ids
stringlengths 6
10
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stringlengths 16
1.02k
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stringlengths 117
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A0A485L2H4 | MILTNGSVATKSLQLRPHRPLEEQTTRDGPARHHVVPFHNPHAPYQPNQRQRPAFNQPQQQYQGNDGFYDPTPAAGAHGGYPDQQAFHRQAPPAPVGGDPKYMGGGAPSAYPDGMMGSNPNQMGAFFGEVGQAVNPELMKFVAFLDVVIVSRRCSNPMAAYAMNQGAKLMEDQVKSFMPGAAAGAMNMFGSVKYYFTVNNTYVLTRLKMLLCPFLHKDWRRIVQTEGGDGRDVTYAPPSMDKNAPDLYIPLMSFVTYILIVGYIKGASGRFNPNVITDVSTYCCFMQAVEICFMKLGLYLLNSQINWLDLVSFTGYKYVPLVINTLVHLVLGPIPYYCVLAYTGIATSFFTLNGLKGTVPEPAYEQRRFRNYMLLAMAVLQLLLIWWNSYSSEIQ | Function: Has a role in transport between endoplasmic reticulum and Golgi.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 395
Sequence Mass (Da): 44035
Location Topology: Multi-pass membrane protein
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A0A291LM93 | MNETLIHKWNLFYQDALTKTDPRTNNLPLVWNDPTPVLYLVTAYLLMVLTGKRIMSYLPEIKVPSWILFAYNFGLVLLSAYMFMEIVVGVYQSGYNYACGEINHKPEETRVTKALWWYFFSKAIEFLDTFWMIIRKRFNQVTFLHVFHHSTMLMIWWVVISWIPAGQAYFGAALNCVVHVFMYTYYAFSVIPSLKDKLWWKKYITTFQLVQFVITFTHTMNGIYLTMSGKCSFPMWGQILLSSYMVIMLVLFGNFYIHEYIKKTNDAKRRKNQTKDLNNNLIKEDKKKYFENNKQKAKKAD | Catalytic Activity: a very-long-chain acyl-CoA + H(+) + malonyl-CoA = a very-long-chain 3-oxoacyl-CoA + CO2 + CoA
EC: 2.3.1.199
Subcellular Location: Membrane
Sequence Length: 301
Sequence Mass (Da): 35796
Location Topology: Multi-pass membrane protein
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A0A183DFV3 | MLQKATTLPPIFLFVVDTCLTAEELNALKESLQTALSLLPADVLVGLITFGRMVELHELNVRGVSRAYVFRGTKEVKQKQIRDVLARDIGRPVNAGPAPGAYPPGAPGAMAQQLPRFPMAPGGPAAAVPGAPSMQGAHGTPNLPFNKFLQVCLLLHSALT | Function: Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules.
Subcellular Location: Cytoplasmic vesicle
Sequence Length: 160
Sequence Mass (Da): 16945
Location Topology: Peripheral membrane protein
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A0A485KQR1 | MIKTTYLVLFNLASCLGWAYVLGQTFQLVYADQDIEKSSQTLWGVVEGPLKIVQTMALMEVLHAMLGLVRSPVGSTFMQVSSRLFLLWAINVLCPDSRYHWGFILMVASWSLVEVPRYAFYALNLLDAVPDWLFFLRYHLFMVLYPSGITGEVTCMLKALPLLASGAYSVQMPNTHNVAISLYIVVVITLITYIPGSPFMFNHMNIQRKKAYAKKNEVKTLKKD | Pathway: Lipid metabolism; fatty acid biosynthesis.
EC: 4.2.1.134
Subcellular Location: Membrane
Sequence Length: 224
Sequence Mass (Da): 25415
Location Topology: Multi-pass membrane protein
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A0A4P9X6L4 | WLWIFPLVTFGLGCWQVYRLRWKRRLIETLEQRSKEPPVPLSALTDEVGRPFTLGAPGQPTYAEFTRVTITGEFLHDQEMYLGPRNRNDAAGVGGGIISNGAGIGYYVFTPFRLAGSGHTILVNRGWIPKAARAQRVPGRDDVTGPVTLVGMTRHGEPSNAFALTNKPQQNEWFWIEVEAMAAHTGALPVLVEMQRAGMALSSPGALMPASPAPRATEIKVRNTHLEYAITWFGLFAFSTWWITRRPRFHR | Function: Probably involved in the biogenesis of the COX complex.
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 251
Sequence Mass (Da): 28084
Location Topology: Multi-pass membrane protein
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A0A5D3D5W8 | MAKTLFIGVLLLGKLAKAGNHVFIHTIKFQPFSILRIKCRKEGGIRYTVSGYGIYLSVLISNVAGAGDVSAVKIKGTRTGWLPMGRNWGQNWHINADLNHQALSFEVTSSDGVTISSYNVAPKDWNFGQTFEGKQFES | Function: Causes loosening and extension of plant cell walls by disrupting non-covalent bonding between cellulose microfibrils and matrix glucans. No enzymatic activity has been found.
Subcellular Location: Secreted
Sequence Length: 138
Sequence Mass (Da): 15191
Location Topology: Peripheral membrane protein
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A0A815CH99 | MEHDQEQAIKNLVVYCYKFYSDNKAELNIISEFQDDYRQEQAIWWYTQESFVYHMLNRALRTLDVDTIINMGFFIRDLHQQLHQLHEQQFPNYHGRPFIVYRGQALLKTDFDKLRKTKDGLLSFNSFLSTSAQPDLPLVYAESSSGNVDKVGIFFIMTIDPRVSSTPFASIKEASYYSDEDEILFSMHTVFRIGTIKQMDNNDQLYQVELQLTADNDEQLQRLTKYISKEVGGDTGWERLGSLSLKIGHFDKAEELYKVLLVQTLNEDDRALYYNQLGSVKHGQGDYEQAIKYFKQGLEIAEETLSANRPSLAVSYNNIGEMYREMGEYSKALSFHEKVLGIEEKTLSANHPSLATSYNNIASVYNNMGEYSKALSCYEKALGILKLTLPANHRSLATSYSNIGSVYNNMGGYSKALSFH | Function: Kinesin is a microtubule-associated force-producing protein that play a role in organelle transport.
Catalytic Activity: L-arginyl-[protein] + NAD(+) = H(+) + N(omega)-(ADP-D-ribosyl)-L-arginyl-[protein] + nicotinamide
Subcellular Location: Cytoplasm
Sequence Length: 420
Sequence Mass (Da): 48208
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A0A183D3Z4 | MTILQYMCYLGWMKVAASLMNPYGDDEDDFECNYLIDKNTATAMFIVDSAHNDIPDLEKDMFWSKSEVELFYPIGSKDSVRNPHIGTAVQAR | Function: Forms chloride channels.
Subcellular Location: Cell membrane
Sequence Length: 92
Sequence Mass (Da): 10534
Location Topology: Multi-pass membrane protein
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E6PBW3 | KALMDDNVMKKYTTRSDEARHYVQYDQGEDRWLCTLLLQRGYRVEYSAASDAYTHCPEGFNEFYNQRRRWVPSTIANIMDLLADAKRTIKINDNISLLYIFYQMMLMGGTILGPGTIFLMLVGAFVAAFRIDNWTSFHYNIVPILAFMFICFTCKSNIQLFVAQVLSTAYALIMMAVIVGTALQLGEDGIGSPSAIFLISMVGSFFIAACLHPQEFWCITCGLIYLLSIPSMYLLLILYSIINLNVVSWGTREVVAKKTKKELEAEKKAAEEAKKRVKQKSMLSFLQSGIGDNGDEEGSVEFSLAGLFRCIFCTHGKTSDEKQQLTSIAESLDTIKHRMDTIESAVDPHGHHASRHGRRRTTSSGSKDHHLLTSVAEKSGDESDESDSDTSAEPKQERDFLTNPYWIEDPDVRKGEVDFLSSTEIQFWKDLIDQYLYPIDNDPVEQVIYTHMLLILNLIFFGVNSCLKYIIS | Catalytic Activity: [(1->4)-N-acetyl-beta-D-glucosaminyl](n) + UDP-N-acetyl-alpha-D-glucosamine = [(1->4)-N-acetyl-beta-D-glucosaminyl](n+1) + H(+) + UDP
EC: 2.4.1.16
Subcellular Location: Membrane
Sequence Length: 472
Sequence Mass (Da): 53478
Location Topology: Multi-pass membrane protein
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A0A815YWA5 | MKVEIETAFIYKSLCQVDADVIDRLNSRYTTFALIGCFLIIAAKIYVGNPINCWTPTQFQSIHSTYVNSICWLKGTYYLPTEEIKIPDRSVPRMYLVSYYQWTTLALVLMALLFILPGQTWQTFSYQSGVNLKNLIKMIKENRHDKEKLDHVIR | Function: Structural component of the gap junctions.
Subcellular Location: Cell membrane
Sequence Length: 154
Sequence Mass (Da): 17981
Location Topology: Multi-pass membrane protein
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A0A183E5D8 | MCIFQNNQGGVITLQMEEDRLGMSITGDVAEIEKNGKGLIGISIGGGAPYCPCIYVVQVSEDSPVARDGRIQAGDEIVSVNGILVKGEKKTAVAAMIQRSDGRVKIGFNVLHAEPKQGHTLDIALKKMKHRVVESMTAETADALGLSRAIICNDLLLRKLSRLEHSAQLYRKLIKHLGELLSCHYRVARTQKDFGDLFCEIAARESSAAANAALTTFGEAHRALEKHTVKSVFLIS | Function: Probable adapter protein that bind to and organize the subcellular localization of a variety of membrane proteins containing some PDZ recognition sequence. Involved in the clustering of various receptors, possibly by acting at the receptor internalization level. Plays a role in synaptic plasticity by regulating the trafficking and internalization of AMPA receptors. May be regulated upon PRKCA activation. May regulate ASIC1/ASIC3 channel. Regulates actin polymerization by inhibiting the actin-nucleating activity of the Arp2/3 complex; the function is competitive with nucleation promoting factors and is linked to neuronal morphology regulation and AMPA receptor (AMPAR) endocytosis. Via interaction with the Arp2/3 complex involved in regulation of synaptic plasicity of excitatory synapses and required for spine shrinkage during long-term depression (LTD). Involved in regulation of astrocyte morphology, antagonistic to Arp2/3 complex activator WASL/N-WASP function.
Subcellular Location: Cytoplasm
Sequence Length: 236
Sequence Mass (Da): 25626
Location Topology: Lipid-anchor
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A0A183EL55 | MSIVFFLIFRGHQIVSLIYMEEFKRIAFTSPFRHDEASRFTGTLQGLALYVSAAYVILIFTIKLVMTRFKPFQLTTALNLWNTWLAVFSILGSFFTTVALFTEIKNHGLVGWCLLLHTPFCFCA | Pathway: Lipid metabolism; fatty acid biosynthesis.
Subcellular Location: Membrane
Sequence Length: 124
Sequence Mass (Da): 14269
Location Topology: Multi-pass membrane protein
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A0A183EG47 | MFVSAFIKGGQYSFGRWLPKAMAAPTPVSCLVHSRTLVTAEVIL | 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 to be ubiquinone.
EC: 7.1.1.2
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
Sequence Length: 44
Sequence Mass (Da): 4782
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A0A817EFB3 | MALSYRFLLCAHNLRSSSIETSLFKDSCTPSPFRDELFKDDHIHLDSSLAGRGCCCLQTTFQDQSFKETTHLYDQLLPLYPIMLCLSAACPILRDFLSDIDCRWNILSEAADDRTTEEKKTKKHSIPLRKYIDEQEDMDANTRHTIE | Pathway: Sulfur metabolism; glutathione biosynthesis; glutathione from L-cysteine and L-glutamate: step 1/2.
EC: 6.3.2.2
Catalytic Activity: ATP + L-cysteine + L-glutamate = ADP + gamma-L-glutamyl-L-cysteine + H(+) + phosphate
Sequence Length: 147
Sequence Mass (Da): 16996
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A0A815XNR0 | MHSSLSSMTSKKLCNCVAVPLIRRHVSATHQAATANATARSFLVRFIEERRKRSQQDDIRLEPYLSKGVYTESGAIRPMPKRYPLGIVKVLLIAIPFLYIGSLVSKYAALGLEKMDLFVYSDDDDDDDDDD | Function: Essential regulatory subunit of the mitochondrial calcium uniporter complex (uniplex), a complex that mediates calcium uptake into mitochondria.
