also acetylates non-histone proteins . Involved in heart and limb de... |
Q92831 | MSEAGGAGPGGCGAGAGAGAGPGALPPQPAALPPAPPQGSPCAAAAGGSGACGPATAVAAAGTAEGPGGGGSARIAVKKAQLRSAPRAKKLEKLGVYSACKAEESCKCNGWKNPNPSPTPPRADLQQIIVSLTESCRSCSHALAAHVSHLENVSEEEMNRLLGIVLDVEYLFTCVHKEEDADTKQVYFYLFKLLRKSILQRGKPVVEGSLEKKPPFEKPSIEQGVNNFVQYKFSHLPAKERQTIVELAKMFLNRINYWHLEAPSQRRLRSPNDDISGYKENYTRWLCYCNVPQFCDSLPRYETTQVFGRTLLRSVFTVMR... | Function: Functions as a histone acetyltransferase (HAT) to promote transcriptional activation . Has significant histone acetyltransferase activity with core histones (H3 and H4), and also with nucleosome core particles . Also acetylates non-histone proteins, such as ACLY, MAPRE1/EB1, PLK4, RRP9/U3-55K and TBX5 . Inhib... |
Q9JHD1 | MAEAGGAGSPALPPAPPHGSPRTLATAAGSSASCGPATAVAAAGTAEGPGGGGSARIAVKKAQLRSAPRAKKLEKLGVYSACKAEESCKCNGWKNPNPSPTPPRGDLQQIIVSLTESCRSCSHALAAHVSHLENVSEEEMDRLLGIVLDVEYLFTCVHKEEDADTKQVYFYLFKLLRKSILQRGKPVVEGSLEKKPPFEKPSIEQGVNNFVQYKFSHLPSKERQTTIELAKMFLNRINYWHLEAPSQRRLRSPNDDISGYKENYTRWLCYCNVPQFCDSLPRYETTKVFGRTLLRSVFTIMRRQLLEQARQEKDKLPLEK... | Function: Functions as a histone acetyltransferase (HAT) to promote transcriptional activation. Has significant histone acetyltransferase activity with core histones (H3 and H4), and also with nucleosome core particles. Also acetylates non-histone proteins, such as ACLY, MAPRE1/EB1, PLK4, RRP9/U3-55K and TBX5. Acts as ... |
Q5QNI1 | METISNIFHNDPLPPLGARANQSIKLRKFIISPYDSRYRTWETFLLVLVVYSAWICPFELAYLRNLSWKVSLVDNIIDSFFAIDIILTFFLAYLDQKSYLLVDDPKRIVARYFSSWFLFDVCSTIPYQLLGQIFKKHENGLAYRLLSMLRLWRLRRLSELFARLEKDIRLNYYWIRCTKLISVTLFAVHCSGCFNYLIADRYPNPARTWIGAAIPNYRSQNLWVRYVTAIYWSITTLTTTGYGDLHAENQREMLFSICYMLFNLGLTAYLIGNMTNLVVQGSCRTRNFRDTIHAASQFAARNQLPGHIKDEMLSHICLRY... | Function: Probable inward-rectifying potassium channel. Assuming opened or closed conformations in response to the voltage difference across the membrane, the channel is activated by hyperpolarization (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 69807
Sequence Length: 601
Domain: ... |
P92960 | MSTTTTEARSPLPLLLRRGRSSTALSASTAEARSPLSILQFRRRSSKDVRNITSVSSSLLPAFGTFIEDDNPSSKPFIVLHFDRRYRLWELFLVILVGYSAWASLFELAFEKAAEGALLTIDLVVDFFFAVDIILTFFVSYLDNTTYLNVTDHKLIAKRYLKSVAFVMDVASTLPIQFIYKTITGDVGRGQAFGFLNLLRLWRLRRVAELFKRLEKDAHFNYFVIRVIKLLCVTIFWIHLAGCILYWIAYHYPRPTDTWIGSQVEDFKERSVWLGYTYSMYWSIVTLTTVGYGDLHAVNSREKTFNMFYMLFNIGLTSYI... | Function: Probable modulatory (alpha) subunit of inward-rectifying potassium channels. Could mediate potassium uptake from the soil solution by plant roots in association with AKT1.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 75598
Sequence Length: 662
Domain: The segment S4 is probably the volta... |
Q6YP21 | MFLAQRSLCSLSGRAKFLKTISSSKILGFSTSAKMSLKFTNAKRIEGLDSNVWIEFTKLAADPSVVNLGQGFPDISPPTYVKEELSKIAAIDSLNQYTRGFGHPSLVKALSYLYEKLYQKQIDSNKEILVTVGAYGSLFNTIQALIDEGDEVILIVPFYDCYEPMVRMAGATPVFIPLRSKPVYGKRWSSSDWTLDPQELESKFNSKTKAIILNTPHNPLGKVYNREELQVIADLCIKYDTLCISDEVYEWLVYSGNKHLKIATFPGMWERTITIGSAGKTFSVTGWKLGWSIGPNHLIKHLQTVQQNTIYTCATPLQEA... | Function: Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA), an intermediate in the tryptophan catabolic pathway which is also a broad spectrum antagonist of the three ionotropic excitatory amino acid receptors among others. May catalyze the beta-eliminati... |
Q71RI9 | MLLAQRRLISLGCRSKPIKTIYSSSKVLGLCTSAKMALKFKNAKRIEGLDSNVWVEFTKLAADPSVVNLGQGFPDISPPSYVKEELSKAAFIDNMNQYTRGFGHPALVKALSCLYGKIYQRQIDPNEEILVAVGAYGSLFNSIQGLVDPGDEVIIMVPFYDCYEPMVRMAGAVPVFIPLRSKPTDGMKWTSSDWTFDPRELESKFSSKTKAIILNTPHNPLGKVYTRQELQVIADLCVKHDTLCISDEVYEWLVYTGHTHVKIATLPGMWERTITIGSAGKTFSVTGWKLGWSIGPAHLIKHLQTVQQNSFYTCATPLQA... | Function: Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA), an intermediate in the tryptophan catabolic pathway which is also a broad spectrum antagonist of the three ionotropic excitatory amino acid receptors among others . May catalyze the beta-eliminat... |
