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stringlengths 6
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stringlengths 16
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stringlengths 117
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A0A2T9Z108 | MEFETIVVPIIVIILVYIFILIIGPLNTFRANPLVQIFFVALYSAGLYIFVVDSLQVLEEAEVNNFYIAVIWLQVFTNLYFYLYCCVSDPGKITKSNIKNALEIFNYDRIIFFPSECKTCKLPKPARSKHCSMCNRCVAMYDHHCIWFNNCMGLQNYRYFLFFLASLLFLLITASSFFLYSVFKINYMNVLSKFQSRFITDKSFSIMKEIIATTLFASPYTSSLALFLLFLVPIIAFFLVYQTRLWLIGKTSNESEKWADIEDAIHDKIGILEIIEPQNQDSDDRPKILVENISMIKNMYNYGWKKNLELLVWPPYL | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 317
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 37071
Location Topology: Multi-pass membrane protein
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A0A024TM56 | MVNPLTRCMEDYCLPPYATFHTDDIVPAVRTALAEYALDLNALEDDLMDAGESNLCWESVMDRLEIIDDPLRRISMFLEHLRSVVDSPDLRAADAEIQPEILAMNNRRDQSDVVFQAMQRLRSRADFNTAFTTEQQRILTRKVLHATLNGAALGPCVKERFNEISVRLETLKMKFSENLMDAMNAFSRIVHDKHELQGLSDATLAHLAQNAVADGHKEATAATGPWKLSLEYPVYMPVMKQCSHRHTREILFRAFVTTASTPPFDNSPVVQEMLELRQARAQLLGFQTYAELSLQDKMAPSVEVVEDMLNDLRDKCLPLSKAELDEVEAFANAHGHISRLEHWDTAYWSEALRKARFDVDDELINPYFPFPRVLEGVFQLASHLFGLHFEAADGQEEIWHPDVRFIQVRDMDEPDTPVVGHFYLDPYARPCQKNIGTWCDAIAYRSKVLRTDKAPVRLPVFCLALNQTPPVDSTTGLMSIDDVLSLVHMFGHGLRMLLTTADYSAASSMDAVEWDAIDIPSQFLSHFCDRRGSWRGDLSKT | Cofactor: Binds 1 zinc ion.
EC: 3.4.24.70
Catalytic Activity: Hydrolysis of oligopeptides, with broad specificity. Gly or Ala commonly occur as P1 or P1' residues, but more distant residues are also important, as is shown by the fact that Z-Gly-Pro-Gly-|-Gly-Pro-Ala is cleaved, but not Z-(Gly)(5).
Sequence Length: 541
Sequence Mass (Da): 61403
|
T2MFJ3 | MFSSIYDFYKRHRKKIIFTGIFVGSTYAITKLVSWKFNEWAELKVKEMEQEAKKQYLFESNQRTCTATFLSFLPDVQEVITSKTNLDQFLEILKLNPANKIEIWENIKILSMAQMIASVLSNILLLVLLKVQLNIIGGYMFVTMMYDKEMDVSDIQKRYLSNVKVFIEQRLPLLVDDVILSVKEIIGNVSLKEKISFLKLQSLTENVIEKLKSNHLKKSVNFSHPFSWYLINNETSNTEERYRRLMFQTNETLSGDSCALVLEDCISSGLQSILNNLKDVFFGYEEDPEAITSIESCAHTSFFKEIELPMAKITPLLNQQLHQIFKSGQNNFLDSVFSQSSLHDFSSNIFDAFSRVYN | Function: Involved in peroxisome biosynthesis and integrity. Assembles membrane vesicles before the matrix proteins are translocated. As a docking factor for PEX19, is necessary for the import of peroxisomal membrane proteins in the peroxisomes.
Subcellular Location: Peroxisome membrane
Sequence Length: 358
Sequence Mass (Da): 41465
Location Topology: Multi-pass membrane protein
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A0A7R9Q7K4 | YYKLPNFIGILCVFGICFCALLYIKGLLLPSKGLYNRTKNPIFDYYWGIELYPHITPIISLKVWIICRFGLILWQYIVLLCWKANYETLPDGSINYSLTATTLLQTIYLMKFYYWEDGYMNTIDTSVDRFGYYVCWGCIAFVPGFYPITSVYLVDNTPYNEFGIKSLIAVLTVGLLVICLNYWADQQKLHFRATNGKCVIWGKPAKLIRAEYIDDFGKRKRSILLTSGFWGITRHMNYTFELLSTFLWCLPALYASPVPYLYLIFLTVLLIHRSVRDDNKCALKYGQYWQQYKHQVKYQMIPYVY | Pathway: Steroid biosynthesis; cholesterol biosynthesis.
Subcellular Location: Membrane
Sequence Length: 305
Sequence Mass (Da): 35911
Location Topology: Multi-pass membrane protein
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A0A7R9L0G5 | MNKLVKKSLPLVCVVTQLMAMLLFAFSFFDVEETLFSPGSAANTGHTIGPRSAVDLIRSDVHYKQIDDYCRPRLTTTTAKPMFNKLVLVVIDALRHDFIPSIDRPPKSVQSGDRRHRHRRASGDSGGHRMPFTESIMQTNGVGLVSISATPTVTMPRIKAMISGTLPSFMDFILNLSAYRFNGENIVENAFKANKKTVFFGDDTWIQLLPKEVFAKYNGTSSFFATDYTEVDTNVTYCVRRELKALHEWDVMITHYLGVDHIGHSHGGYHSKLMPKKLLEMDAVVESIYTRVSAPDVREPYLVVITGDHGMTDIGNHGGNTPAETDTALVFLTTNGTKVGPKPVKASPDGRAERVLQVDISPTLSALIGLPLPNKSIGKVMLNVLDALSMPTDQQLCHMFANAVQISRLLPELSADHKSAAEKAFKFHTKLMANQTDTTFNADYHYKTAADSYDTLIASIQLKLMTKYTEKSFFSLITLSLLFAIVSIVGFAFIDYRNRCSILWTKVKDIQTVFAIVVVALNCVLLLSTSYMEYEHYFWYYMTSTIAFIQLAIAVRNHYRSAHPAIVSLVDPFTTLQENTLLQMLAVVLILILARVCNYWNVLNGEDIGQWLNKSDNKRVLSALVICSLIAISYLMSTKRFGKQQCLLISGLFWVYLY | Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 658
Sequence Mass (Da): 73719
Location Topology: Multi-pass membrane protein
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N6TRR3 | MALLIALGLLLSIILLYCVYSKWMFQHWARKGVPQLNPRLFFGDTLPLVRGQALRDFHLGLYQNFKSTGAKCVGIYNTHKPELVPIDINLLKDILVKDYSSFSSHGVFYHENNVLTSHVFNMEGQPWKDRRTKLTPIFTSGTRLYIPVIGVHLDPEYYPDPERFDPERFSPENKATRPDIAWMPFGEGPRQCLGMRFGMLQSKVALASLLHKFRFTLSKAMKPPFIADAGTLVYMFKQDVLLDATRVN | Function: May be involved in the metabolism of insect hormones and in the breakdown of synthetic insecticides.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 248
Sequence Mass (Da): 28439
Location Topology: Peripheral membrane protein
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A0A072VFT5 | MGTTVDDSCATQLIDGDGVFNLTGLDNFIKTSNMANTGLSYAVVAIMGPQSSGKSTLMNHLFHTSFREMDAFRGRSQTTKGIWIAKCTGIEPCTIAMDLEGTDGRERGEDDTAFEKQSALFALAVSDIVLINMWCHDIGREQAANKPLLKTVFQVMMRLFSPRKTTLLFVIRDKTKTPLENLEPILREDIQKIWDGVPKPQAHLHTPLSEFFNVEVTALSSYEDKEEKFKEEVAQLRQRFYHSIAPGGLAGDRRGVVPASAFSLSAQHIWKVIRENKDLDLPAHKVMVATVRCEEIAYEKLSQLRSDKGWLELEEAVQSGPVQGFGEKLSSIIDTYLSLYDEETIYFDDSVRNAKRKQLESNALDTVYPAYSTMIGHLRSKALDDFKTKLDQSLNNGEGFASSVRTWTQSIMLEFEKGSADASVRQANWGSSKVRDKLRRDIDSHALSVRNAKLSEITTNFEKQLAKALVAPVESLFEEGGKDTWLSIRKLLKSETEAAVSEFSAHVAGFELEEETVEKMQQSLRDYARKLVENKAREEAGKVLIRMKDRFSTVFNHDNDSLPRVWTGKEDIRAITRDARSASMKLLSDMAAIRLDEKPDQIERVLDLSLVNKTSAATSSQYTDREASVDPLASSTWEEVSPGDVLISPVQCKSLWRQFQGETEYTITQAIAAQEAYKRNNNWLPPAWTIMAMAIFGFNEFMMLLKNPLLILGIFVAYLLGKAIWVQMDVGGEFRHGALPGILSISSKVVPTIMNLLKRLAEEAQGNPAPERTEQHHSDSQIFRNEVSKPDSVSSSISNTGLSSVASSDGDGEFSTTNLSQRQRTNVSEAESL | Function: Probable GTP-binding protein that may be involved in cell development.
