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Synthyra 5

A0A251S005

MNYSYSSDEDDKPLVFKRTSAADKLKHSGQLKSASSADKLKHSGQLKSASSADKLKHSGQLKSASSADKLKHSGQIKSTSIVNREKPSTSTKPKPPAKQESDTEDSEDDKPLSARISTAPKTNSNHAKTGPVSASQRPKPQVKNDDSDDKKPLSSKFTSVGPSVKKPDDSDDDDKPLSARVKQNGSTSRDNNNNNNNNNNQLNKKPNIGLNKRPPNEERLAGQSSVKKPKLSDSEDENDHVPISQRMKKQTPSGSKPSSSVKQKVVKVNSSSFKKTFKKSNKFEKKSKYSKSSKVPPGSGEGQKWTTLVHNGVIFPPPYKPHGIKILYKGKPVDLTPAQEEVATMFAVMLDTDYMTKPVFKENFWNDWRKILGRNHTIQNLEDCDFKPIYDWHQREKEKKKQMSTEEKKAIKEEKMKLEEKYMWAIVDGVKEKVGNFRVEPPGLFRGRGEHPKMGKLKKRIRPSDITINIGKGAPIPECPIPGESWKEVRHDNTVTWLAYWNDPINGKDFKYVFLAASSALKGQSDKEKYEKARSLKKYIEGIRKAYTKDFINKDVTKRQVAVATYLIDKLALRAGNEKDDDEADTVGCCTLKVENVEPKPPNILKFDFLGKDSIRYQNEVEVELPVFKAIQQFRSGKKGNDDLFDKLDTSTLNAHLKELMPGLTAKVFRTYNASITLDDMLSKGATGGNVAENVVVYNQANKEVAIICNHQRSVSKSHTAQMMRLNEKIEELKGVLEELETDLARAKKGKPPLKGSDGKIKRNMNPEALQKKIDQTYAKIEKMERDKETKEDLKTVALGTSKINYLDPRITVAWCKRQEVPIEKIFNKSLLAKFAWSMDVDPSFRF

Function: Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at the specific target site 5'-[CT]CCTTp site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(3'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 5'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand thus removing DNA supercoils. Finally, in the religation step, the DNA 5'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone. EC: 5.6.2.1 Catalytic Activity: ATP-independent breakage of single-stranded DNA, followed by passage and rejoining. Sequence Length: 847 Sequence Mass (Da): 95330

A0A251NC15

MESSEEQKLQVRKLELSDKSKGFIELLQQLTVCDSVSDKDFEDRFRELNARAEDHRVLVIEEDRSGKIVATGSVFIERKFIRNCGKVGHIEDVVVDANARGMQLGKKIINALTDYAHSLGCYKVILDCNVENKAFYEKCGYKQKEIQMFERSWGTHMIKPFICLNKNWRSSSKSKHLAGGQVWTGKPIILENEYPRGLGSDLDLIAHPLLCFQSLQHSLLCLLVSGSTSNWFFYFIL

Pathway: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route I): step 1/2. EC: 2.3.1.4 Catalytic Activity: acetyl-CoA + D-glucosamine 6-phosphate = CoA + H(+) + N-acetyl-D-glucosamine 6-phosphate Sequence Length: 237 Sequence Mass (Da): 27098

U9UPF8

MSSETKAETSSGSNKINGKAKGNLNSYLLLYNAASWAGWTYVLTVSVLELFKNGGDVTKLYDRIGWTLTLVQTAAILEIFHVLLGLVRSPFITTVIQVSSRLTLVWLIVNKFPEVRSHWAFTSMTIAWSITECIRYAFYGLNLIGNQPGWLLWCRYTFFFILYPVGAGSESILVFESLRFAIRISQSFYWILVILLLIYVPGFYTMYNHMIGQRRKILGKGKVKKNQ

Pathway: Lipid metabolism; fatty acid biosynthesis. Function: Catalyzes the third of the four reactions of the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of two carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme catalyzes the dehydration of the 3-hydroxyacyl-CoA intermediate into trans-2,3-enoyl-CoA, within each cycle of fatty acid elongation. Thereby, it participates to the production of VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. Catalytic Activity: a very-long-chain (3R)-3-hydroxyacyl-CoA = a very-long-chain (2E)-enoyl-CoA + H2O EC: 4.2.1.134 Subcellular Location: Endoplasmic reticulum membrane Sequence Length: 227 Sequence Mass (Da): 25905 Location Topology: Multi-pass membrane protein

A0A3T0I7W5

TLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLASSLVENGAGTGWTVYPPLSAGIAHAGASVDMAIFSLHLAGVSSILGAVNFITTVINMRSSGMSLDRMPLFVWAVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF

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: 219 Sequence Mass (Da): 23355 Location Topology: Multi-pass membrane protein

A0A251SDR6

MDKGVFLEKTKERSLKITPSWAVAVVVFVILAISIALEYILHLIGHWLQHKQKKSLHEALEKIKAELMLLGFISLLLTVGQEPIASICISSKVARTWHPCNDDSADTDFYDPCLKKGKVQMVSNYGIHQLHIFLFVLAVVHVAYCLLTLALGRLKMRRWKAWEDETRTSEYQYHHDPERFRFARETTFGRRHLRSWSTSSILMWIGCFFRQFFSSVAKVDYLTLRHGFINTHLNHLSPESQHKFDFHKYITKSLEEDFKEVVGISPIVWFFAVLLLLTNTHDWYAYLWLPFIPLVIILLVGAKLQLIITQMGRRTNDMADVVKGTPVVKPADDLFWFGRPHLVLLLINFVLFQNAFQLAFLWWSWDTFGFTCFHRRTEDIVIRITMGVVIQFLCSYVTLPLYALVTQMGSRMKPTIFGDNVAKGLKTWHHTAKKNIKHGHHSSTNTPFTSRPGTPLHGSTSPISLLHRHQEDSLDSPSESPRGEHEGWANESSLNDRYQYHEPENFRRDSHTDLEEEEIQELGPTSTRLPSRPRPVRSQSAVDMTEFSFGQSK

Function: May be involved in modulation of pathogen defense and leaf cell death. Subcellular Location: Membrane Sequence Length: 553 Domain: The C-terminus contains a calmodulin-binding domain, which binds calmodulin in a calcium-dependent fashion. Sequence Mass (Da): 63987 Location Topology: Multi-pass membrane protein

A0A7S3MQT2

MAPKMTDFSKGTTTLAFEFQEGVLVAVDARATQGSFISSNQVRKVIEINDFLLGTMAGGAADCQFWEGYVAMLCRIHQLRHGEAPSVAMASMMLCSIMRQYKGYGLSMGTMFTGSDKTGASLYYIDNDATRLRGRLFAVGSGGTFAYGVLDTNYRYDMSLDEAVNLGIRAIASATFKDSASGGVVRIYHVTNNGDWNLVHDQIDVSQ

Function: Component of the proteasome, a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. Catalytic Activity: Cleavage of peptide bonds with very broad specificity. Subcellular Location: Cytoplasm Sequence Length: 207 Sequence Mass (Da): 22510

R4J886

EFRGLGDCLTKIYKSDGLFGLYRGFTVSVQGNFMYRASYFGFYDTVKGMLPDHLRRNILISWVVAQTVTTCSGIIAYPFDTL

Function: Catalyzes the exchange of ADP and ATP across the membrane. Subcellular Location: Membrane Sequence Length: 82 Sequence Mass (Da): 9304 Location Topology: Multi-pass membrane protein

K3ZQJ4

MAQPLVVKKDDDLDEEEYYSPFLGIEKGAVLQEARVFHDPQLDARRCCQVITKLLYLLNQGDTFTKVEATEVFFATTKLFQSKDAGLRRMVYLMIKELSPSADEVIIVTSSLMKDMNSKTDMYRANAIRVLCRIIDSTLLTQIERYLKQAIVDKNPVVASAALVSGIYLLQTSPEVVKRWSNEVQEAVQSRAALVQFHALALLHQIRQNDRLAVSKLVTSLTRGSVRSPLAQCLLIRYTSQVIRESGTNQSGDRPFFDFLESCLRNKAEMVILEAARAITELNGVTSRELTPAITVLQLFLSSSKPVLRFAAVRTLNKVASTHPLAVTNCNIDMESLISDQNRSIATLAITTLLKTGNESSVDRLMKQMTNFMSDIADEFKIVVVEAIRSLCLKFPLKYRSLMNFLSNILREEGGFEYKKAIVDSIIILIRDIPDAKESGLFHLCEFIEDCEFTYLSTQILHFLGNEGPKTSDPSKYIRYIYNRVILENATVRAGAVSTLAKFGALVDSLKPRIFVLLRRCLFDGDDEVRDRATLYLKLLGGEATVGETEKDVNEFLFGSLDVPLVNLETSLRNYEPSDVPFDISSVPKETKSQPLAEKKSTGKKPTGPASALSGPVSTVDASYEKLLSSIPEFADFGKLFKSSAPVELTEAETEYSVNVVKHIYDGHIVLQYNCTNTIPEQLLEQVIVFVDASEADEFLEVTSKPLESLPYDSPGQTFVAFEKPEGVIATGKFSNILKFIVKEVDPSTGEAEDDGVEDEYQLEDLEIVSADYMLKVGVSNFRNAWESMDPESERVDEYGLGVREGLAEAVSAVISILGMQPCEGTDVVPSNSRSHTCLLSGVFIGNVKVLVRLSFGITSSKEVAMKLAVRSDDPEISDKIHEIVANG

Function: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. Subcellular Location: Cytoplasm Sequence Length: 888 Sequence Mass (Da): 98552 Location Topology: Peripheral membrane protein

K4AL20

MAAADCSGRRRFAVACGVLSRCVRAEAAAGKMVAAESHARAGSASTMLLMPGADVALDVVGEGAAEATPAPTRARLTIMHGGRVLVFDDVTADRAAELVRVAAGQQVILGGSRTTDDVPVARKASLRRFMEKRRDRIATRSPYAAAAAFPTAAENGKEGEADTAGCCLELGISGGSAC

Function: Repressor of jasmonate responses. Subcellular Location: Nucleus Sequence Length: 178 Domain: The jas domain is required for interaction with COI1. Sequence Mass (Da): 18191

A0A1E1FA49

SGSTKEEIKTAVNNGVVKMNVDTDTQFAYLAGIRDFVIKKKDYLQTQVGNPEGS

Cofactor: Binds 2 Zn(2+) ions per subunit. One is catalytic and the other provides a structural contribution. Pathway: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4. Function: Catalyzes the aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and the reverse reaction in glycolysis. EC: 4.1.2.13 Catalytic Activity: beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate Sequence Length: 54 Sequence Mass (Da): 5907

A0A191T686

MNLSVIIQLVVLALIVISGPVVIGLLALRKGNL

Function: A core subunit of photosystem II (PSII). Subcellular Location: Membrane Sequence Length: 33 Sequence Mass (Da): 3440 Location Topology: Single-pass membrane protein

K3Y980

MSLWRAAASRLLLRRSPPLSPSTAASSYALLLHARPFSPPPPPPPPPPRPAPAEAEVTPAEARRLVRLVGVEALKHRLRDGRDEVVGYSELLDACVEAGAARTHAEAEELARAMDDAGVVLLFRDKAYLHPEKVVDLVKRAVPLALGPENDPRKEEFKQLQEKKEEIDKLAHKQVRCILWSGLGFFMCQVGLFFRLTFWEFSWDVMEPIAFFTTASGLLVGYAYFLITSRDPTYQDFMERLFLSRQRKLCAAQKFDMERYMELQKHCRCPLEGHHPHGPKLHGL

Function: Mitochondrial inner membrane calcium uniporter that mediates calcium uptake into mitochondria. Constitutes a pore-forming and calcium-conducting subunit. Mitochondrial calcium homeostasis plays key roles in cellular physiology and regulates cell bioenergetics, cytoplasmic calcium signals and activation of cell death pathways. Subcellular Location: Membrane Sequence Length: 284 Sequence Mass (Da): 32205 Location Topology: Multi-pass membrane protein

K3ZJ60

MHAAAAAEEERAAELAGPLRDILPPVDFCCAYGSTLLHARPDGTSMVDYILGVADPLHWHSENLKRNPAHYSRWMGCLGASAITGLADRIGVGVYFNPFVEWRDKRIKYGVVRMKDLAMDVLTWDRFYLSGRLQKPVHVLVDNWDIRKVNTINLEMATSASLLLLPEEFNEYDLYAQICSLSYMGDLRMLFAEDKNKVKKIVEGSFQSFQTMYRPLLQEYIAEGLLKTSSHGQQKIFRQDCGPSTTNELFSVLPWTIQRQMQGRYGSHGKEMPTRMVVSSKEMAANCVRRALRRRVMVSSVRQAVSGLLASGGAVAAQYLGKKMAKAWQSRAA