Q5JM04 | MPRSSRMNLWPHCFPCFDDGDRSGNRFSTVCNFPDDLLPSLGATAHQPPKLRKYLVSPYDPRYKVWETFLIILVVYSAWICPLEFAFLRYLPSAPFVVDDVVNGFFAVDIMLTFFVPFVDKKSYLLVNDPKKIAVRYLSSWFVFDVCSTVPFHSISLLFNEHGHDLGFKFLNVLRLWRLRRVSSMFARLEKDIRFNYAVIRCTKLISVTLFAIHCAGCINYLIADRYPDPRRTWIGAVMPNFREDGLWIRYVTAMYWSITTLTTTGYGDLHAENAREMLFGICYMLFNLWLTAYLIGNMTNLVVHSTSRTRDFRDVVQAA... | Function: Probable inward-rectifying potassium channel. Assuming opened or closed conformations in response to the voltage difference across the membrane, the channel is activated by hyperpolarization (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 58008
Sequence Length: 502
Domain: ... |
Q652U9 | MAARSELLRPAFGEASPSLGRFVINPHSCSYRWWHMFLIMLVLYSAWASPFELSMEKAASIALVVTDLVVDVFFAIDIALSFFVAYRDTSTGLLITDRRKITMRYLKRPCFALDVASTIPLQIIYQLVTGKRQGLWGLLNLLRLWRLRRVSKLFARVEKDIRFNYLWTRLIKLLCVTLFALHFAACIYLWMAFNYKIKELTWIGSQIHSFEDRSVWFCYTCAVYWSITTLATVGYGDLHATNIGEMLFSIAFMLFNMGLTSYIIGNITNLVVRETSNTFKMRDMVQRVSEFGRMNRLPEAMREQMLASVQLRFRTDEQLQ... | Function: Probable inward-rectifying potassium channel. Assuming opened or closed conformations in response to the voltage difference across the membrane, the channel is activated by hyperpolarization (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 67394
Sequence Length: 591
Domain: ... |
Q92993 | MAEVGEIIEGCRLPVLRRNQDNEDEWPLAEILSVKDISGRKLFYVHYIDFNKRLDEWVTHERLDLKKIQFPKKEAKTPTKNGLPGSRPGSPEREVPASAQASGKTLPIPVQITLRFNLPKEREAIPGGEPDQPLSSSSCLQPNHRSTKRKVEVVSPATPVPSETAPASVFPQNGAARRAVAAQPGRKRKSNCLGTDEDSQDSSDGIPSAPRMTGSLVSDRSHDDIVTRMKNIECIELGRHRLKPWYFSPYPQELTTLPVLYLCEFCLKYGRSLKCLQRHLTKCDLRHPPGNEIYRKGTISFFEIDGRKNKSYSQNLCLLA... | Function: Catalytic subunit of the NuA4 histone acetyltransferase complex, a multiprotein complex involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H2A and H4 . Histone acetylation alters nucleosome-DNA interactions and promotes interaction of the modified histone... |
Q9NYS0 | MGKGCKVVVCGLLSVGKTAILEQLLYGNHTIGMEDCETMEDVYMASVETDRGVKEQLHLYDTRGLQEGVELPKHYFSFADGFVLVYSVNNLESFQRVELLKKEIDKFKDKKEVAIVVLGNKIDLSEQRQVDAEVAQQWAKSEKVRLWEVTVTDRKTLIEPFTLLASKLSQPQSKSSFPLPGRKNKGNSNSEN | Function: Atypical Ras-like protein that acts as a potent regulator of NF-kappa-B activity by preventing the degradation of NF-kappa-B inhibitor beta (NFKBIB) by most signals, explaining why NFKBIB is more resistant to degradation. May act by blocking phosphorylation of NFKBIB and mediating cytoplasmic retention of p65... |
Q8CEC5 | MGKGCKVVICGLLSVGKTAILEQLLYGNHTIGMEDCETLEDVYMASVETDRGVKEQLHLYDTRGLQKGVELPKHYFSFADGFVLVYSVNNLESFQRVELLKKEIDKFKDKKEVAIVVLGNKLDLSEQRQVDADVAQQWARSEKVKLWEVTVTDRRTLIEPFTLLASKLSQPQSKSSFPLPGRKNKGNSNPEN | Function: Atypical Ras-like protein that acts as a potent regulator of NF-kappa-B activity by preventing the degradation of NF-kappa-B inhibitor beta (NFKBIB) by most signals, explaining why NFKBIB is more resistant to degradation. May act by blocking phosphorylation of NFKBIB and mediating cytoplasmic retention of p65... |
Q6DGL2 | MGKSCKVVVCGQGSVGKTAVLEQLLYANHVVGSETMETLEDIYIGSVETDRGTREQVRFYDTRGLRDGQEFPRHYFTFADGFVLVYSIDSRESFKRVEALKKEIDRCRDKKEVTIVVVGNKLDLQDQRRVDSSAAQQWARQEKVRLWEISVTDRRTLIEPFVHLASKMTQPQSKSTFPLSRNKNKTSGSLDS | Function: Atypical Ras-like protein that acts as a potent regulator of NF-kappa-B activity by preventing the degradation of NF-kappa-B inhibitor beta (NFKBIB) by most signals, explaining why NFKBIB is more resistant to degradation.
Sequence Mass (Da): 21913
Sequence Length: 192
Domain: In contrast to other members of t... |
Q9NYR9 | MGKSCKVVVCGQASVGKTSILEQLLYGNHVVGSEMIETQEDIYVGSIETDRGVREQVRFYDTRGLRDGAELPRHCFSCTDGYVLVYSTDSRESFQRVELLKKEIDKSKDKKEVTIVVLGNKCDLQEQRRVDPDVAQHWAKSEKVKLWEVSVADRRSLLEPFVYLASKMTQPQSKSAFPLSRKNKGSGSLDG | Function: Atypical Ras-like protein that acts as a potent regulator of NF-kappa-B activity by preventing the degradation of NF-kappa-B inhibitor beta (NFKBIB) by most signals, explaining why NFKBIB is more resistant to degradation. May act by blocking phosphorylation of NFKBIB and nuclear localization of p65/RELA NF-ka... |
Q32NS2 | MGKSCKVVICGQHGVGKTSILEQLLYGNHVVGSDMIETQEDIYIGSVETDRGVREQVRFYDTRGLKDGLELPKHCFCGTDGYVLVYSVDNKDSFKRVEALKKEIDRSKDKKEVTIVVLGNKSDMKDQRRVDHEAAQQWAKAEKILLRNGPTHGSANWNLHPDH | Function: Atypical Ras-like protein that acts as a potent regulator of NF-kappa-B activity by preventing the degradation of NF-kappa-B inhibitor beta (NFKBIB) by most signals, explaining why NFKBIB is more resistant to degradation.