EC: 3.6.5.-
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 833
Sequence Mass (Da): 93010
Location Topology: Multi-pass membrane protein
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A0A6L7ZXX0 | MLVSEAWAQSGGGGSPDFSFLLMIVLLFVVMYFFMIRPQQRRAREHREMVAAVKRNDRIVTSGGLIGKITKAGEGPEIEMEIAPEVKVSIDRNSIQGVLNKKPGQKPSAANDSGERRSLLGGLFGGFGGRRN | Function: The SecYEG-SecDF-YajC-YidC holo-translocon (HTL) protein secretase/insertase is a supercomplex required for protein secretion, insertion of proteins into membranes, and assembly of membrane protein complexes. While the SecYEG complex is essential for assembly of a number of proteins and complexes, the SecDF-YajC-YidC subcomplex facilitates these functions.
Subcellular Location: Cell inner membrane
Sequence Length: 132
Sequence Mass (Da): 14391
Location Topology: Single-pass membrane protein
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A0A938ENP5 | MRIGVMGGTFDPPHDGHLALARAAAAQLGLDRVMLVPAAEPPHKPGGATMPAAQRMALVQAAVEGDPVLEASREEIDRPGPSYTADTLERIAGANPAADLWFILGADQLEGFPGWSRPERIVEIARLAVASRPGAGDPAMDVLAGTVAAGRVDVVDMPEIPISSTEVRARIARGEDVSALVPPAVAAMLRADTSS | Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1.
Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
EC: 2.7.7.18
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Length: 195
Sequence Mass (Da): 20194
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A0A966V5T1 | MPSKKNDDLGKIGYEDAVSELEEILEELEGDDIDVDKLAERVKRASDLVKACRDRIAAAKLHVERVVAEVDDK | 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: 73
Sequence Mass (Da): 8166
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Q08W44 | MIRIDGSKGEGGGQVLRTSLALSLVTGTPFQLVNVRAKRAKPGLLRQHLTAVKAAAEVGAAEVEGAELGSRELTFKPRALSAGNYYFSVGTAGSATLVLQTVLPALMVASGPSTLMLEGGTHNPAAPPFDFLEKAYLPLVRRMGPRVDAVLERHGFFPAGGGKFRVNVLPAPLRPLVLLERGRVKRRQATALFSQIPFNVAQRELATVEQVLGWRPDEQRVEELKRSQGPGNALMLEVESEHVTEVFTGFGERGVRAEEVAGRAAEAAKRYLDAEVPVGENLCDQLLLLLALAKGGAFRTLPLDGHSQTQLETFAHFLEVKVKVSEVSKEVREVEVRG | Function: Catalyzes the conversion of 3'-phosphate to a 2',3'-cyclic phosphodiester at the end of RNA. The mechanism of action of the enzyme occurs in 3 steps: (A) adenylation of the enzyme by ATP; (B) transfer of adenylate to an RNA-N3'P to produce RNA-N3'PP5'A; (C) and attack of the adjacent 2'-hydroxyl on the 3'-phosphorus in the diester linkage to produce the cyclic end product. The biological role of this enzyme is unknown but it is likely to function in some aspects of cellular RNA processing.
Catalytic Activity: a 3'-end 3'-phospho-ribonucleotide-RNA + ATP = a 3'-end 2',3'-cyclophospho-ribonucleotide-RNA + AMP + diphosphate
EC: 6.5.1.4
Subcellular Location: Cytoplasm
Sequence Length: 338
Sequence Mass (Da): 36485
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A0A7V6V2F2 | MRRKTLQIPIGNILIGSEYPIIIQSMTNTLTSDIQSTVNQCIRLFDADAKLVRITARNLKEAECLKLIKNDLINMGYELPIAADIHFNPHLAKVAANYVEKIRINPGNFVNLFPNNKSYTNEQYKLEVDAIKNEIEKLLPILVANKVAVRIGVNKGSLSQRLIDKFGNTTEALVESAIENVKIFNKLNFNNIVISIKTSSVYETIAANRLLVSKLDKLGLYYPIHLGVTEAGIDKEGIIKSSVAIGNLLLDGIGDTIRVSLTGDPVKEISVAETIIKTYQKFLPLPPMPTYSYTLENAPKIFTINDLTTEHLDLNNLFIDLPKNRPFDFIANKLKTVEQVNIKIDIDKFDLYELSIILGRGWIDGWLKDVYLVCDNLKNEKVNDVYQILQVTGKKKLLTEVISCPSCGRTMFDIESITRQVKKRFSIYPGLTLAVMGCIVNGPGEMREAQAGIVGNGINKADIYVFGRVVAKNIPVDKVVDEFEKQLKIHNLI | Cofactor: Binds 1 [4Fe-4S] cluster.
Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 5/6.
Function: Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate.
EC: 1.17.7.3
Catalytic Activity: (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate + 2 H(+) + H2O + oxidized [flavodoxin] = 2-C-methyl-D-erythritol 2,4-cyclic diphosphate + reduced [flavodoxin]
Sequence Length: 493
Sequence Mass (Da): 55206
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A0A7J3LYM8 | MPYRILFLGTSAGMPTLNRNLPGILIEWDSDLILFDCGEGIQLRFIEYRIGMGRPLRVFISHMHGDHILGLPGLLQTFSLLDRKTPVEVYGPSRLGEYIHCLRDTIGLNTTYDLKIFKVEDNVYYDFGAYRILCRRVQHGGESYGYRFEEKDRPGLFYPDKAIALGIPKGPLWKKLQLGESIKLNDGRIIKPSDVLGPPRRGFKLAYTGDTVPCRAIEELAEGVDILIHEATFTEDLADKAMAERHSTAAQAAYIALRSSVKLLVLTHISARYVTSDILLDEARRIHPNVVVAEDGLTIEISRTEEDYEYRVIPRMHIDT | Cofactor: Binds 2 Zn(2+) ions.
Function: Zinc phosphodiesterase, which displays some tRNA 3'-processing endonuclease activity. Probably involved in tRNA maturation, by removing a 3'-trailer from precursor tRNA.
EC: 3.1.26.11
Catalytic Activity: Endonucleolytic cleavage of RNA, removing extra 3' nucleotides from tRNA precursor, generating 3' termini of tRNAs. A 3'-hydroxy group is left at the tRNA terminus and a 5'-phosphoryl group is left at the trailer molecule.
Sequence Length: 320
Sequence Mass (Da): 36264
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A0A7R9M0L8 | MTNEEIVRVIDIWIKESRELGSKYNWVQIFENKGAIMGCSNPHPHCQVWASNYLPNEARIKDQTQRQYKETHNKPLLMDYLTKELDKKERIVLQNENWVVLVPFWAVWPFETMILPKKQIIRLEDLSESEKHDLSDAMKRLLIKYDNLFEISFPYSMGF | Pathway: Carbohydrate metabolism; galactose metabolism.
EC: 2.7.7.12
Catalytic Activity: alpha-D-galactose 1-phosphate + UDP-alpha-D-glucose = alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose
Sequence Length: 159
Sequence Mass (Da): 19033
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A0A173R2N7 | MKKVLLEIFDWVKTFVIIFIIVTLVHKYVFTPVKVDGPSMYPTLHHEDSVILWEFNYKPKAFDVIVFEYSPDVYYVKRVIGLPGQTVRYEDDQLYIDNQPIAEPFLEAGKEIISYVDDFTFDFTLQEICQFDPCDVIPEGYYLVLGDNRPHSKDSRHIGLISEDQILGKATWIQWPLSHFGKVE | Catalytic Activity: Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins.
EC: 3.4.21.89
Subcellular Location: Cell membrane
Sequence Length: 184
Sequence Mass (Da): 21529
Location Topology: Single-pass type II membrane protein
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Q9C8T3 | MVGVSPKIAPSMLSSDFANLAAEAKRMIDLGANWLHMDIMDGHFVSNLTIGAPVIESLRKHTNAYLDCHLMVTNPMDYVDQMAKAGASGFTFHVEVAQENWQELVKKIKAAGMRPGVALKPGTPVEQVYPLVEGTNPVEMVLVMTVEPGFGGQKFMPSMMDKVRALRNKYPTLDIEVDGGLGPSTIDAAAAAGANCIVAGSSVFGAPKPGDVISLLRASVEKAQPST | Cofactor: Binds 1 divalent metal cation per subunit.
EC: 5.1.3.1
Catalytic Activity: D-ribulose 5-phosphate = D-xylulose 5-phosphate
Sequence Length: 227
Sequence Mass (Da): 24111
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C9LX83 | MRRVFLEGEIADTMEVRGADAHHLQRVMRAKLGEKLLVADGAGGSAEAEVAGFADGRVQLRFVRRLSEAAESQAEIELFQCLPKGDRMDFIVQKTTELGVACIRPVLSQNVVVRYDEKKARARVERWQKIAAEAAKQCGRTRIPEVMPIVPLRAAMEGQGAAEYALRLFFYEMEERRELRTVLSDSEARRIFMLVGPEGGFDEAEAQLAVAHGFSAVTLGRRILRVDTAAIVALALVQYEKGDLGFAKSSIDDLGLQGQSV | Function: Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit.
