ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q99J85 | MKFLAVLLAAGMLAFLGAVICIIASVPLAASPARALPGGTDNASAASAAGGSGPQRSLSALHSAGGSAGPSVLPGEPAASVFPPPPVPLLSRFLCTPLAAACPSGAEQGDAAGERAELLLLQSTAEQLRQTALQQEARIRADRDTIRELTGKLGRCESGLPRGLQDAGPRRDTMADGAWDSPALLLELEDAVRALRDRIERIEQELPARGNLSSAPAPAMPTALHSKMDELECQLLAKVLALEKERAALSHGSHQQRQEVEKELNALQGRVAELEHGSSAYSPPDAFKVSIPIRNNYMYARVRKALPELYAFTACMCVRS... | Cofactor: Binds 2 calcium ions per subunit.
Function: May be involved in mediating uptake of synaptic material during synapse remodeling or in mediating the synaptic clustering of AMPA glutamate receptors at a subset of excitatory synapses.
PTM: Ubiquitinated by a cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-prot... |
O35764 | MKFLAVLLAAGMLAFLGAVICIIASVPLAASPARALPGGTDNASAASAAGAPGPQRSLSALQGAGGSAGPSVLPGEPAASVFPPPPGPLLSRFLCTPLAAACPSGAEQGDAAGERAELLLLQSTAEQLRQTALQQEARIRADRDTIRELTGKLGRCESGLPRGLQDAGPRRDTMADGAWDSPALLVELENAVRALRDRIERIEQELPARGNLSSSAPAPAVPTALHSKMDELEGQLLAKVLALEKERAALSHGSHQQRQEVEKELDALQGRVAELEHGSSAYSPPDAFKVSIPIRNNYMYARVRKAVPELYAFTACMWLR... | Cofactor: Binds 2 calcium ions per subunit.
Function: May be involved in mediating uptake of synaptic material during synapse remodeling or in mediating the synaptic clustering of AMPA glutamate receptors at a subset of excitatory synapses.
PTM: N-glycosylated.
Location Topology: Single-pass type II membrane protein
Se... |
Q9Z7G2 | MKITVNRGLDLSLQGSPKESGFYNKIDPEFVSIDLRPFQPLSLKLKVEQGDAVCSGAPIAEYKHFPNTYITSHVSGVVTAIRRGNKRSLLDVIIKKTPGPTSTEYTYDLQTLSRSDLSEIFKENGLFALIKQRPFDIPAIPTQTPRDVFINLADNRPFTPSPEKHLALFSSREEGFYVFVVGVRAIAKLFGLRPHIVFRDRLTLPTQELKTIAHLHTVSGPFPSGSPSIHIHSVAPITNEKEVVFTLSFQDVLTIGHLFLKGRILHEQVTALAGTALKSSLRRYVITTKGASFSSLINLNDISDNDTLISGDPLTGRLCK... | Function: NQR complex catalyzes the reduction of ubiquinone-1 to ubiquinol by two successive reactions, coupled with the transport of Na(+) ions from the cytoplasm to the periplasm. NqrA to NqrE are probably involved in the second step, the conversion of ubisemiquinone to ubiquinol.
Catalytic Activity: a ubiquinone + H... |
P43955 | MITIKKGLDLPIAGKPAQVIHSGNAVNQVAILGEEYVGMRPSMKVREGDVVKKGQVLFEDKKNPGVIFTAPASGTITAINRGEKRVLQSVVINVEGDEKITFAKYSTEQLNTLSSEQVKQNLIESGLWTALRTRPFSKVPSIESEASSIFVNAMDTNPLAADPSVVLKEYSQDFTNGLTVLSRLFPSKPLHLCKAGDSNIPTADLENLQIHDFTGVHPAGLVGTHIHFIDPVGIQKTVWHINYQDVIAVGKLFTTGELYSERVISLAGPQVKEPRLVRTTIGANLSQLTQNELSAGKNRVISGSVLCGQIAKDSHDYLGR... | Function: NQR complex catalyzes the reduction of ubiquinone-1 to ubiquinol by two successive reactions, coupled with the transport of Na(+) ions from the cytoplasm to the periplasm. NqrA to NqrE are probably involved in the second step, the conversion of ubisemiquinone to ubiquinol.
Catalytic Activity: a ubiquinone + H... |
P71342 | MEHYISLFVKAVFIENMALSFFLGMCTFLAVSKKVSPAFGLGIAVTFVLGIAVPVNQLIYANVLKENALIEGVDLSFLNFITFIGVIAGLVQILEMVLDKFMPSLYNALGIFLPLIAVNCAIFGGVSFMVQRDYNFPESIVYGFGSGLGWMLAIVALAGLTEKMKYADIPAGLKGLGITFISVGLMALGFMSFSGIQL | Function: NQR complex catalyzes the reduction of ubiquinone-1 to ubiquinol by two successive reactions, coupled with the transport of Na(+) ions from the cytoplasm to the periplasm. NqrA to NqrE are probably involved in the second step, the conversion of ubisemiquinone to ubiquinol.
Catalytic Activity: a ubiquinone + H... |
O00482 | MSSNSDTGDLQESLKHGLTPIGAGLPDRHGSPIPARGRLVMLPKVETEALGLARSHGEQGQMPENMQVSQFKMVNYSYDEDLEELCPVCGDKVSGYHYGLLTCESCKGFFKRTVQNNKRYTCIENQNCQIDKTQRKRCPYCRFQKCLSVGMKLEAVRADRMRGGRNKFGPMYKRDRALKQQKKALIRANGLKLEAMSQVIQAMPSDLTISSAIQNIHSASKGLPLNHAALPPTDYDRSPFVTSPISMTMPPHGSLQGYQTYGHFPSRAIKSEYPDPYTSSPESIMGYSYMDSYQTSSPASIPHLILELLKCEPDEPQVQA... | Function: Nuclear receptor that acts as a key metabolic sensor by regulating the expression of genes involved in bile acid synthesis, cholesterol homeostasis and triglyceride synthesis. Together with the oxysterol receptors NR1H3/LXR-alpha and NR1H2/LXR-beta, acts as an essential transcriptional regulator of lipid meta... |
P45448 | MSASLDTGDFQEFLKHGLTAIASAPGSETRHSPKREEQLREKRAGLPDRHRRPIPARSRLVMLPKVETEAPGLVRSHGEQGQMPENMQVSQFKMVNYSYDEDLEELCPVCGDKVSGYHYGLLTCESCKGFFKRTVQNQKRYTCIENQNCQIDKTQRKRCPYCRFKKCIDVGMKLEAVRADRMRGGRNKFGPMYKRDRALKQQKKALIRANGLKLEAMSQVIQAMPSDLTSAIQNIHSASKGLPLSHVALPPTDYDRSPFVTSPISMTMPPHSSLHGYQPYGHFPSRAIKSEYPDPYSSSPESMMGYSYMDGYQTNSPASI... | Function: Nuclear receptor that acts as a key metabolic sensor by regulating the expression of genes involved in bile acid synthesis, cholesterol homeostasis and triglyceride synthesis. Together with the oxysterol receptors NR1H3/LXR-alpha and NR1H2/LXR-beta, acts as an essential transcriptional regulator of lipid meta... |
Q9XUB9 | MNQPIGIADSSRPKTNVRLTISANNLMDLDVFSKSDPICLIYEKTSGRKATTTEEITVPTWKDKQWTERGRTEVVMNNLNPQFTKTFLLPYFFEETQLLRFEIYDADSPTVGQDLSSHDFLGRFECVLAQIVSYSTLKAHLGKTGQIGAQWRNKDKNTKTGSITIYAEEDEKAEKIQFDVCGEGLDKKDFFGKSDPYLNFKRKFDDGSTHLIHRTEVKPKTLDPRWATVQINTQTLCAKDGDRPIIIECYDHDKWKKGEEPRGDAKFSRDDLIGTAQTTLNELLRGSSDAVEILLTNEKKKAKKGDKYKCSGTLKIWNSR... | Function: Exhibits calcium-dependent phospholipid binding properties (By similarity). May function in membrane trafficking. Regulates synaptic levels of nicotinic acetylcholine receptor subunit lev-1 and unc-38 in the nerve cord . Involved in nicotinic acetylcholine receptor (nAChR)-mediated sensitivity to nicotine and... |
Q8CJ26 | MLYNVSKGVVYSDTALQGQDGDREGMWVGAGGALAPNTSSLFPPEPPGASSNIIPVYCALLATVILGLLAYVAFKCWRSHKQRQQLAKARTVELGDPDRDQRRGDSNVFVDSPPSLEPCIPSQGPHPDLGCQLYLHIPQQQQEEVQRLLMMGEPAKGWQELAGHLGYQAEAVETMACDQMPAYTLLRNWAAQEGNRATLRVLEDALAAIGREDVVQVLSSPAESSSVV | Function: Modulates NTRK1 signaling. Can activate several intracellular signaling pathways, leading to activation of JUN. Promotes apoptosis. Promotes translocation of SORT1 to the cell membrane, and thereby hinders lysosomal degradation of SOTR1 and promotes its interaction with NGFR.