Pathway: Lipid metabolism. EC: 2.7.7.41 Subcellular Location: Mitochondrion inner membrane Sequence Length: 333 Sequence Mass (Da): 37461 Location Topology: Peripheral membrane protein

A0A5D2DRU7

MSASMLLCKYEYDELALAEVIFVITSAVKDVCGKLPTERLFLGKYGRICLTLDEIIWKIFFSSELELMELLDGHCDILALIAYQFEDINVHYCYFHDLTNLRLYITQIIWYCVFPVTHMYITCYVVSTGIIGIMRPLHLHELLMKLYQLRF

Function: The zeta subunit may be involved in regulating the coat assembly and, hence, the rate of biosynthetic protein transport due to its association-dissociation properties with the coatomer complex. Subcellular Location: Cytoplasm Sequence Length: 151 Sequence Mass (Da): 17764 Location Topology: Peripheral membrane protein

U9UUL8

MSQKNINKPPLSHSASWSAGVASSEHTSSSIYSEHKNISNASINSEKFINDDSYSNIHPYIGLRGKLSLAWITYPIISFIFVIGRLFIAMNSIDPIIEDIRQRVNKSCDALELATSSLISLPHFMAGPFNDSITDTINSTIRGFVRTLDLGIQALNGIIVFFINLYKSTFRCLLELAVRGSISAVSEAVIFLQGFSNNALAGIKTAIDNSIAGINSSLEGVRNALSNVGGLLNLPEIPTVSIPAAEDLNKVTFPTTGIVNGLDTLNASIPSMDEIENRLTNLISIPFNELRVIINNSMSDIKFNSSILPVPPMGNNIKFCENNLNLEVLDNIKNDLKRTAWIGLSILFALSILLILANIFYIWISHKRFMNKVDKSLNNFKRTNSNINKNSIIDIIKFSENPFLQNYIVKTSTYFKNRENQKIYRWFWDYILFKPAIICFIIGLSGIISIFIQIAILNGVRHTYKDEISESIANFGNTVMGLMNSNLQESSKQYSTQSNNIIINLENDINQNLFGWVNITTTALNNTLNTAVDEIVGFVNTTFGGVPFIRNVIDELLNCLILVKIKGIQSGLTFIKDNSHLGLPRVSENILMIKPDKMNSVISEATIRFAGEPDEEGTGGQIGRLFDAYEDRLKSELPLFWILIACWGVVLIFGLIRIIWFKLHH

Function: Involved in cell fusion during mating by stabilizing the plasma membrane fusion event. Subcellular Location: Cell membrane Sequence Length: 665 Sequence Mass (Da): 74176 Location Topology: Multi-pass membrane protein

A0A251TJP5

MEVNNIMQFLEDRTILVTGGTGFLAKVMVEKILRVQPNVRKLYLLIRACDLEEAIKRFQMEVCLTLANVVFVRVSLLSTPIHAMLSNVLYMGLAKVQLAIHFNGHFF

Function: Catalyzes the reduction of fatty acyl-CoA to fatty alcohols. EC: 1.2.1.84 Catalytic Activity: a long-chain fatty acyl-CoA + 2 H(+) + 2 NADPH = a long-chain primary fatty alcohol + CoA + 2 NADP(+) Sequence Length: 107 Sequence Mass (Da): 12195

A0A0K3CG06

MTSVLSERQKDELHKSILDYLRTNGFTETLNAFKAEAKQEDFQPDGKAKWSGLLEKKWTSVIRLQKKIMDLETRNSQLQEELSTAPSKRPSASSPDWTPRTPARHSLSGHRSPVTRVTFHPLFSVVVSASEDSTLKVWDWETGDFERTVKGHTKAVQDVDFDSKGNLLVSCSSDLTIKLWDTNNDWKNIRTLHGHDHSISTARFLPNDDFIVSASRDRTIRIWEVASGFCTRTISGHNDWVRSVLPSSDGQQLISCSVDQTARIWDLGKGDTKAELRGHEHVIEAAVFAPVAAYPAIRELAGMTVPSGRSAEAKAVGLFAATGSRDKTIKIWDAVSGQCLKTLVGHDNWIRALVFHPSGKFLLSASDDKTIRTWDLATGRCLKTLEAHSHFVTTMAWGRAPAPGASQPNGAATNGTNGAHAEAARLVNVVATGSVDQTVKIWLP

Function: Positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus end. Required for nuclear migration during vegetative growth as well as development. Required for retrograde early endosome (EE) transport from the hyphal tip. Required for localization of dynein to the mitotic spindle poles. Recruits additional proteins to the dynein complex at SPBs. Subcellular Location: Cytoplasm Sequence Length: 444 Domain: Dimerization mediated by the LisH domain may be required to activate dynein. Sequence Mass (Da): 48885

A0A4Q9LMA0

MGQAVFVMGPAGSGKTTFCKKLYEHGIAIHRSFHLINLDPAQIQENTVYSIDLRDFVTVEDIMENYDFGPNGGLIVALEELYDNIDELDLESLSSDFLIVDCPGQIELFTHSDTFKNIVEHFKKYFTCCIVYLIEAQFVSDPTKFISGCFVALLSMCRFSLPHLNIISKLDQLEISREILEEFCQLSESIKDHIQKKKGEYNQLCLKMYDFIVENNLVSFLELNYDDENTFDTILYSIDEAVQYFDDAEPKDHSYN

Function: Small GTPase required for proper nuclear import of RNA polymerase II (RNAPII). May act at an RNAP assembly step prior to nuclear import. EC: 3.6.5.- Subcellular Location: Cytoplasm Sequence Length: 256 Sequence Mass (Da): 29478

A0A0R3SE48

MTFRKIGVCPEIIELLHDKGILIPSEVQAACIPEILNGRDVVACAQTGSGKTAAFVIPILQALMSEPRPFYALIITPTRELAHQIGEQTAGLNLVQGSSICTVQVITGGRSIVKQGIDLALGPHVIVATPGRLADLLRTQKASAESDSTPEWSLSRLKVLVLDEADRLLEDNFGQDLTEIMSSLPRQRQTLLFSATFSDTVKRAMEAAKMSAVAENRKPPVMWQSKGITQSTEEKAAKSATVDTLSQYYLITKPELKDSFLVYIVDHFLTENPHSLIIVFSNKCKWCHLLGMIMQSVGIQSVVLHSSMSQNDRISSLNAFKSSHVRVMIATDLASRGLDFPTVDAVINHNVPIRPKDYVHRVGRTARAGKAGMALTLADLFEINRLREKLDEIRFDEKREIIKAKNLLKAQSAKREAQEAQHSGSKKKRTKVGTVDENA

Function: RNA helicase. EC: 3.6.4.13 Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate Sequence Length: 439 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): 48371

A0A8S3C1Y3

IKSLIKDIDQWNKIIEQLGTPPREFLCRLQPTVRNYVENRPKYAGYSLDRLFPDQLFPPDSEQSKLTGLSLCIYFVK

Function: Responds to activation by environmental stress and pro-inflammatory cytokines by phosphorylating a number of transcription factors, and thus regulates transcriptional activity. Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein] EC: 2.7.11.24 Subcellular Location: Cytoplasm Sequence Length: 77 Sequence Mass (Da): 9045

A0A251VP85

MASSILISFALLASTLFFMSGPSSAQLTPNFYSKSCPKVFDVVGSVVRAAVAKEKRMGASLLRLHFHDCFVNGCDGSILLDDTSSFTGEKTARPNVNSVRGFNVIDDVKKKVEGVCPGVVSCADILAISALESMLALGGPEWTVKLGRRDSKTASFSAANSGVIPPPTSTLSNLINRFQAVGLSTRDMVALSGAHTIGQARCTTFRARIYNDTNIDAAFARSRRSNCPRPSGSGDNNLAPLDVKTPNSFDNAYYGNLISQKGLLRSDQQLHNGGSTDSLVEQYNKNPRSFYADFAAAMVRMGDIRPLTGRNGEIRKNCRVPN

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: 322 Sequence Mass (Da): 34600

A0A1C9P7I0

TLYFIFGAWSGMVGTSLSILIRAELGXPGALIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALTLLLTSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGITFDRMPLFVWSVAITALLLLLSLPVLAGAITMLLTD

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: 196 Sequence Mass (Da): 20921 Location Topology: Multi-pass membrane protein

A0A1W5LC88

YQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGSLGMIYAMMAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQMNYSPSMIWALGFVFLFTIGGLTGVILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGLIQWYPLFTGLTLNNKFLKIQFLVMFLGVNLTFFPQHFLGLAGMPRRYSDYPDAYSTWNIISSIGSLISLLAIIFFLFIIWESMISSRKSINAINMSTSIEWLQNMPPAEHSYSELPMLTNF

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: 284 Sequence Mass (Da): 32089 Location Topology: Multi-pass membrane protein

A0A2S1CR63

TLYLLAGAWAGFIGTALSMIIRLELGSAGSLIGDDQIYNTIVTAHAFVMIFFMVMPILIGCFGNWLVPLMLGAPDMAFPRLNNMSFWFLLPALVLLLMSSMVESGAGTGWTVYPPLSGNLAHSGSSVDFAIFSLHLAGISSLLGAVNFISTLGNLRIFYMGLDNVPLFGWAVFITAVLLLLSLPVLAGAITMLLTDRNLNSSFYDVGGGGDPVLYQHLF

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: 219 Sequence Mass (Da): 23446 Location Topology: Multi-pass membrane protein

K4A6T9

MRRSPGPGAPCRRRAIQGFVALFLAYALVVLLLESPLVSTSLPGAAGASAAASRKLHLDGAWEGGRAAPARPSKHPHRETLSADGGRRRSGIVSGLELRHLNSTRSGSLRKVAAEAAELGARVFSDLQTLATTLPSLEDSSDEEEKSKCPHSIVLSGDEFRERGRAVELPCGLTLGSHITVAATPHEAHPERDPKITLLKDGEEPIMVSQFMMELQGLKTVDGEDPPRILHFNPRLRGDWSGKPVIEQNTCYRMQWGTPLRCEGWRSRADEETVDGLVKCEKWIRDDERRLEESKTSWWLNRLIGRTKTVSVDWPYPFVEDRLFVLTLTAGLEGYHVNVDGRHVTSFPYRTGFVLEDATGLSLNGDLDVQSVFAGTLPTTHPSFSPQKHLEMLPSWQAPPLPDEPVEIFIGILSAGNHFAERMAARKTWMSAAHKSLNVVARFFVALHGRNEVNAELKKEAEFFGDIVIVPFMDSYDLVVLKTIAICEYGVRVVSARYIMKCDDDTFVRLESVITEVRKIRNGESLYIGNMNYHHKPLRNGKWAVTYEEWPEEDYPIYANGPGYVISSDIADSILSEFVNHKLRLFKMEDVSMGMWVERFNNTRLVKYVHSVKFCQFGCIDDYYTAHYQSPRQMLCLWDKLQAGKAQCCNMR

Pathway: Protein modification; protein glycosylation. Subcellular Location: Golgi apparatus membrane Sequence Length: 652 Sequence Mass (Da): 73320 Location Topology: Single-pass type II membrane protein

A0A0K2TK56

MTTRLLVCLTVLSTISGWRSKNINGEYWKSFDIFKTCKHGRKQSPVNIIKNDASIMQCAPMNFSYYDHPNDFDILNNGHTVILTLKNGTSRIPHITGEQLPKGVFRFSQLHFHWGKNNTIGSEHQINGCQYPLEGHFVHFNTNYGSTLDEALKVNGVKDNLFVIAVLFHLSSQKSNSGLQPIIKSLKSIKKCQRKSTISKLNLRKLLPRKLTEFYSYEGSLTIPPCQEIVLWTVFKKRCPVSAGQMRTFRKVFNDGDTHMNIFRLPQPLNGRTVLYNRS

Function: Reversible hydration of carbon dioxide. EC: 4.2.1.1 Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O Sequence Length: 279 Sequence Mass (Da): 31935

A0A397ERE9

MDGVTASKDDDDDTTNYVELKTFRMLNTSKDRFTFERYKLLAFWIQSYLVGVPTIRVGFRNESFILTKEQAFETDHLPRYGDKHWCMTMSLSSTTPPFVKTPLSNY

Function: Decapping enzyme for NAD-capped RNAs: specifically hydrolyzes the nicotinamide adenine dinucleotide (NAD) cap from a subset of RNAs by removing the entire NAD moiety from the 5'-end of an NAD-capped RNA. EC: 3.6.1.- Subcellular Location: Nucleus Sequence Length: 106 Sequence Mass (Da): 12405

