ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
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Q84HC8 | MGKRAAHIGLRALADLATPMAVRVAATLRVADHIAAGHRTAAEIASAAGAHADSLDRLLRHLVAVGLFTRDGQGVYGLTEFGEQLRDDHAAGKRKWLDMNSAVGRGDLGFVELAHSIRTGQPAYPVRYGTSFWEDLGSDPVLSASFDTLMSHHLELDYTGIAAKYDWAALGHVVDVGGGSGGLLSALLTAHEDLSGTVLDLQGPASAAHRRFLDTGLSGRAQVVVGSFFDPLPAGAGGYVLSAVLHDWDDLSAVAILRRCAEAAGSGGVVLVIEAVAGDEHAGTGMDLRMLTYFGGKERSLAELGELAAQAGLAVRAAHP... | Function: S-adenosyl-L-methionine-dependent O-methyltransferase that catalyzes regiospecific methylation at the 7-hydroxy group of 2,7-dihydroxy-5-methyl-1-naphthoate in the biosynthesis of the naphthoate moiety of the neocarzinostatin chromophore. Also recognizes other dihydroxynaphthoate as substrates and catalyzes t... |
Q84HC5 | MHETAAAPAPAGFVPWPDDVAARYTAAGHWEGRSLGTHLAEAARKVPEAVCLVDGPVRMSYSELMARADGAAVRMRGLGIRPADRVVVQLPNCWEHVVVTMACLRLGALPIWALPQYRHRELSGVVTHARASALVVPDVYREFDHQALAHEVAEAQPTVRHVLVAGSDVRPDSVDLRALCEPLDADEAARVAAELDRSAPRGEEVAMLKLSGGTTGLPKLVARTHNDLSYMIKRAAQVCGFGRDTVYLAVLPLGHGFPNTGPGVLGTLLAGGRVVISGSPAPEAAFALMERERVTATSVVPAIVMRWLQYRDERPGADLG... | Function: Catalyzes the activation of 2-hydroxy-7-methoxy-5-methyl-1-naphthoate in the biosynthesis of the naphthoate moiety of the neocarzinostatin chromophore. Also catalyzes the activation of other 1-naphthoic acid analogs such as 2-hydroxy-5-methyl-1-naphthoate or 2,7-dihydroxy-5-methyl-1-naphthoate in vitro.
Catal... |
Q84HB6 | MCPYRLDPEGADTHGETARLREQGPIARVELQDGVLAWSVHDYAVAKQIMADERFSKNPRKNWPAYINGEISNGWPLITWVAMDTMATQDGADHARLRKLLLKAFTERRVESMRPHIEKTVKELLDNMAAKADDEIVDIKEMFHAELPTRLMCDLFGVPEERRAEVLAGGHKNIDTRISSEAAEANLGQWQEAISDLVEYKRHHPGDDLTSALIEARDEGSRLSDSELIGTLHLLLGAGSETLVNALAHSSLALLVDADLRKKVTSGEIPWVNVWEETLRVESPVAHLPFRYATEDFEIGGVKISKGDPLLVDFAGIGRD... | Function: Involved in the biosynthesis of the naphthoic acid (NA) moiety in the chromophore of the enedyine antitumor antibiotic neocarzinostatin (NCS). Catalyzes the hydroxylation at C-7 position of 2-hydroxy-5-methyl-1-naphthoate to yield 2,7-dihydroxy-5-methyl-1-naphthoate.
Catalytic Activity: 2-hydroxy-5-methyl-1-n... |
Q54BK2 | MKRSIVFIYSLVILLLSVGFIDAFKISIENHIKLSDDSSYQIGTGIYDITGPGAETNMMGYAMPGQITGGIHFRQRARAFVFIDSEGNRAVYVSTDSCMIFQEVKIQVIQDLQEIFGPTLYTHDNVLLSGTHTHSGPAGFSEYALYGITALGFYKKNFDTICDGIVQAIVKAHKSVQPARMLTQQGELWNSNINRSPYAYDNNPEEEKAMYDANVDKNMTVIRIEDMSGNPFAAISFFGVHCTSMNNTNHLISGDNKGYASYLWEKHANGQSSLPGTGPFIAAFGQSNEGDVSPNTRGPTCRDGKPCDYKTSTCNGKVEE... | Function: Hydrolyzes the sphingolipid ceramide into sphingosine and free fatty acid at an optimal pH of 3.0. Has no activity toward glycosphingolipids, such as GalCer and Galbeta1-3GalNAcbeta1-4(NeuAcalpha2-3)Galbeta1-4Glcbeta1-1'Cer or sphingomyelin.
Catalytic Activity: an N-acylsphing-4-enine + H2O = a fatty acid + s... |
Q67A25 | MMKMEVVFVFLMLLGTINCQKLILTGRPFLHHQGIINQVSTVTKVIHHELEVAASADDIWTVYSWPGLAKHLPDLLPGAFEKLEIIGDGGVGTILDMTFVPGEFPHEYKEKFILVDNEHRLKKVQMIEGGYLDLGVTYYMDTIHVVPTGKDSCVIKSSTEYHVKPEFVKIVEPLITTGPLAAMADAISKLVLEHKSKSNSDEIEAAIITV | Function: Involved in the biosynthesis of the common precursor of all benzylisoquinoline alkaloids such as morphine, sanguinarine, codeine or berberine. Condenses dopamine and 4-hydroxyphenylacetaldehyde.
Catalytic Activity: (4-hydroxyphenyl)acetaldehyde + dopamine = (S)-norcoclaurine + H2O
Sequence Mass (Da): 23341
Se... |
O76036 | MSSTLPALLCVGLCLSQRISAQQQTLPKPFIWAEPHFMVPKEKQVTICCQGNYGAVEYQLHFEGSLFAVDRPKPPERINKVKFYIPDMNSRMAGQYSCIYRVGELWSEPSNLLDLVVTEMYDTPTLSVHPGPEVISGEKVTFYCRLDTATSMFLLLKEGRSSHVQRGYGKVQAEFPLGPVTTAHRGTYRCFGSYNNHAWSFPSEPVKLLVTGDIENTSLAPEDPTFPADTWGTYLLTTETGLQKDHALWDHTAQNLLRMGLAFLVLVALVWFLVEDWLSRKRTRERASRASTWEGRRRLNTQTL | Function: Cytotoxicity-activating receptor that may contribute to the increased efficiency of activated natural killer (NK) cells to mediate tumor cell lysis.
PTM: N-glycosylated.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 34481
Sequence Length: 304
Subcellular Location: Cell membrane
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P56753 | MKRPVTGKDLMIVNMGPHHPSMHGVLRLIVTLDGEDVVDCEPILGYLHRGMEKIAENRAIIQYLPYVTRWDYLATMFTEAITVNGPEQLGNIQVPKRASYIRVIMLELSRIASHLLWLGPFMADIGAQTPFFYIFREREFVYDLFEAATGMRMMHNFFRIGGIAADLPYGWIDKCLDFCDYFLTEVVEYQKLITRNPIFLERVEGVGIIGGEEAINWGLSGPMLRASGIPWDLRKIDRYESYDEFEWEIQWQKQGDSLARYLVRLSEMTESIKIIQQALEGLPGGPYENLESRGFDRKRNPEWNDFEYRFISKKPSPTFE... | 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... |
A6H5H8 | MGSTESPLLGQTTPNSVISTTLNDLSNWARLSSLWPLLYGTSCCFIEFASLIGSRFDFDRYGLVPRSSPRQADLIITAGTVTMKMAPSLVRLYEQMPGPKYVIAMGACTITGGMFSTDSYSTVRGVDKLIPVDVYLPGCPPKPEAIIDAIIKLRKKVAREIYEDRTKLQQGKRYFTQNHKFRVGSSLYTGNYDQKLLHKSPEPQSESTSEILSKTFESTSEIPSDFVKYENSVSFQESRNEEYFVKSNEQEINFQKFHWKC | 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... |
Q1KXV5 | MNSIEFPLFHRTTQNSVISTTLNDLSNWSRLSSLWPLLYGTSCCFIEFASLIGSRFDFDRYGLVPRSSPRQADLILTAGTVTMKMAPSLVRLYEQMPEPKYVIAMGACTITGGMFSTDSYSTVRGVDKLIPVDVYLPGCPPKPEAIIDAITKLRKKISREIYPDRIMSQRENRCFTTNHKFQVGHSIHTGNYDQGFLYQPPSTSEIPPETFFKYKSSVSSHELVN | 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... |
Q2JVL1 | MLLVGSGAKFVQQLEQCGALAIFVTPEGGSEGHYLRRLRGAGYEVVTLSSKGIGDLASYLTSSHGVRPATLGKSQRRTYFYPSLIEQYRATLPPKAKGLVFWFYEGHVLSRQELSYLVKLSQEDKGVKFVVELGRERSIRWQPLQSA | Function: NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, a... |
P74069 | MLPLPLIANGKGFIRALENDGALAVYAPLEGGYEGRYQRRLRANGYASISLSARGLGDVEAYLMQVHGVRPAHLGKKNIAQEGAVGPIYFAQPIAGYQLENLPAQSKGLVLWILEGYILSQTEIQDLISLTKRVPKLKVVLEMGGDRVFRWQPLLDCLQAA | Function: NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, a... |
Q8DJU2 | MGLLAGYQFVKDLESAGALALFVPPEGGFEGRYQRRLRSKGYTTLPMSAPGLGDLAAYLTQEHGIRPAHTGKEDIRVYFQPPLVTYHLENLPPNAKGLVLWLIDGKRLSKQEFAYLAQLTQTLPKFKVVVEVGGDRVVRWEPLADWVAAA | Function: NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, a... |
Q7Z8P9 | MSNEQTFIAIKPDGVQRGLIGPIISRFENRGFKLVAMKLVSPPQSQLEQHYADLSDKPFFKGLVSYMLSGPICAMVWEGRDVVKTGRTILGATNPLASAPGTIRGDFAIDVGRNVCHGSDSVENAKKEIALWFKPEELISWKSATFDWVYEKA | 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... |
Q73AY0 | MEKTFLMVKPDGVQRAFIGEIVARFEKKGFQLVGAKLMQVTPEIAGQHYAEHTEKPFFGELVDFITSGPVFAMVWQGEGVVDTARNMMGKTRPHEAAPGTIRGDFGVTVAKNIIHGSDSLESAEREIAIFFKEEELVDYSKLMNEWIY | 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... |
Q65I26 | MEKTFVMVKPDGVQRQLIGEILLRFERKGLQLIGAKLMKVSEETAGEHYKEHNGKPFFGELVDFITSGPVFAMVWEGEDAIAVARQLIGKTNPKEALPGTIRGDFGMFVGKNIIHGSDSPESAAREINLFFKEDELVEDEKLMNQWIY | 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... |
P31103 | MMEKTFIMVKPDGVQRQLIGDILSRFERKGLQLAGAKLMRVTEQMAEKHYAEHQGKPFFGELVEFITSGPVFAMVWEGENVIEVTRQLIGKTNPKEALPGTIRGDYGMFVGKNIIHGSDSLESAEREINIFFKNEELVSYQQLMAGWIY | 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... |
P36010 | MSSQTERTFIAVKPDGVQRGLVSQILSRFEKKGYKLVAIKLVKADDKLLEQHYAEHVGKPFFPKMVSFMKSGPILATVWEGKDVVRQGRTILGATNPLGSAPGTIRGDFGIDLGRNVCHGSDSVDSAEREINLWFKKEELVDWESNQAKWIYE | 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 . Required for repair of UV radiation- and etoposide-induced DNA damage .