Sequence Mass (Da): 18398
Sequence Length: 163
Domain: In contrast to other members of t... |
B0VHH0 | MEPLILTAAITGAETTRADQPNLPITPEEQAKEAKACFEAGARVIHLHIREDDGRPSQRLDRFQEAISAIREVVPEIIIQISTGGAVGESFDKRLAPLALKPEMATLNAGTLNFGDDIFINHPADIIRLAEAFKQYNVVPEVEVYESGMVDAVARLIKKGIITQNPLHIQFVLGVPGGMSGKPKNLMYMMEHLKEEIPTATWAVAGIGRWHIPTSLIAMVTGGHIRCGFEDNIFYHKGVIAESNAQLVARLARIAKEIGRPLATPEQAREILALNK | Function: Involved in the anaerobic fermentation of lysine. Catalyzes the reversible reaction between 3-keto-5-aminohexanoate (KAH) and acetyl-CoA to form 3-aminobutyryl-CoA and acetoacetate. The reaction involves the deprotonation of KAH, the nucleophilic addition onto acetyl-CoA and the intramolecular transfer of the... |
Q8RHX2 | MMEKLIITAAICGAEVTKEHNPAVPYTVEEIAREAESAYKAGASIIHLHVREDDGTPTQDKERFRKCIEAIREKCPDVIIQPSTGGAVGMTDLERLQPTELHPEMATLDCGTCNFGGDEIFVNTENTIKNFGKILIERGVKPEIEVFDKGMIDYAIRYQKQGFIQKPMHFDFVLGVQMSASARDLVFMSESIPEGSTWTVAGVGRHQFQMAALAIVMGGHVRVGFEDNVYIDKGILAKSNGELVERVVRLAKELGREIATPDEARQILSLKK | Function: Involved in the anaerobic fermentation of lysine. Catalyzes the reversible reaction between 3-keto-5-aminohexanoate (KAH) and acetyl-CoA to form 3-aminobutyryl-CoA and acetoacetate. The reaction involves the deprotonation of KAH, the nucleophilic addition onto acetyl-CoA and the intramolecular transfer of the... |
P47114 | MFNHDWKYSINSKTFADLNIELFRNHKFKTVLNYIIGVVGWNGLKLALFVSDIYTCIKLLAFNSWSNNIIKPYLPFKISKWLFSGCILASIVLLIWEAIAGMRIYKTGNISLTYVNNFSRNLNSVLNYSKFCVYNMIERKGFRQKMTFFTFFQLKDCIRLIFTDTPRQVINGLTLWSVLVTVNKNEDLGDLESFTGLINKIKNIGQTNHEEAVILSLMLFSFIIWALFVFKFLLAVICSIFVYYKIINDQEYSGLREYICVTVSENVDELVERQRKKENDDTIYKTGLLESQTFDDFKEVENKIETSFNDTSYASNNDSM... | Function: Low affinity potassium transporter that, with PRM6/KCH2, participates in high-affinity Ca(2+) influx system (HACS) activation during the response to mating pheromone . Directly promotes K(+) influx and HACS may electrochemically respond to this K(+) influx . KCH1 and KCH2 act at the apex of the calcium signal... |
P31069 | MSHWATFKQTATNLWVTLRHDILALAVFLNGLLIFKTIYGMSVNLLDIFHIKAFSELDLSLLANAPLFMLGVFLVLNSIGLLFRAKLAWAISIILLLIALIYTLHFYPWLKFSIGFCIFTLVFLLILRKDFSHSSAAAGTIFAFISFTTLLFYSTYGALYLSEGFNPRIESLMTAFYFSIETMSTVGYGDIVPVSESARLFTISVIISGITVFATSMTSIFGPLIRGGFNKLVKGNNHTMHRKDHFIVCGHSILAINTILQLNQRGQNVTVISNLPEDDIKQLEQRLGDNADVIPGDSNDSSVLKKAGIDRCRAILALSD... | Function: K(+)-specific ion channel. May play a role in the defense against osmotic shock.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 46063
Sequence Length: 417
Subcellular Location: Cell inner membrane
|
Q9JJ57 | MGAVMGTFSSLQTKQRRPSKDIAWWYYQYQRDKIEDELEMTMVCHRPEGLEQLEAQTNFTKRELQVLYRGFKNECPSGVVNEETFKQIYAQFFPHGDASTYAHYLFNAFDTTQTGSVKFEDFVTALSILLRGTVHEKLRWTFNLYDINKDGYINKEEMMDIVKAIYDMMGKYTYPVLKEDTPRQHVDVFFQKMDKNKDGIVTLDEFLESCQEDDNIMRSLQLFQNVM | Function: Regulatory subunit of Kv4/D (Shal)-type voltage-gated rapidly inactivating A-type potassium channels. Regulates channel density, inactivation kinetics and rate of recovery from inactivation in a calcium-dependent and isoform-specific manner. Modulates KCND2/Kv4.2 currents . In vitro, modulates KCND1/Kv4.1 cur... |
Q8R426 | MGAVMGTFSSLQTKQRRPSKDIAWWYYQYQRDKIEDDLEMTMVCHRPEGLEQLEAQTNFTKRELQVLYRGFKNECPSGVVNEETFKQIYAQFFPHGDASTYAHYLFNAFDTTQTGSVKFEDFVTALSILLRGTVHEKLRWTFNLYDINKDGYINKEEMMDIVKAIYDMMGKYTYPVLKEDTPRQHVDVFFQKMDKNKDGIVTLDEFLESCQEDDNIMRSLQLFQNVM | Function: Regulatory subunit of Kv4/D (Shal)-type voltage-gated rapidly inactivating A-type potassium channels . Regulates channel density, inactivation kinetics and rate of recovery from inactivation in a calcium-dependent and isoform-specific manner . Modulates KCND2/Kv4.2 currents . In vitro, modulates KCND1/Kv4.1 c... |
Q9NS61 | MRGQGRKESLSDSRDLDGSYDQLTGHPPGPTKKALKQRFLKLLPCCGPQALPSVSETLAAPASLRPHRPRLLDPDSVDDEFELSTVCHRPEGLEQLQEQTKFTRKELQVLYRGFKNECPSGIVNEENFKQIYSQFFPQGDSSTYATFLFNAFDTNHDGSVSFEDFVAGLSVILRGTVDDRLNWAFNLYDLNKDGCITKEEMLDIMKSIYDMMGKYTYPALREEAPREHVESFFQKMDRNKDGVVTIEEFIESCQKDENIMRSMQLFDNVI | Function: Regulatory subunit of Kv4/D (Shal)-type voltage-gated rapidly inactivating A-type potassium channels. Modulates channel density, inactivation kinetics and rate of recovery from inactivation in a calcium-dependent and isoform-specific manner. In vitro, modulates KCND2/Kv4.2 and KCND3/Kv4.3 currents. Involved i... |
Q9JM59 | MRGQGRKESLSESRDLDGSYDQLTGHPPGPSKKALKQRFLKLLPCCGPQALPSVSETLAAPASLRPHRPRPLDPDSVEDEFELSTVCHRPEGLEQLQEQTKFTRRELQVLYRGFKNECPSGIVNEENFKQIYSQFFPQGDSSNYATFLFNAFDTNHDGSVSFEDFVAGLSVILRGTIDDRLSWAFNLYDLNKDGCITKEEMLDIMKSIYDMMGKYTYPALREEAPREHVESFFQKMDRNKDGVVTIEEFIESCQQDENIMRSMQLFDNVI | Function: Regulatory subunit of Kv4/D (Shal)-type voltage-gated rapidly inactivating A-type potassium channels. Modulates channel density, inactivation kinetics and rate of recovery from inactivation in a calcium-dependent and isoform-specific manner . In vitro, modulates KCND2/Kv4.2 and KCND3/Kv4.3 currents. Involved ... |
