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stringlengths 6
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stringlengths 16
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stringlengths 117
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A0A426YH66 | MREEYGKLDRVEMSIWECIELLNELVDESDPDLDEPQIEHLLQTAEAIRKDYPDEDWLHLTGLIHDLGKVLLHPSFGQLPQWAVVGEHEPHHLLASLSSGNHFKENPDYSNPKYNTKLGVYSEGCGLENVLMSFGHDDYMYLVAKENKTTLPSAALFAIRYHSFYRNSINSSHLLTWLPLT | Cofactor: Binds 2 iron ions per subunit.
Pathway: Polyol metabolism; myo-inositol degradation into D-glucuronate; D-glucuronate from myo-inositol: step 1/1.
Catalytic Activity: myo-inositol + O2 = D-glucuronate + H(+) + H2O
EC: 1.13.99.1
Subcellular Location: Cytoplasm
Sequence Length: 181
Sequence Mass (Da): 20806
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I1IY91 | MVMWVFGYGSLVWNPGFAYDARLVGFVRDYRRVFYQGSTDHRGTPEFPGRTVTLEHQPGATCWGVAYKISREEDKQTALEYLEVREKQYDEKVYLDLYTDSSPKTPAVQNMMVYLATTNKEANVNYLGPASLEEMAKQIYLAVGPTGPNKEYLFKLEDALNKIGVVDEHVQDLANAVREYSSTMLS | Cofactor: Binds 2 Mn(2+) ions per subunit.
Function: Catalyzes the formation of 5-oxoproline from gamma-glutamyl dipeptides and plays a significant role in glutathione (GSH) homeostasis.
EC: 4.3.2.9
Catalytic Activity: an alpha-(gamma-L-glutamyl)-L-amino acid = 5-oxo-L-proline + an L-alpha-amino acid
Sequence Length: 186
Sequence Mass (Da): 21173
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A0A961XQ45 | MKSQMKRMATTTLCAAALMAAPVSGGVSEAQAGNSNIIKGIIGGVIAGAVIGSIVRAGQNHCHGSACHAHGYARAGHYHDAYGNIIYQAPPQTVIVAPPPPPPPAYSGSYPQAHYDWCFGKYRSYHAQSNSYQPYGYSGRRQCISPYM | Function: Has immunoglobulin-binding and hemagglutination properties, and can bind to mannose. Essential for virulence. May be involved in LPS biosynthesis or polysaccharide transport.
Subcellular Location: Cell membrane
Sequence Length: 148
Sequence Mass (Da): 15701
Location Topology: Single-pass membrane protein
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A0A0R3PTP2 | VIPLQKPLIDDSLSVASSKSVVISGSSYPTSFDYSAYNPQYYNGMRAGYYGNALAAGASAYAVRFASSVCLQGLVTVTYNFLLQGGKSAKKKKTDSCSPADTHFARVFVWELDDICTLSTASLNEVARKVGHVDSLNDSRGGVEVMRRMASKYLALRQLYLECALKPDAQLCDYGAGLVHFSQADRKYAEVKIIFRTAVSSEKYANVVLCGDPLVPAVVQLLLAGLAPVAPIENVYSTNKTGRVRMVSKLPLNWQLMSFAGSGDRSNSEPSIPVWPIVTTDDFEKLYTAQTNYLLGSL | Cofactor: Binds 1 Mg(2+) ion per subunit.
EC: 3.1.3.48
Catalytic Activity: H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate
Sequence Length: 298
Sequence Mass (Da): 32389
|
A0A2A6CXA9 | MGGRRADLRSPSATHFCFSLNETQKGPSLYSIPFCSSFSCSSCSIFSSATTNTPDMETHSIAAIFLLLISLLFIFIAQTDPQRLDTSISSFIILNITAAETKRVPKILAWTPYFSRKLEDRIRSDSCPFQCDVFNRSQLSEEAADAIVFHFRDLHENMPLPRTRRPDQIYVSFLKEAPAHAGSGMNSRIVRFAIFSRPESKGTQEAFDKIVNSKTDAVLAIISNCHAESGRLEYIRELDKYINVTKVGACFGSRISNEDVEKMIASHSFVIAFENIQCEYYATEKFWRITKDIVPIVLQRSILKDLVPSSAFVAADDFRSPLELAEHLMRAAECKDEYRKYFAWRNTHYRQQVDGFCNLCRDLHFKNVSTSAHLNMKEYYSVSRECEFDTAAKLLGKLLGNHLLSTSSIPNPSLLFSSITMRFFFILSLLALILAVFAQDAAAPAETAAVDAVDGATSAPLDFNNEEAVDNAVAELAASQEEGDEKKVILFLRLWWTIIWRSPAHEPSTAMLDHLVNYCLDKTRPCLNSCDESMQCRNALNAWRNAFNATPIDFTISKS | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus
Sequence Length: 559
Sequence Mass (Da): 62920
Location Topology: Single-pass type II membrane protein
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A0A662IKL2 | MFVKELDLKRSKVVVVPESTDDLYRLSLILERDDLVYAWTLRTLRISDGLTERRGERVKAYIGIRLEKVEFQEFSEKLRVHGVVIEAPDFLHAQGSHHTHIIEPGKEVLIVKKSRFKRYQLKLLEERGRNWALILSVGEDETAISVLRDQGVEVLLTIHRSKGDIKTSIRERYYDYLSEVARKSLEILSRRELGVETLIVASTPLLLKWFREELNRTVLPQVRGKGYTIYEVEVSEGGIAGVYELLRSGKVQKLFRNLRIVFFESLMNEVFQRFSSSPEKVSVGLEEIELAASIGAIDKLIVVDNFLREHLSEELIIRIFEAVDRSRGEIIIVPLKSEAGLKLRALGGIVALLRYPLKYS | Function: May function in recognizing stalled ribosomes, interact with stem-loop structures in stalled mRNA molecules, and effect endonucleolytic cleavage of the mRNA. May play a role in the release non-functional ribosomes and degradation of damaged mRNAs. Has endoribonuclease activity.
EC: 3.1.-.-
Subcellular Location: Cytoplasm
Sequence Length: 360
Domain: The N-terminal domain has the RNA-binding Sm fold. It harbors the endoribonuclease activity.
Sequence Mass (Da): 41372
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A0A158PFK8 | MVLITSSTVYALISVVYGVATFNDCPLAKEELLKEIKEARDDLKQRKRPLGRSSGVMYVFVIATKRCKSFVKRIMIPTDIVLEAGCQRGSKLSYIDDAEELRERLRRLWGKMHSSITQFFKQIYGEVKHVVSEIPLVNEVVMENLLESLALIRTIVRLSGFHSHSSLSIQPKS | Pathway: Protein modification; protein glycosylation.
Function: Stabilizer subunit of the dolichol-phosphate mannose (DPM) synthase complex; tethers catalytic subunit to the ER.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 173
Sequence Mass (Da): 19671
Location Topology: Multi-pass membrane protein
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A0A2A6CFB3 | MSGKKTKRAEPGGPKGAEIVRKKGKGGGEEAEGEVKEKKQEKDVEVLSKEEIEEKLREIKQSSTEETLRKKRGDKMQRATHGKALRLQRAAAKRERQSQRAKLREKHGEAMVPKEVPKTIESTREYDETMVAEQDEEVEHDEANDEFAAYYRKDVAPKVLITMSPYARVRTWKLCYELQRCIPHAEIFSRKGVPLKKVVEQAKAKGYTDLLVVHENMREPNGIVFCHLPEGPTAFFKINNLTFTKDIKKTGDSSDHYPEVVVNNFNTRLGHTIARMFTCLFPQNPEFKGRRVVTLHNQRDYLFFRHHRYEFKKEGTKAALLELGPRMTLRLKWLQKGTFDTRCGEFEWVLKMSGRLLAGLGRVAAMRALSSSASRAPSGAAFLAPRASAARTLGAARTRFAWGDDAKGPEVPVGGRMGPSENPELHTYDGDYRGTISKGDKPIPDYFYRTPTMGTTYIDRCLTYTISAILWFWFSYHMYYHSGHILGHWYMPYLHEFSDAELGIPADSAADPEYWGQHKKN | 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: 521
Sequence Mass (Da): 59472
Location Topology: Peripheral membrane protein
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I1J3P7 | MAFSRAAKLGMVVVAVLLLSAPAALSLPSLISMPNNDAGGLSYDFHDASCPNLDQMVHDAVKKAKEADVGVVAGLLRLSFHDCFPQGCDASILLLNKFWGELNMPQNHGIRRSAVHLIEDIRKAVHEACGATVSCADILNLATRQAVMQSGVPGYEVPLGRLDSPWPAALKKVQELPGPGFNATELKESLASRGLDTTDLVALSGAHTIGRASCRSFSDRFHENNDGFVRRLRDNCTGNADRLQELDVTTPDTFDNKYYSNLVNGEGVLSSDMALTRDAETGMLVRNFAGNQGWFFSQFGTSMRKVAHLPGAQEANGQIRRYSCFWNNAWGPAGPPAAYLAGEELLKASV | Cofactor: Binds 2 calcium ions per subunit.
Function: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress.
EC: 1.11.1.7
Catalytic Activity: 2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O
Subcellular Location: Secreted
Sequence Length: 350
Sequence Mass (Da): 37751
|
A0A2A6BH45 | MSIFAVAMTISYQTGFFHLIFRWYGSIWRSIYKELTVYLVLFFSIRLFHTLAIPWLDGDGEKNMKVRFEAICRQFDNYTKLIPLTFLLGFYVSNVVSRWWRQFECLNWPEDLLSLLCVCVKDKDGTDDRAHRVRHRIARYLNAKEECPYTRWMTPLHWVQQIMANEVANHDMQVTYLTNFMSELKNFRASFRRLFCHDWVCVPLVYTQVAAIATYGFFFFALFGRQNINQNDVDTIFPIFTVVQFLFFVGWYKVGLDLMRPFGLDDDDIELAYILERNINVSFAIVGKLQKQPPPPYEEDKFLNSDVRIELHSLTSDKTNQKFRGPKLNTYDQLVDLEQSMEEGYEENGRGQKEKMGSFMDVAEKVIKEERRARVTHGLNKWLPTWKEDIPKEKKMFYW | Function: Forms chloride channels.
Subcellular Location: Cell membrane
Sequence Length: 399
Sequence Mass (Da): 47485
Location Topology: Multi-pass membrane protein
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C1ING1 | MQLFFKSNLMITLLMLILAGTSMNNFLLIWVFMEMSTLVFIFIVSMDQYTLSSLSLKYFITQSFISMVMVITFLLFDGEAIMLKEMILSGLSLWKLGVPPFQNWFMNLIMDASWHVFFLISTVMKVIPFLILSMFFSYMAFTIATLSVLAPSFMGASQICMKKIMGVSSMFTSGWVIFSMISSKSDWLIILLLYSLMLLVFCANVSAESMSTLDNSFGLSSSDSLLMFFVLLSLSGIPPMSGFFMKIYILMSVLSKGYLAISAAIVVMSSFSVYMYIKNTFKYMTLNILSPSYMNFKLNFIGWIIIMNMASAIILYM | 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: 317
Sequence Mass (Da): 35982
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A0A662HTM9 | MKIGLIAKADKDTLDIVLRTLRLLERRDIEVLLEHKLAEALDERGYDMDFIDQNSDTFIIIGGDGTLLRTIFRLKTVAEKPVVGIRTRESLGFLMSIYDLNKLEHYLGMFLEGSYSIQRIARLRVKFRNTDINFLNDLIVQSSLPHKLLYLSVKDVDTNEIILNGGMDGVLIATTIGSTAHSLSLGGPVLDPRLVAFILHPIAPLSPLNRITILPSDFKICLDSFSSDVKLIGDGFYIAEIGKEESIEISKGKDIKMVKFKNEFYRKLRARLVWMG | Function: Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP.
