ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
O99826 | MVTLVIALYFIGMLMLFINRHFLMMILLSIESMYMSLLLMLCIYFCFFNLLSIFVFLISIVCEAGLALSLLVMMSFFYGNELMMSMNLIKC | 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... |
Q9B6D6 | MFLTSILLSSLYLFNRILAWQGNVKHFYLFASNLLLLFIVVLYINFNTFSNSFQFNFELFNSLNPFGLSNSDISNGLLFGIDGLSLTFILLTVLLIPLTLLGNWYNINFNSNLYYTLVLAIGLVILLNFWALDYISFYILFEATLPLLFILIHIYGSSDSERASFYVLMFTLSGSLFMLLSIVVISIVLNTTNFINHNLFVLSLDLQTIIWLGLFIAIMVKTPLFPIHVWLPVVHSESPLAGSMILAGLILKLALYAILRLLLPLLCEAQILYTPMIYIISLLTIILTSLATLRQIDLKVIIAYSSISHMGIAILGVCSN... | 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... |
Q9C829 | MGDSENVQQPSKKRGALKQLSRDNPGLDDDDDSAELESGTFKKASDEVLASRRIVRVKRKEPSAAPVAASNPFAGIQLVPTTAPASTPVGTNAPLAESKLAPAEAVVEDNQKASDIEEGDEVDSKKVDVKDAVGEETEKTKDKDDNHCGKSADVQVAATEVAQMVSCDTNVCNNAVEGTDQTDFPLEKDSGGDQAEKKEKEGNGIEEADKNGDNGAFSSFQQHSSNKNAFTGLASTEASGSSFSFGLVSQDGSTGTGSLFGFGLPSSNSSSIFGATGSSIIKKSEGSGFPPKQEVSTETGEENEKVAFSADSIMFEYLDG... | Function: Probably involved in nucleocytoplasmic transport via its interactions with importins and Ran, rather than by forming part of the nuclear pore complex (NPC) scaffolding.
Sequence Mass (Da): 46592
Sequence Length: 440
Domain: Contains FG repeats mediating the translocation through the NPC by interacting with tr... |
B1X5V5 | MSLSTVLSLSTQFAWLIPIYGFAGMVVSLPWATGWIQRNAPRTPAYLNLIISLVAFLHGSLALQDVLQNGAHIIRFPWLNLSQADLQLNISLDISPTNLAALELITGLSFIAQLYALGYLDKEWALARFFALAGFFEGAMSGVVLSDSLFQSYFLLEMLTLSTYLLVGFWYAQPLVVTAARDAFLTKRVGDVMLLMGVVALSAFAGGMEFEDLYTWADKNTLTPLATTLLGLALIAGPIGKCAQFPMHLWLDEAMEGPNPASILRNSVVVTCGAIVLMKLMPILHHSQITIAVLLAIGTISALGGSLVSIAQVDIKRTLS... | 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... |
Q85FH9 | MKLSNEYAWIIPLCPLIASCCTGSLSFFFPRVARGFHRLCALLNVFSLAISMFVSLAIFQEQFVKNPIQQYLWIWIPRSTFCVEIGFLVDSLTLVMSLLVTTVGVLVMIYSDSYMCYDRGYTRFYAYLSLFTASMLGLVLSPNLIQLYVFWELVGMCSYLLVGFWFARSSAANACQKAFVTNRIGDFGLLLGILGIYWTTGSFEISELCDRFAKLKEIGFSNPILTNIIAFLLLAGPVAKSAQFPLHVWLPDAMEGPTPISALIHAATMVAAGIFFIARIYGLISTLPLVMQASSWLGGATALLGATLALAQRDLKKGLA... | 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... |
P56752 | MEHTYQYSWIIPFIPLPVPILLGVGLLLFPTATKNLRRMWTFLSIFLLSIVMIFSIYLSIQQIFLSCIHQNVWSWTINNEFSFEFGYFIDPLTSIMSILITTVGILVLIYSDNYMSHDQGYLRFFAYMGFFNTSMLGLVTSSNLIQVYFFWELVGMCSYLLIGFWFTRPIAANACQKAFVTNRVGDFGLLLGILGLYWITGSFEFQDLFEIFNNLILNNRVNLLFLTLCAFLLFVGPIAKSAQFPLHVWLPDAMEGPTPISALIHAATMVAAGIFLVARLLPLFIVIPSIMYIISLIGIITVLLGATLALAQKDIKRGLA... | 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... |
Q27RZ6 | MDLSEPIHDFLLVFLGSGLILGGLGVVLLPNPIYSAFSLGLVLICTSLFYILSNSYFVAAAQLLIYVGAINVLIIFAVMFMNGSEYYKDFHLWTVGDGITSMVCISLFISLITTISDTSWYGIIWTTRSNQIIEQDFLSNSQQIGIHLSTDFFLPFELISIILLVALIGAIAVARQ | 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... |
Q9M3I8 | MDLPGPIHDFLLVFLGSGLILGALGVVLFTNPIFSAFSLGLVLVCISLFYILANSHFVASAQLLIYVGAINVLIIFSVMFMSGPEYDKKFQLWTVGDGVTSLVCISLFVSLISTILNTSWYGIIWTTKSNQILEQDLINASQQIGIHLSTDFFLPFELISIILLVSLIGAIAVARQ | 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... |
Q32S04 | MNMVSLPETINSPILYFLDVGILLGGLGVVFFGKIIYSALFLGVVFVCVALLYLLLNADFLAAAQILIYVGAINVLIVFAIMLINKPETKINKKKITFGDILSGFSVFGLFSFLIIMILNTTWLQPTLVSQEVKNSFQSIDIIGIHLLTDLLLPFELLSILLLVALVGAITIARKEISPKI | 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... |
P26523 | MNLAEGVQYISFLILAFLVIGAALGVVLLSNIVYSAFLLGGVFLSISGIYILLNADFVAAAQVLVYVGAVSVLILFAIMLVNKREDFSKIPGRWLRNVSTALVCTGIFALLSTMVLITPWQINETGPFVENTLVTIGKHFFSDYLLPFELASVLLLMAMVGAIILARRDLIPELSEENKTATALTLPERPRELTSASK | Function: NDH-1 shuttles electrons from NAD(P)H, 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 plastoquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hyd... |
Q0ZIW5 | MDLPGPIHDFLLVFLGSGLILGGLGVVLLTNPIYSAFSLGLVFVCISLFYIPSNSHFVAAAQLLIYVGAINVLIIFAVMFMNGSEYYKDFNLWTVGDGVTSVVCTSIFASLITTILDTSWYGIIWTTRSNQIIEQDLISNSQQIGIHLSTDFFLPFELISIILLVALIGAIAVARQ | 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... |
Q37371 | MLTNYLLIIFCFLALFCSFMIIASKNPIHSILYLILVFCNVTFVLIILGVEFIAIIFLIVYVGAIAVLFLFVVMMLNIKILELDEVFWRYIPAGLLISSCFLFQLFTFVFNFSVVEVFGLFFYNGFYSINKLALNFSEIHTVPSGLLINGIYIFPNLSNLGIDQVFINSIYKEESFFCFVKLNEASTNLLGLSFELTNTEILGWLVYTYTFFIFLVVSLILLISMIGSIILVLNQNINIKRQVIFRQSLRDLKSSVSLKN | 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... |
Q02819 | MPTSVPRGAPFLLLPPLLMLSAVLAVPVDRAAPPQEDSQATETPDTGLYYHRYLQEVINVLETDGHFREKLQAANAEDIKSGKLSQELDFVSHNVRTKLDELKRQEVSRLRMLLKAKMDAKQEPNLQVDHMNLLKQFEHLDPQNQHTFEARDLELLIQTATRDLAQYDAAHHEEFKRYEMLKEHERRRYLESLGEEQRKEAERKLQEQQRRHREHPKVNVPGSQAQLKEVWEELDGLDPNRFNPKTFFILHDINSDGVLDEQELEALFTKELEKVYDPKNEEDDMREMEEERLRMREHVMKNVDTNQDRLVTLEEFLAST... | Function: Major calcium-binding protein of the Golgi which may have a role in calcium homeostasis (By similarity). Acts as a non-receptor guanine nucleotide exchange factor which binds to and activates alpha subunits of guanine nucleotide-binding proteins (G proteins) (By similarity).