Location Topology: Single-pass ty... |
Q8K5A9 | MLHNVSKGVVYSDTALKGQDGDREGMWVGAGGALAPNTSSLFPPEPPGASSNIIPVYCALLATVVLGLLAYVAFKCWRSRKQRQQLAKARTVELGDPDRDQRHGDSSVFVDSPHGLEPCIPSQGPHADLGCRLYLHIPQQQQEEVQRLLILGEPAKGWQGLAGQLGYQAEAVETMACDQDPAYALLRDWAAQEGSGATLRVLEDALTAIGREDVVQVLSSPAEGCSVV | Function: Modulates NTRK1 signaling. Can activate several intracellular signaling pathways, leading to activation of JUN. Promotes translocation of SORT1 to the cell membrane, and thereby hinders lysosomal degradation of SOTR1 and promotes its interaction with NGFR (By similarity). Both isoform 1 and isoform 2 promote ... |
Q9SAH8 | MAATGSGRSQFISSSGGNRSFSNSPLIENSDSNQIIVSEKKSWKNFFAYLGPGFLVSIAYIDPGNFETDLQAGAHYKYELLWIILVASCAALVIQSLAANLGVVTGKHLAEQCRAEYSKVPNFMLWVVAEIAVVACDIPEVIGTAFALNMLFSIPVWIGVLLTGLSTLILLALQKYGVRKLEFLIAFLVFTIAICFFVELHYSKPDPGEVLHGLFVPQLKGNGATGLAISLLGAMVMPHNLFLHSALVLSRKIPRSASGIKEACRFYLIESGLALMVAFLINVSVISVSGAVCNAPNLSPEDRANCEDLDLNKASFLLRN... | Function: High affinity manganese (Mn) transporter involved in Mn acquisition from the soil. Required for Mn uptake into the root in conditions of low Mn availability. Can transport iron (Fe), cadmium (Cd) and cobalt (Co).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 57562
Sequence Length: 532
Sub... |
Q27981 | MSGDTGPPKQGGTRYGSISSPPSPEPQQAPPGGTYLSEKIPIPDTESGTFSLRKLWAFTGPGFLMSIAFLDPGNIESDLQAGAVAGFKLLWVLLWATVLGLLCQRLAARLGVVTGKDLGEVCHLYYPKVPRILLWLTIELAIVGSDMQEVIGTAIAFSLLSAGRIPLWGGVLITVVDTFFFLFLDNYGLRKLEAFFGFLITIMALTFGYEYVVAQPAQGALLQGLFLPSCPGCGQPELLQAVGIIGAIIMPHNIYLHSSLVKSREVDRSRRADIREANMYFLIEATIALSVSFLINLFVMAVFGQAFYKQTNQAAFNICA... | Function: Macrophage-specific antiporter that fluxes metal ions in either direction against a proton gradient. Localized to late endosomal lysosomal membranes, delivers bivalent cations from the cytosol into these acidic compartments where they may directly affect antimicrobial activity. Involved in iron metabolism and... |
Q9NSY0 | MAAPEPAPRRAREREREREDESEDESDILEESPCGRWQKRREQVNQGNMPGLQSTFLAMDTEEGVEVVWNELHFGDRKAFAAHEEKIQTVFEQLVLVDHPNIVKLHKYWLDTSEACARVIFITEYVSSGSLKQFLKKTKKNHKAMNARAWKRWCTQILSALSFLHACSPPIIHGNLTSDTIFIQHNGLIKIGSVWHRIFSNALPDDLRSPIRAEREELRNLHFFPPEYGEVADGTAVDIFSFGMCALEMAVLEIQTNGDTRVTEEAIARARHSLSDPNMREFILCCLARDPARRPSAHSLLFHRVLFEVHSLKLLAAHCF... | Function: May regulate apoptosis of neural progenitor cells during their differentiation.
Sequence Mass (Da): 57803
Sequence Length: 501
Domain: The protein kinase domain is predicted to be catalytically inactive.
Subcellular Location: Cytoplasm
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Q91V36 | MAAPEPAPRRGREREREDESEDESDILEESPCGRWQKRREQVNQGNMPGIQSTFLAMDTEEGVEVVWNELHFGDRKAFAAHEEKIQTMFEQLALVDHPNIVKLHKYWLDASEARARVIFITEYVSSGSLKQFLKKTKKNHKAMNARAWKRWCTQILSALSFLHACSPPIIHGNLTSDTIFIQHNGLIKIGSVWYRIFSNALPDDLRSPIRAEREELRNLHFFPPEYGEVNDGTAVDIFSFGMCALEMAVLEIQANGDTRVTEEAIARARHSLSDPNMREFILSCLARDPARRPSAHNLLFHRVLFEVHSLKLLAAHCFIQ... | Function: May regulate apoptosis of neural progenitor cells during their differentiation.
Sequence Mass (Da): 57348
Sequence Length: 499
Domain: The protein kinase domain is predicted to be catalytically inactive.
Subcellular Location: Cytoplasm
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Q9Y0Y6 | MSNSQANAGISGSTVADEPIQHHPSLAAGPVSASCPAATPPSQSTQQPPPHIVSASTADAGSSAAVGVGVVAGSEGVNLDSSPRESGDDSEDESEILEESPCGRWLKRREEVDQRDVPGIDCVHLAMDTEEGVEVVWNEVQYASLQELKSQEEKMRQVFDNLLQLDHQNIVKFHRYWTDTQQAERPRVVFITEYMSSGSLKQFLKRTKRNAKRLPLESWRRWCTQILSALSYLHSCSPPIIHGNLTCDSIFIQHNGLVKIGSVVPDAVHYSVRRGRERERERERGAHYFQAPEYGAADQLTAALDIYAFGMCALEMAALE... | Function: May play a role in subcellular trafficking between the endoplasmic reticulum and Golgi apparatus.
Sequence Mass (Da): 70508
Sequence Length: 637
Domain: The protein kinase domain is predicted to be catalytically inactive.
Subcellular Location: Cytoplasm
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Q297L2 | MSNSQANAGSSGSADEPTLNPSGSATLVPNLTTTNASSQATPASTIPQQQQPQQSQPQPQPQPPPHIVGASTADAGGGVGVVVAGGSEGVNLDSSPRESGDDSEDESEILEESPCGRWLKRREEVDQRDVPGIDCVHLAMDTEEGVEVVWNEVQYANMQELKSQEEKMRQVFDNLLQLDHQNIVKFHRYWTDTQQAERPRVIFITEYMSSGSLKQFLKRTKRNAKRLPLESWRRWCTQILSALSYLHSCTPPIIHGNLTCDSIFIQHNGLVKIGSVVPDAVHYSVRRQWDRESAREQERERGAHYFQAPEYGAAEQLTAA... | Function: May play a role in subcellular trafficking between the endoplasmic reticulum and Golgi apparatus.
Sequence Mass (Da): 73520
Sequence Length: 663
Domain: The protein kinase domain is predicted to be catalytically inactive.
Subcellular Location: Cytoplasm
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Q9UHY1 | MSEGESQTVLSSGSDPKVESSSSAPGLTSVSPPVTSTTSAASPEEEEESEDESEILEESPCGRWQKRREEVNQRNVPGIDSAYLAMDTEEGVEVVWNEVQFSERKNYKLQEEKVRAVFDNLIQLEHLNIVKFHKYWADIKENKARVIFITEYMSSGSLKQFLKKTKKNHKTMNEKAWKRWCTQILSALSYLHSCDPPIIHGNLTCDTIFIQHNGLIKIGSVAPDTINNHVKTCREEQKNLHFFAPEYGEVTNVTTAVDIYSFGMCALEMAVLEIQGNGESSYVPQEAISSAIQLLEDPLQREFIQKCLQSEPARRPTARE... | Function: Required for embryonic development (By similarity). Plays a role in intestinal epithelial cell fate and proliferation, thereby involved in the architectural development of the intestine potentially via the regulation of Wnt-responsive genes (By similarity). May play a role in subcellular trafficking between t... |
Q99J45 | MSEGESQTVVSSGSDPKVESSSLAPGLTSVSPPVTSTTSAASPEEEEESEDESEILEESPCGRWQKRREEVNQRNVPGIDSAYLAMDTEEGVEVVWNEVQFSERKNYKLQEEKVRAVFDNLIQLEHLNIVKFHKYWADVKENKARVIFITEYMSSGSLKQFLKKTKKNHKTMNEKAWKRWCTQILSALSYLHSCDPPIIHGNLTCDTIFIQHNGLIKIGSVAPDTINNHVKTCREEQKNLHFFAPEYGEVTNVTTAVDIYSFGMCALEMAVLEIQGNGESSYVPQEAISSAIQLLEDSLQREFIQKCLQSEPARRPTARE... | Function: Required for embryonic development . Plays a role in intestinal epithelial cell fate and proliferation, thereby involved in the architectural development of the intestine potentially via the regulation of Wnt-responsive genes . May play a role in subcellular trafficking between the endoplasmic reticulum and G... |
O42626 | MPSTKNANGEGHFPSRIKQFFRINSGSKDHKDRDAHTTSSSHGGAPRADAKTPSGFRQSRFFSVGRLRSTTVVSEGNPLDESMSPTAHANPYFAHQGQPGLRHHNDGSVPPSPPDTPSLKVDGPEGSQQPTAATKEELARKLRRVASAPNAQGLFSKGQGNGDRPATAELSKEPLEESKDSNTVGFAEQKPNNDSSTSLAAPDADGLGALPPPIRQSPLAFRRTYSSNSIKVRNVEVGPQSFDKIKLIGKGDVGKVYLVKEKKSGRLYAMKVLSKKEMIKRNKIKRALAEQEILATSNHPFIVTLYHSFQSEDYLYLCME... | Function: Controls entry of the cell into the asexual developmental program. Required to repress entry into the conidiation program.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 68628
Sequence Length: 623
EC: 2.7.11.1
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Q9Z4P4 | MKFKLLLAGSLVAVGAMALLASNINEKEKQRVELAKAPSEAGIAGKEKSEEWAKYYPRQFDSWKKTKEYDSFTDMLAKDPALVIAWSGYAFSKDYNSPRGHYYALQDNVNSLRTGAPVDAKTGPLPTACWTCKSPDVPRLIEEDGELEYFTGKWAKYGSQIVNVIGCANCHDDKTAELKVRVPHLNRGLQAAGLKTFEESTHQDKRTLVCAQCHVEYYFKKTEWKDAKGADKTAMVVTLPWANGVGKDGNAGVEGMIKYYDEINFSDWTHNISKTPMLKAQHPGFEFWKSGIHGQKGVSCADCHMPYTQEGSVKYSDHQV... | Cofactor: Binds 1 Ca(2+) ion per monomer.
Function: Catalyzes the reduction of nitrite to ammonia, consuming six electrons in the process . Has very low activity toward hydroxylamine, and even lower activity toward sulfite. Sulfite reductase activity is maximal at neutral pH (By similarity).