PTM: The N-terminus is b... |
Q9ULP0 | MPECWDGEHDIETPYGLLHVVIRGSPKGNRPAILTYHDVGLNHKLCFNTFFNFEDMQEITKHFVVCHVDAPGQQVGASQFPQGYQFPSMEQLAAMLPSVVQHFGFKYVIGIGVGAGAYVLAKFALIFPDLVEGLVLVNIDPNGKGWIDWAATKLSGLTSTLPDTVLSHLFSQEELVNNTELVQSYRQQIGNVVNQANLQLFWNMYNSRRDLDINRPGTVPNAKTLRCPVMLVVGDNAPAEDGVVECNSKLDPTTTTFLKMADSGGLPQVTQPGKLTEAFKYFLQGMGYIAYLKDRRLSGGAVPSASMTRLARSRTASLTS... | Function: Contributes to the maintenance of intracerebral BDNF levels within the normal range, which is necessary for the preservation of spatial learning and the resistance to neuronal cell death caused by ischemic stress (By similarity). May enhance growth factor-induced ERK1 and ERK2 phosphorylation, including that ... |
Q02827 | MMTGRQGRATFQFLPDEARSLPPPKLTDPRLAFVGFLGYCSGLIDNAIRRRPVLLAGLHRQLLYITSFVFVGYYLLKRQDYMYAVRDHDMFSYIKSHPEDFPEKDKKTYGEVFEEFHPVR | Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis but required for the complex assembly. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the... |
O95298 | MIARRNPEPLRFLPDEARSLPPPKLTDPRLLYIGFLGYCSGLIDNLIRRRPIATAGLHRQLLYITAFFFAGYYLVKREDYLYAVRDREMFGYMKLHPEDFPEEDKKTYGEIFEKFHPIR | Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis but required for the complex assembly. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the... |
A4FUH5 | MGAAVARAVRNFNLENRAEREISRMKPSPAPRHPSTKNLLLEQMSSHPEIKGEIDRKDDKLLSLLKDVYVDSQDPVSSLQVKDATARQKPKEFRLPKDHQFDMMDVKNIPKGKISIVEALTLLNNHKLYPDTWTAKKIAEEYHLEQQDVNSLLKYFVTFEVKIFPPEGKKAIESK | Function: Involved in the assembly of mitochondrial NADH:ubiquinone oxidoreductase complex (complex I) (By similarity). May be involved in cell proliferation and survival of hormone-dependent tumor cells. May be a regulator of breast tumor cell invasion (By similarity).
PTM: Phosphorylated on serine. Prolactin stimulat... |
Q26783 | MLRRTSFNFTGRAMISRGSPEWSHRLDLKKGKKTTMMHKLGTSKPNNALQYAQMTLHDLTEWCLAYSPWPLTFGLACCAVEMMHAYASRYDLDRFGIVPRPTPRQAEIIIVSGTVTNKMAPILRNIYVQMVNPKWVISMGSCANGGGYYHFSYAVLRGCERAIPVDFWIPGCPPSAESLVFCLHTLQKKIRWHEIQKYSVRD | 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... |
P42028 | MRCLTMPMLLRALAQAQAARAGHASVRGLHSSAVAATYKYVNLREPSMDMKSVTDRAAQTLLWTELIRGLGMTLSYLFREPATINYPFEKGPLSPRFRGEHALRRYPSGEERCIACKLCEAVCPAQAITIEAEPRADGSRRTTRYDIDMTKCIYCGFCQEACPVDAIVEGPNFEFSTETHEELLYNKEKLLNNGDKWEAEIAANIQADYLYR | Cofactor: Binds 2 [4Fe-4S] clusters per subunit.
Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor . Essential for the catalytic activity and assembly o... |
Q9VF27 | MSLTMRIFTASRNGQRLFGSHGARLLAAQRAEPKDIVEVPKGYVYVNNKELSMEFADITDRAASTMFFGELLRGFAVTLAHIFKEPATINYPFEKGPLSPRFRGEHALRRYPSGEERCIACKLCEAICPAQAITIEAEERADGSRRTTRYDIDMTKCIYCGFCQEACPVDAIVEGPNFEFSTETHEELLYNKEKLLCNGDKWESEIASNLQADHLYR | Cofactor: Binds 2 [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... |
O00217 | MRCLTTPMLLRALAQAARAGPPGGRSLHSSAVAATYKYVNMQDPEMDMKSVTDRAARTLLWTELFRGLGMTLSYLFREPATINYPFEKGPLSPRFRGEHALRRYPSGEERCIACKLCEAICPAQAITIEAEPRADGSRRTTRYDIDMTKCIYCGFCQEACPVDAIVEGPNFEFSTETHEELLYNKEKLLNNGDKWEAEIAANIQADYLYR | Cofactor: Binds 2 [4Fe-4S] cluster.
Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor . Essential for the catalytic activity and assembly of complex I .... |
Q60HE3 | MRCLTMPTLLRALAQAAHTGPPGGRTLHSSAVAATYKYVNMQESKTDMKSVTDRAARTLLWTELFRGLGMTLSYLFREPATINYPFEKGPLSPRFRGEHALRRYPSGEERCIACKLCEAVCPAQAITIEAEPRADGSRRTTRYDIDMTKCIYCGFCQEACPVDAIVEGPNFEFSTETHEELLYNKEKLLNNGDKWEAEIAANIQADYLYR | Cofactor: Binds 2 [4Fe-4S] cluster.
Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor (By similarity). Essential for the catalytic activity and assembly... |
Q8K3J1 | MYRLSSSMLPRALAQAMRTGHLNGQSLHSSAVAATYKYVNKKEQESEVDMKSATDNAARILMWTELIRGLGMTLSYLFREPATINYPFEKGPLSPRFRGEHALRRYPSGEERCIACKLCEAICPAQAITIEAEPRADGSRRTTRYDIDMTKCIYCGFCQEACPVDAIVEGPNFEFSTETHEELLYNKEKLLNNGDKWEAEIAANIQADYLYR | Cofactor: Binds 2 [4Fe-4S] cluster.
Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor (By similarity). Essential for the catalytic activity and assembly... |
Q12644 | MLTTTASSAAAVARQLTTRRVIAPSFVSQAIRTYATPAGPPPKGFRIPTPKTWDQEEEHVLDKNGRYFLLTEMFRGMYVAMEQFFRPPYTIYYPFEKGPISPRFRGEHALRRYPSGEERCIACKLCEAVCPAQAITIEAEERADGSRRTTRYDIDMTKCIYCGFCQESCPVDAIVESPNAEYATETREELLYNKEKLLSNGDKWEPELAAAIRADSPYR | Cofactor: Binds 2 [4Fe-4S] clusters per subunit.
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 immed... |
O21233 | MTIINKTAQTLFLTELVKGMSLTLDYFFRKKVTLNYPFEKGPLSPRFRGEHALRRYQTGEERCIACKLCEAICPAQAITIESEPRIDGSRRTTRYDIDMTKCIYCGFCQEACPVDAIVEGPNFEFATETHEELLYDKEKLLQNGDRWETEIAANLANEALYR | Cofactor: Binds 2 [4Fe-4S] clusters per subunit.
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 immed... |
P80269 | MAAILARKSLSALRSRQLVLAGHTIEGTNGYNRTLLGTRSFATKHSFSTDKDDEEREQLAKELSKDWNSVFERSINTLFLTEMVRGLMLTLKYFFEKKVTINYPFEKGPLSPRFRGEHALRRYATGEERCIACKLCEAICPAQAITIEAEEREDGSRRTTRYDIDMTKCIYCGFCQEACPVDAIVEGPNFEFATETHEELLYDKEKLLENGDRWETEIAENLRSESLYR | Cofactor: Binds 2 [4Fe-4S] clusters per subunit.
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 immed... |
P52466 | MLKEKMYDELILSTCRVLKLGPADFRVTDKNLFSKNPKFPLCDILLKLDFAYSLEYLLSLWEDLTKQEARFIFKNTGGAVSMSCYLHAPIKQESQNIVKECNILNVNECLSVCLNDIEAIKPSSSGVLTKCIIRRNRDAAFIVEFVAFGPESESEYIALLKAIILKKKFLERQDLEKHRAARHIKKPLRLQLKSVGEMTSFRSINYMGNTKDAAVFPVTVPIFARRNNILCGFLVAALLIVCYVIFKEFALSADFSAV | Function: Plays an essential role in virion nuclear egress, the first step of virion release from infected cell. Within the host nucleus, NEC1 interacts with the newly formed capsid through the vertexes and directs it to the inner nuclear membrane by associating with NEC2. Induces the budding of the capsid at the inner... |
F5HA27 | MSVVGKRVVDELCRVVSSYLGQSGQSLDLERCIDGAPVYAKGGATAICTVRMQHGCVYHLEFVYKFWAHLLEEMHYPFSPCFVISNNGLSTTLKCFLCRPSDAVSQFGHVLPVESDVYLAKNTSVVLGQDDFTKFKASLVFSKNLGVYNSMVICRTYFTDYRQVLQFLVVTPKSHKRLKSLLETVYCLAAPVADSAAQGGAGFPTNGRDARACTSDVTAVYWAGQGGRTVRILGAFQWSLGRAVALVRRSWPWISAGIAFLCLGLVWMRPS | Function: Plays an essential role in virion nuclear egress, the first step of virion release from infected cell. Within the host nucleus, NEC1 interacts with the newly formed capsid through the vertexes and directs it to the inner nuclear membrane by associating with NEC2. Induces the budding of the capsid at the inner... |
P16519 | MKGGCVSQWKAAAGFLFCVMVFASAERPVFTNHFLVELHKGGEDKARQVAAEHGFGVRKLPFAEGLYHFYHNGLAKAKRRRSLHHKQQLERDPRVKMALQQEGFDRKKRGYRDINEIDINMNDPLFTKQWYLINTGQADGTPGLDLNVAEAWELGYTGKGVTIGIMDDGIDYLHPDLASNYNAEASYDFSSNDPYPYPRYTDDWFNSHGTRCAGEVSAAANNNICGVGVAYNSKVAGIRMLDQPFMTDIIEASSISHMPQLIDIYSASWGPTDNGKTVDGPRELTLQAMADGVNKGRGGKGSIYVWASGDGGSYDDCNCD... | Function: Serine endopeptidase which is involved in the processing of hormone and other protein precursors at sites comprised of pairs of basic amino acid residues. Responsible for the release of glucagon from proglucagon in pancreatic A cells.