Location Topology: Peripheral memb... |
Q63083 | MPTSVPRGAPFLLLPPLLMLSAVLAVPVDRAAPHQEDNQATETPDTGLYYHRYLQEVINVLETDGHFREKLQAANAEDIKSGKLSQELDFVSHNVRTKLDELKRQEVSRLRMLLKAKMDAKQEPNLQVDHMNLLKQFEHLDPQNQHTFEARDLELLIQTATRDLAQYDAAHHEEFKRYEMLKEHERRRYLESLGEEQRKEAERKLQEQQRRHREHPKVNVPGSQAQLKEVWEELDGLDPNRFNPKTFFILHDINSDGVLDEQELEALFTKELEKVYDPKNEEDDMREMEEERLRMREHVMKNVDTNQDRLVTLEEFLAST... | Function: Major calcium-binding protein of the Golgi which may have a role in calcium homeostasis . Acts as a non-receptor guanine nucleotide exchange factor which binds to and activates alpha subunits of guanine nucleotide-binding proteins (G proteins) .
Location Topology: Peripheral membrane protein
Sequence Mass (Da... |
P80303 | MRWRTILLQYCFLLITCLLTALEAVPIDIDKTKVQNIHPVESAKIEPPDTGLYYDEYLKQVIDVLETDKHFREKLQKADIEEIKSGRLSKELDLVSHHVRTKLDELKRQEVGRLRMLIKAKLDSLQDIGMDHQALLKQFDHLNHLNPDKFESTDLDMLIKAATSDLEHYDKTRHEEFKKYEMMKEHERREYLKTLNEEKRKEEESKFEEMKKKHENHPKVNHPGSKDQLKEVWEETDGLDPNDFDPKTFFKLHDVNSDGFLDEQELEALFTKELEKVYDPKNEEDDMVEMEEERLRMREHVMNEVDTNKDRLVTLEEFLK... | Function: Calcium-binding protein which may have a role in calcium homeostasis (By similarity). Acts as a non-receptor guanine nucleotide exchange factor which binds to and activates guanine nucleotide-binding protein (G-protein) alpha subunit GNAI3 (By similarity).
Location Topology: Peripheral membrane protein
Sequen... |
Q9JI85 | MRWRTIQARYCFLLVPCVLTALEAVPIDVDKTKVHNVEPVESARIEPPDTGLYYDEYLKQVIEVLETDPHFREKLQKADIEEIRSGRLSQELDLVSHKVRTRLDELKRQEVGRLRMLIKAKLDALQDTGMNHHLLLKQFEHLNHQNPDTFESKDLDMLIKAATADLEQYDRTRHEEFKKYEMMKEHERREYLKTLSEEKRKEEEAKFAEMKRKHEDHPKVNHPGSKDQLKEVWEETDGLDPNDFDPKTFFKLHDVNNDGFLDEQELEALFTKELDKVYNPQNAEDDMIEMEEERLRMREHVMNEIDNNKDRLVTLEEFLR... | Function: Calcium-binding protein which may have a role in calcium homeostasis (By similarity). Acts as a non-receptor guanine nucleotide exchange factor which binds to and activates guanine nucleotide-binding protein (G-protein) alpha subunit GNAI3 .
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 5... |
P42983 | MKKWMAGLFLAAAVLLCLMVPQQIQGASSYDKVLYFPLSRYPETGSHIRDAIAEGHPDICTIDRDGADKRREESLKGIPTKPGYDRDEWPMAVCEEGGAGADVRYVTPSDNRGAGSWVGNQMSSYPDGTRVLFIVQ | Cofactor: Mn(2+) ion stimulates activity.
Function: Degrades both double-stranded linear and covalently closed circular DNA. Likely to play a scavenging role in order to supply nutrients under starvation conditions.
Sequence Mass (Da): 14968
Sequence Length: 136
Subcellular Location: Secreted
EC: 3.-.-.-
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P0DTF8 | MSQWSLSQLLSSLHEDIQQRLSVVRKTFGHPGTKGDASENVWIDMLDTYLPKRYQAAKAHVVDSLGNFSQQIDVVVFDRQYSPFIFTYENETIIPAESVYAVFEAKQTADAGLVAYAQEKVASVRRLHRTSLPIPHAGGTYPAKPLIPILGGLLTFESEWSPALGPSMDKALNANLTEGRLDIGCVAAHGHFFYDQASGAYSYTNENKPATAFLFKLIAQLQFSGTVPMIDVEAYGQWLTK | Function: CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell ... |
O67335 | MKWVNKGTVERVKQEFKDEVKYYETKHTKGFEVSHDFLKPLLKFLKERERFLHFVDMTCIDFPEHPNRFQGVYILYNPEENERVIVKSWAKDGKLPTVEDLWPGAKWAEREAYDMFGVVFEGHENLRRMFMWEGYEHYPLRKDFPLQGIPEVELPSLTEVLHGRTDPPSHDFELVHTKLPTLEDLERTEKARLKKKAELVLNWGPLHPGTHGTIWFLFDLEGEKVVQSDVILGQLHRGMEKLAENLHYFQFIPYTDRMDYISAICNELAYVETVERLLGVEVPEKARYIRTMFAELQRINSHLLWLGTGALDLGALTVFL... | 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 ... |
P0A3S3 | MNKKTRQTLIGLLVLLLLSTGSYYIKQMPSAPNSPKTNLSQKKQASEAPSQALAESVLTDAVKSQIKGSLEWNGSGAFIVNGNKTNLDAKVSSKPYADNKTKTVGKETVPTVANALLSKATRQYKNRKETGNGSTSWTPPGWHQVKNLKGSYTHAVDRGHLLGYALIGGLDGFDASTSNPKNIAVQTAWANQAQAEYSTGQNYYESKVRKALDQNKRVRYRVTLYYASNEDLVPSASQIEAKSSDGELEFNVLVPNVQKGLQLDYRTGEVTVTQ | Function: By degrading DNA that enters the cell, plays a role in the competence of cells to be transformed.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 29891
Sequence Length: 274
Subcellular Location: Cell membrane
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Q95NM6 | MIGKVAGTAAIAGISFLAGKYSNDDLPIFRNVQSATNVPMNQIQVSEPMTVKPASLNADAMGPSRSAEIMKHGYPGFTNVRTYEDFVLSYDYKTRTAHWVCEHLTPERLKHAEGVDRKLCEFKPDITFPQKFLSQNTDYKCSGFDRGHLAAAGNHRKSQLAVDQTFYLSNMSPQVGRGFNRDKWNDLEMHCRRVAKKMINSYIITGPLYLPKLEGDGKKYIKYQVIGDNNVAVPTHFFKVALFEVTPGKFELESYILPNAVIEDTVEISKFHVPLDAVERSAGLEIFARLDPKSIVKENGAKKGGLLW | Function: Endonuclease important for programmed cell death; it mediates apoptotic DNA fragmentation.