Q6GN39

MARFRPINVTVAGFFLLQTIFLILIYSRHTVLPDTETKTEKVHLLILSSWRSGSSFIGQIFSQHPDVFYLMEPAWHVWMSMFQNNAKVLHMAVRDLIRSVFLCDMSVFDAYIPNKKNVSELFQWAVSRALCSYPACSHFDREAITNETVCKIICKHNPFSKIEESCNTYSHIVLKEVRFFDLKVLYPLLTDPSLNLKIIHLVRDPRAVAKSREQAMKYLTRDNGIVLNTNGTKIDDIRYDVMREICQSHAQMYETAMDKAPSFLKGRYMLVRYEDVVRDPLREINQMYEFANLKLTAKLKNWFYNITHGVGPGTKKEEFQTTSRNAVNVSQAWRKDLSFQKIQKIQTICKSEMNLLGYQFIDSEKERKDMSMDFVLPKRNYQFSWLPNKEKK

EC: 2.8.2.- Subcellular Location: Membrane Sequence Length: 392 Sequence Mass (Da): 45969 Location Topology: Single-pass type II membrane protein

A0A1T0A052

MNKPVINVCDEFDGREQVRTLVLALGSNHHHERSFELALAKLGELGELDCSDVAASKDFTGKTERVYHNACVLLDAAAPNTVRAWIAATKEIERQCGRGDGQDVAMDIDVLAVQGSDGAWCVHQKRLPFKAHERTGLMQVAAWLI

Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 4/4. Function: Catalyzes the transfer of pyrophosphate from adenosine triphosphate (ATP) to 6-hydroxymethyl-7,8-dihydropterin, an enzymatic step in folate biosynthesis pathway. EC: 2.7.6.3 Sequence Length: 145 Sequence Mass (Da): 15939

A0A0K3CHL3

MSDDWSASAVQALQIRFARSKAQAADLSEDERSLVDPFSPIFVYPIYGEEETIFGYKGLTIDYRFASGSLNQYLNVSWEDKFPETTTVKADDPEKTLYEFIPPSYTKSLERFQETVEKDALEFKPLGKRVGAYRMKGEDELTGGGKGKGKAKSQGGPILPERSWEAIDDFENDGEDGVRYEAYWTNWDTPGFKEYHRKMQIFVLLFIEGASYIDEEDGRWEFVTLFERRKKGDSTSYHFVGFVSFYSFFCWPDTKRLRLAQFVLLPPWQGQGHGSALYSLCYRNILSRDEISELTVEDPSEAFEDMRDKCDLYTLISTNALDGLKAPLDRQFTETVRKKYKLADRQFYRLVEMMLFLSTDPNDEAQQRAIRLTVKKRLYLFNKEQLLQIEDKEERKAKLQETFESVEADYQRLTAKFVS

Function: Catalytic component of the histone acetylase B (HAT-B) complex. Has intrinsic substrate specificity that modifies lysine in recognition sequence GXGKXG. Involved in DNA double-strand break repair. Catalytic Activity: acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-lysyl-[protein] EC: 2.3.1.48 Subcellular Location: Cytoplasm Sequence Length: 419 Sequence Mass (Da): 48746

A0A1I8GHC0

MQRKRKLWEINMSSRRQVHFLDAKENGCTNNAQQKQQSLQQRKEKQSPSKASWDQLEILGGVKIFPQGLCSMSFLRYLYMSHNRISVIPPEIAQLKNLVHLDLSYNMVKILPPEIGEITELKELHLQCNQIRCLPMQLGRLFQLTVLNLNHNPLNPDMLQLYNSETTQSMLSWLLDSEGFAMTPPPSRKWCYLGGRSNTDSISRNGHASAPNNSQSTTSGSNGTTSGANGSSIHGTAFTVMCYNVLCEAYATKKQYPYCPSWALQWEYRRRGIMDELRAYQADILCLQEVETEQFGVFFRPELAKAGYEGIFSPKSRARTMTANESKYVDGVAIFWKRDRFTLVKEDLIEFSQMAVEKYEKDCKANHQMINRVMVRDNVAIMAIFEVLEESTGQRRQLVVSTAHIHWDPEYSDVKLIQSIMLLSALWKKIENHLREQNPQADKVDVASMPTIICGDFNSLPDSGVFEYLSRGRVNKSHLDFKELGYAKILDKLTPRRSQLAPTEEHLEHDFNLLPCYFGSNNCTNFTYGFRGVIDYIFFTADHFNNIGYLDMIPESWFAQNGILGCPHPHISSDHFSLLAELELLPASGSSSNHGNGDERQTS

Catalytic Activity: Exonucleolytic cleavage of poly(A) to 5'-AMP. EC: 3.1.13.4 Subcellular Location: Cytoplasm Sequence Length: 603 Sequence Mass (Da): 68804

A0A819Q138

MDNITLQKQVENLRQQLKVDRAPLSRTLMERIIPNACLVEKQARILSLKIQPLSDSCRPRSKTQADIMDKSSLQKQIDSLRYQLRVEKVPLSKTLQELKRYIQENEQADPLIHPPDKKSNPWAEKGKCTVI

Function: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction. Subcellular Location: Cell membrane Sequence Length: 131 Sequence Mass (Da): 15188 Location Topology: Lipid-anchor

A0A2E4X165

MRVRLFCKKSSAQAEALAQDLIDHRSEDLDIARLQDDEILQKDDLALVLGGDGTLIQWARRWGSSGASVLGVNLGRLGYLTPFAPGTAKAALDAALAGELERESRMRLRVVSDSLPDLGPALNEVVISGKDAGRIGEFSLRREGKALARLRGDALLVATPTGSTAYALSAGGPVLAPDLEAMVVVPVAPHSFSFRPLVLRPDERIEVEIHGEGWVSVDGQARFALEHGQIVEMTRAPSPITLLRQRTDDPLDHLRKKLGWGLSPQT

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: 266 Sequence Mass (Da): 28718

A0A109L1B7

MDVLNSISLERLESTQADYEISRLRECCVNDGFFYLADHGIRPSLIADALETARQFFALPLSTKNQFCQDRQVVIPKTCRGYVDTFGETLHPPTGPDRKQHFDMGREAPACDLPFTGPNLLPSEGQAPGFAKSMLALQQEVLDRVVPALLRGLALSLGLDRDFFQAFFSNPVLIQRALYYPPSGSGAGKHTDNGMFTLLFQDPRDACALSAFSQGRWIDVPCRANEVVVNLGDMLMKWSNGLFTSTPHQVIHRASSARVSLPFFVYPDIAAVFTPLGSDQTVACRQVMLDNFNSIWVSGQGAGRAREFA

Pathway: Alkene biosynthesis; ethylene biosynthesis via 2-oxoglutarate. EC: 1.13.12.19 Catalytic Activity: 2-oxoglutarate + 2 H(+) + O2 = 3 CO2 + ethene + H2O Sequence Length: 309 Sequence Mass (Da): 34144

A0A251SR57

MAMTNTKAAALAVGFIFLNLTCVLGGLQYGFYDGKCETSDVEAIVRNTVFSEFLVDQTIAPALIRMHFHDCFVNGCDASILLDGHNAEKTAPPNLSVRGFDVIDAAKAAVEGVCPGVVSCADIIAIATRDVVALSGGGRYTVQTGRRDGLVSLAENTIVLPAPNASVSSAIHTFASKGLTATDMVYLSGNCFTEFLSHVL

Cofactor: Binds 2 calcium ions per subunit. EC: 1.11.1.7 Catalytic Activity: 2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O Sequence Length: 200 Sequence Mass (Da): 20994

G9D7H7

MNNLSFWLLPPSLFFLLMSSMSDTGVGSGWTIYPPLSSISGHGGVCMDFAIFSLHLAGASSIMGAINFISTIINMRLGAMKMDKVPLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPSGGGDPILFQHLFWFFGHPEVYILILPGFGMVSHIVSSSVGKREPFGALGMIYAMAGIGLMGFLVWAHHMFSVGMDVDTRAYFTSATMIIAVPTGIKVFSWMATLFGSYFKFDAPLMWSMGFIFLFTIGGITGVILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMSGITYWFPLFFGMMMNPNRLILQFLVMFVGVNMT

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: 328 Sequence Mass (Da): 36059 Location Topology: Multi-pass membrane protein

A0A146PQQ5

MPQVDKTAKRLWARHSSETIFSPIWEQPFNIEPFAFEGKRIPFKMTDVDRARRKRWLKELRLNPDDVKNVPELKKLLYNPIRRFIRAPLDWVFTKYXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXGLGIFGPYNGVARKLVPKLGYIYLTFLSLTYAMIYHSNDWEMRHTNQIRMKHLRVSDDPEYQKERKPQDFSDRKFQKRKVFTGPQFAY

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: 221 Sequence Mass (Da): 26364 Location Topology: Single-pass membrane protein

F3L1P2

MKKAPLVMMMAGGTGGHIFPALAVAKALEVKGYRVSWLGTQAGLEARIVPAAGIPLHNLSVRGLRGKSLTRIVSGVARLIWSIEQATFLMLRHRPSLVIGMGGYVAAPGGVAAMLMGRPLFIHEQNAVAGSTNRWLRRIASRIFAAFDGAFNASVNAEVVGNPVRAEIVAVGEQRQAFDGQRDLRVLVLGGSQGALAINRVIPDAVAQFETNEASDGLSVWHQVGQAHMADVGAMYAARGITHVRISPFIDDMAAAFAWADVVVARAGALTCSELLAAACPAALIPLPIAIDDHQRKNAQHLVNAGAAIVIEQDTLNAADLSSQWAQWLRQPETLAAMSRAAKQAAKTDATDRIVQACEEVLGGA

Pathway: Cell wall biogenesis; peptidoglycan biosynthesis. Function: Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II). Catalytic Activity: di-trans-octa-cis-undecaprenyl diphospho-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + UDP-N-acetyl-alpha-D-glucosamine = di-trans-octa-cis-undecaprenyl diphospho-[N-acetyl-alpha-D-glucosaminyl-(1->4)]-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + H(+) + UDP EC: 2.4.1.227 Subcellular Location: Cell membrane Sequence Length: 365 Sequence Mass (Da): 38507 Location Topology: Peripheral membrane protein

A0A126G1W9

ALSLLIRAELGQPGALLGDDQVYNVVVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGISSILGAINFITTAINMKPPALSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLLWFF

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: 207 Sequence Mass (Da): 22146 Location Topology: Multi-pass membrane protein

A0A1F2PLG6

MIKTENLTYQYPDGTTALKGVSIDGSRGNCIALIGENGAGKSTLMSALIGLLKPTGGTVFFKDQPLSYQKKKLYEFRKSIGLVIQESDKQVFYSGIYDDVAFALRNMGMAAEQIDQRVQAAMEATGITQLADRPVHYLSYGQKKRVAMAGVLAVEPEIILMDEPTLGLDPKSKAGVKAIIEGALAKGIKIILSSHDMDFIYEFCDYTYVLHHGGVLVEGETTDVFKNTEALETASLEQATMTRLEQCLGIKGFRSIAALEEAIRNQKKEVQTDETGSSGH

Function: Part of an ABC transporter complex. Responsible for energy coupling to the transport system. Subcellular Location: Cell membrane Sequence Length: 280 Sequence Mass (Da): 30543 Location Topology: Peripheral membrane protein

A0A1S3GVX4

MLNYDYVWDMIFHPNGAIEVKVHTTGYISSVFLFGDALKYGNRVGEHTLGTVHTHSVHFKVDLDVAGLENWVWAEDMAFVPTAVPWNPEYQIQRLQVTRKLLETEEQAAFPMG

PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue. Cofactor: Contains 1 topaquinone per subunit. EC: 1.4.3.- Sequence Length: 113 Sequence Mass (Da): 12938

A0A3B6EDY5

MEAKSSSIKKETEAMEEAERVVKKQNVTMAMEVFDCPVCSTPLRPPVFQCALGHFVCSPCRDKLPDSKCQACSGVVLKSSCYGIERIVESILVPCPYAEHGCTDMITYYLKGEHKQACPHEPCYCPEPGCGFAGTTAALLDHFTSQHKWPTTVFKYYVPFDLIAKPGMHVLRAQDGNLFLLNVSSPESVLHGISLVRIQPKVSELSRFGCSVGFSCWKGHYQLSSLDAITSTSLSDGLPKSSFFSFVPKSSAVLTVTIDMELMCDINDDELEEETSDDDDSYGEEDGGEE

Pathway: Protein modification; protein ubiquitination. EC: 2.3.2.27 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. Sequence Length: 290 Sequence Mass (Da): 31916

