ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
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P23649 | MLLLFLNSVGFIVPVLLAVALLTLIERKMLGYMHVRKGPNNVGPYGLLQPIADGFKLLIKETLKPSNASPYLFYSSPALFLFLAILLWSIIPVGESTLNFNLSLVLILGLSSLSVYSLLGSGWSSNS | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed... |
P03887 | MFMINILMLIIPILLAVAFLTLVERKVLGYMQLRKGPNVVGPYGLLQPIADAIKLFIKEPLRPATSSASMFILAPIMALGLALTMWIPLPMPYPLINMNLGVLFMLAMSSLAVYSILWSGWASNSKYALIGALRAVAQTISYEVTLAIILLSVLLMSGSFTLSTLITTQEQMWLILPAWPLAMMWFISTLAETNRAPFDLTEGESELVSGFNVEYAAGPFALFFMAEYANIIMMNIFTAILFLGTSHNPHMPELYTINFTIKSLLLTMSFLWIRASYPRFRYDQLMHLLWKNFLPLTLALCMWHVSLPILTSGIPPQT | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor . Essential for the catalytic activity of complex I . Essential for the assembly of complex I (By simi... |
Q8HEC4 | MILVLIMVILMMIFIVQSIAFITLYERHLLGSSQNRLGPTKVTFMGLAQALLDGVKLLKKEQMTPLNSSEVSFLLVPGISFIVMYLEWFTLPYFFDFISFEYSVLFFLCLIGFSVYTTLVSGIVSKSKYGMIGAIRASSQSISYEIAFSLYVLCIIIHNNVFNFMCKFNLSLLIVYIPFLIMIIAELNRAPFDFSEGESELVSGYNVEFASVAFVLLFLSEYGSLIFFSVLSSAMFFSFSILASFSIFSILIFIRSSYPRYRYDLMMSLFWFKLLPVSLIMLCFYAVVFYY | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed... |
Q9B8D6 | MQYIELLIMFLSVLLAVAFLTVAERKTLGYMQRRVGPNAVGYYGILMAIADAAKLLLKEIVVPTHADKLILFVSPMISLISALLCWSVIPFAPGVTIYDSNYGFILTLAISSVGVFGTLLAGWSANSKYSLLGSIRSTAQLISYELVLTTIILLCILIGGTMNVSKYIEIQQAIWYGIPLLPLAIIFFIGCVAECARPPFDNVEAESELVSGHMTEYSSSIFVLFFLSEYASILFLSTLTAILFMGGGTGIILGLKANLFAFTYIWVRATLPRVRYDKLINLCWMIFLPILFGSAIAVPAYLYALDAIIILYRPGGL | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed... |
O99824 | MILNFIYYFILILMVLLSIAFFTLMERKFLGYCHIRKGPNKTGAMGLLQPISDALKLFSKEMNKMFYMNKFIQIISPLIMILMMMMMWMIFYFSNNALNLNMSIIFFLCISSLASYAILFSGWSSNSKYSLIGSYRGFAQVISYEVSMAMILISLAIIPQSYNFISFLKIQETFPLIFSFLPIFIIWIITVLAELNRVPFDLAEGESELVSGFNIEYGSWLFAIIFMSEYGDIMMISFLTYYLFLGLKNLILFFVLILMTMIIMIRGTYVRMRYDQLMMMAWKMILPQSIIFLFLSYFIFLNINNFICINFCN | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed... |
O47495 | MTPPSTGGEATPVLVLMVALGSILLVSASNWLSVYLAIELPTLSLFILVAQKRGSGFSAEAGLKYFVLGALASGLFLFGCALLCGLTGGTSIPCIDLVLNQGRGPALDPSGVITPIGSLLITGALLFKLSAAPFHMWAPDVYDGAPTTTTALLATVPKVGVFSILVSIGPVANVLLIATIFSMVVGALGALNQTKIKRLLAYSGIAHMGFVLWGIEIGTFESVQASLIYMILYVIMSVCAFAMVLALGGLKNLIVEFSGLSRKEPALAITLALTFLSIAGVPPLIGFFSKWWILLSGITYQYYLVSILAVICSVVAGVYY... | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed... |
Q00229 | MVVCGETMKLVSLGVMLIGTILSVSSEELVGVWLGLELNLYGFLVIMNPDGHYSPEPCVKYFVVQSTGSILMLVGFVSLMEQHVVSGLVMSTAXTVLKSGVFPLHSWVPSVIKNSSWLASGLMLTWQKVAPLVFLSMILPSKSLWVVIVSMAGIGAVGGLNQNSVRVMSAYSSFVHTSWMLLGLTWSSVVFVGYFAVYSLSVGLFFYGCSLMNKMSMGSQLSSAASGMGLLMLMGMPPFLGFLAKVLVFLMSGSPVIVACIMGSVISLKFYIDFFYSMVMKSLVDKNKVEVKAIWSLVICMNIMGGALILVSFI | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed... |
O21078 | MMTLILILGIFLGTMTTMFSSSWFFAWLGLEINMMAIIPMMLFPLSQRALESSMKYFISQAVASSTIILASSWNYFSSGQWTISFMSDNLAITLIILALLLKLGLAPLHFWLPEVLQGVNLHMGLIISTWQKLAPLTLLIQVSSNLNNMYILISISVMSVLAGGFGGLNQTQLRKLLAYSSISHMGWIVGVMAVSASLSWVTTVIYLIINFSIFTILIELNSTKISDLMLSWSKTSWSHTKCILVLLSLGGLPPFTGFFLKLSISNALISNSLILMTILLMAGSLISLFFYLRLSFMTALLLAPTNLQIKGTWKSPHYSN... | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed... |
Q8DJ02 | MVAIPRLRDTATVFVLSGYEYFLGFLIICSLVPVLALAASALLRPKSGRMIRLTTYESGMEPIGGAWIQFNVRYYMFALVFVIFDVETVFLYPWAVAFHQLGLLAFIEALIFIAILVVALVYAWRKRALEWS | Function: NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, a... |
Q85FH3 | MFEQGLILSAYLLCVGFFGLITSRNMVRALMSLELIFNAITLNFITLSNLFDNRETGEIFTLFVIAVAAAEAATGLAIALSIHRNRRSTRIDQSNLLKW | Function: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to prot... |
P26289 | MILEHVLVLSAYLFLIGLYGLITSRNMVRALMCLELILNAVNMNFVTFSDFFDNSQLKGEIFCIFVIAIAAAEAAIGLAIVSSIYRNRKSIRINQSTLLNK | Function: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to prot... |
A9RAH1 | MIAMFTTLLMFYVSQNNIISLLIAIEILLLTVTVKIIYLGGQFDDVQSTMFALFIITLAGAESAIGLSLLVSYYRLRGKVTNIL | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed... |
P0C5X9 | MNLIDLILIAIYVIGISGLIFNKNNIINILIISELNLGTLGMLFVLASVELNDILGELSGLYILTFTAAESAIGLAIVVILYSKTGIINIRNLNKLKG | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed... |
P18934 | MIMILYWSLPMILFILGLFCFVSNRKHLLSMLLSLEFIVLMLFFMLFIYLNMLNYESYFSMMFLTFSVCEGALGLSILVSMIRTHGNDYFQSFSIM | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed... |
P07708 | MIMILYWSLPMILFILGLFCFVSNRKHLLSMLLSLEFIVLMLFFMLFIYLNMLNYENYFSMMFLTFSVCEGALGLSILVSMIRTHGNDYFQSFSIM | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed... |
P18939 | MLKIILPTIMLLPTALLSPAKSMWTNTTMYSLLIASISLHWLTPSYYPTKTLTLWTGMDQISTPLLVLSCWFLPLMIMASQGHLQHEPHKRKRMFISTLIIIQPFIILAFSATELMLFYISFEATLIPTLILITRWGNQPERLSAGIYLLFYTLISSLPLLVSILYLHTNTGTLHLPIIKLTHPNLPASWTSLLSSLALLMAFMVKAPLYGLHLWLPKAHVEAPIAGSMLLAALLLKLGGYGIMRVTLLMEPVSNFLHYPFLTLALWGALMTSSICLRQTDLKSLIAYSSVSHMGLVIAASMIQTQWSFSGAMILMISHG... | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity and assembly of complex I.
