ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
I3R635 | MGLVKMTRWRTLVLATAAFNLSFLIWFSFAPFTGQIAAEFGLSLTDLGILASAAIWSAPPGRILTGWLSDRFGASTVFGIVLAYVGIFSMASAFATSYEVFFVERVVVASAGITFVVGIQHVSQWFPEEELGTAEGIYAGIGNAGAAGGALILPRAFGNWSGPLFSTGWRAAFFYTGVVAILMAIVYVVFGQDAATKARAAATSESATLSTWVHTATRYGVVALALGYVMSFGLEISMNGWLPTYFREGFGSNLVIASTFAATFSLAAGLLRPIGGYVSDRLVRDQRDILPFFAGRYREQWTVLCMTFIVVSMTGLTFAG... | Function: Is likely responsible for nitrate uptake in the nitrate assimilation pathway.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 46239
Sequence Length: 437
Subcellular Location: Cell membrane
|
P42434 | MTERLLRYFRDKQQDVQSEKTYDTQCPFCSMQCKMQLVEQTIVTRKKYTAIGIDNPTTQGRLCIKGMNAHQHALNSSRITRPLLKKNGEFMPVSWEEALNHIKDQVTMIQTEHGHDAMAVYGSASITNEEAYLLGKFARVGLQTKYIDYNGRLCMSAAATAANQTFGADRGLTNPLSDIPHTRVIILAGTNIAECQPTIMPYFEKAKENGAYFIAIDPRETATTKIADLHLKIKPGTDAALANGLVKIIIDEQLINEDFIQSRTNGFEELKQHTDSLDLNDIAEQTSVSLVDIRKAAVKFAKETSGMLFTARGIEQQTDG... | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: Nitrate reductase is a key enzyme involved in the first step of nitrate assimilation in plants, fungi and bacteria.
Sequence Mass (Da): 78622
Sequence Length: 710
Pathway: Nitrogen metabolism; nitrate reduction (denitrification); dinitrogen from nitrate: step 1/4.
EC: 1.7.-... |
I3R636 | MAEQSSRNLDTGRAGIILAGGRSRRFDGIDKATAPVGGRPMIHRVAASLDPAVDELVINCRADQRDTFAAALSDFDVRFAEDSHPDHGPVFGLRTAVRASNAEYAAILPCDMPLVPTGFISHLFGRVQGGTGVIPSVSETPVPLPSVVHCRAGEVACTETIRAGSDRLKDVMSTLGVNVLDGREVQAHAGLDAFSNVNTIDDLRALSSRR | Function: Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor.
Catalytic Activity: GTP + H(+) + Mo-molybdopterin = diphosphate + Mo-molybdopterin guanine dinucleotide
Sequence Mass (Da): 22257
Sequence Length... |
P42435 | MGKKQLVLVGNGMAGVRAIEEILSVAKDEFQITIFGAEPHPNYNRILLSKVLQGDTDIKDITLNDWDWYEENNIQLYTNETVIKVDTENKTVITDADRIQPYDELILATGSVPFILPIPGADKKGVTAFRDIKDTDTMLAASKQYKKAAVIGGGLLGLEAARGLLNLGMDVSVIHLAPFLMERQLDATAGRLLQNELEKQGMTFLLEKQTEEIVGDDRVEGLRFKDGTSIEADLVVMAVGIRPNTTLGAESGIPVNRGIIVNDYMQTEIPHIYAVGECAEHRGIAYGLVAPLYEQAKVLAKHMCGIETKPYEGSVLSTQL... | Cofactor: Binds 1 siroheme per subunit.
Function: Required for nitrite assimilation.
Catalytic Activity: 2 H2O + 3 NADP(+) + NH4(+) = 5 H(+) + 3 NADPH + nitrite
Sequence Mass (Da): 88432
Sequence Length: 805
Pathway: Nitrogen metabolism; nitrate reduction (assimilation).
EC: 1.7.1.4
|
I3R637 | MASKKEQWKSDLYGDAVRDELEAFAEEGFESIPEDERDKWFTRFKFWGVFQQRTGQESYFMMRLTNANGVLEPGQLRTIAEVARDYATGPVDNPEFGNGWVDLTTRQSIQLHWLELEDIPEIWEQLESVGVTSRSAGGDTMRNITGCPVAGKDTHELVESKPLLDRFQSELREDDALSNMPRKFNISVTGCREGCAQDSINDIGLEPARKEVDGEVITGFNVRVGGGLGSRKPRVARSLDVFVADEERAYEVVRGFVELYHDHGNRDVRARARSRFFVDDWGTEKIRDRLESEYLDFELQSAGEDIRDEYTYNAGRPQSA... | Cofactor: Binds 1 siroheme per subunit.
Function: Catalyzes the reduction of nitrite to ammonium in the nitrate assimilation pathway, using ferredoxin as the electron donor. Can use reduced methyl viologen but neither NADPH nor NADH as electron donors.
Catalytic Activity: 2 H2O + NH4(+) + 6 oxidized [2Fe-2S]-[ferredoxi... |
P39459 | MKPLIQVQGVSQRFSTASGEFLALQNVSFDIYEGETISLIGHSGCGKSTLLNLIAGIALPTEGGLLCDNREIAGPGPERAVVFQNHSLLPWLTCFDNVALAVDQVFRRSMSKGERKEWIEHNLERVQMGHALHKRPGEISGGMKQRVGIARALAMKPKVLLLDEPFGALDALTRAHLQDAVMQIQQSLNTTIVMITHDVDEAVLLSDRVLMMTNGPAATVGEILDVNLPRPRNRVQLADDSRYHHLRQQILHFLYEKQPKAA | Function: Probably part of a high-affinity binding-protein-dependent transport system for nitrate. Probably responsible for energy coupling to the transport system.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 28996
Sequence Length: 262
Subcellular Location: Cell membrane
|
P42436 | MVNKDVTKVCIGKIEELPEQLGKTVYIEDKELAVFKLSDGSIRAIENRCPHKGGVLAEGIVSGQYVFCPMHDWKISLEDGIVQEPDHGCVKTYETLIEGEHVYLVY | Cofactor: Binds 1 [2Fe-2S] cluster.
Function: Required for nitrite assimilation. Required for activity of the reductase (By similarity).
Catalytic Activity: 2 H2O + 3 NADP(+) + NH4(+) = 5 H(+) + 3 NADPH + nitrite
Sequence Mass (Da): 11895
Sequence Length: 106
Subcellular Location: Cytoplasm
EC: 1.7.1.4
|
A0A0H3JXA8 | MNNFNNEIKLILQQYLEKFEAHYERVLQDDQYIEALETLMDDYSEFILNPIYEQQFNAWRDVEEKAQLIKSLQYITAQCVKQVEVIRARRLLDGQASTTGYFDNIEHCIDEEFGQCSITSNDKLLLVGSGAYPMTLIQVAKETGASVIGIDIDPQAVDLGRRIVNVLAPNEDITITDQKVSELKDIKDVTHIIFSSTIPLKYSILEELYDLTNENVVVAMRFGDGIKAIFNYPSQETAEDKWQCVNKHMRPQQIFDIALYKKAAIKVGITDV | Function: Catalyzes the nucleophilic attack of one alpha-aminobutanoate moiety from SAM onto D-histidine to produce the intermediate (2S)-2-amino-4-{[(1R)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino}butanoate. Functions in the biosynthesis of the metallophore staphylopine, which is involved in the acquisition of nickel, ... |
A0A0H2ZHV3 | MQGRTPLLETLRELECEIRLLTVYARECCGCYEILRRKLDRLSGLIGEDCSRAQWQADSDDPALQALGLRLRDAAVQALCELEKHLCQGVLHEPGEMGRYLGSLLESIRGELDSAGIDADARVLFVGSGALPTSALVLAREVGAHLCCLDIDEEALGYAREIARCQGLEARMQFSSLPPAELAFSRDATHFLIASLVQQKSAVLAQIRQVMRADAKVLLRHGSGIKGLFNYPVEPAELEGWQVCAERVSQPLYDTLILEKAGR | Function: Catalyzes the nucleophilic attack of one alpha-aminobutanoate moiety from SAM onto L-histidine to produce the intermediate (2S)-2-amino-4-{[(1S)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino}butanoate. Functions in the biosynthesis of the metallophore pseudopaline, which is involved in the acquisition of nickel a... |
Q8D035 | MYTLMKADVLAQLAGLQQEISQLHDNAQQNQSHFVLLERRFSRLQSFNDEPQLQDYRLQLEHDDAVVKQIAQLRQVANAALCDYEKHQVCALCSPSSKTDDYLTSFNQSLQQEIKLAGMQMGEKVLLVGSGALPTTALVLVAKLGATVFCYDHDPAAQQLARQLVQSLGLEKQVQFIDNLKELTDRPVDHIIVASLVADKQALLAQLVPYVTRSSKLVMRYGNGLKSIFNCPYCHEVNCSHWRTASKPVTTGLYDLIILEPNHHA | Function: Catalyzes the nucleophilic attack of one alpha-aminobutanoate moiety from SAM onto L-histidine to produce the intermediate (2S)-2-amino-4-{[(1S)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino}butanoate. Functions in the biosynthesis of the metallophore yersinopine, which is involved in metal acquisition and thus e... |
Q9DE07 | MWKLVPAAGPGEPFRLLVGTEYVVGRKNCAFLIQDDQSISRSHAVLTVSRPETTHSQSVSVPVLTIKDTSKYGTFVNGSKLSGASRSLQSGDRVNFGVFESKFRVEYESLVVCSSCLDVAQKTALNEAIQQLGGLVVNEWTKECTHLIMESVKVTVKTICALICGRPIVKPEFFSELMKAVQSRQQLPTPESFYPSVDEPAIGIDNMDLSGHPERKKIFSGKTFVFLTAKQHKKLGPAVILGGGEAKLMAEERKETSLLVSPEVCVVDVGVTNSQILGSESMRNWTDSILAVLESNNLRAIPEAEIGLAVIFMSTEIYCN... | Function: Component of the MRE11-RAD50-NBN (MRN complex) which plays a critical role in the cellular response to DNA damage and the maintenance of chromosome integrity . The complex is involved in double-strand break (DSB) repair, DNA recombination, maintenance of telomere integrity, cell cycle checkpoint control and m... |