A0A7M7R8B7

MSTQFPHYIAVIVLLLLKSIMDSDGKELISVIQWGCIGNQSIEKYTLKNKVGQEVDIITYGATITSIRIPDKYGNIADIVLGFDSIEEYMMPYNPYFGATIGRVANRIKKGEFTLKGKKYHLTKNEGQNHLHGGTKGWNSKIWHADVQYNQLVLSLLSEDGDEGYPGDTIASVIFQLTKDGELCIEMKVFVTKATPINLTNHSYFNLAGHTGNASELYKHQFTINADHWTVTDAESIPTGEIRSVDNSVMDLRNSTILGDVIDKVPGGGYDYNFCLTMNDTENEKNLVATVLHPTSGRYLKVFSNQPGIQFYTANFLPESNSTGIRGKNGSEYFKHAAFCLETQNYPNAINHENFPNSILEPGKIYHHTVVYKFGIIV

Pathway: Carbohydrate metabolism; galactose metabolism. EC: 5.1.3.3 Catalytic Activity: alpha-D-galactose = beta-D-galactose Sequence Length: 378 Sequence Mass (Da): 42255

A0A3B6JBS9

MSAAQIRAEINGLIASKFAEGTVDQYFLQLYVMRRYKKIRKGMVVEVMERFLQDADKILTEIAVLLNEPQLDYDKVEGIADQLEGCSSSSVGAKRVNLSCVEYFHPEAKTEEGNQPVVDFDKVDALVQQLKGCSSSVGANKLSVSCMHFRRFNHSKSKEGYLIALAPIMNEFCDVRNMFLTILQMEEQVDALGPKY

Function: Functions as two-component phosphorelay mediators between cytokinin sensor histidine kinases and response regulators (B-type ARRs). Plays an important role in propagating cytokinin signal transduction. Subcellular Location: Cytoplasm Sequence Length: 196 Domain: Histidine-containing phosphotransfer domain (HPt) contains an active histidine that mediates the phosphotransfer. Sequence Mass (Da): 22071

A0A662IWY4

MVSELLKDVPGERLFLLGNEAIARGALEGGVQVAAAYPGTPSSEILMTLASIAKDAGIYVEWSTNEKVALEVALAASICGLRAMCSMKHVGLNVAHDPFVTAGYIGAKGGFVVVSADDPWAWSSQNEQDNRWVAKQAYIPVLEPSDVQEAKDMMAAAFNLSEQFNHVFMLRSVTRIGHARGDVTLGPLFKEKRKGVFKKDPSWLTYVPATARKNRPLMIQRLEKIKKAVNGWPFNKLDLVDGAKLGIIASGLSYAYAIEAVKWLGLEGKVSMLKIGTTHPIPEELTKKLLSSVEEVLVIEELEPFVELHVKALACEEDIKVKVHGKDLIPVIGELSTRIAVEAIAKLTGTPTPVDFSMLDKVSSEVAPILPFRPPIMCPGCPHRASFYAIKVAAQRVIKSYGEGVEPIYPGDIGCYTLAFQPPLSTVDTTICMGGSIGIANGLAHVVNAPIIPCLGDSTFFHAGIPPLINAVYNKAKITVVVLDNLTTAMTGFQPHPGTGLTAMGDSTVRLKPEDVARGCGVEFVEVADPYDVKKAIDIMVKALKFEGPSLVVMRRLCALEALRQKRKKGEKIVPYTIDQEKCKKCDVCVKMFACPSIVKTGDTYTIDPITCVGCGVCAQICPYKAIIPLEEG

Cofactor: Binds 2 [4Fe-4S] clusters. In this family the first cluster has a non-standard and varying [4Fe-4S] binding motif CX(2)CX(2)CX(4-5)CP. Function: Catalyzes the ferredoxin-dependent oxidative decarboxylation of arylpyruvates. EC: 1.2.7.8 Catalytic Activity: CoA + indole-3-pyruvate + 2 oxidized [2Fe-2S]-[ferredoxin] = (indol-3-yl)acetyl-CoA + CO2 + H(+) + 2 reduced [2Fe-2S]-[ferredoxin] Sequence Length: 633 Sequence Mass (Da): 68405

A0A657APS2

MPKVFLNLGSNVERDQNFRSGLSSLKRTFGDLSLSSIYESEPVGFDGACFYNMAVSIETELSLPKVIKALKTIEDSHGRLRGDKHFAPRTLDIDVVSYGQLTGFHDGVELPRPELYYNGFVLWPMAELAPDDIDSKTGLSYQVLWQLKQVEIEAKQKVWRIDPSSVAAILKP

Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 4/4. Function: Catalyzes the transfer of pyrophosphate from adenosine triphosphate (ATP) to 6-hydroxymethyl-7,8-dihydropterin, an enzymatic step in folate biosynthesis pathway. EC: 2.7.6.3 Sequence Length: 172 Sequence Mass (Da): 19307

A0A536YAH7

MPDLTAKKKRPLWYNLSPLNLPVPGLVSIFHRISGVLLFLGLVAFLYLLDLSLASESGYAQAGEYLRTPIAKLLVIASIWALLHHMCAGIRHLFLDIDVGTSLHAARRSALAVFIVSLALTASIAVRMW

Cofactor: The heme is bound between the two transmembrane subunits. Function: Membrane-anchoring subunit of succinate dehydrogenase (SDH). Subcellular Location: Membrane Sequence Length: 129 Sequence Mass (Da): 14163 Location Topology: Multi-pass membrane protein

A0A158PJK0

MNVSSKAVVGPGSCGAVKSKALPPRFQTQNDLDFLKSEVAKNVLSSSEHSISRLRRIQKYMIPLVLNEISFLAIGPSGSGKTCGYLLPLINKLIELKEMVVSLEFVRFFVIEDFERCVEKSFYKEDLTILKKHLSESEAIPVCIFLSNAVHEKGIFDINFMKELAKTKLTKLMVSSLSDNESISCILFELPVDSSSNFKRRLLDLSAKLNYSGRIHIMVDVDLDREKAKTILTANSSFNEESHLRNEALQFLEELDQRVPEFLVDMLSCVGEPSTEVELPHSSDVSNGQQVGAKPSVEFGERHFIGRTNTPLVLILGNTQNLMYQTFKFACSMAGYEPYAKVARCGVRIFDLFAGKGTLRLNRMDTVRDEIVVATTGGVLKGFEQNKLDFSNLEMLIIDEFDKMVDEVHGFGRDLYQILAKIPARPTVAGFSATLSDENSVRTLSDLELKLFRRLRTSWRLRVSGGISITLTKFSRPALIKQRFIAALISFEIKGNRNGAEKAEYLPNEPYWECGFTKNLSLLVGLIESDLALHKMKKGGPYKKSTVIFVERKRTSNYLALFLLQIGYDFEPMNASYKYFYLWPISTAKNVTKTVLLDDIYLVGLVLQFRDYTLDDNETTLRRMKTGKIQGVVATNKLARGQDIPEVDHVIIYEMSTDFSDYKHRIGRTGRMGRGGRSTVMLSSKSDRALVNPLVRKRSGLELPFAKDYWFYRIVPTKVPSLCGGQLVANYHDRVALKLDSDQ

Function: RNA helicase. EC: 3.6.4.13 Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate Sequence Length: 743 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): 83870

A0A497GJG0

MRGEPLTSEDVRRLDENAQLLGLTALQLMENAGRSVADIISSHINIKGKNVVVICGLGNNGGDGFVVARHLANKGAHVDVILVGSAEMIRTDEARHNWAILEGMELSIRLHEARSTDEVKEYKDKIMNADVVVDAIFGIGFKGTVREPYRTAIELMNKSKGFKVAVDIPSGIDADTGEIGGIAFKADLTVTFHAPKVGLDKAKEYVGKVVVADIGIPKEAEYIVGLYDVRKCFKTRDPLSKKGDNGRVLIIGGSRLYSGAPALSGMAALRAGIDIAVITTPKSAAWIIKTFSPALIVWPLKSDEYLGLDDIEYIMSVKERFDCIILGPGLGLNEETMEAVREIVRTVDKPMVIDADGLKALKDNLDLIRNKQVVITPHAGEFAIVTGINVSNMSWNERMEIVKEIARKYNITILLKGKLDIISDGKKVRINCTGNASMTVGGTGDTLTGIIGAMLSRGINTFDAACAAAFINGLAGELASEKYTYITPLDLVQEIPEAIRIACERKLIIPSRIYRNLLSRIRGEVKSER

Cofactor: Binds 1 potassium ion per subunit. Function: Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. Catalytic Activity: (6R)-NADHX = (6S)-NADHX Sequence Length: 529 Sequence Mass (Da): 57473

I1H7Q3

MQAIRAVLLGIAVVLGLGGVPGGEAQLDEKFYDGSCPGVHRIVRRVLKEAHQADVRIYASLTRLHFHDCFVQGCDGSILLDNSTSIVSEKFAKPNNNSVRGYTVVDAVKAALEEACPGVVSCADILAVAAKISVELSGGPRWRVPLGRRDGTTANLTAANHVLPSPRDNITMLQRKFRAVGLDDTDLVALSGAHTFGRAQCQFVTDRLYNFSKTGKPDPTMDAGYRVQLARSCPRRHGNRTALRDLDPATPDAFDKSYFTNLQASRGFLQSDQELLLAPGAPTAAIVARFAGSEKAFFRSFASSMVNMGNIRPLTGGQGEVRKNCWKVNGS

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: 331 Sequence Mass (Da): 35690

A0A074ZZ64

MSWNNIPADPKQPLLFPDVDYPRQPNFIEKDVNPSVRVKLDAESTTPYRRTRDVDLTDWDDDAAAHLRSTADTPGDLIDCLSPCRGILGLRKPSKRKFLSLRQLSRFRRPFGVIWLVRDVCGIVCLVFTWVLILYAEFVISSVILMRAPSSSFCWITGSMYHLFVSLACISHIFAFSTDPGTVPIGNATREAGIFLCEVYGDPRPPIIRCPKCLCIKPPRAHHCRICFRCVRKMDHHCPWINNCVGEANQKYFVLFTLYICLQSTMAIYMCVHFVVQCIESDWEACQLNTSHHGWSHLLAFEFSPFVTCVFILGLIVEAFVFGLFTMIMFITQVYSIADDETGIESLTKNGPKSEQLSRWKRLTLACGSPFSWRWFSPFSPPPPVTPVFPGFGGRGEDFVYSDSGTPTNLTDLSYSSCVVMATTSPYSRKEHNDVIGNGVPNSVIAL

Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein] EC: 2.3.1.225 Subcellular Location: Membrane Sequence Length: 447 Domain: The DHHC domain is required for palmitoyltransferase activity. Sequence Mass (Da): 50432 Location Topology: Multi-pass membrane protein

A0A3B6FJR6

MAEVVQVHKDWVGSFPSGKKITVVFVIGGPGSGKGTQCAKIVSQFGFTHLSAGDLLREEVKSDTEQGATIKNLMHEGKLVPSEIIVRLLLKAMLASGNDKFLIDGFPRNEENREAYEKIIKIEPEFALLIDCSREEMERRILHRNQGRDDDNMETIRRRFEVFQQSTLPVIQHYEKMGKLRRVDGDRQPDMVFEDVKAIFAQLNTQANQGSNVSRAQTNPFKSWFLDIFCSCFDVADRRN

Cofactor: Binds 1 Mg(2+) ion per monomer. Function: Catalyzes the phosphorylation of pyrimidine nucleoside monophosphates at the expense of ATP. Plays an important role in de novo pyrimidine nucleotide biosynthesis. Has preference for UMP and CMP as phosphate acceptors. EC: 2.7.4.14 Catalytic Activity: AMP + ATP = 2 ADP Subcellular Location: Cytoplasm Sequence Length: 240 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): 27337

A0A2U3PYW3

MRIDVSLLPALAASFMLAFARVGAMVMLLPGLGETNIPTRIKLSIALLLTLIILPLHRNAYHVDMGSLAPLLVLMLHEIAIGIVLGATARVTLSALQVAGSVIAQQMGLGFVTSVDPTQGQQGVLVGNFLTMLGVTLLFATDSHHLVIAALNDSYTIFSPGETVSSGDVASLATRAFAAAFRLGLQLSGPFLVFGLVFNIGLGVLARLMPQMQVYFVGVPLSIFAGFLVLAVVLTAMMGTFLDYFIGVMHQMMPLK

Function: Role in flagellar biosynthesis. Subcellular Location: Cell membrane Sequence Length: 256 Sequence Mass (Da): 27084 Location Topology: Multi-pass membrane protein