Catalytic Activity: a ubiquinone + 5 ... |
P20113 | MFISVLLILFALCVTLIPEAHYHMVRVWSFVATIIPMWVVTWMWWNFDASGHGLQMLVILGRSHLAFGIDGVALSLMLLTTVLFPICMMLLRTVAGFMTFILLEVLVLSALCVLDLLGFYILFEASLILLFLLIGRAPYGSLEAAYKIVLYTMAGSLVLLPTLFMIYSECGTTNVLYMTCAYNHQTVLGWGLLAVLAVKIPLMPVHLWLPEAHVAAPTAGSVLLAGVLLKLGGIGFLRFMLPVVPEFCVSVFPLVSTLCLVSFLFSTLSTLRQIDLKKIVAYSSIAHMSMVTLAIFSQSEFSAYSSSFLMIAHGLISPAL... | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed... |
O21047 | MTIIAISIMNVVIGIAILGVILRKKIMPNQKFQRIFILGVQGILIVLSGIMLIGCEGTDIINRISPYINMVTVYSNNVNINIGYSIDGISAIFIFLTIILILSCNLISIRVIKEKTEQKFQIMLLLTEILIINFFAATDLVQLYIVYEATLIPMVIMIGVWGSRTEKKIAAFQILIYTLIGSIFMLMSIGILYSTLGTTDYIMIREYIDVLPENVRKLIFIGFFIGFAVKIPIAPLHLWLLRAHVEAPTAGSVLLAGILLKLGGYGYIRYNIGLFPDLCEYYFPIIGGICLISILYTGIATLTQLDVKRIVAYSSISHMN... | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed... |
P18931 | MLKIIFFLLFLIPFCFINNMYWMVQIMMFFISFIFLLMNNFMNYWSEISYFLGCDMLSYGLILLSLWICSLMLLASEMINKHNNYKNLFLLNIIILLLLLILTFSSMSLFMFYLFFESSLIPTLFLILGWGYQPERLQAGLYLLFYTLLVSLPMLIGIFYLMNKIGSMNFYLMNNFMFNYDLLYFCLLCAFLVKMPMFLVHLWLPKAHVEAPVSGSMILAGIMLKLGGYGMLRVISFLQLMNLKYSFVWISISLVGGVLVSLVCLRQTDLKALIAYSSVAHMGIVLSGLLTMTYWGLCGSYTLMIAHGLCSSGLFCLANV... | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed... |
Q85CT7 | MNIINLPELNYEVFFVFIELGLIFGSLGVVFLTNIVYSAFLLGLVFVCISFLYLLLDADFVATAQILIYVGAVNILIVFAVMLINKPQSLQFLPSWTVGDTITLILCTSLFFLLISMILSISWSNIFSIAQSNKIGEQVLKSSVQGIGSSLLIDFLLPFELLSIVLLVALIGAITIARREKKVKLQKNRTLQVTKDSFIL | Function: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to prot... |
Q95695 | MDLPGPIHDFLLVFLGSGLLVGGLGVVLLPNPIFSAFSLGFVLVCISLLYILSNSHFVAAAQLLIYVGAINVLIIFAVMFMNDSEYSTDFNLWTIGNGITSLVCTTILFLLMSTILDTSWYGVIWTTKLNQILEQDLISNSQQIGIHLSTDFFLPFELISIILLVALIGAISVARQ | Function: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to prot... |
Q8M9T8 | MLEQSAQITLFVLDFFIFVGALGVVFFNNIIYSALFLGLTFLSVALLYLLLGSEFLSVAQVIIYVGAINVLIVFAIMLVNKPEFDKKDMIWVPIDLKSFCVNFILFSTIVTMIVTTPWKLLVNNIDVKLNSLNFLSPIAKIGYQFLSTLVLPFELLSLLLLIALIGAVIIARRELIEDT | Function: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to prot... |
Q1ACE6 | MDFLNMSYQLIVAYLIQLGIYIGALAVIFFNNIVYAAISLALVLSLIALLYLFFDADFLAVTQILIYVGAINVLILFAIMLISLPKSSTFIFYFTKKSQISAFACISLFVLLVKIILQTPWSTQSSYILLNENNKLDQIGIYLLSNFLLPFELISLLLLIALIGAVSIARYQNTEETE | Function: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to prot... |
Q19V56 | MILAEGVQKFSLFFLEGAVLVGALGVVLLPNILYSAFLLGGVLMSIAGIYLLLNADFVAAAQVLIYVGAINVLILFAIMLVNKNDGRVAAGTSNSSGVTNNIIGLTCIGLAGFLIDMIVTTPWLPKGVAVATSLSAKADSTAAQTQLKGSISIIGLHIFSDFLLPFEVISLLLLVTLVGAIVIARRERLSDLEISKISLLNLPDPSNGKTPSLK | Function: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to prot... |
P10329 | MFFENSAILLCALLSIAVGYTKSPFMSLMYSVMLFINSSFVLMMLGFEFLALVNLLVYVGALAVLFLFVIMLLEIPATELRAYSRGWSTLGIFVFIINGVFQITPSMGPRGIITGLPGAESITNLGHALYLYFADLLILNSLVLTVALFGRFAIAPVRTTGR | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed... |
P48924 | MNIDIFLFYLFSIFALISSLMVIGLTNAVHSVLFLILVFCNVAGLLLLLGPEFFSFMLIIVYVGAIAVLFLFVVMMLNIKLKSTNISFSSLWPIGILTFVILLSQFFSSFYELDLVKFQGKELFFISWANENSNLTNIKVIGKVLYTHFNLLFLICGLILLVAMIGVIVLTMHQRVDVKKQQIALQLARTAPNVIKFIILRRKR | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed... |
P48925 | MIKLVLFYFFSGLSLVSASIVISVKNPVFSVVFLILVFFNVVGLLLLLGAEFLSLLFLIVYVGAIAVLFLFVVMILNLKFIELRSSFFYYAFFGSLIMAIFLFEIFIILNSDLTFASSYFLERKRIWVQELYSYTNLQILGNVLYTSYSYLFILSGFVLLVAILGAIILTLYQRSQIRRQDPNVQVVRNFDDTIRFFKFLK | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed... |
A9RAG2 | MNTISGMSSLTAIGMLTPVQSMTCLMILFVSTAMCLYSQGFVLMGMLYVTMYVGAMAMLFLFMLSLLKMEYTPQGTITPLMVTLLAMCLMPLDITYETYGMVTQMENVTDELVMVGNQLYTEYAMLLMLTGMMLMLSVMGAMSITK | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed... |
Q37314 | MSTLGLLIMLLGIIIMCTLVILRSVNPIYSILNLIVIYGCYASILLTVEMEFLACIYILVNVGAIAVLFLFIVMMININIVEIQETMKKYNIYMIVGIIGVVGLLGILITNYQIRIKEEVIADFSMFLINSEVVQLQATPSYLDFYSLFVETTDIRTMGSNVIYGSYSIWFIMACIILLIGMVGVIYITEDLIIEKRTLNERRRQDINSQVLREYKITIRNYRESK | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed... |
P18933 | MIQLMLYSLIITTSIIFLNMIHPLALGLTLLIQTIFVCLLTGLMTKSFWYSYILFLIFLGGMLVLFIYVTSLASNEMFNLSMKLTLFSSLILIFMLILSFIMDKTSSSLFLMNNDMQSIINMNSYFMENSLSLNKLYNFPTNFITILLMNYLLITLIVIVKITKLFKGPIRMMS | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed... |
A0A2A5JY22 | MRKSKVLTLGFQHVLAMYAGAVIVPLIVGSSLKLNAEQLAYLVSIDLLTCGIATLLQVWRNKFFGIGLPVMLGCTFTAVGPMIAIGSEYGMPAIYGSVLASGLFLALFAGFFGKLARFFPPIVTGSVVTIIGITLIPVAVQDMGGGQGSADFGSLSNLALSFGVLLFIILANRFFTGFIRAISILLGLIFGTIAGAFMGKVDIGPLLDASWFHGIHPFYFGFPTFHLPSILTMTLVAIVSVMESTGVFVALGKITEKELTADDLKRGYRSEGLASILGSIMNSFPYTTYSQNVGLIQISKVKSRDVVITAGFILVILGFM... | Function: Uptake of the purines adenine and guanine, and the pyrimidine uracil. Transport is probably proton-dependent.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 45792
Sequence Length: 434
Subcellular Location: Cell membrane
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P15771 | MVKLAKTPKNQMKQKKMAPPPKKVEESEEEESSDLEESSGEEVMVPPKKQQKAAVTPAKKAATPAKKAATPAKKAVTPAKKAVATPAKKAVAPSPKKAAVVGKGAKNGKNAKKEESEEEDEDDEDDEEDEDEEEESDEEEEPAVPVKPAAKKSAAAVPAKKPAVVPAKQESEEEEEEDDEEEDEEDDESEDEAMDTTPAPVKKPTPAKATPAKAKAESEDEEDEEDEDEDEEDEDDEEEDEEESEDEKPVKEAPGKRKKEMANKSAPEAKKKKTETPASAFSLFVKNLTPTKDYEELRTAIKEFFGKKNLQVSEVRIGSS... | Function: Nucleolin is the major nucleolar protein of growing eukaryotic cells. It is found associated with intranucleolar chromatin and pre-ribosomal particles. It induces chromatin decondensation by binding to histone H1. It is thought to play a role in pre-rRNA transcription and ribosome assembly.