Subcellular Location: Membrane
Sequence Length: 131
Sequence Mass (Da): 14739
Location Topology: Single-pass membrane protein
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A0A336LBU4 | MRNNFIYCLRRYEYLEASFTISDSVYGSTFFLATGFHGLHVLIGTSFLAVCLIRHLNNHFSNSHHFGFEAAA | Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Subcellular Location: Membrane
Sequence Length: 72
Sequence Mass (Da): 8234
Location Topology: Multi-pass membrane protein
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A0A336K917 | MTDVSEWFKTIPIFTRYWFAGTVGISLLSRFNILPAQYLILIPELITSKLQIWRIVTALFFYPLSPQTGFHFMFNCYFLYNYSRRLEEDHFKNTPGDYLFMLLLNWACCVILGIVANFYYLMDPMVLSVLYVW | Function: May be involved in the degradation of misfolded endoplasmic reticulum (ER) luminal proteins.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 133
Sequence Mass (Da): 15872
Location Topology: Multi-pass membrane protein
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A0A5A7TGZ4 | MRNKIGGWLWLWSWKVSEDSNMGASVLACQVDLKADNLIDKLPKIQFNEELKIRDSLCCVCLGEFEIKEELLQVPSCKHVFHIDCMNHWLISNSTCPLCRCSVIPTTQCSDPTVIAPPPPPPLPLPRAGSSELSLTSDHSAEMRSYSL | Pathway: Protein modification; protein ubiquitination.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
EC: 2.3.2.27
Subcellular Location: Membrane
Sequence Length: 148
Sequence Mass (Da): 16553
Location Topology: Single-pass membrane protein
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A0A5Q0U0T1 | SFWLLPPSLALLISSSIIGSGSGTGWTVYPPLSSQIAHSGPSVDFTIFSLHIAGVSSIMGAINFISTTLNMRPKGMTIEKMPLFCWSVLITAILLLVSLPVLAGAITMLLTDRNMNTSFFDPTGGGDPILYQHLF | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
EC: 7.1.1.9
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 135
Sequence Mass (Da): 14415
Location Topology: Multi-pass membrane protein
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A0A336MWM1 | MLKRIIPGFYTQIKSFRMNNKMWNILDFHHDGLLLFNHSYTNLSASVLNFNQNLNLPLCGFALILTVILWILFYYPLSITKDLCDVGFHHETEKTRSNTFKRTLINRARRLRCIGEKVPPPFPNGWFSIMESSDLKVGQAKNVNCLGKNYAVFRSEQGEVHVIDAYCPHMGANLGVGGIVRGNCIECPFHRWSIRGTDGECVNISYSNNSVPKLPKTQTYVSREVNGWIFVWNHAEKASPWEIPVIQEIETEEWTFQGRNEYYINCHIQEIPENGADVSHLNAVHGPSIVSGVDLRTTRSIWSSFIQHIWNASWQPSETKPHVADVALKHSIRLCNKIEVCELNISTKQVGPGYVQLLFSTNYGRLVCLQTVTPVEPFVQKVVHRFYSPRYLAPFAKFILLGECIQFERDIMVWNSKKFVDNPILIKEDRQIKSYRTWYSQFYSENSISFKAATSNNLEW | Pathway: Hormone biosynthesis.
EC: 1.14.19.21
Catalytic Activity: cholesterol + H(+) + NADH + O2 = 7-dehydrocholesterol + 2 H2O + NAD(+)
Sequence Length: 460
Sequence Mass (Da): 53066
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A0A959ZDA4 | MASSPEGLFRHDLDLGADQVAGADEAGRGCLAGPIVAAAVLLDRGCLESEGDGRLSGIRDSKKLTAKARERLYPEVLACAVRAVVVMRSARYIDENGLHVSNIECLGRAIEGLDPDPGAVILVDGFALKGCQVPHRRLVKGDSTSAAVAAASIIAKVTRDRCMARAGNAYAGYGFEGHKGYASAAHRDAIRLLGPSPIHRLSFDSEAYRS | Cofactor: Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
EC: 3.1.26.4
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Subcellular Location: Cytoplasm
Sequence Length: 210
Sequence Mass (Da): 22113
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A0A553RLG8 | MAIIVLGVGTGVFIIALTWIVTLALAIILCRATGPTKLGIIPIFLLAVIITLVLVFFPHSGSVLHRALCAPLSGEPGVLGSTVHVAALTLPGACICQAHENTLDHEASCANLQWIASQWDGKAFHHRALLENNRSFQSFGLSDAIRACSKFLPRSTGKLGRRDVFRRTFLKTYCFNSMWRCIFNHAYF | Function: May be involved in ciliary biogenesis or function.
Subcellular Location: Cell projection
Sequence Length: 188
Sequence Mass (Da): 20594
Location Topology: Multi-pass membrane protein
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A0A336KC81 | MYQKLAKIVAFLALIGCSCAAICTGPSVKSTSFTTTDGKIVSQVAFIGEFTLKCSNNAEKVALFAEVDGKVTPVVRVGDNQYQISWSEDLKKASSGDHNVNLYDEEGYAAYRKAQRSGESTSSVKPLTKLSVYHSGTYKGAWIKSELLATILITGAAYVAFSTRNKLIS | Function: TRAP proteins are part of a complex whose function is to bind calcium to the ER membrane and thereby regulate the retention of ER resident proteins.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 169
Sequence Mass (Da): 18208
Location Topology: Single-pass type I membrane protein
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A0A814VLI8 | MVEKFDEMNLHEPLLRGIYGYGFEQPSAIQQRAIKPCILGHDVIAQAQSGTGKTATFSISILQRIDINFKETQALILAPTRELAQQTQKVVLALGDYMGVTCYACVGGTKVQNDMKRLESGVQIVVGTPGRVHDMLSRSILRRKNIKMLVLDEADEMLKEGFKEQIYNIFVMMPEDIQTILISATMATEILNVTKRFMENPIKILVKKEELTLEGIRQFYINVGRENNKLDTLCDLYETMSITKAVIFCNTRRKVEFLTEKLSSRDFTVSAMCGNMDQKDRETIMKEFRSGSSRILIATDLLARGIDVQQVNIVINYDLPNNRENYIHRIGRGGRFGRRGVAINFVTDEDRSVLRDIEQFYNTRIQEMPMNVAEFL | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 376
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Sequence Mass (Da): 42915
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A0A8J7RWJ9 | MNLKFCIAALVCKVLAFGANLLGGGTDSPGRIALKLYPAVLRQLRYDGKIIAVTGSNGKTTTSNLIAHVLRQQGYSVINNEKGSNLTSGIATTLLCGATLGGRLRADYIVLEVDECYSRFIFADVPVDYYLVLNLLRDQVVRNGNPDLVLEKVAAAIAQRPDCTLILNANEPISQQLADCGNQCIYFAMDKTVRSTDTCVSGTHDCRICPRCFHRMSYSFYHYNHLGLFRCEHCGYRSHEPDFLGSGVDFAARRLLINGVPVEVTYNTTFNMFNTVAAAAVCCSASGMSLEQFARGAKSFHVAKERLDSFAFDGRKTVLMMTKQNAASLDQSISYVLEQEGEKTVVLYINNVLYLEYKDISWLYDVAFERLRGKVANILCTGNRALDAAVCVKAAGFTEPTLVYETDLDKTKEAFRKTKGDIYILAASAFGNEGKILEVLKREDR | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: The lipid II isoglutaminyl synthase complex catalyzes the formation of alpha-D-isoglutamine in the cell wall lipid II stem peptide. The MurT subunit catalyzes the ATP-dependent amidation of D-glutamate residue of lipid II, converting it to an isoglutamine residue.
EC: 6.3.5.13
Catalytic Activity: ATP + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate + H2O + L-glutamine = ADP + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-D-isoglutaminyl-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate + H(+) + L-glutamate + phosphate
Sequence Length: 445
Sequence Mass (Da): 49145
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A0A820AL20 | MINFAKNVPSSERQYKDVVDVYKKTLATEGIAGLYRGFVISCVHAVIYRGCYFGFYDTLKPILLGPDAGFMLSFLLGYGVTVTSGFISYSVDTIRRRMMMTSGHAVKYKGSMDCMFQIIRSEGMISLFKGAHTNILGSIAGAGCLSGFDKLVQLYTCIKFDTSDG | Function: Catalyzes the exchange of ADP and ATP across the membrane.
Subcellular Location: Membrane
Sequence Length: 165
Sequence Mass (Da): 18147
Location Topology: Multi-pass membrane protein
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A0A817DT64 | MVWFEILPSLFITAAPLLVVAAPTLYVCNWYFLNGKKHGPKNMTKDDRDYYMYLRDRRITGNEYYPRGVDAIDDRPTLVKLRNLWNM | Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 87
Sequence Mass (Da): 10346
Location Topology: Single-pass membrane protein
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A0A485LMQ6 | MVRFPGPNPYEPRIFPFFTPYEVMYRELKSENETLFRRNGVLAMLERDIITKKAPQKWQDNTIDDLAKLDVVLCFEDRIFDIVVEDLQLRKPKDLRPLHVICLDIKDTPKDAKIGGSLALDLCKLINELPDLEDGVPQAIDTFETQKQLKLIYALLYI | Function: Protein phosphatase that catalyzes the dephosphorylation of the C-terminal domain of RNA polymerase II. Plays a role in RNA processing and termination.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
EC: 3.1.3.16
Subcellular Location: Nucleus
Sequence Length: 158
Sequence Mass (Da): 18393
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A0A2D5EPE8 | MSRPPLSRLRSSLAELKAYRVPPEPPPIKLDANESPWPLPEDARRTLAEALAALPLHRYPDGLARGLRSALAAHLDAPEEGLLLGVGSDECITMLYGGLAKPGPSGEAVVLFPGPTFVMYAHTARAHGLVPVEVPLADDWTLDPEAMHAALERHRPNLVFYASPNNPTGNAFDPETIRALADAHPETLHVVDEAYGPFHRDRPEEPAKTLRPWVAERPQVAVMSTLSKCGLAGARLGWLYADPAFVAELEKVRQPFNLNALTQEAARLALTDLAPVIEEQLRAIVRERAVLRGALEAIEGLHVWPSDANFLLVRVPGDAVALRERLWAEGIAVRVFASHPRLAGHLRLTVGTPDENAALVDALRRAL | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
EC: 2.6.1.9
Catalytic Activity: 2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
Sequence Length: 367
Sequence Mass (Da): 39962
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A0A7Z9GC12 | MKLVVGLGNPGPEYSGNRHNVGFMVVDELLRRAHETTTTKFKGQIARASVGRENAILLKPMTYMNNSGISVGMCAGFYNIEVGDTLIVYDDLDLNFGNLRMKESGGHGGHNGLRSIFSHFSPGEFPRLRVGIGRPQHGTPAKHVLSNFTADERIVLSRVVSSAADAVEMWACDGATVTMNEFNRRQSLENTEH | Function: The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Catalytic Activity: an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-amino acid + H(+)
EC: 3.1.1.29
Subcellular Location: Cytoplasm
Sequence Length: 193
Sequence Mass (Da): 21163
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A0A3B8LW73 | MDARTSTRGEDDVSVKLLSTLLATSFGLPEQASTVAPSVDRVYLIILGLSTFFFVAIIATLIYFLIKYRRKDPNQRTSPIHENLVLEITWIIIPSVLLVWIFLEGFWAWVPMNYAPADAIEVRVTAQQWKWLFDYPKANVKNAPELVVPVGKPVKLIMSSVDVIHSFFVPAFRLKRDVLPNRYTTLWFQATKKGVYNMLCTEYCGKDHSTMVTRVRVVDQADFDKWVKKKQDEGANGKLLYANLGCNTCHSIDGSKKAGGGPSFKNLFGKMEKVKEGGVVKTIKVDENYIRTSIVNPNQHIVVGYPPLMPTFKGRITTSEINALTDYIKELSGAKKKKK | Cofactor: Binds a copper A center.
Function: Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).
EC: 7.1.1.9
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
Subcellular Location: Cell membrane
Sequence Length: 339
Sequence Mass (Da): 38243
Location Topology: Multi-pass membrane protein
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A0A9E4ML43 | MLWADLLSLVRIPLGVVFLFVADWPIGALGVIALAGLTDMLDGYVARRVMGPRAGGRHRGDWLDPLCDKIFVAFMLAGLVFVRGTPWLFVLVLLLRDLLQVVSLGVLALIPALHRRPYDYRANRLGKLTTVFQFLAALVILAGQPPPWPLAIVTASLGVTSLVTYIARVRAPAAAPLP | Pathway: Phospholipid metabolism.