Catalytic Activity: ATP + NAD(+) = ADP + H(+) + NADP(+)
EC: 2.7.1.23
Subcellular Location: Cytoplasm
Sequence Length: 276
Sequence Mass (Da): 31154
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A0A454XR39 | MATQLVIYVKRVAILTLLWISCLLLLNVVDVPITGIQHFITYAPVYGVFLLGLHAALSVLLGVANFNDCSDARKELLEEIKEARADLTKRKVL | Pathway: Protein modification; protein glycosylation.
Function: Stabilizer subunit of the dolichol-phosphate mannose (DPM) synthase complex; tethers catalytic subunit to the ER.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 93
Sequence Mass (Da): 10336
Location Topology: Multi-pass membrane protein
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A0A2A6CYT2 | MAPPSMFTLPFLAKKDAPISVGTLKQGYEEVIRAMRENFVHGWEPEGCNFAAYVDGELVVDLWGGYADKSCGRLWDAETLATFFSCSKALTAITMAMQADRGQLRYSDTIEKYWPEFGQNGKETITILNALQHQAGLQYLREDDGNAAVLDHDTLTDLKAMDRWVEKQSPIFPPGEISIYHALSFGWILDGLMRRADEKGRTVGEFLKEEIVDKLGIQDVYIGGTQEVEYRIARIRSHTRSNRMVIMEWMCDVAAITTTAPIYYWPKSIFRKEIKNVNGAKDFKLANHPATRKVGQPAANGVGNARNLAKVLDVFESGKLCSREMLDKLRVPQIVGKFDPVLGARVHKGYGFCYSKSPLGDWQYGHLGVGGQNLRTDTKRRITFAYITNGMKAGQGEHTRTMKRLEAALIPSLFRLPFVDRSHIPITIGTLKEGKTSNTDMNLKDAILQLTLTVNLHADKSCDWRWDESTVATLSAISVAMLVDRGQLQYTDTIAQYWPEFVCEGKDVITVQQDLQHEGGLPYFRNKDETVASYGMDVLSDMSEMDKLVETQKLHFPPGLCDIRIGDTRDIEYRLARIQSHLRNNLMATLEYFCNPIKLTKCKKVTAINYYRKSSPVRRALININGARDFEVFNHPGFRSQPAVNGIGRARDLAKVLDLFEGGNLCSMTLLDKFRLPTIFNQMDPLFGVELSKGHGFFYTRSPLGDWQYGHPGVGGQFVKTDTKRRITFTYLTNGMKASCNKWALRNRLSRQQTAETHPKSEGERIAAARRHIAQLSAAPSECPSAGGAAAKGCPVDHTGINPLNNELEHPNQKPAPDQPFPLQTKREKSTIPKAEAPGETWTYPSPQMFWNAMLKKGWRWEEDRLSDKDMENIIKIHNANNEEAWREVLKWENLLHPECDTPKLRSFKGDAKNISPRARFRSLLGYDLPFDRHDWIVDRCGARDVQYVIDYYDGGAVDPRSKLFTHLDVRPAMNHPGNMWDRVVVAYWRFKFEYLGMVPNLPHPPIEAEAKQ | Catalytic Activity: holo-[cytochrome c] = apo-[cytochrome c] + heme b
EC: 4.4.1.17
Subcellular Location: Membrane
Sequence Length: 1013
Sequence Mass (Da): 114789
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C3ZLP7 | MASLVLRGAVRLSSGARMGLLRPSCAARETVSTPRGCSRGLASGATEKVTHTGQVYEEKDYRKVRFIDAKKEVNPHFAIDLVAEEPPIEVASSTACCDGGGGALGHPKVYINLDQEGPHPCGYCGLRFVKKH | 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: 132
Sequence Mass (Da): 14110
Location Topology: Peripheral membrane protein
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J7EYT0 | TLYLIFGAFSGVLGGCMSALIRMELAQPGNHFFLGNHQVYNVLITAHAFIMIFFMVMPVMIGGFGNWLVPIMIGSPDMAFPRLNNISFWLLPPSLCLLLASAVVEVGVGTGWTVYPPLSSIQSHSGAAVDLAIFSLHIAGASSILGAINFITTIFNMRNSGQSMYRMPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLF | 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: 221
Sequence Mass (Da): 23942
Location Topology: Multi-pass membrane protein
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A0A8H2PGT7 | MTWVLHVDLDQFLASVELRRHPELVGQPVIVGGSGDPTEPRKVVTCASYEAREFGVHAGMPLRSAARKCPDAVFLPSDAPAYDEASEQVMCLLRDLGHPVEVWGWDEAYVGAAVADPFALAEKIRAVIAAETGLSCSVGISDNKQRAKVATGFGKPAGVFALTAENWMTVMGDRPVDALWGVGPKTAKKLAELDITTVAELARTDAELLTSTFGPTTGLWILLLAKGGGDSNVTAEPWVPRSRSHVVTFPADLTDVAEMDAAVRDLARQTLDEIVEQGRIVTRVAVTLRTKTFFTRTKIRKLPVAGTDLETITRTAIDLLHDFELDRPVRLLGVRLELEMPQPKPVDSGPPQKPVDSAPPQKPVDSAPPKC | Cofactor: Binds 2 magnesium ions per subunit.
Function: Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII.
EC: 2.7.7.7
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Subcellular Location: Cytoplasm
Sequence Length: 371
Sequence Mass (Da): 40079
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T1SQK7 | SFFGDDHLYNVVVTAHALVMIFFMVMPVLIGGFGNWLVPLMLGAPDMAFPRMNNLSFWLLPPSVILLVLSSMVEMGVGAGWTIYPPLSSSIGHFGVSMDMAIFSLHLAGVSSIMGAINFISTIINMRMEGLSMDSVSLFVWSVLITAILLLLSLPVLAGAITM | 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: 163
Sequence Mass (Da): 17568
Location Topology: Multi-pass membrane protein
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G3FID0 | GSLIGDDQIYNVVVTAHAFIMIFFMVMPILIGGFGNWLVPLMLGAADMAFPRMNNMSFWFLLPALVMLLSSSLVESGAGTGWTVYPPLSSNIAHAGSSVDFAIFSLHLAGVSSILGAVNFISTLGNLRTFGMILDRMPLFAWSVLIPAVLLLLSLPVLAGAITMLLTDRNLNSSFYDASGGG | 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: 182
Sequence Mass (Da): 19347
Location Topology: Multi-pass membrane protein
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A0A5P2XMV6 | MTTTPWHPREPSPTRPAHAPPWVSSVLYTAVLFAGVYYDLVGDEPQPPVRAAGFVAALGALFALDAAERWRHRRSGASRALAVGVLVARVGLFAAVASCDSAGLSRALFVLVPFTAYFALGRRASLVLGAGCAGALLGRYAVTADGWYTDAEAISDLLMFALVLTLTVSMAAVATGEQDARWRLESTVRELSASHRRLRAYAARVAELSTAEERNRLAREIHDSIGHHLTAIAVQVEKAEAFRDLDRAESDRALAAARWSARRALEEARRSVRALRDEPEPFSLSGALWDLVRHAAGGGGPHLTLDVTGEESAYGDVQLTALYRAAQEALTNARRHADAAHVHLGVEYGPAEARLTVTDDGRGLPASAAARTVPGVGLRGLRERLQPLGGELRVRGTPGGGTTFTATVPRVPSAAEAVPEPGPGTADIPDPPAPTGRT | Function: Member of the two-component regulatory system NreB/NreC involved in the control of dissimilatory nitrate/nitrite reduction in response to oxygen. NreB functions as a direct oxygen sensor histidine kinase which is autophosphorylated, in the absence of oxygen, probably at the conserved histidine residue, and transfers its phosphate group probably to a conserved aspartate residue of NreC. NreB/NreC activates the expression of the nitrate (narGHJI) and nitrite (nir) reductase operons, as well as the putative nitrate transporter gene narT.
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Cytoplasm
Sequence Length: 438
Sequence Mass (Da): 46405
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A0A497GSS4 | MAIAPEENEVLLATKDVVKLVRRPLGMLLSEDPKTTPHMVKSIIELFSPPLLITVGDFVSQLLERQDIVADVMILDGRIMRRKSYHSLEEGSRRIIVTANPPSCITYNSWKAVEKAISSPPSLLKVQGEEDLLTLAAIYISPLNSFIIYGQPREGMVLVIANEEKKLYIARIIASMERRRLNEPD | Pathway: Cofactor biosynthesis; coenzyme A biosynthesis.
Function: Catalyzes the GTP-dependent phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A (CoA).
EC: 2.7.1.237
Catalytic Activity: 3'-dephospho-CoA + GTP = CoA + GDP + H(+)
Sequence Length: 185
Sequence Mass (Da): 20809
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A0A2A6D382 | MTVTYSLDVANSSFFSLYRLLFRWKGSIWKYVISDLIIWCVFYSILSASYRFGMNPRNREIFEDYIPMTFMLGFYVSTVFTRWWDIFSNVGWIDTPALLVAACITGTDESTRILRRNLIRYLVLTQALVFRDVSACVKKRFPTMNHLVTAGLMTCREKEEFDKIDSPHIKYWQPMHWVFSLLKEAKAHGRISDIVFIDMLEKMRQFRVNVLNLTLYDWVSVPLGYTQVVHVAVRSYFAVALFGRQYLSTTRDIPMSKTIDLIIPIMTILQYMFFIGWMKVAEVLLNPLGEDDDDFECNYILDRNLQVRSPFYSNQLNIFLVGFAIVDEAYTNVPPQEKDSFWDVRIPQPLYTSESAIRPVNPIVGSCANLETNFDDEEKEAVMVLPRRTSTNSRMLEWDCTSEIIVPVLRDRRGSVMSIDSASMGASMRPNSKIRDIFRRMNGRNKWNASVSSRQRASRSNSNVSSYPSMSRQDSIISMTPSVISIEVQTEDKGEERMERGVEKGVDTMSPSWKGDDHLPVIMEDDERNTRWRGSIISRNSTSSQETARKETKDHLTIREEE | Function: Forms chloride channels.
Subcellular Location: Cell membrane
Sequence Length: 562
Sequence Mass (Da): 65171
Location Topology: Multi-pass membrane protein
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A0A2A6CYN2 | MAQSVPPGDIATQPGTKIVFNAPYDDKHTYHIKVTNSSARRIGWAFKTTNMKRLGVDPAAGVLDPKENALIAVSCDAFAYGQEDTNNDRVTIEWTNTPDGAAKQFRREWFQGDGMAQVASCLSLARGTMAPKKFKEPSIFRSADMSLCQLFLQTDAAYQCVTELGEIGMVQFRDLNEEMNTYQRKFVNEVRRCDEMDRKLRFIEEEIVKDNVFITETTDPIRAPQPKDMNDLEARNIHPHEFVATFEKIEEELLEINKNTKGLKDSHVQLWEMNQVIEKVKMMLDAGHNRHHASSVIQEAAHHPGLFDDEGKERGGTELKLVTGVIRRDRVRAFEQFLWRMCKGKVFMRTHDCDGEHDLFDGLEEKSVFILFFSGDQLAQRVNKICLGFHARLYDCPEEPHLRLSMHKQIDERLADLNNVIEKTLEHRKRVITAASNSVYAWKIKVLKIKMVFHTLNMFSIDVTQKCLIAECWIPTNDLDDVRVALRQGTIAAGSLVHPVLNEMEHHETPPTHFTLNKFTQGYQNIVNAYGMADYKELNPAPWCIISFPFLFGVMFGDVGHALIMFSFALMFIIFEKKLEAMKIKDEIFNTFYSGRYIVLLMSMFSFYTGFIYNDIYSKSINIIGSSWATGANNNSCWEWQGLKDSTTGLDYRDWEKTAAKNNQTFEIMLDPIYCYDKETGPYIFGLDPVWNLASNKLTFTNTMKMKSAVILGIMQMTFGLFVSLGNHIYNGSLVDVFFMFIPQMLFLGCIFIYLCVQILVKWIFFPVDAAWVFGRFYPGSNCAPNLLIGLINMFMMTPRTDGFGEFKNTSAPYNIGDDVNLLDFDNDPNCGLAFWYPGESIAEKVLLVVAVVSIPLMLLVKPFYIKWRSVTHL | Function: Essential component of the vacuolar proton pump (V-ATPase), a multimeric enzyme that catalyzes the translocation of protons across the membranes. Required for assembly and activity of the V-ATPase.