Catalytic Activity: 6 Fe(II... |
Q9S1E5 | MTKFKLLLAGSLVAIVSMGLLASNINEREKERVALNKTAHSQGIEGKAMSEEWARYYPRQFDSWKKTKESDNITDMLKEKPALVVAWAGYPFSKDYNAPRGHYYALQDNINTLRTGAPVDGKTGPLPSACWTCKSPDVPRIIEQDGELEYFTGKWAKYGDEIVNTIGCYNCHDDKSAELKSKVPYLDRGLSAAGFKTFAESTHQEKRSLVCAQCHVEYYFKKTEWKDDKGVDKTAMVVTLPWSKGISTEQMEAYYDEINFADWTHGISKTPMLKAQHPDWELYKTGIHGQKGVSCADCHMPYTQEGAVKYSDHKVGNPLD... | Cofactor: Binds 1 Ca(2+) ion per monomer.
Function: Catalyzes the reduction of nitrite to ammonia, consuming six electrons in the process. Has very low activity toward hydroxylamine, and even lower activity toward sulfite. Sulfite reductase activity is maximal at neutral pH.
Catalytic Activity: 6 Fe(III)-[cytochrome c]... |
P0ABL2 | MSVLRSLLTAGVLASGLLWSLNGITATPAAQASDDRYEVTQQRNPDAACLDCHKPDTEGMHGKHASVINPNNKLPVTCTNCHGQPSPQHREGVKDVMRFNEPMYKVGEQNSVCMSCHLPEQLQKAFWPHDVHVTKVACASCHSLHPQQDTMQTLSDKGRIKICVDCHSDQRTNPNFNPASVPLLKEQP | Function: Plays a role in nitrite reduction.
PTM: Binds 5 heme groups per subunit.
Sequence Mass (Da): 20714
Sequence Length: 188
Pathway: Energy metabolism; nitrogen metabolism.
Subcellular Location: Periplasm
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P45016 | MIFKVKFEVTQMILTSLINKSAKALVIVAFVAAPFLAHADDAQKPAVHVTYEPQLDNQRDPNQYCAKCHKFDKIDKNQTLDQSGGELHFGKFHGAHLDKKNPNNGKAITCVSCHGNISENHRRGAKDVMRFEGDIFGNKKPMYSVQEQNQVCFACHQPDKLREKLWAHDVHAMKLPCASCHTLHPKEDAMKGIQPKQRVKLCVDCHGEQQKRKAEQDKLIEQKDKL | Function: Plays a role in nitrite reduction.
PTM: Binds 5 heme groups per subunit.
Sequence Mass (Da): 25664
Sequence Length: 226
Pathway: Energy metabolism; nitrogen metabolism.
Subcellular Location: Periplasm
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P32709 | MTQTSAFHFESLVWDWPIAIYLFLIGISAGLVTLAVLLRRFYPQAGGADSTLLRTTLIVGPGAVILGLLILVFHLTRPWTFWKLMFHYSFTSVMSMGVMLFQLYMVVLVLWLAKIFEHDLLALQQRWLPKLGIVQKVLSLLTPVHRGLETLMLVLAVLLGAYTGFLLSALKSYPFLNNPILPVLFLFSGISSGAAVALIAMAIRQRSNPHSTEAQFVHRMEIPVVWGEIFLLVAFFVGLALGDDGKVRALVAALGGGFWTWWFWLGVAGLGLIVPMLLKPWVNRSSGIPAVLAACGASLVGVLMLRFFILYAGQLTVA | Function: Probably involved in the transfer of electrons from the quinone pool to the type-c cytochromes.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35042
Sequence Length: 318
Subcellular Location: Cell inner membrane
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P45014 | MTLDYPVPFHTPNLVWDYTIAIYLFLLGISSGAVQLAIAYKRSNKLENLSQNWIIRSGVILGSVPTLIGLTLLIFHLTRPWTFWKLMFNYQFNSVMSMGVMLFQIYMLFLVIWGVVIFKKEIEALINRFIPKLQFVMKLIGIAERIVSPVEVILFILAAVLGAYTGFLLSALISYPMLNNPVLPALFLASGTSSGIAATFLIILIAGKLKGDSHESHFIHKFEVPIMVTELGLIVCFFVGLHFGGGQKTVALHNALSGFWGVVFWVGVLIIGILIPLIANMFVNDRLKYNRNFIILVSIFDLIGVFCLRFFILYAGQLTV... | Function: Probably involved in the transfer of electrons from the quinone pool to the type-c cytochromes.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35944
Sequence Length: 321
Subcellular Location: Cell inner membrane
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P32710 | MLTPLTAFAGVRLRWPAMMRLTCIGILAQFALLLLAFGVLTYCFLISDFSVIYVAQHSYSLLSWELKLAAVWGGHEGSLLLWVLLLSAWSALFAWHYRQQTDPLFPLTLAVLSLMLAALLLFVVLWSDPFVRIFPPAIEGRDLNPMLQHPGLIFHPPLLYLGYGGLMVAASVALASLLRGEFDGACARICWRWALPGWSALTAGIILGSWWAYCELGWGGWWFWDPVENASLLPWLSATALLHSLSLTRQRGIFCHWSLLLAIVTLMLSLLGTLIVRSGILVSVHAFALDNVRAVPLFSLFALISLASLALYGWRARDGG... | Function: May be required for the biogenesis of c-type cytochromes. Possible subunit of a heme lyase.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 61295
Sequence Length: 552
Subcellular Location: Cell inner membrane
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P44944 | MLPELGFFLLLLATASAFFLALVPQFGLFKKNPTLINAAWPLSYIFTLATTLSIGLLAYSFAVDDFTLEYVAAHSNSQLPTFFKVAATWGGHEGSMLFWLFSLSLWLAAFAFFNRKNDRTFSAQSLSLLGLICFGFAVFILFYSNPFGRIFPAPAEGRDLNPMLQDVGLIFHPPLLYVGYVGFAVNFAMSLSALIYNQSARQIARSMRGWVLVSWLFLTIGIVLGAWWAYYELGWGGWWFWDPVENASLMPWLLGLALLHSLMATEKQGVFSYWTTLFSLLAFAFSVLGTFIVRSGALTSVHAFALDNTRGYVLLLIFFV... | Function: Required for the biogenesis of c-type cytochromes. Possible subunit of a heme lyase (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 71274
Sequence Length: 635
Subcellular Location: Cell inner membrane
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Q94JG1 | MEAKPVAMEVEGVEAAGGKPRFRMPVDSDLKATEFWLFSFARPHMASFHMAWFSFFCCFVSTFAAPPLLPLIRDTLGLTATDIGNAGIASVSGAVFARLAMGTACDLVGPRLASASLILLTTPAVYCSSIIQSPSGYLLVRFFTGISLASFVSAQFWMSSMFSAPKVGLANGVAGGWGNLGGGAVQLLMPLVYEAIHKIGSTPFTAWRIAFFIPGLMQTFSAIAVLAFGQDMPGGNYGKLHKTGDMHKDSFGNVLRHALTNYRGWILALTYGYSFGVELTIDNVVHQYFYDRFDVNLQTAGLIAASFGMANIISRPGGGL... | Function: Involved in nitrate transport, but does not seem to be able to mediate transport by its own. Acts as a dual component transporter with NAR2.1. Imports nitrate with high affinity when expressed with NAR2.1 in a heterologous system (Xenopus oocytes). Plays a key role in long-distance nitrate transport from root... |
Q9FJH8 | MADGFGEPGSSMHGVTGREQSYAFSVESPAVPSDSSAKFSLPVDTEHKAKVFKLLSFEAPHMRTFHLAWISFFTCFISTFAAAPLVPIIRDNLNLTRQDVGNAGVASVSGSIFSRLVMGAVCDLLGPRYGCAFLVMLSAPTVFSMSFVGGAGGYITVRFMIGFCLATFVSCQYWMSTMFNGQIIGLVNGTAAGWGNMGGGVTQLLMPMVYEIIRRLGSTSFTAWRMAFFVPGWMHIIMGILVLTLGQDLPDGNRSTLEKKGAVTKDKFSKVLWYAITNYRTWVFVLLYGYSMGVELTTDNVIAEYFFDRFHLKLHTAGII... | Function: Involved in high-affinity nitrate transport. Might be involved in the transfer of nitrate from stored pools to cytoplasm.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 57768
Sequence Length: 527
Subcellular Location: Membrane
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A2ZU80 | MVAMEKKTKLVEEEDGCYYYDYGGYGDGVVDDEGRATELRPMALSRPHTQAFHLAWMSLFACFFAAFAAPPILPAMRPALVLAPSDASAAAVASLSATLVGRLAMGPACDLLGPRRASGVASLVCALALALAAVFASSPAGFVALRFVAGLSLANFVANQHWMSRIFAPSAVGLANAVAAGWANVGSAAAQVVMPVAYDAVVLRLGVPVTVAWRVTYLLPCAMLVTTGLAVLAFPYDLPGGGGGRCPGGGGGRRRSFWAVVRGGVGDYRAWLLGLTYGHCYGVELIMENVAADFFRRRFRLPMEAAGAAAACFGAMNAVA... | Function: Involved in nitrate transport.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 50199
Sequence Length: 485
Subcellular Location: Cell membrane
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Q9LPV5 | MEVEGKGGEAGTTTTTAPRRFALPVDAENKATTFRLFSVAKPHMRAFHLSWFQFFCCFVSTFAAPPLLPVIRENLNLTATDIGNAGIASVSGAVFARIVMGTACDLFGPRLASAALTLSTAPAVYFTAGIKSPIGFIMVRFFAGFSLATFVSTQFWMSSMFSGPVVGSANGIAAGWGNLGGGATQLIMPIVFSLIRNMGATKFTAWRIAFFIPGLFQTLSAFAVLLFGQDLPDGDYWAMHKSGEREKDDVGKVISNGIKNYRGWITALAYGYCFGVELTIDNIIAEYFFDRFHLKLQTAGIIAASFGLANFFARPGGGIF... | Function: Nitrate transporter involved in the constitutive high-affinity transport system (cHATS) under long-term N starvation conditions . Predominantly expressed in roots of nitrate-deprived plants as a 150 kDa molecular complex with NRT3.1 representing the major contributor to cHATS influx . The principal role of th... |