Catalytic Activity: Release of protein hormones and neuropeptides from thei... |
G4NEA9 | MASSRDRAYVTVYSPTLLTWVYDYYVLGFNLRYIWGCPTDAVLLPFFAENFSRRHLDVGVATGYLPARVLASPWRRAAAHRQHLTLLDINANSLRASDARVRAAAPGIETTCVEADVVADLPPVLASVVEEERARVEKAGGEAGSSSRSCLYDSISMFNLFHCVPGGPAKLRAISTYKALLADHGVLSGCTVLGERHATGWFSRWYLRLYNRKGIFNNINDTREEFEEVLNKEFEEVDTWMFGMVLLFRASKPRREGSGYVDLLA | Function: O-methyltransferase; part of the gene cluster that mediates the biosynthesis of nectriapyrone and its analogs phomopyrone A, acropyrone and zaepyrone . The nectriapyrone biosynthetic gene cluster consists of two genes, the highly reducing polyketide synthase NEC1 that produces a demethylated analog of nectria... |
P0DO51 | MAFLSNMAMFITMLMFSSMMHPCFSQPSCAPMDTMDTNGVDEADIDMMQFPINLEFLEAEFFLWGALGHGLDVVAPQLAMGGPPPYGAQKANLDPLTQNIITEFAYQEVGHLRALERTVGGFPRPLLNLSASNFANLIEAAFGYHLVPPFNPYRDGLSYMLASYAVPYMGLVGYVGTNPNLKGHQTKRLLAGLLGVESGQDAVIRMYLYERQGHVVAPYRHTVAEFTARISELRNRLAMCGVKDEGVIVPRQLGAENQTMSNVLSANYDSISYRRTPGEILRVVYSTGNESVPGGFYPNGGNGRIARRFLV | Function: Involved in the production of blood-red nectar containing the alkaloid nesocodin and that serves as a visual attractant for pollinator visitation, including vertebrates such as Phelsuma geckos . The nectar is initially acidic and pale yellow, but slowly becomes alkaline before turning into red within 24 hours... |
Q6UDJ7 | MRSDKYSQLVSVVNAGLGACGTSATLVYIRNNARVAPTGDIITLPARLDGPPIPAEYILEAMTSLLSIRTAWLRIQNTGQAVIVAGCSTQNFHHGDVTWEPPASTVTLTTAKSLWVSASAVREMKVIQRIRTAPLAAMMFMCFYRGGKNEVTVRFAFYKSDSEPNLLKISKCVYEAIDAEATRNLPKPRGFDTPPCAVLAQRMRPLGAAEGGDRETSAQTHSPAAQAQHVMQHATATKSWGALGRTLKHKKNLGWILFTCALSLAAAFVTAYIK | Function: Plays an essential role in virion nuclear egress, the first step of virion release from infected cell. Within the host nucleus, NEC1 interacts with the newly formed capsid through the vertexes and directs it to the inner nuclear membrane by associating with NEC2. Induces the budding of the capsid at the inner... |
Q01045 | MNSTRLVYELCDIVNLYLCQPGVQIDVDRCASGPHVFTKGGTEAICTVKLSHGLVYNIEFVYKFWAHKLESVKYPFSPCFIISNNGLATTLKCFLSRPRNVNHFGHVLNIDSDVYLTKNTSVILSQDDFVKFKTNLVFSKDLDVFHSMVVFRTYLIEHRQALQFLVVKPRSSKRVNSILSSVAKTASQNFILDPPRRSEETRVCIKPWTLSKKNIWTIILSLVAVVAIILKWREL | Function: Plays an essential role in virion nuclear egress, the first step of virion release from infected cell. Within the host nucleus, NEC1 interacts with the newly formed capsid through the vertexes and directs it to the inner nuclear membrane by associating with NEC2. Induces the budding of the capsid at the inner... |
P09280 | MSRRTYVRSERRRGCGDNLLQRIRLVVPSALQCCDGDLPIFDPQRPPARCVFQFNGEDNVSEAFPVEYIMRLMANWAQVDCDPYIKIQNTGVSVLFQGFFFRPTNAPVAEVSIDSNNVILSSTLSTGINLSALESIKRGGGIDRRPLQALMWVNCFVRMPYVQLSFRFMGPEDPSRTIKLMARATDAYMYKETGNNLDEYIRWRPSFRSPPENGSPNTSVQMQSDIKPALPDTQTTRVWKLALPVANVTYALFIVIVLVVVLGAVLFWK | Function: Plays an essential role in virion nuclear egress, the first step of virion release from infected cell. Within the host nucleus, NEC1 interacts with the newly formed capsid through the vertexes and directs it to the inner nuclear membrane by associating with NEC2. Induces the budding of the capsid at the inner... |
P0DO52 | MATMAILQRTFSFILIFSIALHLKSLFAMETDSGAELKYLELIHEANEFTPDEEYDYIVVGGGTAGCPLAATLSENYSVLVLERGGDQHSHPNIIRQENVANNALPADDENSPSQAFTSEDGVPGLVRGRVLGGSSMINFGFYSRGDDYFFKNTGIEWDMDSVKTAYEWVEETLVHRPDNVSTWESSVRDALLEVGVLPDNGNTLDHLVGTKVSGSTFDSTGNRHGAVELLNKANPNNLRVIVHATVDRIIFSSSESSGPSVVRVVYHDSHGKSYQVGIRENGEVILSAGAFGSPQLLLVSGVGPSQNLTSLEIPVVHDQ... | Function: Involved in the production of blood-red nectar containing the alkaloid nesocodin and that serves as a visual attractant for pollinator visitation, including vertebrates such as Phelsuma geckos . The nectar is initially acidic and pale yellow, but slowly becomes alkaline before turning into red within 24 hours... |
Q84UV8 | MRMAAITKMLFISFLFLSSVFLARSGEVDDESEFSYDEKSENGPANWGNIRPDWKECSGKLQSPIDIFDLRAEVVSNLRILQKDYKPSNATLLNRGHDIMLRLDDGGYLKINETQYQLKQLHWHTPSEHTINGERFNLEAHLVHESNNGKFVVIGIVYEIGLWPDPFLSMIENDLKVPANKKGIERGIGIIDPNQIKLDGKKYFRYIGSLTTPPCTEGVVWIIDRKVKTVTRRQIKLLQEAVHDGFETNARPTQPENERYINSTYHSFGIEKQQ | Function: Bifunctional enzyme which has both carbonate dehydratase and monodehydroascorbate reductase activities. May be involved in regulation of nectar pH. May also regulate nectar ascorbate concentration, protecting floral tissues from free radical damage.