Subcellular Location: Membrane
Sequence Length: 874
Sequence Mass (Da): 100009
Location Topology: Multi-pass membrane protein
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A0A183LVA1 | VIVDNSIGEDKLEYWLVTEYHPLGSVYDYLHAYDIQWIDLLKICTGIAQGLAHLHMEIPNLSKPSIAHRDLNSRNVLLKSDLTACIADFGLAIRFEAGQCMRDAHLQLGTRRYMAPEVLDGAIQFSKDAFLRIDIYAMGLVFWELMMRCCCGSSKNAIIHITSYLAPYEIELGPQPSMEALQRWVAHAKQRPKFNPQWASDGGLCTLWETIEECWDQDAEARLSAGCVTKRLTTLLRLSVINQQYNDSYITNSNNNDSNGINEKDNNNDNNTVMSNYLTNSQKTDCNPPPPYYYCYYSPCITTSTTTIATVTTTTLMDVPKDLCNGRYTTTSLMNYSRKEDIGVYNCSDVLSTTTTITDNINNGNNDKSNTILTRGNTGCPPTICLPYSMNINFSTLTDHRSNKINSEILQCKRKNQTLCFNDILNRTENQIQCDSTEYLKPIQPNQQSKTIVNEEQSTEYQKLLSSVTNMK | Catalytic Activity: ATP + L-threonyl-[receptor-protein] = ADP + H(+) + O-phospho-L-threonyl-[receptor-protein]
EC: 2.7.11.30
Subcellular Location: Membrane
Sequence Length: 472
Sequence Mass (Da): 53422
Location Topology: Single-pass type I membrane protein
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A0A811LNM8 | MKVTFLHPDFGVGGAERLVLDAAIAFDQNGHQIEIVTNQFSETHCFSDALKFKDSIIVTAQWVPRTLFNKFYALFAYLRLCIAALYVIFDATADVVFIDQISLPLFLFKLAGFFYRPKLVFYCHFPDQKLTKREGSLKKAYRYFIDGLENKTLALADKIYVNSLFTKNVCKETFPSVDPSRFDVLYPSVNTDFLDKSTDGHLDVEDKYEFVFVSLNRFEGKKNHLLALNVFERLKHRIPAEKFDKCLLVFAGGYDPLNGENKVIYNELAEKTDKFGLNDNVKFLKSPSDDVKIELLKRATLLFYTPENEHFGIVPLESMWLETPVLALRSGGPIETVEDTKTGILVDPEADEDSFAHVFVKAVEDSKSFQQMGKAGRTRVQDYFSFDAFTRKLLDTAL | Pathway: Protein modification; protein glycosylation.
Function: Mannosylates Man(2)GlcNAc(2)-dolichol diphosphate and Man(1)GlcNAc(2)-dolichol diphosphate to form Man(3)GlcNAc(2)-dolichol diphosphate.
Catalytic Activity: alpha-D-Man-(1->3)-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + GDP-alpha-D-mannose = alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + GDP + H(+)
EC: 2.4.1.132
Subcellular Location: Membrane
Sequence Length: 398
Sequence Mass (Da): 45453
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A0A427AXP6 | MEGGAGGCNQRSPEEVFRDFRGRRAGIVKALTTDVEKFYRQCDPGKVSRSWFRPLTSAYIMELDGSAPAPFIYLVVSLKSKGRSE | Function: Histone-binding component that specifically recognizes H3 tails trimethylated on 'Lys-4' (H3K4me3), which mark transcription start sites of virtually all active genes.
Subcellular Location: Nucleus
Sequence Length: 85
Domain: The PHD-type zinc finger mediates the binding to H3K4me3.
Sequence Mass (Da): 9476
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A0A811KUN1 | MRKSSPYQHIILGHNLTNWIAKTTFIDGLTFLLGETWTGGLERYIQIDIDDIFVGQIGTRLVKDDISELIEVQKRWRSYFVDQFSFTLGFSGAFFGRGTEEEVKGDEELLRQSHHFLWFPHMWKHNHAHEYSYDNLTLLMDLNKQFAHSNNLNVTLNYAVSPQHHGVYPIHEPLYKAWTKVWEVKVTSTEEYPHFQPASRRRGFTYNGISVLPRQTCGLYTHTMYFHALPNGFRKFKENIEGGTVFDDILFNKIKWIKPTEMVDKYMKAQKNFDLYYTDECGDKRHLQGLSYLKKCDNSTNLPNLIILGPQKTGTTALAEFLKVHPDVATNLNVAGSFEEPQFFGQKNYDNGLDWYRALYNESAKIIFEKSANYFDNSKVALQMSYLLPKAKFLVILKDPVDRAYSWYQHMLAHNDSIASKYSLEHILKNKNKPEMKRLVARMINPGKYAQHFHRWLEHFNMDQFIIVDGNELKQIPSAVMNQLIKDLRLRFMDYRRILKFNVKKGYYCVEYQSKKKCLGASKGRKYDKMSEEARKMLQEEFRESNQDLKRLLRHFRLKLPYFLL | Pathway: Glycan metabolism; heparan sulfate biosynthesis.
EC: 2.8.2.8
Subcellular Location: Membrane
Sequence Length: 565
Sequence Mass (Da): 66649
Location Topology: Single-pass type II membrane protein
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A0A444F193 | MTTSLSSDVPVGYFSWAEYDIMTPMQPKTEEALAAAFISNCGAQNFRLQALTMLEELGIKIDSYGGCHRNRDGNVDKVETLKRYKFSLAFENSNEEDYVTEKFFQSLVAGMPIKLLYF | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus
Sequence Length: 118
Sequence Mass (Da): 13385
Location Topology: Single-pass type II membrane protein
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A0A662J3E1 | MDSTLVFLVVGLLQGVLEWLPVSSEGVNTLVLASMGFDPRSLIPATIWLHLGTLLAAALYFRRDIVKLAKSVPRAFKSGDGGVELLAFIAVATIITCILGLPLYVAVKGLTLLEGSILMALVGCFLIVNGLIQKLAKERRVFREEVRLRDAILLGVVQSLSVIPGLSRSGLTVSTLLLCGYGASTSLKLSFIVSIPVVAVADAYLALSGEVASFTYPSLIGVLAAFVVGYATISLLMKLARRLRFWAFCIAIGALSFIPLILELLKQL | Function: Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP).
Catalytic Activity: di-trans,octa-cis-undecaprenyl diphosphate + H2O = di-trans,octa-cis-undecaprenyl phosphate + H(+) + phosphate
EC: 3.6.1.27
Subcellular Location: Cell membrane
Sequence Length: 268
Sequence Mass (Da): 28634
Location Topology: Multi-pass membrane protein
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I1H748 | MEPAARPSNATLLARLGEGAARFELVDGAAPDPAPPVWPRLHCFARIGSSLRGGWSAALNKVEHYGVQRVTGDGRCMFRALAKGMAKSRGIPLSAMEEVQDADDLRLAVKEVLCDNQTERQKYEEAIIAITVDESLKRYCQRIRRPDFWGGESELLVLSRLCRQPIIIYIPEHEYRGRGNGFIPIAEYGLEFTKNSKERKKRVPVRLLYSGRNHYDLLI | Function: Hydrolase that can remove conjugated ubiquitin from proteins and may therefore play an important regulatory role at the level of protein turnover by preventing degradation.
Catalytic Activity: Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).
EC: 3.4.19.12
Subcellular Location: Cytoplasm
Sequence Length: 219
Sequence Mass (Da): 24708
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A0A0R3PUC1 | MVLEKGWWLRNVGLKLPTMFLFNLIATIVLWMIGEANLAYLTIAFDISDTNGGADEEKSQKLSYRSVIDGSRPAQRTAVANGLIFDFITVCNRPYYGLMCAQYCAYAAGDHHICDSSGKKVCLPGWTGKDCTIATGDVSTTRIDDITTPSPTKSSSSKSTAARETRRQCRFFTVRSAPVDDIIHDYWISGQKTHAIIMDAELAQ | Function: Putative Notch ligand involved in the mediation of Notch signaling.
Subcellular Location: Membrane
Sequence Length: 204
Sequence Mass (Da): 22544
Location Topology: Single-pass type I membrane protein
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A0A6A4X2R0 | MLEDRQVLRDVWDGRLPVCFRLADNEVHTVSAPDPFYMLIPRMTYFPLVIDKVRRHFSQSVHPDHAKSDVWLEWGDMPLQWHYPVGLQFDLLATDSVLPWNLVVHFTDRPDQCPFMKREAMESFFFSTVKEADQLKHKGSAISSLGKRDHSQLWTGLAFDDARAIIHGIEPPMDTPLQWLSQHFSYADNFLHIVVFP | Function: Involved in autophagic vesicle formation.
Subcellular Location: Preautophagosomal structure membrane
Sequence Length: 197
Sequence Mass (Da): 22988
Location Topology: Peripheral membrane protein
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A0A2A6B4A8 | MGSLSSGLSIGVIYSLLLLISTEECSWIQKMTKRDVKMVVAGEGLHRNLIVSTQLESTERFIECRILYNLKVPKGMYVDSDSVNSSLPLHSLHSRHYFDVEAPEKDSKEVQVSIVSTKITRKQFIISDHFTLPIHIRYHSPDSIGQSTISPPRILIDCPADYGIHSLDKCHTATSKSVQSLAAKWVIVDPLSVSAPVTVSIPTGNRSMLPTVVTVTSSVVVLSLIFLARTLFFSK | Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Function: Essential component of glycosylphosphatidylinositol-mannosyltransferase 1 which transfers the first of the 4 mannoses in the GPI-anchor precursors during GPI-anchor biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 235
Sequence Mass (Da): 25968
Location Topology: Single-pass membrane protein
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A0A7R9MYT7 | MIIGFDDTDSKTMGMCTTYLGALMLEEIPLPPDEITPYLLRLNPNVRFKTRGNAAVSLKLAPREDYTDDLWKICCELLEEFAVFDDENTNPGIVFLSEEEAAGMHRELERFSLRAVRDFITIDETKDFLKRHKIKHRGYKNGRGLIGALAAAGFALNGLSDWTYELVAYRKPENWGRRRSLNEETVWAADRASYPFTWDTVDHQNKKIVFSPHGPDPVLFGIRGSDQKRIMDAFRIIRSEPIDRYLIYTTNQGTDMHITEARINDAREGRSYKIRGRVTAPPRTIHGGHVIFTIEDESGEVDCAAYEPTKNFREVVRRLAPGDTVTVYGALKNQTINLEKIQIERLIPRRVLRNPLCGCGKRMKSVGKNQGYRCKRCGTRSDSPEIVEVDPGIRVGVYETPPVARRHLAKPLIRCNEGKVKTYPSR | Function: ATP-dependent agmatine transferase that catalyzes the formation of 2-agmatinylcytidine (agm2C) at the wobble position (C34) of tRNA(Ile2), converting the codon specificity from AUG to AUA.