Catalytic Activity: S-adenosyl-L-methionine + uridine(1498) in 16S rRNA = H(+) + N(3)-methyluridine(1498) in 16S rRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.193
Subcellular Location: Cytoplasm
Sequence Length: 261
Sequence Mass (Da): 28806
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A0A537F297 | MQLRMLKGKIHRARVTGADINYEGSIEIDSSLLDAAGILPFEQVEIWSLTSGDRLTTYALPAPRGTGKIAVNGAAARKVQVGDEIIIAAFAIMSETEARNWKPLVVHVDEKNRLMPFPKITKPLARN | 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: 127
Sequence Mass (Da): 13952
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J3JUZ7 | MSGDEKPKDHPEHPRNLIPELCRQFYNLGWVTGTGGGISIKDGSKIYIAPSGVQKERIKPEDLFVQNIKGEDLELPPPAKKLKKSQCTPLFMCAYTMRNAGAVIHTHSKSAVLITMLFPGNEFKCTHLEMIKGIKNQKLGRNFRYDEELIVPIIENTPFEEDLADRLEQTIKDYPHTCAVLVRRHGVYVWGDTWQQTKCMSECYDYLFDVVVQFKQHGIDPSLTPDQYELEYQKNGKV | Cofactor: Binds 1 zinc ion per subunit.
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 2/6.
Function: Catalyzes the dehydration of methylthioribulose-1-phosphate (MTRu-1-P) into 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P).
EC: 4.2.1.109
Subcellular Location: Cytoplasm
Catalytic Activity: S-methyl-5-thio-D-ribulose 1-phosphate = 5-methylsulfanyl-2,3-dioxopentyl phosphate + H2O
Sequence Length: 238
Sequence Mass (Da): 27275
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A0A072TYF3 | MLKDLSQKPLISILVLIFSTVIVLSTPPEDPIKCSNSQNTTCTITNSYGMFPDRTICQASQVFYPTSEQELVSMVASASREKIKVKVATRYSHSVPKLVCPEDSNGILISTKYLNKVVKIDVEEKTITLESGVTLKQIINEASKNGLALPYTPYWYGLTIGGMIGTGAHGSTLSGKGSAVHDYVVEIRIVRPSDSDDGYAKVEILNEQNNEDFNAAKVSLGVLGVISQVTLKLEPIFKRSITYVAKSDSDLGDQVVSFGHEHEFADISWYPSQHKAMYRVDDRVPINTSGNGLYDFIPFRPTPSIALAAIRITEDLDEFTGNVDGKCRVAKLTTNILFKSAYGLTNNGIIFTGYPVIGFHNRLQSSGSCLDSHQDAKITTCAWDSRIKGEFFQQSTFRVSLSKVKNFIEDIQKLVQLVPKGLCGIEQYNGILMRYVTASSAYLGNQEDALDFDITYYRSKDPMAPRLYEDILEEIEQIGIFKYGGLPHWGKNRNVAFEGVFKKYKDIEKFLKVKEKYDSQGLFSSTWTDQVLGIKEGVTILKNGCALEGLCICSQDSHCNPSKGYFCRPGKIYKDARVCSRV | Pathway: Cofactor biosynthesis; L-ascorbate biosynthesis.
EC: 1.1.3.8
Catalytic Activity: L-gulono-1,4-lactone + O2 = H(+) + H2O2 + L-ascorbate
Sequence Length: 582
Sequence Mass (Da): 64705
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A0A7M7L828 | MIEMASIIVRRSFYASASQARSVGVLGIPMWRGQKKLGTDLAPAKIREDGRLISGVETVVGKPVRDFGDLDLSSYSQCDKNVTHYMAKTAQSIRKSVIHCLRECEQLITLGGDHSIAIGTVTGHADYVKEQGRDLAVIWMDAHADINTPMTTPSGSWHGMPVSFLMHEMMAHLPRIEDFKDWPSSISAHALVYVGLRDVDPQERWFLEKLQVPNFSMRELDALGIHKVTEIALDKVDPLGRKSLHVSFDIDCLDPLVAPSTGTPVPGGMSLREVAVLAEAIASTHSLTVFDLVEVNSLIGSYEDASKTIQSAALITRWMFGDGRQGNTSSSGTLES | Cofactor: Binds 2 manganese ions per subunit.
Pathway: Nitrogen metabolism; urea cycle; L-ornithine and urea from L-arginine: step 1/1.
EC: 3.5.3.1
Catalytic Activity: H2O + L-arginine = L-ornithine + urea
Sequence Length: 336
Sequence Mass (Da): 36761
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A0A173RXA8 | MGIILASQSPRRKELLELAGIEHRVVVSAVDEVMDADLDVAGQVQDLAIQKACAVADLFESETVIGADTIVVCDGKILGKPKNEEDAFNTLKNLSGRKHQVMTGVSIINKEKELLTSFVNITDVEFYYVTDEWILNYIKSGEPMDKAGSYGIQGKGFELVKSISGDYYSVMGLPIAQLKRTLTHLNLI | Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: H2O + UTP = diphosphate + H(+) + UMP
EC: 3.6.1.9
Subcellular Location: Cytoplasm
Sequence Length: 188
Sequence Mass (Da): 20636
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A0A350H6V9 | MSNETNVEGKEKEVVEGVNMAKENIAIESTTKKKKKGKKKSWKYFLRKLLAKVAVTVVGVWLILTYVCGVYVNHNNSSYPMVKDGDLCITYKRSEVVKGDVVAYKKGDKVCFGRIIAKEGEEVDIRDGVVLVDGYNVVEDTVYETSAEESKIKYPYIVPQGKVFILNDFRKEVTDSRVLGGISEKDLCGELIFLIRRRGF | Catalytic Activity: Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins.
EC: 3.4.21.89
Subcellular Location: Cell membrane
Sequence Length: 200
Sequence Mass (Da): 22575
Location Topology: Single-pass type II membrane protein
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A0A968KA93 | IDEIHRLNRVVEEYLYPAMEDFSLEIMLDKGPSARSVQLPIKHFTLVGATTRAGLLTSPLRSRFGVVGRLDYYDVDSLQKIVKRSARILGVKIDQEGSFEIARRARGTPRVANRLLKRVRDFAEVAGNGGIDRAVASDSLARLDVDNLGLDEMDTRILEVIIHKFKGGPVGINTLAVAVGEEQDTIEEIYEPFLIQEGLLNRTPRGRVVTSNGYKHLNLKKSEKDQRELF | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. RuvB forms 2 homohexamers on either side of HJ DNA bound by 1 or 2 RuvA tetramers; 4 subunits per hexamer contact DNA at a time. Coordinated motions by a converter formed by DNA-disengaged RuvB subunits stimulates ATP hydrolysis and nucleotide exchange. Immobilization of the converter enables RuvB to convert the ATP-contained energy into a lever motion, pulling 2 nucleotides of DNA out of the RuvA tetramer per ATP hydrolyzed, thus driving DNA branch migration. The RuvB motors rotate together with the DNA substrate, which together with the progressing nucleotide cycle form the mechanistic basis for DNA recombination by continuous HJ branch migration. Branch migration allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves cruciform DNA.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
EC: 3.6.4.12
Subcellular Location: Cytoplasm
Sequence Length: 230
Domain: Has 3 domains, the large (RuvB-L) and small ATPase (RuvB-S) domains and the C-terminal head (RuvB-H) domain. The head domain binds DNA, while the ATPase domains jointly bind ATP, ADP or are empty depending on the state of the subunit in the translocation cycle. During a single DNA translocation step the structure of each domain remains the same, but their relative positions change.
Sequence Mass (Da): 25813
|
V6LXD6 | MSVVQTQPTASAVGSTPEYCVRALQLEDLHALAALLSQLSTVGELPLSAAEAFFADVSTSSFHQVQVIEDAKGSLVGAATLLVERKLLHGGSRVGHIEDVVVDQAIRGRGFGRQLVSVLVARAQELGCYKVILDCSDDNTGFYTKCGMERMGNEMAVYFQ | 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: 160
Sequence Mass (Da): 17136
|
T2M3R3 | MVSKVYVNGFVDCCFKKYILNQMKPNRRFFCLSSIVTNDFNEKDYKFHYLNSNVFQSKSTKDLIRSFVVLKTSSIGRFVDYSERMFLIGEKIIWAPLFRWLMKSTYYGNFAAGETVDEAKATADKLKTHNVLTMLCVPIESKKFSSNQEAEFEYEKNFNTVLRCIEETAAIESNGFAQLKITALCDKELLVNANKQLEKYQYSHNEDENWDIRTVVDLIKSCQYSKIKLSGLSDESNKKFVKLLSYLDKLAQHSAKHGVRLMVDAEQTYMQATLNYLVLVLQAKYNKERHIVYNTYQCYRKDTFKRLQADHNLAKNLGFLIACKTVRGAYMVEEKHYANKNNISDPINETFMDTTIMYHSVVSYLLPYIANKEVSLMVASHNEDTVLFVKEKMAEIGLKNNDRNICFGQLYGMCDHVSYSLGKEGYFVYKSVPFGQINETLLYLVRRAHENKSVIQRTNFEILLIKKELIKRLMGVKMIKS | Function: Converts proline to delta-1-pyrroline-5-carboxylate.