Q9LYK2 | MEPSQRNTKPPSFSDSTIPVDSDGRATVFRPFSLSSPHSRAFHLAWLSLFSCFFSTFSIPPLVPVISSDLNLSASTVSAAGIASFAGSIFSRLAMGPLCDLIGPRTSSAILSFLTAPVILSASLVSSPTSFILVRFFVGFSLANFVANQYWMSSMFSGNVIGLANGVSAGWANVGAGISQLLMPLIYSTIAEFLPRAVAWRVSFVFPAIFQVTTAVLVLLYGQDTPHGNRKNSNQNKLTIPEEEEVLVVEEDERSSFVEILIGGLGNYRAWILALLYGYSYGVELTTDNVIAGYFYERFGVNLEAAGTIAASFGISNIAS... | Function: Involved in high-affinity nitrate transport. Controls nitrate content in seeds.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 52678
Sequence Length: 493
Subcellular Location: Vacuole membrane
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P55807 | MELLALRWVLLAGTLLSTSAASSALQEGDLGSITVIMDMAPNSFDDQYVGCAHVMWANLQKLKCTEFARNYAYAVGWRKAAAEWQKRWGYLAHPMQLRPEQAIALLAYSAASNLYQQFNAATRQGGCSHQYYVHFYHFKTLHFLLTQALFALRASQPRCYYVYRGVRGIRFMTQRGKSVRFGQFTSTSLRKDVAVNFGQDTFFVVKTCYGVPIKQFSFYPSEDEVLIPPFEVFEVTNFCTGNGRIQIYLRSKGKMSRHNCELLKPRGGQWGRGHQEVGLGLSPGLALPVLPCSNCSCWGSGHRAGDPIPAAV | Catalytic Activity: L-arginyl-[protein] + NAD(+) = H(+) + N(omega)-(ADP-D-ribosyl)-L-arginyl-[protein] + nicotinamide
Sequence Mass (Da): 34966
Sequence Length: 312
Subcellular Location: Secreted
EC: 2.4.2.31
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Q9FGS5 | MAIQKILFASLLICSLIQSIHGAEKVRLFKELDKGALDVTTKPSREGPGVVLDAGKDTLNITWTLSSIGSKREAEFKIIKVKLCYAPPSQVDRPWRKTHDELFKDKTCPHKIIAKPYDKTLQSTTWTLERDIPTGTYFVRAYAVDAIGHEVAYGQSTDDAKKTNLFSVQAISGRHASLDIASICFSVFSVVALVVFFVNEKRKAKIEQSK | Function: Acts as a dual component transporter with NTR2.1. Required for high-affinity nitrate transport. Acts as a repressor of lateral root initiation. May be involved in targeting NRT2 proteins to the plasma membrane.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 23403
Sequence Length: 210
Subc... |
P38043 | MSQFSRRKFLLTAGGTAAAALWLNACGSNNSSTDTTGSTSTPAPSGTSGGDAPEVKGVTLGFIALTDAAPVIIALEKGLFAKYGLPDTKVVKQTSWAVTRDNLELGSDRGGIDGAHILSPMPYLLTAGTITKSQKPLPMYILARLNTQGQGISLSNEFLAEKVQIKDPKLKAIADQKKASGKLLKAAVTFPGGTHDLWMRYWLAANGIDPNNDADLVVIPPPQMVANMQTGTMDTFCVGEPWNARLVNKKLGYTAAVTGELWKFHPEKALTIRADWADKNPKATMALLKAVQEAQIWCEDPANLDELCQITAQDKYFKTS... | Function: Part of the ABC transporter complex NrtABCD involved in nitrate uptake . The complex is probably also involved in nitrite transport . NrtA is the substrate-binding protein . Binds both nitrate and nitrite with high affinity .
PTM: The N-terminus is blocked.
Location Topology: Lipid-anchor
Sequence Mass (Da): ... |
P73452 | MSNFSRSTRRKFMFTAGAAAIGGVVLHGCTSPTTTSTGTGTGSSTDQAISPLVEGENAPEVTTAKLGFIALTDAAPLIIAKEKGFYAKYGMPDVEVLKQASWGTTRDNLVLGSASGGIDGAHILTPMPYLITMGTVTDGKPTPMYILARLNVNGQGIQLGNNYKDLKVGTDAAPLKEAFAKVTDPKVAMTFPGGTHDMWIRYWLAAGGMEPGKDFSTIVVPPAQMVANVKVNAMESFCVGEPWPLQTVNQGVGYQALTTGQLWKDHPEKAFGMRADWVDQNPKAAKALLMAVMEAQQWCDQAENKEEMCQILSKREWFKV... | Function: Part of the ABC transporter complex NrtABCD involved in nitrate uptake . The complex is probably also involved in nitrite transport (By similarity). NrtA is the substrate-binding protein . Binds nitrate .
Location Topology: Lipid-anchor
Sequence Mass (Da): 48967
Sequence Length: 446
Domain: Composed of two do... |
P38044 | MTVTLRPPSSVRRSAWVKNPKLKPFLPYVVCLPIFLAIWQVISAILGQDRLPGPINVVANTWMPYIVEPFFDNGGTSKGLGLQILISLQRVAIGYLLAACTGILVGGVLGMSKFLGKGLDPVIQVLRTVPPLAWFPISLMVFQDANTSAIFVIFITAIWPIIINTAVGINQIPDDYNNVARVLKLSKKDYILNILIPSTVPYVFAGLRIAVGLAWLAIVAAEMLKADGGIGYFIWDAYNAGGDGSSSQIILAIFYVGLVGLSLDRLVAWVGRLVSPVSR | Function: Part of the ABC transporter complex NrtABCD involved in nitrate uptake . The complex is probably also involved in nitrite transport . Probably responsible for the translocation of the substrate across the membrane .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 30207
Sequence Length: 279
... |
P38045 | MSVFLAVDHVHQVFDLPGGGQYIALKDVSLNIRPGEFISLIGHSGCGKSTLLNLIAGLAQPSSGGIILEGRQVTEPGPDRMVVFQNYSLLPWRTVRQNIALAVDSVLHDRNRTERRTIIEETIDLVGLRAAADKYPHEISGGMKQRVAIARGLAIRPKLLLLDEPFGALDALTRGNLQEQLMRICQEAGVTAVMVTHDVDEALLLSDRVVMLTNGPAAQIGQILEVDFPRPRQRLEMMETPHYYDLRNELINFLQQQRRAKRRAKAAAPAPAVAASQQKTVRLGFLPGNDCAPLAIAQELGLFQDLGLSVELQSFLTWEA... | Function: Part of the ABC transporter complex NrtABCD involved in nitrate uptake . The complex is probably also involved in nitrite transport . Probably responsible for energy coupling to the transport system .
Catalytic Activity: ATP + H2O + nitrate(out) = ADP + H(+) + nitrate(in) + phosphate
Location Topology: Periph... |
P38046 | MTAILPSTAATVNTGFLHFDCVGKTFPTPRGPYVAIEDVNLSVQQGEFICVIGHSGCGKSTLLNLVSGFSQPTSGGVYLDGQPIQEPGPDRMVVFQNYSLLPWKSARDNIALAVKAARPHLSTSEQRQVVDHHLELVGLTEAQHKRPDQLSGGMKQRVAIARALSIRPEVLILDEPFGALDAITKEELQEELLNIWEEARPTVLMITHDIDEALFLADRVVMMTNGPAATIGEVLEIPFDRPREREAVVEDPRYAQLRTEALDFLYRRFAHDDD | Function: Part of the ABC transporter complex NrtABCD involved in nitrate uptake . The complex is probably also involved in nitrite transport . Probably responsible for energy coupling to the transport system .
Catalytic Activity: ATP + H2O + nitrate(out) = ADP + H(+) + nitrate(in) + phosphate
Location Topology: Periph... |
P03495 | MDSNTVSSFQVDCFLWHVRKQVVDQELGDAPFLDRLRRDQKSLRGRGSTLGLNIEAATHVGKQIVEKILKEESDEALKMTMASTPASRYITDMTIEELSRDWFMLMPKQKVEGPLCIRIDQAIMDKNIMLKANFSVIFDRLETLILLRAFTEEGAIVGEISPLPSFPGHTIEDVKNAIGVLIGGLEWNDNTVRVSKTLQRFAWGSSNENGRPPLTPKQKRKMARTARSKVRRDKMAD | Function: Inhibits post-transcriptional processing of cellular pre-mRNA, by binding and inhibiting two cellular proteins that are required for the 3'-end processing of cellular pre-mRNAs: the 30 kDa cleavage and polyadenylation specificity factor/CPSF4 and the poly(A)-binding protein 2/PABPN1. In turn, unprocessed 3' e... |
P74836 | MSSVSELGYLGMSVTDLDAWRAYAAEVAGMEVVDEGESDRIYLRMDLWHHRIALIKGDTDDLAYMGWRLGDPTEFESMVEKLTNAGIAVTVASDAEARERRVLGLAKLTDPGGNPTEIFYGPQVDAHKPFHPGRPMFGKFVTGSEGIGHCILRQDDVEAAAAFYRLLGLRGSVEYQLHLPNGMVAMPYFMHCNERQHSVAFGLGPMEKRINHLMFEYTELDDLGLAHDIVRERQIDVALQLGKHANDLALTFYCANPSGWLWEFGWGARKAPAQQEFYTRDIFGHGNEAQGYGMDVPL | Function: Involved in the naphthalene and naphthalenesulfonate catabolic pathway. Catalyzes the meta-cleavage of 1,2-dihydroxynaphthalene (1,2-DHN) to yield 2-hydroxychromene-2-carboxylic acid. Can also cleave 1,2,5-trihydroxynaphthalene (1,2,5-THN), 1,2,6-trihydroxynaphthalene (1,2,6-THN), 1,2,7-trihydroxynaphthalene ... |
Q9X9Q7 | MTKTIDFYFDFISPFSYLAQVKLPDLARRTGCVIEYRPIDIPEAKIAAGNYGPSNREVVPKIKVMMADLERWAAKYEVPLTFPASFACSDWNCAALYARGQDQAEAFVTAAYHRIWGIGIDPRDQNELRGCAEDVGLDADALCEFVRSPAGQGEYRKARTQAYQRGVFGAPMMFVDDQIFWGNDRLDFLESYLLD | Cofactor: Glutathione seems to stabilize the enzyme, which loses activity rapidly in the absence of this compound.