Catalytic Activity: agmatine + ATP + cytidine(34) in tRNA(Ile2) + H2O = 2-agmatinylcytidine(34) in tRNA(Ile2) + AMP + 2 H(+) + 2 phosphate
EC: 6.3.4.22
Subcellular Location: Cytoplasm
Sequence Length: 426
Sequence Mass (Da): 48562
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I1I0V5 | MRWTAFVWDGATRAMKHRPTFTNLVLVLAASSGGGLVAYADSQSDGVVDMPQGPKKKKVVVLGTGWGGTTFLRNLDSKLYDVQVISPRNYFAFTPLLPSVTCGTVEPRSVVEPIRRILEKKGGDFKFWEAECFKIDPANKKIHCRSNAGTNLDGNGEFLVDYDYLVVAVGARSNTFNTPGVEENCHFLKEVEDAQKIRRSVMNCFEKASLPYLNEEEKKKNLHFVIVGGGPTGVEFAAELHDFVTEDLSKLYPSIQHLVKISLIEAADHILTMFDKRITNFAEDKFGRNGIDVKTGYKVVKVSKDAITMQNPATGDIAVPYGMAVWSTGIGTRPFIVDFMKQIGQANRRVLATDEWLRVRECDDIYAVGDCATINQRRVMEDIAEIFRVADKDKSGTLTVKEIQDILEDIYVRYPQVKLYMKSKQMNGIADLISTGEGDTKKENVELNIEEFKKALSLVDSQVKNLPATAQVAAQQGQYLARCFNKMPDAEENPEGPIRIRGEGRHRFRPFRYRHLGQFAPLGGEQTAAQLPGDWISIGHSSQWLWYSVYATKQISWRTRALVISDWGRRFIFGRDSSCI | Catalytic Activity: a quinone + H(+) + NADH = a quinol + NAD(+)
EC: 1.6.5.9
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 580
Sequence Mass (Da): 65137
Location Topology: Peripheral membrane protein
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A0A482P1C6 | VKEFAEFPTLEQLPLWGFDGSSTMQAEGHSSDCVLKPVAVYPDPTRTNGVLVMCEVMMPDGVTPHASNKRATILDDEGAWFGFEQEYFFYKDGRPLGFPETGYPAPQGPYYTGVGYKNVGDVARQIVEEHLDLCLAAGINHEGINAEVAKGQWEFQIFGKGSKKAADQMWIARYLLLRLTEKYRIDIEFHCKPLGDTDWNGSGMHANFSTAYMREVGG | Function: Catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia.
EC: 6.3.1.2
Catalytic Activity: ATP + L-glutamate + NH4(+) = ADP + H(+) + L-glutamine + phosphate
Sequence Length: 218
Sequence Mass (Da): 24314
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W8BAF1 | MALVNYDSSCSSDEQEETNLETFEAPKSKMPKLSETAEDKKALPCAVSLLGAKNTGDVVHNAHADDPTEHDGRVRSFKHERGNWATYVYIKAMSDQLEDMQEVSQGALAGVVDCLHAIEDLHISLSRTVVLQYHHIDSFVESLRTTLEVSGSFSISLRRLHIYTNAERTRTFIALKVDDMYFEKVHQLMAKVDGVMKEYRLQLFYEEPSFHISFMWCLGDKVAVLNEHLDTLKSAINVVLGDSEAISLFIHEINCKSGNKEFVFKLK | Function: Phosphodiesterase responsible for the U6 snRNA 3' end processing. Acts as an exoribonuclease (RNase) responsible for trimming the poly(U) tract of the last nucleotides in the pre-U6 snRNA molecule, leading to the formation of mature U6 snRNA.
Catalytic Activity: a 3'-end uridylyl-uridine-RNA = a 3'-end 2',3'-cyclophospho-uridine-RNA + uridine
EC: 3.1.4.-
Subcellular Location: Nucleus
Sequence Length: 267
Sequence Mass (Da): 30220
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A0A811LD03 | MRISQLCSSRIGILMLLLVQMFEQTHALSILTFNFSNQFRSNHCKARNCRTKICVKQYQHKFTPNEYCIFGGHTVDWTWVEEGDSHVTKIPINNTRNSVTVIIETFLFNITTLKPLEKDENGNSLVDLQVWKGTLPSKYAHIDTKKDLTFKSECALDYYGEDCWTHCQIQDFDKRIGEFECNSKGEKVCKAGFYGQKCDRATACSSDCLNGYCNKNGECMCNIGYQGENCDRCKPSKGCANGYCERPNECKCFPGYSGINCTFLSSVCEAKRPCLNGGKCKNMDRGSYRCDCPPGFIGTQCEKKINSCNDSPCQNGGKCVQPFGHPLSCKCPEGTFGQYCQVKSQSCDDLPCQNGAQCFQIRGKVHCACSQGYRGDICDQKVLACTESSCGNGGECVENPLKPGGIECKCPTGFFGSHCEMVVHDCRSSPCLNQGKCVKNETGYNCQCKSGFTGGYCEIVIRQMEVEHKAYVFFSIPIIIITIIVITAFIALLLFVKKNLNMPAFLEQIQRESPAPPPYSEASIVGTKLLVRSMSNTEELKELRADELGKGDKSRRKRSPSNDYSSEPTEVDSLYNHKS | Function: Putative Notch ligand involved in the mediation of Notch signaling.
Subcellular Location: Membrane
Sequence Length: 579
Sequence Mass (Da): 64548
Location Topology: Single-pass type I membrane protein
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A0A2V7WQ73 | MLFIRALRRGPTSEKQSSFSPGPIPESRGRHASPMIKAPDVTLLYVMFAFVASYVLLKRFLFGPLGAILAEREREEREASQIHQESLKELERTIAEAERRLAEARRDALRTREGLRAEGLAKFETELARAKQSAATFIGSATGEIGSEVQKAAAEIPTRARTLAVQLAEKILGRKLAA | 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: 178
Sequence Mass (Da): 19673
Location Topology: Single-pass membrane protein
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A0A2V8FCD8 | MECNSYLEPSVSRPNSLPTSPGRSTIGSPPAANLRHSTVPPPPLVAIASSYGGPVRSASGAKGGQSPVGYCVAVRLLVATTNQNKVREIRQILDGLPVEVATLDEWPGLEAPEETGCTFEENARAKALYYAAATGELTVAEDSGLAIDALDGMPGVESARFGGANTSYPDKFALIYEALRAKGSLESSARFVCALVLAKGDRVLFETRGIVEGRIAREPQGDGGFGYDPIFFYPPYGLTLAEAGDLKAAVSHRGKAFRALGAFLRSQR | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions.
EC: 3.6.1.66
Catalytic Activity: H2O + ITP = diphosphate + H(+) + IMP
Sequence Length: 268
Sequence Mass (Da): 28250
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A0A0K6BST5 | MRYDIAIIGGGPAGYTAAERAGANGLRAVLFEKKAMGGVCLNEGCIPTKALLYSAKVLDGIKSAPKYGVSVEGAPAFDMEKIIGRKNKTVQKLTGGVRMTVNSYGVTIVDKEAVIEGEGEEGFHIRCDGEVYEATYLLVCTGSDTVIPPIKGLSDVDYWTSREALDSTVLPSSLAIIGGGVIGMEFASFFNSMGVRVKVIEMMPEILGAMDKETSAMLRADYTKKGVNFYLNTKVTEVSDKGVTVEKDGKSSFIDADRILVSVGRKANITQVGLDKLNIELHRNGVVVDEHMLTSHPRVYACGDITGFSLLAHTAIREAEVAINHILGIDDRMDYDCVPGVVYTNPELAGVGKTEEELIAKGIYYRIQKLPMVYSGRFVAENELGNGLCKLIIDHNDRIVGCHMLGNPASEIIVVAGIAIQRGYTVDEFRKSVFPHPTVGEIYHETLFA | Cofactor: Binds 1 FAD per subunit.
EC: 1.8.1.4
Catalytic Activity: (R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + NAD(+) = (R)-N(6)-lipoyl-L-lysyl-[protein] + H(+) + NADH
Sequence Length: 449
Sequence Mass (Da): 48601
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A0A1D6YDB8 | VGTALSILIRSELGQPGALLGDDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMTQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYL | 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: 204
Sequence Mass (Da): 21709
Location Topology: Multi-pass membrane protein
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H9T9D2 | TLYLIFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLTSSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGISSILGAINFITTIINMKPPATTQYQTPLFVWAVLVTAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHL | 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: Membrane
Sequence Length: 218
Sequence Mass (Da): 23223
Location Topology: Multi-pass membrane protein
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A0A0H5BCW1 | MSLILPPLAVFDLDGTLVDTLPDLIDVLADTLNELGLPPLSVEEGRRLVGAGIKPLIVRALAELGRDTAADELERIYADYIDAYSARIARLSRPYPGMEAALDRLAGQGFRFAVCTNKVTALAVQLLTELKLIDRFAAVAGCDRFAMRKPDAGHLWGTIADAGGDPTRTVMVGDSRTDVATARNAALPVVAVSFGYSDVPPEDLGADRLIDHFDSLPQAIGELLGSAGHGR | Pathway: Organic acid metabolism; glycolate biosynthesis; glycolate from 2-phosphoglycolate: step 1/1.
Function: Specifically catalyzes the dephosphorylation of 2-phosphoglycolate. Is involved in the dissimilation of the intracellular 2-phosphoglycolate formed during the DNA repair of 3'-phosphoglycolate ends, a major class of DNA lesions induced by oxidative stress.
EC: 3.1.3.18
Catalytic Activity: 2-phosphoglycolate + H2O = glycolate + phosphate
Sequence Length: 231
Sequence Mass (Da): 24562
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A0A1B9P5A1 | MTKKSLFAGLLLIISQIFSPAIHAEEEVAPQMGYFTLAPDLTTNFVTTGKKLGYIQIRVDILVADNRDLPQLERHNPQIRNALVEVLGQQPEQRIKSLAGREEIRKECLTAINELLLAETGKTLAVDLLFTKYIYQ | Function: Controls the rotational direction of flagella during chemotaxis.
Subcellular Location: Cell inner membrane
Sequence Length: 136
Sequence Mass (Da): 15323
Location Topology: Single-pass membrane protein
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A0A2G6Q595 | MTSPSLHGRRILMTRQHRSRCSLTDRLQASGAEVYSLPCIERRVLINREERQRYLRKLADFDWLVFTSPFAVQVFFGNERVRLPDTLKVAVVGPATAEALVPYGVPSDLMPRVYKAHNLVSEMRPLTGKRVCVPRSKRGNPAFISQLEAAGAVVTEIWTYDTWSLTPDSFLLTSLMKEVDTIVFMSGSAVKGFESGIFPCFQNKGCFGFPPGPDVPPEMFAKIKLVCIGPSTAAVCERLLKRVDAVADPHTEEGIFQTLIQMQYSGAKT | Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 3/4.
Function: Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III.
EC: 4.2.1.75
Catalytic Activity: hydroxymethylbilane = H2O + uroporphyrinogen III
Sequence Length: 269
Sequence Mass (Da): 29974
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A0A3D3FGS7 | MDRLIEAIRTKKNPTVAGLDPKLSYIPSFLRKAAYAKYGKTLEGAAEAILQFNHGLIDALAAIVPAVKPQCAYYEQFGWQGMRTLEATIRYAQQKGLYVIIDGKRNDIGTTMEAYAKAHLGTTEVEETQIPVFDGDALTVNPYLGSDGIQPLLPICKERDKSIFALVKTSNPSSGELQDRTFADGKTLYVTIGSLCEDWGKESRGQYGYSRVGAVVGATYPAQLGELRK | Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2.