Sequence Mass (Da): 34511
Sequence Length: 308
Subcellular Location: Mitochondrion
EC: 3.1.30.-
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Q14249 | MRALRAGLTLASGAGLGAVVEGWRRRREDARAAPGLLGRLPVLPVAAAAELPPVPGGPRGPGELAKYGLPGLAQLKSRESYVLCYDPRTRGALWVVEQLRPERLRGDGDRRECDFREDDSVHAYHRATNADYRGSGFDRGHLAAAANHRWSQKAMDDTFYLSNVAPQVPHLNQNAWNNLEKYSRSLTRSYQNVYVCTGPLFLPRTEADGKSYVKYQVIGKNHVAVPTHFFKVLILEAAGGQIELRTYVMPNAPVDEAIPLERFLVPIESIERASGLLFVPNILARAGSLKAITAGSK | Function: Endonuclease that preferentially catalyzes the cleavage of double-stranded 5-hydroxymethylcytosine (5hmC)-modified DNA . The 5hmC-modified nucleotide does not increase the binding affinity, but instead increases the efficiency of cutting and specifies the site of cleavage for the modified DNAs (By similarity)... |
O08600 | MRALRAGLTLALGAGLGAAAEHWRRREGKAPGLLGRVPLLPVVAADLPALPGGPAGGTGELAKYGLPGVAQLRSRESYVLSYDPRTRGALWVLEQLRPERLRGDGDRSACDFREDDSVHAYHRATNADYRGSGFDRGHLAAAANHRWSQRAMDDTFYLSNVAPQVPHLNQNAWNNLERYSRSLTRTYQNVYVCTGPLFLPRTEADGKSYVKYQVIGKNHVAVPTHFFKVLILEAAGGQIELRSYVMPNAPVDETIPLERFLVPIESIERASGLLFVPNILARAGNLKAITAGSK | Function: Endonuclease that preferentially catalyzes the cleavage of double-stranded 5-hydroxymethylcytosine (5hmC)-modified DNA . The 5hmC-modified nucleotide does not increase the binding affinity, but instead increases the efficiency of cutting and specifies the site of cleavage for the modified DNAs . Shows signifi... |
Q9H1E3 | MSRPVRNRKVVDYSQFQESDDADEDYGRDSGPPTKKIRSSPREAKNKRRSGKNSQEDSEDSEDKDVKTKKDDSHSAEDSEDEKEDHKNVRQQRQAASKAASKQREMLMEDVGSEEEQEEEDEAPFQEKDSGSDEDFLMEDDDDSDYGSSKKKNKKMVKKSKPERKEKKMPKPRLKATVTPSPVKGKGKVGRPTASKASKEKTPSPKEEDEEPESPPEKKTSTSPPPEKSGDEGSEDEAPSGED | Function: Chromatin-associated protein involved in DNA repair by promoting homologous recombination (HR) . Binds double-stranded DNA (dsDNA) and secondary DNA structures, such as D-loop structures, but with less affinity than RAD51AP1 .
PTM: Phosphorylated in an ATM-dependent manner in response to DNA damage . Phosphor... |
P45799 | MSKSLQKPTILNVETVARSRLFTVESVDLEFSNGVRRVYERMRPTNREAVMIVPIVDDHLILIREYAVGTESYELGFSKGLIDPGESVYEAANRELKEEVGFGANDLTFLKKLSMAPSYFSSKMNIVVAQDLYPESLEGDEPEPLPQVRWPLAHMMDLLEDPDFNEARNVSALFLVREWLKGQGRV | Cofactor: Mg(2+). Other divalent cations can also be used.
Function: Active on adenosine(5')triphospho(5')adenosine (Ap3A), ADP-ribose, NADH, adenosine(5')diphospho(5')adenosine (Ap2A).
Catalytic Activity: ADP-D-ribose + H2O = AMP + D-ribose 5-phosphate + 2 H(+)
Sequence Mass (Da): 21153
Sequence Length: 186
EC: 3.6.1.... |
P77788 | MKMIEVVAAIIERDGKILLAQRPAQSDQAGLWEFAGGKVEPDESQRQALVRELREELGIEATVGEYVASHQREVSGRIIHLHAWHVPDFHGTLQAHEHQALVWCSPEEALQYPLAPADIPLLEAFMALRAARPAD | Cofactor: Divalent metal ions. Mg(2+) or Mn(2+).
Function: Hydrolase with a preference for pyrimidine substrates. Has high activity with 5-methyl-dCTP, and much lower activity with CTP, dCTP, 5-hydroxy-dCTP, 2-hydroxy-dATP and 8-hydroxy-dGTP.
Catalytic Activity: CTP + H2O = CMP + diphosphate + H(+)
Sequence Mass (Da): ... |
B3QY48 | MDYTISEFGKVFLFLLFGVVFVIGGYVSSRMLRPHRPNDEKLTSYECGEEAVGSAWVQFNIRFYVVALIFIIFDVEVLFLFPWATVFKQLGGFALFEAVIFVTILTLGLVYAWVKGDLDWVRPTPNVPKMPEKRFDNISSGRSQVVKEESVS | 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... |
Q746S3 | MQPAGISHSLFPSLPPEFLPLALYTLAASILIGVLLLAAWWLGAKTTNRNKELPYESGAIPTGSARLAYPVPFYLIAIFFIVFDVEAAFIFAWATAWRELGLQGLVHITFFIVILLLGLVWLWLKGGLDWGPSRARRGHVRD | 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 ... |
P56895 | MTAMEFLPVLFMVTGIVLVAAATLFVSSLLRPSNPYPEKNAPYECGMEAAGEAAGGRFRVPFFILAILLVVFDVEAMFLFPWAVVLKEIGFVGYIEMFVFMLLLLVGFAYAWLKGALEWQE | 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 ... |
Q6FE71 | MSAITPYDWAIIAFVIGVTFLCVFMLTVPLLLGGKSWGRAKQEQFESGVVSAGGARIRLSAKFYLVAIFFVVFDLEALYLYAWATSVREVGWMGFTTMVIFVVDLLIALIYVFATGALTWSPSDRRKAAGIKPKIGSPNMNIAEITRFNSIEELVIDPTGHIPAQSSGRMKSKTSTAPSSKQE | 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 ... |
B0V7U8 | MSAITPYDWAIIAFVIGVTFLCVFMLTVPLLLGGKSWGRAKQEQFESGVVSAGGARIRLSAKFYLVAIFFVVFDLEALYLYAWSTSVREVGWLGYTTVVIFVVDLLIALVYAFSVGALSWAPADRRKLAGEKVKVGSPTMNIAEITRFNSIEELVTDPTGQIPAQSSGRVKSKTTPALSSEKE | 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 ... |
B5EN71 | MLNHYLPVLIFLLVALVVGVAPLLMGSSLGPHRPDSEKLSPYECGFEAFEDARMKFDVRYYLVAILFILFDLEIAFLFPWAVVFDQIGMTGFLAMMLFLAILVVGFIYEWKKGALEWE | 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 ... |
A6TBX4 | MRMSTSTEVIAHHWAFAIFLIIAIGLCCLMLVGGWYLGGRARARSKNTPFESGIDSVGSARLRLSAKFYLVAMFFVIFDVEALYLYAWSTSIRESGWVGFVEAAIFILVLLAGLVYLVRIGALDWTPARSRRTLVNPETDSPTNRHMQ | 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 ... |
Q608X7 | MSSAGVPHTDLWPLLLYFELVLVVVGTMLALPPFLGERRTRRTPATEQPYESGIVAVGSSQLRFSVRFYLIAIFFVIFDLEAVFIFAWAIAFRESGWPGYIEILIFIGVLVATLVYLWRIGALDWRTPRQRSIEATIHQ | 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 ... |
P65564 | MNVYIPILVLAALAAAFAVVSVVIASLVGPSRFNRSKQAAYECGIEPASTGARTSIGPGAASGQRFPIKYYLTAMLFIVFDIEIVFLYPWAVSYDSLGTFALVEMAIFMLTVFVAYAYVWRRGGLTWD | 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... |
Q1D8S2 | MTPTPLTPYLPLAVVLLLAGGMAMLIPQITTRLGPRRPSAIKATSFEAGSESSGPARQRFAVKFYVVALLFIVFDVEAVFLYPWAVNFQALGWFGYVEMLVFAVTLVVGLIYIWKKGALDWES | 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 ... |
Q2GDY1 | MLESSVVGIGKWVVEDYIFVGLFFVVACFISCVMLALPVFIAPSSHERHKGDSYECGFDKLSSTGERFNVRFYLVGILFIIFDLEIIFLFPWAVSARELGPAAFVSVLIFLIILTVGFVYEFVSGALDWR | 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 ... |
Q2YAA5 | MNASATQATEIWPLVAYFFLVVMLVVGVMALSYIIGERHRSKATDEPFESGIVTVGLARFRLSAKFYLIAVFFVIFDVEAVFLFAWAVAFRELGWPGYIEAIIFISILGAALAYLWRLGALDWGPPRHSAGRFAKDSRSPNHAVVSK | 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 ... |
Q3JC15 | MQFTEFWPFILYAGMVLVLVALIVGFSYILGQRPRERATDEPFESGVVTVGFARLRFPAKFYLVAVLFVIFDMEAAFIFAWAVAFRETGWIGYGGALAFITILGVALIYEWRVGALDWQPKGRKHKKHR | 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 ... |