Function: Involved in the naphthalene and naphthalenesulfonate catabolic pathway. Catalyzes the reversible glutathione-dependent isomerization of 2-hydroxychromene-2-carboxylate (HCCA) to trans-O-hydroxybe... |
Q9X9Q6 | MARTLMKPDDVKGAWAIIPTPAKDDASDWRATKTVDLDETARVVNGLIDAGINGILSMGTLGEAATMTHDEKLDFIKALVDAAAGRVPIFVGTTCLNTRDTIALTRQALDIGADGTMLGVPMWCAPSVDVAVQFYKDLAEAVPEMNIAIYANPEAFKFDFPRSFWAQVAEIPQVVTAKYIGVAHLLPDLAAIRGRIKLLPIDFDYYGAARMDESIDAFWSSGAVCDPLVTTTLRDLVSQARATGDWSAARAFMGRLGPTAAPLFPNGSFKEFSTYNIALEKARMNAGGWMNAGPVRPPYHLCPEPYLEGARLSGRMWAEL... | Function: Involved in the naphthalene and naphthalenesulfonate catabolic pathway. Catalyzes the transformation of trans-O-hydroxybenzylidenepyruvate (THBPA) to salicylaldehyde and pyruvate. The reaction is reversible. Can also use 2,4-dihydroxybenzalpyruvate (2,4-DHBP) and 2,6-dihydroxybenzalpyruvate (2,6-DHBP).
Cataly... |
Q44244 | MKLSGVELRRVQMPLVAPFRTSFGTQSVRELLLLRAVTPAGEGWGECVTMAGPLYSSEYNDGAEHVLRHYLIPALLAAEDITAAKVTPLLAKFKGHRMAKGALEMAVLDAELRAHERSFAAELGSVRDSVPCGVSVGIMDTIPQLLDVVGGYLDEGYVRIKLKIEPGWDVEPVRAVRERFGDDVLLQVDANTAYTLGDAPQLARLDPFGLLLIEQPLEEEDVLGHAELARRIQTPICLDESIVSARAAADAIKLGAVQIVNIKPGRVGGYLEARRVHDVCAAHGIPVWCGGMIETGLGRAANVALASLPNFTLPGDTSAS... | Cofactor: Binds 1 divalent metal cation per subunit . Enhanced by the addition of divalent metal ions such as Co(2+), Mn(2+) and Fe(2+) .
Function: Acts as a N-succinylamino acid racemase (NSAR) that catalyzes the racemization of N-succinyl-phenylglycine and N-succinyl-methionine . Can catalyze the racemization of a br... |
Q81IL5 | MKITAIHLYAIRLPLRNPFVISYGSYSDMPSIIVKMETDEGIIGYGEGVADDHVTGESWESTFHTLKHTLTPALIGQNPMNIEKIHDMMDNTIYGVPTAKAAIDIACFDIMGKKLNQPVYQLIGGRYHEEFPVTHVLSIADPENMAEEAASMIQKGYQSFKMKVGTNVKEDVKRIEAVRERVGNDIAIRVDVNQGWKNSANTLTALRSLGHLNIDWIEQPVIADDIDAMAHIRSKTDLPLMIDEGLKSSREMRQIIKLEAADKVNIKLMKCGGIYPAVKLAHQAEMAGIECQVGSMVESSVASSAGFHVAFSKKIITSVE... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes efficient racemization of N-succinyl-L-Arg and N-succinyl-L-Lys, suggesting that these are physiological substrates of this enzyme. Has low activity with L-Asp-L-Lys, and even lower activity with L-Leu-L-Arg, L-Leu-L-Lys, N-succinyl-L-His and N-succinyl-L-Me... |
Q9RYA6 | MAHTGRMFKIEAAEIVVARLPLKFRFETSFGVQTHKVVPLLILHGEGVQGVAEGTMEARPMYREETIAGALDLLRGTFLPAILGQTFANPEAVADALGSYRGNRMARAMVEMAAWDLWARTLGVPLGTLLGGHKEQVEVGVSLGIQAGEQATVDLVRKHVEQGYRRIKLKIKPGWDVQPVRATREAFPDIRLTVDANSAYTLADAGRLRQLDEYDLTYIEQPLAWDDLVDHAELARRIRTPLCLDESVASAADARKALALGAGGVINLKVARVGGHAESRRVHDVAQSFGAPVWCGGMLESGIGRAHNIHLSTLPNFRLP... | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Acts as a N-succinylamino acid racemase (NSAR) that catalyzes the racemization of N-succinyl-L-phenylglycine and N-succinyl-D/L-phenylalanine . Can catalyze the racemization of a broad range of N-acylamino acids, including N-acetyl-D/L-methionine, N-acetyl-... |
Q84940 | MATFKDACYYYKRINKLNHAVLKLGVNDTWRPSPPTKYKGWCLDCCQHTDLTYCRGCTMYHVCQWCSQYGRCFLDNEPHLLRMRTFKNEVTKDDLMNLVDMYDTLFPMNQKIVDKFINNTRQHKCRNECVNQWYNHLLMPITLQSLSIELDGDVYYIFGYYDDMNNVNQTPFSFVNLVDIYDKLLLDDVNFTRMSFLPVTLQQEYALRYFSKSRFISEQRKCVSDSHFSINVLENLHNPSFKMQITRNCSELSSDWNGACKLVKDTSAYFNILKTSHVEFYSISTRCRVFTQRKLKIASKLIKPNYITSNHRTSATEVHN... | Function: Plays a role in the inhibition of host innate immunity by inducing the degradation of key host factors required to activate interferon production such as IRF3, IRF5 or IRF7. Associates with components of cullin RING ligases (CRLs) including CUL1 or CUL3, which are essential multisubunit ubiquitination complex... |
A2T3M4 | MATFKDACFHYRRLTALNRRLCNIGANSICMPVPDAKIKGWCLECCQIADLTHCYGCSLPHVCKWCVQNRRCFLDNEPHLLKLRTVKHPITKDKLQCIIDLYNIIFPINDKVIRKFERMIKQRKCRNQYKIEWYNHLLLPITLNAAAFKFDENNLYYVFGLYEKSVSDIYAPYRIVNFINEFDKLLLDDINFTRMSNLPIELRNHYAKKYFQLSRLPSSKLKQIYFSDFTKETVIFNTYTKTPGRSIYRNVTEFNWRDELELYSDLKNDKNKLIAAMMTSKYTRFYAHDNNFGRLKMTIFELGHHCQPNYVASNHPGNAS... | Function: Plays a role in the inhibition of host innate immunity by inducing the degradation of key host factors required to activate interferon production such as IRF3, IRF5 or IRF7. Associates with components of cullin RING ligases (CRLs) including CUL1 or CUL3, which are essential multisubunit ubiquitination complex... |
Q10168 | MSFNPGNNQNSGFSFGKPAQPNSAAQGAATPAATGLFGNTNNNTSSTAPSGGLFGSNNASNTSAPSTFSFGKAATTGNSTNASTSSPFSFGSTNTNNTAGAKPLFGGLGSTGSANSTGDKSKNTASSATGAATTNPSGSTFNFGSSNNSFNFGKPASTTNTTTPAAASTGSLFGKPAATGTTSNAPPASSTSTTPATGSGGFSFGKPASLGSTNNASTSTTANSGFSFGKPATTSAPGSNTTVTPSSSITGTNDSKPAASNTGSAPTTGFSFGKPAGQAASTATDKGTTTTSSAGTGFSFGKPATTEDTNKPTAPNSAFT... | Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured ... |
P14907 | MNFNTPQQNKTPFSFGTANNNSNTTNQNSSTGAGAFGTGQSTFGFNNSAPNNTNNANSSITPAFGSNNTGNTAFGNSNPTSNVFGSNNSTTNTFGSNSAGTSLFGSSSAQQTKSNGTAGGNTFGSSSLFNNSTNSNTTKPAFGGLNFGGGNNTTPSSTGNANTSNNLFGATANANKPAFSFGATTNDDKKTEPDKPAFSFNSSVGNKTDAQAPTTGFSFGSQLGGNKTVNEAAKPSLSFGSGSAGANPAGASQPEPTTNEPAKPALSFGTATSDNKTTNTTPSFSFGAKSDENKAGATSKPAFSFGAKPEEKKDDNSSKP... | Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured ... |
Q45UF0 | MSEVPRFELRSKRKIGKKQKVDIFGDKDDESMLQIDCETDSLISESVSSTHSYEDYSKAYKELTLETPADVNDSASTIVDSVCEESWYDKTIKDEQTKEDKKTDKKLKRIEKVKENNQNDSMSLQIAQLSLRIQRIESETKLKTLDSAYNTIITQADNLTTPQKKSLISAILATMR | Function: Plays an essential role in the viral genome replication. Participates, together with NSP2, in the formation of viral factories (viroplasms) which are large inclusions in the host cytoplasm where replication intermediates are assembled and viral RNA replication takes place. Orchestrates the recruitment of viro... |
P19715 | MSLSIDVTSLPSISSSIFKNESSSTTSTLSGKSIGRSEQYISPDAEAFNKYMLSKSPEDIGPSDSASNDPLTSFSIRSNAVKTNADAGVSMDSSTQSRPSSNVGCDQVDFSLTKGINVSANLDSCVSISTDNKKEKSKKDKSRKHYPRIEADSDSEDYVLDDSDSDDGKCKNCKYKKRCFALRVRMKQVAMQLIEDL | Function: Plays an essential role in the viral genome replication. Participates, together with NSP2, in the formation of viral factories (viroplasms) which are large inclusions in the host cytoplasm where replication intermediates are assembled and viral RNA replication takes place. Orchestrates the recruitment of viro... |