Q6PIL6 | MNVRRVESISAQLEEASSTGGFLYAQNSTKRSIKERLMKLLPCSAAKTSSPAIQNSVEDELEMATVRHRPEALELLEAQSKFTKKELQILYRGFKNECPSGVVNEETFKEIYSQFFPQGDSTTYAHFLFNAFDTDHNGAVSFEDFIKGLSILLRGTVQEKLNWAFNLYDINKDGYITKEEMLDIMKAIYDMMGKCTYPVLKEDAPRQHVETFFQKMDKNKDGVVTIDEFIESCQKDENIMRSMQLFENVI | Function: Regulatory subunit of Kv4/D (Shal)-type voltage-gated rapidly inactivating A-type potassium channels. Modulates KCND2 channel density, inactivation kinetics and rate of recovery from inactivation in a calcium-dependent and isoform-specific manner . Modulates KCND3/Kv4.3 currents . Isoform 4 does not increase ... |
Q6PHZ8 | MNVRRVESISAQLEEASSTGGFLYAQNNTKRSIKERLMKLLPCSAAKTSSPAIQNSVEDELEMATVRHRPEALELLEAQSKFTKKELQILYRGFKNECPSGVVNEETFKEIYSQFFPQGDSTTYAHFLFNAFDTDHNGAVSFEDFIKGLSILLRGTVQEKLNWAFNLYDINKDGYITKEEMLDIMKAIYDMMGKCTYPVLKEDAPRQHVETFFQKMDKNKDGVVTIDEFIESCQKDENIMRSMQLFENVI | Function: Regulatory subunit of Kv4/D (Shal)-type voltage-gated rapidly inactivating A-type potassium channels, such as KCND2/Kv4.2 and KCND3/Kv4.3 . Modulates channel expression at the cell membrane, gating characteristics, inactivation kinetics and rate of recovery from inactivation in a calcium-dependent and isoform... |
Q8NCM2 | MPGGKRGLVAPQNTFLENIVRRSSESSFLLGNAQIVDWPVVYSNDGFCKLSGYHRADVMQKSSTCSFMYGELTDKKTIEKVRQTFDNYESNCFEVLLYKKNRTPVWFYMQIAPIRNEHEKVVLFLCTFKDITLFKQPIEDDSTKGWTKFARLTRALTNSRSVLQQLTPMNKTEVVHKHSRLAEVLQLGSDILPQYKQEAPKTPPHIILHYCAFKTTWDWVILILTFYTAIMVPYNVSFKTKQNNIAWLVLDSVVDVIFLVDIVLNFHTTFVGPGGEVISDPKLIRMNYLKTWFVIDLLSCLPYDIINAFENVDEGISSLF... | Function: Pore-forming (alpha) subunit of voltage-gated potassium channel. Elicits a non-inactivating outward rectifying current. Channel properties may be modulated by cAMP and subunit assembly.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 111877
Sequence Length: 988
Domain: The segment S4 is pro... |
O54853 | MPVRRGHVAPQNTYLDTIIRKFEGQSRKFLIANAQMENCAIIYCNDGFCELFGYSRVEVMQRPCTCDFLTGPNTPSSAVSRLAQALLGAEECKVDILYYRKDASSFRCLVDVVPVKNEDGAVIMFILNFEDLAQLLAKSSSRSLTQRLLSHSFLGSEGSHSRPSGQGPGPGRGKYRTVSQIPQFTLNFVEFNLEKHRSGSTTEIEIIAPHKVVERTQNVTEKVTQVLSLGADVLPEYKLQAPRIHRGTILHYSPFKAVWDWLILLLVIYTAVFTPYSAAFLLSDQDESQRGTCGYTCSPLTVVDLIVDIMFVVDIVINFR... | Function: Pore-forming (alpha) subunit of voltage-gated potassium channel. Elicits a slowly activating, rectifying current. Channel properties may be modulated by cAMP and subunit assembly.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 105706
Sequence Length: 950
Domain: The segment S4 is probably ... |
P48048 | MNASSRNVFDTLIRVLTESMFKHLRKWVVTRFFGHSRQRARLVSKDGRCNIEFGNVEAQSRFIFFVDIWTTVLDLKWRYKMTIFITAFLGSWFFFGLLWYAVAYIHKDLPEFHPSANHTPCVENINGLTSAFLFSLETQVTIGYGFRCVTEQCATAIFLLIFQSILGVIINSFMCGAILAKISRPKKRAKTITFSKNAVISKRGGKLCLLIRVANLRKSLLIGSHIYGKLLKTTVTPEGETIILDQININFVVDAGNENLFFISPLTIYHVIDHNSPFFHMAAETLLQQDFELVVFLDGTVESTSATCQVRTSYVPEEVL... | Function: In the kidney, probably plays a major role in potassium homeostasis. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external po... |
P63252 | MGSVRTNRYSIVSSEEDGMKLATMAVANGFGNGKSKVHTRQQCRSRFVKKDGHCNVQFINVGEKGQRYLADIFTTCVDIRWRWMLVIFCLAFVLSWLFFGCVFWLIALLHGDLDASKEGKACVSEVNSFTAAFLFSIETQTTIGYGFRCVTDECPIAVFMVVFQSIVGCIIDAFIIGAVMAKMAKPKKRNETLVFSHNAVIAMRDGKLCLMWRVGNLRKSHLVEAHVRAQLLKSRITSEGEYIPLDQIDINVGFDSGIDRIFLVSPITIVHEIDEDSPLYDLSKQDIDNADFEIVVILEGMVEATAMTTQCRSSYLANEI... | Function: Probably participates in establishing action potential waveform and excitability of neuronal and muscle tissues . Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it . Their voltage dependence is regulated by the concentrat... |
O15554 | MGGDLVLGLGALRRRKRLLEQEKSLAGWALVLAGTGIGLMVLHAEMLWFGGCSWALYLFLVKCTISISTFLLLCLIVAFHAKEVQLFMTDNGLRDWRVALTGRQAAQIVLELVVCGLHPAPVRGPPCVQDLGAPLTSPQPWPGFLGQGEALLSLAMLLRLYLVPRAVLLRSGVLLNASYRSIGALNQVRFRHWFVAKLYMNTHPGRLLLGLTLGLWLTTAWVLSVAERQAVNATGHLSDTLWLIPITFLTIGYGDVVPGTMWGKIVCLCTGVMGVCCTALLVAVVARKLEFNKAEKHVHNFMMDIQYTKEMKESAARVLQ... | Function: Forms a voltage-independent potassium channel that is activated by intracellular calcium . Activation is followed by membrane hyperpolarization which promotes calcium influx. Required for maximal calcium influx and proliferation during the reactivation of naive T-cells . Plays a role in the late stages of EGF... |
Q7KVW5 | MSIQKLNDTTNSGYVSSEETDSLLVSSSNPSKGGGRTALLRQVKSNSTNGPTTGASTSSSGSVSGGGGGSGSGGGSASGSAAGASKPTLMRQDRTSTYLTSPQQSQHARMGSEESMRGGASGAAGHDEDVEQGLVRSSIVPDIEVHEEDQEQHSQQLNATTMATMTNNQQQQQPTISIMNLSLKPGDSHSHSSSPGSHPNLGTSSYQNLASSIPPSVPSRCRACRNCSRRASTTPTTLIDRSASRDSVKSAFQQGNLSGSMAICISNSALPQQQQLQQQYHLQQQQQQHYQLQQHHLHQQQLQQSQQQVPPVLITSSPTN... | Function: Forms a voltage-independent potassium channel activated by intracellular calcium. Activation is followed by membrane hyperpolarization. Thought to regulate neuronal excitability by contributing to the slow component of synaptic afterhyperpolarization. The channel is blocked by apamin (By similarity).