A0A3B6PQR9

MANTGLSRRNSCPKVHSALCSELTMMLDKISSILPSIEAARPGCRAGIQELCNLYHIVEKGRLITQHCIECSKLYLAITGEAILSRCERVRDSLKRSLFLIQNMVPTVLANQIADVHNDLRDVKFSVDPLEQEAGKSILEMLRQSDATEELLLQTFMQAASKLNLTSPKAILIERRAIKKLLDKITGTDQKKEQVLKFLLHLVTKYGKNVKPDTGERNENLQSESKSLSPSLSLASDASTPEKCDKPTYFQGYEYQSSMSGETTPPTEFCCPISTKLMHDPVIITSGQTYEREYIEKWFSEGYNTCPKTQKKLENFAMIPNTCMRDLICNWCREHGFTISDFLPSKDSYSYLPEQLHGHSMSSLHNVSVPLIAGNARNFVIDHSSSSVAFSDASYVSDSSHVKDMEEPKDTFSQFSWSVDYQKHLSFHNFNQCMFLRFFCELSKLPLEIQGSSIKDLKNILHDDDDVSWAMASHGFVEAFLEFLRNDSSSYSMKAQQAGLHFFLNFLSNSRAKIPSMDEEAFRLITSFLSSELKTEALLVLHELIRHLSRQQSCQMASVVTPPVLAILASEDIEGLELPLKIICDLSSDADVKSELISLGIISKLVPILAEGSFVECCLEILRNLCDMEEAMVLITRTDRCLGSIAEYLDTGSPKERELAVIILLAICSRSVEDCSQVMKEGVIPALVDLSVNGIDEAKSCSFKLLNLLRDMRQSELNNSCSQEVAAAAEVIEDPPTESPIHRRPASKSSGFFQRKLNIFSKPRSLTLF

Pathway: Protein modification; protein ubiquitination. EC: 2.3.2.27 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. Sequence Length: 769 Sequence Mass (Da): 86157

A0A3B6LPX2

MIRWGDVYKVVAAMAPIYFALGLGYGSVRWWKLFTPDQCDAVNRLVAYFAVPFFALDFAARMDPYALNYRVLAADALSKLAVALALAAWAAASTHCCRGGGKRGGELASSWCITGFSLATLTNTLVVGVPLLDAMYGGWARDLVVQISVVQIIVYFPLLLLAFEARRAWGGGPGKPGAEAALASDGDVEDGGAEDSRQRQPVWPLVRAVWLKVARNPNVYAGMLGVAWSCITNRWHIETPSIIEGSVLIMSRTGLGLCMFSMGQFMALQERVVACGAQLTAVGMALRFLVGPAATAAGAVALGLHGDVLRVTIIQAALPQAITTFVFAREYGLHADVLSTAVIFGTLMSLPVLIVYYIALPFIE

Function: May act as a component of the auxin efflux carrier. Subcellular Location: Membrane Sequence Length: 364 Sequence Mass (Da): 38967 Location Topology: Multi-pass membrane protein

A0A139JR63

MFYNNLLKESFFLSNFQLKQLEKYYFFLKSYSNKINLTSLLSEKEVYLKHFYDSFLVSKIINLIKFEHLCDLGTGAGFPGIPLKILYPHLKVFLLESISKKIIFLKKLVSILNLSNIFIFHHRIEEHKNKYNFIITRSLGKMDVIFKLSSLVIKKKGYLIAMKGPNYIEELKNIKKKFSFHLKKKKKSELPFNLGKRVNLLFQKK

Function: Specifically methylates the N7 position of a guanine in 16S rRNA. EC: 2.1.1.- Subcellular Location: Cytoplasm Sequence Length: 205 Sequence Mass (Da): 24311

W8C3N7

MREVVRLGFDLNGAWRISKANEEFKLCPTYPKKILVPGCITDDTLQIVANYRASRRLPSVVWRHKRNGAIIARCSQPEVGWLGWRSESDEQFLKALADACAFDRGEQMRRLMQTARSAVPAMFLPPDTQPTNADVESHEEVSLDEVRKVLIVDARSYTSAIGNRARGGGCECIEYYPFAEIQFMCLGNIHVIRKSFHALRTLCAAPPTDANWLGLLEKTNWLQHLSGLFAATTTVLQAIEKKGCPVVVHCSDGWDRTPQIVATAQLCLDPYYRTVEGFRILVEREWLSFGHKFAKRCGHGPESDDLNERSPIFIQWLDLVHQLHIQFPCSFEFNRAYLIKLAQHLHSCLFGTFLGNSYKYRLENSIFERTFSVWPFLSGPMYRNPLYLPSRDAVLWPKYNVRDLHLWTEVYMGSLGNQNYNDLINGSSEIEEQSNDLASVMSNVPVRSFSDPNVVAQQLQTEATNSANSSEREDSPDNAAGAIPKIQERNSHQNNRAMAADELQSLNERKELHENLTNAEDTHRQDNSQFSTNGNAKNGTNEKKSKNSEGDNNLYDFHTCASAQGSDTASNTNDQQNTLTSNENRSITPPGKEANARNDFITPEKLSTAADKEELGLSSPYVLLKSENQSPSTSGNNATRKNMSNSGVNNSILQKMNGTNGTSNCSKFLSKSSSNGSVSSTSSSLNNRNNSNSNSSLATTDRSCDNKSENKDEVDSEVDGAVGISNTQRHSNDSMNDSIIISPTHRKLEISPSGRCEAISNSGSSVPATPTDSVDKASTSSNGDNSRQRGTVAATSASDTQRCGRPRLEK

Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + phosphate EC: 3.1.3.64 Subcellular Location: Cytoplasm Sequence Length: 810 Sequence Mass (Da): 89757

A0A147E9G4

MGFSRGVRMGVDVGNARVGLALSDPDGILATPLKTLKRNLNTDSDRRVLRRLLEIHEVAEVYVGLPRTLSGGSSASTQMAEDYASGLVAELAAEGREIPVWLVDERLSTVSAQRSLHEAGVSSRRFKTMVDQVAAVAILQQSLDALKADRAVAGYRVEAPTVPREDARSQHLDPTSEPRPEQNGDPA

Function: Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA. EC: 3.1.-.- Subcellular Location: Cytoplasm Sequence Length: 187 Sequence Mass (Da): 20169

A0A7S3N2X0

MTRDDLKKWSHRLHMNQPPNLFGKDKVPYRTIGYSFFLFLVGTIFLCLGFMDYVETGSMTTATSEESGRPYEKLLLGALMFIPGSYHVFVGLLAYLKVDGFKYKDVASFESDQWWNDHCD

Function: Involved in trafficking and recycling of synaptic vesicles. Subcellular Location: Cytoplasmic vesicle Sequence Length: 120 Sequence Mass (Da): 13894 Location Topology: Multi-pass membrane protein

A0A183LVI7

MVFRLDPCEQLLNPLFYHLPFLYSFWAILNTICFNIVASLLLFSHICAAVTDPGLIPLHRYTVSQLASVQKPDGWTTCNKCGIHRPPRAHHCRICRRCVRRMDHHCPWLVIYVCI

Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein] EC: 2.3.1.225 Subcellular Location: Membrane Sequence Length: 115 Domain: The DHHC domain is required for palmitoyltransferase activity. Sequence Mass (Da): 13404 Location Topology: Multi-pass membrane protein

A0A672FDE9

MSQPAEAGCCPDGYRALSTAELRELLRDDGKMERIIRLDEKFQELQLDRESLLTSNRSLAEESLARKPRLRTGTLQLAHSYRELARLAAACGDKQSRLEGGVQRRGLQTAQNLLQEEVTRAEEQSEELLERFMEGTVDLDRFLDSFQSSRKTYHVRRAQAEKLQEFIQSRRQGGGGGRPGPPQGQRAAAGPPQAQRLHGTGPAPGLPGPLRPDARHPAAPLPRRPPGPRPRPRPGPPAGTCPAAAARPARRPAGHRTAVGRLAGRRAAGSSPAAVQAPAARAPLPIDHRGGGGAQAPGPDPGPDPGPDPGPDPHQTHAGRDAPVCLRLHTA

Function: Component of the ESCRT-I complex, a regulator of vesicular trafficking process. Required for the sorting of endocytic ubiquitinated cargos into multivesicular bodies. May be involved in cell growth and differentiation. Subcellular Location: Endosome membrane Sequence Length: 331 Sequence Mass (Da): 35421 Location Topology: Peripheral membrane protein

A0A0Q3PR06

MANASRRPATATMALLLLLVLLELAAMTGLSQGQLQVGFYSESCPDAEDIVSSAVQDAAASDPTLLPALVRLQFHDCFVRGCDGSVLIAGAEVKNSKHQGLRGLDVVDAAKALLEEQCPGVVSCADVLALAARDAIGMTNGPSFDVPTGRRDGLASNVRDADVLPDASDNIQTLRSKFATAGLDDRDLVLLTAAHTIGTTACFFVKDRLYGASGSDPGIPAGYLAELKARCAPGDFNTRVPLDRGSEARFDGSILRNIQAGLVPIASDAALVADNATAALVGAYIGSPRFRRDFVGAMVKMGTIGVITGGNGEIRDVCSAFNTN

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: 324 Sequence Mass (Da): 33640

A0A7C7HEX0

MINKKLDYRANSSVIRKLVLRCLVQLERRNSQIAPVIDMVIRQNQLNNVDRGLLTEIVYGAIRWRGHLDWIIRQFVKPDFQLDLQMRNILRIGVYQLLYLDKIPAHAAINETVKLANQKGQKSKNFVNAILRSIQRSTNSLTPPRFKLDPISHISTKLSYPGWLVKKWIRQSNPEWTLKFCHASNQVAPVSIRTNTLRTDRKKLAKSLQEDGNQVVESQISPDGLLLTKTNPIRSLSDFQAGLFQIQDEAAQLVSHLLDPQEKSQIVDLCASPGGKTTHLAQLVGNVTNIVAIDLSTKKIKRIQENCKRLGITNVRTQVANATTDEIKALATADSILIDAPCSGTGTLRRHPDIRWKRTAKQIVDLANLQLEILIKTAMQIKSGAVIIYSTCSTEVEENQGVITRFLEVCPQFAVEPAHDFLPFLPADAITSEGHLQVFPHTHKVDGTFAVRLRKND

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: 457 Sequence Mass (Da): 51468

B2C5W3

MAYSSINNLGWTIMIMALSPNLAVMNISIYIIMTTPIFLMMTSTSTKTLQNLATTWTTSTATTLSIALLMLSTSGLPPFTGFMPKMLALNELITQKLTALATLTIMTSLISLLFYLRIAYLTMMLTPPMTTPSSTKWRTQNQKSQLMTMMTPTALFITHLIPAIPF

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: Membrane Sequence Length: 166 Sequence Mass (Da): 18386 Location Topology: Multi-pass membrane protein

V4L1I2

MSFVDRTHIHVTAGDGGNGCVSFRREKYVARGGPDGGDGGRGGDVILRASAGVRTLAEYGRKHHFKAAPGGHGSGADKHGKSGADCILEVPVGTTVYAKNDEARVLADLVSDGQYYVAAKGGRGGSGNRQYAGGARRAPKFAGKGKAGEQRWLTIELKLIADIGLIGMPNGGKSSLLAALTAATPKVADYSFTTLAPQLGVLQHGFMEPLILADIPGLIKGAHAGKGLGHHFLRHVERTSILVHVVDCALGDFERNYHAINEELSIYDRSLIGRVKIVVLNKIDLLDDRQRAEVYEKAGHFAAGVVGVSARTGEGIDTLRGTLIEAASESSDDRSGV

Function: An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate. Plays a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis control. EC: 3.6.5.- Subcellular Location: Cytoplasm Sequence Length: 337 Sequence Mass (Da): 35425

A0A7M7IK12

MIQFKVSAPGKVILFGEHAVVYGKTAVAASIDLRTVLNFTELPEAEQVVKICFSKVNLFITIPLQQIQNFFFINKNVEFIENYEIFYNKIKEFVCIVSYANFQQKLSLEAFFYTLIYIAQKEEMEIKPFQIQLNTELAINSGLGSSASFAVCLAACFVHWSHLQKNIYKVFDFSTLDVISKYALNCERIMHGNPSGIDNCICTYGSIIEFKKGNYIQPINTNNIQAMKILLVDTRVNRSTKALLEKVLELKHTYPVIIDLIMDSIDNISKEAVKIIQKLKTFSNTNEFFLEGYKQLMILINMNQGLLATCQISHPSLDRICAEAQNYGLAAKLTGAGGGGHAYILLLPDTQPETISSISRKLIADGFTVKLTTLGCSGVQIN

Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via mevalonate pathway; isopentenyl diphosphate from (R)-mevalonate: step 1/3. Catalytic Activity: (R)-mevalonate + ATP = (R)-5-phosphomevalonate + ADP + H(+) EC: 2.7.1.36 Subcellular Location: Cytoplasm Sequence Length: 382 Sequence Mass (Da): 42825

A0A5Y4YMA5

MKILGVIPARYASTRFPGKPLADILGKPIIWWVYQQAKKSEKLTDLVVATDDERISKACDKFDIPNITTKIHESGISRIHEVSQKIAADLYVQINGDEPLIEPKIIDRIVPKTINKDFVANLICKIKSPNELLDPSNIKIIFDSNKKAIYMSRTPIPTPYKSLNFDYYKHIGVLAYAKSMLDFFVLSKPSKYEKIEGLETLRFIEYGKNFYCIEVENIKSLSVDTPKDLEEVESILKLRTKN