PTM: Proteolytically cleaved to produce a shorter protein, n... |
Q9SLI2 | MEQYEFLEQIGKGSFGSALLVRHKHEKKKYVLKKIRLARQTQRTRRSAHQEMELISKMRHPFIVEYKDSWVEKACYVCIVIGYCEGGDMAQAIKKSNGVHFQEEKLCKWLVQLLMGLEYLHSNHILHRDVKCSNIFLTKEQDIRLGDFGLAKILTSDDLTSSVVGTPSYMCPELLADIPYGSKSDIWSLGCCIYEMAYLKPAFKAFDMQALINKINKTIVSPLPAKYSGPFRGLVKSMLRKNPEVRPSASDLLRHPHLQPYVLDVKLRLNNLRRKTLPPELPSSKRIMKKAHFSEPAVTCPAFGERQHRSLWNDRALNPE... | Function: May be involved in plant development processes.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 68836
Sequence Length: 612
EC: 2.7.11.1
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Q9CAU7 | MENYEVLEQIGKGSFGSALLVRHKHEKKLYVLKKIRLARQTGRTRRSAHQEMELISKIHNPFIVEYKDSWVEKGCYVCIIIGYCKGGDMAEAIKKTNGVHFTEEKLCKWLVQILLALEYLHANHILHRDVKCSNIFLTKDQDIRLGDFGLAKVLTSDDLASSVVGTPSYMCPELLADIPYGSKSDIWSLGCCMYEMTAMKPAFKAFDMQGLINRINRSIVPPLPAQYSAAFRGLVKSMLRKNPELRPSAAELLRQPLLQPYIQKIHLKVNDPGSNVLPAQWPESESARRNSFPEQRRRPAGKSHSFGPSRFRGNLEDSVS... | Function: May be involved in plant development processes.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 68035
Sequence Length: 606
EC: 2.7.11.1
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Q55BN8 | MDQYEILGALGKGSFGVVSKIKRKEDGRVLVWKEICYENMQEKEKQLLVNEVNILQKLKHQNIVRYYDRIIDKPSSRLYIIMEHCSGGDLSQLIKKCRNERTYMDEEVIWRTLLQILSALQEIHNRKDGVILHRDIKPGNLFLDENKNIKLGDFGLAKILNESLYAHTFVGTPYYMSPEQIHGLKYNERSDVWSVGCLIYEMATLSPPFEATNQAQLTSKIQVGRYNPIPSQYSEHLSKVISLMINVDPKSRPNVNELLGYSFISFKVKERKLNIYYQGLKQMDEDLKIKEKKLSDIERDLQVKEQHLLLREQQINQREK... | Function: Involved in centrosome biogenesis. Seems to be required for recruitment of centrosomal material and might be involved in de novo centrosome formation.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 48933
Sequence Length: 418
EC: 2.7.11.1
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P51955 | MPSRAEDYEVLYTIGTGSYGRCQKIRRKSDGKILVWKELDYGSMTEAEKQMLVSEVNLLRELKHPNIVRYYDRIIDRTNTTLYIVMEYCEGGDLASVITKGTKERQYLDEEFVLRVMTQLTLALKECHRRSDGGHTVLHRDLKPANVFLDGKQNVKLGDFGLARILNHDTSFAKTFVGTPYYMSPEQMNRMSYNEKSDIWSLGCLLYELCALMPPFTAFSQKELAGKIREGKFRRIPYRYSDELNEIITRMLNLKDYHRPSVEEILENPLIADLVADEQRRNLERRGRQLGEPEKSQDSSPVLSELKLKEIQLQERERAL... | Function: Protein kinase which is involved in the control of centrosome separation and bipolar spindle formation in mitotic cells and chromatin condensation in meiotic cells. Regulates centrosome separation (essential for the formation of bipolar spindles and high-fidelity chromosome separation) by phosphorylating cent... |
P51956 | MDDYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCDGGDLMQKIKQQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAFACTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCISPLPSHYSYELQFLVKQMFKRNPSHRPSATTLLSRGIVARLVQKCLPPEIIMEYGEEVLEEIKNSKHNTPRKKTNPSRIRIALGNEASTVQEEEQDRKGSH... | Function: Protein kinase which influences neuronal morphogenesis and polarity through effects on microtubules. Regulates microtubule acetylation in neurons. Contributes to prolactin-mediated phosphorylation of PXN and VAV2. Implicated in prolactin-mediated cytoskeletal reorganization and motility of breast cancer cells... |
Q9R0A5 | MDNYTVLRVIGQGSFGRALLVLQESSNQTFAMKEIRLLKSDTQTSRKEAVLLAKMKHPNIVAFKESFEAEGYLYIVMEYCDGGDLMQRIKQQKGKLFPEDTILNWFIQICLGVNHIHKRRVLHRDIKSKNVFLTHNGKVKLGDFGSARLLSSPMAFACTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCALKHPFQANSWKNLILKICQGPIHPLPALYSCKLQGLVKQMLKRNPSHRPSATTLLCRGSLAPLVPKCLPPQIIREYGEQILDEIKISTPKNMKKQDSNRVRRALGEANSASMQEEERGRKCSHTE... | Function: Protein kinase which influences neuronal morphogenesis and polarity through effects on microtubules. Regulates microtubule acetylation in neurons. Contributes to prolactin-mediated phosphorylation of PXN and VAV2.
PTM: Phosphorylation at Thr-477 regulates its catalytic activity.
Catalytic Activity: ATP + L-se... |
Q6ZEZ5 | MEQYEVLEQIGKGSFGSALLVRHKVEKKRYVLKKIRLARQTDRCRRSAHQEMELIAKVRNPYIVEYKDSWVEKGCYVCIVIGYCEGGDMSEAIKKANSNYFSEERLCMWLVQLLMALDYLHVNHILHRDVKCSNIFLTKDQNIRLGDFGLAKVLTSDDLTSSVVGTPSYMCPELLADIPYGSKSDIWSLGCCLYEMTALKPAFKAFDMQTLINKISKSVLAPLPTIYSGAFRGLIKSMLRKSPDHRPSAAELLKHPHLQPFVLELQLKSSPARNLFPDTNKASCSDDENNWKAKYSKSHSFKVDRIVKVDKVAANNGHPS... | Function: May be involved in plant development processes (Probable). May function downstream of DCW11 in retrograde signaling from the mitochondria to the nucleus. Seems to be involved in the mechanism of cytoplasmic male sterility (CMS) occurrence .
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-... |
P51957 | MPLAAYCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAAEQEAQLLSQLKHPNIVTYKESWEGGDGLLYIVMGFCEGGDLYRKLKEQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCDMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLPPMPRDYSPELAELIRTMLSKRPEERPSVRSILRQPYIKRQISFFLEATKIKTSKNNIKNGDSQSKPFATVVSGEAESNHEVIHPQPLSSEGSQTYI... | Function: Protein kinase that seems to act exclusively upon threonine residues (By similarity). Required for normal entry into proliferative arrest after a limited number of cell divisions, also called replicative senescence. Required for normal cell cycle arrest in response to double-stranded DNA damage.
Catalytic Act... |
P0C566 | MNENIAEKFRADGVARPNWSAVFAVAFCVACLITVEFLPVSLLTPMAQDLGISEGVAGQSVTVTAFVAMFSSLFITQIIQATDRRYIVILFAVLLTASCLMVSFANSFTLLLLGRACLGLALGGFWAMSASLTMRLVPARTVPKALSVIFGAVSIALVIAAPLGSFLGGIIGWRNVFNAAAVMGVLCVIWVVKSLPSLPGEPSHQKQNMFSLLQRPGVMAGMIAIFMSFAGQFAFFTYIRPVYMNLAGFDVDGLTLVLLSFGIASFVGTSFSSYVLKRSVKLALAGAPLLLALSALTLIVWGSDKTVAAAIAIIWGLAFA... | Function: Involved in the efflux of purine ribonucleosides, such as inosine and guanosine.
Catalytic Activity: H(+)(out) + inosine(in) = H(+)(in) + inosine(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 41690
Sequence Length: 397
Subcellular Location: Cell inner membrane
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Q18673 | MYTRFGPPIVFLISCYALILCGTVDALPRAPYFNDDINKTTTTSEDKTVGNTVVEEEKKTYTVGDSEGYQEASRLLQKSLNLSLDPCDDFFEYACRAWVDSHPIPDDLTSYSQFTATREKVLAEMRKLYEDNTSIPTSKSIALIKQIYNTCMDTEKHNAVGARDLLEKIKTYGYWPMVHNEKWRESTFDLTKLLSNTIQSRDVSVFFDFGPAEDSRNVSRRLLSFDQGSLGLGYSTRDYYLDEKKYEKQMKAYRKYTIGKVRYYTEDAGMAVNESKIESDVDEIIAFEKEWAQILVAEEDRRNYTKLYNVRRFDDLKEYM... | Cofactor: Binds 1 zinc ion per subunit.
Function: Probable cell surface protease. Required to control the neuronal innervation of pharyngeal pumping.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 86945
Sequence Length: 754
Subcellular Location: Membrane
EC: 3.4.24.-
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P84883 | AQENETNESGSID | PTM: This peptide displays a high degree of glycan microheterogeneity resulting mainly from a variable number of mannose residues in each glycan. Both N-linked and O-linked glycans are high mannose.
Location Topology: Lipid-anchor
Sequence Mass (Da): 1393
Sequence Length: 13
Subcellular Location: Cell membrane
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Q8TDF5 | MIHGRSVLHIVASLIILHLSGATKKGTEKQTTSETQKSVQCGTWTKHAEGGIFTSPNYPSKYPPDRECIYIIEAAPRQCIELYFDEKYSIEPSWECKFDHIEVRDGPFGFSPIIGRFCGQQNPPVIKSSGRFLWIKFFADGELESMGFSARYNFTPDPDFKDLGALKPLPACEFEMGGSEGIVESIQIMKEGKATASEAVDCKWYIRAPPRSKIYLRFLDYEMQNSNECKRNFVAVYDGSSSVEDLKAKFCSTVANDVMLRTGLGVIRMWADEGSRNSRFQMLFTSFQEPPCEGNTFFCHSNMCINNTLVCNGLQNCVYP... | Function: Involved in the development and/or maintenance of neuronal circuitry. Accessory subunit of the neuronal N-methyl-D-aspartate receptor (NMDAR) critical for maintaining the abundance of GRIN2A-containing NMDARs in the postsynaptic density. Regulates long-term NMDA receptor-dependent synaptic plasticity and cogn... |
Q8R4I7 | MIYGRSLFHIIASLIILHSSGATKKGTEKQITPETQKSVQCGTWTKHAEGGVFTSPNYPSKYPPDRECVYIIEAAPRQCIELYFDEKYSIEPSWECKFDHIEVRDGPFGFSPIIGRFCGQQNPPVIKSSGRFLWIKFFADGELESMGFSARYNFTPDPDFKDLGVLKPLPACEFEMGGPEGIVESIQILKEGKASASEAVDCKWYIRAPPRSKIYLRFLDYEMQNSNECKRNFVAVYDGSSSVEDLKAKFCSTVANDVMLRTGLGVIRMWADEGSRNSRFQMLFTSFQEPPCEGNTFFCHSNMCINNTLVCNGLQNCVYP... | Function: Involved in the development and/or maintenance of neuronal circuitry. Accessory subunit of the neuronal N-methyl-D-aspartate receptor (NMDAR) critical for maintaining the abundance of GRIN2A-containing NMDARs in the postsynaptic density. Regulates long-term NMDA receptor-dependent synaptic plasticity and cogn... |
Q8NC67 | MALERLCSVLKVLLITVLVVEGIAVAQKTQDGQNIGIKHIPATQCGIWVRTSNGGHFASPNYPDSYPPNKECIYILEAAPRQRIELTFDEHYYIEPSFECRFDHLEVRDGPFGFSPLIDRYCGVKSPPLIRSTGRFMWIKFSSDEELEGLGFRAKYSFIPDPDFTYLGGILNPIPDCQFELSGADGIVRSSQVEQEEKTKPGQAVDCIWTIKATPKAKIYLRFLDYQMEHSNECKRNFVAVYDGSSSIENLKAKFCSTVANDVMLKTGIGVIRMWADEGSRLSRFRMLFTSFVEPPCTSSTFFCHSNMCINNSLVCNGVQ... | Function: Accessory subunit of neuronal kainate-sensitive glutamate receptors, GRIK2 and GRIK3. Increases kainate-receptor channel activity, slowing the decay kinetics of the receptors, without affecting their expression at the cell surface, and increasing the open probability of the receptor channels. Modulates the ag... |
C6K2K4 | MALEQLCAVLKVLLITVLVVEGIAVAQKTQDGQNIGIKHVPATQCGIWVRTSNGGHFASPNYPDSYPPNKECIYILEAAPRQRIELTFDERYYIEPSFECRFDHLEVRDGPFGFSPLIDRYCGMKSPALIRSTGRFMWIKFSSDEELEGLGFRAKYSFIPDPDFTYLGGILNPIPDCQFELSGADGIVRSSQVEQEEKTKPGQAVDCIWTIKATPKAKIYLRFLDYQMEHSNECKRNFVAVYDGSSAIENLKAKFCSTVANDVMLKTGVGVIRMWADEGSRLSRFRMLFTSFVEPPCTSSTFFCHSNMCINNSLVCNGVQ... | Function: Accessory subunit of neuronal kainate-sensitive glutamate receptors, GRIK2 and GRIK3. Increases kainate-receptor channel activity, slowing the decay kinetics of the receptors, without affecting their expression at the cell surface, and increasing the open probability of the receptor channels. Modulates the ag... |
Q5G270 | MTLARFVLALMLGALPEVVGFDSVLNDSLHHSHRHSPPPGPHYPSYYLPTQQRPPRTRPPPPLPRFPRPPRALPAQRPHALQAGHTPRPHPWGCPAGEPWVSVTDFGARCLRWAEVPPFLERSPPASWAQLRGQRHNFCRSPDGAGRPWCFYGDARGKVDWGYCDCRHGSVRLRGGKNEFEGTVEVYASGVWGTVCSSHWDDSDASVICHQLQLGGKGIAKQTPFSGLGLIPVYWSNVRCRGDEENILLCEKDIWQGGVCPQKMAAAVTCSFSHGPTFPIIRLAGGSSVHEGRVELYHAGQWGTVCDDQWDDADAEVICR... | Function: Plays a role in neuronal plasticity and the proteolytic action may subserve structural reorganizations associated with learning and memory operations.