Subcellular Location: Membrane
Sequence Length: 178
Sequence Mass (Da): 19328
Location Topology: Multi-pass membrane protein
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A0A956LJD1 | MPAAELSLRAAERADLDAIAALERRCFHRPWTRSMLAEELTRGFARVDIAARGGGVLGYTCVWEQPPEAHLLKIAVAPEARGGGVGGALLRRALHQARVSGCEQVQLEVARANASALRLYQRAGFTVVGTRPGYYRDPVDDAVLMTRLVDH | Function: Acetylates the N-terminal alanine of ribosomal protein bS18.
Catalytic Activity: acetyl-CoA + N-terminal L-alanyl-[ribosomal protein bS18] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-alanyl-[ribosomal protein bS18]
EC: 2.3.1.266
Subcellular Location: Cytoplasm
Sequence Length: 151
Sequence Mass (Da): 16446
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A0A935P0Q3 | MDSSHRSSSHSSHSSHSGHSSHSGHLGAPARQARAAHGDAAEELIGFDFTRYFRSLRKYAWAILALMALAITGAVFYTDRQPKIYEATASIQIEPRMVDLLGTGQEVGGGAGADYYKQQQEKLGSYMMARMTVEAHGLHQKLLTEPESARGKLEDHYDLATRRLRETLAVRYPQQNRTMYVTVRSEDPQLAADIANAHCKQFEDYSRGTLAGDTKKQSEALAGEFANVETRLRDAEAALFQFQKDNDLLAVSLEDRQNTVSSNISAYSQKVNEARAKRIELSAKLDRMKKAAQIDVLESPLLTISDVSSFDSLRAQYYTERSKLLEMEQDFGPKNAEYQKQKAKVDSLLSALRAESRRQLAGVEEQFLAALTTERALLAEIDRYRKEAFELGPKIVSFNELARKKKGFEDKYNILVARLSTTEMTGRMNDRIDNANIRRLDPALVPTKPVSPNLQINLMVAGTLALMAGVGLVMLVTFLDRSVKSAEDAQQAAGVPVLGVIPMLAESELSSNDDRARDLYVHQHPTSRTAECCRSLRTNIMFSAADRQLKTLVVSSANPREGKTTSVFYLGTTMAQSGQRVLLIDTDMRRPRLHASMGVSRQKGLSNLILGEDAYDDVIKTTEIPNLFVLPCGPLPPNPAELLMTKRFEVVLAELAKRFDRVILDSPPLQAVTDAVVLSKLADGVIIVVRASKTLREEVKRSARQIRDVDGAIYGVILNEFDITHRGAYYYSYYGYGDKQEPSSTAA | Catalytic Activity: ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]
Subcellular Location: Cell inner membrane
Sequence Length: 747
Sequence Mass (Da): 82970
Location Topology: Multi-pass membrane protein
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A0A3A4JXD0 | MNRRVLLKLSGEALQPKQGQKIIDTEFVRFMGTQILEAVEEAKIEVAIVIGGGNIFRGEMAQALGMDRVKGDFMGMMATVINAMALESVFSMIGLDTLAQSALAVGSAVPGFNQAKALAALEKKKVVIFAGGTGNPYFTTDTAAALRAVELHCNALLKATKVDGIYDDDPKKNHSAKLFPELTFHQVIERELRVMDQTAFSLCRENKMPINVFNVNTPGNIKRALLGEKIGSIVR | Pathway: Pyrimidine metabolism; CTP biosynthesis via de novo pathway; UDP from UMP (UMPK route): step 1/1.
Function: Catalyzes the reversible phosphorylation of UMP to UDP.
Catalytic Activity: ATP + UMP = ADP + UDP
EC: 2.7.4.22
Subcellular Location: Cytoplasm
Sequence Length: 235
Sequence Mass (Da): 25512
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A0A3M1IDJ7 | MPAKRIIPCLDVKDGRVVKGIQFVSLRDAGDPVENALKYDRQGADELVFLDITASSDRRAIILDLVKHVSEVLFIPYCVGGGIRTLEDIRLILSEGADKVALNTAAVQNPDVLTEGARHFGAQCIVCAIDAKFNGEFYEVYLHGGRTPTGIDAVKWAYEAQERGAGE | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 5/9.
Function: IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisF subunit catalyzes the cyclization activity that produces IGP and AICAR from PRFAR using the ammonia provided by the HisH subunit.
EC: 4.3.2.10
Catalytic Activity: 5-[(5-phospho-1-deoxy-D-ribulos-1-ylimino)methylamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + H(+) + L-glutamate
Sequence Length: 167
Sequence Mass (Da): 18189
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A0A7Z9GBV7 | MAVSLVVVKIGGDVVADSLGLDELIAEFEALHAQGSRLIVIHGGGPQATHLTRRLGLQPTVVGGRRITSPQVLEVMKMTLAGSVSVDLMAACRAHKLPALGLSGVSAGLIQATKRPPRIVSGCGDEAVDFGEVGDVTGVNIQAIQALLDAGFIPMISSLSADKNGRVLNINADIVACQMAIALQADALVLVTGADGVMADLEIADTRYPELTVSEAKALISDGTVYGGMIPKLEESFRVVEAGVGRVIILRMGTAGCISTAIAGSTEHGTTLHADV | Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4.
Function: Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate.
Catalytic Activity: ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate
EC: 2.7.2.8
Subcellular Location: Cytoplasm
Sequence Length: 276
Sequence Mass (Da): 28352
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A6W953 | MRGGIALGRPFGVPLLLAPSWFLFAALIVWIFAPVVQRQVPGPASYLVAFGYAVLLLVSVLLHEVAHALAAKWSGMRVTGIVLNVWGGFTSHEGRTGPGRSLVIAVVGPVVNAVIALVAWRVGAVVREQPDGGGVLALLLGALTLSNALLAVFNLLPGLPLDGGHALEAIVWKLRGDRLTGTVVAAWVGRVLAVVVFVAALFGPRLLGWETSLTDVVWAGLVGALLWQGASTALTYAGQQRRVPALSARVLQRPAIAVNARATVEEVVRSARAAIDAGAAAGSTRDLEVVLVTDDGVPVAVVDTAALRRVPAERRTSLGAGATARALPPRSWLPEDLAGEDLLEAVQARPGEHVVLDGTGRVRGLLHTGDVVAAVTR | Cofactor: Binds 1 zinc ion per subunit.
Subcellular Location: Cell membrane
Sequence Length: 377
Sequence Mass (Da): 39229
Location Topology: Multi-pass membrane protein
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A6WC16 | MIGGVTGPDRDDEPPGPPRRGPAGRAGARGLVATARETALVVAVALVVSMVVKTFLLQAFFIPSESMEPTLAVGDRVVVSKLTPGPFPLQRGDVVVFADPGGWLPPAAPTRRGPVGTAVTGALTFVGLLPDDADEHLVKRVVGLPGDHVACCDGQGRLTVDGAPLDESAHLAAGAAPSEQPFDVTVPPGELWVMGDNRPRSCDSRCHADEPRGGFVPLDLVTGRAVAVVWPPGHLDRLSTPDDDGGAPGAP | Catalytic Activity: Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins.
EC: 3.4.21.89
Subcellular Location: Membrane
Sequence Length: 251
Sequence Mass (Da): 25807
Location Topology: Single-pass type II membrane protein
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A0A7K5Z438 | ARVSPQSEAKKTQFGSLKDEDRIFTNLYGRHDWRLQGALRRGDWYKTKEMLLKGADWILGEIKASGLRGRGGAGFPTGLKWSFMNKPPDGRPKYLVVNADEGEPGTCKDREILRHDPHKLLEGCLLAGRAMAARAAYVYVRGEFYNEASNLQVAAREAYEAGLLGPDACGSGYAFDVFVVRGAGAYICGEETALIESIEGKQGKPRLKPPFPADVGVFGCPTTVANVETVAVAPTICRRGGTWFAGFGRERNSGTKLFNISGHVNNPCTVEEEMSVPLKELIEKHAGGVRGGWDNLLAVIPGGSSTPLLPKSVCETVLMDFDALIQAQSGLGTAAVIVMDKSTDVVKAIARLIEFYKHESCGQCTPCREGERGAGAGCGVMARFVQGNAQAAEIDALWEISKQIEGHTICALGDGAAWPVQGLIRHFRPELEERMRRYEEGKARAVSA | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity and assembly of complex I.
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
EC: 7.1.1.2
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 448
Sequence Mass (Da): 48491
Location Topology: Peripheral membrane protein
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A0A0L0VNB3 | MRSFGFLATLFALASSIHADAGLNPNDAPDDVIELTSENFDTVVTPAPLILVEFMAPWCGHCKALMPEYKRAATLLKKGGIPVAKADCTEQSELCAKYEIQGYPTLKIFTNGVSSEYKGPRKADGIVSYMEKRAHPVVTIVTSDNHTDFTKSGNVVVIAYLDHSDKDGLDAFTSFAEAKRDDYVFGVCYDHSSIKEVSSLSQGSIVLWKKFDEGRNDFHGEKLTQESIAKFVNTNSVPLFDELTPANFALYSEIGLPLAYTFIEANNPKREELIKSLEPVAKDHKGHVNFVWIDATKFGDYAKSLNLPGSDWPEFVIQDLSNQDKFPLEPKKEVNKHNIAEFIKLFRAGKVTKSVKSQPIPTKQDDGSYVLVANAFEDVVYANNNHQDVFLEFYAPWCGHCKLLKPIWDNLARSFKDSKDKVLIAKFDATENDIPSTAGIQVQGYPTLKFKPAGSREFIDYDDERELDAMIAFVEKNSVNKVKAVKVELPEPVEGGEGGDQVVFDSEESEPVPEDEDKDAEHDEL | Function: Participates in the folding of proteins containing disulfide bonds, may be involved in glycosylation, prolyl hydroxylation and triglyceride transfer.
Catalytic Activity: Catalyzes the rearrangement of -S-S- bonds in proteins.
EC: 5.3.4.1
Subcellular Location: Endoplasmic reticulum lumen
Sequence Length: 525
Sequence Mass (Da): 58477
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A0A955Z7W1 | MGNPSVEFKTSLGSFTIELDPAIAPKTVENFLAYVDAGHYEGTLFHRVIPGFMVQGGGYGADQKKKPTKPAVENEASKEGKNVRGSVAMARTGDPHSATAQFFVNVADNGFLDHTEKEGKGWGYCVFGKVTSGMDVIDAIVKVKTGPKGPFEKDAPEEDVTIEKAIRVDADAKKDDEKKDDADKGDDKKDEAKAESKDDEKKDD | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
EC: 5.2.1.8
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Length: 204
Sequence Mass (Da): 22060
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A0A956EP14 | MHVYGLTGGIGSGKSTVAAILEEYGIPVVSADELSRMVVTPGSPGLAAVVALFGDEILDAQGHLDRSKLGAIVFADPEQRVALERLLHPRIRERFEEVLDALEKAGHTKVVYEVPLLFENKLEEMMDGVIVVTTRDDLRIARVGARDGLDAAAIRARMAAQLDDKTRQKLADYVITNNGDAMDLRREVEIMLSDYLKVPIPGRSGPHRRAGPPPPPRQSS | Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
EC: 2.7.1.24
Subcellular Location: Cytoplasm
Sequence Length: 220
Sequence Mass (Da): 23982
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A0A955XC53 | MSNEETTTPASPEGEDFKVRSLERKTDTSERKEYTGASIEVLEGLEAVRLRPGMYIGETDVTGLHHLVYEVVDNSVDEALAGHATHVAITIHVDGSLTVSDDGRGIPVEWKPDQNKSAAEVVMTVLHAGGKFSSDSYKVSAGLHGVGVSCVNALSEWLQLEIHRKGRIHTMRFERGKPVTASGTPDAPLTVAGATDKTGTVVTFKPDKEIFSTVTFNYDRLATRMSQLAFLNKGLRVDMVDERDERKDTFIYEGGIVSYVEHLNRHREPLHRDIMYFSSLMEVSGSDNEPVEVDVEVALQWTSAYNELIYCFANNVYNDEGGTHAIGLRSALTRSINSYAQKENLLKGMKEPPTGDDVREGLTAVVSVKMSDPKFDSQPKHKLLNTEAKSAVESLLNQKLTAYLLENPGISKTVVGKCCDAARARIAARKAREMVQRKNALESSSLPGKLADCQEKDPTKCEIYIVEGESAGGSAKQGRDRKFQAILPLKGKILNVEKARVDKMLSSQEIVALVTALGTGIGTENFDINRLRYGRVIIMTDADVDGSHIRTLLLTFFYRQMPQLVEQGHLFIAQPPLYRATRNKKETYLKDDDAKADYVLSLGVQGVLLTPTAGGVVEGEHLKNVAKNVLRYRETLRVVDRRRDLRLVDALVRSTSLSLEMLRPKSSVGTQVSGGVDVEALERDVIAPLKAYLASHYPEVIAKLGAEIVTKEHGAELVFESRRQGARRKTVVDPVFLASRDFLRLQQLARSFRELEGPFELTVEGGSALTLARIEDVVTELEARGSKGISVQRYKGLGEMNAEQLWETTMDPSIRVLLEVQVNKSDAENDIFETLMGDQVEPRREFIELNALEVANLDI | Cofactor: Binds two Mg(2+) per subunit. The magnesium ions form salt bridges with both the protein and the DNA. Can also accept other divalent metal cations, such as Mn(2+) or Ca(2+).