Q5I2W8 | MWKLQPTESGGESVILLAGQEYVVGRKNCEILLTNDQSISRVHAVLTVTEQAVTLKDSSKYGTFVNGEKLESGSTKTLQTGYKITFGVFQSKFSLEKECIVVCSSCVDNEGKVTLSQDIRSVGGRLVSSWTSDCTHLVMPTVKVTIKTICALLCCRPIVKPAFFSALSKAVQQKLPLPKAERFRPQIDEPSLARDDVDLSARPERKSLFKGKTFLFLSSKQMKRLSVAVSCGGGVSQLLDEGALPVSLLESSSTCVLDMISGNSQPVISPASKKWLDSVGQILHRKGLRFITESEVGLAAIHVSNQTYCNPCSSLQSESV... | Function: Component of the MRE11-RAD50-NBN (MRN complex) which plays a critical role in the cellular response to DNA damage and the maintenance of chromosome integrity. The complex is involved in double-strand break (DSB) repair, DNA recombination, maintenance of telomere integrity, cell cycle checkpoint control and me... |
O60934 | MWKLLPAAGPAGGEPYRLLTGVEYVVGRKNCAILIENDQSISRNHAVLTANFSVTNLSQTDEIPVLTLKDNSKYGTFVNEEKMQNGFSRTLKSGDGITFGVFGSKFRIEYEPLVACSSCLDVSGKTALNQAILQLGGFTVNNWTEECTHLVMVSVKVTIKTICALICGRPIVKPEYFTEFLKAVESKKQPPQIESFYPPLDEPSIGSKNVDLSGRQERKQIFKGKTFIFLNAKQHKKLSSAVVFGGGEARLITEENEEEHNFFLAPGTCVVDTGITNSQTLIPDCQKKWIQSIMDMLQRQGLRPIPEAEIGLAVIFMTTK... | Function: Component of the MRE11-RAD50-NBN (MRN complex) which plays a critical role in the cellular response to DNA damage and the maintenance of chromosome integrity. The complex is involved in double-strand break (DSB) repair, DNA recombination, maintenance of telomere integrity, cell cycle checkpoint control and me... |
Q93NF6 | MGDTDLPCVTGVLLAAGAGKRLGRGPKALLPYRGRTLVEDAAETMLVGGCHEVVIVLGANAQAVCARANLEPYRIVVNHDWSSGMGSSYLAGDAAAHTKNHILVALVDQPGLSVTTVGRLLVSHRPGRISSAAYSSLDSPRVLRRGHPMVIDAGLRPAVASTVSGDAGARVFLRQKPWLVDLIDCSDESTGEDVDTVEQMYRLL | Function: Catalyzes the reduction of nicotine blue to its hydroquinone form. Nicotine blue is the name given to the compound formed by the autocatalytic condensation of two molecules of 2,3,6-trihydroxypyridine, an intermediate in the nicotine degradation pathway. May play a role in preventing the intracellular formati... |
P03416 | MSFVPGQENAGGRSSSVNRAGNGILKKTTWADQTERGPNNQNRGRRNQPKQTATTQPNSGSVVPHYSWFSGITQFQKGKEFQFAEGQGVPIANGIPASEQKGYWYRHNRRSFKTPDGQQKQLLPRWYFYYLGTGPHAGASYGDSIEGVFWVANSQADTNTRSDIVERDPSSHEAIPTRFAPGTVLPQGFYVEGSGRSAPASRSGSRSQSRGPNNRARSSSNQRQPASTVKPDMAEEIAALVLAKLGKDAGQPKQVTKQSAKEVRQKILNKPRQKRTPNKQCPVQQCFGKRGPNQNFGGSEMLKLGTSDPQFPILAELAPT... | Function: Packages the positive strand viral genome RNA into a helical ribonucleocapsid (RNP) and plays a fundamental role during virion assembly through its interactions with the viral genome and membrane protein M. Plays an important role in enhancing the efficiency of subgenomic viral RNA transcription as well as vi... |
P04134 | MANQGQRVSWGDESTKTRGRSNSRGRKNNNIPLSFFNPITLQQGSKFWNLCPRDFVPKGIGNRDQQIGYWNRQTRYRMVKGQRKELPERWFFYYLGTGPHADAKFKDKLDGVVWVAKDGAMNKPTTLGSRGANNESKALKFDGKVPGEFQLEVNQSRDNSRSRSQSRSRSRNRSQSRGRQQFNNKKDDSVEQAVLAALKKLGVDTEKQQQRSRSKSKERSNSKTRDTTPKNENKHTWKRTAGKGDVTRFYGARSSSANFGDTDLVANGSSAKHYPQLAECVPSVSSILFGSYWTSKEDGDQIEVTFTHKYHLPKDDPKTG... | Function: Packages the positive strand viral genome RNA into a helical ribonucleocapsid (RNP) and plays a fundamental role during virion assembly through its interactions with the viral genome and membrane protein M. Plays an important role in enhancing the efficiency of subgenomic viral RNA transcription as well as vi... |
P04665 | MSNMDIDSINTGTIDKTPEELTPGTSGATRPIIKPATLAPPSNKRTRNPSPERTTTSSETDIGRKIQKKQTPTEIKKSVYKMVVKLGEFYNQMMVKAGLNDDMERNLIQNAQAVERILLAATDDKKTEYQKKRNARDVKEGKEEIDHNKTGGTFYKMVRDDKTIYFSPIKITFLKEEVKTMYKTTMGSDGFSGLNHIMIGHSQMNDVCFQRSKGLKRVGLDPSLISTFAGSTLPRRSGTTGVAIKGGGTLVDEAIRFIGRAMADRGLLRDIKAKTAYEKILLNLKNKCSAPQQKALVDQVIGSRNPGIADIEDLTLLARS... | Function: Encapsidates the negative strand viral RNA, protecting it from nucleases. The encapsidated genomic RNA is termed the ribonucleoprotein (RNP) and serves as template for transcription and replication. The RNP needs to be localized in the host nucleus to start an infectious cycle, but is too large to diffuse thr... |
Q6I7C0 | MSDRRQNRKTPDEQRKANALIINENIEAYIAICKEVGLNGDEMLILENGIAIEKAIRICCDGKYQEKREKKAREAQRADSNFNADSIGIRLVKRAGSGTNITYHAVVELTSRSRIVQILKSHWGNELNRAKIAGKRLGFSALFASNLEAIIYQRGRNAARRNGSAELFTLTQGAGIETRYKWIMEKHIGIGVLIADAKGLINGKREGKRGVDANVKLRAGTTGSPLERAMQGIEKKAFPGPLRALARRVVKANYNDAREALNVIAEASLLLKPQITNKMTMPWCMWLAARLTLKDEFANFCAYAGRRAFEVFNIAMEKIG... | Function: Encapsidates the negative strand viral RNA, protecting it from nucleases. The encapsidated genomic RNA is termed the ribonucleoprotein (RNP) and serves as template for transcription and replication. The RNP needs to be localized in the host nucleus to start an infectious cycle, but is too large to diffuse thr... |
B1YBH2 | MKVAVASRNPNKVRAVEEAYRLFGIPARVSSVDKPPSLPPQPVGLEAVVAGAVERAKAALAAAGEAEHGVGIEAGALEAGGRHLDVTVAAVADRGGLVTLGFGPAFQIPDVFLGDVLRGVELGVLAERHFGKAAVGYREGIIGLLTRGRVTRLDLNVVAVAMALVPRLPANAQLYRFWKTAP | Cofactor: Binds 1 divalent metal cation per subunit; can use either Mg(2+) or Mn(2+).
Function: Phosphatase that hydrolyzes non-canonical purine nucleotides such as XTP and ITP to their respective diphosphate derivatives. Probably excludes non-canonical purines from DNA/RNA precursor pool, thus preventing their incorpo... |
Q97WI6 | MVTIALGSKNPVKISATKEALEILRLNWDLIATDIDSGVDKQPFCDQTYVGARNRALNAIKATNADIGLGIEGGVCNVYGKFIANAVVYVITKEGVENFAISSSFTLPSSIVSLILQGKELGEASDIIFKTINSKTKEGAVGLLTNNIIDRKTLYVQPIILALYPIYNTIINNTLF | Cofactor: Binds 1 divalent metal cation per subunit; can use either Mg(2+) or Mn(2+).
Function: Phosphatase that hydrolyzes non-canonical purine nucleotides such as XTP and ITP to their respective diphosphate derivatives. Probably excludes non-canonical purines from DNA/RNA precursor pool, thus preventing their incorpo... |
P39432 | MHQVISATTNPAKIQAILQAFEEIFGEGSCHITPVAVESGVPEQPFGSEETRAGARNRVDNARRLHPQADFWVAIEAGIDDDATFSWVVIDNGVQRGEARSATLPLPAVILDRVRQGEALGPVMSQYTGIDEIGRKEGAIGVFTAGKLTRSSVYYQAVILALSPFHNAVYR | Cofactor: Binds 1 divalent metal cation per subunit; can use either Mg(2+) or Mn(2+).
Function: Phosphatase that hydrolyzes non-canonical purine nucleotides such as XTP and ITP to their respective diphosphate derivatives. Probably excludes non-canonical purines from DNA/RNA precursor pool, thus preventing their incorpo... |
P16603 | MPFGIDNTDFTVLAGLVLAVLLYVKRNSIKELLMSDDGDITAVSSGNRDIAQVVTENNKNYLVLYASQTGTAEDYAKKFSKELVAKFNLNVMCADVENYDFESLNDVPVIVSIFISTYGEGDFPDGAVNFEDFICNAEAGALSNLRYNMFGLGNSTYEFFNGAAKKAEKHLSAAGAIRLGKLGEADDGAGTTDEDYMAWKDSILEVLKDELHLDEQEAKFTSQFQYTVLNEITDSMSLGEPSAHYLPSHQLNRNADGIQLGPFDLSQPYIAPIVKSRELFSSNDRNCIHSEFDLSGSNIKYSTGDHLAVWPSNPLEKVEQ... | Cofactor: Binds 1 FAD per monomer.