PTM: Highly phosph... |
P19338 | MVKLAKAGKNQGDPKKMAPPPKEVEEDSEDEEMSEDEEDDSSGEEVVIPQKKGKKAAATSAKKVVVSPTKKVAVATPAKKAAVTPGKKAAATPAKKTVTPAKAVTTPGKKGATPGKALVATPGKKGAAIPAKGAKNGKNAKKEDSDEEEDDDSEEDEEDDEDEDEDEDEIEPAAMKAAAAAPASEDEDDEDDEDDEDDDDDEEDDSEEEAMETTPAKGKKAAKVVPVKAKNVAEDEDEEEDDEDEDDDDDEDDEDDDDEDDEEEEEEEEEEPVKEAPGKRKKEMAKQKAAPEAKKQKVEGTEPTTAFNLFVGNLNFNKSA... | Function: Nucleolin is the major nucleolar protein of growing eukaryotic cells. It is found associated with intranucleolar chromatin and pre-ribosomal particles. It induces chromatin decondensation by binding to histone H1. It is thought to play a role in pre-rRNA transcription and ribosome assembly. May play a role in... |
P09405 | MVKLAKAGKTHGEAKKMAPPPKEVEEDSEDEEMSEDEDDSSGEEEVVIPQKKGKKATTTPAKKVVVSQTKKAAVPTPAKKAAVTPGKKAVATPAKKNITPAKVIPTPGKKGAAQAKALVPTPGKKGAATPAKGAKNGKNAKKEDSDEDEDEEDEDDSDEDEDDEEEDEFEPPIVKGVKPAKAAPAAPASEDEEDDEDEDDEEDDDEEEEDDSEEEVMEITTAKGKKTPAKVVPMKAKSVAEEEDDEEEDEDDEDEDDEEEDDEDDDEEEEEEEPVKAAPGKRKKEMTKQKEAPEAKKQKVEGSEPTTPFNLFIGNLNPNK... | Function: Nucleolin is the major nucleolar protein of growing eukaryotic cells. It is found associated with intranucleolar chromatin and pre-ribosomal particles. It induces chromatin decondensation by binding to histone H1. It is thought to play a role in pre-rRNA transcription and ribosome assembly. May play a role in... |
P13383 | MVKLAKAGKTHGESKKMAPPPKEVEEDSEDEEMSEDEDDSSGEEEVVIPQKKGKKATTTPAKKVVVSQTKKAAVPTPAKKAAVTPGKKAAATPAKKAVTPAKVVPTPGKKGAAQAKALVPTPGKKGAVTPAKGAKNGKNAKKEDSDEDEDEEDEDDSDEDEDEEDEFEPPVVKGVKPAKAAPAAPASEDEDEEDDDDEDDDDDDEEEEEEDDSEEEVMEITPAKGKKTPAKVVPVKAKSVAEEEEDDEDDEDEEEDEDEEDEEDDEDEDEEEEEEPVKAAPGKRKKEMTKQKEAPEAKKQKIEGSEPTTPFNLFIGNLNP... | Function: Nucleolin is the major nucleolar protein of growing eukaryotic cells. It is found associated with intranucleolar chromatin and pre-ribosomal particles. It induces chromatin decondensation by binding to histone H1. It is thought to play a role in pre-rRNA transcription and ribosome assembly. May play a role in... |
P37994 | MLRNLVIFAVLGAGLTTLAAAGQDINNFTQAKAAAAKIHQDAPGTFYCGCKINWQGKKGTPDLASCGYQVRKDANRASRIEWEHVVPAWQFGHQRQCWQDGGRKNCTKDDVYRQIETDLHNLQPAIGEVNGDRGNFMYSQWNGGERQYGQCEMKIDFKSQLAEPPERARGAIARTYFYMRDRYNLNLSRQQTQLFDAWNKQYPATTWECTREKRIAAVQGNHNPYVQQACQP | Function: May protect the bacterium against the invasion of foreign DNA. It may have a random endonucleolytic activity. May be implicated as well in pathogenicity.
Sequence Mass (Da): 26456
Sequence Length: 232
Subcellular Location: Periplasm
EC: 3.1.21.-
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Q9HSL7 | MPRTLTDPTADRAAAFATDAAADGLTVSLIGSCVATLTGRSQRDLAAGVRTLLWKPDDTVVVHGASGRDPDAWASGGPVTVDAADGLTVACDGGHTAGALRVRFDAVHTATAFDAAGADATTVSGTEAALKDRVLDTPDLVEPGFQPLATERDTPAGPIDIYGRDADGTVTAVELKNVRAGPAAASQLQRYVAALRRTLHADATVRGILVAPAVTAKTRRLLADRGLTFSPVSPPGSRDR | Function: Cleaves both 3' and 5' ssDNA extremities of branched DNA structures.
Sequence Mass (Da): 24602
Sequence Length: 240
Subcellular Location: Cytoplasm
EC: 3.1.-.-
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Q9HNR1 | MTVERVSAPTPAAFVDAANAAFRNGAVLSVQARCEVEYNGRTSGYLGDGDRLLVAKPDGTFLVHQPTGHKPVNWMPGGGTVEARTSQGDAVLLARRSNPTERVETRLHEVYGVTRFDAEDGATYEESGTEAEMHEYIEANPDALEAGLRIVEHERETKYGFIDFYAVDGDGTPVVIEVKRIQATLNHFDQLKRYVDRYAETNDDVRGMLVAPSASERVTRALRDNGLEFVALAEFGLDAKGATEAKLTDF | Function: Cleaves both 3' and 5' ssDNA extremities of branched DNA structures.
Sequence Mass (Da): 27412
Sequence Length: 250
Subcellular Location: Cytoplasm
EC: 3.1.-.-
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Q9L9I5 | MDRIIEKLESGWWIVSHEQKLWLPYGELPHGLAANFDLVGQRALRIGEWQGEPVWLVLQHRRHDMGSVRQVIDQEAGLFQLAGRGVQLAEFYRSHKFCGYCGHPMHPSKTEWAMLCSHCRERYYPQIAPCIIVAIRREDSILLAQHVRHRNGVHTVLAGFVEVGETLEQAVAREVMEESGIKVKNLRYVTSQPWPFPQSLMTAFMAEYDSGEIVIDPKELLEANWYRYDDLPLLPPPGTVARRLIEDTVAMCRAEYD | Cofactor: Divalent metal cations. Mg(2+) or Mn(2+).
Function: mRNA decapping enzyme that specifically removes the nicotinamide adenine dinucleotide (NAD) cap from a subset of mRNAs by hydrolyzing the diphosphate linkage to produce nicotinamide mononucleotide (NMN) and 5' monophosphate mRNA. The NAD-cap is present at th... |
Q87KQ7 | MLRKGDVNRVANAYWCVVAGSEIWLVDGAVPFGSAEQFSLPEENARQIGDYLGSPVMWINFADLEQDLPLVSLRDCLHFPEPLFMLLSKAIQYGHMTQSLRFCPQCGGRNFLNNNQFAMQCGECRTLHYPRIFPCIIVAVRKENQILLAQHPRHRNGMYTVIAGFLEAGETLEDCVAREVHEETGIHVKNIRYFGSQPWAFPSSMMMAFLADYDSGELNPDYTELSDAQWFGVKEMPPVAPTGTIARALIEQTISDILSD | Cofactor: Divalent metal cations. Mg(2+) or Mn(2+).
Function: mRNA decapping enzyme that specifically removes the nicotinamide adenine dinucleotide (NAD) cap from a subset of mRNAs by hydrolyzing the diphosphate linkage to produce nicotinamide mononucleotide (NMN) and 5' monophosphate mRNA. The NAD-cap is present at th... |
P40010 | MRVRKRQSRRTSTKLKEGIKKKASAHRKKEKKMAKKDVTWRSRSKKDPGIPSNFPYKAKILEEIEAKKMKDLEERELAKQQRLEARKAAKEQGVDAMDEDMIEDDENGLAALVESAQQAAAEYEGTPSNDADVRDDELDVIDYNIDFYGEDVEGESELEKSRKAYDKIFKSVIDASDVILYVLDARDPESTRSRKVEEAVLQSQGKRLILILNKVDLIPPHVLEQWLNYLKSSFPTIPLRASSGAVNGTSFNRKLSQTTTASALLESLKTYSNNSNLKRSIVVGVIGYPNVGKSSVINALLARRGGQSKACPVGNEAGVT... | Function: GTPase required for 60S ribosomal subunit export to the cytoplasm.
Sequence Mass (Da): 57709
Sequence Length: 520
Domain: In contrast to other GTP-binding proteins, this family is characterized by a circular permutation of the GTPase motifs described by a G4-G1-G3 pattern.
Subcellular Location: Nucleus
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Q9C923 | MVKKEKKANVSGKPKHSLDANRADGKKKTTETRSKSTVNRLKMYKTRPKRNAGGKILSNEYQSKELPNSRIAPDRRWFGNTRVVNQKELEYFREELQTKMSSNYNVILKERKLPMSLLTDNKKQSRVHLLDMEPFQDAFGRKTKRKRPKLVASDYEALVKKAAESQDAFEEKNGAGPSGEGGEEEDGFRDLVRHTMFEKGQSKRIWGELYKVIDSSDVIVQVIDARDPQGTRCHHLEKTLKEHHKHKHMILLLNKCDLVPAWATKGWLRVLSKEYPTLAFHASVNKSFGKGSLLSVLRQFARLKSDKQAISVGFVGYPNV... | Function: GTPase involved in pre-60S ribosomal subunit maturation.