Function: A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner.
EC: 5.6.2.2
Catalytic Activity: ATP-dependent breakage, passage and rejoining of double-stranded DNA.
Subcellular Location: Cytoplasm
Sequence Length: 859
Sequence Mass (Da): 95089
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A0A2K3DZY2 | MDRSMLGTTMPQGMPGAAQRRLRGTSAGVRGRGASLVRRTIAGDRPQVATPPAPAVPTLCVPEDFVLAPGELSPVDRNGKNLPEDVFRCFGCTLPACKGAGGCASNLWRNQQDGYLRAILTARVYDVAIQSPLEEARKLSEAVGNTILLKREDLQPVFSFKLRGAYNKMAKLPAEARARGVITSSAGNHAQGVALAASRMGCTAIICMPVNTPEIKVANVRKLGGQVVLVGESYQEAQAAAVARAVKEGLTFIPPYDDPYTIAGQGTIGDEIMRQISDPEKLDAIFVPVGGGGLIAGIAAYTKALKPDIKIFGVEPTGANAMAISLARGERVALSRVDAFADGVAVKQVGQETFRLCRELVDGIVLVDNSAVSAAIKDVFNETRSILEPAGALAVAGAKAWLKRNSMKGATVVAVTSGANMNFERLRLVAELANVGGRTEAMLTTTIPERPGAFKEFISIALSSDADLSVTEFKYRYSAGSTAQVLWGVGIRNPEQLTALTDRLNAAGMVSHDISGLEVAQVHLRHLAGGRARSYTGRIEDEKIYQVTFPERSGALRRFLDIISPAWNVTLFHYRNSGNRESSVLLGVQVPKFDEARFATAVASLRGDGEGFAFNELQGAVREVFDQFIQ | Pathway: Amino-acid biosynthesis; L-isoleucine biosynthesis; 2-oxobutanoate from L-threonine: step 1/1.
EC: 4.3.1.19
Catalytic Activity: L-threonine = 2-oxobutanoate + NH4(+)
Sequence Length: 630
Sequence Mass (Da): 67244
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A0A2D8JF56 | MTPRERLIVAIDEPDVAAARALIARLEGAVDRVKVGMTLYYRAGPAFVRELVSEGWNVFVDLKCHDIPHQVAGAVGGLAELGAELITVHVAGGRQMLEASVRAAEGSGTKILGITALTSLDAQSLSEIGPSTTPEALVATRASLAYDAGLDGVVSSPLEAASVRARVGSSFEIVTPGVRPHGSSTDDQRRIATPGDAISWGASRLVVGRPITRAEDPATVAAQILGEIEAAL | Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2.
Function: Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP).
EC: 4.1.1.23
Catalytic Activity: H(+) + orotidine 5'-phosphate = CO2 + UMP
Sequence Length: 232
Sequence Mass (Da): 24036
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A0A0T6B2W6 | MGITGLLPFLEKASKRCHVAEFRGCTVAIDTYCWLHKGAFGCAEKLIRGEDTNGYVHYCLKYIKMLKSYDIHPILVFDGQHLPAKKHTEEKRREQRKLSRKKAAELLRLGRVDEARVQMKCAIDITHKMALALIKECRENGVDCIVAPYEADAQLAYLNIKKFVHFIITEDSDLLLFGCNKIFYKMDIQGFGMLVEAEKINNCMKLRPDNYNFDKFRYMCILSGCDYLQNLPGVGIKKALKFISLTADPSIYNVLLKLPSYLKLPNVVVTDDYREGFMIADATFKHQLVFDPVKRKLLPLHDPQISGTREEYCRNAGHLIDETLAFEMALGNVDPFTHEPYDDWSPDLVPLPTTSIWSKQYNKPTLPVKKTPKLNAPSTKNMQVDIKVIEEEKFVYDLKLEKELEMYKVIEQAPKKQKTEEDSEALSEVVSQEINVPFRRLKKFSKFERTVVNYEDVLTSRFFTPKKPASIEEPSISNYDTLLSGINSYSNKTVCSESLKDENYGKDEESHYKLEVYARKPI | Cofactor: Binds 2 magnesium ions per subunit. They probably participate in the reaction catalyzed by the enzyme. May bind an additional third magnesium ion after substrate binding.
Function: 5'->3' double-stranded DNA exonuclease which may also possess a cryptic 3'->5' double-stranded DNA exonuclease activity. Functions in DNA mismatch repair.
EC: 3.1.-.-
Subcellular Location: Nucleus
Sequence Length: 522
Sequence Mass (Da): 60117
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A0A971FJQ0 | MREIKRVAVLGSGVMGAAIAAHLANCGIPSVMLDIVPPNLSDEDKKNKAKRDAIAAGAKAALLKAKPAPLYVKSYIDMIEIGNFEDDMEKISDCDMIIEVVIEKLDIKKKIFAQVAKYRKPGSIVSSNTSGILISAMAEDMPDEMAQHFLGTHFFNPPRYLKLLEVIPTAKTKPEVVKEVGAFGENVLGKGIVYAKDTPNFVANRIITFAMQYLMHEMTKAGLGVEEIDALTGPAIGHASSATFRTADLVGLDTLQKVVGNVYNGCPDDERRDMMKGPDWFDKMIEKGYFGNKSGSGFYKATKERDEKGKKVILGFDPATVDYRAPVKPRFACTGAARSAGSLAEKLKVMHFGDDEGSKFLFKFFANMAQYAGNRIPEITDDIVNLDNACKWGFAWEVGIFETWDILGFDEVCERMAAEGIALPPIAQAVKEAGGKSFYKSEKGVDLFFDLATKTYKPVPTNPNELKLINVKANPTNIVEKMDEASLVDLGDGIICAEFHCKMNAIGPDIVAVLNKGVDLLEEGKFEGMVIGNQGPHFCAGANLMLVLGDAMQENWKGLEDMVRGLQGIGMRMKYCSAPVVAAPHHYTFGGGVEICQHADKVVLAGETYAGLVEVGVGVIPAGGGTTELLVRALEYMPENIQPNDAFPFVRRAFENIATAKVGTSGAEVIELGYFRASDIVLPNYDHQIQKAKAVCRGMVVAGYAPPRKPRLYALGESAKAVFAAGVWGMKEAGWASEHDMLISSHIANILCGGDRAAGTPMTEQDFLDLECEAFVSLCGTEKTQARIQNMLASGKPLRN | Pathway: Lipid metabolism; fatty acid beta-oxidation.
EC: 1.1.1.35
Catalytic Activity: a (3S)-3-hydroxyacyl-CoA + NAD(+) = a 3-oxoacyl-CoA + H(+) + NADH
Sequence Length: 800
Sequence Mass (Da): 86721
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A0A2E6VMW6 | MNFLSALNRALALPFLGLVWLYTTCCRPLMQGRCRFHPSCGDFCQHAFQQHGFGGGLLLAMHRLLRCHPFHPGGVDQVPQSFSWRRFLPRTKAKTCDS | Function: Could be involved in insertion of integral membrane proteins into the membrane.
Subcellular Location: Cell membrane
Sequence Length: 98
Sequence Mass (Da): 11162
Location Topology: Peripheral membrane protein
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A0A2S7UYN4 | MADYFVGDLQGCFDGLQQALAEVEFNSSKDTLWLTGDLIARGEQSLQTLEFLYKNQDSVKTVLGNHDLHFLSVANKIKKENPKDLLTPLLQSPKLTRYIDWLRLQPLVLALPDNSGFMSHAGLAPHWQAEDAVYWSEQVQSILMAKDYTDFLPSMYGKKPTKWHQDLSELDKIKYAINALTRMRYCSLDGELEFDSKCAPQDLADKNLQPWFEYDKQRFIQNKWIFGHWASLMGETKNKNILALDTGYVWGQYLTIYELKKDSYIKIRAIDK | Function: Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate to yield ADP.
EC: 3.6.1.41
Catalytic Activity: H2O + P(1),P(4)-bis(5'-adenosyl) tetraphosphate = 2 ADP + 2 H(+)
Sequence Length: 272
Sequence Mass (Da): 31488
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A0A2E7BRU6 | MPELPEVETCRAALAPLLSQARVGVFQRSDKDLRFPWPAPEDLKRLEGRRIEGVRRRGKYLIISMGDHHLLVHLGMSGQVFFGASSEPWLPHEHWRLRVDDQLLRYRDPRRFGFLQLYIGPRPEAHERLVHLGPEPLCQDSFNTSYLHSVCRGSKRPIKSLIMDGTVVVGVGNIYASEALYRAGIQPFRRAGAIATHRLDGLVVGIRAVLEAAIAAGGTTLKDFQSVEGNPGYFRRELAVYGRAGAPCRRCPGTIRQRTLSSRATYWCPNCQR | Cofactor: Binds 1 zinc ion per subunit.
Function: Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates.
EC: 3.2.2.23
Catalytic Activity: 2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-monophospho-2'-deoxyribonucleoside-DNA + H(+)
Sequence Length: 273
Sequence Mass (Da): 30736
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A0A955RBK1 | MRQKLDNLVAWHGELESRKRVQLYAAGAITLIAVALTGSWLSFTPYRPLISGRAYDEVLDAAAALQPAEIPYRIEDNGTLSVPATRLGEARAALGSRQGLPALGDVADLRLGLTPKAQDWAFLRAREGDIARMINGIDGVSASRVNITPRVEALFADEEEPARASVFLKQRPGRKVGTAQVEAVVNLVASAVEGLEPQHVSVVNERGQLLSAGSFGTAGSANTPEKLLEYQQAQERRYEGAVANALNPLLGYNGGFSVTATVDLEMTEEERLEKAVDTEKQALLSEQLHDSKSEKGEVGGIPGVDANLPERPAPAAGNSGRTETSAVTSNYVYPTVDTKTVRPSGEVRRVSVAVQVDDKIVAGLAEAGGVAVEDVKSRIEQAVKASVGFDEKRLDTVSVTFLPFAEPQWVEGGGAVLPWTEVASDVAPWGVAALALILGFLFVVRPLMAAVTRQEQHDIDEAAWLAEHGGPSSAVDPNAGLVDRLRQAASSFEAVDPGDLNKLAKQQSAAAAHVLRQWHRNAGE | Function: The M ring may be actively involved in energy transduction.
Subcellular Location: Bacterial flagellum basal body
Sequence Length: 524
Sequence Mass (Da): 55818
Location Topology: Multi-pass membrane protein
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A0A5E4PHU1 | MRPLQFQKTILNWFDQHGRKHLPWQQDKTPYRVWISEIMLQQTQVNTVIPYYEQFMQRFPSLKALAQASVDDVLHSWAGLGYYSRARNLHRAAKWILEEVNGIFPDNIADLMQLPGIGRSTAGAILSIAFGKKAPILDGNVKRVLSRFAGIDEPVNDKTTENKLWALAERYTPEKRVDHYTQAIMDLGATLCTRSKPQCGTCPLGKNCYAYRMGMADLLPKKKSARTLPVRAAAFLILRNKGRILLHKRPETGIWGGLWSLPEIPGKPDEGKIREYCRRQLRHPIACYQPLEPFRHTFSHYHLDIHPVIVTIRPSHRPALDTEMEAGMQIWYNPREAKAVGLPKPIQLLLRGLDDQNHTMRKTAQRSGRTRPASASRRAG | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: Adenine glycosylase active on G-A mispairs. MutY also corrects error-prone DNA synthesis past GO lesions which are due to the oxidatively damaged form of guanine: 7,8-dihydro-8-oxoguanine (8-oxo-dGTP).