Function: This enzyme is required for electron transfer from NADP to cytochrome P450 in microsomes. It can also provide electron transfer to heme oxygenase and cytochrome B5. Involved in ergosterol biosynthesis. Has NADPH-dependent ferrireductase activity on the plasma membrane.
Catal... |
Q8VYY5 | MKMRVETALAILLVLISIQQCYGGVSNYTCTCFSSGNRSDILESNCSTSCNCRPDRDQWVCLCPANGFPVIAIGGSNSSCFTSCNCSAGATKSSKKQYLSRKLVIVILLFCGVLISLAFLASMICYICRKDKFSGQTPSVSSDRESSWHSSANLINRKSSVSQSKISISSSVAGCFFQNASLFCVSKPETIHGAIFQFSYTELEQATNKFSSNSVIGHGGSSCVYRGQLKDGKTAAIKRLNTPKGDDTDTLFSTEVELLSRLHHYHVVPLIGYCSEFHGKHAERLLVFEYMSYGSLRDCLDGELGEKMTWNIRISVALGA... | PTM: Phosphorylated.
Location Topology: Single-pass type I membrane protein
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 62192
Sequence Length: 565
Subcellular Location: Cell membrane
EC: 2.7.11.1
|
Q9LZD0 | MVSNCLSLSLHLNLHPHKHNRHSLSSLRSRTKAKLYQHVSFTDSSHKSSYTSCVSTFDIQRKSSKHYELGKHSFSPILPGDNLVLSRSGVIRPRLSAMTGSEINDHGYDESQFDPSLTNDDLKPTTPSQRTFSWLDMSSLWIGLVVGVPTYYLAGSLVDLGMAWWQGIATVVTANLILLVPLVLTAQPGTLYGISFPVLARSSFGIRGAHIPTLLRALVGCGWYGIETWIGGEAIFLLLPGHIKKSALSHTLPWLGTSPLEFSCFIVFWLAQLCIVWRGMDGIRKLEKYSAPILISLTSCLLAWSYLKAGGFGHMLSLSS... | Function: Nucleobase-proton symporter that facilitates the uptake of nucleobases in the cells. Can transport adenine, guanine and uracil . Contributes to uracil import into plastids for plastidic uracil salvage which is essential for plant growth and development .
Location Topology: Multi-pass membrane protein
Sequence... |
Q2V8Y7 | MGKSNSKLKPEVVEELTRKTYFTEKEVQQWYKGFIKDCPSGQLDAAGFQKIYKQFFPFGDPTKFATFVFNVFDENKDGRIEFSEFIQALSVTSRGTLDEKLRWASKLYDLDNDGYITRNEMLDIVDAIYQMVGNTVELPEEENTPEKRVDRIFAMMDKNADGKLTLQEFQEGTKADPSIVQALSLYDGLV | Function: Neuronal calcium sensor, regulator of G protein-coupled receptor phosphorylation in a calcium dependent manner. Directly regulates GRK1 (RHOK), but not GRK2 to GRK5. Can substitute for calmodulin (By similarity). Stimulates PI4KB kinase activity (By similarity). Involved in long-term synaptic plasticity throu... |
P36608 | MGKGNSKLKSSQIRDLAEQTYFTEKEIKQWYKGFVRDCPNGMLTEAGFQKIYKQFFPQGDPSDFASFVFKVFDENKDGAIEFHEFIRALSITSRGNLDEKLHWAFKLYDLDQDGFITRNEMLSIVDSIYKMVGSSVQLPEEENTPEKRVDRIFRMMDKNNDAQLTLEEFKEGAKADPSIVHALSLYEGLSS | Function: Neuronal calcium sensor, regulator of G protein-coupled receptor phosphorylation in a calcium dependent manner. Can substitute for calmodulin and directly activate PDE, NO synthase, and calcineurin. Regulates associative learning and memory in a calcium dependent manner.
Location Topology: Lipid-anchor
Sequen... |
A2A1A0 | MSKNLTGVGGSLPVENVQVLAGKELKNLPNRYVRPELEHDDVVPIDNSLEIPVIDLSRLLDQQYACDELAKFHSACLDWGFFQLINHGVREEVIEKMKVDTEDFFRLPFKEKNAYRQLPNGMEGYGQAFVTSEEQKLDWADMHFLITKPVQERNMRFWPTSPTSFRETMEKYSMELQKVAMCLTGMMAKNLGLESEILTKPLRTVFNREDELLPSMSSCGEGLGLSPHSDATGLTLLIQVNEVNGLHIKKDEKWVPIKPILGAFVVNIGDVIEIMSNGIYKSIEHRAVINTDKERLSIAAFHDPEYGTKIGPLPDLVKEN... | Cofactor: Binds 1 Fe cation per subunit.
Function: Involved in the biosynthesis of the common precursor of all benzylisoquinoline alkaloids such as morphine, sanguinarine, codeine or berberine. Condenses dopamine and phenylacetaldehyde, 3,4-dihydrophenylacetaldehyde or 4-hydroxyphenylacetaldehyde.
Catalytic Activity: (... |
P62166 | MGKSNSKLKPEVVEELTRKTYFTEKEVQQWYKGFIKDCPSGQLDAAGFQKIYKQFFPFGDPTKFATFVFNVFDENKDGRIEFSEFIQALSVTSRGTLDEKLRWAFKLYDLDNDGYITRNEMLDIVDAIYQMVGNTVELPEEENTPEKRVDRIFAMMDKNADGKLTLQEFQEGSKADPSIVQALSLYDGLV | Function: Neuronal calcium sensor, regulator of G protein-coupled receptor phosphorylation in a calcium dependent manner. Directly regulates GRK1 (RHOK), but not GRK2 to GRK5. Can substitute for calmodulin (By similarity). Stimulates PI4KB kinase activity (By similarity). Involved in long-term synaptic plasticity throu... |
Q4QTJ2 | MSKLITTEPLKSMAEVISNYAMKQQSVSERNIPKKQSLLRKEITYETEVQTSADSIWNVYSSPDIPRLLRDVLLPGVFEKLDVIAGNGGVGTVLDIAFPLGAVPRRYKEKFVKINHEKRLKEVVMIEGGYLDMGCTFYMDRIHIFEKTPNSCVIESSIIYEVKEEYAGKMAKLITTEPLESMAEVISGYVLKKRLQVFGFEIKPKLRFNLLLCLIICLVIAGGMFVAGVPL | Function: Involved in the biosynthesis of (S)-coclaurine, the common precursor of all benzylisoquinoline alkaloids such as morphine, sanguinarine, codeine or papaverine. Condenses dopamine and 4-hydroxyphenylacetaldehyde.
Catalytic Activity: (4-hydroxyphenyl)acetaldehyde + dopamine = (S)-norcoclaurine + H2O
Location To... |
Q09711 | MGKSQSKLSQDQLQDLVRSTRFDKKELQQWYKGFFKDCPSGHLNKSEFQKIYKQFFPFGDPSAFAEYVFNVFDADKNGYIDFKEFICALSVTSRGELNDKLIWAFQLYDLDNNGLISYDEMLRIVDAIYKMVGSMVKLPEDEDTPEKRVNKIFNMMDKNKDGQLTLEEFCEGSKRDPTIVSALSLYDGLV | Function: Negatively regulates sporulation perhaps by controlling Ca(2+)-dependent desensitization of git3.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 22033
Sequence Length: 190
Subcellular Location: Membrane
|
Q9SKT7 | MSFHSFYQRASSLFKAYPSTSKILLLSTFSGGGGVLVYSDSNPLKRILHADATLDSDGNPIRKKKVVVLGSGWSGYSFLSYLNNPNYDVQVVSPRNFFLFTPLLPSVTNGTVEARSIVEPIRGLMRKKGFEYKEAECVKIDASNKKIHCRSKEGSSLKGTTEFDMDYDILILAVGAKPNTFNTPGVEEHAYFLKEAEDALNIRHSVIDCFERASLPNLTEEERKKILHFVVVGGGPTGVEFSAELHDFLVQDVAKIYPKVQEFTKITLLEAGDHILNMFDKRITAFAEEKFQRDGIDLKTGSMVVGVTADEISTKERETG... | Cofactor: Binds 1 FAD per subunit.
Function: Alternative NADH-ubiquinone oxidoreductase which catalyzes the oxidation of mitochondrial NADH does not translocate protons across the inner mitochondrial membrane (By similarity). NAD(P)H dehydrogenase; more efficient on NADH.
Catalytic Activity: a quinone + H(+) + NADH = a... |
Q94C12 | MGRKKGLPEFEESAPDGFDPENPYKDPVAMVEMREHIVREKWIQIEKAKILREKVKWCYRVEGVNHYQKCRHLVQQYLDSTRGVGWGKDHRPISLHGPKPEAVEAE | Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (... |
P73735 | MTDARPRICILGGGFGGLYTALRLGQLSWEGHTPPEIVLVDQRDRFLFAPFLYELVTEEMQTWEIAPPFVELLAESGVIFRQAEVTAIDFDHQKVLLNDQDKGTESLAFDQLVIALGGQTPLPNLPGLKDYGLGFRTLEDAYKLKQKLKSLEQADAEKIRIAIVGGGYSGVELAAKLGDRLGERGRIRIIERGKEILAMSPEFNRQQAQASLSAKGIWVDTETTVTAITATDVTLQFREQEDVIPVDLVLWTVGTTVSPLIRNLALPHNDQGQLRTNAQLQVEGKTNIFALGDGAEGRDASGQLIPTTAQGAFQQTDYCA... | Cofactor: Binds 1 FAD per subunit.