Sequence Mass (Da): 97259
Sequence Length: 876
Subcellular Location: Secreted
EC: 3.4.21.-
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P56730 | MTLARFVLALMLGALPEVVGFDSVLNDSLHHSHRHSPPAGPHYPYYLPTQQRPPRTRPPPPLPRFPRPPRALPAQRPHALQAGHTPRPHPWGCPAGEPWVSVTDFGAPCLRWAEVPPFLERSPPASWAQLRGQRHNFCRSPDGAGRPWCFYGDARGKVDWGYCDCRHGSVRLRGGKNEFEGTVEVYASGVWGTVCSSHWDDSDASVICHQLQLGGKGIAKQTPFSGLGLIPIYWSNVRCRGDEENILLCEKDIWQGGVCPQKMAAAVTCSFSHGPTFPIIRLAGGSSVHEGRVELYHAGQWGTVCDDQWDDADAEVICRQ... | Function: Plays a role in neuronal plasticity and the proteolytic action may subserve structural reorganizations associated with learning and memory operations.
Sequence Mass (Da): 97067
Sequence Length: 875
Subcellular Location: Secreted
EC: 3.4.21.-
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O08762 | MALARCVLAVILGALSVVARADPVSRSPLHRPHPSPPRSQHAHYLPSSRRPPRTPRFPLPLRIPAAQRPQVLSTGHTPPTIPRRCGAGESWGNATNLGVPCLHWDEVPPFLERSPPASWAELRGQPHNFCRSPDGSGRPWCFYRNAQGKVDWGYCDCGQGPALPVIRLVGGNSGHEGRVELYHAGQWGTICDDQWDNADADVICRQLGLSGIAKAWHQAHFGEGSGPILLDEVRCTGNELSIEQCPKSSWGEHNCGHKEDAGVSCVPLTDGVIRLAGGKSTHEGRLEVYYKGQWGTVCDDGWTEMNTYVACRLLGFKYGK... | Function: Plays a role in neuronal plasticity and the proteolytic action may subserve structural reorganizations associated with learning and memory operations.
Sequence Mass (Da): 84118
Sequence Length: 761
Subcellular Location: Secreted
EC: 3.4.21.-
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O66824 | MNTELLEKLKKIQLECAKKVIARDDFEKVETIGGMDLTFEKINENPTRAWASLVVVELKTLKPVYQHVVKDIVDFPYIPTFLAFREMPLLLKLYETAKVKPDVYFIDGQGIAHPRGCGIASHFGVETGEVTVGVAKSKLFGYAKEPAPQRGSYTYLKYKGKIIGAVVRTKDNTAPVYVSVGHRISLKTAIDLVLKTSKYRVPEPTRLAHNLLQVVRRKELRR | 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'-... |
O30108 | MLQMNLEELRRIQEEMSRSVVLEDLIPLEELEYVVGVDQAFISDEVVSCAVKLTFPELEVVDKAVRVEKVTFPYIPTFLMFREGEPAVNAVKGLVDDRAAIMVDGSGIAHPRRCGLATYIALKLRKPTVGITKKRLFGEMVEVEDGLWRLLDGSETIGYALKSCRRCKPIFISPGSYISPDSALELTRKCLKGYKLPEPIRIADKLTKEVKRELTPTSKLK | 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. Recognizes only deoxyinosine.
Catalytic Activity: Endonucleolytic cleavage at apurinic or apyrimidini... |
P96724 | MKVFDVHKFDMKKEQDFLQVQFNLKNRINLSPTIHPDSINTCAGVDLAYWEQDGEPYGVCCIIVIDADTKEVIEKVHSMGRISVPYVSGFLAFRELPLIIEAAKKLETEPDVFLFDGNGYLHYNHMGVATHAAFFLGKPTIGIAKTYLKIKGCDFVTPEIEVGAYTDIIIDGEVYGRALRTRRDVKPIFLSCGNYIDLDSSYQITMSLINQESRLPIPVRLADLETHVLRTFYQKNHV | 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'-... |
Q97M37 | MKTVNVHGFEASSKEEFQVIQSSLVKRIKLISDFKEEDIKLCAGVDLAYWTKGEKQYGVCCIIVIDYNTGEIIEKAYDYGEIEVPYMPGFLAFRELPLVIKTVKKLKNEPDIFMFDGNGYLHYNHMGIATHASFFLNKPTIGVAKSYLKVAGVDFEMPESFEGAFKDIVINEEVYGRVLRTKKDVKPIFVSCGNYIDLETCTKICSKLINNDSRLPITVRLADLETHKRRSELS | 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'-... |
Q3ZWY7 | MNVKIKKLHNWDMTPTEAILLQRELAQKVSACGTLSSISLVAGADVWHSRTSGMGRAAVVVLSYPDMNLVEVSRSEGDCHIPYIPGLLSFREMPLLLSAFEGLESMPDFILMDGQGLAHPRRLGIASHLGLFLNKPVIGCAKSRLVGEYAPLADEAGSYSDLYHNSQLVGRVLRTRRGVNPLFISVGHKICLEEACSRVADCCRGYRLPEPLRHAHLAAAQLI | 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'-... |
B8D509 | MGFDYQRAVMLQRILSERVLAELDSFPRIDPSRIRSVAGVDASYRGGVQVGSAVLMDYRAKMPLAYTCLTSKPPIPYVPGLLAFREAPVYIKALHRLPAKPDIILVDGHGLSHPRAFGIATHIGLVLSTPSIGVAKKPLYGEVEEVNGRKLVRAHGRIVGEVVETNQGSEIYVSIGYLIRLEDAVEVVRHLMEPGLKLPLPIHLADNYSRSKCIKELRL | 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'-... |
B8DZX0 | MDWGREFFKWRGYEETVKLQEELSKKIILEDKFKELRYIGGVDTSSLGEKIVGIITILVFKTLELVEISVALSEVNFPYIPGFLSFREGPVILRAWEKLKIKPDLLIFDGQGIAHPRRLGIASHIGYVLDVPSIGCAKNILVGFYKEPDKRKGSFEYIYHKGEIVGAAVRTKDNVKPVFVSLGHKISLNTSIDIILKTSTKYRIPEPVRLAHLYSKRMLNSEIEGEPF | 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'-... |
Q2NWR1 | MDIAVLRAEQIATEGKVIRHDDFAFSQPGLIAGADVGFEQGGEVTRAAIALLRFPSLELVEFQVARVTTTMPYIPGFLSFREYPALLAAWDKLGHRPDLLLVDGHGISHPRRLGVASHFGLLVDTPTIGVAKRRLCGKFAPLAEAQGALAPLMDKGEQLAWVWRSKLRCNPLFISTGHRVGLASALHWVQLCMRGYRLPEPTRWADAVASNRTAFKRWQQEREEADFFPPQ | 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'-... |
Q82MH6 | MTTVRIPAGWPATEEEARAVQDELRGRVILDEPGPPPGTGRVTGVDVAYDDERDVVVAAAVVLDAATLDVVAEATAVGEVSFPYVPGLLAFREIPTVLAALDALPCPPGLIVCDGYGVAHPRRFGLASHLGVLTGLPTIGVAKNPFTFSYEDPGAPRGSAAPLLAGADEVGRALRTQSGVKPVFVSVGHRVDLDHACAHTLALTPKYRIPETTRRADSLCRRALKEATA | 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'-... |
Q6DHR8 | MASLYEMVWRFLHALLYLQRAIVAWFRVHIWRWKLAVVDLLLPLALGFHNQKKTGPKGTRTSRRVRWGADGRTLEKLPLHVGLLVTEEEIHYTDIANLVVWCMAVGISYVSVYDNQGVFKRNNSRLMEEILKQQQELLGMGSSKYSVEILKNGTNKQEHQVLSCQSMVKVLSPDDGRLSIVQAAQQLCRAVEQKEKTSKDINVSVLDSLLKESKNIPDPDLVLKFGTVQSTLGFLPWHIRLTEIISMPSHIDASYDDLYDALQRFAGCEQRLGK | Function: With DHDDS, forms the dehydrodolichyl diphosphate synthase (DDS) complex, an essential component of the dolichol monophosphate (Dol-P) biosynthetic machinery. Adds multiple copies of isopentenyl pyrophosphate (IPP) to farnesyl pyrophosphate (FPP) to produce dehydrodolichyl diphosphate (Dedol-PP), a precursor ... |
Q96E22 | MTGLYELVWRVLHALLCLHRTLTSWLRVRFGTWNWIWRRCCRAASAAVLAPLGFTLRKPPAVGRNRRHHRHPRGGSCLAAAHHRMRWRADGRSLEKLPVHMGLVITEVEQEPSFSDIASLVVWCMAVGISYISVYDHQGIFKRNNSRLMDEILKQQQELLGLDCSKYSPEFANSNDKDDQVLNCHLAVKVLSPEDGKADIVRAAQDFCQLVAQKQKRPTDLDVDTLASLLSSNGCPDPDLVLKFGPVDSTLGFLPWHIRLTEIVSLPSHLNISYEDFFSALRQYAACEQRLGK | Function: With DHDDS, forms the dehydrodolichyl diphosphate synthase (DDS) complex, an essential component of the dolichol monophosphate (Dol-P) biosynthetic machinery. Both subunits contribute to enzymatic activity, i.e. condensation of multiple copies of isopentenyl pyrophosphate (IPP) to farnesyl pyrophosphate (FPP)... |