Location... |
P51787 | MAAASSPPRAERKRWGWGRLPGARRGSAGLAKKCPFSLELAEGGPAGGALYAPIAPGAPGPAPPASPAAPAAPPVASDLGPRPPVSLDPRVSIYSTRRPVLARTHVQGRVYNFLERPTGWKCFVYHFAVFLIVLVCLIFSVLSTIEQYAALATGTLFWMEIVLVVFFGTEYVVRLWSAGCRSKYVGLWGRLRFARKPISIIDLIVVVASMVVLCVGSKGQVFATSAIRGIRFLQILRMLHVDRQGGTWRLLGSVVFIHRQELITTLYIGFLGLIFSSYFVYLAEKDAVNESGRVEFGSYADALWWGVVTVTTIGYGDKVP... | Function: Potassium channel that plays an important role in a number of tissues, including heart, inner ear, stomach and colon . Associates with KCNE beta subunits that modulates current kinetics . Induces a voltage-dependent current by rapidly activating and slowly deactivating potassium-selective outward current . Pr... |
P97414 | MDTASSPPSAERKRAGWSRLLGARRGSAVVKKCPFSLELAEGGPEGSTVYAPIAPTGAPGLAPPMSTPVSPAPAPADLGPRPRVSLDPRVSIYSARRPLLARTHIQGRVYNFLERPTGWKCFVYHFTVFLIVLVCLIFSVLSTIEQYAALATGTLFWMEIVLVVFFGTEYVVRLWSAGCRSKYVGIWGRLRFARKPISIIDLIVVVASMVVLCVGSKGQVFATSAIRGIRFLQILRMLHVDRQGGTWRLLGSVVFIHRQELITTLYIGFLGLIFSSYFVYLAEKDAVNESGRIEFGSYADALWWGVVTVTTIGYGDKVPQ... | Function: Potassium channel that plays an important role in a number of tissues, including heart, inner ear, stomach and colon (By similarity) . Associates with KCNE beta subunits that modulates current kinetics (By similarity) . Induces a voltage-dependent by rapidly activating and slowly deactivating potassium-select... |
Q9MYS6 | MAAASTPPRAERKRXSWSRLPGAQRESAGLAKKCPFSLELAESGPPSSALYAPVSPPSAPEPAPPASPASPAPPAADQGPQPPVSLDPRVSIYSVRRPLLARTHIQGRVYNFLERPTGWKCFAYHFTVFLIVLVCLIFSVLSTIEQYATLATGTLFWMEIVLVVFFGTEYVVRLWSAGCRSKYVGLWGRLRFARKPISIIDLIVVVASMVVLCVGSKGQVFATSAIRGIRFLQILRMLHVDRQGGTWRLLGSVVFIHRQELITTLYIGFLGLIFSSYFVYLAEKDAVNESGRVEFGSYADALWWGVVTVTTIGYGDKVPQ... | Function: Potassium channel that plays an important role in a number of tissues, including heart, inner ear, stomach and colon (By similarity). Associates with KCNE beta subunits that modulates current kinetics (By similarity). Induces a voltage-dependent by rapidly activating and slowly deactivating potassium-selectiv... |
O73925 | MSSEVKSRWSGSGSQKSGTARKPTMLEMAENAASRHYEPVPLPLQRSNSPDSSTDKNPESRAADSRAEVIINPDIPPKAIALPLSRYRGRNPFFSKVNIQGRTYNFLERPTGWKCFIYHFTVFLIVLVCLIFSVMSTIEQYHYFANRALVWMEIVLVVFFGTEYIVRLWSAGCRSKYVGFWGRLRFARKPISIIDLIVVVASVIVLCVGSNGQVFATSAIRGIRFLQILRMLHVDRQGGTWRLLGSVVFIHRQELITTLYIGFLGLIFSSYFVYLAEKDAVDDSGSQQFGSYADALWWGVVTVTTIGYGDKVPQTWIGRT... | Function: Potassium channel that plays an important role in a number of tissues, including heart, inner ear, stomach and colon (By similarity). Associates with KCNE beta subunits that modulates current kinetics (By similarity). Induces a voltage-dependent by rapidly activating and slowly deactivating potassium-selectiv... |
Q9Z351 | MVQKSRNGGVYPGTSGEKKLKVGFVGLDPGAPDSTRDGALLIAGSEAPKRGSVLSKPRTGGAGAGKPPKRNAFYRKLQNFLYNVLERPRGWAFIYHAYVFLLVFSCLVLSVFSTIKEYEKSSEGALYILEIVTIVVFGVEYFVRIWAAGCCCRYRGWRGRLKFARKPFCVIDIMVLIASIAVLAAGSQGNVFATSALRSLRFLQILRMIRMDRRGGTWKLLGSVVYAHSKELVTAWYIGFLCLILASFLVYLAEKGENDHFDTYADALWWGLITLTTIGYGDKYPQTWNGRLLAATFTLIGVSFFALPAGILGSGFALKV... | Function: Associates with KCNQ3 to form a potassium channel with essentially identical properties to the channel underlying the native M-current, a slowly activating and deactivating potassium conductance which plays a critical role in determining the subthreshold electrical excitability of neurons as well as the respo... |
Q8K3F6 | MGLKARRAAGAAGGGGGEGGGGGGGAANPAGGDSAVAGDEERKVGLAPGDVEQVTLALGAGADKDGTLLLEGGGREEGQRRTPQGIGLLAKTPLSRPVKRNNAKYRRIQTLIYDALERPRGWALLYHALVFLIVLGCLILAVLTTFKEYETVSGDWLLLLETFAIFIFGAEFALRIWAAGCCCRYKGWRGRLKFARKPLCMLDIFVLIASVPVVAVGNQGNVLATSLRSLRFLQILRMLRMDRRGGTWKLLGSAICAHSKELITAWYIGFLTLILSSFLVYLVEKDVPEMDAQGEEMKEEFETYADALWWGLITLATIGY... | Function: Associates with KCNQ2 or KCNQ5 to form a potassium channel with essentially identical properties to the channel underlying the native M-current, a slowly activating and deactivating potassium conductance which plays a critical role in determining the subthreshold electrical excitability of neurons as well as ... |
Q88M04 | MNSMAPVITIDGPSGSGKGTVAGLIARELGWKLLDSGALYRLLAFNASNHGVDLTNEELLTKLAAHLDVQFIAAEPGKLQQIILEGEDVSNVIRTETVGAGASMVASLPAVRDALLVRQREFREVPGLIADGRDMGTVVFPDAPLKVFLTASAEERARRRYLQLKGKGEDVSLSSLLDEIRARDERDTQRAVAPLKPAADAIQLDSTELSIEQVLQRIRSEIAQRDLI | Catalytic Activity: ATP + CMP = ADP + CDP
Sequence Mass (Da): 24691
Sequence Length: 228
Subcellular Location: Cytoplasm
EC: 2.7.4.25
|
Q885T2 | MKIKAPVITIDGPSGSGKGTVAGLLAKKLGWCLLDSGALYRLLAFAARNHGVDLTNEEALKLLAAHLDVQFETTAAGQGQRIILEGEDVTQAIRNEQIGSGASQVASLPAVRDALLMRQRAFQEEPGLVADGRDMGTVVFPDAPLKVFLTASAEERARRRYLQLKAKGDDVSLSSLLDEICARDERDTQRAVAPLKPAHDAIQLDSTELSIEQVLERILSEIALRDIAG | Catalytic Activity: ATP + CMP = ADP + CDP