Q142H3 | MNLAAYFPVLLFLIVGTGLGVALVSIGKILGPNKPDTEKNAPYECGFEAFEDARMKFDVRYYLVAILFIIFDLETAFLFPWGVALRDIGWPGFMAMMIFLLEFLLGFAYIWKKGGLDWE | 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 ... |
B3QY47 | MGLLDQKFDKGGVVITAAENVLNWARLSSLWPMGFGLACCAIEMMATNASNYDLERFGIFPRSSPRQSDLMIVAGTVTFKMAERVVRLYEQMPEPRYVLSMGSCSNCGGPYWEHGYHVVKGVDRIIPVDVYVPGCPPRPEALIGGLMKVQELIREEKFAGDRREAIERLKPKKVKAEDVIVETSASAKKLQEAAS | 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... |
Q1IL91 | MSWIENKFEKNFLLSSVDYVFNWARKSSVWPMTFGLACCAIEMITASTARYDIARFGSEVFRPSPRQSDLMIVAGTVTLKMAPVVQRIYEQMPEPKWVMAMGACASVGGPFNTYATLQGVDKIVPVDVYVVGCPPRPENLFYGLLKLQDKIDHMTLAKRPTDVRLDETMLDEFRKSVRIAQAGSTVVIQPAAPPVVPGLQTK | 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 ubiquinone. Couples the redox reaction to proton translocation (for every two e... |
B1ZUJ0 | MESPLTPSAQPAPMPSLVAATGPSTPEIPPEVSQIARFAKLDDLLALGRANSLWPLTFGLACCAIEMMAAGMARFDISRFGAEVFRPSPRQADVMIVAGTVNKKMAPAVKLLYDQMLEPKWVIAMGQCAISGGPFKYPGQYAVVEGVDQLFPVDVYVPGCPPRPEALIEGILKLEEKITGKRRFPVAQLKE | 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 ubiquinone. Couples the redox reaction to proton translocation (for every two e... |
Q6N1Y9 | MTMTPQHPGMPDEQRSVEEHMALSSLFTTLEDLTAWSRKHSLWPFNFGLSCCYVEQVTVLTPVYDQARFGAEVIRASPRQADLLVVSGTVFHKMAAPLLRLYEQMRAPRWVIAMGACACSGGMYDIYSVVQGVDRFIPVDVYIPGCPPRPEAVLDALIMLQQQVGSERRPLGVTVGNTAGLGFDAPRRRDQRRDERMAQTLLDPPESL | 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 ubiquinone. Couples the redox reaction to proton translocation (for every two e... |
Q2GG48 | MINKNDSVLNNQFWQSYNHQGFMVTQFSDLINYISNWARSNSLWPMTFGLACCAVEMMHTAASRYDLDRYGVMFRASPRQADVMIVAGTLTNKMAPALRKVYDQMTEPRYVISMGSCANGGGYYHYSYSVVRGCDRIVPVDIYVPGCPPTAEALLYGIFCLQQKINRGNTSITRKSTQD | 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 ubiquinone. Couples the redox reaction to proton translocation (for every two e... |
Q5FHF7 | MINKHNSVLHNQFWQSYNHRGFMVTKLSDLMSYVSSWARSNSLWPMTFGLACCAVEMMHTAASKYDLDRYGIMFRASPRQADVMIVAGTLTNKMAPALRKVYDQMTEPRYVISMGSCANGGGYYHYSYSVVRGCDRIVPVDIYVPGCPPTAEALLYGILCLQQKINRTATST | 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... |
A6H1R3 | MSSNINIVEAPEGVTGEGFFATKLNDVVGLARANSMWPLPFATSCCGIEFMATMASHYDLARFGSERVSFSPRQADMLMVMGTISKKMAPILRQVYEQMAEPRWVIAVGACASSGGIFDTYSVLQGIDKVIPVDVYVPGCPPRPEQIVDGVMRLQELVKSESVRRRSSPEYQELLASYNIK | 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... |
Q0RRW7 | MGLEEKLPGGVLLASVEKLANWSRRSSLWPATFGLACCAIEMMSTGAGRYDLSRFGMEVFRASPRQADLMIVAGRVSQKMAPVLRQIYDQMPEPKWVLSMGVCASSGGMFNNYAIVQGVDHIVPVDMYLPGCPPRPEMLMDAIIKLHEKILAGPVTGRTAHTESGSSPYPKPIDVATARAGLPAGELDTRTLSVNDRKRFRIPAGAPVPTGRGAVEPVLDTRRPAAIAPPSVFGRAKGIPVDAKPLDESRAHGPGPTTADIADAADTADSDAAPGATHDTP | 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... |
Q0A777 | MAKKLEQLQTAVQERLGERLRDCVLDADRGELAIEVAPADLHQAMTTLRDAEGLRFDMLMDLAGVDYAAWGEDEWFTDTAEGTGFSRGVQGNNFARLGITGIYGVQEITENTGRRFAAVYQLLSVELNQRLRVRCFCEDDRFPVLDSVVDVWSGANWFEREAFDLYGIIFDGHPDLRRILTDYGFVGHPFRKDFPLIGNVEVRYDEQKRRVIYQPVSIEPRVLVPRVVREDNRYADRKRREEGASDA | 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 ... |
B2HGE6 | MSSPDQNPSDAAGQTGSSNEEVVDVRRGMFGVKGTGDTSGYGRLVREIVLPGSSPRPYGFYFDEIADRLAEALNRDGVEFEDAIEKVVVYRNELTLHVRREALLRVAQSLRDEPELRFELCLGVNGVHYPHETGRELHAVYPLQSITHNRRLRLEVSAPDSDPHIPSLYAVYPTNDWHERETYDFFGIIFDGHPSLTRIEMPDDWQGHPQRKDYPLGGIPVEYKGAQIPPPDERRGYN | 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... |
A0QU34 | MSTSNGSANGTNGVGLPRGDEPEIIAVRRGMFGNRDTGDTSGYGRLVRPVALPGSTPRPYGGYFDAVMDRLAEVLGEERYAMSIERVVVYRDQLTIEVSRVQLPAVASVLRDDPDLRFELCLGVSGVHYPEDTGRELHAVYPLMSITHNRRIQLEVAAPDADPHIPSLYAVYPTTDWHERETYDFFGIIFDGHPSLTRIEMPDDWEGHPQRKDYPLGGIPVEYHGAQIPPPDQRRSYS | 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... |
Q9K1C1 | MASIQDLYETVSRVLGNQAGKVISALGEITVECLPEHYISVMTALRDHEELHFELLVDLCGVDYSTYKNEAWQGKRFAVVSQLLSVKNNQRIRVRVWVSDDDFPVVESVVDIYNSADWYEREAFDMYGIMFNNHPDLRRILTDYGFVGHPFRKDFPISGYVEMRYDEEQKRVIYQPVTIEPREITPRIVREENYGGQ | 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 ... |
Q2GDX8 | MTIDTTEVDALINAPGRCVVNSSLESLVELISHLSSCGFEQLTDIFGIDYLEREKRIEVVYLLLDLKRNRRCCVKVSVDPASEKVPTCCGVFSVANWFEREVYDMYGVVFEGHPDLRRILTDYEFEGFPMLKDFPLTGYKEVRYDLESKEVVYEKVDLSQDYRSFDSLTPWKGVGRPSDPFDGRKE | 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 ... |
A4J657 | MTIKTEEFLLNLGPQHPSTHGVFRIVLTLDGETVVKAVPVPGYLHRGIEKLLESRTYTQVIPYTDRLDYLAGMLMNWGYVHAVEKLMEVEIPERAEYIRVIVGELSRIASHLVATGAYAADIGGLTGFIYTFRDREEIMDLFEMISGARLTPSFMRIGGVAYDIPDGFMERCKKFVDYLPEAIKEYNTLITGNEIFQARTKNVAILSAEKAIDMSLSGPVLRATGVNYDLRKVRPYSVYERFEFEVPLGTKGDCFDRYYIRLLEMEQSARIIQQAMDQIPEGPIRAKIPKMIKPPVGEAYAEIESSKGIMGTYVVSDGST... | 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... |
A6H1R1 | MSELLLPPEHRYAKIIKEKLNEDGSELSILNLGPTHPATHGIFQNILLMDGERIVDAEPTIGYIHRAFEKIAENRPFYQITPLTDRMNYCSSPINNMAWWMTLEKLLDIEVPKRAQYLRVIVMELARITDHIICNSILGVDTGAYTGFLYVFQFREKIYEIYEEICGARLTTNMGRIGGFERDWSPKAFQLLNTFLEEFPIAWKEFENLFERNRIFIDRTVNVGAISAEKAMAYGFTGPNLRAAGIDYDVRVAEPYSSYEDFEFIIPVGKSGDTYDRFCVRNAEVWESLSIIRQALAKMPEGNVYHAEVPDYYLPPKEDV... | 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... |
Q2JFL7 | MTTNTSTSSTTDDLTTGAPNGTGAPDGANGVGGPTGTVGGPGEHPAYEAGFTESANGRVYTVTGSDWEQILGVGEEENERIVVNMGPQHPSTHGVLRLVLEIEGETVTETRLVIGYLHTGIEKSCEYRTWTQAVTFLTRADYLSPLFNEAAYCLSVERLLGITEQVPERATVIRVMVMELQRIASHLVWLATGGMELGATTAMIFGFREREKVLDLLELITGLRMNHAYIRPGGLAQDLPDGAERAIRAFLADMPKRIREYHALLTGQPVWKARMVDVNVLDAAGCIALGTTGPVLRAAGLPWDLRKTMPYCGYETYEFD... | 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... |
P56912 | MLRDEDRIFTNIYGLKDKSLRGAMARGHWDGTKQFLEKGRDWIINEVKASGLRGRGGAGFPTGLKWSFMPKESDGRPHYLVVNADESEPGTCKDRDIMRHDPHTLIEGCVIASFAMGAHAAYIYVRGEFIREREALQAAIDECYEYGLLGKNNKLGYDIDIYVHHGAGAYICGEETALLESLEGKKGQPRLKPPFPANMGLYGCPTTVNNVESIAVTPTILRRGAGWYTSFGRPNNHGTKLYSVSGHVNRPCTVEDAMSIPFHELIEKHCGGIRGGWDNLLAVIPGGSSVPCVPGAQMKDAIMDYDGLRELGSGLGTAAV... | Cofactor: Binds 1 FMN.