A6H0G8 | MKITGLFKEFFESEKSSGLFLISCTLFSLVIANSAIANSYLHFWHANLAGNSLEYWINDGLMTIFFLLIGLELEREVYDGELSNIKDAMLPIFGAIGGMIVPAGLFLVMNFGTKTQSGAGIPMATDIAFALAILSLLGNKIPLSLKIFLTALAVIDDLGAILIIAVFYTKTLLWTNLCIALGIFGFLLILNRLKIRNLIPYLIGGVFMWYFMLHSGVHATITGVLLAFAIPFGNGDSRSTSYILQHFLHKPVAFFILPLFALANTAIVLSSNISETLIQNYSIGIALGLIIGKPLGIFLLSMLAVSLGICKLPDDLNWKS... | 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): 41843
Sequence Length: 384
Subcellular Location: Cell inner membrane
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Q5FNE6 | MTAPFVPAAAHVRRFLKSSAGGAFFLLLASLAGFVLANSPWAAGYRTLTTLPLKFPFLGKRGPDNVAAWVSDGLMTLFFLVVILEIKKEIVSGHLSSLRRVALPLIGAVGGMVVPALTYLLVTWGHPEATSGWAIPVATDAAFTLPIILALGRRVSPGARAWLMALAIFDDVLGIVVIALFYGGSMYWPALLAVVLVTAALIGANRGRIRTLWAYGTGGILLWTALLDSGLHPTLAGVITGLCLPAGDAKGAATLDWVSSAVTPLVTWIVLPLFGFMNVGMSAAGMKPDMMLEAVPLGIMLGLMLGKPVGVFGATLLSIR... | 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): 42239
Sequence Length: 403
Subcellular Location: Cell inner membrane
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Q0BSV4 | MQNRHHARLLPSSALLSHEAAAGVMLMAASAIGMVFANSIWQASYEYWLNIETGPLTMRGWINDALMALFFLLAGLEIKREILYGHLSHWSQRLLPGVAAIGGMVVPAIIYVAFNHSGEALRGWAIPTATDIAFALGVLALAGSRVPGILKVFLTALAIVDDLGAVIVIALFYTGTLSVLPGAGVAAILGLLLMLNRQGVRTLFPYLLAGVPLWWLTLKSGIHPTVAGVGLALLIPAGHDEASPLMRLEHMLSWPVRFVILPLFGFANAGISLHGVTVGQMLSPLTLGVGAALMLGKPLGVLGAVSILQLSGASGFPPYI... | 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): 40361
Sequence Length: 383
Subcellular Location: Cell inner membrane
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Q8FI24 | MEISWGRALWRNFLGQSPDWYKLALIIFLIVNPLIFLISPFVAGWLLVAEFIFTLAMALKCYPLLPGGLLAIEAVFIGMTSAEHVREEVAANLEVLLLLMFMVAGIYFMKQLLLFIFTRLLLSIRSKMLLSLSFCVAAAFLSAFLDALTVVAVVISVAVGFYGIYHRVASSRTEDTDLQDDSHIDKHYKVVLEQFRGFLRSLMMHAGVGTALGGVMTMVGEPQNLIIAKAAGWHFGDFFLRMSPVTVPVLICGLLTCLLVEKLRWFGYGETLPEKVREVLQQFDDQSRNQRTRQDKIRLIVQAIIGVWLVTALALHLAEV... | Function: Na(+)/H(+) antiporter that extrudes sodium in exchange for external protons.
Catalytic Activity: 3 H(+)(out) + 2 Na(+)(in) = 3 H(+)(in) + 2 Na(+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 56705
Sequence Length: 513
Subcellular Location: Cell inner membrane
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C5B9W2 | MTITYTQAFAKNFLGNAPGWYKIAILAFLIINPLVFSLSPFYAGWLLVIEFIFTLAMALKCYPLQPGGLLALEAVFIGMTSPEKIAHEVAANLEVLLLLIFMVAGIYFMKQLLLFVFTKLLLNIRSKIVLSLAFCLAAAFLSAFLDALTVIAVVISVAVGFYGIYHQVASGGGSNVALSDDSLLTDSAKRDALDQFRAFLRSLLMHAGVGTALGGVMTMVGEPQNLIIAKNADWHFVSFLLRMAPVTVPVFCCGILTCYLVERFSLFGYGAQLPDRVRQILLNFDRESTNSRSRQDKLRLMIQALVGVWLVSALAFHLAE... | Function: Na(+)/H(+) antiporter that extrudes sodium in exchange for external protons.
Catalytic Activity: 3 H(+)(out) + 2 Na(+)(in) = 3 H(+)(in) + 2 Na(+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 57119
Sequence Length: 524
Subcellular Location: Cell inner membrane
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Q87KV8 | MDADTINSFFLIGALLIALSVLLSPVSSKLGIPILLVFLAVGMLAGEDGLGGILFDNYSIAYLVSNLALAIILLDGGMRTRVASFRVALWPSVSLATIGVAITTLLTGLMATWLFDLDLLQGILVGAIVGSTDAAAVFSLLKGRSLNERVGSTLEIESGTNDPMAVFLTVTLIAILSSTGTGLSAGFLALSFVKQFGIGALLGFAGGWVLWKVINRNQLPDGLYSILTVSGGLIIFALSNSLGGSGILSIYLVGLLLGNRPTRSRHSILHVLDGMTWLAQIGMFLVLGLLVTPSNLLSIAVPGLALAFGMILFARPISVW... | Function: K(+)/H(+) antiporter that extrudes potassium in exchange for external protons and maintains the internal concentration of potassium under toxic levels.
Catalytic Activity: H(+)(out) + K(+)(in) = H(+)(in) + K(+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 62639
Sequence Length: 581
... |
Q0ZAH6 | MEAINLTILVIGVLFLISIVATLISSRIGAPILLVFLIIGMLAGEQGLGGITFNNPQVAFLIGSIALVIILFDGGMRTHPERFRVALAPAAMLATLGVVVTCTVTGLAAAWILGLHWLQGLLLGAILSSTDAAAVFSIFQSRGIRIKDRVASTLEIESGSNDPMAVMLTITLVGVLAEYTALDWSVLIVFLKQAIIGGAVGYGAGRLFVFLCRKLPLSFAFFPLMAVACCISVYAVTTQFEGSGFLAVYLMGYFVGNARLPQVLYILRVHDGLAWLSQIVMFLMLGLLVVPSQLLDHLLPALAIAGVLIFIARPLAVLLS... | Function: K(+)/H(+) antiporter that extrudes potassium in exchange for external protons. Can also catalyze NH(4)(+)/H(+) antiport. Could have weak activity with Na(+).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 62268
Sequence Length: 574
Subcellular Location: Cell inner membrane
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G3XD29 | MLDLVAAFIALTTLLTYVNYRFIRLPPTIGVMATALVFSLIVQGLSELGYPILEVEMQEIIRRIDFSEVLMTWFLPALLFAGALHVDLSDLRSYKWPIGLLATAGVLIATFVIGGLAYYTFPLFGWQVDFIYCLLFGALISPTDPIAVLGILKSAGAPKPLATTIVGESLFNDGTAVVVFAIILGILQLGEAPTVSATAILFVQEAIGGVVFGAVLGYGVFVMMRGIDQYQVEVMLTLALVIGGAALAARLHVSAPIAMVVAGLIIGNHGRHYAMSDETRRYVDKFWELIDEILNALLFALIGLELLLLPFSWLHVAAAF... | Function: Na(+)/H(+) antiporter that extrudes sodium in exchange for external protons. Has also weak Li(+)/H(+) antiport activity.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 45486
Sequence Length: 424
Subcellular Location: Cell inner membrane
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P73863 | MDTAVNESLSISYNLEQFLIVLSVSLSIATLSKTVPILRKIPYTLLLVIVGMALAFVDVKLINLSPELIMEIFLPPLLFEAAWNLQWRNLKENWFPITLFATLGVVICVVGIAFPLSYWGGMELAIAFLAAAALSATDPVSVIALFKELGASKKLNTLMEGESLFNDGVAVVVFLILVGIPLGTSTFDLSVTLARFVTVIGIGVGCGLVIGFSLSLLTQRFDLPFVEQSLTLVSAYGAYILAENLGGSGVIGVVVVGMVLGNYGSRIGMNPRTRLIVSIFWEFVAFFVNSIIFLLIGDQIGLSSLSDHLNLILIAIAAVV... | Function: Na(+)/H(+) antiporter that extrudes sodium in exchange for external protons. Might be able to function at relatively high concentrations of Na(+) ions. Has also Li(+)/H(+) antiport activity under K(+)-rich conditions, but it might not have any physiological relevance.