P36358 | MSDFGINLDAICDNVKYKSSNSRTGSQVSNRSSRRMDFVDEEELSTYFNSKASVTQSDSCSNDLAVKTSIITEAVICDESEHVSADAIQEKEESIMQVDDNVMKWMMDSHDGISMNGGINFSRSKSKTGRSDFTESKSETSVSAHVSAGISSQLGMFNPIQNTVKKEAISEMFEDEDGDGCTCRNCPYREKYLKLRNKMKSVLVDMINEM | Function: Plays an essential role in the viral genome replication. Participates, together with NSP2, in the formation of viral factories (viroplasms) which are large inclusions in the host cytoplasm where replication intermediates are assembled and viral RNA replication takes place. Orchestrates the recruitment of viro... |
Q14973 | MEAHNASAPFNFTLPPNFGKRPTDLALSVILVFMLFFIMLSLGCTMEFSKIKAHLWKPKGLAIALVAQYGIMPLTAFVLGKVFRLKNIEALAILVCGCSPGGNLSNVFSLAMKGDMNLSIVMTTCSTFCALGMMPLLLYIYSRGIYDGDLKDKVPYKGIVISLVLVLIPCTIGIVLKSKRPQYMRYVIKGGMIIILLCSVAVTVLSAINVGKSIMFAMTPLLIATSSLMPFIGFLLGYVLSALFCLNGRCRRTVSMETGCQNVQLCSTILNVAFPPEVIGPLFFFPLLYMIFQLGEGLLLIAIFWCYEKFKTPKDKTKMI... | Function: As a major transporter of conjugated bile salts from plasma into the hepatocyte, it plays a key role in the enterohepatic circulation of bile salts necessary for the solubilization and absorption of dietary fat and fat-soluble vitamins . It is strictly dependent on the extracellular presence of sodium . It ex... |
O08705 | MEAHNVSAPFNFSLPPGFGHRATDTALSVILVVMLLLIMLSLGCTMEFSKIKAHFWKPKGVIIAIVAQYGIMPLSAFLLGKVFHLTSIEALAILICGCSPGGNLSNLFTLAMKGDMNLSIVMTTCSSFTALGMMPLLLYIYSKGIYDGDLKDKVPYKGIMLSLVMVLIPCAIGIFLKSKRPHYVPYVLKAGMIITFSLSVAVTVLSVINVGNSIMFVMTPHLLATSSLMPFTGFLMGYILSALFRLNPSCRRTISMETGFQNVQLCSTILNVTFPPEVIGPLFFFPLLYMIFQLAEGLLFIIIFRCYLKIKPQKDQTKIT... | Function: As a major transporter of conjugated bile salts from plasma into the hepatocyte, it plays a key role in the enterohepatic circulation of bile salts necessary for the solubilization and absorption of dietary fat and fat-soluble vitamins . It is strictly dependent on the extracellular presence of sodium . It ex... |
O07566 | MQKQVKISGKSKENMSLLKHLKGDVQGKELVIEDSIVNERWKQVLKEKIDIEHDLFNYQKNREISKVPFLPVDRLITNDEVEDILNTLTEVLPTGKFTSGPYLEQFEKVLSTYLHKRYVIATSSGTDAIMIGLLALGLNPGDEVIMPANSFSATENAVLASGGVPIYVDINPQTFCIDPDKIEEAITPYTKFILPVHLYGKHSDMQHIRQIANRYKLKVIEDACQGIGLTDLGKYADITTLSFNPYKNFGVCGKAGAIATDNEELAKKCIQFSYHGFEVNVKNKKVINFGFNSKMDNLQAAIGLERMKYLSLNNFKRLFL... | Function: Involved in the biosynthesis of kanosamine (3-amino-3-deoxy-D-glucose), which is known to have antibiotic and antifungal properties, and to be a precursor of the antibiotic neotrehalosadiamine (3,3'-diamino-3,3'-dideoxy-alpha,beta-trehalose (NTD)). Catalyzes the reversible pyridoxal phosphate-dependent transa... |
O07565 | MLLSKKSEYKTLSTVEHPQYIVFCDFDETYFPHTIDEQKQQDIYELEDYLEQKSKDGELIIGWVTGSSIESILDKMGRGKFRYFPHFIASDLGTEITYFSEHNFGQQDNKWNSRINEGFSKEKVEKLVKQLHENHNILLNPQTQLGKSRYKHNFYYQEQDEINDKKNLLAIEKICEEYGVSVNINRCNPLAGDPEDSYDVDFIPIGTGKNEIVTFMLEKYNLNTERAIAFGDSGNDVRMLQTVGNGYLLKNATQEAKNLHNLITDSEYSKGITNTLKKLIGS | Function: Involved in the biosynthesis of kanosamine (3-amino-3-deoxy-D-glucose), which is known to have antibiotic and antifungal properties, and to be a precursor of the antibiotic neotrehalosadiamine (3,3'-diamino-3,3'-dideoxy-alpha,beta-trehalose (NTD)). Catalyzes the dephosphorylation of kanosamine 6-phosphate to ... |
O07564 | MKKIGIIGAGGIARAHATALSTIKNAELVGVYDINQQNAESFVKTFGGKSFENVDELIDASEGLIVASPNFCHKEHALQALGKHKHVLCEKPMAISLEEASIMKDTAERLSVRASMGFNYRYLSYVNILKSLIINNELGNILSIKVHFKKNSALRRKKFTWRDDANSKKTSGSLGDLGIHLIDMVWYLFESDFITESVRAKMNTNVKTKEDKQVLVDDYAEIYGQLKNKVFVNIITSKCSVPEDCGFSIEVVGHKKEFKYHTGNPHVYKLIDGLNVVDCPVPQSLLNDPPNEFYGWADSFRSELINWIASTQNDWVEIPS... | Function: Involved in the biosynthesis of kanosamine (3-amino-3-deoxy-D-glucose), which is known to have antibiotic and antifungal properties, and to be a precursor of the antibiotic neotrehalosadiamine (3,3'-diamino-3,3'-dideoxy-alpha,beta-trehalose (NTD)). Catalyzes the oxidation of glucose 6-phosphate to 3-oxo-D-glu... |
Q03614 | MQLVPTDDPDEKIGRTSNGMQNATLPIDGPVNTEPKDPAREQWSGKLDFLLSVVGFAVDLGNIWRFPYLCFKNGGGVFLIPYSIMVLLTGVPLFYMELCLGQYYRKGAITTWGRICPLFKGIGYCVILTAFYVDFFYNVILAWGLHYLYTSFSFNLPWASCNNSYNSPACYEPHWSEDGTAMCRSANQSVSAEKISAAEEYFYKGFLGLHEANAPNSHVIRSVTDLGNVRWDIALSLFVVYLICYFSMWKGIHTSGKVVWFTALFPYVVLGILFIRGVTLPGWQNGIEYYLRPNFEMLKRPSVWQDAATQVFFSLGPGFG... | Function: Dopamine transporter . Terminates the action of dopamine by its high affinity sodium-dependent reuptake into presynaptic terminals.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 69266
Sequence Length: 615
Subcellular Location: Cell membrane
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Q74LQ9 | MAGWFTETQNKAYKDAMSALNANPTIDLENSYVPLQNQYKDIRVDEHPEYLHDKEWAQATYNGDLVGIKTSDVMLGVYVPKEEDVGLGMELGYAMSQGKYVLLVIPDELYGESINLMSWGVADNVIKMSELATFDFNRPRYNFYDGAVY | Function: Catalyzes the cleavage of the glycosidic bond of 2'-deoxyribonucleosides and the transfer of the deoxyribosyl moiety to an acceptor purine or pyrimidine base.
Catalytic Activity: 2-deoxy-D-ribosyl-base(1) + base(2) = 2-deoxy-D-ribosyl-base(2) + base(1).
Sequence Mass (Da): 16941
Sequence Length: 149
Pathway: ... |
Q9R5V5 | MPKKTIYFGAGWFTDRQNKAYKEAMEALKENPTIDLENSYVPLDNQYKGIRVDEHPEYLHDKVWATATYNNDLNGIKTNDIMLGVYIPDEEDVGLGMELGYALSQGKYVLLVIPDEDYGKPINLMSWGVSDNVIKMSQLKDFNFNKPRFDFYEGAVY | Function: Catalyzes the cleavage of the glycosidic bond of 2'-deoxyribonucleosides and the transfer of the deoxyribosyl moiety to an acceptor purine or pyrimidine base.
Catalytic Activity: 2-deoxy-D-ribosyl-base(1) + base(2) = 2-deoxy-D-ribosyl-base(2) + base(1).
Sequence Mass (Da): 18080
Sequence Length: 157
Pathway: ... |
Q6YNI5 | MKNTDPVANTKIYLATSFFNEEQRARIPQALAQLEANPTVGVVHQPFDFQYKDARVDSDPAGVFGSLEWQIATYNNDLNAVGTSDVCVALYDMDQIDEGICMEIGMFVALHKPIVLLPFTKKDKSAYEANLMLARGVTTWLEPNDFSPLKDFNFNHPMAQPFPPFKVF | Function: Catalyzes the cleavage of the glycosidic bond of 2'-deoxyribonucleosides and the transfer of the deoxyribosyl moiety to an acceptor purine or pyrimidine base.
Catalytic Activity: 2-deoxy-D-ribosyl-base(1) + base(2) = 2-deoxy-D-ribosyl-base(2) + base(1).