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 tran... |
P56913 | MFEPVLLRNVDVPDGHLLSTYEAGGGYRALRKALGEYTPDEIVELVKESNLRGRGGAGFPTGMKWSFVPKAAGKPKYLCCNADEGEPGTFKDRIIMERDPHQLIEGLAVSAYAIGAETAYVYIRGEYVTAIRRMEQAIAEAHENGYLGIGILGSGFNFMVHIHRGAGAYICGEETAMLESLEGKRAQPRLKPPFPAVAGLYASPTVINNVETLACVPHIVMRGSAWFRGIGPDRSPGPKLYCLSGQVRKPGLYELPMGISLRELVEEHAGGPLPGRKVKAVIPGGVSAPVIPEGELEVGMDFDSLTAAGSMLGSAGVVVI... | Cofactor: Binds 1 FMN.
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 tran... |
O66841 | MRSYPAIPRIYAETTLNMLLKRAKKPRVHSIDEYLKDGGYQALEKALNMSPEEIIDWVDKSTLRGRGGAGFPTGKKWKFAVQNPGPRYFICNADESEPGTFKDRIIIERDPHLLIEGIIISSYAIGANEAYIYIRGEYPAGYYILRDAIEEAKKKGFLGKNILGSGFDLEIYVARGAGAYICGEETALIESLEGKRGHPRLKPPYPVQKGLWGKPTVVNNVETIANVPFIISMGWEEYRYIGPSDYAGPKLFPVSGKVKKPGVYELPMNTTLREVIFKYAGGTLGNKKVKAVFSGALDCFSSEELDIPMDYSPLGFGGTG... | Cofactor: Binds 1 FMN.
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), and thus conse... |
P31979 | MKNIIRTPETHPLTWRLRDDKQPVWLDEYRSKNGYEGARKALTGLSPDEIVNQVKDAGLKGRGGAGFSTGLKWSLMPKDESMNIRYLLCNADEMEPGTYKDRLLMEQLPHLLVEGMLISAFALKAYRGYIFLRGEYIEAAVNLRRAIAEATEAGLLGKNIMGTGFDFELFVHTGAGRYICGEETALINSLEGRRANPRSKPPFPATSGAWGKPTCVNNVETLCNVPAILANGVEWYQNISKSKDAGTKLMGFSGRVKNPGLWELPFGTTAREILEDYAGGMRDGLKFKAWQPGGAGTDFLTEAHLDLPMEFESIGKAGSR... | Cofactor: Binds 1 FMN.
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 tran... |
P65568 | MTTQATPLTPVISRHWDDPESWTLATYQRHDRYRGYQALQKALTMPPDDVISIVKDSGLRGRGGAGFATGTKWSFIPQGDTGAAAKPHYLVVNADESEPGTCKDIPLMLATPHVLIEGVIIAAYAIRAHHAFVYVRGEVVPVLRRLHNAVAEAYAAGFLGRNIGGSGFDLELVVHAGAGAYICGEETALLDSLEGRRGQPRLRPPFPAVAGLYGCPTVINNVETIASVPSIILGGIDWFRSMGSEKSPGFTLYSLSGHVTRPGQYEAPLGITLRELLDYAGGVRAGHRLKFWTPGGSSTPLLTDEHLDVPLDYEGVGAAG... | Cofactor: Binds 1 FMN.
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 menaquinone. Couples the redox reaction to proton translocation (for every two electrons tra... |
Q9I0J7 | MTLTSIGPANRMARSAETHPLTWRLREDAQPVWLEEYQSKDGYAAARKALTQMAQDDIVQTVKDSGLKGRGGAGFPTGVKWGLMPKDESLNIRYLLCNADEMEPNTWKDRMLMEQLPHLLVEGMLISARALKAYRGYIFLRGEYVDAARNLNRAIDEAKAAGLLGKNILGSGFDFELFVHTGAGRYICGEETALINSLEGRRANPRSKPPFPAAVGVWGKPTCVNNVETLCNVPAIVGNGVDWYKTLARPGSEDMGTKLMGFSGKVKNPGLWELPFGVSARELFEDYAGGMRDGFQLKAWQPGGAGTGFLLPEHLDAQMF... | Cofactor: Binds 1 FMN.