Sequence Mass (Da): 24634
Sequence Length: 229
Subcellular Location: Cytoplasm
EC: 2.7.4.25
|
Q8ZTJ1 | MVVIAVSGQPGSGKTTIAREIARVLGLPLVSSGLLFREMAARMGMDFIEFHKYAETNPDIDKKVDSLAIERAKAGDVVLEGHLTAWIVRPYADVCIYLKASLETRARRVALRDGKSLQDALREVAEREELNRRRYLSIYGIDINDLSIFDLVLDTSHLSVNDAVRISLDYTCTSLSFKYSRKIC | Catalytic Activity: ATP + CMP = ADP + CDP
Sequence Mass (Da): 20611
Sequence Length: 184
Subcellular Location: Cytoplasm
EC: 2.7.4.25
|
A1RRJ5 | MVVIAISGQPGSGKTTVAREVARVLNLPLVSSGSLFRELAAKMGIDFIEFHKYAEKNPDIDKVVDSMAIERAKAGNVVLEGHLAAWIVRPYADICIYLKASSEIRARRISIRDKKSFEDALREVREREELNRRRYLSLYNIDINDLSVFDLVLDTSYLSINDAIRISLDYICTVLGFKYSRKFC | Catalytic Activity: ATP + CMP = ADP + CDP
Sequence Mass (Da): 20895
Sequence Length: 184
Subcellular Location: Cytoplasm
EC: 2.7.4.25
|
Q8Y0Y5 | MSDVAAFTAYPVIAIDGPTASGKGTVAHQIADLLGFHYLDSGSLYRLVAFVSIRENIDDHDVNSLVRIASELDVRFKADHIWLKGEDVSLALRHESVGNQASAIAVHGPVREALRARQRAFLEAPGLVADGRDMGTVIFPEAVLKVFLTASVQARAERRYKQLIAKGFSATVESLSRDLEARDLRDRTRSVAPLRPAEAARLLDSSDMSVDEVVAQVLDWYRQVQGVKAR | Catalytic Activity: ATP + CMP = ADP + CDP
Sequence Mass (Da): 25221
Sequence Length: 230
Subcellular Location: Cytoplasm
EC: 2.7.4.25
|
Q67NU0 | MTDGTRELVIAMDGPAGAGKSTVARIVANRLGYLYIDTGAMYRALALKALRLGIPETDAAALADLADATEVELQRAPDGGNRVLLDGEDVTAEIRSPAVSAVVSQVSAVPRLRQRLIEVQRSMARAGGVVMDGRDIGSYVLPHADRKFYITASLQERARRRVAQLRAEGHEADLAAVEAEIARRDEQDMNKGVHSLVQLPESIVIDTTGKRVDEVVEEILRHCRRT | Catalytic Activity: ATP + CMP = ADP + CDP
Sequence Mass (Da): 24562
Sequence Length: 226
Subcellular Location: Cytoplasm
EC: 2.7.4.25
|
A0LK48 | MNNATIIAIDGPAGAGKSTVSRLLAKELGYTYLDSGAMYRALAWALQREGVDLEAEAHVARALPELPLEFSTRGGSLLIHCGGKALEDELRNPEMAAYASRISQMRAVRTFLTEWQRKLAEAGKVVAEGRDTATVVFPHAGVKVFLTADPAARAGRRHAEYLAKGIRVDYAVLERQIRERDEADSTRCLAPLRPADGAVILDTSDLDISEVMSRLMDLIREKSRG | Catalytic Activity: ATP + CMP = ADP + CDP
Sequence Mass (Da): 24577
Sequence Length: 225
Subcellular Location: Cytoplasm
EC: 2.7.4.25
|
Q9HIT3 | MRITIAGKIGSGKSTVSSELSRITGYTVYSSGTFFRETARKMNMSIEDFNVYSESHPEADYYTDETQKAFMQANDNIIVEGRLAGWISYLNGINAFRIFLYATYYTRLVRFAGRENIDIDSARDLMEKREKSEKERYRKLYGIDVDDLSIYDIVVNTEFMKPPEIAVYIANRIDEMSRKDIFTPRILR | Catalytic Activity: ATP + CMP = ADP + CDP
Sequence Mass (Da): 21864
Sequence Length: 188
Subcellular Location: Cytoplasm
EC: 2.7.4.25
|
Q5JJE3 | MPKGCLVITVSGLAGSGTTTLCRNLAKHYGFKHIYAGLIFRQMAKEMGMTLEEFQKYVELHPEIDREIDRRQIEAAKECNVVIEGRLAGWMVKNADLKIWLDAPIMERAKRVAKREGISVEEAFVKIAEREKQNRKRYLNLYGIDIEDKSIYDLIINTAHWGPDGVFAIVKAAIDHLSPSGDAGEDEKEKEVG | Catalytic Activity: ATP + CMP = ADP + CDP
Sequence Mass (Da): 21790
Sequence Length: 193
Subcellular Location: Cytoplasm
EC: 2.7.4.25
|
Q9X1F6 | MGFQIAIDGPAASGKSTIAKLLAEKLGFDHLNTGATYRAVAVYLHEKGLSSSSAEEEIENVLKDLKIDYVNGRVYINGEDYTEKIQSPEAGVLASNFARLEVVRRHLVRIQREICDDKNIVVEGRDIGTVVLPNAHLKIFLTASLEARVERKLKEYQKRGLKVTKEEVERELISRDEQDSKRNVAPLKPAEDAVIIDTTSMSVEEVLDRILKLVRERMNT | Catalytic Activity: ATP + CMP = ADP + CDP
Sequence Mass (Da): 24702
Sequence Length: 220
Subcellular Location: Cytoplasm
EC: 2.7.4.25
|
B5YH69 | MKKVVAIDGPSGAGKSTVSKEIAKALGFQYLDTGALYRAVAYYFSIKFNYIDDFSLLTEQEIEEELKNIKIHYKNGRVFLSGEDVSDFIRDPKIGEITSQLSTQKVVRDFLMPLQRSFAEKVDIVAEGRDMTTVVFPDAWKKFYLDASPQVRAKRRFEQLIQSGKKISFEEALRDVIERDKRDCSRENAPLRLSKDAFYIDTSELTLQEVISIVLKKVAEDA | Catalytic Activity: ATP + CMP = ADP + CDP
Sequence Mass (Da): 25338
Sequence Length: 222
Subcellular Location: Cytoplasm
EC: 2.7.4.25
|
O83362 | MRIAVSGASGCGNTTVSALLAERLGLPLVNYTFRNIARELGISLSEVLERARTDNHFDKAVDARQLCLAMRSSCVVGSRLAIWLVKDAALKVYLLASLKERVKRVLQREGGDVQDVERFTSMRDAEDMSRYKKLYRIDNTNYSFADLVLNTEGCDQETVVSIIIEMLRARGIAW | Catalytic Activity: ATP + CMP = ADP + CDP
Sequence Mass (Da): 19505
Sequence Length: 174
Subcellular Location: Cytoplasm
EC: 2.7.4.25
|
B5ZBF2 | MKKYINVAIDGPSGSGKSTAAKGLANKLGFLYINTGLMYRAYAYFLNENNLDINTNETACIEAIKNARFIFNGDDVKIDDQDVSDILRSNDVAMLASVVAANAKIRNLATNEQRKIASENNVVMDGRDIGSIVLVDADLKFYLNTSIQTRAKRRLAQNKDIEKLDYESIYNDIKERDYRDMTRDIAPLKKAIDAIEIFNDNMNLDQCVAHLYEIYLNKIKKS | Catalytic Activity: ATP + CMP = ADP + CDP
Sequence Mass (Da): 25063
Sequence Length: 222
Subcellular Location: Cytoplasm
EC: 2.7.4.25
|
O86224 | MHQFQQDNQYFIFNFDRTFEQATEFFQAEFWQKQERVIGSAKGRGITYFLQTEDWFGVNCALRHYYRGGLWGKLNKDRYRFSALETTRSFAEFHLLQRLYEAGLPVPKPIAARIQKGKLGICYQADILTEKIENAQDLTALLQTQTLPKETWMQIGRLIRKLHDLQICHTDLNAHNILLQQTEQGQKCWLLDFDKCGEKSADFWKVQNLNRLKRSFEKEVGRMNIQFTEQNWADLTSAYHQ | Function: Catalyzes the ATP-dependent phosphorylation of the 3-deoxy-D-manno-octulosonic acid (Kdo) residue in Kdo-lipid IV(A) at the 4-OH position. To a lesser extent, can use GTP instead of ATP as substrate.