Function: Bifunctional oxidoreductase probably ables to act both on prenyl naphthoquinones and on prenyl benzoquinones . Catalyzes the penultimate step in the biosynthesis of vitamin K1 .
Catalytic Activity: demethylphylloquinone + H(+) + NADPH = demethylphylloquinol + NADP(+)
Sequenc... |
P84189 | MKMMIPVIFSILLLIFSLSSTAMSLEDEQENMEERAEIDFSGIPEDIIKQIKETNAKPPARFDPAAFEKSDD | Function: Agonist of the B2 bradykinin receptor (BDKRB2) . Potentiates the hypotensive effect of bradykinin (BK) and induces a direct vasorelaxing effect independent of BK, by endothelium- and nitric oxide (NO)-dependent mechanisms in rat aortic ring preparations . Also exerts proangiogenic, antiinflammatory, and antif... |
Q9BBN8 | MNVPATRKDLMIVNMGPHHPSMHGVLRLIVTLDGEDVIDCEPILGYLHRGMEKIAENRTIIQYLPYVTRWDYLATMFTEAITVNGPEQLGNIQVPKRASYIRVIMLELSRIASHLLWLGPFMADIGAQTPFFYIFREREFIYDLFEAATGMRMMHNFFRIGGVAADLPHGWIDKCFDFCNYFFTRVVEYQKLITRNPIFLERVEGVGVVGGEEVINWGLSGPMLRASGIQWDLRQVDNYECYEEFDWEVQWQKEGDSLARYLVRIGEMMESIKIIQQALEGIPGGPYENLEIRCFGREKEPEWNDFEYRFIGKKPSPTFE... | 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... |
Q85FL7 | MNTVDKEKFNLKTRGRLSAWLTKHNFSHRPLGYDYRGVEILEVKSEEWLSTAVALYAYGFNYLRSQCAYDATPGGSLVSVYHLTQMQDQSDQPEEICVKVFVSRTNPQIPSVYWVWKSAEFQERESYDMLGIIYQGHPYLRRILMPESWIGWPLRKDYVVPNFYELQDAY | 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... |
P56754 | MQGTLSVWLAKRGLVHRSLGFDYQGIETLQIKPEDWHSIAVILYVYGYNYLRSQCAYDVAPGGLLASVYHLTRIEYGVNQAEEVCIKVFTHRSNPRIPSVFWVWKSTDFQERESYDMLGITYDSHPRLKRILMPESWIGWPLRKDYIAPNFYEIQDAY | 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... |
Q9BBT7 | MNSIEFPLIDRTTQNSVISTTLNDLSNWSRLSSLWPLLYGTSCCFIEFASLIGSRFDFDRYGLVPRSSPRQADLILTAGTVTMKMAPSLVRLYEQMPEPKYVIAMGACTITGGMFSTDSYSTVRGVDKLIPVDVYLPGCPPKPESILDAITKLRKKISREIHEDQTSSLSSQRENRCFTTNHKFYVERSTHTGNYDQVLFHQPPSTSEISSDTFFRYQKVQYPPRNEIVN | Cofactor: Binds 1 [4Fe-4S] cluster.
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... |
P06670 | MSLIEFPLLDQTSSNSVISTTLNDLSNWSRLSSLWPLLYGTSCCFIEFASLIGSRFDFDRYGLVPRSSPRQADLILTAGTVTMKMAPSLVRLYEQMPEPKYVIAMGACTITGGMFSTDSYSTVRGVDKLIPVDVYLPGCPPKPEAVIDALTKLRKKIAREIIEDRTLCQSQKKNRSFTTRHKLYVRRSTHTGTYEQELLYQSPSTLDISSETFFKSKSSVSSYKLVN | Cofactor: Binds 1 [4Fe-4S] cluster.
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... |
Q50KA9 | MANSERTFIAIKPDGVQRSLVGEIIKRFEQKGFRLIAMKLIQASEDLLKEHYIDLKDRPFFAGLVKYMQSGPVVAMVWEGLNVVKTGRVMLGETNPADSKPGTIRGDFCIQVGRNIIHGSDSVESAEKEIGLWFQPEELVDYKSCAQNWIYE | Function: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. Possesses nucleoside-diphosphate kinase, serine/threonine-specific protein kinase, geranyl and fa... |
P15531 | MANCERTFIAIKPDGVQRGLVGEIIKRFEQKGFRLVGLKFMQASEDLLKEHYVDLKDRPFFAGLVKYMHSGPVVAMVWEGLNVVKTGRVMLGETNPADSKPGTIRGDFCIQVGRNIIHGSDSVESAEKEIGLWFHPEELVDYTSCAQNWIYE | Function: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. Possesses nucleoside-diphosphate kinase, serine/threonine-specific protein kinase, geranyl and fa... |
P15532 | MANSERTFIAIKPDGVQRGLVGEIIKRFEQKGFRLVGLKFLQASEDLLKEHYTDLKDRPFFTGLVKYMHSGPVVAMVWEGLNVVKTGRVMLGETNPADSKPGTIRGDFCIQVGRNIIHGSDSVKSAEKEISLWFQPEELVEYKSCAQNWIYE | Function: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. Possesses nucleoside-diphosphate kinase, serine/threonine-specific protein kinase, geranyl and fa... |
Q05982 | MANSERTFIAIKPDGVQRGLVGEIIKRFEQKGFRLVGLKFIQASEDLLKEHYIDLKDRPFFSGLVKYMHSGPVVAMVWEGLNVVKTGRVMLGETNPADSKPGTIRGDFCIQVGRNIIHGSDSVESAEKEISLWFQPEELVDYKSCAQNWIYE | Function: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. Possesses nucleoside-diphosphate kinase, serine/threonine-specific protein kinase, geranyl and fa... |
Q50KA8 | MAHQERTFIAIKPDGVQRGLVGDIVKRFEQKGFRLVAMKFLRASEDLLKEHYIDLKDRPFYPGLVKYMHSGPVVAMVWEGLNVVKTGRMMLGETNPADSKPGTIRGDFCIQVGRNIIHGSDSVKSAEKEISLWFKPEELVDYKSCAFDWIYE | Function: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate (By similarity). Negatively regulates Rho activity by interacting with AKAP13/LBC. Acts as a trans... |
P22392 | MANLERTFIAIKPDGVQRGLVGEIIKRFEQKGFRLVAMKFLRASEEHLKQHYIDLKDRPFFPGLVKYMNSGPVVAMVWEGLNVVKTGRVMLGETNPADSKPGTIRGDFCIQVGRNIIHGSDSVKSAEKEISLWFKPEELVDYKSCAHDWVYE | Function: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate (By similarity). Negatively regulates Rho activity by interacting with AKAP13/LBC . Acts as a tran... |
P85288 | MEQTFVAIKPDGVQRGLCGEVMKFIQPMKHYLDLKDMPFYAGLCKYMSSGPVFAMVWEGEGIVKMMLGETNPADSKPGSIRGDFCINIGRNIIHGSDTVENAKMEVGLWFKPEEFVAYAEKAKAWVYE | Function: Major role in the synthesis of nucleoside triphosphates other than ATP.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'-deoxyribonucleoside 5'-triphosphate + ADP
Sequence Mass (Da): 14393
Sequence Length: 128
Subcellular Location: Cytoplasm
EC: 2.7.4.6
|
Q3YQT1 | MLERTLSILKPDVVKRNITGQVNSYIENSGLKIVTQKMCLLTRFQAEEFYAIHKSQHFFIPLVDFMVSGPIIVQVLEGENAISLYRELMGATDPKKANPGTIRGDFAENIDANCVHGSDSLDNAVREIRFFFSDYELLSLK | Function: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'-deoxyribonucleoside 5'-t... |
B4RCP4 | MTERTFSIIKPDATRRNLTGKVNAVIEDAGLRIVAQKRIRMSRAQAEKFYEVHKERPFFGELVEFMTSAPVVVQVLEGENAVARYREVMGATNPAQAADGTIRKLYAESVGENSVHGSDSLENAKIEIAQFFTEDEIVG | Function: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'-deoxyribonucleoside 5'-t... |
Q6KZI4 | MERCLILVKPDGVERNLIGEVISRFERKGLAIKALKMMRVTREQAEDHYSVHRLKPFFDDLVSYLTSGPIVAMIVEGNNAIASSRMLAGATDGSKAAPGTIRGDFSLDIERNIVHASDSLESYEHEYKIFFNENEIMD | Function: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'-deoxyribonucleoside 5'-t... |
A9B9E7 | MVAERTFLAIKPDGVQRGLVGEILSRFERKGFKLIALKQLIPSRALAEQHYGVHRERPFFKGLVDFITSGPVIAMIWEGEGVILGARKLIGSTKPLDADPGTIRGDLAIDIGRNVIHGSDGPETASFEIGLWFESSELSDWNPSDQLWRVE | Function: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'-deoxyribonucleoside 5'-t... |
Q803Q2 | MDTEMMPKFSSKDEEIDYWKCLSLKYKKSCHDAQEELQEFQEGSRELEAELEAQLGQAEHRIRDLQSENQRLKSEVDILKEKLEQQYAQSYKQISMLEDDLLQTRGIKEQLHKYVRELEQANDDLERAKRATITSLEDFEQRLNQAIERNAFLESELDEKESLLVSVQRLKDEARDLRQELAVRERTSDVTRMSAPSSPTLDIDKTDSAVQASLSLPATPVGKTMEHPFIGTKALTNGCGNGSPLTPSARISALNIVGDLLRKVGALESKLAACRNFAKDQAARKNYTTGNGNLINSNATKFSHSLHTTYFDKTTMNGLD... | Function: Required for organization of the cellular microtubule array and microtubule anchoring at the centrosome. Positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus end (By similarity)... |
Q0QLF2 | MGKDYQVLGKNKVKVDSLEKVMGTAKFAADYSFPDMLYAGVFRSTVPHARIVSLDLSKARAIDGVEAVLDYHAIPGKNRFGIIIKDEPCLVDDKVRRYGDAIAVVAAQTPDLVQEALDAITIEYEELEGIFTMERALEEDSPAIHGDTNIHQVKHLEYGDVDAAFKQCDIVVEDTYSTHRLTHMFIEPDAGVSYYDNEGMLTVVVSTQNPHYDRGEVAGMLALPNSKVRIIQATTGGGFGGKLDLSVQCHCALLTYHTKKPVKMVRSREESTTVSSKRHPMTMHCKTGATKDGRLQAVQVEMFGDTGAYASYGPAVITRA... | Cofactor: Binds 1 Se-Mo-molybdopterin cytosine dinucleotide (Se-Mo-MCD) cofactor per heterotetramer. The cofactor is bound between the NdhL and NdhM subunits.