Sequence Mass (Da): 65038
Sequence Length: 576
Domain: In contrast to other GTP-binding proteins, this family is characterized by a circular permutation of the GTPase motifs described by a G4-G1-G3 pattern.
Subcellular Location: Nucleus
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P25710 | MAPQGDDTVFQPKDAIKSGVSGALFSGGAGLLMASLRTSMKKNNVGSMHVFTHGGGTIISFTLAGGIYRFAQQASANLREKEDGWNHAIGAFLGGSVMGLRSLRFPVILGFGAMAGSVVGAFAFSGGLTGWGRDPNVDEFERKEAMRLNRRRPVEETLAEVGEGRGIYPPGYQERRRQRLLEKYGVEVKPVSADPNVASA | Function: Transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 21349
Sequence Len... |
Q9XTY6 | MSASQGNVFTRGLSRISRRKKKTKSIQNSLVSEQQPSFDAAIVPMPIPNDKSSIFSKGMDRLRRSLRLPKKRRDRSHDRHLSPDVTGGSKTEQWQPDEGAVRTGTCCFNVKYLGSVEVYESRGMQVCEGALKSLKASRRKPVKAVLYVSGDGLRVVDQGNSRGLLVDQTIEKVSFCAPDRQTDKGFAYICRDGASRRWMCHGFLATKETGERLSHAVGCAFSICLEKKKRRDEETAQVNVQSAQESTSSTPPKDIFHPNWEDNTSEGTSTQNPSNSRSNLAYQSFRKHVSIEDRYLDPQSVIINEVPASNHMDEIRRISK... | Function: Involved in the tethering and targeting of pkc-3 to modulate the intracellular distribution of the kinase. The complex formed with pkc-3 complexes are likely to be involved in assembly, maintenance, and/or regulation of protein complexes that execute asymmetric and/or polarized cell functions.
Location Topolo... |
Q8A0F5 | MEITKKPKIKSIPYDEFIDNESLEKLVKELNTGGANVFLGVLDDLVNWGRSNSLWPLTFATSCCGIEFMALGAARYDMARFGFEVARASPRQADMIMVCGTITNKMAPVLKRLYDQMPDPKYVVAVGGCAVSGGPFKKSYHVLNGVDKILPVDVYIPGCPPRPEAFYYGMMQLQRKVKIEKFFGGTNRKEKKPEFMK | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every tw... |
A9II02 | MAIDGILKQGFITTSADKFLNWAKTGSMWPMTFGLACCAVEMMHAGAARYDLDQFGIIFRPSPRQSDLMIVAGTLCNKMAPALRKVYDQMPEPRWVVSMGSCANGGGYYHYSYSVVRGCDRIVPVDVYVPGCPPTAEALVYGLLQMQNKIRLTNTIAR | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), a... |
Q2RJU6 | MAVTRLKPADPQIPDNIILSTVDAMLNYCRAHSFWPVTFGLACCAIEMMAAGGARYDIARFGYEVFRPSPRQADLMIVAGTVTRKMAPLVRRLYEQMPAPKWVIAMGSCAISGGPFVDSYNVVPGVDTIVPVDVYVPGCAPRPEALINGLLALKKKVINPKVALVK | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every tw... |
A0RMD1 | MLEKFSSKFNVLKHSTTNGLLSVQINPNDIYEAVLFVRDNIGFEILADIVCVDNLYIDKEKRFSLYYIFRKISSENLCIYIDIDINQSVKSVESIYKSANWGERECFDQFGVKFENHPNLKRILNHKDFQGYPLRKDYPITKYQVLYESDDLVGEMKNEMQRAGLASEENDEFKTKYTFLNIGPSHPATHGTIRNFVALDGEKIISCVTEIGYLHRGFEKACENHSYAQIIPYTDRLNYCSAMLNNVGYAKAVEEALGLNLPDRGIFMRVILGELARIIDHEVCLGAMFVDMGGLTNYWYLYNPRERIYNFLSKLTGARF... | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ... |
Q3J1Q7 | MSLDQAIPEALQALRTRFGAAVRAEQATGEAFPVLWLDASVWEAAHRFLREEIAAPFPLLADLWAIDESLRQHRTGQPASRITLCSHLVSLVRNADLRLKLATDGRAPSIAGVYANADWYEREAHDMFGLDFGRETRRILMPPTWEGHPLLKTHYARATEKPPFVLTDRLFEAEERATITDPDLLGLPKLRDGEELMVLNFGPHHPSTHGVLRILLGLDGEEVVWAWPDIGYHHRGAEKMAERQTWHGFIPYCDRIDYLGGVISELPYLLAVERLCGIAVPPRAQMIRVMLCEFYRIMNHLLFYGTMAQDVGAMSPVFYM... | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ... |
Q2NA62 | MAVVHSAPKYASNDGVRGTLVKALGDYVAASHEKYGEIIITVERDAIEDVLRTLRDDHDYQQLMEIAGVDYPERPERFEVVYMLLSLTKNHRVMVKVSTDEKTPVPTVTTLWPNAGWLEREVFDLYGVLFDGNTDLRRILTDYGFEGHPFRKDFPLTGYTELRYSEEEQRVVYEPVELAQDLRTFDFLSPWEGMTPPLPGDEKADMPPIDDPMVTEGPEDTGAGARANAKAAEGTPADPPAMDDEEEDDA | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ... |
B0TWP6 | MSARLQDHFNNVEKILNGFSVECYVAYGEINISIKDQRDIHLVLKKLKKEYHFKQLTDITAVDYLTYGQSDWQVGKVVSQTGFSRGRQQGFKTADVNNRFEIIYQLLSMANNVRVRVKCKLKDAQIIMVDSVEDLWPSANWAEREVYDMFGIYFNNHPDLRRVLTDYGFVGHPLRKDFPQTGYVEMRYDENLGKVVYEPVEIDDRVNAPRVIRNQ | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ... |
Q74GA6 | MAENNRAVIKLKEKFAASILDVREFRGEVTVTVAREKVVDICRFLKESLQYNLCTDVTAVDYLGKQEPRFMVVYNLYSIPNKDRLRLKAGVPDADCSIDTVSCVWNSANWLEREVYDLMGVQFNNHPDLRRILMTDDWVGHPLRKDYPLQGPDREPYKGRLS | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ... |
A9B4Z6 | MIDRATLEQRVSAQFPTVRIGDESGDLCLTVERQQLPALAGWLRDEPDLAFTFLNQLCGVDYLGRDPRFEVVVHLTSFQNKMRVTLHIEVPEADPTIPTLARLFPTANFQERETYDMFGIIFTGHPGLERILMPEDWLGHPQRKDHPLGYEEVAFTHNEDWIYANKPFAKE | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ... |
B3ES55 | MGKHIQYQGGNFKNTAPTKYQPTDLKVEEVLINIGPQHPATHGILRLEVILDGEIVVDVVPHLGYLHRCFEKHAATLPYNQTIPFVDRLDYLAAMNSEHAFAMGVEHMLGLTGKLPRRVEYIRVLMAELNRLASHFMAIGTYGIDLGAFTSFLWLMRDREYILRLFEWASGARMLYNYIWIGGLYYDLPVGFEERCLEFITYLKPKLEEINQLLIDNTLFIKRTANVGVLPLATAINHGVSGPILRASGLRLDLRRIDGYSIYPELSFDIPIGEGLMGHVGDCWDRTWVKFQECKESIKITEQCLVRLTSDLKRTADFNP... | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrog... |