Catalytic Activity: an alpha-Kdo-(2->6)-lipid IVA + ATP = a 4-O-phospho-alpha-Kdo-(2->6)-lipid IVA + ADP + H(+... |
P58551 | MQIIQTKQQYICYNPELLTETPEMAFSSEFWQQQNKIIGSAQGRGTTWFVQGEKLAMALRHYRRGGLFGKLVADSYLFSGWDKTRSVAEFSLLNHLIAHQVNVPKPVAARAVRLGWFRYQADILVEKIANSRDLVGILGQETLSQQVWFDVGAMIKRMHDAGVCHTDLNCHNIILDDHKTVWIIDFDKCYRLEGANWQEKNLARLHRSFIKEQGKRGILFNEDNWQWLCKVIRVNGNKGQ | Function: Catalyzes the ATP-dependent phosphorylation of the 3-deoxy-D-manno-octulosonic acid (Kdo) residue in Kdo-lipid IV(A) at the 4-OH position.
Catalytic Activity: an alpha-Kdo-(2->6)-lipid IVA + ATP = a 4-O-phospho-alpha-Kdo-(2->6)-lipid IVA + ADP + H(+)
Location Topology: Peripheral membrane protein
Sequence Mas... |
Q9KVB9 | MIQTFNDAQQKVWFDDALLHEDPSQCCNPEFWQQNGKVLGSATGRGTTWFVQLQQTQGALRHYRRGGLFGKLVADSYWFTGWEKTRSYQEFMLLNHLRDAGVNVPRPIAARVQKHGLLYKADLLSEKVPNARDLVSILQESPISDELYRKIGREIRKMHDAQVNHTDLNIHNILIDDQEKVWIIDFDKCYVQIGDSWKQGNLKRLKRSFEKEVCKRGINWSLEAFAIISSYKHEE | Function: Catalyzes the ATP-dependent phosphorylation of the 3-deoxy-D-manno-octulosonic acid (Kdo) residue in Kdo-lipid IV(A) at the 4-OH position.
Catalytic Activity: an alpha-Kdo-(2->6)-lipid IVA + ATP = a 4-O-phospho-alpha-Kdo-(2->6)-lipid IVA + ADP + H(+)
Location Topology: Peripheral membrane protein
Sequence Mas... |
Q7NN41 | MAFEGVLQIVATLVLMVAIVPFFGTYMARVFQGESTWLDRVLGPIENLVYRLGGVRPELTMDWWSYARAVLASNAAMFVPVFAVLLLQGSLPLNPNGISGMSWDLALHTAISFLTNTNQQHYSGETGASHLAQMVCFQFLMFTSAATGLAVGIAFIRGLLGKPLGNFYVDLTRSVSRILMPISIAFAVVLLSQGVPQSLGGTTEAQLVDPYRTEQDGKREQVTAQKLVSGPFASMESIKELGENGGGSYGINSAHPYENPNPFTNLLEILLLLAVPTSLIYTFGVLANNKKQGWVLFGTIFVLFVGLVGVAALGEYWGNP... | Function: Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit binds the periplasmic potassium ions and delivers the ions to the membrane domain of KdpB through an intramembra... |
B0R9L9 | MASPPPIVEYAVFFTILAVLVFVAGEYLAWVYREQANSDHRPPGYLSWFERLDEIFTPIENGLYRLSGINPRREMTWKGYLKAVLVFNVCIWVLLFVVLMFQDALPMNFVGVGGESWDLAFHTASSFTSNTNQQHYSGETLSVFTHTFGIGIAMFLTPATGLALMPAFARAFTNKEDPRLGNFYENVVRGLVRFLLPISLLIAIILMAEGSVQTILGGQLTANTFTMGIQNIRIGPHAGIEAIKMFGTNGGGINAANAATAFENPTPLSNLVLTLAMPIGTFSAIYAWGAWVGNRSHGVAIVAAFFVIYMALTGVAVVGE... | Function: Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit binds the extracellular potassium ions and delivers the ions to the membrane domain of KdpB through an intramemb... |
B4U8E3 | MNIFLDIFSFILFFGILTIISPILGKYMADIYEGRVHPSLKPIRYVEKTIYKILGIDESKEMNWKEYLYALLSFNFLGFLVLFLTLLFQKYLPLNQYHIPNMSWDLAFNTAVSFVTNTNWQAYAGETQATYFSQITGLALQNFLSAASGIVVALVLIRAFARKNTIYLGNFYVDFTRTILYVLLPVAFFSALFLVSQGVIQNFSHYKTIELLEPYKDSKNIITTQTLPMGPVASQEAIKLLGTNGGGFFNANSAHPFENPTPLSNVFEAFLIILIPASLVFTFGYMIKDKRQGWFLYSVMLFVLMLFMGIQYYFEWFGNP... | Function: Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit binds the periplasmic potassium ions and delivers the ions to the membrane domain of KdpB through an intramembra... |
Q8F1M1 | MVTEWIQLLIFLFALLIFSPLFGLGLYKVYLYKTSGFEKFLYKICGIDPNRNMDWKEYALSLLVFNFFGFLLLFLILFFQNYLPLNPENFPGLVWDLAFNTAVSFATNTNWQAYSGESTLSFFSQMAGLTTQNFLSATTGLCVLLALSRGISVNYNVFALGNFWKDMIRGTLYVLLPLSFIFALFLVGFGVVQTFSESVSAITLEGNTQIIPLGPVASQVAIKQLGTNGGGYFGVNASHPFENPSPISNFLQMFSILILPGACVFLYGRITGSIRHAWAIFSVMFTILCVGILIVWTFESSWNPISGTLGFWEGKEIRFG... | Function: Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit binds the periplasmic potassium ions and delivers the ions to the membrane domain of KdpB through an intramembra... |
B3DWJ8 | MKIFSLLILSLKITFLLTLLLGGLYPLAVFIVGKIFFPYQSEGSLIKDATGNVIGSALIGQKFDSPWYFHSRPSASDYDGLSSGGSNLAPSSLALIDTLRERTLRYRKENALSPTTPVPSDAVCASASGLDPHISFENGLLQVPRVAHERKADPKSIEELLRKHTEAPTWGILGERVVNVLLLNLELDKRYPKKIGY | Function: Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit acts as a catalytic chaperone that increases the ATP-binding affinity of the ATP-hydrolyzing subunit KdpB by the... |
B8GER0 | MTLRASLRAAVVLFGGCLLVLGLLYPLAMTGIAGVVFPVQAHGSLMYDVNGSVSGSELIARPVTDPRYFQPRPSAVSYNASASGGSNLGPTNPVFLDQVNTSIASLRDAGVTGPIPAELVMASASGLDPDLSVEAALVQAPAVAAARNSSVDEIRALVIAHRVTDLMPFHPEYVNVNTLNQALDGR | Function: Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit acts as a catalytic chaperone that increases the ATP-binding affinity of the ATP-hydrolyzing subunit KdpB by the... |