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 tran... |
Q3Z7Z7 | MSDFWVHLLVYLVILFGFVIVSVLLFIWLERRFIGRFQLRPGPNRAGPFGLLQPIADAIKVLIKEDIIPTESDKGVFWLAPLVAFVPVMLMFAAIPFADGAMLVDLNIGILYILAVSSVTVIGIFMAGWSSNSKYSLLGAMRTIAQEVSYEIPLVLSILGVVMLTGSLSMNEIVKAQSVPFVLLQPLGFFVYLSAAMAEINRTPFDLLEAESEIIAGFHTEYSGMKFGLFYLMEYAEVLAISAIATTLFLGGWQGPLLHPVIWFITKVLIIFMFIIWVRATIPRLRIDQVMAFGWKFLLPLSLANLVITAFEILAAPDMN... | 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 ... |
C1D0H8 | MPDWLLTLLITVVKAVAVILALLTTFAYMTLVERKLLGRFQIRVGPNRVGPMGLLQPAADAIKSIFKEDLQVTLADKLVYTLAPIIAIGMALTAFGGIPAGPEGSLFGENPWVYNLDAGVLALLALTSMGVYGIFLGGWASGSKYPMLGGLRSSAQMISYELGMGLSILGLLMLVGSTRFTDIVLWQGANGWMILFQSLGFALFLISSFAETNRTPFDLVEAEQELVAGYLTEYSAIKWALFQMAEYVNMITASALMSTLFFGGWRGPGFLNGIIPGIADIPILWLVVKIGFFLFVFIWVRATLPRLRYDQLMRFGWKLL... | 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 ... |
Q6ANM8 | MSLTLINVLAAALIALAFVAVNAAYLVWAERRGAAFIQRRLGPVENGPWGLLQPPVDGIKLMTKQLVIPGGVDKILFMVAPVLAMFPALMSFVTIPFSENIVAHNMDIGLLVILAFASFAGLAILLAGWSSRNKYSMMAAIRAVSQTIAYEIPMLITAITVVLVSGSVDFIEIVHSQSGGFWHWNLWPLKPGLFNIFMPISFLIFFICSLAETNRAPFDLGEAESELVAGFHTEYSSMGFGLFFMGEYANIVIGACLTTLLFLGGWDCPFGLFPGVWWFLIKIYILIFTFIWIRWTFPRTTIYGLLNLSWKILIPLSLIN... | 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 ... |
Q1AVI7 | MALEYLEQEPWRFLISSATVIFLVLNIAAVLTLAERKVSAYIQLRYGPNRVGPRGLLQPAADVVKLFIKENVSPGRADRWVFLAAPIAMFLPAAAVWLVIPFGPGMVVADLNIGLVYFFAITSIGALGVIMAGYGSRSNFSLLGALRGAGQMISYEVPLILSLLGVAMLTGSLSMVDIVEYQAGGFWNWIIWPQLPMFLAFFVSGLAEVKRIPFDLPEGESEIVGGFMIEYSGMTWALIQASEFASMAVMSAVASTLFLGGWQPPLPFLDLGVFNWLWLGIKTTLLIFVFQWIRWTLPRLRMDQLMDLGWKILVPVTILW... | 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 ... |
A9MJA3 | MSWITPDLIEILLSILKAVVILLVVVTCGAFMSFGERRLLGLFQNRYGPNRVGWGGSLQLVADMIKMFFKEDWVPKFSDRVIFTLAPMIAFTSLLLSFAIVPVSPNWVVADLNIGILFFLMMAGLAVYAVLFAGWSSNNKYSLLGAMRASAQTVSYEVFLGLSLMGVVAQAGSFNMTDIVNNQAHLWNVIPQFFGFVTFAIAGVAVCHRHPFDQPEAEQELADGYHIEYSGMKFGLFFVGEYIGIVTVSALMVTLFFGGWHGPFLPPFVWFALKTAFFMMMFILIRASLPRPRYDQVMSFGWKVCLPLTLINLLVTAAVI... | 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 ... |
Q2RYV5 | MIPSMVWTALGAFLVINAMLLSASLLVFAERRVSAFIQNRPGPNRVGPLGLLQPFADVLKFVLKEDVQPAQSNKFIHSMAPVVMVVIAMTTASLIPFAEGVVVADLNVGVIMLLALTSISVYGVTLAGWSSNSKFSLLGGLRSAAQMVSYELSMGLAVISVVLIAGSLNFMEIVEHQSSGGALLGWNAVRNPIGCLIFIVTAFAETNRAPFDLPEAEEELVAGYHTEYSGMKFGMFFLAEYVNWFIASFFIVTLFFGGYLVPLEPQLIALFPALEGSTLLALLQFVSLMLKVSFFSFVFIWVRWTFPRFKYNQLMKVGWK... | 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 ... |
P0AFD8 | MTLKELLVGFGTQVRSIWMIGLHAFAKRETRMYPEEPVYLPPRYRGRIVLTRDPDGEERCVACNLCAVACPVGCISLQKAETKDGRWYPEFFRINFSRCIFCGLCEEACPTTAIQLTPDFEMGEYKRQDLVYEKEDLLISGPGKYPEYNFYRMAGMAIDGKDKGEAENEAKPIDVKSLLP | 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... |
Q2GGD7 | MIYKKNFSKLSPITNLIRSALLNCRGMYITLRYMFKPKVTLNYPLEKGPLSTRFRGEHALRKYKNGEERCIACKLCEAICPAQAITIEAQERDDGSRRTVRYDIDMTKCIYCGFCQEACPVDAIVEGPNFEYATETREELMYNKSKLLHNGQIWEEAIDLRIKKNSQFY | 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... |
A6H1Q5 | MSTTIQNISLSGRKKQVSNKEMTFLESLYLVAIVKGLLITIKHFFRKKVTIHYPEQVREMSPVYRGQHMLKRDEQGRENCTACGLCALSCPAEAITMKAAERKSNEKHLYREEKYAEIYEINMLRCIFCGLCEEACPKDAIYLTTSKVLVPSNYERENFIFGKDKLVMPLDIAMQNAQLKNAN | 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... |
A0RMD8 | MLDFYILVALILFFIGVLGVILRKNIFTIFMSVELMLNATALIFATFARQSLNLDGQVIVMLIIAIAAAEASFGLALIVLLYKKKQSLNIDIFDELKDRDVS | 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 ... |
A9WFC1 | MVPTSYYVLLSAILFTIGVLGVLLRRNAIVVFMAVELMLNAANLALVAFARERLGVEAQVIVFFVITVAAAEVAVGLALLVSIFRTKRTADVDEVSTLKG | 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 ... |
C4XMN4 | MIVPLSHVLAVAALLFAVGGVMAAARRSILLILIGVEFMLAAAGLAFAGAGLAWNNLDGQAAVIIIMGLASAEAGLGLALLVHGRRGGGTDRADSYDRLGEES | 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 ... |
A9EX69 | MISVPIEYYLVVAAVLFLIGSIGFLLRRNLLVLLMSIELMLNAVNLTLVAYNRVHPHDHAGQIFTFFVIAIAAAEAAVGLAIVLAFYRIRKTMRSDDADLLRS | 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 ... |
Q30PI9 | MMEIGLNHYLVLSTILFAIGLVGVMRRKNLLMLFFATEILLNSVNISFAAISHYYGDLTGQMFAFFVIAIAASEVAVGLGLLIVWHKKHNNIDLDNMSTMRG | 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 ... |
B9L175 | MSELSATHFLLLSAALFIIGMVGVLTRRNVLVIFMCIELMLNAVNVSLIGFAWELHQLTGQVFALFVIAIAAAEAVVGLGIVMALTRRTDTVDIDELRQLRE | 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 ... |
B5YKI9 | MIPLSWYLLLSATLFSIGLIGFVIRRDLIVMLMCLEIMFNAVNIAFASFSYYNSNLTGQIFVLFSIAVAACEAVIGLAIVLALVRNTGINHSDEIVNLRG | 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 ... |
A9HRS3 | MNWTLALPEIVLALCGLAILVFGVVQKKEQPFLSCSMLTIGAFVLTGFLVVMSPDGVGYNHIFVNDDFARFMKILSLAGGAFATMLTVGYARNMKVERFEFPVLLLFSTLGAMMMASSENLMTLFIGLELSSLAIYILCAFARDEVRGGEAGLKYFVLGSLASGLLLYGSSLVYGYAGTMEYGGIQMALSTSSTAVPMGLMFGIVFMLAGLTFKLSAVPFHMWTPDVYQGAPTSVTAYMAGAPKFAAFALLLRVMAGPFGHVAPQWQILVEGVSMLSMLFGSLAAIPQTDIKRLMAYSSIGHMGYALMGLCAGTAEGMRG... | 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 ... |