Q2GJY9 | MSDSSDGYAKPMTINFGPQHPAAHGVMRLILEMSGEVIERIDPHIGLLHRGTEKLIEYKTYLQALPYFDRLDYVSPMSQEHAYSLCVERLLGCEVPIRAKYLRVIFCELTRLLNHLLNVACQALDSGATTPLLWIFEEREKILSFYERASGARFHSAYIRPGGLAADVPDGLLDDIHEFTNYFPKLLDSVDDLLTENSIWKQRNVEIGKVTKQQALDWGFSGPMLRACGIPWDLRKSQPYEIYDILDFKVPVGSNGDCYDRYLVRMAEIRESLYILEQCLRDIPSGPVKTDDRKIAPPKREELKYSMEALIHHFKLFSEG... | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ... |
Q89KJ5 | MEFFESAFWTGFLWPLIIMVAESVLVLVVLLVAIAYILLADRKIWAAVQIRRGPNVVGPWGLLQSFADLLKFVLKEPIIPAGANKGVFLLAPLVSCVLALAAWAVIPTNLGWVISDINVGILFIFAISSLSIYGIIMAGWSSNSKYPFLAALRSAAQMVSYEVSIGFVIITVLLCAGTLNLSAVVEAQHVRGLASLIGLPQLTILNWYVWPLFPMFVVFYVSALAETNRPPFDLVEAESELVAGFMVEYGSTPYLLFMLGEYVAIVTMCAMATILFLGGWLPPVDLPPFNWVPGIIWFLLKVFFMFFLFAMAKAIVPRYR... | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ... |
C0Z769 | MMNTLLQQAPSWGTTLWFIIAAVLLLAVVLGFVTYAIYFERKVIGWMQLRIGPNRVGPLGLLQTVADVAKLLLKEDIRPQHADKALFTLAPILAYAPAFAVLAVMPFTDSIRFADLGIGLLYYIALSGITVLGVITAGWASNNKYSLIGGLRSAAQMISYEVPLVMSVVGIVLLTGSMNLKDIVEAQRDVWNIVPQFIGFAVFIIAAQAELNRTPFDLPEAESELVGGYHVEYSGFRFAMFMLAEYVYMFGMGALITILFFGGWLPIHPSLDFIPGIVWFILKFSVYVFLQFWIRATMPRLRVDQLMSFAWKVLLPVALF... | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ... |
P57258 | MIWLEENMIKITFCFFKVIFILLLIVFSSAMLSIVERRLLAVFQNRYGPNRVGWMGSLQLCADMIKILFKEDWIPPFSRKFIFVLSPVIAFTSLLCVIPIIPFTSHFVIIDLNIGILFFLMMASLSVYAILFAGWSSNNKYALLGAMRACVQTLSYEVFLGLSLMGVVAQSGSFKISDIVNSQKYIWNVFPQFFGFLTFLIAGLAVCHRHPFDQPESEQELADGYHIEYSGMKFGLFFIGEYISIITVSSLIVTLFFGGWLGPWIPSCIWFILKIIFFIFLFILIRAALPRPRYDQVLLFGWKFCLPLTLFNLFLTAFLI... | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ... |
Q87ZQ3 | MTWFTPDVIDAIIAVVKAIVVLLAVVVCGALLSFVERRLLGWWQDRYGPNRVGPFGMFQIAADMLKMFFKEDWTPPFADKVIFTLAPVVAMSALLIAFAVIPITPTWGVADLNIGLLFFFAMAGLSVYAVLFAGWSSNNKFALLGSLRASAQTVSYEVFMGLALMGIVVQVGSFNMRDIVEYQAQNLWFIIPQFFGFCTFFIAGVAVTHRHPFDQPEAEQELADGYHIEYAGMKWGMFFVGEYIGIILISALLVTLFFGGWHGPFDILPSLAFFWFALKTAFFIMLFILLRASIPRPRYDQVMDFSWKFCLPLTLINLLV... | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ... |
A0RMD6 | MAIKTKTIRRKKIPFLQRIYLPFIFAGMARTFRHFFRNLKDSSNIDFLEYPEQKPTDITNRYRGLHRLTKNEKGDLKCVACDMCATACPANCIFITATEIEGSKEKAPSKFTIDLLECVFCGLCVEACPKDAIRMDTGIFTKVGNTRESFLADIKTLSQREEGSF | Cofactor: Binds 2 [4Fe-4S] clusters per subunit.
Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (fo... |
A6H1Q3 | MNNILVEIGIENYIYLCVVLFCIGIFGVLYRRNAIIMFMSIEIMLNAVNLLFVAFSTFHQDAQGQVFVFFSMAVAAAEVAVGLAILVSIYRNLSSIDIDNLKNLKG | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrog... |
B0TWQ4 | MNSISVSVTNGLIFSTLLFVISVAGIIINRRNILILLMSIELMLLAVNTNFLIFANMHHQAMGGVFVFFIMAVAAAETAIGLAIVVAIFRKRKTIDLSKLNTLRG | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ... |
B9KIT6 | MCWRELLYMLPELYLLGSAMIALLLGIVVDARWVHRLSAVSMGVVVVLSWWSGVTDHVAEDVHLFNGLVLHTRYTCISRMLVGVAGFVASLLFLCARREVRYEFSVVMLFATLGAMTLVQAGHFLSLYISLELNSLSSCVLVCFNRSSERASESALKFFILSALSSCIMLYGISLVYGYSTGLECNVMQEILAGRASLGATLGCAFVLVGVLFKLAVVPFHMWAVDTYHGSPMAAMAFFLIVTKSAAILLLARIVGENGILQQSILYGIISVSGLSALVGELGALRQSNIKRLLAYSNIGQLGYVLPVVVLHGTSSYAIF... | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ... |
Q2GKQ9 | MYLSDFLYIVPEITVLGSALALLVLGMFTSERRVRSMSLISVAIAAVLACKELIYFSGEEVSLFGGFVVRTAHTCLARAVVAVSGLFAFLLFFFAKRSYRYEFAVLMLFAFLGTLTLVEAHHFLSFYLSFELIGFASYILVCFNRSSIKASEAAIKFFVLGALSSCIMLYGISLVYGYASEFSLGVVSKVLGGEESLGATFGCALVLVGLLFKLGAVPFHMWIPDTYEGAPTVAVVFFTIVTKTAMVLVFAGLMQGVVIPITGFVWSMLLMAALSMVVGEFSAMQQKNVKRLFAYANIGHIGYVLAGMSTGVVTFKPVLF... | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ... |
B6YQ48 | MDFSNFLCIEQELKLIALLVILFLYDTFCSKEWKKYFQNIAIVGFAIVIISEFPPYFTMYGEAFGGIHISSQLTFFMKSILNVATFLVFLQANKWLSSEKMLLRQGEFYVIMLISLLGMYFMISAENFVMLYIGMETASLPLACLVAFDKYQEKSAEAAVKYILTSALSSGVMLFGLSFLYGSLGSFYYSDIALNIVSSPLVKLGFVFFFGGLGFKLSLVPFHLWTADVYEGAPTSVTAYLSVVSKGAATFALIFVLYKVFGRIELIWNNILCWLLLATIVLGNLFAIRQQNIKRFFAFSSISQAGYILLGIIAGTAQGM... | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrog... |
A1K5C1 | MNFVVPDFYPATAEIFVAVMALVIMLATTFARSVARGLAYGLTLVTLIGAAIITYNTANPRAVTTFSNMFIGDLLGDVLKLLIYFSMAVALLYGRSYLADRKLDKPEYYVLALLMTLGMMVMVTSNHLLSMYIGLELMSLSLYALVAFDRDSARGTEAAMKYFVLGALASGLLLYGMSMLYGATGTLEISGIAKSVYNQAANDTVLLFGLVFLMAGICFKLGVVPFHMWIPDVYHGANTAVTLIIATAPKLAAFAMAVRLLVWGLFDVAEHWQTMLMFVAVLSIVLGNLAAIAQTNLKRMLAYSGISHMGFMLLGLLSGV... | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ... |
Q81K10 | MDMNTLLSLSWHLMVPEFIILGAAILLSICDLFFKLNHRYVALGAIAAVVLAIVSLITLYSEPAGDILNGSFVLDGFSKGFKTLLLGGAALILCTAMSDDKKNPIEDKGEYYYLFLMALLGAMFMASSVDFVTLFVGLELLSLSSYILVGIRKKNRASNEAAMKYVINGGIGTAITLFGMSYLYGITGSTNIVDMQKVFAGELASGIQLLLALAFLLLLVGLSFKIATVPFHMWAPDVYEGAATPVTAFLGTISKMAGFLLIIRLFLMVFASVSVQGDMQSLYGRMSIYIAVLASITMIIGNVVALKQYNVKRLFAYSGI... | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrog... |