EC: 1.5.5.2
Catalytic Activity: a quinone + L-proline = (S)-1-pyrroline-5-carboxylate + a quinol + H(+)
Sequence Length: 481
Sequence Mass (Da): 55913
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A0A0H1FGX0 | MLKDKMIAKGAKYIQSIYQDPFIQGIIKGRLDHDVICHYLQADNIYLGKFADIYALCLAKSDNLRDKQFFLEQIDFTLNRELADGEGPHQALAAYTNRSYQDIIEKGVWYPSADHYIKHMYFHFYENGIAGALAAMSPCPWIYHQLAKKIIEENQFLNGNPFNNWITFYANDTVEELMENYFRMMDYYAQNLSKEKQADLVDAFVKSCQHERRFFQMAINQEKWED | Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
Function: Catalyzes an amino-pyrimidine hydrolysis reaction at the C5' of the pyrimidine moiety of thiamine compounds, a reaction that is part of a thiamine salvage pathway.
EC: 3.5.99.2
Catalytic Activity: 4-amino-5-aminomethyl-2-methylpyrimidine + H2O = 4-amino-5-hydroxymethyl-2-methylpyrimidine + NH4(+)
Sequence Length: 226
Sequence Mass (Da): 26650
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A0A7M7MCT0 | MGLLTRLGILCLRTKQIPRLNSRGLLEEPRNSRATFIYARSTWATRTNDNVNISNQTTPKAQDIKTVSLERFVSVSPSWLQPYLRLMRIERPVGTWLTLLPSLWALTTAAPAGSLPDPRLAALFCTGALLMRGFGCTINDMWDRDIDRQVERTRQRPLAAGRLSRWDALWFAGGQAGLACLVLLHFNWNTVMLGLASVGLVVIYPVMKRFTYWPQAILAVVFNWGALLGFSAVQGADMSWTTALPMYAGAFSWTLIYDTIYAHQDKRDDLLVGMKSTALRFGARTPLWLGAFSTSMTTGLIVAGITENMGWPYYAAIAASSALLTKQVATLKIDDPADCAKKFVAHRNIGLLVLLGCIGGSLLKSV | Pathway: Cofactor biosynthesis; ubiquinone biosynthesis.
Function: Catalyzes the prenylation of para-hydroxybenzoate (PHB) with an all-trans polyprenyl group. Mediates the second step in the final reaction sequence of coenzyme Q (CoQ) biosynthesis, which is the condensation of the polyisoprenoid side chain with PHB, generating the first membrane-bound Q intermediate.
Catalytic Activity: 4-hydroxybenzoate + an all-trans-polyprenyl diphosphate = a 4-hydroxy-3-all-trans-polyprenylbenzoate + diphosphate
EC: 2.5.1.39
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 366
Sequence Mass (Da): 40389
Location Topology: Multi-pass membrane protein
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A0A6P8YVC0 | MDAGGLCDRLRHLHVRDDELAGQDAVNAVTNPDDIFQRWRCDARAAQLVMPDSAIITTCSRLGQASARTVCLRRMDEGRFVFLTDSRSKKCRELAENPKAVVTFLWAFVDRSGLRIAREVRIGGAVQPQPPSAYEDLYWSLIPNRRIRAYICEQGAAADWDRLKERHDQLLVEVEAGKRLPMPAHFVAYELFPCTMEFYEQVEEEEVCQSLQFIRAESGAWTLEESS | Pathway: Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal 5'-phosphate from pyridoxamine 5'-phosphate: step 1/1.
Function: Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP).
EC: 1.4.3.5
Sequence Length: 227
Sequence Mass (Da): 25895
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C9LTK7 | MKIIAGLGNPGAEYARTKHNVGFMLVDALAERLGVDAWREKFNALTAEGRIGAQKVLLVKPLTYMNESGRAVGPLLDWYKLAPEDLIVAHDDMDIAAGTIRLRRKGSAGGHNGIKSLLAHIGSEDFSRVRIGIGRPLPGWTVVKHVLAPFPADDAPKIQEAISYLLPAVECIVTDGIDMAMNRYNPRRKKAAKQEAQERESAEKSSAVPQAERQEGEA | Function: The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Catalytic Activity: an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-amino acid + H(+)
EC: 3.1.1.29
Subcellular Location: Cytoplasm
Sequence Length: 218
Sequence Mass (Da): 23745
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A0A7R9KVR2 | MAPNIQSPIEPEISDISDGIKTRRDFKVEIVWRNVAIMSGLHLAALYGLYLCFTSAHWQTMAFAVFLYVISGLGITAGAHRLWSHRAYKAKWPMRVILTIFNTVAFQNSIYEWSRDHRVHHKYSETDADPHNANRGFFFAHCGWLLCRKHPDVIEKGRNVSCEDLLQDPLVRFQRKFYLPLVLVFCFVLPSIIPNILWGESCFNAYFVCGLLRYCWTLNMTWLVNSAAHFWGRKPYDRHISPAENKVTIIGAIGEGFHNYHHTFPWDYATSELGRDYNLTTCFIDVCAKIGWAYDRKTVSPNMIRQRKERTGDVKEKGPYGPSIGNLLLAGSQATLSHTDTVAIGAQKGLNECSRQFSYERWSCPEMIFADVFQNSLPANREIAFVQAIISAGIVYTVTRNCSLGQIDDCKCVVHKNNRENTAKNGFLWGGCSDNTELGSRIAVTYLDEREMGHDSKAIVRLHNHEVGRQVSRYCSQRRTRGVSKEEKRSCRKLCTLCGHKIKRERRRVITSCNCKFKYCCEVECQSCAKEQFSFVCSRDH | Function: Ligand for members of the frizzled family of seven transmembrane receptors.
Subcellular Location: Membrane
Sequence Length: 541
Domain: The histidine box domains are involved in binding the catalytic metal ions.
Sequence Mass (Da): 62028
Location Topology: Multi-pass membrane protein
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T2M855 | MSVLVETTLGDLVFDLYTEERPRSCMNFLKLCKIKYYNFCCFHSVRRNFIAQSGDPTETGRGGVSVYSFVYGDQAKYFELELKPRIKHRTKGTISFVNNGNDMHGSQFFITLGDGLDFLDGKHTVFGQLAEGFDVLEKLNEVICDDSHKPFQDVRITHTIVLEDPFDDPKDLPIPDKSPEPTKEVLESGRIAAGEKINDDDVSKEELLKKIEDKELAIGTKILETVGDIDDADLKPPENVLFVCKLNPVTNADDLKIIFSRFGKILSCEIIKDQKTGDSLCYGFVEFKEVEACEKAYFKMDNVLIDDRRIHVDFCQSVSKINKWHKSAAYTKANSSKDGFGYEMKEKKNPKDKYSMIFDDEDKGKKSQVQEKNKKKDSYKSKKKSQKRRSDSSDSVSDSSSKSIDDKRSARKKTLKSHKKRVDSKNDPKKSLKRNYSSSDDDDDDVDLKTAEKKKKNEKSKKHTEKSSDDSDSDDCDIKKSKTLKESSKNLKESSKYLKESSKYSNSDSEDSDHKQSKKFQEEFKKKKKAISKNNRDDIRKTISDDDKKNEFSRKKNDHRSSISKEKRDVRSSSSSLQKRDARSSLQKEKKTDVKEQTKYSDDSDESVKNEKREKKFKKISLEECDTEEYTGEKSSNKKNNRSEPSDSDDSSDEDKKKSRDYKKHTKRHSEGNKKRKKRNNSTDSSD | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
EC: 5.2.1.8
Subcellular Location: Nucleus
Sequence Length: 687
Sequence Mass (Da): 78975
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A7YD67 | EMALAYRDRIQAHNQTEQFSPLMSLYLTDNTTADEVRKAKASGAVVAAKLYPAGATTNSDSGVTDVKKIYPVLQAMQEVDMLLLVHGEVTTHDVDIFDREKTFLDNVLAPIVQDFPDLKIVLEHITTSDAVVFVKNANENVAATITAHHLLYNRNHMLVGGIKPHFYCLPILKRNTHQLALISAATSGNKKFFLGTDSAPHAKGAKESACGCAGSYTAHAAVELYAEVFEQAGKLENLEAFASHNGPDFY | Cofactor: Binds 2 Zn(2+) ions per subunit.
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3.
Function: Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate.
EC: 3.5.2.3
Catalytic Activity: (S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-aspartate
Sequence Length: 250
Sequence Mass (Da): 27275
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N6UJR2 | MNLLQIVFCVLTATLIVYSSLINLLEPRLPQFLSRVFRYGKFAVPGKSVFAVEVPKAWFKHFYILAVVEYICFMGLLSLVYFAGMAVPPQINSILNTLCGPDRIARCGKHNVYLAACLLTTQVFRRFYDTQKVSVFGEQSKMNLSHYVVGHLHYLGTILAVLCEAPEFAYTSESHKQLNLITTSISDKISVLIFLCAWKHQHILGNLRKNEDGDVVSNGYKIPQGDWFKYLSCPPHQTAEIIMYSCVTWILWYNVSWFFIFTWVLVNQVETILLSHWWYKEKFDDFPKERKALIPFLY | Pathway: Protein modification; protein glycosylation.