Q0BSL5 | MNWTLASPEIVLALCGLVILLVGVARNRREDTFLCAMLTLGAFLVTGLLTVSGALGLGFQGQFVADPFAVMVKLLILSGASIAVVLSLDYNRHHGMERFEFPVLTLFSTVGMMVMVSASNFMTLYMGLELMSLAIYVLAAFARDELRSAEAGLKYFVLGSLASGLLLYGISLIYGFAGTMDFSALREALAHPAGTSPGLTVGVVFVIAGLAFKISAAPFHMWTPDVYEGSPTPVTAFMGTAPKVAAIAMMLRTLVTPFHGVLVQWQHVVALISVVSMVWGALAAIGQTSIKRLMAYSSIGHMGYALVGLAAGSQAGIRGL... | 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 ... |
A1WXV4 | MSFETPDFSLALPEIWLLAATCGVLVVDLFSSDPRRSATFYLTQGALLVTAVLALSTQWGVNEVTFSGHYMADSLGAVVKASVALLSVLALAYTRPYLGDRGLLQGEFYLLALFANLGMLVIASGGSLLSLYLGLELLSLALYALVAYHRDSRQAAEAAMKYFVLGSLASGILLYGMSMVYGATASLELSVIAEVAGRHSDPLMLLFGVVFMLVGVAFKLGAAPFHAWVPDVYQGAPTPVTLFLSTAPKVAAVALFMRLLVDGLGPMHEQLEPMLMILAVASLLVGNLIAIVQTNFKRMLAYSAIAHAGFIMVGFTAGTD... | 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 ... |
Q17Z65 | MLIDSLHISFDSFNFESILPMLVLVCGGIFTLLINAFTSRFSRNLNMFLCMLFLVLDFLVVLGLEQQENAFFGFLSLDTLSLVSQSIVLISAFLLIFLALSKERFNEFQTAEFYPLYLFIIAGFQFMVSSNHLLLMLIGLETASLPICVLMALSGKRYGLEAGIKYFTMGAMASAFFAMGAMAFYLLTGSLNLEVITLYLYTEGVTNPMLFAMGVIFLIGAIGFKVSLVPFHTWMPDVYEGNNPVFASYISIVPKIAGFVVATRLFGAFIDTRIAWVEDIFYALILITITIPNLIALWQEDVKRMLAYSSISHSGFALAC... | 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 ... |
Q7VFT5 | MPESMSFSLNQLNLQLLIPMCISLFGGIILLGVGVFNKTKSRDLYITISMLFVVLNLGFLFLEGNPIRQFGFFNLLLVDGISLLTQIIMLLATFVLLLFFMNQNNLPETQGAEFYALLLFSIAGFAFMASSQNLILILLGLETASLCLYALIALHNQKSAFEASIKYFIMGALATTFYAFGAMLLYAATGSVDIISIATFLHQQSYQPSILVFAGFVFLLCALGFKVTLVPFHSWGPDVYEGSNALLAAFIAIVPKIVTFAVIIRIFSVFIDSHSAFVEYTLYVIVVLTMTIPNLIALTQKDVKRMLAYSSISHSGFVLA... | 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 ... |
B0TH87 | MNFSLLTTEMLTALLGIGLLAIGLLNRKKDSHRGVAYAAVFGLLGILVVTFFQYGINTNTFHQLWILDDYSVFMKEIFLVAAILVILSAIDYVDGLPRFKTEFYALLVFATLGMMVMASANDLVTLYVGMELMTITFFILVAYILGDGRSSEAGVKYLLLGGASSAVLLYGLSLLYGLTGTTVIPDLLARLTWSPALAIAVVTIIAGFGFKISAVPFHMWSPDIYEGAPTPVTGFLAAASKAAGFAVLVRLFLEGMPLQGGADWLTVIAVLAGVTMVIGNVVAIPQTNIKRMLAYSSVAQAGYLLVGLMSTDAPGVKGIL... | 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... |
C6XJX0 | MDILNDISIAAPEALLIGVALIGVLLGATFKQSFNGLSRLLGALALAGAAFLAASQSAVDASTAFNGLYKVTPFIAIAKAVSYGVGAIALLVAGGYLHRENMNKFEYTLLVMFGSAGMGVMLSANNLMTLYMGIETLSLSSYVLAAFNRDSRRSAEAGLKYFVLGALASGLLLFGCSLVYGYTGFASFEQIAAADQSIGLTFGLVLILMALSFKASAAPFHVWTPDVYEGAPTPVVTFFSTAPKLATVAVLANIMFTVFGVYEESWMLIIAIVSAISMLVGAFGGLAQNNIKRLLAYSSIANVGYALMGVAAGEVNGAAS... | 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 ... |
Q5WT33 | MMTLLENIHVAIPEMIILITACLALLSDLFFRHKLKSIAFYISCVGIIVSAAVSFVFIGSYKLLIFNKLFISDDISHLMKLFIDITVLLSFVYSQNYLDERQMPTGDYYVLGLFSTLGMMILVSAHSLLTLYLGLELMSLPLYAMTAIRRTDSDASEAAMKYFVMGAIASGMLLYGISLVYGATGKLDLLDVANAVAVNWQQQNTLFAFAMVFILAGVGFKLAAVPFHMWAPDVYQGAPSSVTLFISTAPKIAALGMALRFLTIGLVDITMQWQQIILVMALLSTGIGNLLAVIQTRIKRLLAYSAISHIGYALFGVLAA... | 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 ... |
B0SFU5 | MSYTPSSNDLIAISPMLILCGVALLSLVVQFLIPEEDEGKPLWVLSILGILVAMYALYHTTNSPGYGKFFGSQISISPLTVWLSAIYLIAGLITLLVAPPFLSQHKTLFPEFFPLMLFCLSGMMFLTSGYDLIVIFVGLEILSLSLYVMIGMARTSVSALESAMKYFLLGTFSSGFMLLGIAFLYGGSGTTNLDGALRGLSLKGYEANFSKLGLGLFFVGVSFKAALVPFHSWTPDVYEGAQTPITGFMASAGKASALGLVIILFNHIPMGEMGNVWKYLMGTIALISMTWGNIVALKQDNLKRMLAYSSISHAGYIVAG... | 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 ... |
Q8F7R0 | MNLFDLSILPFLNLAQVVNESRVPNVPDLLSVLPALVLATGGVFLICLSVLFKTKEFIIVRYVSGLILLLAFAAVFYTSFRFPGNGFHFSGQIENSVLSFWLNLIYISMAIGTAAIVPRILKNHKIEFPEFYPLLLFATCGMTLMTTGQDFILVFVALELMSICLYILIGMARSDLFSLEATLKYFLLGSFSSGFMLMGIAFLFGGSGSTNITEALKPLTIAGYQGNFAKIGLVLFITGVAFKIALFPYHAWTPDAYEGALTPVTGYMSTAAKAASIGLLLILYTKLPLPLENSTWAWLPGILALCSMIYGNLLALKQEN... | 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 ... |
A0LDR4 | MAIQMPDINLALMLPEIVISVVAMGLLLASAWWEGAEGARRIRRIAAGALMVAMVITLLGVGATQSSTFGGMFVNDRFAAFMKVMLYLSTLLPMVVSWVYLEKSKLGNGEYFVLTLFAMLGGMFMISSGSFLVLYLGIELLSLAIYVLAAYKRDDLASNEAGLKYFVLGSMASGILLYGISLIYGVTGSVDFATINAYLQQDHHSMLGITMGLILVVSGLSFKIAAAPFHMWAPDVYEGAPTSVTAFMAAMPKIAAFAALFRVLVEAFGPMHATWGPIMALLAVVSMGVGALAGLGQSNIKRLLAYSSIGHVGYALIGLA... | 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 ... |
Q6P0U9 | MPVCNFFLQGRCRYGDTCWNEHPTGGRGGDYRGNQQPSNRGGFGNRVWINPSQRGGGGSSSAGGSNEWGRGAASARDVQSSEFSFSQNRFSALETQRAGAEDTHTTLDTIQKEMEVWQTSGQWPFSCYSAVNRQISGFIELCPEELRLEYYTSRASGDIQPYINSVQQLANQWRSRVQELRNMSSSTQISVIAELKSSSPPASAPGFGSPGPGFGSATSGFGNTSLSSPPAGFGGAGFGSGPQSSSTFSFAQSKTDFGASNTQQASGFGSSAFAQPSSGFGNPAPSAASFSFAAADSESKPSAGGFGSASGFSFKTATAG... | 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): 42580
Sequence Length: 414
Domain: The FG repeats are interaction sites for karyopherins (importins, exportins) and form probably an affinity gradie... |
O15504 | MAICQFFLQGRCRFGDRCWNEHPGARGAGGGRQQPQQQPSGNNRRGWNTTSQRYSNVIQPSSFSKSTPWGGSRDQEKPYFSSFDSGASTNRKEGFGLSENPFASLSPDEQKDEKKLLEGIVKDMEVWESSGQWMFSVYSPVKKKPNISGFTDISPEELRLEYHNFLTSNNLQSYLNSVQRLINQWRNRVNELKSLNISTKVALLSDVKDGVNQAAPAFGFGSSQAATFMSPGFPVNNSSSDNAQNFSFKTNSGFAAASSGSPAGFGSSPAFGAAASTSSGISTSAPAFGFGKPEVTSAASFSFKSPAASSFGSPGFSGLP... | Function: Required for the export of mRNAs containing poly(A) tails from the nucleus into the cytoplasm.