EC: 3.2.2.31
Catalytic Activity: Hydrolyzes free adenine bases from 7,8-dihydro-8-oxoguanine:adenine mismatched double-stranded DNA, leaving an apurinic site.
Sequence Length: 380
Sequence Mass (Da): 43452
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A0A1Z8KTZ2 | MTLSTLLIILISYLVGSISGGVIIGKIRNVDIRQKGSKAAGATNAFRTMGALFAISVLVIDVYKGYFSVYYIPLLFLDESTNIVKALAGFSAILGHVFPLFFKFKGGKGVGTALGTLLAFPQFYFTAGIGFLTWLINLFITGFVSLGSILAGIMVSVVFIFENDFILNELSIYIIFISIFFILTHRENIKRLFNGSENQFKKIMLINLFKKND | Pathway: Lipid metabolism; phospholipid metabolism.
Function: Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP.
Catalytic Activity: an acyl phosphate + sn-glycerol 3-phosphate = a 1-acyl-sn-glycero-3-phosphate + phosphate
Subcellular Location: Cell membrane
Sequence Length: 213
Sequence Mass (Da): 23542
Location Topology: Multi-pass membrane protein
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A0A2R6C7D7 | MLKQFRGYNMVLEGPTVSVGYIVECAARTLGFTSEDPVKRAIGRIIHERVERELKSSSRVFGKIASIEMLYESENLGLRGVPDIVLSDGTPVEIKSGEVPKQGVYFLHQLQVCLYALLLEDVLEWDIDRGYVYYTRTREKKDVKLGEELRIKSLKTLRTAKKLKTQEEVYQV | Cofactor: Mg(2+) or Mn(2+) required for ssDNA cleavage activity.
Function: CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA).
EC: 3.1.12.1
Sequence Length: 172
Sequence Mass (Da): 19701
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A0A7C3SVN7 | MPWKYCLRDLAKVVAGKLQGDEHIEFTGVSIDTRTIQPGDVFFALPGNRVDGHQFVPEAFKKGAVAVVVSKDNGFPSICVRDTLQAIQKLARWHRTNIKSQVFAITGSCGKTTTKELISAVLAKKYKVVASRGNYNNELGCPLSLLQMDEDTDWGVIEMGAGKAGDIAELSAIAYPDESVITTIAPAHIERLGSLEGIAREKSNIAKCLPPWGYFYVNMDNPYCVSIGNRIIANRIYYGKKGDVRLKSVRKISLEEMEVEIEPVGKLRLPLCSSSLLSNFLLAVAVSLKHKIPIDEQTLAEAYYKAGRIKTYQVGHFTIIDDSYNANPASMKSALEYLQLTGVEGYRCAVLGDMLELGEESEKYHYLLGKQVGECGVDVLFLYGNYAQEVQRGALEAGVKSVTVCSNHDEIVNKIIEMLPPLSRILVKGSRGMTMEKVIQGLKEKIMNE | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Involved in cell wall formation. Catalyzes the final step in the synthesis of UDP-N-acetylmuramoyl-pentapeptide, the precursor of murein.
Catalytic Activity: ATP + D-alanyl-D-alanine + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptanedioate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine
EC: 6.3.2.10
Subcellular Location: Cytoplasm
Sequence Length: 449
Sequence Mass (Da): 49537
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A0A7C3A138 | MSDGKETNRRVSRFAAVFAGGTMLSRALGLVRDMVIGGLVPDASRDAFLFAFRFPNMLRDMLGEGAANAAFVPVFAEAREKDSEAKYRELVSACLSAMILLFGALTVIGLLLIPWVPAIIEALRPLTRAEPKDAEQLRLTVRLIYWTFPYLFFIGLAVFAMGPLFVARHYGTPSWSPVLLNLALIATCLGLRDWFPDPAWALVTGVWLGGVAQWAAMWLAMKRHTGVLLPNFQLGHPGIRRAAWLLGPVILGQAAGEVNKLVDGFFAYSLSDGVVSALFYANRLVQLPLSVFGVAVAVAILPDISRAAARRDDLAIRETLLHGYRQSFFLAAPAMLGLLALGRPIVRLLFERGHFGEEMTNMTSISLFYYGLGILSFVWVKISVQGFYAEQNTRTPVIIASASMVLNILLNCALVGLLGYRGLAIATTLSFTVNFLLLYVFLCNRHGLLWDAATASALGRTTLAALIATAAAYGLWTRIALLTTGASLWAQCLAVGTAIMGACLVYLGLCKSLKIKELNYFMEMFDRRHASR | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Involved in peptidoglycan biosynthesis. Transports lipid-linked peptidoglycan precursors from the inner to the outer leaflet of the cytoplasmic membrane.
Subcellular Location: Cell membrane
Sequence Length: 532
Sequence Mass (Da): 58127
Location Topology: Multi-pass membrane protein
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A0A3B1KJK7 | MGRQLLAVFLAVIGFLGTILICALPMWKVSAFVGANIVTAQVFWEGLWMNCVMQSTGQMQCKVYDSILYAFFFLFFLNLFGISGEPFFFLVTTGLLVSCYKNQVGLEKRKTGFSVSDKDEDTDSSLLFFDLENIKWGQ | Function: Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity.
Subcellular Location: Cell junction
Sequence Length: 138
Sequence Mass (Da): 15575
Location Topology: Multi-pass membrane protein
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A0A524NK35 | MRSCGRTFAGGRRAVMDRDSPVKTVALALSVCLVCSLVVSVTAVALRPLHVANRERERRQHVAAILAAVPGIEAVIGAVDVDELEIRLVDLESGAYVDGVDPAGYDARQAATDPAHSIELAPERDAAGVGRREKLAPVYVVGDDDEIALVILPVYGSGYLSTLRGYVALGADTNTILGLTFYEHDETPGLGAEIQEAGWLAQWKGKRVRDDSGRIRVRVAAGTVDANDPGRPYEVDGISGATMTGDGVTALLRFWLGDDGFGPYLDRLRAARKQ | 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(+) + n Na(+)(in) + NADH = a ubiquinol + n Na(+)(out) + NAD(+)
EC: 7.2.1.1
Subcellular Location: Cell membrane
Sequence Length: 274
Sequence Mass (Da): 29237
Location Topology: Single-pass membrane protein
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A0A518BZJ6 | MDLARCIDHTNLNPEAEPAAIDRLVNETIEHDFASACVSGRYVARVAERLDGRTPLTCAVVNFPSGLCKVDVASIEATIACKDGADEIDIVAYIPHLMNADAESARAELSEVIAGARAVRSSVVVKVIVESAYLMKEADAATAEKRIEAACVACRESGADFIKTSTGKHPAGGATMEAIALMKKYGETLKIKAAGGIRTYDDAKRMLDAGADRLGCSSSIAILGQADSAEQA | Pathway: Carbohydrate degradation; 2-deoxy-D-ribose 1-phosphate degradation; D-glyceraldehyde 3-phosphate and acetaldehyde from 2-deoxy-alpha-D-ribose 1-phosphate: step 2/2.
Function: Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate.
Catalytic Activity: 2-deoxy-D-ribose 5-phosphate = acetaldehyde + D-glyceraldehyde 3-phosphate
EC: 4.1.2.4
Subcellular Location: Cytoplasm
Sequence Length: 232
Sequence Mass (Da): 24375
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A0A7X7JJZ2 | MGNITRRLAILIPLLFLVGCDHATKGVAKAGLDGGAVRELIRGVVDFRYVENTDIAFNLLRWIPEHIRFPALLVSGAIAVVVMLALLFQGYGEGRLPRIALVLVTAGAIGNYLDRVVRGYVVDFVHVHHWPVFNVADVYITVGYALFACAFFLHRRAQALAHRTAS | Pathway: Protein modification; lipoprotein biosynthesis (signal peptide cleavage).
Function: This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Catalytic Activity: Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, in which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) and Zaa (Gly or Ala) have small, neutral side chains.
EC: 3.4.23.36
Subcellular Location: Cell membrane
Sequence Length: 166
Sequence Mass (Da): 18279
Location Topology: Multi-pass membrane protein
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A0A6A6VYX8 | MDKNFEITDSTDWLDTPLSSFSVLETALRCQVCKDFFDTPMITSCSHTFCSLCIRRCLASDGKCPACRASDDASKLRRNWTVQEVVDGFSGARPQALELARKESEEKEDQGKGRRKLKRKIVDTDLEEHTSPRRSQRTTRSQASRTEVTPAHAEAISIEDSDATAEESEDEQPEPDDGLVPCPMCSKRMKEESVFVHLDRCEEEQKQDKKRAAQVRLSETRSAHTLPQHNSTAPQRLPQLNYSILKDIALRKKLQELGIPAWGPKQLLARRHTEWINLWNSNCDSSRPRKKSELLRELDQWERSQGGHTRDSAIPSVMRKDFDGKSWAQDNSDQFQSLIAAARAKRNQKKEGQESKDTNGDTEMLETRTGPPNAANTETATNSDDSKIAHDADEAAVVSRVIPDVQALSSIRNKVQAANDGVLVQETPEDASTRILSLNGNSDQSQQMTSVPSLHPGSSESLGMSPVKKIPMFAIPEEPVKDIETEQAAQ | Pathway: Protein modification; protein ubiquitination.
Function: E3 RING-finger protein, member of the UBC2/RAD6 epistasis group. Associates to the E2 ubiquitin conjugating enzyme UBC2/RAD6 to form the UBC2-RAD18 ubiquitin ligase complex involved in postreplicative repair (PRR) of damaged DNA.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
EC: 2.3.2.27
Subcellular Location: Nucleus
Sequence Length: 490
Sequence Mass (Da): 54752
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A0A7Y3BV04 | MRRTKIVCTLGPASDTKAKLDELVRAGMNCARLNFSHGDHTSHAEMAKLVRRAAADARRPMAILADMQGPKMRVGKFAQGPIDLKQGDHFALTTNEVEGNQDIVSVTHESLGADLKPGDAIALDDGFIRLRVDRVAGNTVHTIVEDGGNLSDHKGLNLPGVSITGPALTEKDREDLAFAVSTLEADYVALSFVRAADDVREAKALAGDVPVIAKIERPEAIEVLSEIVDAADGIMIARGDLGVELGAEKVPMIQKRIIRETNAHGKIVITATQMLDSMIRNPRPTRAEAADVANAVMDGTDAVMLSGETAAGRYPLQALQMMDAIVREVESDYVEDLSREFRELKSVVEEDWSFANAAARAAAELTTHLPLKAVVVFTQDGRSAGLLAEHRPRAPILAITSDTRVARRLALEWGVIPRIEVPPESLDETLRIASSLLVREQLCQRGEAFAMVLGWPPSGRTNTLKLHRL | Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 5/5.
EC: 2.7.1.40
Catalytic Activity: ATP + pyruvate = ADP + H(+) + phosphoenolpyruvate
Sequence Length: 469
Sequence Mass (Da): 50820
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A0A7Y3M6A7 | KDLPTAIRFHEKLQAKRSELDFEIDGSVLKVNSIALQRDLGELSSRPRWAIAIKFPPQQETTVVKKIFASVGRTGALTPVAQLEPVFVGGVTVSNASLHNQDEVDRKDVRVGDTVVVQRAGDVIPQVVSVVRSKRPKKTRRYRLPKKCPVCRAETVRPEGEVVTRCPNLDCPAQLKNNIFHMASRGALDIDGLGEKLIDQLVEAGLVTRLSDVFTLDAETLQRLERMGQKSAENLVVALARAKQTTLRRFLIALGIRDVGGGVAQLLADAFGDLDPLMAADREALEAVEGVGPTIAEGVVGFFADPHNAAEIARLRELGLRWPKGSARQKPAAGGALEGKTFVLTGTLDGITRDEAKARIEAQGGKVTGSVSKKTSYVVVGDSPGSKLKKAEELGVEVLDQSAFEDLVT | Function: DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA.
EC: 6.5.1.2
Catalytic Activity: NAD(+) + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + beta-nicotinamide D-nucleotide.