EC: 4.1.1.23
Catalytic Activity: H(+) + orotidine 5'-phosphate = CO2 + UMP
Sequence Length: 229
Sequence Mass (Da): 25091
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A0A5M3YS32 | MRLSRSKWELLDAKGQEAMRKVCRLAREVLDITAAAVKPGVTTDYLDEVCHNACIERESYPSPLNYSHFPKSICTSANEVVCHGIPDQRVLLDGDILNLDVSLYHGGYHADLNETYYVGDKAKADPDSVRLVETTRQALDMAIEIVKPGVPIREFGKIIEKHAASRGLVVIKKWGGHGINSEFHPPPWIPHYAKNKAVGTCKPGMTFTIEPILTLGANREKYWPDDWTNVTVDGKRTAQFEHTLLVTETGVEVLTARLENSPGGPIPIPEVANGDANGKGEE | Cofactor: Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with cobalt, zinc, manganese or divalent iron ions. Most likely, methionine aminopeptidases function as mononuclear Fe(2+)-metalloproteases under physiological conditions, and the catalytically relevant metal-binding site has been assigned to the histidine-containing high-affinity site.
Function: Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val).
EC: 3.4.11.18
Catalytic Activity: Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.
Sequence Length: 282
Sequence Mass (Da): 31120
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A0A173GG83 | SLLGDDQIYNVIVTAHAFVMIFFMVMPILIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTTINMKPPAISQYQTPLFVWAVLVTAVLLLLSLPVLAAGITMLITDRNLNTSFFDPAGGGDPILYQHLFWF | 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: Membrane
Sequence Length: 192
Sequence Mass (Da): 20611
Location Topology: Multi-pass membrane protein
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A0A6H5GGX0 | MFWLMFISVLFAAIQLANTECQTRSIYCYECDSWKDPRCKDPFNYTALPRDQPPLMPCNGCCVKMVRNSKTQYESVRRTCTSQLQINLFMVDHVCMLESSGTGHMCFCEEDMCNSAHWGARPSVLFLLAPFASLFHR | Function: Required for homeostatic regulation of sleep under normal conditions and after sleep deprivation. Important regulator of the Sh K(+) channel, acting as a signaling molecule that connects sleep drive to lowered membrane excitability, possibly by enhancing K(+) channel activity and thus reducing neuronal excitability.
Subcellular Location: Cell membrane
Sequence Length: 137
Sequence Mass (Da): 15814
Location Topology: Lipid-anchor
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A0A7Y2XMZ8 | MSRQDPLTGVEKSGHFYHRGKDTTRLEAFVDAAFAFALTLLVVSFDAVPQSFDELMIALRAVPAFLFAFCILAMFWIAHRNWSIRFGLDTTFSTLISLALIFVLLVYVYPLRAMATAAMSALTNGWLPSEFYIDTVSKVRGLFAIYGIGFFVSCLCLVSLNWHALRRASSLALTPQERLLTIYEVLAWSIVGSFGLVSLILAMTLPDRLVGLAGWSYMAMAVVMPTFGLVTARQFSARFPDTSPGRN | Catalytic Activity: K(+)(in) = K(+)(out)
Subcellular Location: Membrane
Sequence Length: 247
Sequence Mass (Da): 27405
Location Topology: Multi-pass membrane protein
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A0A7S2WQ11 | TIFHTLVKAKMLYGTSAVTEGSLGTIGVVVEDQQGGNQGFGECGRVDLHKKRNCCCMCCFNCTQPGNIGEMMVIYGTPTGNSLSRTCIIGPDWVCTAIAMALFIGPGVVWVKLVAFKLHVVMGFFGALILVVTVVSFALTSFSDPGMVLKQPVLKENSSTDGLLACTRCNIYRKPGTIHCSECDICIEGLDHHCPWTGKCIGRKNILYFRVFLGMVCVFLIAVVASVIVYGSVEM | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 235
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 25365
Location Topology: Multi-pass membrane protein
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F0URT1 | MPFSHHSHSGQFCEGHAKNSLEDIIRTAIGNRMRVFALSEHMPRMAQDFYPEEIEANATEASLIENESAYFKESQRLREKYISEINIPIGFECDWIRPSSLTWIQNSLARFPFDFFVGSVHHVHTIPIDYDTLLYQKARGIAGGTDERLFEDYFDAQLAMLKALNPPVVGHFDLIRLKSDDPERSFQQWPAVWEKILRNLDYVAEYGGILELNSASLRKGMTEPYPKAEICKEFLARNGRFCMSDDSHGIDQVALNYNRMLEFIEQVGISTLHYLEYCSELPSSSNSFDRRFPHTGLRSVSLADLKQLAFWS | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 8/9.
EC: 3.1.3.15
Catalytic Activity: H2O + L-histidinol phosphate = L-histidinol + phosphate
Sequence Length: 312
Sequence Mass (Da): 35947
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A0A0M0VJ23 | MTENATSTDMNTPATSLTDKERELIAQMPYEEARDKLIQAVQALETGGLNLDQSMRQWEIGEALAKRAQGLLNDVRAKLDQAQAEQAANEATAGTQSNLD | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
EC: 3.1.11.6
Subcellular Location: Cytoplasm
Sequence Length: 100
Sequence Mass (Da): 10906
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A0A2V9J994 | MTNRLARTALLGIACIGLAPFGDAVAARKEKVREEVAVIDTNLGKFAFRFFSQESPRTVEAFKKLVRAGFYNGTLVHGVLPGLLIQAGDPQTRQDNAEVAFVDVEALEIEKNDLRHLAGTVSMAHPRNDPTSRSEFFICLQEVTYFDGKYTVIGEVISGIKVVDAISQVPRNAKQSPLFPVRIRRISLETQEFLKEAK | 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: 198
Sequence Mass (Da): 21948
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A0A2V7UTU9 | MERYLDLLADWSARVNLTGARTPVERVALLVGEVLPAAPLARPGRLLDVGSGNGSPGLVLALLRPELQVTLLEPRRRRWAFLREACRAAGRADVEVRRERHDEYAGPPAATVTVRGLALSPAHLAALVEDDGRVLFFGSRRLPGAGWREEPAPPGIQSLRRLAVPRET | Function: Specifically methylates the N7 position of a guanine in 16S rRNA.
EC: 2.1.1.-
Subcellular Location: Cytoplasm
Sequence Length: 168
Sequence Mass (Da): 18345
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A0A2V9IKR8 | MPIAIANRYARALVDVVSQKGDYRQVRQELESFAAVYSESAELREVFDTPALPLTEKLKVLAAITGKMGTTSITTNFLSVLGQNYRMNLLEEICRAFHKLANDRLGVVEVKVVSAAGLSETERQALRARFIDLTGKEVEFDFRLDRELLGGVLAQIGSTVYDGSVRGQLDRIRERLTGQ | 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: 179
Sequence Mass (Da): 19923
Location Topology: Peripheral membrane protein
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A0A4S9ZGC8 | MAFHGRGDSGSAMESNSGLSIERINPYGISVYPTAIKDQDQQNTWQGDPSYATNRTVDDIGFVRALVTNISAQYCVDTSRVFAAGMSNGGGFVNVLACDPVMSSVFNAFAPHSGAFYTSTGDSNTVCFPNTVLTNDLVHTTCSPSRRVPMIEFHGDADGTIGYFGGGRRGYCLPAIPHWTQDWAIRNNLTSDNVTTVTNGGNLTRYEFGAASGYPGLVTHFRLAGLPGANLHIDCKHHWSYDHANYDHYHNNFFQCDNIEYRCTFRCLEFRQQSHRQLDYQRGYWYRVPSNRLYNNRHHLDFELFFVQHCSIRGKFVVQCFFKLTFQSFQSVFECFIGFVVILQSHIDGFEFIIKFGVKFLVSSIIELIIFVHRWLFLRKFAVEFCIKPVIECLVSFKFFVKSGLEFVVVVHTWLFFSKLPIEFCFEFVIKCLFGSVIYLEFLVIERECFVEPGLEFLVSRWFVFGKFTIKCCLELIFKCLISPFLYFKLISECFLESGISLIVGRRLFIVKLAFKHIFQFCFGPVFERFFGSVICHQLIILIFEPCIIVVKRCTNL | Catalytic Activity: feruloyl-polysaccharide + H2O = ferulate + polysaccharide.
EC: 3.1.1.73
Subcellular Location: Secreted
Sequence Length: 557
Sequence Mass (Da): 63930
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A0A0H5BBM8 | MHLRMFWSKIHRATITHADLHYEGSCTIDADLMDAARMLPNQELHVWNVTRGTRLVTYAIDGPRGSGVICINGAAAHGNQPGDLVILATFADMTAEEARGHCPTVVRVDGKNAIIDIRAEIAGPAEPAMPRLMS | PTM: Is synthesized initially as an inactive proenzyme, which is activated by self-cleavage at a specific serine bond to produce a beta-subunit with a hydroxyl group at its C-terminus and an alpha-subunit with a pyruvoyl group at its N-terminus.
Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; beta-alanine from L-aspartate: step 1/1.
Function: Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine.
EC: 4.1.1.11
Subcellular Location: Cytoplasm
Catalytic Activity: H(+) + L-aspartate = beta-alanine + CO2
Sequence Length: 134
Sequence Mass (Da): 14556
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A0A094ZUU6 | MFRCTQINGVNNAVKLFGLCSVCIWTLFIISKHIIHNQPELTQSMDKLEEIPKLSTDADSRNLPLIFIGGHQSSGTGLLRVLLDVHPMVRCGPEPVVTREILRLRPKNRDGQDWLSQSGITQSVLDNAIAGFIVSILKNMGPPADRLCHKDPSSYIYLRYLSELFPKAKFIHAVRDGRGAIMSTIIRRINPTYTSDNIPEALNQWTDYTSQMIKDCQHIGIHRCMTVRYECLVIKPKREIQKILNFLDLPWDEKLLNHEKYVNETSMINKYEASSVQFVKAIHKESLYAWSNSNSIIPRNLITTMHKNNSLLARLGYTSGNIPPDYEEVCEVDLKL | Function: Catalyzes the O-sulfation of tyrosine residues within acidic motifs of polypeptides, using 3'-phosphoadenylyl sulfate (PAPS) as cosubstrate.
EC: 2.8.2.20
Catalytic Activity: 3'-phosphoadenylyl sulfate + L-tyrosyl-[protein] = adenosine 3',5'-bisphosphate + H(+) + O-sulfo-L-tyrosine-[protein]
Sequence Length: 336
Sequence Mass (Da): 38349
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H3DNU2 | MALQELAISLSMLGVAGTVLICALPMWKVTAFIGTHLVVMQVFWEGLWMTCVSEYTGQMQCKLYDALLDLSPELQAARGLICISLVLGCLGFLIFLLGARCTNCLSHPRVKARLVQSSGAIYCLGALTTIVAVSWTANSIISDFNNPRVPEVLKRELGAAIYIGFVTSGLLFCGGAILCMSCPPQTARFSSRRYMLARTPPSSSYAFKNYV | 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: 211
Sequence Mass (Da): 22919
Location Topology: Multi-pass membrane protein
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A0A024RD60 | MQLVPDIEFKITYTRSPDGDGVGNSYIEDNDDDSKMADLLSYFQQQLTFQESVLKLCQPELESSQIHISVLPMEVLMYIFRWVVSSDLDLRSLEQLSLVCRGFYICARDPEIWRLACLKVWGRSCIKLVPYTSWREMFLERPRVRFDGVYISKTTYIRQGEQSLDGFYRAWHQVEYYRYNCSTLSEWKILSLHVLVKWTSVLCCF | Pathway: Protein modification; protein ubiquitination.
Function: Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins and plays a role in several biological processes such as cell cycle, cell proliferation, or maintenance of chromosome stability. Ubiquitinates mTORC1-bound TTI1 and TELO2 when they are phosphorylated by CK2 following growth factor deprivation, leading to their degradation. In contrast, does not mediate ubiquitination of TTI1 and TELO2 when they are part of the mTORC2 complex. As a consequence, mTORC1 is inactivated to restrain cell growth and protein translation, while mTORC2 is the activated due to the relief of feedback inhibition by mTORC1. Plays a role in maintaining epithelial cell survival by regulating the turn-over of chromatin modulator PRMT4 through ubiquitination and degradation by the proteasomal pathway. Regulates also PPARgamma stability by facilitating PPARgamma/PPARG ubiquitination and thereby plays a role in adipocyte differentiation.