Q64Y15 | MDYSQFLYMKEELSLIAVILILFVVDLLTCPDQKGATPKVNVRSLTLPAVILMTLHTVINLFPGTPAEAFGGMYQYTPMQTIIKAVLNVGTIIVLLMAHEWLKREDTRIKQGEFYVLTLSTLLGMYFMISAGHFLMFFIGLEMASIPMAALVAFDKYRHHSAEAGAKYILTALFSSALLLFGLSMIYGTSGTLYFNDLPGHITGNMLQIMAFVFFFAGMGFKISLVPFHLWTADVYEGAPTAVTSYLSVISKGSAAFVLMTILMKVFAPMVAQWQEVLFWVTIASITIANLFAIRQQNLKRFMAFSAISQAGYIMLGVIG... | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrog... |
Q1LTA1 | MKIITQILPLLIIGFTIILILLSIAWQRNHFMHASLTVVGLLLAIFSLFFVVHGSIANFTTLIHVDSFSIFYTGLVLIASLATSTLSYTWLSNNKDYKPDEFYILLLISTMGGILLTCAHHLTALFLGIELMSLPLLGMVGYTYRKKKVLEACIKYTIISSVASSFLLFGIALVYAVTGQLSFIGISNYALNEINYPLMLLAGLGMMIVGISFKLSLVPFHLWTPDIYQGAPTPVSTYLATVSKIAIFASLMRLFFYAPFNTHYEVKLLLCIIAICSMFIGNLMALSQNNLFRILGYSSTAHFGYLLVSWLVIQNVLVLE... | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ... |
Q6MGN8 | MNINIGLSDVLLISPMIALFLASLLPITMKVLRGNREQHALITLGQALMGIVAAVVLLVVFGGSDKTAFNNGLIFDGVTQWMGIIALAGAGAAMVMMYENPSTTGKQFSELIFLAMSSAVGMLILVSAVDLLMVFIGLEMMSLALYLMIAMSHEEKLSKEAALKYFILGSFASAIFLYGVAFIFGSTGGTNILSFMDNAAELVQTSRLFLFGVTFVILGFCFKVSIAPFHAWTPDVYQGAPTPHTAFMATAVKTVSFAAFLRIIATKSLTGSDQLFDILQWMAVITMIVGNAAAIMQNNFKRMIAYSSVAHSGYLMVGLI... | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ... |
B2IHV3 | MTPLPVVLAHALPELILAGGVLLLILIGAIRGKDSDGPMTELAVGLLGIAILTLVLGTKTQAVLFDGSFIDDAFGRFMKVLVLIGSLVSLIMGQTYLAREKIDKFEFPILILLSTLGMLMLISATGLIALYLGLELMSLALYVIAAFHRDDVKASEAGLKYFVLGALSSGMLLYGASLIYGFAGTVNFTGIATALHGETSLGVVFGLVFLTAGLAFKMSTVPFHMWTPDVYEGAPTPVTAFFASAPKLAAIAITMRIMITAFAGIKPQWQQIIVFISILSMALGSFAAIGQTNIKRLMAYSSIGHMGFALVGLAAGTETG... | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ... |
C5C0R4 | MNFVQPVIQWASLAPILIVLGAAVLGVLIEAFAPRRVRRPVQVTLALLAAAGAFGAIAWRWAEVIGGGGGAPSTVVVGQLVEDGPALAAQGIIAILAFVGILVIAERGRRGAPGSEDAFAPQGASVPGSDYEDRARRAGLVQTEVYPLVLFSVGGMLVFPAAGDLLTLFIALEVLSLPLYLLSGLARRRRLLSQEASMKYFLLGAFSSALLLFGIALLYGYSGSVAIGEIHAATQATTGMDGLLVVGLVLLISGLLFKVGAVPFHAWTPDVYQGAPTPITGFMAACTKVAAFGALLRVVYVVAPAMTWDIQPFLWVVAVL... | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrog... |
Q492I8 | MLITWTHIILLLPILIIGMTTVIVMLSIAYRRNLFLHTSLTIFGFSLAIISVGLVWDQRDRNFLQLICVDDFSILYIILVLVSGLSSSVLAYKWLLIYPSNNRDEFYLLLLISSIGGILLATTNHLVILFLGMELISLPLFGLIGYSFFNKFSLEASIKYIILSGVSSSFILFGIALIYAATGFLSFTSISQLLRLHIIASNQSIFMSTIGLGMMMVGFGFKLSLVPFHLWTPDVYQGAPSSISLYLTTSSKIAVISVLIRLLMVFPNQYNTVFCIFLLGIACCSALFGNLMAIKQDNIKRVLAYSSIAHTGYVLIGVIA... | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ... |
Q2KUY6 | MMQSHIDFALATPEILLLVLALAVLLIDAVSSHPDRKTTYVLSLATLAILTVVSLFQWSNGVSGKTFNGMYVTDSFSHLLKITSYIAVAVTLIYGRVYAQSRDMLRGGELYVLTLLALLGQMVMISAGSLVSVYLGLELMSLALYALIALRRDDVVATEAAMKYFVLGALASGFLLYGMSMVYGSTGHLDLAEISRVIGSGQAKELPLVFGIVFLVAGLAFKLGAVPFHMWVPDVYQGSPTAVTLILGGAPKLAAFAMTLRLLVDGLHGLAADWQSMLMILAVLSLAIGNLTAIVQTNFKRMLAYSTISHMGFVLLGLAS... | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ... |
C0Z763 | MEVKDIFSYDWSYLLPEFIILGFATFLSLLDLFAGKRLGKQVIGWLSFLGTVIAAIFVIINMNALNKPYSYMIDMIRIDDYGNAFKLIFLAGTAFAILISLSYLKAGEVQHRGEYYYLLLTGLLGAMVMASSADLITLFVGLELLSLSSYVLVGLRKKSRLSNESAFKYVVSGSIATAVLLFGMSYVYGLAGTTHIYEISFRLAEAGMAGYQFLVYTAFAFLAVGLAFKISAAPNHMWAPDVYQGAPTPVTVFLAVVSKAAGFALIFRVMMISFFNVSDGTGSGRFFFEEGSLYLGLMAAASMIIGNTMALRQTNVKRMM... | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrog... |
P57264 | MIINLQQLTALLPLLIIMLTVITVILSISYNRNHFFVAVFSILGLIFALCSLYFLIEIIPINVSILFHFNSNAILYIGMILISSICTCIFSYPWLLKYPFNKEEFYLLVIISTLGAISLTISHHMASFFINIELISLPMFGLIAYSRYQKYSLESSLKYIILSGVSSSFLLFGIAWVYSISGGLDFLSIHKSFNFASEKEILVVLFGISMILLSLFFKLSIVPFHLWTPDIYQGSPTSVLSFFSTAGKISVFSVLLNFLSYFSNSDNKVIYFILSLIIILSILVGNLMALFQKDIKRFLGYTSISQIGYLLIVLLVSHKN... | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ... |
Q89AT4 | MIITGQQLVALSPLLILMSIAIVVMLFIAYNRNRYIVFLLTSFGFLSVFISLFIVKKIVPIHATTLFHIDKYSLLYIGIVIISSFLACIFSHYCSLTNYLYNFEEFYLLLLFCTIGCVSIIISNNLCTFFIGSELISLSSIGLISYTFFEKKALEASIKYMVLSGIMSTLLLFGIALIYSVSGSLEFSSIIYELTMITKSFHNAIILFFGVSLFIIACSFKLSLFPFHIWTPDVYQGMSSEALMIFSTSVKIAIFSVLFKIFIVLSYFHIEEVFYYLVSIISCLSMIFGNIMAINQTSIKRLMGYSSISQLGYLFIVLVI... | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ... |
P24289 | WGALGHATVAYVAQHYVSPEAASWAQGILGSSSSSYLASIASWADEYRLTSAGKWSASLHFIDAEDNPPTNCNVDYERDCGSSGCSISAIANYTQRVSDSSLSSENHAEALRFLVHFIGDMTQPLHDEAYAVGGNKINVTFDGYHDNLHSDWDTYMPQKLIGGHALSDAESWAKTLVQNIESGNYTAQAIGWIKGDNISEPITTATRWASDANALVCTVVMPHGAAALQTGDLYPTYYDSVIDTIELQIAKGGYRLANWINEIHGSEIAK | Cofactor: Binds 3 divalent metal cations.
Function: Hydrolyzes only single-stranded DNA and RNA without apparent specificity for bases.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomononucleotide and 5'-phosphooligonucleotide end-products.