Pathway: Nucleotide-sugar biosynthesis; CMP-3-deoxy-D-manno-octulosonate biosynthesis; CMP-3-deoxy-D-manno-octulosonate from 3-deoxy-D-manno-octulosonate and CTP: step 1/1. Function: Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria. Catalytic Activity: 3-deoxy-alpha-D-manno-oct-2-ulosonate + CTP = CMP-3-deoxy-beta-D-manno-octulosonate + diphosphate EC: 2.7.7.38 Subcellular Location: Cytoplasm Sequence Length: 242 Sequence Mass (Da): 27684

I1HWH6

MSAPDGSGPEPVVMLHGDLDLTIHEARGLPNMDVLSTLLRRLCLFRPPRRSSRPLPPRSVSASDEEDNPSTSSSHHHRHHHLHRRRPRRPKQPHGPRHLLPTSDPYAVLLIPPATVLARTHVVRNADRPVWSARIRVPLAHAASRIVFNVRDADPFGSDLIAAASLPASDLLSGTPIVSRWLDLLRPDGRGGKPKPDSAIRISASFTPAYSSLSRGGGIIPAYFPERRGCEVKLYQDAHGGAAKGGCWEDVCMAVLGAQSLVYVAGWAVGARVRLARKGEMSPEMEEKAAEVMALSSAAGGGGGDEAASPELGEMTLGDLLKYKSQEGVRVCLLVWDDKTSHDKFFLKTGGVMGTGDEDTKKFFKHSTVMCVLSPRYPSSKLSMAKQKLVGTLYTHHQKLVLVDTPASDTTRRVTAFLGGLDLAAGRYDTPAHRLFAGLGTVFRGDVRNPTLGLGSGSGGGETAGPRMPWHDLHCRVDGAAAYDVLANFEQRWRKATRLNDALGRKRWMDDALLRLHRIPWILSPNNVAGAGEDDPALRVFPEDDDPRQWHAQIFRSIDSGSVKGFPRSWETQEMAERNLQCDKNVAVEASIHAAYVAAIRRARRFVYIENQYFIGSSYAWPESYYRSSAAGNLVPMEIALKVASKIYAGEDFAAYVVLPMFPEGGSPASGPAQEILFWQAQTMRAMYNIVADAIATAAGSSKLAGSRRAHPQDYLNFYCLGNREPLGGGDNGASRARPAPETTRWGTTTSSSSAPSASVATATALESARRNRRFMVYVHSKGMIVDDEYVLLGSANINQRSLAGSRDTEIAVGAYQPHHSGNSPRGEVYRYRKSLWEEHLGAAAMAAAAVESPEKEECVRMVNRTARENWERYAAEEATAEMPMRGHLMRYPVEVGADGSVGPLQGHEFFPDVGGRVLGSTNKLPDDLTM

Function: Hydrolyzes glycerol-phospholipids at the terminal phosphodiesteric bond. EC: 3.1.4.4 Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1,2-diacyl-sn-glycero-3-phosphate + choline + H(+) Sequence Length: 931 Sequence Mass (Da): 101541

A0A9J7LL07

MELMGEFDYEILSLPDDQATDCLYMNGTILHCTKEEFPDSYKVFETVTDYHRVAVSNRELRKVGGALSRLALLIPLTKTK

Function: Hydrolyzes N(G),N(G)-dimethyl-L-arginine (ADMA) and N(G)-monomethyl-L-arginine (MMA) which act as inhibitors of NOS. Has therefore a role in the regulation of nitric oxide generation. EC: 3.5.3.18 Catalytic Activity: H2O + N(omega),N(omega)-dimethyl-L-arginine = dimethylamine + L-citrulline Sequence Length: 80 Sequence Mass (Da): 9143

A0A7M7FYE4

MAMQVPTNVDPEQIKSVRDFVASYNKLIETCFLDCINEFTTRDVKAKEETCALNCMEKYLKMNQRISQRFEEFQMLANENILAAQKKLDSKES

Function: Mitochondrial intermembrane chaperone that participates in the import and insertion of some multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. Acts as a chaperone-like protein that protects the hydrophobic precursors from aggregation and guide them through the mitochondrial intermembrane space. Subcellular Location: Mitochondrion inner membrane Sequence Length: 93 Domain: The twin CX3C motif contains 4 conserved Cys residues that form 2 disulfide bonds in the mitochondrial intermembrane space. Sequence Mass (Da): 10847 Location Topology: Peripheral membrane protein

A0A199P8N7

MQHGQYLLLLGACLLLTLPLEFVFRARVYRRPLLTLRVIGVVLVLFGAWDVIAYHRGHWTYDAQYFLGISIPGGLPLEEILFFVAIPLCALLTYGAVGTCLGWLRRLRRGTGALARGPRDPRAPGAGEGPHA

Pathway: Carotenoid biosynthesis. Subcellular Location: Membrane Sequence Length: 132 Sequence Mass (Da): 14566 Location Topology: Multi-pass membrane protein

A0A2A6CX70

MPETATDGAPSVGGGGSSSRGGKGGGRSRGGGGNRGGGRTGNADSNGGNSRRGEGRGGGGGAGENNGRRSPQQHNHQQGGRNEQRKTKVGDHKVDMRKYERMITATQSNFSDIKATDPITEDCLICCKPNDIFGVGACRHPLCIECAIRIRVIANSEGCPVCRQPMEKMAFVFASANPTTASLSMPHIHPDEKRYKVCFQNKEASARYEQYLSHVCKLCVVDGERKEFASFVSLRQHMAATHQLSFCHHCVANLQLFSRERTTYSRAQLQEHIRGGDRDDRSQKGHPKCLFCEDRFFDEDDRYRHLRREHFFCQLCETTGAAANVFFGKHDELLKHYEAKHFLCEVDECKKAGIAFATKLDLDIHTSREHGKVNLAVDFSFNDRQVGGPTRNRGGRQYGGGAPPPPPVPQGPRGVGLVPAAEPAPPRSDPSQFVVVPSAQASRPSLRYARQGGYNGLAGLSDADAFPSLGPAVAASSAGINYASGPPVVVPSDFPRLKPQPNRPPPPPAVSAANIASGAAKKKEKKKETREEAFPSLGGSSRAQQQQQQETAQWARHTERFDVIDDDERDAFQTVGRHGLGPPPRVGPAVQPSRVAVIKRGAMQQQPPRGKQPAPMPAALSGEPEEDYPSLPPPAPTTRIDYSRVGGPLAQTSKWGKKKAEEAKKRPPPPPLPEPEMWPAMSSSTTAARPIENPDWQEVSIPLSKKALAKRENAEKNARKKEEKRLAREAREAEERAAVRMDTEEEDEDEDEEEEEEVVEEVKEVKKTEPVLGLSEISRLITSAPPAETQKKDGKGRGKEQPKAIPPKKEEPSKTAASSSNSKKKDKKGGADSAPSPIDKRPPAPTTTVPSQTSSSSLGLIGSVLCLLAALCKLVSCLLEMLFNSVYTSFVGGGDATAAAAAAAQNGSAAKPTAAAAAAADARARGLSTAPPPGISFAPPPGFGPPPGFENVVKRS

Pathway: Protein modification; protein ubiquitination. EC: 2.3.2.27 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. Sequence Length: 956 Sequence Mass (Da): 102622

A0A2C9L2D7

MTLTNRSRQDSTKLGVHVLVVLLGITSWSIMNGLWVELPILVVHLPEGWTLPSYLTIICQFGNIGPIVFSLLVYLTPRKKIETPTSFVIVVALTLCAALYGFLWKKTSPIGSNEHSVALMSLTLCQSIFAATTSTAYLAFMSHLKAQYIGSIFIGMSLSGLIPALAAVVQIPGEVECLRGAINSTNESVAYQLKNFTQSNLFDLNAFEPVIEAASNQTIHMTRLLQNSSDFENTLQLYKEEPSFSVKYFFLMLASLGGLSFLSLVLLIYHPYCKTEHADIKKEDNCRLVPIKRSNSSANDSNNSQGVNLEPTEQAQLDNKDEQDEQLSKAESWYLLCLLAWINMLQTSFVLAIQVYSSLPYGLFFYNGATKAENIVDPIACFLTMWVKVKSIRVISSLTLLGTLFSAYIIIVAAMSPNPFLVKHIAGGILIVSLENVCLFQNSFLF

Function: Plasma membrane transporter mediating the uptake by cells of the water soluble vitamin B2/riboflavin that plays a key role in biochemical oxidation-reduction reactions of the carbohydrate, lipid, and amino acid metabolism. Catalytic Activity: riboflavin(in) = riboflavin(out) Subcellular Location: Cell membrane Sequence Length: 446 Sequence Mass (Da): 49405 Location Topology: Multi-pass membrane protein

A0A8E0WQ72

MTESVKPPFGLSLSKPSAERSEAPSTSSGEPFDKLRANGGVKVRSDFPGLLNGEGGDWHYLDSAATAQKPNAVIDAIARAYGPDYATVHRGVYERSANMTLAYEAARRKVAQFIGAASDSEIVYVRGATEGINLVAQCWAGTQLKTGDRILLSMLEHHSNIVPWQIAAEKVGAAIDVVPLTPDGRIDLDAMQAMITPAHRMVALAHVSNVLGSVLDVRRAADIAHSVGAKILIDGCQAVPRLAVDVQALDCDFYVFSAHKLYGPTGIGALWGRKELLDAMPPYQGGGSMIDKVTFEKTTYAPPPTRFEAGTPHITGVVGLSAAIDYVQAIGLDAIHAHECALVGKARAALESLNSVRVFGPEDSAGILSFEVEGVHPHDVGTILDETGVAIRAGHHCAQPLMRHLGVEATARASFGIYSDEGDVDALVKGIERVRKIFG

Function: Catalyzes the removal of elemental sulfur and selenium atoms from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to produce L-alanine. EC: 2.8.1.7 Catalytic Activity: [sulfur carrier]-H + L-cysteine = [sulfur carrier]-SH + L-alanine Sequence Length: 439 Sequence Mass (Da): 46601

A0A7M7LK33

MSIRKAFSLVFIRKSTEILLGLKKRGFGKDKWNGFGGKIEPGESILHGAMRELKEECGLSAQELRKIGILEFEFEENEVLLEVHVFETYKYYGEIIESEEMRPKWYNLKDIPFKEMWPDDEYWFPYMLRGQFFKGYFLYRGQDLILKYNIETMEELPSLDHIS

Catalytic Activity: 2-oxo-ATP + H2O = 2-oxo-AMP + diphosphate + H(+) EC: 3.6.1.56 Subcellular Location: Nucleus Sequence Length: 163 Sequence Mass (Da): 19471

A0A2A6BVP6

MDYITLNPQESGDHIMKTAKHVKVDLEKCKEAALLVMDAVVEGKIGEIDYSANPLHPSGLSDEEKMLWVFLLDVLNFSFWPDEGEEYNVTFEGQTYTGYLAMCAAFRKAHKELNAPIATVQWMLTVDVGVLDFILKDDKGFSIPMITQRKQAVKEAGEWLFWSHDASFLNVVRKSNCNAQVFLRYILACESFRDYGFYNNRKVSFFKRAQILINDTVGALIGSEENKHLVDFKDLDTLSMFADYRVPQALNYLECLEYSPELLDELQSNKLLTYGAEKEVEIRGASIYAVQQMYKEIQRVRAAGPYSECDVDTVSGEYRLMGATGGDMDFTNARRLLPIDIDVWLWMFRREHADEVESIVPFHRTRSIYY

Function: Catalyzes the hydrolysis of queuosine 5'-phosphate, releasing the nucleobase queuine (q). Is required for salvage of queuine from exogenous queuosine (Q) that is imported and then converted to queuosine 5'-phosphate intracellularly. EC: 3.2.2.- Catalytic Activity: H2O + queuosine 5'-phosphate = D-ribose 5-phosphate + queuine Sequence Length: 370 Sequence Mass (Da): 42535

A0A536XYD5

MSEFFAMGGYGFYVWGAYGVSFALLALEVFLLMKRKREAKA

Function: Required for the export of heme to the periplasm for the biogenesis of c-type cytochromes. Subcellular Location: Cell inner membrane Sequence Length: 41 Sequence Mass (Da): 4657 Location Topology: Single-pass membrane protein

A0A0W0TSZ4

MKPMRVFFALAMPKSTQRLLAEILASAQRYIPAAEAHWVPKENLHITLQFIPEVHINDLPQLIENVRSSLTNLSSFYLELKGMEFFPTPTHPRIISLAVGPSDCLTQLSAAIGQGIKASNYPVETRAFRGHLTLGRLRRVHQSFSLEQIKIPLIPRIWIDVIHLFESRSGKEHSNYIPLAHLELNKN