Function: Plays a key role in early steps of protein N-linked glycosylation by being required for the conversion of polyprenol into dolichol. Dolichols are required for the synthesis of dolichol-linked monosaccharides and the oligosaccharide precursor used for N-glycosylation. Acts as a polyprenol reductase that promotes the reduction of the alpha-isoprene unit of polyprenols into dolichols in a NADP-dependent mechanism.
Catalytic Activity: di-trans,poly-cis-dolichol + NADP(+) = di-trans,cis-polyprenol + H(+) + NADPH
EC: 1.3.1.94
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 298
Sequence Mass (Da): 34523
Location Topology: Multi-pass membrane protein
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A0A7M7JRE0 | MGDGWALFVLSSSMFVGCYLSGLIPVSMKLSEDKINVVSILGAGLLVGTALTVIIPEGVSTLYLSRLEKAHTDHHQEVATEARHSGHHHEAHHFDDPHSLIGITLVIGFVFMLLVDQCSKRGKSSEELLPTGPNKTGAISIWKTRPATATLGLVVHAAADGIALGAAATTTRAEIEMIVFLAIMLHKAPAAFALVSFLLHEGLDRSTIKKHLLLFSAAAPILAITTYFGISQNTKESMASMNATGIAMLFSAGTFLYVATVHVLPELAASKGNVLGNKRRRCVSPTIQRRPSFLGKYLGRFYRSESYDWKLLSENSAFLSERLPNVQTVMDLHERLDLSDEGNGGHSHHLAESSDASGFTRKELVLLVLGAMMPSFLSFGHHH | Catalytic Activity: Zn(2+)(in) = Zn(2+)(out)
Subcellular Location: Golgi apparatus
Sequence Length: 383
Sequence Mass (Da): 41458
Location Topology: Multi-pass membrane protein
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C9LTV2 | MDINGKDYLTIAFPKGKLFGLSKELFSRVGYTAEGLEEKSRKLIISNEEKKIRFIVAKTADVPTYVEYGAADIGVIGKDVLAEAEKDVYEVLDLGFGKCHLMMAVDKAQRRAKLADYAHTRVATKFPHIAEQFFTKKGMQMEYIKLNGSIELGPLVGLSESIVDIVETGTTLKENNLEEIAHIMDATARLIVNRVSYKLKFERIYRLVEDLRSALESGEAKS | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9.
Function: Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity.
Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + ATP
EC: 2.4.2.17
Subcellular Location: Cytoplasm
Sequence Length: 222
Domain: Lacks the C-terminal regulatory region which is replaced by HisZ.
Sequence Mass (Da): 24871
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A0A8T4Z7E4 | MVTEGFPFPTTILSEGKVRILVPRATIEGPSLKGPSSRRFPVFYNPGMALNRDLSVLALRVERRLLGREALACDAMAGCGAKGLRLAAEVEGTRILLNDINPMAVRLINYNVRLNALEERAIVRNEDARLLLLERAFREGTLDYVDVDPFGSPAVFVEAALCSLVDGGFLALTATDTAVLNGVHAEACIRKYWAKPLRCEYHHEVGARILLGYTARVAAMHGFGISPLLTERSSHYVRTIVSINRSSKSLRETMNSLGFLFHCHSCFHRHLEPYDHAHKRTGLVCSCGSKLSWAGPLWIGRLGDKAFLKSMLQESEKGAMQEPRRVRRLLELLVDEVEAPPTYFVPQEICKELGIPIPSLKEIALRLQSLGYSFFLTHFSPGSFRTDAPAKALAELLRRG | Function: Dimethylates a single guanine residue at position 26 of a number of tRNAs using S-adenosyl-L-methionine as donor of the methyl groups.
EC: 2.1.1.216
Catalytic Activity: guanosine(26) in tRNA + 2 S-adenosyl-L-methionine = 2 H(+) + N(2)-dimethylguanosine(26) in tRNA + 2 S-adenosyl-L-homocysteine
Sequence Length: 400
Sequence Mass (Da): 44423
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A0A7M7KLG9 | MQTSSGQRPRNGGRTSDRPRGFGGGGVNRGEGGGRGENGGRDEVTYSRFEGTIGRGFRNEGAHSRAGGSGGCGGEKGDRRRLSPSSRQQGAPGEGRGPPRMKTLPIVDTGGENTTSAVNECVVCCREILVYAVGSCDHSVCYVCSTRLRVLCKTQECPVCRATVEEVYFVKENTPFGELKEKTFNLKQKQFSIFFQDDEVQLKYEELLRHKCKECERRALIAARSGERPSALEVFPTFDDLTDHVLKEHRRHFCALCVEHLNLFTFERQAYSKNDLRRHMIEGDLDDKSHKGHPRCDFCKEHFLDKDELYRHLKVEHFTCFICNASSSISRVFQYYAFYDDLRQHFKRSHYFCEQGECATARFVAFASELEHKAHCATAHTDHLSREEQRAARSMNLDFGTLPHDRELIGADGRSGGRRGPREGGRRDDRRRREGSPNGNGVPYPGRTMTDEWGSEVPVMDMSSTTDFPSLEGAPASINRPLVPTPQYGRKMTVLQSVEEFPSLGPPTEAETPLTVPIRRATPNFKNAIGAISNSSSLTSVLASSSANRQPNRAVHSASPTIQKTSTPLGGSGTSRQHGRPAVRVGGDLFPSLPEPVPNNTFGNVLKPLPTKKTNSGRPQAMPQSGKNENGLALAGRLTGVNTGWAAVAAGGVTISQKLNSSDNSGNENNKKNRKKGDSTKSGASSEMNGNANQSTSVQQHLVDLRTILPSFSEIENNNQKSVKTNNRQTEPERKQELTPQKRELKGGENLDGFDLNVCGASWGSTAITNKQSEAEKAPRPPTQPRGLRKDEDFPTLGPAQAKDATTTGIRYMKPKYKGLKPGEAVADMKRLEGAFIQPPFYSKRNTEFMGMLKLLLDGNPEQVFEYRILLGNFRSDVITAEEFVQHCLELFPDPAEFVKIFPDLVCLLPNINKQNQLVPIYDQLRIRFGGPCGSSKKGDKSPEPWVRCSECGQITTPEDIQPHLRAH | 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: 968
Sequence Mass (Da): 107019
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T2M3E7 | MRKKYVVFTFLLLFLAAICIYEWSTNLEEVIILPEKPVNSFNRFSLKSILLWNDLFGKENWGFPRSTNYDFKELECRVQNCFITTNRDLTLDADAVIFHISGKLNSRPKLKPVNQRWVFLMHEAPCLHNFKSLRQWNSLFNWTMTYRLDSDIPIPYVHTCKKRNSKVNLLEKDIMGKKKKLAAWMVSNCNSQSQRNQYMNELLKYIPVDIFGKCSALFGQNNKCEKNDEENCMNMISSQYKFYFSFENSFSVDYATEKFIKVLNTNAVPVVRGDANYTVLGPPNSFIDTKKFKSAKHLAEYLLRLDQNEVEYLEFLKWKEDYEGHDCGPGDIVQKRFCDLCEKLNSPQSVKSVYTNIYDWYHKCREPNDLNV | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus
Sequence Length: 372
Sequence Mass (Da): 43844
Location Topology: Single-pass type II membrane protein
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G7L858 | MLVAFFICALMITNIIQVNANFSKSMYLTWGAQHASIVGEDLHLVLDKTSGSAARSKRSFLFGSIEMLIKLIPGNSAGIVTAYYLSSTGSQHDEIDFEFLGNSTGQPYTVNTNLFTQGKGSREQQFHLWFDPTADFHNYTIHWNPTEIVWYVDSMPIRVFRNYEHEGIAYPNKQGMRVYTSLWNADNWATRGGLVKTDWSKAPFKVGFHHFRARACKWNGAASINQCASNVKANWWTSSVYKHLSYGKIRQLNWVKKNFMTYDYCKDYKRFNGHIPHECFKTQF | PTM: Contains at least one intrachain disulfide bond essential for its enzymatic activity.
Function: Catalyzes xyloglucan endohydrolysis (XEH) and/or endotransglycosylation (XET). Cleaves and religates xyloglucan polymers, an essential constituent of the primary cell wall, and thereby participates in cell wall construction of growing tissues.
EC: 2.4.1.207
Subcellular Location: Secreted
Sequence Length: 284
Sequence Mass (Da): 32724
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A0A960GHH2 | MIRVAVVGAAGRMGSTVCAAVDAADDMEVLAKVDLGDPLDLVDDCDVVVDFTAPDVVMETLRHCVPAGVHVVVGTSGFDTARLAQVEDLLQGHPDVGVLVAPNFSIGAVLMMRFAATAAPFFESVEVIEMHHPDKVDAPSGTAVRTAEMISRTREGRPSPDATTTALDGARGAQVEGVTVHSVRARGLVAHQEVLLGGVGETLTIRHDSLDRASFMPGVLLGVREVGTHPGLTVGLDSFLGLA | Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4.