Sequence Mass (Da): 29227
Sequence Length: 270
Subcellular Location... |
P32499 | MAKRVADAQIQRETYDSNESDDDVTPSTKVASSAVMNRRKIAMPKRRMAFKPFGSAKSDETKQASSFSFLNRADGTGEAQVDNSPTTESNSRLKALNLQFKAKVDDLVLGKPLADLRPLFTRYELYIKNILEAPVKSIENPTQTKGNDAKPAKVEDVQKSSDSSSEDEVKVEGPKFTIDAKPPISDSVFSFGPKKENRKKDESDSENDIEIKGPEFKFSGTVSSDVFKLNPSTDKNEKKTETNAKPFSFSSATSTTEQTKSKNPLSLTEATKTNVDNNSKAEASFTFGTKHAADSQNNKPSFVFGQAAAKPSLEKSSFTF... | Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured ... |
Q8NFH5 | MAAFAVEPQGPALGSEPMMLGSPTSPKPGVNAQFLPGFLMGDLPAPVTPQPRSISGPSVGVMEMRSPLLAGGSPPQPVVPAHKDKSGAPPVRSIYDDISSPGLGSTPLTSRRQPNISVMQSPLVGVTSTPGTGQSMFSPASIGQPRKTTLSPAQLDPFYTQGDSLTSEDHLDDSWVTVFGFPQASASYILLQFAQYGNILKHVMSNTGNWMHIRYQSKLQARKALSKDGRIFGESIMIGVKPCIDKSVMESSDRCALSSPSLAFTPPIKTLGTPTQPGSTPRISTMRPLATAYKASTSDYQVISDRQTPKKDESLVSKAM... | Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. May play a role in the association of MA... |
O13838 | MSFGGSGSITNRSTLKPLSVDDLRSPSPQKEYRGFRTSVSNIPQEKKFVPSHLSHFGSSQQRRFAPEVSSPLAEPYESSSSFRLSLSSPPSSKFGGPSFGTPKPFLHTNRLGTGSLIEDAPPTQSIYDFSSSRQINALNVGQSSSPFSPVSEKVYDPSFTMSGAPQDSNTSVIVFGFPPELTNQVIAEFSRFGTIISENSLTASSAGFTPSKGPISGNWLQLTYAEPSSAAKAVLSNGMLINDSFMVGCIYSPAEAKEHVPKTLRNSNKDLEMTDASSSETSMSIPVHADAHFQSQSGLGKKVIVQHKNDIFKSSQKHQP... | Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured ... |
Q5ZI22 | MTICQFFLQGRCRFGDRCWNEHPRGGGGRPHSAGPVRGAGGGWGAASQRYANVIQPPIFKHSTWGGSGDGGGFSGASDFGSPGNKSAVFSQNRFSALSSAHPADGFSDEEQRLLDCVAKDMATWESSGQWMFSCYSPEAGKPNVSGFREFSAEEVRLEYYNCSANNNTENYINSVNQLVQERRNRLQELKALNASGKESLLSQLKNAVTQPLPSLGFGGQQASSFGFPSFPVSSSSGAASFSFKANPSVPPGNAAAVGSSAAASNPPTFGVTSSPSVPNPVGSGNSSAPSAASFSFKTSGTTSGCGTSGLSGFGSSAAAN... | Function: Required for the export of mRNAs containing poly(A) tails from the nucleus into the cytoplasm.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 42317
Sequence Length: 413
Domain: The FG repeats are interaction sites for karyopherins (importins, exportins) and form probably an affinity gradie... |
Q02854 | MSSTSSPTYTISKTLNTNYPLIDNDPHFRRVIGYARPSDYVHGTVAGAAGPGLLYLMEKMAPSGVGKGGFPKAMRLATAVGFFGGFLYFYQRSILRFYGMSENAREVQMDMREMVDKVKAGQPLYGVSTLPVDVQGMAARQSRYSALFFAVLPWFNFVNHNQHGVDTAKYYQQAERELEAERLGKGSSS | Function: Transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
PTM: The N-terminus is blocked.
Location Topology: Single-pass membrane protein
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
Seque... |
P19968 | MASKVVTGVVKTTAGGVVPVSQKYTVQSVGVWERIRRAFAIDPNRSNGVPLVPYNRNPSPGSLDPLAYDDPVTIPAGDIADNPYWKRDARRNYPRLSVVGQAEAVALLSVGSASHPRVELVGENGSKQLVAAQEAGKTGGLAKYFEGTGVEAGKLVLAETGGLPPLPSGEKLGEGGKWDVYKYQLAEEPSYSEAYPCRSFS | Function: Transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
Sequence Mass (Da): 21333
Sequence Length: 201
Subcellular Location: Mitochondrion in... |
F7J186 | MISRIPRLLFENILVPVADVLTKSVSNFAGHKSDQSYNSNATRVSTISDEEIEFYLNLKSAVLLLCLALCIAGFSVLMYFLYVLVFVPYNRVKRLGSIGYQNHEEGHLSKKDIANLVRRRRKVGDDLPPVFPNGWFRLVDSQQLEPGQVKQVTALGEHFAVFRSKSGKASILDAYCPHMGGNLAVGGIVKNDCLECPFHGWRFDGDGKCVAIPYSEKIPTFAKTKSWPCREVNKAIFVWFHCDGKEPEWEIPDISEISTGKFTYKGRVEHHANTHIQDVPENGSDLAHLSHLHVPHAMSGANLSTQYSSWWNFAEHIFKA... | Cofactor: Binds 1 [2Fe-2S] cluster per subunit.
Function: Catalyzes the production of 7-dehydrocholesterol (7-DHC or cholesta-5,7-dien-3beta-ol) by inserting a double bond (desaturating) at the C7-C8 single bond of cholesterol. Essential regulator of steroid biosynthesis as this reaction is the first step in the synthe... |
F7J187 | MLIEYLIRITVMVITSERLLILMGLCDESFHFPVMIRVVFNAAVAIVIALVMSKLYKVLFAPLDLRRKLEDVGYVHHDHSVSREENIRDTQRRKKLGNTPPVFPNGWFKVADSTWIKKGQVKSIYFFGEQLALFRNKRGLLRALDAYCPHLLANMAAGGKVVNSDCLECPFHGWKFSGETGKLVDVPYAQKVPTFVSVKKWSCCEVDGMAYLWYHCDGGEPKWVLPSSVTINTLKYAGKTEHIINSHIQDIPENAADISHLDHLHKPVIGSDVEKTNESLLNNLIFHSIQASWKPPTDPNEPHRSTMSIKDNIHLSIFNI... | Cofactor: Binds 1 [2Fe-2S] cluster per subunit.
Function: Catalyzes the production of 7-dehydrocholesterol (7-DHC or cholesta-5,7-dien-3beta-ol) by inserting a double bond (desaturating) at the C7-C8 single bond of cholesterol. Essential regulator of steroid biosynthesis as this reaction is the first step in the synthe... |
Q1JUZ2 | MADRQHFPSAITEAVSSNTACPDTGPKAETTNIFLLLQRNITIESSKHVFSSIVEYILILTLMFAFSAILYVIYKSYISPVFYKKELTEVGFDHIPQGPDKGRRISRAQASRRMGSKLPPPYPNGWFAVAETRELKVGSVLSIDALGQNLCVYRGEDGLARCVDAYCPHLGANLAVGGTVRGSCIECPFHKWRFNAAGTCVSLPGSDIAPKGVSIRTWCVVETDGAIWIWHDAEGREPLWEITDPPELKDFGYRGRNEFEVSAHIQEIPENGADVPHLNAVHSSSLLSDLGERYPVLHEIIGRHVWNADWTKSDDHTSLM... | Cofactor: Binds 1 [2Fe-2S] cluster per subunit.
Function: Catalyzes the production of 7-dehydrocholesterol (7-DHC or cholesta-5,7-dien-3beta-ol) by inserting a double bond (desaturating) at the C7-C8 single bond of cholesterol. Essential regulator of steroid biosynthesis as this reaction is the first step in the synthe... |
Q6DHJ3 | MENTRASLMFKTLAVAAIGLSATFVMLVRDPSDTLFGGGYPELWRRTGLAGAPTRAAACIFAGVFLLAMGWLYRLLFAPLELLRGVDEVGYIAEDGRSRAQAANEVRRRRKTGELPPVYPNGWYRVLDSHMLERGDVKSVTVLGQQVAVFRGQDGKAYVVDAYCPHLGANLAVGGRVVGGCIECPFHGWQFRGVDGRCVKIPYADKVPEFAKVRCWPSCEINGLVLVWFHCDGLEPSWRVPEQSQITRGEWVYRGRTEHFINAHIEEIPENAADIAHLAHLHTPGIVSGVDLRYTNSKTWEFIRHDWKVEWKPEPEPNKH... | Cofactor: Binds 1 [2Fe-2S] cluster per subunit.