Subcellular Location: Cytoplasm
Sequence Length: 205
Sequence Mass (Da): 24266
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A0A0W0TT65 | MSEFLRQKPLILASGSTNRRMLLESLGLSFEIHPPLCDEDALKDTFTGSNDKLAAFLACEKAREVSLRFPDAFVLAADQVCLHQDTVFNKPLTLENARLQLEKLSGHTHQLMNAVCLMSEGKVIWEHEETATLTMRALTSVAINAYLQADTPLQSCGSYHFESRGKWLFTHIEGHESTITGLPLLALANALLQHGVVSLP | 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 2'-deoxyribonucleoside 5'-triphosphate + H2O = a 2'-deoxyribonucleoside 5'-phosphate + diphosphate + H(+)
EC: 3.6.1.9
Subcellular Location: Cytoplasm
Sequence Length: 200
Sequence Mass (Da): 22128
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A0A3D0J6A6 | MGIWQKTVGVITGKRSLSPQELSELEELLILSDVGVEAGERLINAVRNGQSDQTAMERLKGEMLGILSLNSNFKFQISKYENKPQVWLIIGVNGSGKTTSIAKLAHYLKEQDRRVMLAAGDTYRAAAIEQLKKWADRLGVEFIGSKTGADPASVAYDAVESAAARKVSHLLIDTAGRLHTQKHLRDELGKIYSTIGKKLPGAPHLTLLVLDATTGQNAVSQAKLFSQAAKIDGIILTKLDGTAKGGIVLAIAMELKIPVFFTGVGEGLDDLLAFEPAAFVDSLLEG | Function: Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Acts as a receptor for the complex formed by the signal recognition particle (SRP) and the ribosome-nascent chain (RNC).
Subcellular Location: Cell membrane
Sequence Length: 286
Sequence Mass (Da): 30736
Location Topology: Peripheral membrane protein
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A0A6T2CGY9 | FFSHLLLWTIMAKVSAIILGALLGWVVGLLVAPAFVTTATSELYLSPTMSPTMASNAAHLAPTAQLDVPQQAVAGFYNHPAEATEMSTMGATKSSVSVGLDVDRSTAAGLPYSFGMLFLTVSSVLLGGGLVARFFRPSTDGSSDPLCVNSQHQQAANLAMMATYSVTLVTPDGEKVIECPDDQYILDVAEEQGIDLPYSCRTGSCSSCAAKILEGEVDQGDQAFLGPDQVEAGFFVPCQAFPKSDCKILTHQEDEIWSPGI | Cofactor: Binds 1 [2Fe-2S] cluster.
Function: Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
Subcellular Location: Plastid
Sequence Length: 261
Sequence Mass (Da): 27592
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A0A0H5BI44 | MIKPVVIIPLKSAAAALTRLSDRFDLRRRRGLQRAMAHDVVAAVRSLRPVPDVALLAEDPLSARRLAGRRGLVVEAALGAGLNLHLACAIPVLGVHRPGATALVLPADIPQVQPRDIVRLLKAVDEHDLVVVPDRHGRDANALAFRLDKPPAFAFGADSCLHHLENAERAGMTARVLELASFALDVDTAADLDLVLAGSGAPRTRAFVCGPNGGEEGSDDDGLEAAE | Pathway: Cofactor biosynthesis; coenzyme F420 biosynthesis.
Function: Guanylyltransferase that catalyzes the activation of (2R)-3-phosphoglycerate (3PG) as 3-[(R)-glyceryl]-diphospho-5'-guanosine, via the condensation of 3PG with GTP. It is involved in the biosynthesis of a derivative of the hydride carrier cofactor coenzyme F420, 3PG-F420.
EC: 2.7.7.106
Catalytic Activity: (2R)-3-phosphoglycerate + GTP + H(+) = 3-[(R)-glyceryl]-diphospho-5'-guanosine + diphosphate
Sequence Length: 227
Sequence Mass (Da): 23985
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A0A0C2WIF8 | MTEQKSWNAFTVEREDNIAQVTLIGPSKGNAMGPDFWSELPEIFADLDADPEVRAIVIAGSGKHFSFGLDLPAMSGEFGAVLADKAQAGPRTKFHDMIKRMQSGINAVADCRKPVVAAVQGWCIGGGVDLITAADIRYASADAKFSIREVKVAIVADMGSLARLPAIIGDGHLRELALTGKDIDAARAEKIGLVNDVFEDADAVLAAARATAKEIALNPPLVVHGIKDVLDHTRSASVNDSLRYVAAWNAAFLPSQDLTEAITAVFQKRPPVFQGE | Pathway: Lipid metabolism; fatty acid beta-oxidation.
Function: Could possibly oxidize fatty acids using specific components.
Catalytic Activity: a (3S)-3-hydroxyacyl-CoA = a (2E)-enoyl-CoA + H2O
Sequence Length: 276
Sequence Mass (Da): 29420
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A0A3B9E6A9 | MNTQKIIRCFIALELPLEIKIKLGDIIGQLKKTGADVKWVDPANIHLTLKFLGETPEADALRAGLALSTLKGKFKAIDSGLGGLGAFPSVDRPKVIWAGLSQGAEEIKEIYRQVEKLTADISQEDKAREFSPHLTLGRVRSNKNLMQLRDAINQAVILQKGFEFNRLVLLKSTLTSEGAIYSELNGVELV | 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: 190
Sequence Mass (Da): 20909
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A0A2V9P7T0 | MQPTIIVKQRVPGMSKRELTKFIADACRATRLRGMVTVMLTDNREIRALNLRFKGKDRATDVLSFPAPIFVRGFAGDIVISAEMAAKNARALGHSVSDEVRILVLHALLHLAGYDHDSDHGEMARREQLMRKRLQLPSGLIERSTSMSSERRRPKSNARSARART | 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: 165
Sequence Mass (Da): 18548
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A0A0H5BJQ3 | MELSARTGCRIATLGAAALILSACSLQERLASRVDPKYGVSASPKVVADGQPIPKGGGTFRTGKPYTIAGKTFVPLDKPQGFREEGVASWYGDDFHGRLTANGEVYDMHSVSAAHPTLPIPSFARVTNLSNRRSIVVRINDRGPFHGNRVIDLSVKTAQALDFHRNGVAKVRVEYVGPASLDGTDDKVLLATLRTDGQPAPSPSPVMVASAAPFVPPVSAYSSASMPPSASTRVAIRGSVPLPPDRPFDVGPSEHPLTSSGLRTSSRPMTTASTTAFAPIEASGANGAVATGRGLY | Function: Lytic transglycosylase with a strong preference for naked glycan strands that lack stem peptides.
EC: 4.2.2.-
Subcellular Location: Cell membrane
Sequence Length: 296
Sequence Mass (Da): 30931
Location Topology: Lipid-anchor
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A0A6V7XLA6 | MEKEAFLDFEAIDADNFSNFNTGAPCILGIDEAGRGPVLGPMVYGCAIVPADKMEDLKSLGVNDSKILSRSQREKVITKMEASEFVTYSLRIVHPRTISAQMQRRTRLSLNEISHNCIIGLIQHALKRIYFVDLVGVKEETFLHFLQSHFPSLKITVSKKADSIFPIVGAASIFAKVTRDRRVSNWILDGFTSPKEGIGSGYPSDPMTKCYISRTLDSLFGFSPLVRFSWRTIEKLLGNKAVKCFWNVQGTDDDPLKQRTLKEIWASNGADGKDKHEQHLKHKKGLVRHRFFAERGIANIDIIV | 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: Catalytic subunit of RNase HII, an endonuclease that specifically degrades the RNA of RNA:DNA hybrids. Participates in DNA replication, possibly by mediating the removal of lagging-strand Okazaki fragment RNA primers during DNA replication. Mediates the excision of single ribonucleotides from DNA:RNA duplexes.
EC: 3.1.26.4
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Length: 304
Sequence Mass (Da): 34215
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A0A2V9MDX8 | MKSSVTENLNEPPPLRTKRVLVASSASKLATLTAGLEKLGARVIPFPTIEIREIADKTAVDAALDALDSYSWIIFTSTHGVSYFLLRMKQRGIPADLWRDRKVCAVGPSTAEALRDAGVLVNLVPQDFVAEGILRALADSHGGLEKLVGCRILLPRAKEARDILPRTLESAGARVDILPCYENVLPEVDEAMVRGIVREPPEIVVFTSSSTVTNFAKILGGNNLKSVFERSTVAALGPITAGTIESLGKRVAILPKENTTASLLQALASHYRGE | Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 3/4.
Function: Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III.
EC: 4.2.1.75
Catalytic Activity: hydroxymethylbilane = H2O + uroporphyrinogen III
Sequence Length: 274
Sequence Mass (Da): 29492
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E3TFX4 | MAGTLARKAVDHLRSKEFRDYLMSTHFWGPVANWGLPIAAISDMKKSPEIISGRMTFALTCYSLLFMRFAYKVQPRNWLLFACHFTNEGAQLIQGGRLIKYNMEKKTAN | Function: Mediates the uptake of pyruvate into mitochondria.
Subcellular Location: Membrane
Sequence Length: 109
Sequence Mass (Da): 12520
Location Topology: Multi-pass membrane protein
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A0A0D6HNF0 | MKIAIAGSGALGSGFGAKLFQAGYDVTLIDGYTSHVEAVKQHGLNITINGEAFELNIPMYHFNDQPDESIYDVVFLFPKSMQLKEVMEDMKPHIDNETIVVCTMNGLKHEEVIAQYVAQSQIVRGVTTWTAGLESPGHSHLLGSGPVEIGELVDEGKENVIKVADLLNEAELNGVISKDLYQSIWKKICVNGTANALSTVLECNMASLNESSYAKCLIYKLTQEIVHVATIDNVHLNVDEVFEYLVDLNEKVGAHYPSMYQDLIVNNRKTEIDYINGAVATLGKQRHIEAPVNRFITDLIHTKESQRHAQD | Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 2/2.
Function: Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid.
EC: 1.1.1.169
Catalytic Activity: (R)-pantoate + NADP(+) = 2-dehydropantoate + H(+) + NADPH
Sequence Length: 311
Sequence Mass (Da): 34444
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A0A179IP59 | MDAFERGGWWTAVVRPDEDGEALGRLMRRRFGLTGRLYQRIVHARAFRLNGRMSHTAARVRAGDRISVRIAPPESYGVTPEPIPIRVVYEDAHYFAVDKPPGMLVHPIGRDGEPGSGGTLAAAVAGWLQARGIRTRIRPVNRLDRETSGLVLFARHALAHARLDAPLRRGMIDRRYLAVVHGVPDPPEGEIDAPIARDPAHSERRIVAPDGQPARTRYRTLAVYAGAALLDVALMTGRTHQIRVHLSHLGHPLFGDRTYGGREHPAAPLGRQALHAYRLAFHHPFEDRPVTVEAPLPPDLERLLQALANQGTGAV | Function: Responsible for synthesis of pseudouridine from uracil.
EC: 5.4.99.-
Catalytic Activity: a uridine in RNA = a pseudouridine in RNA
Sequence Length: 315
Sequence Mass (Da): 34772
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A0A7S3G8M9 | MVIRNTLFVTASGVVAHWYMGQAEGKKPAAVVGKVFGVAVSKNFGSIIFGSLLVSFIRLIRVIVEGLRRYNPLQNGWLWMVADFCFGCVEALVRYFNGFAYAYIAIYGRSFIASAKAAWELFRRSGLDRVVNDDVISGTLFLTYLLVACLCGGMGAFWVYQQDSAESDWFYGAALPCAIIGFIMGVVTLDTVAGAVTTLFVCFGEEPEKLYAHFPDLGTGRNISNHVAFEEA | Function: Choline transporter.