Sequence Mass (Da): 18896
Sequence Length: 168
Pathway: ... |
Q27895 | MWLPVYVPLLLVFGVSLSLPHGSLGTDSSSLRGVDADTEKRINVGKTHLQTLRNLETRCHDSLQALVVIDAGSSSTRTNVFLAKTRSCPNKGRSIDPDSIQLIREGKRFTGLRVVLEEWLDTYAGKDWESRPVDARLLFQYVPQMHEGAKKLMQLLEEDTVAILDSQLNEEQKVQVKALGIPVMLCSTAGVRDFHEWYRDALFVLLRHLINNPSPAHGYKFFTNPFWTRPITGAEEGLFAFITLNHLSRRLGEDPARCMIDEYGVKHCRNDLAGVVEVGGASAQIVFPLQEGTVLPSSVRAVNLQRERLLPERYPSADVV... | Function: May perform an important processing step in the conversion of high energy nucleotides prior to uptake by the parasite. NTPAse-II has a specific activity 4.5-fold lower than NTPAse-I in hydrolysis of ATP. The primary difference between these isozymes lies in their ability to hydrolyze nucleoside triphosphate v... |
Q7T0V6 | MGLLERLRKEWFIVGIILVIAAAKLEPTVGVKGGPLKPEITITYIAVSAIFFNSGLSLKTEELTNALMHVKLHLFVQLFTLVFFPTAIWLFLQVLSLTPINEWLLKGLQTVSCMPPPVSSAVILTKAVGGNEAAAIFNSAFGSFLGIVVTPLLLLLFLGSSSSVPFTSIFSQLFMTVVVPLIIGQIVRRYIKDWLERKKPPFGAISSCVLLMIIYTTFCDTFSNPNIDLDTFSLVVIVFIIFFIQLAFMLLTFLFSTSKNSGFTPADTVAIVFCSTHKSLTLGIPMLKIVFVGYEHLSLISVPLLIYHPAQILLGSVLVP... | Function: Involved in teeth and skeletal development. Has an essential role in the biosynthesis and trafficking of glycosaminoglycans and glycoproteins to produce a proper functioning extracellular matrix. Required for extracellular matrix mineralization. Also involved in the regulation of cellular calcium homeostasis.... |
Q08636 | MQIGKIIKVSGPLVMAENMSEASIQDMCLVGDLGVIGEIIEMRQDVASIQVYEETSGIGPGEPVRSTGEALSVELGPGIISQMFDGIQRPLDTFMEVTQSNFLGRGVQLPALDHEKQWWFEATIEEGTEVSAGDIIGYVDETKIIQHKIMVPNGIKGTVQKIESGSFTIDDPICVIETEQGLKELTMMQKWPVRRGRPIKQKLNPDVPMITGQRVIDTFFPVTKGGAAAVPGPFGAGKTVVQHQIAKWSDVDLVVYVGCGERGNEMTDVVNEFPELIDPNTGESLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDM... | Function: Involved in ATP-driven sodium extrusion.
Catalytic Activity: ATP + H2O + 4 Na(+)(in) = ADP + H(+) + 4 Na(+)(out) + phosphate
Sequence Mass (Da): 65770
Sequence Length: 593
EC: 7.2.2.1
|
P52914 | MELLIKLITFLLFSMPAITSSQYLGNNLLTSRKIFLKQEEISSYAVVFDAGSTGSRIHVYHFNQNLDLLHIGKGVEYYNKITPGLSSYANNPEQAAKSLIPLLEQAEDVVPDDLQPKTPVRLGATAGLRLLNGDASEKILQSVRDMLSNRSTFNVQPDAVSIIDGTQEGSYLWVTVNYALGNLGKKYTKTVGVIDLGGGSVQMAYAVSKKTAKNAPKVADGDDPYIKKVVLKGIPYDLYVHSYLHFGREASRAEILKLTPRSPNPCLLAGFNGIYTYSGEEFKATAYTSGANFNKCKNTIRKALKLNYPCPYQNCTFGGI... | Function: Might be involved in RNA transport out of nuclei.
Catalytic Activity: a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + H(+) + phosphate
Sequence Mass (Da): 50072
Sequence Length: 455
Subcellular Location: Nucleus
EC: 3.6.1.15
|
Q9BSD7 | MARHVFLTGPPGVGKTTLIHKASEVLKSSGVPVDGFYTEEVRQGGRRIGFDVVTLSGTRGPLSRVGLEPPPGKRECRVGQYVVDLTSFEQLALPVLRNADCSSGPGQRVCVIDEIGKMELFSQLFIQAVRQTLSTPGTIILGTIPVPKGKPLALVEEIRNRKDVKVFNVTKENRNHLLPDIVTCVQSSRK | Function: Has nucleotide phosphatase activity towards ATP, GTP, CTP, TTP and UTP. Hydrolyzes nucleoside diphosphates with lower efficiency.
Catalytic Activity: a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + H(+) + phosphate
Sequence Mass (Da): 20713
Sequence Length: 190
EC: 3.6.1.15
|
Q9CQA9 | MSRHVFLTGPPGVGKTTLIQKAIEVLQSSGLPVDGFYTQEVRQEGKRIGFDVVTLSGAQGPLSRVGSQPLPGKPECRVGQYVVNLDSFEQLALPVLRNAGSSCGPKHRVCIIDEIGKMELFSQPFIQAVRQMLSTPGIIVVGTIPVPKGKPLALVEEIRKRRDVKVFNVTRDNRNSLLPDIVAVVQSSRT | Function: Has nucleotide phosphatase activity towards ATP, GTP, CTP, TTP and UTP. Hydrolyzes nucleoside diphosphates with lower efficiency.
Catalytic Activity: a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + H(+) + phosphate
Sequence Mass (Da): 20667
Sequence Length: 190
EC: 3.6.1.15
|
P43439 | MAVTKMEKVTLISDKKNREILLQAVQGLHAVEIRDLFQESENNQWVETFFPEPEMIDKDKELAKLSYKLTDIRTAIQFIEHHGEKSQKKQHLKRRELSLDTLEKNYSEEAFSKKLEEVLLLKEQWEQLVDERQQLEDQENWLLNWQNLDLAPKAFDSQMTKLVIGTVNAKNAESFKAEVAEINEAYLEEINSSPTTTYFAYIVLRADESRMEEIASRYGFVKEDYLYEGTPQQQLVAAKQSLQEIKDQQKKLSSAIGACSGYIKDFEWTEEIFLARSEREAIKDRIIHTPYLILIQGWVDHEEKQELIHMLQNILASEEV... | Function: Involved in ATP-driven sodium extrusion.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 75504
Sequence Length: 664
Subcellular Location: Cell membrane
|
A6L8E5 | MLENLKKYKIVLASNSPRRRNLLSGLDIDFEVRVISDIDESYPDSIDSMEIPLYIARSKAEAYKPTMADDELLITADTIVWTFDGVMGKPANREEAYAMLHALSDHVHQVITGVCIMTKDKNVGFSVESAVCFAKLGDEEINYYLDKYKPYDKAGGYGIQEWIGYIGVEAINGSFYNVMGLPVQKLYQELKHF | Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: dTTP + H2O = diphosphate + dTMP + H(+)
Sequence Mass (Da): 21836
Sequence Length: 193
... |
Q6MDL5 | MKIILGSQSPRRKEILNFFSLPFEQVSPVFDEETVPFGGNPEHYVLSLSAGKTKSLRYQFPKDILISADTIVYKEGKVFGKPRSKEEAFQNLRELAGHWHSVYTGVNVSNENQEIQQFEETKVLFNSLTDDEIHQYQEKIHCADKAGGYMVQGAGSLIIKKLEGCYYNVMGLPINTLRLCLSEIGIDLWKYLKD | Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: dTTP + H2O = diphosphate + dTMP + H(+)
Sequence Mass (Da): 22112
Sequence Length: 194
... |
Q9CLG6 | MTDFQFYLASNSPRRAQILQQLGFRFALCCCEIDETPLPDEKGADYVLRMAIEKNNAARQQWQQAKFSQNRPHLPFLSADTSVILEDKILGKPKNEADARAMLRALSARTHQVITAVCVADENQMQTVIQTSHVRFKVLTEKEIQGYIATGEPMDKAGAYGIQQLGGVFVEHIEGSFSGVMGLPVCETVALLKAFGVELF | Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: dTTP + H2O = diphosphate + dTMP + H(+)
Sequence Mass (Da): 22225
Sequence Length: 200
... |
A5D426 | MKEIVLASSSPRRRDLLKQLGLTFRIMTAGVDETPPGGLTPAEMVEVLAGRKAAAVAGMLEDALVIGADTVVVLNGRVLGKPADREEAAGMLRQLQGTDHTVYTGVAVMDAASKKMQVAHEKTRVFFKSLDEHEIRRYVATGEPMGKAGAYAVQGRAAAFIKGLEGCYTNVVGLPLARLADMLKKFGYNVL | Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: dTTP + H2O = diphosphate + dTMP + H(+)
Sequence Mass (Da): 20430
Sequence Length: 191
... |
Q12C38 | MPAADFVYLASQSPRRAQLLEQLGVRYQRLAPAPDEDTEALEAVLGKESPVAYVKRVTRLKLDAASERAKRQGLAPAPILCSDTTVALGRSILGKPANAAEATRMLRQLSGATHRVLTAVAVQQGRRRIEALSISRVTFAPMTAAQISSYVASGEPMGKAGAYAVQGRVAMYISHISGSYSGIMGLPLHETAWLLRAAGLKI | Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: dTTP + H2O = diphosphate + dTMP + H(+)
Sequence Mass (Da): 21554
Sequence Length: 202
... |
Q7MWG0 | MLDNLKKYKIVLGSQSPRRKELLSGLDIRFEQKAMPDIAEDYPAGLDREKVPLYLARMKAEAYRSKGMMQDSTLLITADTVVIIDGTILGKPQDREEAARMLRTLSGRTHQVVTGVCISHRWETRAFSCSSLVTFAHLSDEEIDYYLERYRPYDKAGSYGIQEWIGYIAIQRVEGSFYNVMGLPVHLLYNELKDFGESN | Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: dTTP + H2O = diphosphate + dTMP + H(+)
Sequence Mass (Da): 22766
Sequence Length: 199
... |
Q9HVU3 | MPSLYLASASPRRRELLTQIGVPLSVLVTAIDESPLPNEAPAAYVERLARGKAAAGLAMLEGRGEDGCVLGADTSVVIDGRILGKPVDQADGLAMLAALSGREHQVLTAVALAAAGGVEARVVECRVRFRQVAPEEALRYWQSGEPADKAGGYAIQGLGAIFVSRIEGSYSAVVGLPLCETAELLREFGIPCWQPVGGNPP | Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: dTTP + H2O = diphosphate + dTMP + H(+)