Function: Catalyzes the production of 7-dehydrocholesterol (7-DHC or cholesta-5,7-dien-3beta-ol) by inserting a double bond (desaturating) at the C7-C8 single bond of cholesterol. This reaction is the first step in the synthesis of the steroid hormone Delta(7)-dafachronic... |
Q8VEY3 | MEIKNCSVVTEFILLGIPHTEGFETLLFVLFLPFYACTLVGNVSILVAVISSTRLHTPMYFFLGNLSVFDMGFSSVTCPKMLFYLMGLSRLISYQDCVSQLFFFHFLGSIECFLYTVMAYDRFAAICHPLRYSVIMNSKICVALAVGTWLLGCFHSSVLTSLTFTLPYCGPNEVDHFFCDIPAILPLASADTSLAQRVSFTNVGLVSLVCFLLILLSYTRITISILSIQSTEGRQRAFSTCSAHLIAILCAYGPIITIYLQPTPNPMLGTVVQILMNLVGPMLNPLIYTLRNKEVKIALKKILHGKGSVSEG | Function: Potential odorant receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34528
Sequence Length: 312
Subcellular Location: Cell membrane
|
Q8NGC3 | MGKTKNTSLDAVVTDFILLGLSHPPNLRSLLFLVFFIIYILTQLGNLLILLTMWADPKLCARPMYILLGVLSFLDMWLSSVTVPLLILDFTPSIKAIPFGGCVAQLYFFHFLGSTQCFLYTLMAYDRYLAICQPLRYPVLMNGRLCTVLVAGAWVAGSMHGSIQATLTFRLPYCGPNQVDYFICDIPAVLRLACADTTVNELVTFVDVGVVAASCFMLILLSYANIVNAILKIRTTDGRRRAFSTCGSHLIVVTVYYVPCIFIYLRAGSKDPLDGAAAVFYTVVTPLLNPLIYTLRNQEVKSALKRITAG | Function: Odorant receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34297
Sequence Length: 310
Subcellular Location: Cell membrane
|
Q8NGC4 | MERINSTLLTAFILTGIPYPLRLRTLFFVFFFLIYILTQLGNLLILITVWADPRLHARPMYIFLGVLSVIDMSISSIIVPRLMMNFTLGVKPIPFGGCVAQLYFYHFLGSTQCFLYTLMAYDRYLAICQPLRYPVLMTAKLSALLVAGAWMAGSIHGALQAILTFRLPYCGPNQVDYFFCDIPAVLRLACADTTVNELVTFVDIGVVVASCFSLILLSYIQIIQAILRIHTADGRRRAFSTCGAHVTVVTVYYVPCAFIYLRPETNSPLDGAAALVPTAITPFLNPLIYTLRNQEVKLALKRMLRSPRTPSEV | Function: Odorant receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35055
Sequence Length: 313
Subcellular Location: Cell membrane
|
Q8NGN3 | MSNASLVTAFILTGLPHAPGLDALLFGIFLVVYVLTVLGNLLILLVIRVDSHLHTPMYYFLTNLSFIDMWFSTVTVPKMLMTLVSPSGRAISFHSCVAQLYFFHFLGSTECFLYTVMSYDRYLAISYPLRYTSMMSGSRCALLATGTWLSGSLHSAVQTILTFHLPYCGPNQIQHYFCDAPPILKLACADTSANVMVIFVDIGIVASGCFVLIVLSYVSIVCSILRIRTSDGRRRAFQTCASHCIVVLCFFVPCVVIYLRPGSMDAMDGVVAIFYTVLTPLLNPVVYTLRNKEVKKAVLKLRDKVAHPQRK | Function: Odorant receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34569
Sequence Length: 311
Subcellular Location: Cell membrane
|
Q8NH81 | MLEGVEHLLLLLLLTDVNSKELQSGNQTSVSHFILVGLHHPPQLGAPLFLAFLVIYLLTVSGNGLIILTVLVDIRLHRPMCLFLCHLSFLDMTISCAIVPKMLAGFLLGSRIISFGGCVIQLFSFHFLGCTECFLYTLMAYDRFLAICKPLHYATIMTHRVCNSLALGTWLGGTIHSLFQTSFVFRLPFCGPNRVDYIFCDIPAMLRLACADTAINELVTFADIGFLALTCFMLILTSYGYIVAAILRIPSADGRRNAFSTCAAHLTVVIVYYVPCTFIYLRPCSQEPLDGVVAVFYTVITPLLNSIIYTLCNKEMKAAL... | Function: Odorant receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 36823
Sequence Length: 332
Subcellular Location: Cell membrane
|
O60404 | MPGQNYRTISEFILSGFSAFPQQLLPVLFLLYLLMFLFTLLGNLLIMATVWIERRLHTPMYLFLCALSISEILFTVAITPRMLADLLFTHRSITFVACAIQMFFSFMFGFTHSFLLMVMGYDHYVTICHPLHYNMLMSPRGCAHLVAWTWAGGSVMGMMVTMMVFHLTFCGSNVIHHFLCHVLSLLKLACGSKTSSVIMGVMLVCVTALIGCLFLIILSFVFIVAAILRIPSAEGRHKTFSTCVSHLTVVVMHYSFASLIYLKPKGLHSMYSDALMATTYTVFTPFLSPIIFSLRNKELKNAINKNFCRRFCPLSS | Function: Odorant receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35721
Sequence Length: 316
Subcellular Location: Cell membrane
|
Q8NGA6 | MQGLNHTSVSEFILVGFSAFPHLQLMLFLLFLLMYLFTLLGNLLIMATVWSERSLHMPMYLFLCALSITEILYTVAIIPRMLADLLSTQRSIAFLACASQMFFSFSFGFTHSFLLTVMGYDRYVAICHPLRYNVLMSLRGCTCRVGCSWAGGLVMGMVVTSAIFHLAFCGHKEIHHFFCHVPPLLKLACGDDVLVVAKGVGLVCITALLGCFLLILLSYAFIVAAILKIPSAEGRNKAFSTCASHLTVVVVHYGFASVIYLKPKGPQSPEGDTLMGITYTVLTPFLSPIIFSLRNKELKVAMKKTCFTKLFPQNC | Function: Odorant receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34900
Sequence Length: 315
Subcellular Location: Cell membrane
|
P30954 | MLLCFRFGNQSMKRENFTLITDFVFQGFSSFHEQQITLFGVFLALYILTLAGNIIIVTIIRMDLHLHTPMYFFLSMLSTSETVYTLVILPRMLSSLVGMSQPISLAGCATQMFFFVTFGITNCFLLTAMGYDRYVAICNPLRYMVIMNKRLRIQLVLGACSIGLIVAITQVTSVFRLPFCARKVPHFFCDIRPVMKLSCIDTTVNEILTLIISVLVLVVPMGLVFISYVLIISTILKIASVEGRKKAFATCASHLTVVIVHYSCASIAYLKPKSENTREHDQLISVTYTVITPLLNPVVYTLRNKEVKDALCRAVGGKFS | Function: Odorant receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35925
Sequence Length: 320
Subcellular Location: Cell membrane
|
Q5JRS4 | MPKLNSTFVTEFLFEGFSSFRRQHKLVFFVVFLTLYLLTLSGNVIIMTIIRLDHHLHTPMYFFLCMLSISETCYTVAIIPHMLSGLLNPHQPIATQSCATQLFFYLTFGINNCFLLTVMGYDRYVAICNPLRYSVIMGKRACIQLASGSLGIGLGMAIVQVTSVFGLPFCDAFVISHFFCDVRHLLKLACTDTTVNEIINFVVSVCVLVLPMGLVFISYVLIISTILKIASAEGQKKAFATCASHLTVVIIHYGCASIIYLKPKSQSSLGQDRLISVTYTHHSPTEPCCVQPEEQGGQRCSAQSRGAKNSVSLMKRGCEG... | Function: Odorant receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 36549
Sequence Length: 329
Subcellular Location: Cell membrane
|
P0C629 | MPRPNFMAVTEFTFEGFSIFEWHHRLILFVIFLVLYVLTLASNAIILIVIRLNHQLHTPMYFFLSVLSISETYYTVAINPQMLSGLLSPQQTISIPGCAAQLFFYLTFGVNKCFLLTAMGYDHYVAICNPLQYSVIMGKKACIQLVSGSWNIGLSTAIIQVSSVFSLPFCDANLISHFFCDIRPIMKLACADTTIKEFITLLISLCVLVLPMVLIFISYVLIVTTILKIASAEGRRKAFATCASHLTVVIVHYGRTSFIYLKPKSQNSLQDRLISVTYTVITPLLNPVVYSLRNKEVKDALLRALGRKPLS | Function: Odorant receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34925
Sequence Length: 311
Subcellular Location: Cell membrane
|
Q8NHC4 | MKRKNFTEVSEFIFLGFSSFGKHQITLFVVFLTVYILTLVANIIIVTIICIDHHLHTPMYFFLSMLASSETVYTLVIVPRMLLSLIFHNQPISLAGCATQMFFFVILATNNCFLLTAMGYDRYVAICRPLRYTVIMSKGLCAQLVCGSFGIGLTMAVLHVTAMFNLPFCGTVVDHFFCDIYPVMKLSCIDTTINEIINYGVSSFVIFVPIGLIFISYVLVISSILQIASAEGRKKTFATCVSHLTVVIVHCGCASIAYLKPKSESSIEKDLVLSVTYTIITPLLNPVVYSLRNKEVKDALCRVVGRNIS | Function: Olfactory receptor. Activated by the synthetic floral odorant, lyral, and by alpha-cedrene, a sesquiterpene constituent of cedarwood oil. Its activation increases intracellular Ca(2+) . Acts as a key regulator of myogenesis through its actions on cell migration and adhesion by activating the Ca(2+)-dependent ... |
Q62007 | MQRNNFTEVIEFVFLGFSSFGKHQITLFVVFLTIYILTLAGNIIIVTITHIDHHLHTPMYFFLSMLASSETVYTLVIVPRMLSSLIFYNLPISLAGCATQMFFFVTLATNNCFLLTAMGYDRYVAICNPLRYTIIMSKGMCALLVCGSLGTGLVMAVLHVPAMFHLPFCGTVVEHFFCDIYPVMKLSCVDTTVNEIINYGVSSFVILVPIGLIFISYVLIVSSILKIVSTEGQKKAFATCASHLTVVIVHYGCASIAYLKPKSESSVEKDLLLSVTYTIITPLLNPVVYSLRNKEVKDALCRAVGRNTS | Function: Olfactory receptor. Activated by the synthetic floral odorant, lyral, and by alpha-cedrene, a sesquiterpene constituent of cedarwood oil . Its activation increases intracellular Ca(2+) . Acts as a key regulator of myogenesis through its actions on cell migration and adhesion by activating the Ca(2+)-dependent... |
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