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: 187 Sequence Mass (Da): 21264

A0A3B6KCR3

MPAHFRCPISLELMKDPVKAPTGINNGRERWLVRGRDTCPITGGPVWLADLVPNNATRHMIQDWCVANRAEQVPVAEADAAEVLAAFVRGNAAACGQGAARAIGKESDRNRRCLVAAGAARQLASAFRSLTGEPVESTSAAALSALGTILAALTMFFPLDDEARRCIASQASHKSQDPCLGALAQPPRPRSSRPTTPSPAATACFADVVVELVVDTDKGTSEKALAVLDGVLCADTGLRSACAYALVMPVLVKKMFRVSNMAKEFARLRALAPLLCRGHRRWRALLRGTACGLLPEAAPSVLRRHDRGSGQRAAQAAQWFQGQRRVHRDDGLQGAQEVKRPF

Pathway: Protein modification; protein ubiquitination. Function: Functions as an E3 ubiquitin ligase. EC: 2.3.2.27 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. Sequence Length: 342 Sequence Mass (Da): 36655

A0A7S3MX72

MCVERYDHHCPWINNCVGVNNHQYFIIFLSSLWVSNVLVFISSIVGLFYLYELPKLKKNELFYDFLPEAFALEKWVYEMASLFVIVLTGFFILPIGFLFYIQVRNFITNKTTNERFSRKKPARRHREPNELRMDSTGSSLVSTTSSMIVEDIINDVGDPEDYYAGGCVGCHNCTKMFCSKPFPSQLEMYNKFISQREALHKQ

Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein] EC: 2.3.1.225 Subcellular Location: Membrane Sequence Length: 202 Domain: The DHHC domain is required for palmitoyltransferase activity. Sequence Mass (Da): 23590 Location Topology: Multi-pass membrane protein

A0A183LSJ3

MKSQRDLVDFGTAAAEEKARRHDVMAHVYTFALACPKAAPIIHLGKSTCATSCFVGDNADLIMLKDGLNILLPKIARCIDRLAKKAMLHKSLICLARTHLQPAQPTTMGRRICMWIQDLLLDLENLERLKNHTIRFRGAKGAVGTQASFMDLFQGDHQKVIKLDEILTKKSGFQRSWCVTGQTYPRKVDSEVSNVLSNIGATVHKICTDIRLLSSFHEVEEPFETKQIGSSAMPYKRNPIRSERACSLARYLMHISTSMVSTASVQWLERSLDDSAIRRIVLPEAFLAADACLILLQNIAEGLIVYPMVMEANLNSELPFLVVERILVKMVSEGAANRQECHERLRKHSHEAAAEIKLKGLKNSLMDKLLNDDYFTPIHSLLPNLLDPSYMIGRAVEQVEVFLNTEVDPAIHSYKDSLALNSNITI

Pathway: Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 2/2. Function: Catalyzes two non-sequential steps in de novo AMP synthesis: converts (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido)succinate (SAICAR) to fumarate plus 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide, and thereby also contributes to de novo IMP synthesis, and converts succinyladenosine monophosphate (SAMP) to AMP and fumarate. EC: 4.3.2.2 Catalytic Activity: (2S)-2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamido]succinate = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + fumarate Sequence Length: 426 Sequence Mass (Da): 47732

A0A1W4WHG4

MAELRKRHETEDKRIESAESDHIDSEDDKHLDPKISTNLSDTIPSGTNKAPLILELLMKGLPDRWKNWFVRGIFTILMIFFFGIVIYGGPLALMITTLIVQVKCFAEIINIGHAVYRIHGLPWFRSLSWYFLVTSNYFFYGESLMDYFALAINRTDFLRFLTTYHRFISFSLYCGGFVWFVLSLVKKYYIKQFSLFAWTHVALLIVVLQSYLIIKNIFEGLIWFIVPVSMIICNDIMAYVFGFFFGKTPLIKLSPKKTWEGFIGGGVSTVVFGFLISHILCKYPYFVCPIQWSDNEGRMTMECTPGPLFTLTEYEVPTFLSGVLKLFGFSNSIYLYPFVLHSLPLSIFSSVIGPFGGFFASGFKRAFKIKDFGDVIPGHGGIMDRFDCQFLMATFVNVYFTSFIQHDSPHKLMHQILYLKPEQQLLLYQMLKETLQDRNVLQPIEDIVV

Pathway: Lipid metabolism. Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphate + CTP + H(+) = a CDP-1,2-diacyl-sn-glycerol + diphosphate EC: 2.7.7.41 Subcellular Location: Membrane Sequence Length: 449 Sequence Mass (Da): 51871 Location Topology: Multi-pass membrane protein

W5JR37

MSATSEYDVLVFGSCIVDFISYVPRLPKVGETLHGTRFATGNGGKGANQCVAAARLGSRTAIIGKLGDDAWGRAYRDALAAEGINVSEVAIMPGESTGIAQINVADGGDNQIVIVTGANKRLEPADAESRHALLQRARILICQLETPLEGTIAALRAFNGISILNAAPAEEHLPDPLLSLPTIFCVNETEAALLTAVPEIVDIPQAKTALLRLRELGCRTVIITLGEKGAVFAENGSTTVYHVQPTKVDKVVDTTGAGDAFIGALAHFMGQHPDAALGNCIAAANHVAALSVQKPGTQTSFPRARDLQLPLDDLKALQDRWNSV

Cofactor: Requires a divalent cation, most likely magnesium in vivo, as an electrophilic catalyst to aid phosphoryl group transfer. It is the chelate of the metal and the nucleotide that is the actual substrate. Pathway: Carbohydrate metabolism; D-ribose degradation; D-ribose 5-phosphate from beta-D-ribopyranose: step 2/2. Function: Catalyzes the phosphorylation of ribose at O-5 in a reaction requiring ATP and magnesium. The resulting D-ribose-5-phosphate can then be used either for sythesis of nucleotides, histidine, and tryptophan, or as a component of the pentose phosphate pathway. EC: 2.7.1.15 Subcellular Location: Cytoplasm Catalytic Activity: ATP + D-ribose = ADP + D-ribose 5-phosphate + H(+) Sequence Length: 324 Sequence Mass (Da): 34089

A0A3B6QLH3

MSRPLYRGFSGGGGGKDRCADEGRHYDPKEPSENGIGAGGCGTPARGRKRHLAAAAARIGVLVLAAAALVGSVAWAGSLYAGRGAAAAMAAASAHRGYRRLQEQLVTDLLDIGALAGGGLRSREAEACAAEYENHVPCYYNGSDAVDVSDLGGGVVISYERQCSREGRATCLVAPPRAYRTPVRWPSSKEFIWKDNVRISGHEFSSGSLFKRMMVEEDQISFPSDAHMSDGVEDYAHQIAEMIGLRNEFNFNEAGVRTVLDIECGFGTMGAHLFERDLLTMCIANYEASGSQVQITLERGIPALIGSFASKQLPYPYLSFDMVHCARCNIEWDKNDGIFLVEVDRLLRPGGYFVWTSSLHTHRALRDKENQKKWATIRDLANNLCWEILSQQEETIVWKKTNKRDCYSSRKSEPVLCARSHDPELPYYKPLNPCIAGTRSKRWIPIEHRTTWPSQARLNSTELDIHGVNSEVFGEDTSTWDSMVRNYWSLLSPLIFSDHPKRPGDEEPHPPFNMLRNVLDMNAHFGGFNAALLKSGKSVWVMNVVPINAPNYLPLIFDRGFIGVQHDWCEAFPTYPRTYDMVHADGFLSLEKRQKRRCSTLDIFLEVDRILRPEGWIIIRDTAPLIEAARSVAAQLRWDARILDLDIASDEKLLVCQKPFLKK

EC: 2.1.1.- Subcellular Location: Membrane Sequence Length: 663 Sequence Mass (Da): 74131 Location Topology: Single-pass type II membrane protein

A0A2D4T5U4

MNLENLNVVRWHQGQGFLVRAGHAPEPLASDEFSLPDNTCLALPSDVVRNMTVPVAPEEVKHLRRALPFMLEESLIEDVTELHFAFSPMRDDLQAVGVVKRSTIAQWMEELPDKVKELPWVTEVLCLPWRAGQCTLIFEDEWVLVRWGEAEGARVEMALLPALLDSLEAEQITLVAYGKDQQSAMVVIPERFHDELQWRQGGLSDALLLAEPLPAGPDLRQGDFAPRLPLMRWWGVWQRVAVALGVALILKTGLSIADYEMLKAEDLQLRQTIQESYRRINPRGAVVNVEKQLNRQLAELGAGARHRAFTPILVSLLSAAAAVPEITLTSVNYSGGSDIRVNFSAPDFQSVEQVRDQLKQRALSAELESSNARREGVVARLRVEI

Function: Inner membrane 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: 385 Sequence Mass (Da): 43069 Location Topology: Single-pass membrane protein

W5JRH7

MCILDTVEDKLSSLTTTTVMVVTPRDLEDVASYPRLFAELLGDGWTVDELEKLAGRNLLRVFEEVEKVRENQRLSGVRPYEDIPPALRPDEHHNCSTNS

Catalytic Activity: an L-aminoacyl-L-amino acid + H2O = 2 an L-alpha-amino acid EC: 3.4.13.19 Subcellular Location: Membrane Sequence Length: 99 Sequence Mass (Da): 11243 Location Topology: Lipid-anchor

A0A2A6BWE7

MPLPFRRLILLIVALALFSLITDWLILRRIEGEEGNENGNNERKEKNEKRSLSSCELPDELAVSAMKRMKNEECKDRLREVACAIEEKRLHETFPHSTCPLYDSGRKDQYIGCYADSKGNRLLSNHSFTWKNDNSREKCGLMCSRAGYVYYGLEFGVECFCGNWIEGGRKIDEEKCRTHSCSSGMEKCGGFESIAVYATGMTKPLIWPQPKYIEVDHNKEYDIRILFVLQLNGRNVRQVRQMLRSVYSRKHHYYIHVDSRQKYMLNGINLVRLYLSPQMGLIILRLRERGDRKGRKFVSERAQKHIVSLLFFPIFELLPFFDRQYGEELLFFLWSSMLFRQSSLDLEWDYIINMSESDELVLSLKELEAQLDSHRGHSFLATHGHSTGRFLEKQGFDYVFLECENRMWRVAHRPSFPSNIGLNGGSDWIVLYRSLAEYSISNEELPTKLKRLFSSVILPVESFFHSLAVNSRFCSSVVGGNLRMTNWNRKQGCRCAWLKKVVDWCGCSPLAFTSETSIKFTLETAQKRGVYFARKFDSVVSNEAILKAYLQSTRFSSLDFDLSHPRANSSLVNIFNVDVDRSSLSHSSFLRSLLPLSTHGRVIDLFMYKQSDHSEEQLVVLFEDGMNDHSERLFRFTNYVNIEEEDSNIGPFFLSSLDIGTDFDHKEEILRGFSKFIPEGGEVTLVLEWILIGETNTSKSSPECIVEWRDRRGIILATHTLQPYDSTRGRQFVQLNLSLLKDAEAGEWTVTVTDGSSRPLGTINFSVFSSDDFISRRTIEKLYRLEDECIGISMDRGRLLEHLSSLARRLITSNAINNELGEITRILQGVTPRSLNLTLPSSSSLLQNGAPILYSAIAESPSMHCSMFGFRTRNDVIPMHDHPTMHGFIRVLRGSLRITSFSLLPTSTLDTPEVRFNGERDVSERDGCIYLSPQMDNIHQVRSLEDGTFFFDLLIPGYKEVDCTYFQLPNPLPAVGTEMELQRCSTPSSYSCLHLPYDTQYYEE

Pathway: Glycan metabolism; chondroitin sulfate biosynthesis. Catalytic Activity: L-seryl-[protein] + UDP-alpha-D-xylose = 3-O-(beta-D-xylosyl)-L-seryl-[protein] + H(+) + UDP EC: 2.4.2.26 Subcellular Location: Golgi apparatus membrane Sequence Length: 1004 Sequence Mass (Da): 115421 Location Topology: Single-pass type II membrane protein

A0A3B6IYZ4

MGLRGRGPPLLLLLLLGLVVATALAADSASASEGDADPLYRACFEECQRTGTLKEDSVKHCIVPTDDQPADKAWYAHEPLYLQWKEWNCNSECRYHCMMEREQEREELGLGPVKYHGKWPLKRASVFQEPLSAALSALTLLVQFNGWLSFFLLLSYKLPLRPETHATYYEYTGLWHINALLAMNSWFWCAIYHSCDTAWTEKLYLSSAAAFLGYSLILVILRTSNLRDEASRVMVAAPILAFVTTHILYLNFYELDKGLNMKVCTVISVAQLLLWTVWAAITRHPSRLKVVFVAIGGVLSIYLEAHDVPPRWGYVDGHAICLAMAIPLSYLWWSFAKEDAEMRTAAIMKKKR