Function: Catalyzes the hydroxylation of nicotinate to 6-hydroxynicotinate. Also active against 2-pyrazinecarboxylic acid, but inactive against other nicotinate ... |
H9N289 | MEQAIINDEREYLRHFWHPVCTVTELEKAHPSSLGPLAVKLLNEQLVVAKLGDEYVAMRDRCAHRSAKLSLGTVSGNRLQCPYHGWQYDTHGACQLVPACPNSPIPNKAKVDRFDCEERYGLIWIRLDSSFDCTEIPYFSAANDPRLRIVIQEPYWWDATAERRWENFTDFSHFAFIHPGTLFDPNNAEPPIVPMDRFNGQFRFVYDTPEDMAVPNQAPIGSFSYTCSMPFAINLEVSKYSSSSLHVLFNVSCPVDSHTTKNFLIFAREQSDDSDYLHIAFNDLVFAEDKPVIESQWPKDAPADEVSVVADKVSIQYRKW... | Cofactor: Binds 1 [2Fe-2S] cluster per subunit.
Function: Involved in the caffeine degradation, which is the essential first step for assimilating the carbon and nitrogen in caffeine. Catalyzes the N1-demethylation of caffeine to produce theobromine and formaldehyde. Also catalyzes the N1-demethylation of theophylline,... |
F0E1K6 | MHAENSFVIDDWYPVGALAETVSGRKYHTRILGTEIWYQLADGTVSAGLADNTAELASKSIYGLLWVSLSDNPRDVIAIPEFAEADRRVVSAGSIRVATSGLRVIENFLDMAHFPFVHTDILGAEPLTEVAAYDVEIDEAADEIRAVNCRFPQPKGSAAASEPVEMQYVYRIARPFIAILYKTCVIDANRLDVLGLFVQPVDQESSIAHTIMCYLDDINTDKQLRDFQQRIFGQDIMILINQVPKALPLNPRHETPVRADALSSAYRRWLNDRNVTFGTTRG | Function: Involved in the caffeine degradation, which is the essential first step for assimilating the carbon and nitrogen in caffeine. Probably catalyzes the N7-demethylation of 7-methylxanthine to produce xanthine and formaldehyde.
Catalytic Activity: 7-methylxanthine + H(+) + NADPH + O2 = formaldehyde + H2O + NADP(+... |
H9N291 | MNKLDVNQWFPIATTEDLPKRHVFHATLLGQEMAIWRDDSGSVNAWENRCPHRGLRLTLGANTGNELRCQYHGWTYESGTGGCTFVPAHRDAPPPNAARVNTFPVREKHGFIWTTLGQPPGEPISILDDAQLVNAVKTNLHSVVIDADIDGVVSVLRQNLSAFIDVFGAASAEDLHLKSMLQDRGILVTRSGSIAIHFYMQRSTISKCVVHAQVLTPGRPGYELQKNYSYAMNVIRRAAEAVATDLISITDISDQTIEKLEVVRENMTKAPPTHYICEVVTRTQETGDINSYWLKPIGYPLPAFSPGMHISITTPEGSIR... | Cofactor: Binds 1 [2Fe-2S] cluster per subunit.
Function: Involved in the caffeine degradation, which is the essential first step for assimilating the carbon and nitrogen in caffeine. Catalyzes the oxidation of NADH and transfers electrons to NdmA and NdmB, which catalyze the N-demethylation reactions.
Sequence Mass (D... |
Q0QLF1 | MKKRGKGVGSMWYGIGNTGLPNPAAAFVEIHGDGSANVMFGAADIGQGSGTAMAQIAAEELGLDYEKIHVTWGDTMVTPDGGATSASRQTLITGNAVILACRQAKETLAKTAAEKLDCAPEELSFRDNTVFITADPERSMTYGELMAAMKAAGRMAVGAGSYNPNTTGLAPENMSGIPFEVYSYATTIAEVEVDTETGEVDVLKVVSAHDVGTPINRSMVEGQIEGGVTMGQGFVLMEEIEVNTKNGAIKNPSMSKYIIPSNRDVPEIHSILVESEGGPGPFGAKGVGEPALIPMIPAVVAAIEDALGTRFTHTPIMPKD... | Cofactor: Binds 1 Se-Mo-molybdopterin cytosine dinucleotide (Se-Mo-MCD) cofactor per heterotetramer. The cofactor is bound between the NdhL and NdhM subunits.
Function: Catalyzes the hydroxylation of nicotinate to 6-hydroxynicotinate. Also active against 2-pyrazinecarboxylic acid, but inactive against other nicotinate ... |
Q9SK66 | MQVVSRRLVQRPLVGGASIYSSSSLRSLYGVSNHLNGTDNCRYSSSLATKGVGHLARKGTGGRSSVSGIVATVFGATGFLGRYLVQQLAKMGSQVLVPFRGSEDSPRHLKLMGDLGQVVPMKFDPRDEDSIKAVMAKANVVINLIGREYETRNFSFEDANHHIAEKLALVAKEHGGIMRYIQVSCLGASVSSPSRMLRAKAAAEEAVLNALPEATIMRPATMIGTEDRILNPWSMFVKKYGFLPLIGGGTTKFQPVYVVDVAAAIVAALKDDGSSMGKTYELGGPDVFTTHELAEIMYDMIREWPRYVKLPFPIAKAMAA... | Cofactor: Binds 1 FAD per subunit.
Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the en... |
Q559Z0 | MLKNLSKGFPSLINKRSFSTINENPLTRIHHGSRTQTTGLVATVFGATGFTGRYLVQLLARTGIQVVVPYRCEDEGFRDLKVLGELGQIIPVRFDIRDSESIERAISHSNIVINMAGRDYETRNFSLDDINVHAASRIADLSKNVEKYIHVSTLRASEDSPSHFSRSKAIGEKLTREIIPNCTVVRPSIIFGDEDKFINKWSKVSQNWPFIPRYNQQHKIQPLHCYDLASGILSILETPGTSGKVYEFAGDEVFTWDEFLDMIIDGTAQYSKLNIPVSNDFMKFISEHLLERFARNPNFIKDQIDYHNQDMTTTVGALTL... | Cofactor: Binds 1 FAD per subunit.
Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the en... |
Q16795 | MAAAAQSRVVRVLSMSRSAITAIATSVCHGPPCRQLHHALMPHGKGGRSSVSGIVATVFGATGFLGRYVVNHLGRMGSQVIIPYRCDKYDIMHLRPMGDLGQLLFLEWDARDKDSIRRVVQHSNVVINLIGRDWETKNFDFEDVFVKIPQAIAQLSKEAGVEKFIHVSHLNANIKSSSRYLRNKAVGEKVVRDAFPEAIIVKPSDIFGREDRFLNSFASMHRFGPIPLGSLGWKTVKQPVYVVDVSKGIVNAVKDPDANGKSFAFVGPSRYLLFHLVKYIFAVAHRLFLPFPLPLFAYRWVARVFEISPFEPWITRDKVE... | Cofactor: Binds 1 FAD per subunit.
Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Required for proper complex I assembly . Complex I functions in the transfer of electrons from NADH to the respiratory chain. T... |
Q9DC69 | MAAAVRFRVVRALPMSRPAITAAATSVFCGSSHRQLHHAVIPHGKGGRSSVSGVVATVFGATGFLGRYVVNHLGRMGSQVIIPYRCDVYDIMHLRLMGDLGQLTFLEWDARDKDSIRKAVQHSNVVINLIGREWETRNFDFEDVFVNIPRAIAQASKEAGVERFIHVSHLNASMKSSSKSLRSKAVGEKEVRSVFPEAIIIRPSDIFGREDRFLNHFANYRWFLAVPLVSLGFKTVKQPVYVADVSKGIVNATKDPDAVGKTFAFTGPNRYLLFHLVKYIFGMTHRTFIPYPLPLFVYSWIGKLFGLSPFEPWTTKDKVE... | Cofactor: Binds 1 FAD per subunit.
Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the en... |
P25284 | MAPLTAAMRSTPRIIVSNAFGFQRRAISDVTITRTGKPIIRNQGGRSSLGGHTATVFGATGQLGRYIVNRLARQGCTVVIPFRDEYNKRHLKVTGDLGKVVMIEFDLRNTQSIEESVRHSDVVYNLIGRDYPTKNFSFEDVHIEGAERIAEAVAKYDVDRFIHVSSYNADPNSECEFFATKARGEQVVRSIFPETTIVRPAPMFGFEDRLLHKLASVKNILTSNGMQEKYNPVHVIDVGQALEQMLWDDNTASETFELYGPKTYTTAEISEMVDREIYKRRRHVNVPKKILKPIAGVLNKALWWPIMSADEIEREFHDQV... | Cofactor: Binds 1 FAD per subunit.
Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the en... |
P80265 | ASNLATGGAGPLIXKGTGGRSS | Cofactor: Binds 1 FAD per subunit.
Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the en... |
P54713 | LQYGPLAXILGE | Cofactor: Binds 1 FAD per subunit.
Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the en... |
P91929 | MTAVFRVGLVRLVSRATQSPNLLQAQTNALPAAFQQRCSISGKTMRGGPRVPKAAPYPYKTKKYSVFNAIFDKTSKRFDENSKVICVEGPIAAGKSKFAKELAEELDMEYYPAVDLDLIYINSYGYDMRKLDPQLPPSCRSYDVRNFCLDPSHDLAAQFQIRMYMLRYSQYIDALQHVLSTGQGVVLERSPYSDFVFMEAMFRQGYLSRGARSVYNELRQNTIGELLKPHLVIYLDLPVDAVKKQIKARNVDYEVQSKVFSDAYLSDLEQLYKQQYLKDISTHAELLIYDWTAGGETEVVVEDIERIDFNQFEADIHNKK... | Cofactor: Binds 1 FAD per subunit.
Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the en... |
O95299 | MALRLLKLAATSASARVVAAGAQRVRGIHSSVQCKLRYGMWHFLLGDKASKRLTERSRVITVDGNICTGKGKLAKEIAEKLGFKHFPEAGIHYPDSTTGDGKPLATDYNGNCSLEKFYDDPRSNDGNSYRLQSWLYSSRLLQYSDALEHLLTTGQGVVLERSIFSDFVFLEAMYNQGFIRKQCVDHYNEVKSVTICDYLPPHLVIYIDVPVPEVQRRIQKKGDPHEMKITSAYLQDIENAYKKTFLPEMSEKCEVLQYSAREAQDSKKVVEDIEYLKFDKGPWLKQDNRTLYHLRLLVQDKFEVLNYTSIPIFLPEVTIG... | Cofactor: Binds 1 FAD per subunit.
Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the en... |
Q9TC96 | MAIEHASSIKKVKNFTLNFGPQHPAAHGVLRLVLELNGEVVARADPHIGLLHRGTEKLIEYKTYTQALPYFDRLDYVSMMCQEHAYSLAVEKLLHCEVPERAQYIRVLFSEITRILNHLLALTTHAMDVGALTPFLWAFEEREKLIEFYERVSGSRMHAAYIRPGGVACDLPANLCEDIYLFCQQFASRIDEMEEMLTNNRIWKQRLVDIGIVTAENAFAWGFSGVLLRGSGVAWDLRKTQPYDVYNRMIFDVPVGTQGDCYDRYLCRVEEMRQSIHIIMQCLNQLPKGMIKADDKKITPPSRSQMKQSMESLIHHFKLF... | Cofactor: Binds 1 [4Fe-4S] cluster.
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... |
Q36450 | MTTKNRQIKNFTSNFGPQHPAAHGVSRSVLEMNGEVVERAEPHIGLLQRGTEKLIEYKTYLQALPYSDRSEYVSMMAQEHAHSSAVERLLNCEVPLRAQYIRVLFREITRISNHSLALTTHAMDVGASTPFLWAFEEREKLLEFYERVSGARMHASFIRPGGVAQDLPLGLCIDIDSFTQQFASRIDELEEMSTGNRIWKQRLVDIGTVTAQQAKDWGFSGVMLRGSGVCWDLRKAAPYDVHDQLDPDIPVGTRGDRYDRYCIRIEEMRQSVRIIVQCLNQMPSGMIKADDRKLCPPSRSRMKLSMESSIHHFEPYTEGF... | 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... |
Q5DUX5 | MMRSSSLQKNIMLLRVGSKDSTRFRILILNFGPQHPASHGVLRLVIVIIGEVVTKLDPHIGFLHRGTERLVEEHSYMNAAVFMDRLDYTTVLTQTHAYCLAVEQALAKSRLCIRTQLLRTIFDELSRILNHLLSIATHALDIGTMAMLFWAFEDRERIMELYEYISGARMHTALYYPNQTLDHILTNELLAKILIFSRNSEKTYTEIYIALYNNRVWRLRLCGIGVVSTEISTSTTISGPVARSTGLQLDMRSGENYQYGYYASLTLRIFLGISGDSFDRFIIRLRELFESTRLIYNSLIELSAYINISVYNMCSYSNNP... | Function: Transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. Component of the iron-sulfur (IP) fragment of the enzyme.
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
Sequence Mass (Da): 46974
S... |
P15689 | MKAICVNFGPQHPAAHGVLRLILQLNGEVVEKMDIHIGLLHRGSEKLMETKPYLQSMPYFDRLDYVSMMVQEHAYCLAIEALLNTTNYTANFVLVRTMFDELTRILNHMLAIACHALDIGSMSSIFWAFEEREKIMEFYERVCGRRMHAAFYRPNEVNLNFLSVKLLTDILEFNNNCLTTLSEMHNILTYNKIWKQRLVNIGSISYKDCLDFGLTGVMARSTGIKRDLRMDAFDTYANYYYLNFRSYTGQAGDSYDRFLIRMNEMSESINIISQAIFKLTTSKNTCSPASILKALNKKKFISQTYKNEYSSMEKLITHFK... | 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... |
Q37619 | MALEKIITAPKYKNFTINFGPQHPAAHGVLRLVLEMNGEVVQRSDPHIGLLHRGTEKLIEYKNYLQALPYFDRLDYVSMMCQEHAYSLAVEKLLNISKDIPLRAQYIRVLFSEITRILNHLLAVTCHAMDVGALTPFLWGFEEREKLMEFYERVSGARMHAAYIRPGGVALDLPLGLCEDIYKFSKQFASRIDEIEEMLTSNRIWKQRLVDVGVVSAEQALDWSFSGVLLRGSGIAWDLRKTQPYEVYDRMKFNIPVGTRGDCYDRYLIRVQEMRESLRIVMQTINEMSKGIIRLDDRKITPPTRDQMKQSMESLIHHFK... | 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... |
P80264 | MTTKNRQIQNFTLNFGPQHPAAHGVLRLVLEMNGEVVERAEPHIGLL | 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... |
P21301 | MLFLVVFLHLYRFTFGPQHPAAHGVLCCLLYFCGEFIVYIDCIIGYLHRGTEKLCEYKSVEQCLPYFDRLDYVSVCCNEHLLSLCFEYMLRCCLSLRCAFMRLLIVEFTRSFNGLLCISCMVLDLGCLSPLLWSFEERDKLMTFFDLCCGCRMHLAFMVLLGILDDFVFGFVDFLLLLIISCLFVMDCYDLLFVGNRLFYLRLRGLSFFDLYDLVFNSLSGVLSRSLGMVWDCRLFSCYELYFMFCYDYCFCFIGDAFDRLFLRLFDMRMSLLICKQCFFVGFFVFGFVCLFDYLYCDITIETIIMLFYSLWCCCLPGIS... | 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... |
Q37383 | MGLNFFMSRKIYYIKLLTGLYKKFIKALIVKKNESNNAYLLVETANFYNLVFSLQRSSLTQFKVLNDVCIVDYPEKIDRFELSYNLSSIKYNFRIFIKTYTSAYVPSISTLFNSANWIERECWDMFGVFFTNHPDLRRILTDYGFEGFPLRKDFPLTGYIEIRYDDEKANIVYEPLELSQEYRLFNFTSPWEKIK | 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... |
Q95748 | MDNQFIFKYSWETLPKKWVKKMERSEHGNRFDTNTDYLFQLLCFLKLHTYTRVQVLIDICGVDYPSRKRRFEVVYNLLSTRYNSRIRVQTSADEVTRISSVVSLFPSAGWWEREVWDMFGVSFINHPDLRRILTDYGFEGHPLRKDFPLSGYVEVRYDDPEKRVVSEPIEMTQEFRYFDFASPWEQRSDG | 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... |
Q00673 | MISRTLLKRTVPASRLLRSFTTSNVRLSAHEEDLVNVNNLPRPKPTENYVPLINPTEKYKVQIEELHKFGTYIMSCLPKYIQQFSVWKDELTIYVAPSAIRPVMSYLKNHTSCQFKAVMDITAADYPSRTNRFDVVYNLLSDRHNSRIRVKTYANETSPVPSVTPLFNGANWYERETYDLFGVFFVGHPDLRRIMTDYGFEGHPLRKDFPTTGYTEVRYDEEKKRVIYEPLELTQAWRNFTVGSSVWEPVGEGKDFTPESFKLPTPQPEPEQEEKK | 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... |
Q2LCR4 | MKDYKNELKVKVDLGENLRGSIPGLIKKVMYKTQYLEIQVEKKNLLPVLRFLKESSKYQCTMLLDIVCIDCLNIEEIKIGRFKIIYVLNSIYNNTRVHISTYVENNGIIETTSGLFESSVWLEREIWDMFGIYFEKHPDLRRILTDYGFVGYPLKKDFPITGYLEVYYDVADKKIIYKPIELMQEYRNYNFGAVWGDYERKVYLENIIK | 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... |
Q2YQ73 | MSLLKIYWRAMQYLAVERTATITMCVASVLVALVTLAEPVLFGRVIQSISDKGDIFSPLLMWAALGGFNIMAAVFVARGADRLAHRRRLGVMIDSYERLITMPLAWHQKRGTSNALHTLIRATDSLFTLWLEFMRQHLTTVVALATLIPVAMTMDMRMSLVLIVLGVIYVMIGQLVMRKTKDGQAAVEKHHHKLFEHVSDTISNVSVVQSYNRIASETQALRDYAKNLENAQFPVLNWWALASGLNRMASTFSMVVVLVLGAYFVTKGQMRVGDVIAFIGFAQLMIGRLDQISAFINQTVTARAKLEEFFQMEDATADRQ... | Function: Involved in beta-(1-->2)glucan export. Its export to the periplasmic space is required to exert its action as a virulence factor. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation (Probable).