Location Topology: Multi-pass membrane pr... |
P74393 | MIKLPVLLADINIQSLPTEPELILNNLAITTLVENLIILLLVATLVALVARWLKIPYVIGLVLAGLAIPRGLSVGLNPELILNFFLPILIFEAAINTDISRLRSTIKPITVLAGPGVVISAAITAVLLKIGLGLAWVTAAGVSVILTITDTVSVIAAFRSVPVPRRLATIVEGESMLNDGVAMVLLSVITTIHIQGGFSAGEGIRQIFVAFVGGGLVGLGLGYLCVGLFRQLNDDLSDILLTVSVSLGTFQIGQMLGVSSAIAVVVAGLVIGNLALKQTSASIKVTLLSFWEYAGFGVNTLIFLLVGIEVYPSILLSTIP... | Function: Required for Na(+) uptake into the cell, especially at low external Na(+) concentrations or low Na(+)/K(+) ratios. May be part of a sodium cycle that permits re-entry of sodium into the cell.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 58117
Sequence Length: 540
Subcellular Location: Ce... |
Q55190 | MFMNPLLPPLWPMIATAVETETEIAPLVLAGVLLSLVVIYFASKLGGEVCLRLNLPPVLGELVGGVLVGVSALKLLLFPEGGLAPEDSLVIQLLMGSADLSPEAAQSVFSAQSEVISVISELGVIILLFEIGLESNLKELIRVGPQAAIVAVVGVVTPFSLGTIGLMTIFGVAAIPAIFAGAALTATSIGITAKVLAEINRLSSNEGQIIIGAAVLDDILGIIVLAVVGSLVKTGEIQISNIIYLILSATGFVVGSILIGRLLSPFYVSLVNRMKTRGQLLLVSICVAFVLSYIAQIVQLEAILGSFAAGLILAETEKRE... | Function: Na(+)/H(+) antiporter that transports sodium from the cytoplasm into the thylakoid lumen in exchange for protons. Contributes to sodium homeostasis and tolerance. Has also Li(+)/H(+) antiport activity under K(+)-free conditions, but not under K(+)-rich conditions.
Location Topology: Multi-pass membrane protei... |
Q3YL57 | MTSIIGAALPYKSPEKAIASSSYSAENDSSPVDAVIFAGTSLVLGTACRYLFNGTRVPYTVVLLVIGIFLGSLEYGTKHNLGKLGHGIRIWNGINPDLLLAVFLPVLLFESSFSMDVHQIKRCMGQMVLLAGPGVLISTFCLGALIKLTFPYNWDWKTSLLLGGLLGATDPVAVVALLKELGASKKMTTLIDGESLMNDGVSVVVFQLFFKMVMGHNSDWGSIIKFLVQNSFGAVGIGLAFGIASVFWLKFIFNDTVAQITVTLSASYFAYYTAQEWAGVSGILTVMILGMFFAAFARTAFKGDSHQSLHHFWEMAAYIA... | Function: May act in low affinity electroneutral exchange of protons for cations such as Na(+) or K(+) across membranes. May also exchange Li(+) and Cs(+) with a lower affinity.
Catalytic Activity: H(+)(out) + Na(+)(in) = H(+)(in) + Na(+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 83476
Seq... |
P35449 | MSSRLFVFFLICYATADKIEKELISDGFQLFTWKWDDVHHVYVITVWLLIASLAKILFNLMKPISKWCPDSSLLIIVGLALGWILHQTSLSGATLDSHTFFLYLLPPIIFDAGYFMPNRALFENFDSVLVFSVFGTIWNTFAIGGSLLLMAQYDLFTMSFTTFEILVFSALISAVDPVAVIAVFEEIHVNEFLFINVFGEALFNDGVTVVLYQMFKSFALIGSENLSVLDYATGGLSFFVVALGGAAVGIIFAIAASLTTKYTYDVRILAPVFIFVLPYMAYLTAEMVSLSSIIAIAICGMLMKQYIKGNVTQAAANSVK... | Function: Serves some physiological function other than regulation of cellular pH.
PTM: Phosphorylated.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 75281
Sequence Length: 667
Subcellular Location: Cell membrane
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P11832 | MATSVDNRHYPTMNGVAHAFKPPLVPSPRSFDRHRHQNQTLDVILTETKIVKETEVITTVVDSYDDSSSDDEDESHNRNVPYYKELVKKSNSDLEPSILDPRDESTADSWIQRNSSMLRLTGKHPFNAEAPLPRLMHHGFITPVPLHYVRNHGAVPKANWSDWSIEITGLVKRPAKFTMEELISEFPSREFPVTLVCAGNRRKEQNMVKQTIGFNWGSAGVSTSLWKGIPLSEILRRCGIYSRRGGALNVCFEGAEDLPGGGGSKYGTSIKKEMAMDPARDIILAYMQNGELLTPDHGFPVRVIVPGFIGGRMVKWLKRI... | Cofactor: Binds 1 FAD per subunit.
Function: Nitrate reductase is a key enzyme involved in the first step of nitrate assimilation in plants, fungi and bacteria.
Catalytic Activity: H2O + NAD(+) + nitrite = H(+) + NADH + nitrate
Sequence Mass (Da): 103041
Sequence Length: 917
EC: 1.7.1.1
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P27967 | MAASVEPRQPFGRLDAPATAPTARAPGSNGIRRRADSPVRGCGFPSLISPPRKGPVAEEEEDDDDEDDEGHEDWREAYGSHLQLEVEPSTRDPRDEGTADAWIERNPSLIRLTGKHPLNCEPPLARLMHHGFITPAPLHYVRNHGAVPRGDWATWTVEVTGLVRRPARLTMDELANGFPAAEVPATLVCAGNRRKEQNMVQQTVGFNWGAAGVSTSVWRGARLRDVLLRCGVMSKKGQALNVCFEGAEDLPGGGGSKYGTSVSREWAMDPSRDIILPYAQNGEPLLPDHGYPVRVLIPGCIGGRMVKWVRRIVVTTAESD... | Cofactor: Binds 1 FAD per subunit.
Function: Nitrate reductase is a key enzyme involved in the first step of nitrate assimilation in plants, fungi and bacteria.
Catalytic Activity: H2O + NAD(+) + nitrite = H(+) + NADH + nitrate
Sequence Mass (Da): 101770
Sequence Length: 915
EC: 1.7.1.1
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P17571 | GFPVRVIIPGCIGGRMVKWLKRIIVTPAESDNYYHFKDNRVLPSHVDAELANAEAWWYKPEYIINELNINSVITTPCHDEILPINAFTTQRPYTLKGYAYSGGGKKVTRVEVTLDGGETWLVCTDHPEKPTKYGKYWCWCFWSLEVEVLDLLSAKEIAVRAWDESLNTQPEKLIWNVMGMMNNCWFRVKTNVCKPHKGEIGIVFDHPTLPGNESGGWMAKEKHLETAEAAAPGLKRSTSTPFMNTTDVGKEFTMSEVRKHASQESAWIVVHGHVYDCTKFLKDHPGGADSILINAGTDCTEEFDAIHSDKAKALLDTYRI... | Cofactor: Binds 1 FAD.
Function: Nitrate reductase is a key enzyme involved in the first step of nitrate assimilation in plants, fungi and bacteria.
Catalytic Activity: H2O + NAD(+) + nitrite = H(+) + NADH + nitrate
Sequence Mass (Da): 69773
Sequence Length: 621
EC: 1.7.1.1
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P16081 | MAASVQPRQFGHLEPGSAPVRGAASSNGAKAYPPANGIPRRADSPVRGCGFPPLVSPPPRKPPSDGSDDEEEEQEDWRELYGSHLQLEVEPPVRDARDEGTADAWIERNPSLIRLTGKHPLNCEPPLARLMHHGFITPAALHYVRNHGAVPRGDWSTWTVDVTGLVKRPMRLTMDELVNGFPAVEIPVTLVCAGNRRKEQNMVQQTVGFNWGAAGVSTSVWRGARLRDVLRRCGIMPSKGGALNVCFEGAEDLPGGGGSKYGTSITRQWALDPSRDIMLAYMQNGEPLLPDHGFPVRAIIPGCIGGRMVKWVKRIIVTTA... | Cofactor: Binds 1 FAD per subunit.
Function: Nitrate reductase is a key enzyme involved in the first step of nitrate assimilation in plants, fungi and bacteria.
Catalytic Activity: H2O + NAD(+) + nitrite = H(+) + NADH + nitrate
Sequence Mass (Da): 101513
Sequence Length: 916
EC: 1.7.1.1
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P11035 | MAASVDNRQYARLEPGLNGVVRSYKPPVPGRSDSPKAHQNQTTNQTVFLKPAKVHDDDEDVSSEDENETHNSNAVYYKEMIRKSNAELEPSVLDPRDEYTADSWIERNPSMVRLTGKHPFNSEAPLNRLMHHGFITPVPLHYVRNHGHVPKAQWAEWTVEVTGFVKRPMKFTMDQLVSEFAYREFAATLVCAGNRRKEQNMVKKSKGFNWGSAGVSTSVWRGVPLCDVLRRCGIFSRKGGALNVCFEGSEDLPGGAGTAGSKYGTSIKKEYAMDPSRDIILAYMQNGEYLTPDHGFPVRIIIPGFIGGRMVKWLKRIIVT... | Cofactor: Binds 1 FAD per subunit.
Function: Nitrate reductase is a key enzyme involved in the first step of nitrate assimilation in plants, fungi and bacteria.
Catalytic Activity: H2O + NAD(+) + nitrite = H(+) + NADH + nitrate
Sequence Mass (Da): 102844
Sequence Length: 917
EC: 1.7.1.1
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P39871 | PQKLGLPVGRHVYVCASIGGKLCMRAYTPTSPVDEVGHFDLLIKIYFKDEDPKYPNGGLMSQYLDSLPLGATIDIKGPHRHIEYTGRRRFVVNGKQRHARRLAMIQAGRGTTPDDDTEQAVLRDQPDDDTEMHLVYANRTDHDMLLREEIDRAWLPRTRRLKVWYVVSKVPEDGWEYGVGRVDEHVMREHLPLGDSETIALVCGPPAMIECTVRPGLEKMGYDLDKACLVF | Cofactor: Binds 1 FAD.
Function: Nitrate reductase is a key enzyme involved in the first step of nitrate assimilation in plants, fungi and bacteria.
Catalytic Activity: H2O + NAD(+) + nitrite = H(+) + NADH + nitrate
Sequence Mass (Da): 26254
Sequence Length: 231
EC: 1.7.1.2
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P27968 | MAASVEYNRQVSAHPWPTNAQPKAAFDLFSSSGGGRRRSGADSDSDDEDSVPPDWRSLYSPRLDVEPSVKDPRDEATSDAWVKRHPALVRLTGKHPFNSEPPLPRLMSHGFITPVPLHYVRNHGAVPKADWSTWTVEVTGLVKRPVKFTMEELVTGFQAVEFPVTLVCAGNRRKEQNMVRQSSGFNWGPGAISTTVWRGVRLRDVLRRCGVMGAGAASNVCFEGAEDLPGGGGCKYGTSLRRSVAMDPARDVILAYMQNGEPLAPDHGFPVRVIVPGFIGGRMVKWLKRIVVACNESESYYHYRDNRVLPSHVDAELANA... | Cofactor: Binds 1 FAD per subunit.