Function: Involved in the lipid remodeling steps of GPI-anchor maturation. Subcellular Location: Golgi apparatus membrane Sequence Length: 352 Sequence Mass (Da): 39943 Location Topology: Multi-pass membrane protein

A0A536WTZ6

MFDIGFSELLVIGIVALIVIGPQKLPGVARTVGHLLGRLQRYVADVKADINREIELEELRKMRDSMQKATSEMQSAVDAELTKTADELNKAAAGTPGTEPPQESAKAAEQKRA

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: 113 Sequence Mass (Da): 12244 Location Topology: Single-pass membrane protein

A0A6I0EQD0

MSLTLEDVRRVAHLARLNLAEDEAAAYVDQLASILDYFERLGAAPTADVPPTVHALALQDVLRDDVPAAGCGPDLALRNAPSADQGYFKVPKVLADGEA

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: 99 Sequence Mass (Da): 10498

A0A356SGH4

MSEDEATAVPPELEDAPSGAAGDIDLDMLMDVPVTMTVEVGRKSLTIKELLSLTPGSVVSFDRSVTEPMDIMINGTLVARGEVVSADGKFGLRLVDVVSPKARLEQLS

Function: FliN is one of three proteins (FliG, FliN, FliM) that form the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation. Subcellular Location: Cell membrane Sequence Length: 108 Sequence Mass (Da): 11430 Location Topology: Peripheral membrane protein

A0A811LIM5

MSRGGFRGARAPPRPGGAFNDDDSSPFGNQEEESRGSSRGPESNGYNDTRGGNNSYNDSRGGNNSYNDTRGGNNGYNDSRGGNQNFGRESRDSNRSGFGDNSDGNRDGFGPSKGNFGGRGAPNAGFGSGGSENFGGHGGFGGSRGGQENSFGNRGNQDNSFGNRGQGNGFPGPGQGFNFKDNSNKGFGNQEEDTRGGGRGPGSNNTFGASRNEGFGNNRGGFGRNESDSGFNRGRGGRGGFSSRGNFGGDSEGGRSGGFGGQSGFGRGGSDSEGFGSRGDGFGGGRGGFGGGSGSGFGGPSEGGFSGRGGGRGGFSGREGSDNSFGARGGFGSDSGFGGGRGGFGGASEGGFSGRGGGFGGGRGNFGGRGGSDNSFGGRGGFGSDGGFGGGGFRGGRVGGFGAAPAGFGGSGGNTAPLGGGFSSGFGGASFGQPGEDRSSLFGYRGDRPRHEPFEPEAKTADDYFKEQCSIDEDELNMEEDGEVTRKGGPEVDRVIETWEDAELDEQILANIKRLGYKAPRNFQKHAIPVILDGFDLKGKSETGSGKSAAFLIPIVHKVKKLLEEEKDREDGVIRMNKPRCLILSPTRELAEQLYCEAEKIANRTGVRVARAYGEISVNLSREQTSKCHILVGTFGRLIHFLVQQYVDFSLLKYFIMDEADELVGYDNIPQLNAIVQHETFPKPADRQSIFFSATFDDIQNETIDDLCRKKECVYLESAAPLNKRIVQEMVCVRESDKDQYVHELLKKEVEEKGKVEKTLIFVSTRKECDGYAGYLSLSDVKSTTVNSDRTQKQRLECYNQFKNGDVDVIVATDVLSKGADFPKLNRVIIKNTSNHQDQNYVHRIGRTGRTRAGLAIVCIDPTLEADQNVAKQAVEYLKKCGKEPPEWMLHVGEDDFVPPYVETEEVVPDSAANAEAKPDGEKAADDEPLF

Function: RNA helicase. EC: 3.6.4.13 Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate Sequence Length: 931 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): 98428

A0A3B6EJD2

MDSVERSRRRAQRWSKRKAAVVHLAVCFVVGAFAPLVATRGPLIDGIRASFLPFGGVQRAPAAPDIGLLLIVTVTRPDDDVVSQEASLTRLGHTLRLVPPPLLWIVVGAENRSASTVQVLRGTGVMFRHLTYANNTTGNVNDEADLKKNVALSHIERHRLAGVVHFAAASAIYDLEFFEELRQTRGVAAWPTATVSSAEQRVTVQGPTCNSSQITGWYSKDSGTNETHRESVAAAQDTGAIHNISSSPPAIETSGLGFRSSILWESEWFVNSNSSQDFIQLVREMAVGDGDERKGIPSNCSESRIMLWHLDMPKHTPEVEEQETPQEQSPLEEDEEDYMT

Function: Involved in the synthesis of glucuronoxylan hemicellulose in secondary cell walls. EC: 2.4.-.- Subcellular Location: Golgi apparatus membrane Sequence Length: 340 Sequence Mass (Da): 37355 Location Topology: Single-pass type II membrane protein

I1IGY4

MLLSPRRLHLRIPHCCSPAPAPSALLGGSGVVRRLGSGARRRGAVAMATDGRVERIASTIRVIPDFPKPGILFQDITTLLLDPQAFHDTTDLFVERYKDKGITVVAGVEARGFIFGPPIALAIGAKFVPIRKPKKLPGEVISEEYSLEYGTDKIEMHVGAVLPSDRALIVDDLIATGGTLCAAAKLIERVGAEVVECACVIELPELKGRDKLGDRPVFVLVKAD

Pathway: Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenine: step 1/1. Catalytic Activity: AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine EC: 2.4.2.7 Subcellular Location: Cytoplasm Sequence Length: 224 Sequence Mass (Da): 24038

A0A6P5G2L0

MTLVLTLLACVIHALNLANKSDASNKTCFGGIDGSIRFDIYQTTCPQAEDIIFAGVEEAVANDPRMAASLLRLHFHDCFVDGCDASVLLDDTPNFVGEKTAGPNLNSLRGFEVIDSIKAELELACPETVSCADVLAIVARDSVVLSGGPTWQVEVGRKDSRSANRQAANTNIPAPTSDVATLIGKFQNLGLSSKDMVALSGAHTIGKARCSSFSSRLNGLVGSSDASMGDRDFLQSLQQLCASSNNTLADLDLSTPATFDNQYYVNLISADGLLQSDQALTSAGSGDVAALVEAYAIDPELFFEDFKASMVRMGRLAMSGGGEVRRSCRVVN

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: 332 Sequence Mass (Da): 35118

A0A7Y5VWC3

MAKRHHEQLAIIHYPDPRLRRAADPVRHFDGELATVAERMLQLMRDAKGVGLAAPQVGLGLRLFVMNATGEPGGDEVFVNPEIVDPQGQREAEEGCLSIPDVHVQVRRAQRCRIVAHDLQGRRIEKSGADLVARIWQHETDHLNGVLIIDRMGPGDRIATRNTLRELEARFVRKSTGR

Cofactor: Binds 1 Fe(2+) ion. Function: Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. EC: 3.5.1.88 Catalytic Activity: H2O + N-terminal N-formyl-L-methionyl-[peptide] = formate + N-terminal L-methionyl-[peptide] Sequence Length: 178 Sequence Mass (Da): 19982

A0A811LQY2

METEADLGDNELSASISCRRRSASVSDDYSVQKTNDDATESKFSAVKVGYWADSFIHHFIVNPEHIHRRAPEILRGYWARHAAFELSLKRISELAGENLQIISLGAGFDTLYFRLKERGVAFKKLVEVDFSSVTARKIRTISKNEHLAAMFDSTSTESQHSDLHSRDYDLLGADIRQPSEFWAKIETAGLDPSLPVVVIAECVLVYLDVKVTENLVRKFAEKFNELVFVSYEQVNMTDKFSDVMQANLQERGIHLAGLPSCNSLDSQKSRFLNNGYPVVNAWTMQDLYAQHFNKDEIARIEKLELLDERELLAQLLEHYCLVLAVKTNGLFAGLVF

Function: Methylates the carboxyl group of the C-terminal leucine residue of protein phosphatase 2A catalytic subunits to form alpha-leucine ester residues. EC: 2.1.1.233 Catalytic Activity: [phosphatase 2A protein]-C-terminal L-leucine + S-adenosyl-L-methionine = [phosphatase 2A protein]-C-terminal L-leucine methyl ester + S-adenosyl-L-homocysteine Sequence Length: 336 Sequence Mass (Da): 38102

A0A3B5ZYN2

MDCVLLSSHLSSHATVNARLQQCSVSLNSIGFAVIRKGCLRLRCYAIGDAGRRNDPLDENKNGPISQELNGSSASFTTVGAEITQETGDFFSSDAEGDPDKPTEGFSSIEDAINSLREGKFVIAVDDEKGDNEGDLIMAADQASPESIAFMIRNGSGIISVGMKEEDLERLMLPMMSPVTEIGDISATASTVTVDARVGISTGVSAADRAKTILALASPDSKPSDLRRPGHIFPLKYRNGGVLKRAGHTEASVDLVALAGLRPVSVLSSIIDPKDGSMASTPALKQMALEHDIPIVSITDLIRLVCLKVQEEKGETGGTDRCISFAY

Cofactor: Binds 2 divalent metal cations per subunit. Magnesium or manganese. Pathway: Cofactor biosynthesis; riboflavin biosynthesis; 2-hydroxy-3-oxobutyl phosphate from D-ribulose 5-phosphate: step 1/1. Function: Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate. EC: 4.1.99.12 Catalytic Activity: D-ribulose 5-phosphate = (2S)-2-hydroxy-3-oxobutyl phosphate + formate + H(+) Sequence Length: 327 Sequence Mass (Da): 34655

I1HJ23

MAQPQRVYEAWKGNNRFFLGGRFIFGPDAKSLLVSVALIVVPVFVFCVFVARYLLHRFSVYNAGYAIPAVAIAFMIYVLLLLLITSAQDPGIVPRASHPPEEEFSYGNPLAGETPGRLQFPRVKEVMVNGMPVKVKYCDTCMIYRPPRCSHCSICNNCVERFDHHCPWVGQCIGQRNYRYFFLFVSSSTLLCIYVFAMSALHIKFLMDGDYPTVWKAFKHSPACLVLMIYCFIALWFVGGLTGFHSYLISTNQTTYENFRYRSDNRPNVYNQGCLNNFLEVLCSKGKPSKHRFRAYVQEEVRAPVVNFGRQMEEEPTGGSRAKVEDDLEIGSDLLKISQRRNYEDVDVEMGNQDHSEMESMANAKLVMGSESQIPAVVSEVRVRHSSWDQRSGNWDMSSDVMGRSASDVIGRSASVSEVASQRETH

Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein] EC: 2.3.1.225 Subcellular Location: Membrane Sequence Length: 426 Domain: The DHHC domain is required for palmitoyltransferase activity. Sequence Mass (Da): 48293 Location Topology: Multi-pass membrane protein

A0A811LD94

MGRRTAAVSQKGSAPPLSEYYLPAEPVYNEIETVPHQTHQFPVVQKTTESQNFHGVVPKQLHGHHFVLTTQRPVVQPVVGQRAANFELRRAEKLLNKNPERAAKKPFNPIVLTRRGCTDVPFCMLFILYLFGWTFVAFIAYKYGKPERILHPTDSWGNSCGSNRPSVYETIDKPYLFFFDLTKCVSYATLLSGCPTFQMCVKKCPTKYWSYLSLNRASLWSQQSVKDNAFCDYTVDIDTIQNFSQLRDLVKAGKCAAYTVPSSVVLGRCVPEVIVEASNVFNENGTLNNLLANFGNEDNLVAPDSKISETQEVVKAIAQGDGRVLQNVVVDLGVSWWQILALLIMSAIVSFVWTLVMRLMGGFMIWMSILLLLLGLAGGTVFCYHKYQILIQDGAINDYSFQPIISVYFEMPNTWLAFGITLAVLLIIIFFGVLFIRSRVSLAVALIGETMRYHMGTLALGSMILSFVKMLQVILDFVYSKLKNVENPVGKAIYRALTCLFWCLEKVLRFLSKNAYIMTAVYGKGFCKSARDSFSLLSRNLVRVVVLNRVSAFLLFIGKALITCGMGALAFYYFTGQIRIDDLPQVNLHYYFVPVIIVVVGTYFICDLFFQVYDMGVDTTFLCFLEDSEANDGTTEKPFYMSDSLKRLLGKENKF

Function: Choline transporter. Subcellular Location: Cell membrane Sequence Length: 655 Sequence Mass (Da): 73882 Location Topology: Multi-pass membrane protein