Sequence Length: 409
Sequence Mass (Da): 44118
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A0A3B1IJI7 | MTCWIIDFWSNLWKMYVFLYIEIHFTDKVTIKIKCFFQVLYSPYYYFYYYYYYFYSLPFRRQDSRYRILTDSARKLNAQGSQLGDCIQKAWPYYEALREAEKVQENTQKAAQRYERAVSVHTAARKMENLAEQCLLADRNTMDPTWQEMLNHATAKVNEAEEERLRSESEHKCLTQRCQEAKTRVQNLHKAFMRVILKSKPYFELKAQFNDILEEHKSKVVQLKERVAKEKTHFLVTLRNLEQISEQIHAQTERIRPARKRNRAHGGRSSSVGAESEGVIKAGTYGGLRQWSEKHREQGWGQREQVERAGLDSMSVISLQNIASDLEKCDSVEGERDGGRKGVKRSGERGGKHSQTGKGSRKRHHRSVSF | Function: Functions as guanine nucleotide exchange factor (GEF) for RAB11A.
Subcellular Location: Cytoplasm
Sequence Length: 370
Domain: The N-terminal half of the protein mediates interaction with RAB11A and functions as guanine nucleotide exchange factor. Four long alpha-helices (interrupted by a central kink) assemble into coiled coils, giving rise to a 'V' shape.
Sequence Mass (Da): 43462
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A0A356TTH6 | MAEEKQDTEESPPRGGGKSTLIIVLVVTNLLVVAGAAAAVVMTMGSQPAATAEADAPAGAAREIGPLLELSALVVNLEDPNGTHFLRAGFQMEIRDAERLAEVETRLIPLRSAILLYLSGKSMDEVVGQDNRVVILEELTELMNEQVGDDLVRAVYFTEFVVQ | Function: Controls the rotational direction of flagella during chemotaxis.
Subcellular Location: Cell membrane
Sequence Length: 163
Sequence Mass (Da): 17476
Location Topology: Single-pass membrane protein
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A0A7Y5H011 | MSGSFVVLEGIDGSGTTTQASLLNSWLVEQGVPSRLTREPSDGPIGSLIRLILKGRIAGSPSSQPFDPRAVALLFAADRLDHIDTVIAPEVRHGTCVISDRYVASSLAYQSVDVDAEWVKSINLMARQPDLTIFLRVGAEAALERITKRQGLHRDLYETLIVQKKVAERYEALLADGAMANAKVLDGTKPVAELALEIRRVVAEQVLEVKRLSL | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
EC: 2.7.4.9
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Length: 214
Sequence Mass (Da): 23299
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A0A2E7ZV52 | MSDVTTNADSPRVRFILIWVAFDGAAFHGFQRQRSIRTVAGTLEQAWLTFQNEQVDARSSSRTDAGVHCRRMPVLLRTVSKIELKGIRFGLDHHLPEDLSVVDAEEVDASFHVRHDAIGKRYIYRIWSGRARDPTLRRDHWHVPWKLDISAMSEAAAMMTGEHDYAAFRTSACTAQSTVRSLNNVQVHVDQQQVEIVVEGNAFLHNMVRIIAGTLIEVGQGRRTSDDVCEALRSGRRQDAGITAPAHGLTLDKVRYGPYGSRQGLQHKTLLARLVQLPPTNE | Function: Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
EC: 5.4.99.12
Catalytic Activity: uridine(38/39/40) in tRNA = pseudouridine(38/39/40) in tRNA
Sequence Length: 282
Sequence Mass (Da): 31670
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A0A3A4K0D9 | MSEQLEKGYDPAAVEAKWYKIWEEAGYFRADENDKTRPAYCLVYPPTNVTGTLHMGHALTVAIQDMIMRWRRMAGDNVLWLPGTDHAGIATQMVVERDLKIKEGKTRHELGREEFLKRVWKWKSEKGDRIYEQLKVLGASLDWTRSRFTMDESCSRAVLEAFVRLYRERLIYRADRLINWCPRCHTALSDLEVEHQEGVAGELWSFAYPLADGSGEIVVATTRPETMLGDSAVAVHPEDPRYLNQIGRNVRHPLLNYEFPIIADAELVDPEFGTGAVKVTPAHDPNDFETGLRHNLKFINILNPDATLNENAGRFAGLDRFAARQAVKEAIAELGLDRGRQDYQMNIGACQRCNTIVEPYISKQWFVKAEPLARPAIEAVESGKTALVPKSWDKTYFEWMRNIRDWCISRQLWWGHRIPAWYCDDCGHVTVARDGATTCEKCGGAAIHQDEDVLDTWFSSALWPFSTLGWPEETKDLQRFYPNTIMETGFDIIFFWVARMMMMGIHFLKQPPFSTVYLHAMVRDHEGRKMSKSLGNVIDPLDIIYGIGREELLAKRKSDAQSLGIQPKQVEAILKATQKLFPDGIPASGADALRFFLISMVGQGRDIKLDARRIEGYRFFANKIWNASRFAMMNLDGYDLSCSPAPEDYSLADRWILSRLRKAAIAVNEGMSEWRFDQAAMGVYHFFWNEFCDWYIELAKSALYKSENPKAKAAAQHVLARVLDAALRLLHPFMPFVTEEIWRKLPRAAGGAASIMIAPYPAPGEFADAAAYESDELPMTRLQDVIRAARNIRGECGIEPGRKIPIVVQAPDAALRALFEAQRPAIVELARLSELSIVETFHKTGPAAKGVVTGAEVFVLLAGLIDIEEEKKRAAQQLAKTTKELAVSESRLASEGFVARAPADVVATERERVRDLSEKKEKLSRHLAELEG | Function: Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a 'posttransfer' editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA-dependent manner.
Catalytic Activity: ATP + L-valine + tRNA(Val) = AMP + diphosphate + L-valyl-tRNA(Val)
EC: 6.1.1.9
Subcellular Location: Cytoplasm
Sequence Length: 932
Domain: The C-terminal coiled-coil domain is crucial for aminoacylation activity.
Sequence Mass (Da): 105406
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A0A2R6CF67 | MNLGVVVSEFNSEITQRMLIEAKEYAKSLGINVEYVCYSPGAFDMPLIVRELLRKDNIHAVVTLGAIVKGETKHDEVIAFILAKQLSELSLEYGKPVALGVSGPGMSWEQGLARASEYARRAVDAALKAYTSLGKLRAGNRECSREVK | Pathway: Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 1/2.
Function: Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin.
EC: 2.5.1.78
Catalytic Activity: (2S)-2-hydroxy-3-oxobutyl phosphate + 5-amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) + 2 H2O + phosphate
Sequence Length: 148
Sequence Mass (Da): 16217
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A0A2E7BTH4 | MDMSKKDKVYCLILAVFCTVLVLTNIIGVKLFHMLPHSLGKVCWGNPASPEGTYCTLTSGIITYPLTFLLTDTVSELYGRKRADFMVAIGFVVSLVMVLFVAAAVALPGSSIWTSSTLGFSTVACQAVDAETGACLVPGMQQGYESVFTLPGTLVLGSMTAYLFAQFLDNRLFHYWRNKTQGRHLWLRNNASTIVSQLVDTLIVNIIFLWWGLGLPIEICFQILIANYVFKVLIAALDTPLVYLLTSFLRKHLNLPPAEAEYQTP | Function: Involved in the import of queuosine (Q) precursors, required for Q precursor salvage.
Subcellular Location: Cell membrane
Sequence Length: 265
Sequence Mass (Da): 29301
Location Topology: Multi-pass membrane protein
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A0A9E5AGA5 | MPQDLGTHPQSGQPQSPQYLTDLCRAFAGVGVLGSHTAVGDATVIVERTALVALMTSLRDDARCTFDVLVDVTAVDYSEFAPLMRAATSPIDADHPSGLTSATLPALEVVYHLLSMRHCHRLRVKVPVNAEDPQVPTLCEMWPAANWGERETFDMYGVRFAGHPDLRRILTYDEFEGHPLLKDFPLRGYQPLMALPTLTEYADQETYR | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Catalytic Activity: a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+)
EC: 7.1.1.-
Subcellular Location: Cell membrane
Sequence Length: 208
Sequence Mass (Da): 23112
Location Topology: Peripheral membrane protein
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A0A3B1JVZ9 | MANCNIRGIQSANNRNTKLNILKTVNLDILCLQETRLTSYKNICDAQTVWGEHLSFFSIGEDKAGGVAILFYTKNVSVLKIREIIPGRLMYVDIYLMGKKIRIINVYAFPNYNKRVSLLNKLKTILYVGFPKIICGDFNTITDLKDSNSDKLSKIGYDGCLLKQIMCENELNDIFRVLFPDKKRVFQI | Cofactor: Probably binds two magnesium or manganese ions per subunit.
Catalytic Activity: Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.
EC: 3.1.11.2
Subcellular Location: Mitochondrion
Sequence Length: 188
Sequence Mass (Da): 21541
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A0A8B9LTA8 | HIACGKILLKQALLIALVDAPMYSLYVGNKLDLSCETKDETQEVSWTKDQVLIINGDHTRLRSGALEIEGVEPADSGLYVCFARSPAGNHTKYFNVSVSDALVSSEDDDDDESSSEETKQSSSQKLLSNTMAPVWAQPDKMEKKLHAVPASRTVKFRCPAVGSPNPTLKWLKNGKEFKRDQRIGGFKVRDHMWSIIMDSVVPSDKGNYTCLVENKYGSINHTYQLDVVERSPHRPILQAGLPANRTVVVGSDVEFECKVFSDPQPHIQWLKHIEVNGSKVGSDGLPYVRTAGLNTTDKDMEVLQLRNVTIEDSGVYTCLAGNSIGNSHHSAWLTVYEAVPPTPLPNQTYLEVLIYCVGFFLICVMVVIAVGVKMHSSSKKSDFNSQMAVHKLAKSIPLRRQVSVDSSSSLHSGAMLVKPSRLSSSGSPMLSGVSEYELPQDPRWELPRDKLVLGKPLGEGCFGQVVMGEVLGMDKDKPNRITKVAVKMLKSDATEKDLSDLISEMEMMKIIGKHKNIINLLGACTQDGPLYVIVEFASKGNLREYLRARRPPGMEYCYNPDQVPVENMSIKDLVSCAYQVARGMEYLASKKCIHRDLAARNVLVTEDNVMKIADFGLARDIHHIDYYKKTTNGRLPVKWMAPEALFDRIYTHQSDVWSFGVLLWEIFTLGGSPYPGVPVEELFKLLKEGHRMDRPTTCTHELYMMMRDCWHAIPSQRPTFKQLVEDLDRTLSMTSNQEYLDLSVSLDQYSPSFPDTRSSTCSSGEDSVFSHDPGADEPCLPKFPPHPNRGVAFKKR | Catalytic Activity: ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]
EC: 2.7.10.1
Subcellular Location: Cell membrane
Sequence Length: 796
Sequence Mass (Da): 88874
Location Topology: Single-pass type I membrane protein
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A0A956ADP8 | MRIGLIGAGNLGEALVRGVGAAFGRVLVAEKRSERLDFMVATYGVEPSTVSSLMSQAEVVIVAVKPTQIAKTLGEMAAAVTQQQIIVSVAAGVSLSQIALYLGAERQLVRVMPNTPAAVGAGVSAIFHPAGERGVLDKVHAVFSCVGDVVEVQDESWFDAITALSGSGPAYICLVLEALVEGGVKAGLPRDVASRLALGTLRGTAALVDARDGDAAATRHAVTSPGGTTAYGLAVLEQRATRSAFIEAVAAAAQRGHELGQRS | Pathway: Amino-acid biosynthesis; L-proline biosynthesis; L-proline from L-glutamate 5-semialdehyde: step 1/1.
Function: Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline.
Catalytic Activity: L-proline + NAD(+) = 1-pyrroline-5-carboxylate + 2 H(+) + NADH
EC: 1.5.1.2
Subcellular Location: Cytoplasm
Sequence Length: 263
Sequence Mass (Da): 26914
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A0A4D7QTE7 | MPPFGFFPALAISFPVLVWLLDGASAAGGGWRTIWAAAKTGWWFAFGYHLAGLWWIGAAFLVEADRFAWALPIAVVALPAGLALFTALGTAVARLLWRPGAGRILALALGLGLAEYGRGTVLTGFPWNLYGYALTQYLWLAQAASLVGVYGLTLVAILVFASPSVLGDDPDDAAGRAFVPAGAILVLMCLGLYGGWRVSTTPVGMVEGVRLRIVQPDIPQDARFRPEERDTILARYLELSDKASSPERMGVRDVTHLIWPESAFPFFLIRDRAALAQIANLLPPGTTLLTGAARPEAPAPGRSDIRVYNSVYMIDDAGQITETYDKVHLVPFGEYLPFQDRLESMGLEAVTRVRGGFSAGDRRRTLTVPGAPPVGILICYEIIFPGEATSGDRRPGWLLNVTNDAWFGFTPGPYQHMHQAQVRAVEEGLPIVRAANNGISAVIDPLGRVLRMLPLGARDSLDADLPTALAPTPFARAGHVPLAVVFFGLFLILARPARRRSLG | Pathway: Protein modification; lipoprotein biosynthesis (N-acyl transfer).