Subcellular Location: Cell membrane
Sequence Length: 232
Sequence Mass (Da): 25457
Location Topology: Multi-pass membrane protein
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W5U8M2 | MAKLVVLLSCCALVSLVVGQHARDRVGPWTQRIHWENNGHVYSLLSTGTEYHSPLHARRESRVYLSSRSQAASPITPGEARDSLAHFRITTTHSGASGTASTVMGPDGRHYVMANGRATGARHAHLVAPPRQGLAGAPGARRYATAAASNYTNSAHLSEYSGSGVPRRSASTPVDDNSANRIVGLPSTAIQELHLESAAPTNLESAHMESVNAHQSYPNPTITGEESIGDVIATAPGPLGTSEEDATPDNMVGDDPRNPLKNHRNTVFYNVYPSGGRAVTARTRRPPPGTGYGTRYFHNGLPDLVPDPYSIQAGSYIQRVQMYALRCAAEENCLARSAYRPVVRDLDYRVLLRFPQKVRNLGTADFLPVKPRHQWEWHSCHQHYHSMDAFSLYDLLDINTGRKVAEGHKASFCLEDTGCNPGFRRRYACTAHTQGLSPGCHDTYAANIDCQWIDITDVRPGNYFLKITVNPNFLVPESDFSNNVVRCEVFYSGHHVQTRNCRITRN | PTM: The lysine tyrosylquinone cross-link (LTQ) is generated by condensation of the epsilon-amino group of a lysine with a topaquinone produced by oxidation of tyrosine.
Function: Mediates the post-translational oxidative deamination of lysine residues on target proteins leading to the formation of deaminated lysine (allysine).
EC: 1.4.3.13
Catalytic Activity: H2O + L-lysyl-[protein] + O2 = (S)-2-amino-6-oxohexanoyl-[protein] + H2O2 + NH4(+)
Subcellular Location: Secreted
Sequence Length: 506
Sequence Mass (Da): 55664
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A0A2G6HVB8 | MLNKKSFSILMLLVSLPLLAAEGGHHGPDVVELIARTLNVAVFAGILFYFLKTPVADFFATRVSKIKSDLEMAKTSRIEAEKRLAEIEEKMSGLDLEVEAIAQKARADAEREKARLKEKVELETEKIREQAAKDIAHAKSEALTEVKRYVVDLAMEQVEDVLKDRMTKQDQERLVQKFAEKLGA | 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: 184
Sequence Mass (Da): 20711
Location Topology: Single-pass membrane protein
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A0A0H4U953 | GTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPAAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPARGGDPILYQHLSWFF | 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: Membrane
Sequence Length: 209
Sequence Mass (Da): 22436
Location Topology: Multi-pass membrane protein
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Q5DEY5 | MCLHILYYVGVIFACIPILYRIPKVQYYTKFTVFCLSILVGSFYYSIRLAFEGRRYENAWMFIKHLTFSGKLIGLNPVVENAQLLPKEPCIYVLNHQSLIDVASVGGIWPKRCAVVSKASLKFIGPLGLIIWLSRTITIDRSHHSDAISTMDKAAEAAKRDQVSVCIFPEGTRSDADNLLPFKKGAFHMAIKCQFPIQPVVIEPYSKFLNHKEKRFESATYRVRVLPKIDTKGMDKSQVDELLNETRKKMVAAIELLRNPSN | Pathway: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 2/3.
EC: 2.3.1.51
Catalytic Activity: a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-phosphate + CoA
Sequence Length: 262
Domain: The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate.
Sequence Mass (Da): 29833
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A0A6P7K4T2 | MMFTLTEVASLNDIQPTYRILKPWWDVFMDYLGLVMLMLAIFAMTMQITKDQVACLPYLEDPDQPKPSSFPQSSTVEESSSAATGAPVTATNVVSGLRTAQQQTAVASETYLNQPPPTGVKTNLDFQQYVFINQMCYHVALPWYSKYFPYLTLIHTIVLMVSSNFWFKYPKTSSKIEHFVSILGRCFESPWTTKALSETACEDSEENKQRLTGTSSAPKQVSLEGDDSTTVSPSTPMLGVKFSADKPIAEVPSSLTILDKKDGEQAKALFEKVRKFRAHVEDSDFIYKLYVAQTVVKTIKFILILSYTSTFFAKINFIHECKPEIKQLTGYKKFFCTHNMAYMLNKLLISYMALILIYGMTCLYSLFWVFRRPLKEYSFEKVREESSFSDIPDVKNDFAFLLHMVDQYDQLYSKRFGVFLSEVSENKLREISLNHEWTFEKLRQLVTRNAQDQQELHLFMLSGLPNAVFDLTDVEVLKLELIPEVRFSAKVSQMTSLRELHLCHSPAKVEQTGFAFLRDNLRCLHVKFTDVAEIPPWVYLLRSLRVLNLIGNLSSENNKMIGLESMRDLRHLKTLSLKSNLTKMPTNITELSPHLIRLVVHNDGTKLLVLNSLKKMVNLVELELHTCELERIPHAIFSLINLQELDLKSNNIRTIEEIISFQHLKRLTCLKLWHNKIITIPSSIGQVKSLEALHLSHNKLESLPPALFTLPKLRHLDVGFNSITVLPPEVGLLHNLQHLAINANKLEVLPKPMFRCTKLKVLCLGNNALTVLPESVGQLVQLTQLELRGNCLDRLPAQLGNCRLLRRNGLVVEDHLFDTLPVEVKESISRETSFTSGL | Catalytic Activity: chloride(in) = chloride(out)
Subcellular Location: Cell membrane
Sequence Length: 838
Sequence Mass (Da): 95619
Location Topology: Multi-pass membrane protein
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A0A3N5XE34 | FSDAADVVVCDGFTGNIALKVSEGLAEMIADMLRERRGDADGPALGSFARRIDWSEYGGVPLLGVAGLALVGHGRSSARAVRNGIEMAYRHAAAGIISRIQHALEPPGAPKT | Catalytic Activity: a fatty acyl-[ACP] + phosphate = an acyl phosphate + holo-[ACP]
EC: 2.3.1.274
Subcellular Location: Cytoplasm
Sequence Length: 112
Sequence Mass (Da): 11671
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A0A523DST5 | MSRTTFRTVGIVAKPSGVAAHKVLVEILTLFRRHKVKVLMDEEAARMAGAPGALPRAEVVTGSDLVIVLGGDGTFLSAARSVRMQGPPLVGINLGSLGFLTEIPRRDVTKALTTILQGEAGEERRLMLAVRVLCKDRLLASYTALNDVVLAKSSLARTVRLRVMVDGHPVSSYRSDGLIISTPTGSTAYSLSAGGPLVHPAMDAILITPICPHALTNRPLLIPARARVEVSRSSGNDPIHLTVDGQTGGPFGPRDRIEVRRSRISLRLMHPFRRTFYDTLRTKLKWT | Function: Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP.
Catalytic Activity: ATP + NAD(+) = ADP + H(+) + NADP(+)
EC: 2.7.1.23
Subcellular Location: Cytoplasm
Sequence Length: 287
Sequence Mass (Da): 31109
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A0A2V9JGJ1 | MAPRSLGSDLSVELIDISTCKRNLVIEVSREEVDDEIHKLAQKYAERVRVPGFRPGKAPLVIIKQRFAAELKSEVTQELIKRYWKTALSDHSLRPLTQPVVEHIDAEPGNPLRFTLSFEVLPPLEVKDYKGVSVPLSEPVVSESDVDQVLESLREQNAQLVPVDEGEIRDGHVVTLAVDGEFEGGGKALHEEDVVCTIGDPGTNSAFSENLRGARVGDELQFNVPYPAEDQRKRFAGKTVRYRVLVKEVKEKHLAELNDDFAKDVGGLENLEELRARIRDDLISKARVAAEKDVREAILNQVVQRHFFDVPESLVREELEDRARRIATQFVRRGIDVNDTSIDWKKIFEGERPHAEQTVRRTLILDAIARQEGIEVLEAELEEEVRTLAETAKKSPVALRAQLEKDQRIQSVKEHLRRKKALDFICRNANISRG | Function: Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
EC: 5.2.1.8
Subcellular Location: Cytoplasm
Sequence Length: 434
Domain: Consists of 3 domains; the N-terminus binds the ribosome, the middle domain has PPIase activity, while the C-terminus has intrinsic chaperone activity on its own.
Sequence Mass (Da): 49157
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A0A2D0R4D5 | MGDWSFLGRLLENAQEHSTVIGKVWLTVLFIFRILVLGAAAEEVWGDEQSDFTCNTQQPGCENVCYDEAFPISHIRYWVLQIIFVSTPTLIYLGHILHIIRMEDKRKEKEEELRKAQGHQEEKELLYRNGEGGRGGGKKEKPSIRDEHGKIRIRGALLRTYVFNIIFKTLFEVGFILGQHFLYGFQLRPLYKCARWPCPNTVDCFLSRPTEKTIFIVFMLVVACVSLLLNLLEIYHLGWKKIKQGVTSGYILEQELLAHTDPVETGAIPAASRTDPATLSYPPKYTKLAAGSASFLQTGSVPVTTEFKIDPLHEEPNSFYISSNNHRLAAEQNWANLATEQQTLEKKAIAPSTSSSSSASSCDNEQRLRDAAPTTSIPSSSGGILSSGKWEPEESHVTTTVEMHEPPSVFTDLRCMSRASKTSSVRARHNDLAV | Function: One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell.
Subcellular Location: Cell junction
Sequence Length: 434
Sequence Mass (Da): 48677
Location Topology: Multi-pass membrane protein
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A0A0H5BNV5 | MQPRTLVLAVVGGLSVAGAAVATAAILAVAHAAGVPPAQAGLHVSVVAGGGLLAGAAGWLLLRAKLVLPLEALTRELRLLKDNPQPRALDLAGGHALGTLPADIDGLFGKLQTSREVTAAAIAAATKRAEEQRSRLEAILVDLAEGVVVCNLDHRILLYNQAARRLLHRPAGLGLDRPLFGVLAEEPIRQTLEMLRRSASDASPVLRIHRCVVPTLDADIWLKARLGLVHEPSGEVSGYVLTFTETAEGTAPAASPIERIAPRPEFYDFDLFKPAGTSLADTPLRKMAFVVFDTETTGLDPDGGDELLSIGAVRVVNGRLLTGETFEQLIDPGRTIPPASIKFHGITADMVAGQPAAREALPRFKAFADDAVLVAYNIAFDMAFLTKREAEAGVAFDNPVLDALLLAAHVFPDQPDHSLSAMAHRLGVDVKGRHTALGDAVATARLWVKLLNMMEMRGLATFGQAVEISQRMMKQRQAQTPGVGW | Function: DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. The epsilon subunit contain the editing function and is a proofreading 3'-5' exonuclease.
EC: 2.7.7.7
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Length: 485
Sequence Mass (Da): 51555
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A0A348VT45 | MFLSPNNIKWHCTLVKKEDRCALNRHSSTVIWLTGLPSSGKSTVANQLEHMLFRYGLRSYILDGDNIRHGLNKNLSFTAEDRKENMRRVGEVAKLFIDAGLITIVAFVSPFRTDRQMVRDMFPKDEFLEVFVKCSLAVCELRDPKGLYKKARKGEIAHFTGVNDPYEAPEQPELEIETDKLSLDDCVRKIFRLLVDKKIVTHSDELGNQKSPGSPVQVPDPLLSFG | Pathway: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 2/3.
Function: Catalyzes the synthesis of activated sulfate.