Function: Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.
Catalytic Activity: (S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH
EC: 1.17.1.8
Subcellular Location: Cytoplasm
Sequence Length: 243
Sequence Mass (Da): 25264
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A0A832FZ07 | MTCHIAYLIDDSIIVPDFESSRRLYSKSFYGTPIGVKKPKRADFNAPLKLSLIEALYLVEKGELKVVDMQGKALDIDELRRIALKSENEYIIYQIYKDLREKELIVRSGLKYGGAFTVYRIGPGLEHAPYIVHIYRRDENLDPIEIIRAGRVGHSVRKTFTLAFLARDGKPIYIMFKWVKL | Function: Endonuclease that removes tRNA introns. Cleaves pre-tRNA at the 5'- and 3'-splice sites to release the intron. The products are an intron and two tRNA half-molecules bearing 2',3' cyclic phosphate and 5'-OH termini. Recognizes a pseudosymmetric substrate in which 2 bulged loops of 3 bases are separated by a stem of 4 bp.
EC: 4.6.1.16
Catalytic Activity: pretRNA = a 3'-half-tRNA molecule with a 5'-OH end + a 5'-half-tRNA molecule with a 2',3'-cyclic phosphate end + an intron with a 2',3'-cyclic phosphate and a 5'-hydroxyl terminus.
Sequence Length: 181
Sequence Mass (Da): 20926
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A0A291E5P3 | MPGSVSRLFFMCMLCTSILSAHALQAATGNELNEALQGCEDQYKKAGNYGDCSLMDYQAGYVILKTRTASDNQFLLLPMDNVTGIEDKGVLSRPYTHPVSSLFYSAWQSRGFVFDQLKQRGKKLAEKDIALTINPVNSRTQNHLHIHISCLAAKTQQSLSDLDIEKLGWGWESKPLKNKNDRDILYDIRKLSATAFLNENIFDLVHERYRSNMKYAEVTVVPARTRSDEFLLLVNPGSVSSPATAEELQDHSCTVAKSAH | Pathway: Lipid metabolism.
Catalytic Activity: a CDP-1,2-diacyl-sn-glycerol + H2O = a 1,2-diacyl-sn-glycero-3-phosphate + CMP + 2 H(+)
EC: 3.6.1.26
Subcellular Location: Membrane
Sequence Length: 260
Sequence Mass (Da): 29094
Location Topology: Single-pass membrane protein
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A0A968KAU8 | MKVREKEDKKTKEKDTKQDGYQVTLEYIKSFLIALLLALLIKATIIEAYKIPTPSMEKTLLAGDFILGNKFIYGINIPFTDIRLPAIREPKRGDIVIFRPPHSPHENYVKRLIGMPGDTIKITRKRVYINGELYNDTAFTQHTSDYIMPRDRVIGPDPFIEAGIPNSGHRPWRPFRDNSYPIVVPEGKYFMMGDNRDNSLDSRMWGFVDRDQILGKALIIHWSWDIHDTSAPAVEFRNPLSIIQNIIYNLIHFPERVLWERLGTIPQ | Catalytic Activity: Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins.
EC: 3.4.21.89
Subcellular Location: Membrane
Sequence Length: 267
Sequence Mass (Da): 30991
Location Topology: Single-pass type II membrane protein
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A0A7C4D8R2 | MMVPRGHHIIGEVFADPEVLDDLEFIKEVFMEATEIAGLNVLDVKFHKFEPVGVSGIILISESHVSIHTWPEDGYAAIDIFTCGDVGKCWEAYRHIISRMRARRHMEIEIKRGLIDEEE | PTM: Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl group blocking the N-terminus of the alpha chain.
Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Pathway: Amine and polyamine biosynthesis; S-adenosylmethioninamine biosynthesis; S-adenosylmethioninamine from S-adenosyl-L-methionine: step 1/1.
Function: Catalyzes the decarboxylation of S-adenosylmethionine to S-adenosylmethioninamine (dcAdoMet), the propylamine donor required for the synthesis of the polyamines spermine and spermidine from the diamine putrescine.
EC: 4.1.1.50
Catalytic Activity: H(+) + S-adenosyl-L-methionine = CO2 + S-adenosyl 3-(methylsulfanyl)propylamine
Sequence Length: 119
Sequence Mass (Da): 13634
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A0A7R9L7G4 | MSAKVTLVSSSGCFGGKQQVWSHDSHELKCKMNFSVYIPPKVTDGVKVPVLFWLSGLTCTEQNFIIKSGFQKYAAEEGIIVVGPDTSPRNVNIEGEDDAYDFGSGAGFYVDATQDKWKQNYRMFSYITKELPKVIDDNFPVIKDCRSVFGHSMGGHGSLICALKNPGLYKSVSVFSPIANPMVGKWGQKCLSGYLGDNQKVWEEWDATVLVKKYKGPPLHLIVEQGADDPYLADELYVQNFVDSCASAHVAVDYRLHEGYDHSFYFISTFLAQHIKHHSRILYNTVWSHDSHELKCKMNFSVYIPPKVTDGVKVPVLFWLSGITCSEQTFIIKSGFQKYAAEEGIIVVGPDTSPRNVVEGEDDLYYFGSGAGFYVDATQDKWKHNYRMYSYVTKELPKVIDDNFPVIKDCRSVFGHSMGGHGALICALKNPGLYKSVSAFSPTANPMVTKWGQTCLSGYLGDNQKVWEEWDATVLVKKYKGPPLHLIVEQGTDDEYVFIKQCVENFVDSCASANLDVDYRLHEGYDHSYYFVSTFIGQHIKHHSRILYNTIY | Function: Serine hydrolase involved in the detoxification of formaldehyde.
Catalytic Activity: H2O + S-formylglutathione = formate + glutathione + H(+)
EC: 3.1.2.12
Subcellular Location: Cytoplasm
Sequence Length: 552
Sequence Mass (Da): 62173
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A0A072UYZ3 | MAGRFLGSSSASIDMIVTNTPSQELALTNLAFISASDLPKFAVPGHDNLYLASIGDSFVFSISYPSFTTHESIRGGHIALNSIQRRCARVSAAESVPVTRFVPPENFNLAVLQLELEFIKKAGNKNEQIDAIVLAKQLRKRFIKQVMTAGQKVLFEHQGNNYSFTVSQVTVEGQQRSSSIDRGMISEDTFIAFEASRDSGIKIINQRESTTSNIFKQKEFNLESLGIGGLGAEFADIFRRAFASRVFPPHVTSKLGIKHVKGMLLYGPPGTGKTLMARQIGKILNGKEPKIVNGPEVLSKFVGETEKNVRDLFADAEQDQRNLGDESDLHVIIFDEIDAICKSRGSTKDGTGVHDSIVNQLLTKIDGVESLNNVLLIGMTNRRDMLDEALLRPGRLEVQVEISLPDENGRLQILQIHTNKMKENSFLAPDINLQELAARTKNYSGAELEGVVKSAVSYALNRQLSLEDLTKPVEEENIKVTMDDFLNALHEVIPAFGASTDDLERCRLHGMVECGDRHKHIYQRAMLIAEQVKVSKGSPLVTCLLEGSRGSGKTAIGATVGIDSDFAYVKIISAETMIGLHESTKCAQIIKVFEDAYKSPLSVIVLDDIERLLEYVAIGPRFSNIISQTLLVLLKRLPPKGKKLMVIGTTSEVDFLESLGFVDTFSVTYNVPTLNKEDAKKVLEQLNVFAEEDIVSAADALDNTPIKKLYMLIEMAAQGAHGGSAEAIYSGQEKINISHFYDCLGDVVRVYR | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Required for vesicle-mediated transport. Catalyzes the fusion of transport vesicles within the Golgi cisternae. Is also required for transport from the endoplasmic reticulum to the Golgi stack. Seems to function as a fusion protein required for the delivery of cargo proteins to all compartments of the Golgi stack independent of vesicle origin.