Function: Catalyzes the phospholipid dependent N-acylation of the N-terminal cysteine of apolipoprotein, the last step in lipoprotein maturation.
Catalytic Activity: a glycerophospholipid + N-terminal S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipoprotein] = a 2-acyl-sn-glycero-3-phospholipid + H(+) + N-acyl-S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipoprotein]
EC: 2.3.1.269
Subcellular Location: Cell membrane
Sequence Length: 503
Sequence Mass (Da): 54260
Location Topology: Multi-pass membrane protein
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A0A971FBC2 | MTRVTIEARNTSGRAGCFRSDALRRLSEKVLADQGMEGAFQVSVLFCGDEFIAGLNREYRGKRGPTDVLSFGQEDGAAPPDGRVLGDIVISLDMVAARCAGDPEAMRAEVRLLFCHGLLHLIGHDHGTAAERRAMQAVQARCLGVSPGDAWRGGKAG | Cofactor: Binds 1 zinc ion.
Function: Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA.
EC: 3.1.-.-
Subcellular Location: Cytoplasm
Sequence Length: 157
Sequence Mass (Da): 16768
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A0A1G1WNF4 | GEAATSNYKIASGDLITLELPSPKAVQIKAEKLSLKVLYEDDDLIVIDKPAGVVVHPTNDHSSGTVVNWLLDHLKGFDKDFTEDSRPGVVHRLDKGTSGLLVIAKNPPAAEKLKKQFSRRMVKKKYLALVSGELVKPFGTIKGKIGRDSRSFQKFAVREDGREAETEYRLFQRYPGASLLEVYPRTGRTHQIRVHLSSIGKPIVGDKLYGGKTALNRPFLHAAALSFLHPTTGKPLNFESPLPPALQAYLDKLSLK | Function: Responsible for synthesis of pseudouridine from uracil.
EC: 5.4.99.-
Catalytic Activity: a uridine in RNA = a pseudouridine in RNA
Sequence Length: 256
Sequence Mass (Da): 28262
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A0A3B1IW40 | NKEIHFSQFSQELKNHKTYIQNSFFDEFLGYRILTDSARKLNAQGSQLGDCIQKAWPYYEALREAEEVSRDQKAALRYERAVFIHTAAREMVCVAEQCLLADRNTMDPTWQEMLNHATAKVNKAQAERLRSERERQWVTQLCQEAKARVQTLQKALMRVILKSKPYFELKSQFIDILEEQKSKVVKLEVRVAEVKTRFGVTLCNLEQISEQIHAQRERFRAARKRNRARGGRSSPVGAESEGVIKGVAYGGLGASLIDNWAENEAVVGEAQGAGLGSERRGERAGLDSMSVISLQNIDLEKCDSVEHLCDLSDVGSLVGEEKETEGESGVRAEVKVVVREVANIARQEKEAERGASAALNSTTGVLASENCIDDTLKQGCAEGQQSCRD | Function: Functions as guanine nucleotide exchange factor (GEF) for RAB11A.
Subcellular Location: Cytoplasm
Sequence Length: 389
Domain: The N-terminal half of the protein mediates interaction with RAB11A and functions as guanine nucleotide exchange factor. Four long alpha-helices (interrupted by a central kink) assemble into coiled coils, giving rise to a 'V' shape.
Sequence Mass (Da): 43485
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A0A2E6VTR8 | MVNGPHNDVSIWRRFILPFLFVLALFVALFLRRPDAEAPVSNSGVEEVAKQPAEMVLRGETMGTTYNIKLVPETLEQAQTWHTLQPKIDQRLEDINNLMSTYRPQSDISKLNANTSIEPVVLQEEFAKVVAASLNIGEQTGGAFDVTLGPLIALWGFDKGERRTTAPSTEEITSLKAFTGLDKISVNQNAFQKKDGRVQINLSGIAKGYGVDAVAALLRNAGVNNFMVEIGGEIFVQGKNSQASQWKLGVNRPTPEAGRYEIIETVALSKGGMATSGSYRNFFNEAGKRFHHIINPKTGQPVDHNLVSVTVVADTCMQADALATAAMVLGQAEFEKVLKAHYPNASAFFVHQNEQRFDAFKTANFPTLD | Cofactor: Magnesium. Can also use manganese.
EC: 2.7.1.180
Catalytic Activity: FAD + L-threonyl-[protein] = AMP + FMN-L-threonyl-[protein] + H(+)
Sequence Length: 369
Sequence Mass (Da): 40469
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A0A956A0K8 | MARDLDRIDARIEASLESLAIAVDAGARRRLAALSLLVAQWNERMNLTGHREPERIADRLAVPAVCLAEALPDFGSLADLGSGAGFPGLPIAILRPEARVTLVESRERRHHFQRAAIREIEIANATPLRGRIEEIEAIPHDVALAQAVGPPSEVLAMIRGWVRPGGLLGIPASGHATPPTSAAGTSAIEVRRYRTPDPDAPGRIEERAVWLSRAT | Function: Specifically methylates the N7 position of a guanine in 16S rRNA.
EC: 2.1.1.-
Subcellular Location: Cytoplasm
Sequence Length: 215
Sequence Mass (Da): 23162
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A0A956CE98 | MRLFFALPLSAQDVAPLLESQKRMRAVTSRLAPRFVKADQLHLTLKFLGNVDRLDELRAALRQVTAPALETRFTGLTGFASPSRARVLVAELADPDGRLAALASTLEEIGTAVGVPRERRPFRPHVTLARIKHPGNARALLEAGALEPYAVRFTELVLFESQLLASTSRYTPRERCALGAE | Function: Hydrolyzes RNA 2',3'-cyclic phosphodiester to an RNA 2'-phosphomonoester.
EC: 3.1.4.58
Catalytic Activity: a 3'-end 2',3'-cyclophospho-ribonucleotide-RNA + H2O = a 3'-end 2'-phospho-ribonucleotide-RNA + H(+)
Sequence Length: 181
Sequence Mass (Da): 19925
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A0A2J0MF30 | YLDIVRQARQKFRFPLAAYNVSGEYSMVKYGAKAGLWDEKKMVFEVLTSIKRAGADWIITYHAKDIAQWLRG | Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 1/4.
EC: 4.2.1.24
Catalytic Activity: 2 5-aminolevulinate = H(+) + 2 H2O + porphobilinogen
Sequence Length: 72
Sequence Mass (Da): 8371
|
A0A1F2Z4U9 | MMPDQFDPDPRLQSVLDRLTTYYPRAIDPNLERTDRLLNDLGNPHLSMPPVLHVAGTNGKGSTLSFMRAVAEAAGLSCHVMTSPHLVRFNERIVLNGQEISTPDLINVIEEVEAANKGQETTSFEIITAAGFLAFSRRQADLCVVEVGMGGRFDATNVIPSPLATTITVISRDHVKFLGTDLAGIAREKAGIIKQNVPCIVGPQIRAGLVAGVMDVFEDIANAHNAPLYRHGIEWGYDVLPDRLILHTQTNIYEFPKPNLLGDHQYGNAATAAMTLLAVQDKLPLPLSAFEHGLTHARWPGRLERLTSGALVDLLPPHIELWIDGGHNDSGGMILGEQASKWAAEDGKPLHLILGMLNTKNPTEFANFLLPKTTSAQAITIPDQPLSLTADELAKSLNIPAASSLDAALRQIAENETKPARVLITGSLYLMGHILSR | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 2/2.
Function: Functions in two distinct reactions of the de novo folate biosynthetic pathway. Catalyzes the addition of a glutamate residue to dihydropteroate (7,8-dihydropteroate or H2Pte) to form dihydrofolate (7,8-dihydrofolate monoglutamate or H2Pte-Glu). Also catalyzes successive additions of L-glutamate to tetrahydrofolate or 10-formyltetrahydrofolate or 5,10-methylenetetrahydrofolate, leading to folylpolyglutamate derivatives.
EC: 6.3.2.12
Catalytic Activity: (6R)-5,10-methylenetetrahydrofolyl-(gamma-L-Glu)(n) + ATP + L-glutamate = (6R)-5,10-methylenetetrahydrofolyl-(gamma-L-Glu)(n+1) + ADP + H(+) + phosphate
Sequence Length: 437
Sequence Mass (Da): 47423
|
A0A5E4PKS4 | MTAGFRDYLILCKPRVVLLMLLTAWAGMYLGASNPIPWWLWLNATAGIALMSGSAATLNHIIDHRIDALMDRTKHRPLASGKLTIQAAWQFAALQGVGGFCILYFGVNALTAILTLLAAIGYSAVYSIYLKRATSQNIVIGGLSGAMPPLLGWTAVTGKLDPQAWLLVLIIFTWTPAHFWALCLHRYHEYKKTSIPMLPITHGISFTKLNIVLYSLLTIACSLLPFAIGMSGQLYLICVLLLDAGLIGYALKLQFAANDQGIALKTFQYSLVYLTGLFLVILLDHHLLVN | Pathway: Porphyrin-containing compound metabolism; heme O biosynthesis; heme O from protoheme: step 1/1.
Function: Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.
Catalytic Activity: (2E,6E)-farnesyl diphosphate + H2O + heme b = diphosphate + Fe(II)-heme o
EC: 2.5.1.141
Subcellular Location: Cell membrane
Sequence Length: 290
Sequence Mass (Da): 31819
Location Topology: Multi-pass membrane protein
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A0A2Z4Y5Y4 | MSLHRHAEKCRWGIYVILDRYLAKKSHLEIAREVIAGGARVIQLRDKHASRSELVEIGRELRQLTRAAGVTFIVNDYPEVAVEVDADGVHLGQEDRAVHEARQLVGRDKIVGLSTHTLDQALAAMELPVDYIGVGPVYATSTKENPWPVVGVELVRKVKKRVALPIVAIGGITEQCIPELVAAGADNVAMIGELMRAAHLREKMESLVQTFENAKALFEQQPGAR | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine phosphate from 4-amino-2-methyl-5-diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)-thiazole: step 1/1.
Function: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP).
EC: 2.5.1.3
Catalytic Activity: 2-(2-carboxy-4-methylthiazol-5-yl)ethyl phosphate + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + 2 H(+) = CO2 + diphosphate + thiamine phosphate
Sequence Length: 225
Sequence Mass (Da): 24794
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A0A1H3W0U0 | MDLLSPIDTIKGVGEKTTKLFNKLGVYTIEDILLFFPRTYLVYPECSIPDKDSVNSLISISGRIKSSPKMFRSKNHMDILSVTTYVNDIPVDLVWFNSNYLRNNFEPGKVYIFYGRLVSEKGRFKISQPAIFTPEKYQELRREIQPIYHLTKGLTNNAVLKAAKSAFEGAKIPEFRLPEELEKKNDFMPYNKALYTYHFPDKFEKLVEARRRLAYEEMFFFILNSKLQEEKSISFPNEFDICHHQETDCFKSKLKYSLTSDQDKVLSEILSDLTGNYATQRLIQGDVGSGKTIVAFLAMLDVALSGYQAAIMAPTEVLAKQHYESFTEWIELAGIDIPVALFTGSMKASEKKAMQKLVDENPNTLIIGTHALITDGREFGNLALVIVDEQHRFGVQQRDKLSSKGNHPHIIVMSATPIPRTLAMILYGNMHVSAIKELPANRLPIKTCVIKESMRPTAYKFVSDEVEKGHQAYIICPLVEASETTEAQNVTDYSKKLKSYFNDKYEIGVLHGKMKPAEKNQVMEDFANHKTQILVSTTVVEVGVNVPNATVIMIENANRFGLAALHQLRGRVGRGDAQSYCILMNESKDDNQSKRLNIMLKSNDGFYIAKEDLKLRGPGDLFGVRQSGEFSFKVADIYQDANELEMASNDVDIILKEDPNLDNHLELRSTLNLFLANQFYVL | Function: Critical role in recombination and DNA repair. Helps process Holliday junction intermediates to mature products by catalyzing branch migration. Has a DNA unwinding activity characteristic of a DNA helicase with a 3'- to 5'- polarity. Unwinds branched duplex DNA (Y-DNA).