Catalytic Activity: [(1->2)-beta-D-g... |
P16009 | MEMISNNLNWFVGVVEDRMDPLKLGRVRVRVVGLHPPQRAQGDVMGIPTEKLPWMSVIQPITSAAMSGIGGSVTGPVEGTRVYGHFLDKWKTNGIVLGTYGGIVREKPNRLEGFSDPTGQYPRRLGNDTNVLNQGGEVGYDSSSNVIQDSNLDTAINPDDRPLSEIPTDDNPNMSMAEMLRRDEGLRLKVYWDTEGYPTIGIGHLIMKQPVRDMAQINKVLSKQVGREITGNPGSITMEEATTLFERDLADMQRDIKSHSKVGPVWQAVNRSRQMALENMAFQMGVGGVAKFNTMLTAMLAGDWEKAYKAGRDSLWYQQT... | Function: Baseplate central spike complex-associated lysozyme that is essential for the localized hydrolysis of bacterial cell wall, so that the tail tube, through which the phage DNA is ejected, can penetrate to the host inner membrane . The tail lysozyme complex at the tip of the tail tube penetrates through the oute... |
Q9FLI7 | MAIIASTFGTGLSYAGELPFKPVTGGEVGRKQQRMVVVRAEGGGGINPEIRKNEDKVVDSVVVTELSKNITPYCRCWRSGTFPLCDGSHVKHNKANGDNVGPLLLKKQ | Cofactor: Binds 1 [2Fe-2S] cluster per subunit.
Function: Plays an important role in plant development, senescence, reactive oxygen homeostasis, and iron metabolism. Acts as an iron-sulfur transfer protein.
Sequence Mass (Da): 11626
Sequence Length: 108
Subcellular Location: Plastid
|
O70903 | MGGKWSKSRMGGWSTIRERMRRAEPVAEGVGAVSRDLDRRGAVTINNTASTNRDAAWLEAQEDGEEVGFPVRPQVPLRPMTYKGAFDLSHFLKEKGGLDGLIYSKQRQDILDLWVYNTQGYFPDWQNYTPGPGERFPLTFGWCFKLVPVNPQEVEQANEGENNSLLHPMSLHGMEDDGREVLMWKFDSRLALTHLARVKHPEYKDC | Function: Factor of infectivity and pathogenicity, required for optimal virus replication. Alters numerous pathways of T-lymphocyte function and down-regulates immunity surface molecules in order to evade host defense and increase viral infectivity. Alters the functionality of other immunity cells, like dendritic cells... |
P03407 | MGGKWSKRSMGGWSAIRERMRRAEPRAEPAADGVGAVSRDLEKHGAITSSNTAATNADCAWLEAQEEEEVGFPVRPQVPLRPMTYKAALDISHFLKEKGGLEGLIWSQRRQEILDLWIYHTQGYFPDWQNYTPGPGIRYPLTFGWCFKLVPVEPEKVEEANEGENNSLLHPMSLHGMEDAEKEVLVWRFDSKLAFHHMARELHPEYYKDC | Function: Factor of infectivity and pathogenicity, required for optimal virus replication. Alters numerous pathways of T-lymphocyte function and down-regulates immunity surface molecules in order to evade host defense and increase viral infectivity. Alters the functionality of other immunity cells, like dendritic cells... |
Q89842 | MGGKWSKRRAEGWQTIRERMRRAEPAEPAADGVGAVSRDLARHGAITSSNTNNADIAWLEAQEEGEVGFPVRPQVPLRPMTYKAAVDLSHFLKEKGGLEGLVHSQKRQDILDLWVYHTQGFFPDWQNYTPGPGIRYPLTFGWCYKLVPVEPDEGENNREDNSLLHPANQHGVEDSERQVLVWRFDSRLAFHHVARELHPEYFKN | Function: Factor of infectivity and pathogenicity, required for optimal virus replication. Alters numerous pathways of T-lymphocyte function and down-regulates immunity surface molecules in order to evade host defense and increase viral infectivity. Alters the functionality of other immunity cells, like dendritic cells... |
P03406 | MGGKWSKSSVVGWPTVRERMRRAEPAADGVGAASRDLEKHGAITSSNTAATNAACAWLEAQEEEEVGFPVTPQVPLRPMTYKAAVDLSHFLKEKGGLEGLIHSQRRQDILDLWIYHTQGYFPDWQNYTPGPGVRYPLTFGWCYKLVPVEPDKVEEANKGENTSLLHPVSLHGMDDPEREVLEWRFDSRLAFHHVARELHPEYFKNC | Function: Factor of infectivity and pathogenicity, required for optimal virus replication . Alters numerous pathways of T-lymphocytes function and down-regulates immunity surface molecules in order to evade host defense and increase viral infectivity . Alters the functionality of other immunity cells, like dendritic ce... |
Q1JQA5 | MAGPAPGRRLVALALIVALAVGLPTAGAGQAPRPAERGPPVRLFTEEELARYGGEEEDQPIYMAVKGVVFDVTSGKEFYGRGAPYNALTGKDSTRGVAKMSLDPADLTHDTTGLTAEELESLDDVFTRVYKAKYPIVGYTARRILNEDGSPNLDFKPEDQPHFDIKDEF | Function: Acts as a neurotrophic factor in postnatal mature neurons enhancing neuronal survival (By similarity). Promotes cell proliferation and neurogenesis in undifferentiated neural progenitor cells at the embryonic stage and inhibits differentiation of astrocytes (By similarity). Its neurotrophic activity is exerte... |
Q923S6 | MGNNFSSVSSLQRGNPSRASRGHPQNLKDSIGGSFPVPSHRCHHKQKHCPPTLSGGGLPATPLLFHPHTKGSQILMDLSHKAVKRQASFCNAITFSNRPVLIYEQVRLKITKKQCCWSGALRLGFTSKDPSRIHPDSLPKYACPDLVSQSGFWAKALPEEFANEGNIIAFWVDKKGRVFYRINESAAMLFFSGVRTVDPLWALVDVYGLTRGVQLLDSELVLPDCLRPRSFTALRRPSLRCEADEARLSVSLCDLNVPGADGDDGAPPAGCPIPQNSLNSQHSRALPAQLDGDLRFHALRAGAHVRILDEQTVARLEHGR... | Function: Plays a role in hippocampal-dependent synaptic plasticity, learning and memory. Involved in the formation of spines and functional synaptic contacts by modulating the translational activity of the cytoplasmic polyadenylation element-binding protein CPEB3. Promotes ubiquitination of CPEB3, and hence induces CP... |
Q9D0S4 | MADPSEHVGLGGPRSPARPEPPPTRFHQVHGANIRMDPSGTRATRVESFAHGVCFSREPLAPGQVFLVEIEEKELGWCGHLRLGLTALDPASLAAVPEFSLPDLVSLGHSWVFAITRHHNRVPREGQPEAEAAVPSGPQALLVEPYLRIEQFRIPRDRLVGRSRPGLYSHLLDQLYEQNVLPPTARRSRLGVLFCPREDGTADMHIIINGEDMGPSARGLPAAQPLYAVVDVFASTKSVRLVQLEYGLPSLQTLCRLVIHKRVVHRLAIDVLHLPKGLKDFCKYE | Function: Plays an important role in the process of myofiber differentiation and maturation. Probable substrate-recognition component of a SCF-like ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complex, which mediates the ubiquitination of proteins. Probably contributes to catalysis through recog... |
Q96EH8 | MGAQLCFEANAKAPREALRFHAEAKGAQVRLDTRGCIAHRRTTFHDGIVFSQRPVRLGERVALRVLREESGWCGGLRVGFTRLDPACVSVPSLPPFLCPDLEEQSPTWAAVLPEGCALTGDLVRFWVDRRGCLFAKVNAGCRLLLREGVPVGAPLWAVMDVYGTTKAIELLDPTASRLPTPMPWDLSNKAVPEPKATPGEECAICFYHAANTRLVPCGHTYFCRYCAWRVFSDTAKCPVCRWQIEAVAPAQGPPALRVEEGS | Function: E3 ubiquitin-protein ligase that plays a role in various biological processes such as lung development or innate immunity . Seems to utilize UBE2E1. Promotes innate antiviral response by catalyzing 'Lys-63'-linked ubiquitination of IRF7 . Inhibits also hepatitis C virus assembly by directly binding to viral E... |
Q8CJC5 | MGSLLSPEANAEVPREALSFHGNATGAQVHLDDQRSTARRRSTFHDGIVFSQRPVWPGERVALRVLRHEEGWCGGLRVGFTRLDPAQVAASCLPPFVCPDLEEQSPTWAALLPEGFVRAGNVVCFWVNRRGWLFAKVNAGRPLLLRKDVLVQGAPLWAVMDVYGTTKAIELLDPKANAWIRSGEPVPESEVISGEECVICFHNTANTRLMPCGHSHFCGSCAWHIFKDTARCPICRWQIEEVAVVSSLKAEEGS | Function: E3 ubiquitin-protein ligase that plays a role in various biological processes such as lung development or innate immunity . Seems to utilize UBE2E1. Promotes innate antiviral response by catalyzing 'Lys-63'-linked ubiquitination of IRF7 .
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-c... |
Q02038 | MIVRCLSAARRLHRVGGSGILLRMTLGREAMSPLQAMSSYTVDGRNVLRWDLSPEQIKRRTEELIAQTKQVYDDIGMLDIEEVTYENCLQALADVEVKYIVERTMLDFPQHVSSDKEVRAASTEADKRLSRFDIEMSMREDIFLRIVRLKETCDLGKIKPEARRYLEKSVKMGKRNGLHLPEQVQNEIKAMKKRMSELCIDFNKNLNEDDTFLVFSKAELGALPDDFIDSLEKTDDNKYKITLKYPHYFPVMKKCCIPETRRKMEMAFNTRCKEENTIILQELLPLRAKVAKLLGYSTHADFVLEMNTAKSTHHVTAFLD... | Cofactor: Binds 1 zinc ion per subunit.
Function: Hydrolyzes oligopeptides such as neurotensin, bradykinin and dynorphin A. Acts as a regulator of cannabinoid signaling pathway by mediating degradation of hemopressin, an antagonist peptide of the cannabinoid receptor CNR1.