PTM: O-glycosylated.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 44872
Sequence Length: 423
Domain: The FG repeats are interaction sites for karyopherins (importins, exportins) and form probab... |
Q8CIC2 | MTICQFFLQGRCRFGDRCWNEHPGARGAGGARQPPPQQQPPSGNNRRGWNASSQRYSNVIQPSSFPKSTPWGGSRDQDKPPFGSFDSGASTSRGFGSSQNPFASPLSDEQKDEKKLLEGIVKDVEVWESSGQWMFSVYSPVRKKPNISGFTDISPEELRLEYHNFLTSNNLQSYLNSVQQLVSQWRNRINELKNLTMSTKGALLSDVKDGVSQAVPAFGFGSKQAGSFGSPGFPVNNSSSSTVQNFSFKTSPGLATPPSGSTSVFGSHPAFGAGPSAGSSISSSTPAFGLGKPEATSAASFSFKSPEASSFASPGFSGFP... | Function: Required for the export of mRNAs containing poly(A) tails from the nucleus into the cytoplasm.
PTM: O-glycosylated.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 44337
Sequence Length: 420
Domain: The FG repeats are interaction sites for karyopherins (importins, exportins) and form probab... |
Q5XGN1 | MAICNFFLQGRCRYGEKCWNEHPRGGGGGGGNRYQSQNRYQEQSRYQEQSRYPEQSRYPEQNRYQEPAGNAKGTWGASSQRYVQPSNFSKSTTWINRDSEKPSAGSFSGFGSRNVKSTAATGLPSTQNRFAALSSQDNSRDGQTDKGNILDDIMKDMEIWESSGQWMFSVYSMLKEKKNISGFTDFSPEELRLEYSVCQAEGNPLKYINAVQQLGSKWKQRILELKNPNPSIKTALLNELNSPSPDVTPGYSGQQNSAFGALSFPTSNTAPTAVTFSFKADTTTAAKPAVPNALAGSDFSAFGNKPTSAPSFGSGVAAAA... | 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): 51705
Sequence Length: 491
Domain: The FG repeats are interaction sites for karyopherins (importins, exportins) and form probably an affinity gradie... |
P49686 | MSAFGNPFTSGAKPNLSNTSGINPFTNNAASTNNMGGSAFGRPSFGTANTMTGGTTTSAFGMPQFGTNTGNTGNTSISAFGNTSNAAKPSAFGAPAFGSSAPINVNPPSTTSAFGAPSFGSTGFGAMAATSNPFGKSPGSMGSAFGQPAFGANKTAIPSSSVSNSNNSAFGAASNTPLTTTSPFGSLQQNASQNASSTSSAFGKPTFGAATNTQSPFGTIQNTSTSSGTGVSPFGTFGTNSNNKSPFSNLQSGAGAGSSPFGTTTSKANNNNNVGSSAFGTTNNQSPFSGGSGGTFGSASNLNKNTNGNFQSSFGNKGFS... | 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 ... |
Q09793 | MFGLNKTPSFGSTGTQNQNTGTSAGTGLFSSNTFGNNTQANTPASTGFGGVTGGAFGQTKPQTGGSLFGNKPNATSTTPGLNLFGQNPQAAPGGSLFGASTTKPQAPGGLFNQNQTQAQPAQAAPTGGLFGLSGQNQTQSQTQPAQANTSLFGQSNIGTTGGLFDQNRPNTSTFGQFSTQPASAGLFGQSTQPSGSTGFGLSNNTQTTPFFSAAQQQPSTTQLPSNPAINATTRYSSLNANTQKFLDDLDKEIFSQIQLAEELQTKLGTVSELVESVPNDVAEVQRRLSSVSTALLIDSDEIETTKRVVDEDTSNARISS... | 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 ... |
G0S4X2 | MSLFGTNTTSQTPAGGGLFGTTTSQSAQTGSLFGTATSQPQQTGGLFGSTATQTPSSQLQSTGLFGSTTATSQPQQTGGLFGSTTTTTSQPQQTGGLFGATATSQPQSTGGLFGNTTTTSQPAQTVGLFGTTTQPQPAQSGGLFGSATQQKPATGGLFGSTTTNTGAGLFGNTSNTIGGGGLFGQTAKPATGGLFGQSTTQPQQQQNATPGLTMGQSTNTQQQVVPGVRIDLSNIKSTTRFNDLTEALQQEIAKIDEEIQKCIRDKEAVDAFLPAHGEQLAAIPTDVNFVTRKSEGAHNALSSDILAIDQLRELVKQDAD... | 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 ... |
Q02199 | MFGLNKASSTPAGGLFGQASGASTGNANTGFSFGGTQTGQNTGPSTGGLFGAKPAGSTGGLGASFGQQQQQSQTNAFGGSATTGGGLFGNKPNNTANTGGGLFGANSNSNSGSLFGSNNAQTSRGLFGNNNTNNINNSSSGMNNASAGLFGSKPAGGTSLFGNTSTSSAPAQNQGMFGAKPAGTSLFGNNAGNTTTGGGLFGSKPTGATSLFGSSNNNNNNNNSNNIMSASGGLFGNQQQQLQQQPQMQCALQNLSQLPITPMTRISELPPQIRQEIEQLDQYIQKQVQISHHLKADTIDHDELIDSIPRDVAYLLKSES... | 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 ... |
Q7K6X4 | MNSLIPPPTSEQQMNMFRLRDKMSLLNAEFLKVINGYFTEKNHYDFSGTMKSYMDHVAQLKQIYKVDDDVAADMTVPRRTENSSESSGETVAPRKIAKAVRKNGTPKNPLNSTVFAASSPAATVASVPKFGDISVITKETPAPLAKTAEPLVAPAAPATARKRAIRGGGPLGGAESVVFKSGEDGQAATSSVKIPATTIKFPEPTKDFWTKKSDAPAAPSNSGSLFAFLGKDGDKPKETPKFSGFSFGKKPAEPSEEPKAADSTPKLTFGSPKEADLPKPASSLFGASPSKPLVFGGSSADSTTSAPKPFSALSTAASLF... | Function: Component of the nuclear pore complex . Plays a direct role in nuclear protein import (By similarity). Required for anoxia-induced prophase arrest; may function in concert with cdk-1 to arrest prophase blastomeres in response to anoxia .
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 52236... |
Q7K0D8 | MAGKRQATSNLNHENWDLEEEPEERGTFRTATEEELKTRVIKKARRKIAGGSSAAEEDGAEEKTAEPKSVFSGFSGFGKPAASPAAGSPFSFLANVTAPATTSSSEPKKSAFSFGFSSSSSSADRPVSTSICGTASTSSTAPSPLPAKESTSTVDGAKPTTSIFGNISAAKKESSEAKTSSSSTSLTSTMETSEYRESVADLNRSVIKFLQDQMGKSPYCILTPVFKNYDEHLKDLQDEESARTNSTKSKTAQARSQEPVAKVSRASSPPKAATTFTFGKPSAPIGASVSPLAKKPNCTITSGGTTTTTATPLVSFGSTA... | Function: Component of the nuclear pore complex that has a direct role in nuclear protein import (By similarity). Actively displaces NLSs from importin-alpha, and facilitates disassembly of the importin-alpha:beta-cargo complex and importin recycling (By similarity). Binds to transcriptionally active chromatin sites wh... |
Q9UKX7 | MAKRNAEKELTDRNWDQEDEAEEVGTFSMASEEVLKNRAIKKAKRRNVGFESDTGGAFKGFKGLVVPSGGGRFSGFGSGAGGKPLEGLSNGNNITSAPPFASAKAAADPKVAFGSLAANGPTTLVDKVSNPKTNGDSQQPSSSGLASSKACVGNAYHKQLAALNCSVRDWIVKHVNTNPLCDLTPIFKDYEKYLANIEQQHGNSGRNSESESNKVAAETQSPSLFGSTKLQQESTFLFHGNKTEDTPDKKMEVASEKKTDPSSLGATSASFNFGKKVDSSVLGSLSSVPLTGFSFSPGNSSLFGKDTTQSKPVSSPFPTK... | Function: Component of the nuclear pore complex that has a direct role in nuclear protein import . Actively displaces NLSs from importin-alpha, and facilitates disassembly of the importin-alpha:beta-cargo complex and importin recycling . Interacts with regulatory proteins of cell cycle progression including CDKN1B (By ... |
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