EC: 3.6.4.12
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 682
Sequence Mass (Da): 77360
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A0A7Y5GVS3 | MAIDWFTVGAQILNFGLLVWLLKRFLYRPVLAAIDAREQKLVASLQQAQDTKAQAERELLEFRSQVAELQTKRDELMRQTHQQAQAERRRLVDEARAEAQRWSEHQHQVVAAELQKLENTFAKAVQKEVFAVSRKVMEELAAVSLETRVVEVFLERLRGIGEPEKGKLAMAWAKSEGPVVVRTTMGLTPQQKSAIAETLYDTFGVKLELTWESAPELVCGIELWAVGQKVAWNIGDRMTSLEKVAAEWMDAEKKGNR | Function: Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0).
Subcellular Location: Cell membrane
Sequence Length: 257
Sequence Mass (Da): 29229
Location Topology: Single-pass membrane protein
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A0A7Y5GYG1 | MPVLRTVGEIRNLVRSWKQDGLRVGLVPTMGYLHQGHLALVQHGLRFCDRIVMSIFVNPTQFGPNEDFDRYPRDEHGDRAKAEEAGVSALFCPYLNEMYPAGAETYVSLDRLPHHLCGPLRPGHFRGVATICTKLFVAVEPDVAVFGEKDYQQAVIIKRLALDLLLPTRIETAPIVRESDGLAMSSRNVYLAPDERRRALCIVQALDQAELSVKRGEYDVRKIRLQIMALLNSANFQVDYVDFVHPDTLENEESIGSPTIVAIAGFIGKTRLIDNRLLIPPNPTDDQKRVW | Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1.
Function: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
Catalytic Activity: (R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+)
EC: 6.3.2.1
Subcellular Location: Cytoplasm
Sequence Length: 291
Sequence Mass (Da): 32770
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A0A7X7UFW2 | MGESLTPKTNSPARARSSISLRRRHPGRSPDTKPLRALVAAAGTRLERAGDRVEILLVGDGASRRYNRDYLGRDRPTNVISFPADEAGEWGQLIVNVDEAARQSGETGYGLLYLTGYYILHGLLHLSGYDHERVSPDEAARMKEREEALRDLLAPLLEQEDGK | Cofactor: Binds 1 zinc ion.
Function: Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA.
EC: 3.1.-.-
Subcellular Location: Cytoplasm
Sequence Length: 163
Sequence Mass (Da): 18081
|
A0A970SBF7 | MQPGTPPLVNQLIDMALEEDLGRGDITCRLTVPEDAHSQGHLIAKQALVVSGIHVFAAVMRRVDPATRIHIEIGDGQSARPGALIARTDGRTASLLMAERVALNFLQRLSGTATLTRELVDALPPDATTRLVDTRKTTPGMRWLEREAVRHGGGHNHRVDLSGGVLIKENHAAAAGGVGRAIALCRQNAPHLLRIEAEVRNAAEFDEALLAGADCIMLDNMSPEQMAECVKKANKRVILEASGGVSRQTVADIAATGVDIISVGAITHSAPGADISFIIDGVTPV | Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-ribonucleotide from quinolinate: step 1/1.
Function: Involved in the catabolism of quinolinic acid (QA).
EC: 2.4.2.19
Sequence Length: 285
Sequence Mass (Da): 30173
|
A0A363TP33 | MRLILLGPPGAGKGTQAQRLVDRYGIVQLSTGDMLRAAVKAGTEVGLRAGDIMARGELVPDEIVVAIIADRIAEPDARNGFILDGFPRTVAQAEALDRLLAERDLTLDAVVELKVDEAILLKRVETRVAQAQARGEAVRADDNPEALKIRLDAYRRQTAPLIDYYWEKGNLRTVDGMAPIDEVAAALVRALEPARPAEPAPGAVPESPAPSRPAASRRAPPARKAARKVVRKVKAAKRSKAGKRAGPAGKQTRKAGSAAKPARKAKPAAKIARKAKAVRKGKAGKAGKARKAAPKARTGVRTAAKSARKAGTAGRRPARKAARAATRGRRG | Pathway: Purine metabolism; AMP biosynthesis via salvage pathway; AMP from ADP: step 1/1.
Function: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Catalytic Activity: AMP + ATP = 2 ADP
EC: 2.7.4.3
Subcellular Location: Cytoplasm
Sequence Length: 331
Domain: Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis.
Sequence Mass (Da): 35010
|
A0A955WAN4 | IAEIKFKSPSVGSIRPPAPGTAAALAQAYQRGGAAAVSVLADGPGFGGSPLTVRRVARACSAPVLFKEFVLHPLQVELARVCGASMVLLLVRAHALGPLQSLCDDVRRAGMEPVVEAADEEELAVALRTDATLVGVNARDLRTFDVDMERAARCLDQVDASRVAIFMSGIRTPTDFARLGGTRADAALIGEGLMRCEDPAAGVRAMLETTI | Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 4/5.
EC: 4.1.1.48
Catalytic Activity: 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate + H(+) = (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O
Sequence Length: 211
Sequence Mass (Da): 22094
|
A0A2N2DSP8 | MYQEKRIAVIIAAAGSGTRMGSGISKQYLTIGDDMVLAKTLQVFGTHPFIDDIFLVVRSEDMEFCRQELVKKLRPAKLRAVITGGKERQDSVYNALQTMQRLIDRWPDDYVLVHDGARPFVSADEISRLTAAAVEHQAAALGVPVKDTIKRSDGKVFLETLDRNTLFAVQTPQGFQRELLLEAHEKARSEKRLSTDDAALVEFIGKKVCLVPGSYDNIKITTREDLPQTETFEWRSGSGYDVHRFTKDRPLVLGGVSVFSEQGLLGHSDADVLTHAIMDALLGAAGLGDIGTHFPDSEVKYKGCSSLVLLGRVRELLLSKGFLVENIDATLIGEQPKIAPYAAEIRTTLGKTLGIPAERINIKGTTTEGLGFCGRREGLAASATAMLSRSKSSK | Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 2/6.
Function: Bifunctional enzyme that catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP) (IspD), and catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP) (IspF).
Catalytic Activity: 2-C-methyl-D-erythritol 4-phosphate + CTP + H(+) = 4-CDP-2-C-methyl-D-erythritol + diphosphate
Sequence Length: 394
Sequence Mass (Da): 43107
|
A0A3B8L8E7 | MCYVQDIALYVRQQLETSNLDGTTMAFVRKDHFHKKAKQAGLRSRAAYKLEELNKRFHLFKQNGKVLDLGAAPGGWMQVAAKAVGRHGRVVGIDRLEMDPLPFSQATILLGDLLDPIVQEQALKEMNGPADCVLSDMAPNITGIRLTDCARSHELAMIALNVARRCLRTGGAFVVKIFPGDDLEDFRKEMKHSFRKVRTTRPEATRKTSSEIYIIGTQFRGTEEHTPSKETTSGH | Function: Specifically methylates the uridine in position 2552 of 23S rRNA at the 2'-O position of the ribose in the fully assembled 50S ribosomal subunit.
Catalytic Activity: S-adenosyl-L-methionine + uridine(2552) in 23S rRNA = 2'-O-methyluridine(2552) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine
EC: 2.1.1.166
Subcellular Location: Cytoplasm
Sequence Length: 235
Sequence Mass (Da): 26295
|
A0A947MPX4 | MNPSPWRPPSRPTPAPAAPVRVLVVDDSAVIRRVLKDGLSKDPLIEVVGVAADAYEARDKILDLNPNVITLDLEMPRMNGIEFLKKLMAQYPLPVIIVSGLSQSGAAATVSAMAAGAFDFVTKPSSSTPDGVALMMDDLRRKVRLAGRAPAQSPGSPRSGVAAPQVVKASPAVRPVAQESNGRMIAIGASTGGTEAIAEVMSALPADCEGVVIVQHMPAGFTRAFAERLDRLSQLRVREAQDGDAILRGEALVAPGGQQLRVVRSQRGLRVQVGPGPLVSGHSPSVDVLMTSVAEACGGNAAGVVLTGMGRDGANGLLALRNAGGRTWAQDEATSIVWGMPRACHEVGAAERLLPLNAVASALASFRSSR | PTM: Phosphorylated by CheA. Phosphorylation of the N-terminal regulatory domain activates the methylesterase activity.
Function: Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irreversible deamidation of specific glutamine residues to glutamic acid.
EC: 3.1.1.61
Catalytic Activity: H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+)
Subcellular Location: Cytoplasm
Sequence Length: 370
Domain: Contains a C-terminal catalytic domain, and an N-terminal region which modulates catalytic activity.
Sequence Mass (Da): 38456
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A0A970M9F8 | MHRYETAFAAEAAAALDLPIDNIQGHVRVPEPERGDFSLPCFPFAKALGQPPVKIAQTLTEKLSQSQRFAVAAAGPYVNATIHPEALLATLIPEVRQLGDRFATSDTGQGQTVIIDYSSPNIAKPLGFHHLRSTMIGNALTRILGALGYTVKGLNFLGDWGKTFGLLAAIYQRKGQRDRLEKEGIAYLLELYVEANREREANPSFDDIARALFKRMEDGDTDALELWQLFRDISLKEFQRVYTRLNVSFDHYEGESDYRDGMDALIETISATAGTRIDQGALVVDMPYGENEPPMMLKKSDGATLYATRDIAAAKDRWQRYAFAKSIYVVGGEQKRHFEQLKRALDAMGDAWQERMVHVSFGRVHGMSTRKGNVVFLEEVLDEAVERAREKMTAESSGRDIDIDKVSEEVGIGGIVFGDLKNLRTSDYNFDWEDILNTKGFSGICVQYAHARCSSILHRAGGAPGIDAYDPSLLVAPEEVALVKEIGRLPAAVLAAAEGFEPSRLARAVYEVARAWNRYQQAGNADKTLRILAEDDALRTARLALVDAARIALKQGLLLLGVAAPEAM | Catalytic Activity: ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg)
EC: 6.1.1.19
Subcellular Location: Cytoplasm
Sequence Length: 568
Sequence Mass (Da): 62726
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A0A9E5VK55 | MNETENSLSAPPETRPEHGTKTRERTRQEAKREMVEFVKMVVWFLLLFLVLRGFVIEGYEVQGPSMEPTLYEQERILVFKLGQHWPFSTFLGTHPGDIVVFDSPDDRGKRYVKRVIAMGPEERSGNTVRAGRDGEPESGVRLRLRDTAIYVNDRKLDQSYLAENALSNEEDREVLIGPDEYFVMGDNRNISKDSRNFGAVGEDLVIGRALLRFWPLDRFGFIK | Catalytic Activity: Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins.
EC: 3.4.21.89
Subcellular Location: Membrane
Sequence Length: 223
Sequence Mass (Da): 25685
Location Topology: Single-pass type II membrane protein
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A0A7X7Z1T1 | MSSNVLGRRYAGALLDLGIRDGHAEPYSGQLEAAAAALGAGPAKKVLTSPLYDLEFKKKLIDQVTGPLGLAAPVANLLRLLLDKHRIGFLTDIAASYRELLDGYLGLMRATVYTAVPLDGAALGRLRVLLQRKMGHRVELTAKTDPAIIGGLRVHVGSKVFDMTITNHLSRLRGMLKHQVL | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.
Subcellular Location: Cell membrane
Sequence Length: 181
Sequence Mass (Da): 19529
Location Topology: Peripheral membrane protein
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A0A1F2Z190 | MAKQPNTTLSVKLNKYHELLLKWSKVINLVAPSTLPDAKMRHFVDSTQIIPLIPADAKTLFDIGSGAGFPGMVLAIECPNLSVHLIESDTKKCSFLATISRETDTPVLIHNRRIESVDKLDGIKPDVITARALASLGELLALTEQWWSNNPQVTLIFPKGAKANEEIADAQKSYQFHVELVPSQTDKLAQILVLRDIKKL | Function: Specifically methylates the N7 position of guanine in position 527 of 16S rRNA.
Catalytic Activity: guanosine(527) in 16S rRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(527) in 16S rRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.170
Subcellular Location: Cytoplasm
Sequence Length: 200
Sequence Mass (Da): 22146
|
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