Sequence Mass (Da): 20974
Sequence Length: 201
... |
Q88PB4 | MTPLYLASGSPRRRELLTQIGVPFIVISAPVDESPLPSESAPAYVERLARAKAAAGLVSVDGPAVVLGADTAVVLDGRILGKPENREDALAMLADLSGREHQVLTAVALDDGQRVHSFCVTSTVRFRAISTDEAQRYWASGEPSDKAGGYAIQGLGAVFVSGLSGSYSAVVGLPLCETADLLGQFGIACWQSLAHTPEVTNPQ | Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: dTTP + H2O = diphosphate + dTMP + H(+)
Sequence Mass (Da): 21232
Sequence Length: 203
... |
B0JH94 | MSIPLILASASPARKKLLQMVGIDPIVRVSNFDESTINADDTLHLVQTLAQCKAQTIAPKFDTGLILGCDSVLEVAGEVYGKPKDKSEAIERWQKMRGQVGTLYTGHALIDRVNNQTLTRCGITKVHFANISDETIIAYVDTEEPLKCAGCFALEGKGGLFVERLEGCHSNVIGLSLPLFRQMLTDFGYQITDFW | Function: Nucleoside triphosphate pyrophosphatase. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-phosphate + diphosphate + H(+)
Sequence Mass (Da): 214... |
B2HEK5 | MTRLVLGSASSGRLKVLQQAGVDPLVVVSGVDEDAIMAGLGPAATPADVVRVLARAKAEQVATTLTGQQASVATDCLVIGCDSMLYIDGRLCGKPETVDDARQLWRSMAGRCGHLYTGHSVVRLTEQRVTHRDDETSTTTVHFATPSDDDLEAYLATGESLKVAGGFTLDGLGGWFITGVEGDPSAVVGIGLPLTRDLISRAGISIAALWASNPLP | Function: Nucleoside triphosphate pyrophosphatase. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-phosphate + diphosphate + H(+)
Sequence Mass (Da): 225... |
A0QTE5 | MTRVVLGSASSGRLSVLRNAGIEPLVVVSDVDEDAIIAAHPSAPPDQVVTALASAKAGEVVTRLSHSDAADAVVIGCDSMLLLDGKLCGKPGSVDAAHRQWQTMSGRSADLVTGHCVIRLHDGEIVGNVTESSGTTVHFGTPSPDDLSAYLATGEPLWVAGAFTLDGLGGWFIDRIEGDPSNVIGVSLPVLRALFERLEVSVADLWSANGR | Function: Nucleoside triphosphate pyrophosphatase. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-phosphate + diphosphate + H(+)
Sequence Mass (Da): 218... |
Q1DAV2 | MSELILASTSSARRALMDGLRLPYRAEAPGVDEVVAPHLSVTEAVRELASRKARAVHQRHPEAWVLGADQLVEVAGEVLSKPVDRNAAREQLRKLVGHTHAIHTGVCLVGPGGKVLDAVETTRLTFYRVKEEELERYLDLNEWEGCCGSYRVEDAGQALLERLDGDRSNVQGLPMVTVVRLLREAGFRFF | Function: Nucleoside triphosphate pyrophosphatase. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-phosphate + diphosphate + H(+)
Sequence Mass (Da): 210... |
Q7NGP8 | MNIDLAALNAGTLWPEYIVTITLIVVLLVDLISGRKASWSLPYLALLGLGIATATLLPMWILENPVSFLGSFTADPLSVVFRAFILISAALTVLMSVRYINQSSLATAEFYVLLLGATLGAMLLSGSSEMAMIFVALELLSITSYLLSGYAKLDKRSNEASLKYLLIGAASSGIFLYGMSLLYGFSGGQTQLTEIAPRIVNLGFPALLSLVLVAAGICFKLSAVPFHQWTPDVYEGSPTPVVAFLSVGSKAAGFALAIRFMTSAYPGFSEQWQTLFVLLAILSMVLGNVVAIAQTSMKRMLAYSSIAQAGYVMIGLAIGT... | 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... |
P06257 | MKLELDMFFLYGSTILPECILIFSLLIILIIDLTFPKKDTIWLYFISLTSLLISIIILLFQYKTDPIISFLGSFQTDSFNRIFQSFIVFCSILCIPLSIEYIKCAKMAIPEFLIFILTATVGGMFLCGANDLVTIFVSLECLSLCSYLLCGYTKRDIRSNEAAIKYLLIGGTSSSILAYGFSWLYGLSGGETNIQKITNGLLNAETYNSSGTFIAFICILVGLAFKLSLVPFHQWTPDIYEGSPTPVVAFLSVTSKIAGLALATRILNILFSFSPNEWKIFLEILAILSMILGNLVAITQTSMKRMLAYSSISQIGYILI... | 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... |
Q4JQI6 | MSPYITASLLFGLLLGPTITATSSHWLIAWMGLEINTLAIIPLMAQHHHPRAVEATTKYFLTQATAAAMLLFASTTNAWLTGQWELQQMTHPLPSTLIILALALKIGLAPLHTWLPEVLQGLDLTTGLILSTWQKLAPFALLLQLQPNNPTLLVILGVLSTLIGGWGGLNQTQLRKILAYSSIAHLGWMILILQFSPTLTLLTLMLYLIMTSSAFLTFILNKTTTINALATSWAKTPILTSLLPLVLLSLGGLPPLTGFMPKWLILQELTKHDLAPTATLAALSALLSLYFYLRLSYAMTLTIAPNNLTGTLPWRTQTTQ... | 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... |
Q37382 | MTLEYIYIFIFFWGAFFISCLLIFLSYFLVYQESDIEKNSAYECGFQPFEDTRSKFNVRYYLIAILFMIFDLEIMYLFPWSISISTGSFFGVWAIFLFLIILTVGFIYEWQKGALEWD | 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... |
B0FWD2 | MIIFTITIIVMMLATILSKKTITDREKSSPFECGFDPMNYSRLPFSLRFFLIAIIFLIFDVEIALILPMILIIKTSNLMNWSMTSLFFIFILLIGLYHEWNQGALEWNN | 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... |
Q3L6W3 | MNLIMTLFINITLTSLLVLIAFWLPQLNIYTEKTSPYECGFDPMGSARMPFSMKFFLVAITFLLFDLEIALLLPLPWATQTVNLTTMLTTALLLISLLAVSLAYEWTEKGLEWTE | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity of complex I.
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NA... |
P48907 | MILYVLPTSLSLCLLLMIIYLLTANLFKFASYELKTPFECGFDPLSNMRSPMTTRFFILTVLFLIFDVEVVLLFPVLSMVSFMTSPLIIMSIILFMMVLLIGLLYEMYYGVLDWVLN | 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... |
Q37399 | MTYLVYIVFTIVLTVGLILVSYLLSQAQPDSEKVSAYECGFSPLGDARQKFDVSFYLIAILFIIFDLEVVFILPFASVIHNVSLLGGWITIIFLVILTIGFIYEFVSGAITDSF | 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... |
P34850 | MLMLSTMTLIIFIITIVVMMLATLLSKKTLLDREKCSPFECGFDPMNSSRLPFSLRFFLIAIIFLIFDVEIALLLPMIMIIKTSNLMNWTITSLFFIFILLIGLYHEWNQGALEWNE | 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... |
P34851 | MKFIFMYFIFIILISSILLLLNKFISIYKKKDYEKSSPFECGFNPITKANLPFSLPFFLMTMMFLIFDVEIILFLPIIFYLKSSSTMISYLMISIFLILLITTLILEWMNNYLNWLF | 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... |
P92533 | MMLEFAPIFIYLVISLLVSLILLGVPFLFASNSSTYPEKLSAYECGFDPFGDARSRFDIRFYLVSILFLIFDLEVTFFFPWAVSLNKIDLFGFWSMMAFLFILTIGFLYEWKRGALDWE | 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... |
P19043 | FYYINPREFVNKKVCLDREKSSPFECGFDPLEFLSYPLFIRFFVITLIFLIFDVEIYLLLPMVYLNMSSP | 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... |
Q37709 | MILIWLSIFMLVFIMLTLGMFVNKKVSLDREKSSPFECGFDPLNSSRTPFSIRFFVITLIFLIFDVEIYLLLPMVYLNMSSPTTYLIIFFTFILVAGVFYEWSEGALSWIK | 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... |
P72823 | MLEHFPWLTTMIALPLVAALFIPLIPDKDGKQVRWYALGVGLADFVLMSYVFWTNYDISSTGFQLQEKFSWIPQFGLSWSVSVDGISMPLVLLAGLVTTLSIFAAWQVDHKPRLFYFLMLVLYAAQIGVFVAQDMLLLFIMWELELVPVYLLVCIWGGQKRQYAAMKFLLYTAAASVFILVAALGLAFYGDVTTFDIAELGLKDYPIALELFLYAGLLIAFGVKLAIFPFHTWLPDAHGEASAPVSMILAGVLLKMGGYGLIRLNLGLLEDAHVYFAPILVILGVVNIIYGGFSSFAQDNMKRRLAYSSVSHMGFVLLGI... | Function: NDH-1 shuttles electrons from NAD(P)H, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hyd... |
Q32RM1 | MLQNYLCVAAYLFCIGIYGLIISRSMVRALMCLELMLNGVNLNLVAFATYLDNQEIKGQVFAVFIIAIAAAEAAIGLAIVLNIYRNRNSVRVDQFDILKW | 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... |
P48928 | MTIYSYLLLLCMVMFVTFFTQKNNILSLMVVLESLMLITLSSVAVSLNYMAGSSMVMILLLCFAAAEAALSLSLLVCFIQVNSSCEMLAMNKILFAKKS | 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... |
Q37403 | MLLEIITAYKIGTILFLIGILGFIINRQNILLLIISIEMTLLAISFIIICSALFLDDSAAACFSLYILALAGSEAAIGLSLLVLFHRFRGSVLISASRQ | 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... |
P34859 | MKLLFVMMLLFFMFLWYYNVNFLSFLILMEFLVITVLFFIIGYEINSWLFLIFLVFSVCELVLGLSLLVSMNYELGHQKLSVMDLIY | 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... |
Q04614 | MDLIKYFTFSMIIFILGIWGILLNRRNILIMLMSIELMLLAVNLNFLVFSVSLDDMMGQVFALLVLTVAAAESAIGLAIFVITFRVRGTIAVEFINSIQG | 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... |
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