Catalytic Activity: Preferential cleavage in n... |
Q9BT67 | MALALAALAAVEPACGSRYQQLQNEEESGEPEQAAGDAPPPYSSISAESAAYFDYKDESGFPKPPSYNVATTLPSYDEAERTKAEATIPLVPGRDEDFVGRDDFDDADQLRIGNDGIFMLTFFMAFLFNWIGFFLSFCLTTSAAGRYGAISGFGLSLIKWILIVRFSTYFPGYFDGQYWLWWVFLVLGFLLFLRGFINYAKVRKMPETFSNLPRTRVLFIY | Function: Activates HECT domain-containing E3 ubiquitin-protein ligases, including NEDD4 and ITCH, and consequently modulates the stability of their targets. As a result, controls many cellular processes. Prevents chronic T-helper cell-mediated inflammation by activating ITCH and thus controlling JUNB degradation (By s... |
Q8R0W6 | MALALAALAAVEPACGSGYQQLQNEEEPGEPEQTAGDAPPPYSSITAESAAYFDYKDESGFPKPPSYNVATTLPSYDEAERTKTEATIPLVPGRDEDFVGRDDFDDTDQLRIGNDGIFMLTFFMAFLFNWIGFFLSFCLTTSAAGRYGAISGFGLSLIKWILIVRFSTYFPGYFDGQYWLWWVFLVLGFLLFLRGFINYAKVRKMPETFSNLPRTRVLFIY | Function: Activates HECT domain-containing E3 ubiquitin-protein ligases, including NEDD4 and ITCH, and consequently modulates the stability of their targets. As a result, controls many cellular processes. Prevents chronic T-helper cell-mediated inflammation by activating ITCH and thus controlling JUNB degradation . Pro... |
Q5U2S1 | MALALAALAAVEPACGTGYQQLQNEEEPGEREQTAGDAPPPYSSISAESAAYFDYKDESGFPKPPSYNVATTLPSYDEAERTKAEATIPLVPGRDEDFVGRDDFDDADQLRIGNDGIFMLTFFMAFLFNWIGFFLSFCLTTSAAGRYGAISGFGLSLIKWILIVRFSTYFPGYFDGQYWLWWVFLVLGFLLFLRGFINYAKVRKMPETFSNLPRTRVLFIY | Function: Activates HECT domain-containing E3 ubiquitin-protein ligases, including NEDD4 and ITCH, and consequently modulates the stability of their targets. As a result, controls many cellular processes. Prevents chronic T-helper cell-mediated inflammation by activating ITCH and thus controlling JUNB degradation. Prom... |
Q9NV92 | MARRRSQRVCASGPSMLNSARGAPELLRGTATNAEVSAAAAGATGSEELPPGDRGCRNGGGRGPAATTSSTGVAVGAEHGEDSLSRKPDPEPGRMDHHQPGTGRYQVLLNEEDNSESSAIEQPPTSNPAPQIVQAASSAPALETDSSPPPYSSITVEVPTTSDTEVYGEFYPVPPPYSVATSLPTYDEAEKAKAAAMAAAAAETSQRIQEEECPPRDDFSDADQLRVGNDGIFMLAFFMAFIFNWLGFCLSFCITNTIAGRYGAICGFGLSLIKWILIVRFSDYFTGYFNGQYWLWWIFLVLGLLLFFRGFVNYLKVRNM... | Function: Activates HECT domain-containing E3 ubiquitin-protein ligases, including ITCH, NEDD4, NEDD4L, SMURF2, WWP1 and WWP2, and consequently modulates the stability of their targets. As a result, may control many cellular processes. Recruits ITCH, NEDD4 and SMURF2 to endosomal membranes. Negatively regulates KCNH2 p... |
Q90932 | MYSPYCLTQDEFHPFIEALLPHVRAFSYTWFNLQARKRKYFKKHEKRMSKEEERAVKDELLGEKPEVKQKWASRLLAKLRKDIRPECREDFVLSVTGKKAPCCVLSNPDQKGKIRRIDCLRQADKVWRLDLVMVILFKGVPLESTDGERLAKAPQCASPGLCVQPHHIGVTIKELDLYLAFFVQAPDSGQSDSSNPQGDADIKPLPNGHLSFQDCFVTSGVWNVTELVRVSQTPVATASGPNFSLADLESPGGYYNISPVTLGRRPLGPPTASGPKRPKALDEGDLEGPGDDVFYSGPGRSPAPGSSQGPWGGDVDTSPA... | Function: Recognizes and binds the palindromic sequence 5'-TTGGCNNNNNGCCAA-3' present in viral and cellular promoters and in the origin of replication of adenovirus type 2. These proteins are individually capable of activating transcription and replication.
Sequence Mass (Da): 46903
Sequence Length: 431
Domain: The 9aa... |
P70257 | MYSPYCLTQDEFHPFIEALLPHVRAFSYTWFNLQARKRKYFKKHEKRMSKDEERAVKDELLGEKPEIKQKWASRLLAKLRKDIRPEFREDFVLTITGKKPPCCVLSNPDQKGKIRRIDCLRQADKVWRLDLVMVILFKGIPLESTDGERLYKSPQCSNPGLCVQPHHIGVTIKELDLYLAYFVHTPESGQSDSSNQQGDADIKPLPNGHLSFQDCFVTSGVWNVTELVRVSQTPVATASGPNFSLADLESPSYYNINQVTLGRRSITSPPSTSSTKRPKSIDDSEMESPVDDVFYPGTGRSPAAGSSQSSGWPNDVDAGP... | Function: Recognizes and binds the palindromic sequence 5'-TTGGCNNNNNGCCAA-3' present in viral and cellular promoters and in the origin of replication of adenovirus type 2. These proteins are individually capable of activating transcription and replication. Isoform NFIX1 acts as a transcriptional activator while isofor... |
Q9YES5 | MNRREVRCAFSASKAARAQLLLRGKVRLEPLPTRPRTVLGLDASYSAKDGVGVGAAVLISLETLEPVDCRVYISRVCIPYIPGLLAFRELAVMAPAAAALSAEADVVMVDGHGIAHPRRFGIASHVGVILERPSIGVAKKKLVGTLVEGPGGMYVVQDGERLAIVLGTRPREVYVSPGHRITLEEAASIARATIRPGGWMPEPTRLADVISKALKTIIGGQSLINSALASLCRVKLGPRLEELERPLRRAGLEVE | Function: DNA repair enzyme involved in the repair of deaminated bases. Selectively cleaves double-stranded DNA at the second phosphodiester bond 3' to a deoxyinosine leaving behind the intact lesion on the nicked DNA.
Catalytic Activity: Endonucleolytic cleavage at apurinic or apyrimidinic sites to products with a 5'-... |
Q0A5M1 | MGVSIRALHPWAVDAAEGRRLQQTLREQLCLKTPRGFRPRLVAGVDAGVVDGGRTIRAAVVVMSLPDLAVVTQSVARAPAIMPYVPGLLSFRELPGVVRALEQLDVTPELLLCDGQGIAHPRRLGIAAHLGLITDLPAIGVGKSRLVGTYREPRPEKGATSGLYDGHERIGTVLRSRDHVRPLYVSPGHRISHEDAVHWVLTCCTRYRLPEPQRAADRLASAKEAPA | Function: DNA repair enzyme involved in the repair of deaminated bases. Selectively cleaves double-stranded DNA at the second phosphodiester bond 3' to a deoxyinosine leaving behind the intact lesion on the nicked DNA.
Catalytic Activity: Endonucleolytic cleavage at apurinic or apyrimidinic sites to products with a 5'-... |
P29378 | MTAHNPVQGTLPRSNEEIAARVKAMEAILVDKGLISTDAIDHMSSVYENEVGPQLGAKIVARAWVDPEFKQRLLTDATSACREMGVGGMQGEEMVVLENTGTVHNMVVCTLCSCYPWPVLGLPPNWYKYPAYRARAVRDPRGVLAEFGYTPDPDVEIRIWDSSAELRYWVLPQRPAGTENFTEEQLADLVTRDSLIGVSVPTTPSKA | Cofactor: Binds 1 Co(3+) ion per subunit.
Function: NHase catalyzes the hydration of various nitrile compounds to the corresponding amides.
Catalytic Activity: an aliphatic amide = a nitrile + H2O
Sequence Mass (Da): 22848
Sequence Length: 207
EC: 4.2.1.84
|
A8EUK5 | MVKKYKVIDNFISKEALSGILLLFVTLFAIIVANSNFGDFYFNLWDKPLGVAIGDFIISMPLRLWINDGLMALFFLMVSLEIKRELLIGELASVSRAMFPFVASLGGMIVPASIYIALNPDNFIGFGIPMGTDTAFAIAMLILLGKRVNTALKLFLVALAVIDDLGAIIVVATVYTSELKLEYFLHAAFVYGLIWLLNYFDVKKLSFYLFLGIFLWIFIHETGVHATIAGVLLAFAIPISSRMNEKKFIEKTKADLEEFERCMDDKPILNHRQINALEGIAYGYDRVQNPLIRLEHDLHGFSAFFIMPIFAFSNAGVLLD... | Function: Na(+)/H(+) antiporter that extrudes sodium in exchange for external protons.
Catalytic Activity: 2 H(+)(out) + Na(+)(in) = 2 H(+)(in) + Na(+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 48002
Sequence Length: 431
Subcellular Location: Cell inner membrane
|
A0RMW2 | MNIIKNFLQKESASGILIILAMILALILANNGVLNKFYSEILRLDSGIIFGEFKLIKPTILWVNDGLMAIFFFFIGLELKYEFLEGELNSISKVALPSIAGIGGVIVPAVIFYVLNHANRFDVNGWAIPTVSDTAFALAVLFLLGSRIPISLKLFLLSLAIIDDVAAIIIIAIFYTKTLSIISLFISFCAIVILTILNYKNNQNIYIYLLCGIVLWVSVLMSGIHATLAGIIASMFIPLRDEDGDPEHGMLQSVMHFLHPIVAFLILPIFAFSNAGVVFSEDSILNLTHPVPLGIIFGLFIGKQIGVFSFAFLAIKCKLA... | Function: Na(+)/H(+) antiporter that extrudes sodium in exchange for external protons.
Catalytic Activity: 2 H(+)(out) + Na(+)(in) = 2 H(+)(in) + Na(+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 42590
Sequence Length: 390
Subcellular Location: Cell inner membrane
|
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.