EC: 2.7.1.25
Catalytic Activity: adenosine 5'-phosphosulfate + ATP = 3'-phosphoadenylyl sulfate + ADP + H(+)
Sequence Length: 226
Sequence Mass (Da): 25708
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A0A0V1EKL9 | MLYLLRPAFARSKCILFDFSNRFSHTALSSEGIIVAYHPEKSFPYEHSKPVLLNVTTTEKEDSILSEELRERYKTFHYPRGPSLPDCQNMFYTNKHVFHINSSCKPIPIYAKWLGKISYVEGLRWQSIYEQKLSRHFSHLIVKKFNEEMIYHTIMLLEHFPVYTIGLRTRSYPEELKKKLECLGADFYKTNRGGLITFHGPGQLVAYPILYLPEFHSRPFSKWYVNQLEKCLIEVCSNFDVKAYAPGSPLTGVWVNDRKIASIGLRLKNDISTHGIALNCNIDLSWFEHIDPCGLIGKQMTSLSSETETDVTVHDVIEPFLKAFNKYFGREVILKDEAELVAS | Pathway: Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 1/2.
Catalytic Activity: L-lysyl-[protein] + octanoyl-[ACP] = H(+) + holo-[ACP] + N(6)-octanoyl-L-lysyl-[protein]
EC: 2.3.1.181
Subcellular Location: Mitochondrion
Sequence Length: 343
Sequence Mass (Da): 39674
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A0A0H5B8K3 | MTTVAELFAADLPPGHRAGGLTVTGLAVDSRRVAPGHVFVAVPGTHADGLAYAPAAVAAGAVAVVAATAPPGDLGVPVVVLQDVRGALARAAARLFPRQPALEVAVTGTSGKTSVTSFVRQVWSALGHAAASIGTIGVVAPSGADYGSLTTPDPLSLHATLDRLAGEGVSHLAIEASSHGIDQRRLDGMRFAAGAFLNLSRDHLDYHITLDAYFASKLRLFEVLLPPGAGVVVDADLPEADRVRAVARPRGLRVFSVGRSGAGIRLISAEVEGFAQRLEVETSGRRYRTLLPLAGAFQVSNALAAAGLAIVTGSEPGAVFAALEHLEGAKGRLEMVAETGGALVFVDYAHKPDGLDKMLATLRPFTTGRLVVLFGAGGDRDPGKRRIMGEVAARLADRVIVTDDNPRSEDPAVIRRAIVQGAPNAEEIAGRGEAIRTAVAGLKAGDVLVVAGKGHETGQIIGDRVLPFSDHDEIAAAVRARNG | PTM: Carboxylation is probably crucial for Mg(2+) binding and, consequently, for the gamma-phosphate positioning of ATP.
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan.
EC: 6.3.2.13
Subcellular Location: Cytoplasm
Catalytic Activity: ATP + meso-2,6-diaminoheptanedioate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptanedioate
Sequence Length: 483
Sequence Mass (Da): 49781
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A0A356Z583 | MSQDNNLDLNRLQNTDLKPAVQVWLESPGGEQQYFFDNSITCTAIIQEKIVVYCYPELITNLSGMAKNYINKNYEEFVYPEDIKKVDQFLYFIYQNNSPKDLLRFRICDWEGNPAWVEITGQPIIYHGKPSALIVATSITNNMRKIQFLKDLTEIYRNFAEQSPDGIVVRQGNRILYANSRAAERSGFSREEIRQVDAFAGVAEDDVNTAREIAAKWDTGQATPSLVELRMVDADGEVFTCEVASSFINYHGEPAVQHTLRDISYRKKIQKELQLQANLLSNVNDCIVVTDSDYQIIFWNQGAERLLGRKEDEVIGQKLGTVLNEDSFVDQIKNDLLMNGHWEGQREIKMTPEGCKTLQLSVTTINDDCDNTSLVLIARDITELLESQRREREANQAKSEFLARLSHEMRTPLVGIVGYCELLRSVSEGPPNQEGLATMEYCARQLLDLANNMLDLSKIEARQVEIKLESVDLYNLINYTVNSFYPNISANVELSVHISSSVPRNVIGDNAKIKQIIANLLSNAFKFTRRGYVKVKVDLANSFKVSEGMYPIRIAIIDTGIGIKETDRIKIFEPFVHDVIAADGEDGTGLGLAICRQLVELMGGSIWCKANPEGGSEFGFVLPLKASAAPPAPVESGQAITNMPVPDGLEVLLAEDISVNRKLITLMLEKLGCEVVAVSNGEQCVNMLDEYKPDIILMDMQMPVMDGYSATRIIKGRSSLAAIPVIALTAYAMTEDVDKCQEAGCDYYLSKPFTNEQLASALKQCSNV | Function: May play the central regulatory role in sporulation. It may be an element of the effector pathway responsible for the activation of sporulation genes in response to nutritional stress. Spo0A may act in concert with spo0H (a sigma factor) to control the expression of some genes that are critical to the sporulation process.
EC: 2.7.13.3
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
Sequence Length: 768
Sequence Mass (Da): 85860
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A0A962GYW4 | MAALFELSTEALDPDALRQRIEDLGCGAVVLFEGRVRDRNRERPVERIVYEAYAAVALAEGQAVVAEMQSAHALSEVLVVHRTGEVGLGELAVWVGVSAPHRDAAFAGCAATISAIKARVPIWKHEHYRDGGPEWLHPLP | Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
EC: 2.8.1.12
Catalytic Activity: 2 [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-NH-CH2-C(O)SH + cyclic pyranopterin phosphate + H2O = 2 [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-Gly + 4 H(+) + molybdopterin
Sequence Length: 140
Sequence Mass (Da): 15230
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A0A962NAD6 | MRERSGQSQRGFTLLEVMVALVVLGLALLAVLQSTGNASRIQARLDETSWARWVASNEIARVRAQAEWPQLGLDRGSTRLGQREWYWRRGISETPEPDLRRIDVQVYSDPAEQQLVTQVSGFIGRRSRG | PTM: Cleaved by prepilin peptidase.
Function: Component of the type II secretion system required for the energy-dependent secretion of extracellular factors such as proteases and toxins from the periplasm.
Subcellular Location: Cell inner membrane
Sequence Length: 129
Sequence Mass (Da): 14622
Location Topology: Single-pass membrane protein
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A0A962HC27 | MFDVGFSELMLIALVALVVLGPERLPGAARTVGALLRKARSSFESVKAEVEREVRDEELKRALKNMPQPSETLRSVTEPLEQQAREIRDSLKSVDDATRR | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. Together with TatC, TatB is part of a receptor directly interacting with Tat signal peptides. TatB may form an oligomeric binding site that transiently accommodates folded Tat precursor proteins before their translocation.
Subcellular Location: Cell membrane
Sequence Length: 100
Sequence Mass (Da): 11206
Location Topology: Single-pass membrane protein
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A0A932QZT9 | MNVVSCQIMKMEITDLDDVMAIEQIAFSAPWTKEMFYSEFFDNSLSFSFVAKEGDDVVGYLFAWEVSEEFHLMNIAVAPKWQRQGIGEALIKKMCDVGTDRSIKQIQLEVRASNTSAISFYGKLRFYKVGIRKNYYRSPHEDALILQYDFPL | 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: 152
Sequence Mass (Da): 17593
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A0A174AB27 | MKISTFFYVLRQGFANIRRNILFSLASLGTIISCLFLFGIIYAVVVNFQSGMQELEKTVTISVFFDEDASDETIQLIGEQIRTVDYVETMDFISADEAWDKFADQNYDDPQVAKNAFGGDNPLKNAASYEITLKDVSRQPEFVAFAQGLSGVRKVKSSDVTADSITTLSSLVGYASIGIVVILMLVSIFLISNTITIGITVRKEEIGIMKLIGATNVFVRAPFIIEGVIIGAVGSAIPLVLLYYMYDKILTYVAGRFKVVTTLFAFVSQQDLFRTMVPVGLVLGIGVGLVGSILTTRKHLRV | Function: Part of the ABC transporter FtsEX involved in asymmetric cellular division facilitating the initiation of sporulation.
Subcellular Location: Cell membrane
Sequence Length: 302
Sequence Mass (Da): 33153
Location Topology: Multi-pass membrane protein
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A0A6M9BN94 | QDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSAVEAGAGTGWTVYPPLASNLAHAGASVDLTIFSLHLAGISSILGAINFITTIINMKPAAISQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPGGGGDPILYQHLFWFF | 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: Membrane
Sequence Length: 226
Sequence Mass (Da): 24280
Location Topology: Multi-pass membrane protein
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A0A2V9IXL3 | MTSKKPTGEPPSHPFRIQVLNRQRRYAIFPRVVESLCFRVLQILRESACSFSVTFVGPRRIRLLNRRYRGKDYPADVLTFRYAGESLEGQPFLGEIVISPEVASRNARQWNATLQREVRRLLIHGVLHLLGYDHETDKGEMRRLENRLMRSRARIRSGPVGRARYAG | 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: 167
Sequence Mass (Da): 19417
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A0A2V8FE64 | MKAKRHPPAGRAGRKGLKAVGLTQQVVAAGUAAKLGPADLVHVLHCLPPLDHADVIVGTETSDDAGVFRLRPDLAIVNTVDFFTPIVDDPYVFGQIAAANALSDVYAMGGEPKTALNIVAFPKGKLDLAILAEILKGGAERVTAAGAVVIGGHSVIDPELKFGLAVTGVIHPARVIRNVGVQPGDALVLTKPLGTGIVSTALKQRKAPASAVRDAVRSMITLNATASTVMRAFPVHACSDITGFGLLGHAHEMASGSDVTLVFESAQLPLLAGAVRLAEKGYVTGGSRRNRDYLGGKVEVKESVGAGLVEVAFDPQTSGGLLIALPRPRAPKLVEALHKKGVNVARVIGHATPPQEAWVRLV | Cofactor: Binds 1 Mg(2+) ion per monomer.
Function: Synthesizes selenophosphate from selenide and ATP.
EC: 2.7.9.3
Catalytic Activity: ATP + H2O + hydrogenselenide = AMP + 2 H(+) + phosphate + selenophosphate
Sequence Length: 362
Sequence Mass (Da): 37566
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A0A132NC91 | MAERLTEETVQKIADAAAIALTDEERQTILKELQEILDFVDVLRAVPVDGVEPTVHPVPLAIFMREDEPERRHDREALLARAPEAEGGFIRVPRVLGD | Function: Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).
EC: 6.3.5.-
Catalytic Activity: ATP + H2O + L-aspartyl-tRNA(Asn) + L-glutamine = ADP + 2 H(+) + L-asparaginyl-tRNA(Asn) + L-glutamate + phosphate
Sequence Length: 98
Sequence Mass (Da): 10996
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A0A0W0U7Q5 | MNRSPRTEALHVLTCLLDKRIPLSHQLQGVSPHAKVLVFGVSRQYYRLVAVADCLMQKRPAKTAVFVAILMGLCELLYLDTPEHAVVSETVGLLRGKSLQFARGFVNALLRRACREKAELQAFLLTLEDKGLAPWLAERIKSDWPHHAGNILAASDCQAPMTLRVNARQSSVSEYLKRLQDSGIEASACQFSADGVVLKVALDVADVPGFFDGVVSVQDEAAQLACALLEVQPHMRVLDACCAPGGKLCHILEQANAEVTGVDADASRMRRVEENCTRLGISPRLLVGDAAHPHTWWDGRPFDRILLDAPCSATGVIRRHPDIRLLRTPKDVETVVVLQRQLLDALWPLLAPGGMLVYATCSILQAENAHQIAGFVAGCEDCLLETPSTPWGHKSDFGTQILPGESGMDGFFYSVLRKKTL | Function: Specifically methylates the cytosine at position 967 (m5C967) of 16S rRNA.
Catalytic Activity: cytidine(967) in 16S rRNA + S-adenosyl-L-methionine = 5-methylcytidine(967) in 16S rRNA + H(+) + S-adenosyl-L-homocysteine
EC: 2.1.1.176
Subcellular Location: Cytoplasm
Sequence Length: 421
Sequence Mass (Da): 46096
|
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