Function: Nitrate reductase is a key enzyme involved in the first step of nitrate assimilation in plants, fungi and bacteria.
Catalytic Activity: H2O + NAD(+) + nitrite = H(+) + NADH + nitrate
Sequence Mass (Da): 98630
Sequence Length: 891
EC: 1.7.1.2
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Q6FFF7 | MDLVSRIENLPIGKFHYTLLWVVGLGWMFDALDTGIIAFIMTTLVKDWALTPAESGWIVSIGFIGMALGAVFSGGLADRFGRKTVFATTLLIYSLATAACAFAPNLTWLLAFRFIVGLGLGGQLPVAVTLVSEYIPAHVRGRFIVLLESFWGLGWLVAALVSYFVIPHFGWHIAFLIGGLPAIYVYVIIKKVPESIPYLINRGRIDEAHELVQQIERHAGVPVIDTIVVKPVAQKQQVSFRQLWSGRFARRSLMLWLVWFGIVFSYYGIFTWLPSLLVKQGYSVVQSFEYVLIMILAQLPGYISAAWLVERLGRKATLAG... | Function: Functions as a high-affinity transporter of niacin (nicotinamide or nicotinate) . Probably substantially contributes to niacin transport when its concentration in the medium is very low .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 48407
Sequence Length: 439
Subcellular Location: Cell i... |
P08201 | MSKVRLAIIGNGMVGHRFIEDLLDKSDAANFDITVFCEEPRIAYDRVHLSSYFSHHTAEELSLVREGFYEKHGIKVLVGERAITINRQEKVIHSSAGRTVFYDKLIMATGSYPWIPPIKGSDTQDCFVYRTIEDLNAIESCARRSKRGAVVGGGLLGLEAAGALKNLGIETHVIEFAPMLMAEQLDQMGGEQLRRKIESMGVRVHTSKNTLEIVQEGVEARKTMRFADGSELEVDFIVFSTGIRPRDKLATQCGLDVAPRGGIVINDSCQTSDPDIYAIGECASWNNRVFGLVAPGYKMAQVAVDHILGSENAFEGADLS... | Cofactor: Binds 1 siroheme per subunit.
Catalytic Activity: 2 H2O + 3 NAD(+) + NH4(+) = 5 H(+) + 3 NADH + nitrite
Sequence Mass (Da): 93121
Sequence Length: 847
Pathway: Nitrogen metabolism; nitrate reduction (assimilation).
EC: 1.7.1.15
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Q06458 | MTKPVLVLVGHGMVGHHFLEQCVSRDLHQQYRIVVFCEERYAAYDRVHLTEYFAGRSAESLSLVEGDFFTQHGIELRLSESVASIDREARVVRDAFGHETHWDKLVLATGSYPFVPPVPGHNLEGCFVYRTLDDLDQIAARAATARRGVVIGGGLLGLEAANALKQLGLETHVVEFAPNLMAVQLDNGGAAMLREKISELGVGVHTSKATTEIVRNEQGLQLNFRDGSSLATDMLVFSAGIRPQDALARSGGLSVGERGGICIDNQCRTSDPDVLAIGECALWENKIYGLVAPGYQMAARRAATLAGEAGSFSGADMSTK... | Cofactor: Binds 1 siroheme per subunit.
Catalytic Activity: 2 H2O + 3 NADP(+) + NH4(+) = 5 H(+) + 3 NADPH + nitrite
Sequence Mass (Da): 104227
Sequence Length: 957
Pathway: Nitrogen metabolism; nitrate reduction (assimilation).
EC: 1.7.1.4
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P0AC26 | MFTDTINKCAANAARIARLSANNPLGFWVSSAMAGAYVGLGIILIFTLGNLLDPSVRPLVMGATFGIALTLVIIAGSELFTGHTMFLTFGVKAGSISHGQMWAILPQTWLGNLVGSVFVAMLYSWGGGSLLPVDTSIVHSVALAKTTAPAMVLFFKGALCNWLVCLAIWMALRTEGAAKFIAIWWCLLAFIASGYEHSIANMTLFALSWFGNHSEAYTLAGIGHNLLWVTLGNTLSGAVFMGLGYWYATPKANRPVADKFNQTETAAG | Function: Catalyzes nitrite uptake and nitrite export across the cytoplasmic membrane. Is up to 10-fold more active than NarK or NarU in nitrite uptake for subsequent reduction in the cytoplasm by the NirB/NirD nitrite reductase.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28563
Sequence Length: ... |
Q51702 | MARLALLLVLLAGTAVAGPPDAARQDELRHLVRQDCGSCHGLRMTGGLGRPITAAALAGRDVEDLSDVILDGMPGTAMPGWRPLLTEDDARWIADYLLKTETE | Function: Monoheme c-type cytochrome.
PTM: Binds 1 heme c group covalently per subunit.
Sequence Mass (Da): 10992
Sequence Length: 103
Subcellular Location: Periplasm
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Q51479 | MNAPPDFRRAASHALWLALALTFACPLPGLADEHPDARRQAQLRHLLLQDCGSCHGLRLTGGLGPALTPEALRGKPRESLVATVLMGRPQTPMPPWAGLLSEDDAGWLVDRLIEGEIAP | Function: Monoheme c-type cytochrome.
PTM: Binds 1 heme c group covalently per subunit.
Sequence Mass (Da): 12801
Sequence Length: 119
Subcellular Location: Periplasm
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D3DFS4 | MGNEFDKILKIIQKDIPLVKEPFSVLAQEVGIEEGKLLKTIEKLVEDGIVRHIAPIYDSRLLGYDSALIAFKVDRQKLEEVANFVNACPGVSHNYERTHDFNLWFTLAVPPEISELEDVVRLMAERERVKDYLVLRVVRLFKIGVKLDYESPAEKESVDTKVYTYTPLTEEEKRIVSITQGSFPLVERPFLEYAKRLRMSEEELLEKLSALKERGVLRRISAVLYHRRAGYVANAMSVWEVPEDAIEEVGRYIAGFKGVSHCYQRTTSEKFRYNLFAMMHGKGQEEIKLLAETISREKALSKYALLFSTREFKKVRIKYF... | Function: Involved in heme d1 biosynthesis. Catalyzes the decarboxylation of siroheme into didecarboxysiroheme. Siroheme is probably decarboxylated to monodecarboxysiroheme, which is in turn decarboxylated to didecarboxysiroheme.
Catalytic Activity: 2 H(+) + siroheme = 12,18-didecarboxysiroheme + 2 CO2
Sequence Mass (D... |
I6UH61 | MTMDDLDLRLLDGFQRDLPLETRPFAAIANRLNTSEAEVIARLARLRDEGLIARIGATCRPNTAGASTLAALRVPVRRIDKVAALVGAEPGVNHSYLREGSDWNLWFVATAPDAEALEESLVRIETATGLVPLSLPLVRAFNIDLGFPLIGPRRAMALDRPTDLDVLRPRDKALMQALTTGLALVPRPFVALGQALGRSEAEVISRIRALAAARILTRVGVIVRHRALGWCENAMVVWRLPEPAVEAAGTALAAVPGVTLCYQRRTVPGLWNWPLFCMIHARSRAEAMEVLVQARALPELQGVPHRILFSTRCFRQRGAV... | Function: Involved in heme d1 biosynthesis. Catalyzes the decarboxylation of siroheme into didecarboxysiroheme . Siroheme is probably decarboxylated to monodecarboxysiroheme, which is in turn decarboxylated to didecarboxysiroheme .
Catalytic Activity: 2 H(+) + siroheme = 12,18-didecarboxysiroheme + 2 CO2
Sequence Mass ... |
P0A9I9 | MSQWKDICKIDDILPETGVCALLGDEQVAIFRPYHSDQVFAISNIDPFFESSVLSRGLIAEHQGELWVASPLKKQRFRLSDGLCMEDEQFSVKHYEARVKDGVVQLRG | Function: Required for activity of the reductase.
Catalytic Activity: 2 H2O + 3 NAD(+) + NH4(+) = 5 H(+) + 3 NADH + nitrite
Sequence Mass (Da): 12284
Sequence Length: 108
Subcellular Location: Cytoplasm
EC: 1.7.1.15
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C4RPA1 | MSNLTEERWVAADLRAPLTPAGRTVVDLLAGVIPRISAEAADRDRTGTFPVEAFEQFAKLGLMGATVPAELGGLGLTRLYDVATALMRLAEADASTALAWHVQLSRGLTLTYEWQHGTPPVRAMAERLLRAMAEGEAAVCGALKDAPGVVTELHSDGAGGWLLSGRKVLVSMAPIATHFFVHAQRRDDDGSVFLAVPVVHRDAPGLTVLDNWDGLGMRASGTLEVVFDRCPVRADELLERGPVGARRDAVLAGQTVSSITMLGIYAGIAQAARDIAVGFCAGRGGEPRAGARALVAGLDTRLYALRTTVGAALTNADAAS... | Function: Nitrososynthase involved in the biosynthesis of everninomicin, a broad spectrum orthosomycin antibiotic . Catalyzes the double-oxidation of TDP-L-evernosamine to TDP-L-evernitrosose . The enzyme first oxidizes the substrate to a transient hydroxylamino intermediate, which is then further oxidized to nitroso s... |
A0A2H3E4G0 | MPISLNPSHSNTQTFKVAAVQAEPVWLDLQGGVEKTIRIINEAAAEGAKIIGFPEVFIPGYPWTPWANNFVDAQVVLKKYQANSMPLHSPEMDRIREAVKEADVNIVLGFSERDGSSLYIAQVTITSDGKIANHRRKIKPTHYEKTIFGDGSAQSIYNVVQTPYGRLGSLNCWEHIQPWLKTHFYSQYPQIFVGGWWPAFPPHTGGSPYIVSGEASSRMSQLVSMEGGLFGIVCCHVVSEAGARKMRMLGFPWFTFPGGGFSVIYGPDGAALTDPVDPGKEVVLYANISLDKIDDVKLVADIMGNYSRFDLFHTTVVNGK... | Function: Catalyzes the hydration of cyanide to formamide. Degradation of cyanide may be important for plant pathogenic fungi in infection of cyanogenic plants.
Catalytic Activity: formamide = H2O + hydrogen cyanide
Sequence Mass (Da): 39050
Sequence Length: 356
EC: 4.2.1.66
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