EC: 3.6.4.6
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Subcellular Location: Cytoplasm
Sequence Length: 752
Sequence Mass (Da): 82746
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A0A6P8ZM77 | MVTLFALVVLVTLWLARYAAGRVKVTSLLAAVPGPSYPLPLIGHLIYMFGPMDGILDRGIRLYRTYGPGPIKFWIGEWPSVQIMRPEDIEPVLNSQKEVEKPDLIYKPVRAFFGDGLITLNGDAWFKHRRALTPAFHFSVLERYAGIFTRRAAAFADLLLAEVPADKTVNIMKFHSAFVTETIMETAFGMPPASRASSVQNKEMSDLVRATEDAFGVIVHRIFHPWLLIDALFKLSHSGRVNQRAEAIITRHAKAVIAQKKLELQQRRAAGDDDDAPDADEDAGVRKKYTFLDMALGGKSDVLSDAEILEEVRTLIAVQQTSASTLSFIMVMLALNPEVQQRARAEVREVDAIEGLHPLDRLKRLKYVERVIKETMRLYPITAIFSRKLKDEVHLPGHTLPAGVLATMFIYMTHRDDRHWPDPERFDPDRFLPDNCVGRHPYAYVPFSAGPRNCIGQRYAMLQMKAVVAAVVAKCVVLPGRGLESRDKIRLNMDTFLYIKGGFNVRLKPVGGGLFE | Function: May be involved in the metabolism of insect hormones and in the breakdown of synthetic insecticides.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 516
Sequence Mass (Da): 57990
Location Topology: Peripheral membrane protein
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A0A2E4AY97 | MANFITLAVDGGAGTGKSTLSKLISSENKFMYVETGSLYRAITYLMLEMKISPIDVGSEISGKELEFTSKIIKNKYFLYVGGRDCSLLDLRTAQINKQVSDYAALPAVRSFLIEFQRSQVGVAKLNGFKGIVMEGRDIGTKILPDADLKIFLFADFETRMKRRKKDGELDEIRNRDLKDLQRKASPLQRAEDALSINTAIHNQTETYSIVNRELLRLK | Catalytic Activity: ATP + CMP = ADP + CDP
EC: 2.7.4.25
Subcellular Location: Cytoplasm
Sequence Length: 218
Sequence Mass (Da): 24554
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A0A173YMP4 | MGNYYQPEIETMPVEKLQALQSERLVEQVKYVYDHVEFYRNKMKEAGVEPEDIKGIEDLHKLPFVTKDDLRDQYPYGFLGVPLSECVRMQSTSGTTGRRVVAFYTQEDIDVWEDCCARAIMAAGGTKDDVCHVAYGYGLFTGGAGLHGGSHRVGCMTLPMSSGNTERQIQFMEDLGSTILCCTPSYAASLGESINEGGHRENIKLKAGIFGAEPWTEEMRHNIEESLGIKAYDIYGLTEISGPGVSFECEEQKGMHIQEDHFIPEIINPDTGEVLPEGEIGELVFTCITKKAYPLLRYRTRDLCYLTRKKCSCGRTHIRMHKPMGRSDDMMVVKGVNVWPSQIEAVLLKQGYQANYQILVDRIGNNDTIEVQVEMTPEMKQEDVAIAAREKKIVHGLKNMLGIKVDVSILEPKTITRSEGKAVRVVDKRNLYNK | Pathway: Aromatic compound metabolism; phenylacetate degradation.
Function: Catalyzes the activation of phenylacetic acid (PA) to phenylacetyl-CoA (PA-CoA).
EC: 6.2.1.30
Catalytic Activity: 2-phenylacetate + ATP + CoA = AMP + diphosphate + phenylacetyl-CoA
Sequence Length: 434
Sequence Mass (Da): 48825
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A0A2E7VC73 | MKRIFIALSFPSDIVEELAALQFGLRGAKWVPSQNFHVTLSFIGDVSIVVLDNIIEMLRDLRSFPFCIKLQGINHFSSAGRVRSVWVNVTDKTALSILQKKIKNCLLRNNVSQDKREFNPHVTLARLKNARPEDVAGFIQFNNLFKTRSFLIESFTLFESIKQKDSSVYSPIEEFQLVHCVQ | 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: 182
Sequence Mass (Da): 20861
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N6T332 | MTEHLHDVVLPDNITEELLTSQHIDFIKKYGEEQNKFEYGMTDYLRLSGMYWGLTALELMNAGVTDTQDAIVEYIVKCQDPDSGGISACIDHDPHILHTLSGIQILAMFDKLDAIDIEGVVKYVQKLQQFDGSFSGDKWGEVDTRFSFCAVMILSILNRISAIKVQKAVKFVKSCKNFDGGFGSRPLAESHAGLTYCCVGFLSITKRFDVLDIDNLAWWLCERQNPSGGFNGRPEKLPDVCYSWWVLATLAMLGKLTWIDGAKLQTFIFACQDQETGGFSDRPKDVPDPFHTLFAVAALSLLDYENIQKVNPTYCMPQHVIDRLQLDPKILPS | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the transfer of a geranylgeranyl moiety from geranylgeranyl diphosphate to both cysteines of proteins with the C-terminal sequence -XXCC, -XCXC and -CCXX.
EC: 2.5.1.60
Catalytic Activity: geranylgeranyl diphosphate + L-cysteinyl-[protein] = diphosphate + S-geranylgeranyl-L-cysteinyl-[protein]
Sequence Length: 333
Sequence Mass (Da): 37450
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T2M6D1 | MGSIISKFQKKKSTQETLEIMEKEIDKLEENQNRNRDLQKSIVLSFLIFSVILYVLAAVIFYLWYFPKKWLQRLLYLLPFIGFPVLIFFLKKLLHFIFVTRIARNARTLANLKKEKKRILENVMETETYKVAKDILQRFDPKRKLVEQDFSIAENKTPSKDSDNKMLTTSITTSQVTPVLRNKPPQVTSNNIVNSRNGPQLVSPGQQGPTPNKFLGQQGPSPYKIAAPILPQNRSAFDKIAEYFVGDGPSNRYALICKQCFSHNGMALAEEFEFISYKCCYCNTFNQARKQRSHAPKLSQHDSDQSDSDHSKDKLNINGIEGRNLKNIVPKEADEAIITATDDEHQDSKKIN | Function: Plays a role in determining ER morphology.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 352
Domain: The C4-type zinc finger motif is necessary both for its ER three-way tubular junction localization and formation.
Sequence Mass (Da): 40395
Location Topology: Multi-pass membrane protein
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N6TQL3 | MLIVHSMIVIIVLSFTDGARILGIFPMAAVSHHTLYSKLMKGLAEAGHDVTVVSPYRLKELPKNGKYRDVVLEGFAAEYEDKLKSLNYFELREKSLIDRYFHFTALMLPTTNHTLHNANLKKLVESNETFDALILEQMFNDNMKVYGYIFNCPVILLSPFGPNSWVNPTVGNPQPPSYVPQMNQQDFSNDLSFFNRANNLYCFIVEYLIFKYYIFPQQERMMHAIYPDAPPLDDLYSNVSLVLLSSHTSIWSPVPLVPNMVEIGGFFIDPPKKLPPDLQEFMDKATEGVIYFSMGSNLRSKNIPLEKKQAFLNVFKKLKQKVIWKFEDENLPNKPQNVLIRKWCPQTDILAHPNTKLFITHGGLLSTTEAIHYGIPLLAIPVFGDQPTNAAKAVMNGYALQLDYHDPNFNEETLDYMLKELLNNPVYMKTAKEKSTIYHDRPMKPMEAAVFWVEYVIKHRGAPHLRVAGLRMPWYQYFMVDVLGCAVLALVLIAYAFNVAIRRVLRQKSGKVTSLKKIN | Catalytic Activity: glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP
EC: 2.4.1.17
Subcellular Location: Membrane
Sequence Length: 519
Sequence Mass (Da): 59483
Location Topology: Single-pass membrane protein
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A0A7C4CQ85 | MVKKRVIAIARERMDILMRMALDMASENINDAEAYVKLAWRIAERYNIRGKPILRRYFRCSKCKSFVIPGRGCRIRILKNRGLGIICMKCGSLKIIPIFNKRDNSLHS | Cofactor: Binds 1 zinc ion per subunit.
Function: Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends.
EC: 3.1.26.5
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Subcellular Location: Cytoplasm
Sequence Length: 108
Sequence Mass (Da): 12585
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H8YHY2 | MIERNPEKNWPACLEHNKPLGPLISMATPATARAFCRVESLADLQAALAWANAESLPYMVLGGGSNLLFVDDYPGLVIQPGFSQLALAPGAEGQYQLVGGAGVPWQQVVDFAVARNLWGLENLTRIPGSLGAAPIQNIGAYGVELDQVFDSLTALDVQRGEVVAFSREQCGFGYRQSVFKGDGKGRYIVLEVRLNLSAEPRPVLSYQGLEDLAGESALTPAKVAAQVAALRGQKLPDPAALPNSGSFFHNPLVSHAQADRLRARYPALVSYPQPDGRVKLAAGWLIEQAGFKGFAEQGVGVHRAQALVLVNPGRESGARVLALAVRIQHKVRELFDVELVIEPGVYP | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation.