P65212 | MRRQLLPALTMLLVFTVITGIVYPLAVTGVGQLFFGDQANGALLERDGQVIGSAHIGQQFTAAKYFHPRPSSAGDGYDAAASSGSNLGPTNEKLLAAVAERVTAYRKENNLPADTLVPVDAVTGSGSGLDPAISVVNAKLQAPRVAQARNISIRQVERLIEDHTDARGLGFLGERAVNVLRLNLALDRL | Function: Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit acts as a catalytic chaperone that increases the ATP-binding affinity of the ATP-hydrolyzing subunit KdpB by the... |
Q1DFX4 | MFSTFLTALRTCVVTMVLTGLLYPLAVTGLAQLLFPGEANGSWVKDGRGRVVGSALIGQGFTRAGYFHPRPSAAGAGYDGAASSGSNLGPTSLKLKERAAAELERLRRENPDAAGPVPAELVTTSASGLDPHLSPEAARWQAARVARARGVALERVLDVVDARVEGRTFGVLGEPRVNVLLLNLALDRRFGPLPDAAPGVGGRASPGQGAP | Function: Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit acts as a catalytic chaperone that increases the ATP-binding affinity of the ATP-hydrolyzing subunit KdpB by the... |
Q1QJ48 | MLKELRPAIVILVALTIITGLIYPLAMTGAAQVLFPYQAQGSLIEQGGKTIGSALIGQSFTADRYFHGRPSATTAPDPKDASKTVPAPYNAVNSMGSNLGPTSKALADRLRQDVATLKAQNPSAAVPVDLVTASGSGLDPDISPQAARFQVPRVAKARNLPEAEVETLIDSRTEGRDLGFLGEPRVNVLKLNLALDRMAASGQPR | Function: Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit acts as a catalytic chaperone that increases the ATP-binding affinity of the ATP-hydrolyzing subunit KdpB by the... |
C5BAD7 | MSFIAIIPSRYASTRLPGKPLADIAGKPMVVHVMAQAQASGAERVIVATDHPDVQHAVLQAGGEVCMTRADHNSGTERLAEVVELCGFADDDIIVNVQGDEPLIPPQIIRQVAENLARCDAGMATLAVPIHDAAEAFNPNAVKVVRDSQGYALYFSRAAIPWDRERFAVSQSQIGQTFLRHIGIYAYRAGFIRRYVNWAPSQLEQIEMLEQLRVLWYGEKIHVDVALQAPGTGVDTPEDLDCVRAILASQGQN | Function: Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria.
Catalytic Activity: 3-deoxy-alpha-D-manno-oct-2-ulosonate + CTP = CMP-3-deoxy-beta-D-manno-octulosonate + diphosphate
Sequence Mass (Da): 27669
Sequence Length: 253
Pathway: Nucleotide-suga... |
B2KD62 | MGDTIIVIPARYGSTRLKAKVLEQLDGKSIVEHVWRAAKAAGEGKVLIATESPVIVEHCAKFGAQAVLTSEACQSGTDRIYEAVKNGSEDYVLNLQGDEPFVKPQTIKGVIKLLKKDSKIDIATACYPTFNDDIYKNPNAVKAVLTKDMRALYFSRSAIPYKRELTEETKKAPYYIHCGIYGYKKTALERFVNLPPSNLEKLEKLEQLRALEDGMVIKSILIEAAGPAIDTAEDLNEARKYIRNN | Function: Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria.
Catalytic Activity: 3-deoxy-alpha-D-manno-oct-2-ulosonate + CTP = CMP-3-deoxy-beta-D-manno-octulosonate + diphosphate
Sequence Mass (Da): 27239
Sequence Length: 245
Pathway: Nucleotide-suga... |
A6GYA2 | MKIIAVIPARYASTRFPAKLMQDLGGKTVILRTYQAAVETNLFDDVFVVTDSELIYNEIITNAGKAIMSIKEHESGSDRIAEAIQNLEVDIVVNVQGDEPFINKEPLEEVIQVFRNDTHKKVDLASLMRNITHKNDIQNPNNVKVIVDQKGFALYFSRSVIPYPREENVGVRYMQHIGIYAFRKQALLDFYHLPMLSLEASEKLEQLRYLEYGKRIKMIETTHVGIGIDTLEDLEKARSML | Function: Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria.
Catalytic Activity: 3-deoxy-alpha-D-manno-oct-2-ulosonate + CTP = CMP-3-deoxy-beta-D-manno-octulosonate + diphosphate
Sequence Mass (Da): 27573
Sequence Length: 241
Pathway: Nucleotide-suga... |
B0U168 | MVNIHVVIPARLKSTRLPGKMLADIAGKPMIQRVYEQVAKSKFKSIIIATDSQEIKEVAENFGAKVILTRDDHESGTDRIAEAVTKLGFADEDIVVNVQGDEPLIPVENIEQAAQLLIEKPEAVVSTLCERITEAEDIYNPNNVKVVFDKNNYALYFSRASIPFERGFSENHQVSISEFFRHIGIYTYRVGFLKHYAELAISPIEKYEALEQLRVLYNGYKIAIEQSAKPTPAGVDTLQDLEKVRKLFDV | Function: Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria.
Catalytic Activity: 3-deoxy-alpha-D-manno-oct-2-ulosonate + CTP = CMP-3-deoxy-beta-D-manno-octulosonate + diphosphate
Sequence Mass (Da): 28199
Sequence Length: 250
Pathway: Nucleotide-suga... |
Q8RFA8 | MKFLGIIPARYSSTRLEGKPLKMIEGHTMIEWVYKRAKKSNLDSLIVATDDERIYNEVINFGGQAIMTSKNHTNGTSRIAEVCEKMTEYDTIINIQGDEPLIEYEMINSLIETFKENKDLKMATLKHKLLNKEEIKNPNNVKVVCDKNDYAIYFSRSVIPYPRKNGNISYFKHIGIYGYKRDFVIEYSKMLATPLEEIESLEQLRVLENGYKIKVLETTHSLIGVDTQENLEQVINYIKENNIKI | Function: Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria.
Catalytic Activity: 3-deoxy-alpha-D-manno-oct-2-ulosonate + CTP = CMP-3-deoxy-beta-D-manno-octulosonate + diphosphate
Sequence Mass (Da): 28426
Sequence Length: 245
Pathway: Nucleotide-suga... |
Q01T78 | MPRKILGVIPARFSSTRFPGKVLAQIANKTMLQHVYERAGLATYLTSTIIATDDERVYTAAKSFGARVRMTRADHLSGTDRVAEVASAENAEIIVNIQGDEPLIDPAAIDAAVLPLVHEPDVLMGTLKKRIEDPREIVDPNVVKVVTDHAGDAIYFSRCPIPFDRDRSADTPYFKHVGLYVYQRDFLLSYSTLPVGPLERSERLEQLRALENGYRIRVVETEYESLGVDTPEDLERVSRLFKASILQGMGNG | Function: Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria.
Catalytic Activity: 3-deoxy-alpha-D-manno-oct-2-ulosonate + CTP = CMP-3-deoxy-beta-D-manno-octulosonate + diphosphate
Sequence Mass (Da): 28087
Sequence Length: 252
Pathway: Nucleotide-suga... |
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