Catalytic Activity: NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
EC: 1.3.1.98
Subcellular Location: Cytoplasm
Sequence Length: 347
Sequence Mass (Da): 37220
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A0A2Y9I3K4 | MTTEEIDALVHQEIISHDAYPSPLGYGGFPKSVCTSVNNVLCHGIPDSRPLQDGDIINIDVTVYYNGYHGDTSETFLVGNVDECGKKLVEVAKRCRDEAVAACRAGAPFSVIGNTISHITHQNGLQVCPHFVGHGIGSYFHGHPEIWHHANDSDLLMEEGMAFTIEPIITEGSPEFKVLEDAWTVVSLDNQRSAQFEHTVLITSGGVQILTKLPHEA | 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: 217
Sequence Mass (Da): 23675
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A0A7V6V3H0 | MDKYIIGITGNIGSGKSTFARWFADYNFYVIDMDLYAKNLYFNYSFRRKATDILGFDPIYNDRLRTQDIADKIYSDENKFKQLTELFLEFLPPLVDNTIKNLNDKYIVIDGALLFEYSLDKFCNLTICIYAPLILRYKRIKKYRNKKISKKRFLQIDKHQLSPDIKCKMADICVKNEGNIEKLKNNFLKILSSIDI | Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
EC: 2.7.1.24
Subcellular Location: Cytoplasm
Sequence Length: 196
Sequence Mass (Da): 23168
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A0A1B1UZ26 | VDTRAYFTSATMIIAIPTGIKVFSWLATYHGSKLNLFNLNNSIMWSLGFIMMFTIGGLTGIMLSNSSIDIILHDTYYVVGHFHYVLSMGAVFAIFNSFVHWFPLFFSMNMNQKWLKIQFWFMFIGVNMTFFPQHFLGMMSMPRRYSDYPDAYYCWNLLSSLGAMISFNSMIFFIFIMMESFMSKRLTIFKFNQTSLEWIMNFPPYNHSFNEIPIIIKNNYKFLIF | 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: 225
Sequence Mass (Da): 26578
Location Topology: Multi-pass membrane protein
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A0A355IKH3 | MHDDNIGKVDHQAEVDALYMRRCLQLAASGRETSQPNPMVGAVVVKDGRIIGEGWHKRVGLPHAEPMAIGAVKNQECLGQSTLYVNLEPCSHYGKTPPCVDLIISKGIPRVVIGTPDLFPLVSGRGIEKLRGAGVEVVVGVEADACRELNRHFFTFHALKRPYVTLKWAMTADGFLDYQREAGDGRVQLHISTPYTRLLTHKSRAEHAVILVGRKTALLDNPNLTVRDWYGPHPIRAVIDRQLSLPLTLNLFDGSVKTLVFTEVERQDREGVSYIRLDFSQPVIEQLLQALYERNLQTLLVEGGSTLHNAFLSSGCWDEIHVEQSDKRIYEGVAAPCIDELRKRLVFEHQYEEAASHQAMTTYRTLRPLVYRMP | Cofactor: Binds 1 zinc ion.
Pathway: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-ribitylamino)uracil from GTP: step 2/4.
Function: Converts 2,5-diamino-6-(ribosylamino)-4(3h)-pyrimidinone 5'-phosphate into 5-amino-6-(ribosylamino)-2,4(1h,3h)-pyrimidinedione 5'-phosphate.
Catalytic Activity: 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)-pyrimidine + H(+) + H2O = 5-amino-6-(5-phospho-D-ribosylamino)uracil + NH4(+)
Sequence Length: 374
Sequence Mass (Da): 42035
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A0A072TRD5 | MGPISDFPLMFIPPAMPSSPSSPELVHSEPNPNPIPEPEPNPESNTSHNAPSSPPQTTTNKPPPTAAEIAARYILQSPPLSFAPKPLSTSEVTAAFGVIDDLPSLTDEEQKPLSSILTTSSGDQFSGTSWWSNQLETGISALADLADLANPSDDDFGYQGYSIHTNLASYNSRKPFEIDNGGWSPVDYGYNFNNFFATASSPRSPSLKSVGAGITNMGNTCFMSAILQCFTHTVQMFLGLRYCTHASSCDVEGFCVICAFRDHLDDALERSRSPIVPRELVKNLNYFSAGFVIGNQEDAHEFMQYALNKLKRGFPVGEENLIDQIFGGRLVSKLRCCCCGHSSDKFEPLIDMSLEIEHVSTIQQALESFTKVEKMDGKFICSDCNQEVTMEKQLMLDKAPSVAAFHLKRFLKDGDSVKKIDKYVDFSKELDLKPYTCGSSSGDNVLLKYELYAVVEHRGPSPNSGHYFSFVRSAPDKWYLMDDDKVSSVSEEEVLNRKAYILFYAQQGTPWFSSIVENEETAPKSKYLHNKYGFDCDNNGEKDDNDSTDANYDNCVSDMDEECDSGMQDVSP | Function: Recognizes and hydrolyzes the peptide bond at the C-terminal Gly of ubiquitin. Involved in the processing of poly-ubiquitin precursors as well as that of ubiquitinated proteins.
EC: 3.4.19.12
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).
Sequence Length: 572
Sequence Mass (Da): 63282
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A0A7R9PX17 | MVRLISMFRVVYRPLRMSSTTTHTNHTWKRLQYNRMKRFVAKFQWFHVPISLVFTFIAFQQFRRIKRREEQKRYEQNPNQILAKPIYTASDLEISMYKLLPLRTVSRIWGWINSIELPLIMRSPILRSYVRAFGCNLDEADVDDLRQYKNLGEFFRRSLKPGVRPIDTTNGIVSPADGTILYFGKANEGTVEQVKGITYSLSSFLGPXILYFGKANEGTVEQVKGITYSLSSFLGPQTWRSNGARNDNYEKSLLINSTGKQSSDLYHCVIYLAPGDYHRFHSPVEWKISFRRHFPGKLLSVRPTFVSWFPNLFNVNERVSYIGQWKYGFFSMTAVGATNVGSVKVYFDEALATNRTKWRIGRDFNDLKLKKNISLGKGDPFGEFNLGSTIVLVFEAPKNIEFDIKSGQKIKYGQLISRFEMAGVAVSRNRFNSDFLGVHSMRALNGVLGKSMVALRTGSGLLLTTLSFKPLKSRAFLIGMTGELITGDLISFSFRFSFGFGVTFGELTATGVLVFGELGSNRSRFGTLGIGVSGNLRLSCGR | PTM: Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The autoendoproteolytic cleavage occurs by a canonical serine protease mechanism, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl prosthetic group on the alpha chain. During this reaction, the Ser that is part of the protease active site of the proenzyme becomes the pyruvoyl prosthetic group, which constitutes an essential element of the active site of the mature decarboxylase.
Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Pathway: Lipid metabolism.
Function: Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer). Plays a central role in phospholipid metabolism and in the interorganelle trafficking of phosphatidylserine.
EC: 4.1.1.65
Subcellular Location: Mitochondrion inner membrane
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phospho-L-serine + H(+) = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + CO2
Sequence Length: 542
Sequence Mass (Da): 61514
Location Topology: Peripheral membrane protein
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A0A520KEY0 | MEEILKEVLSRIKPKDEERNKVRQIFEEIKNRIEEKAKSLGINVRVELEGSVAKDTWISTDKDIDIFILFPHGTDKEKAKEIGLEIAKYGAGENWKIAYAEHPYIKKKIDEYEVDIVPGIEIKEGERPLTAVDRTPLHTKFIKSKMNEEMKDEVRLLKQFMKGIGVYGAELKIEGFSGYLCELLVLYYKNFKNVIKNASNWRPKTIIDYMNYYKDIPCEEIFDAPLIVIDPIDRRRNVAAAVSLQSYSIFVMASKFFLEKPSIEFFFPSKLNVNLNDIINEIKKREISLVMIKMKCPKIPSDILWGEIKKTINKFVKLIENYDFEVIDYKSWSDEENRIIFLIEVEKRKLRRGKIHQGPKIWYDEDLKKFLDKYINNEKVLAGPFIKNERIYVEILRKYNDIKDLLINEIKNLKLSKDIMNEINKGFEVYVDEEILKECEGIEDEIFSFIRKKPLWLK | Function: Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate. tRNA 3'-terminal CCA addition is required both for tRNA processing and repair. Also involved in tRNA surveillance by mediating tandem CCA addition to generate a CCACCA at the 3' terminus of unstable tRNAs. While stable tRNAs receive only 3'-terminal CCA, unstable tRNAs are marked with CCACCA and rapidly degraded.
EC: 2.7.7.72
Catalytic Activity: a tRNA precursor + ATP + 2 CTP = a tRNA with a 3' CCA end + 3 diphosphate
Sequence Length: 458
Sequence Mass (Da): 54094
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C9LVK2 | MRTQYFSKERLAKLVEVFPKATFDAEAEEPAFIVTAADFPAVLRALKEKEGFDRLGNLTAVDWKDHIEMVYHLYNMEENVKLEVKAALDSAAPVIESATSLYPGAEFEEREVYDLMGVEFLSHPDLRRILMPDNYPAHPLRKDFVAPVPKMEGGKLVWLKKAPTS | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain.
EC: 7.1.1.-
Catalytic Activity: a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+)
Sequence Length: 165
Sequence Mass (Da): 18757
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A0A938EMP7 | MSGVPMMPGMRPLFDAAAVRDADARAIAGGIPGEVLMETAGTLATREILAAFPPGSTATVLVGPGNNGGDGMVVARLLAEAGWDVRVQAPGAREPETPDGALMTARAAEAGIGVGDVDLHELRAGRRLVVDALLGTGTAGAPRGGVADAVEALVASGAAVVALDMPTGVDGDTGAAPAPAVRADLTITFAAEKVGLRVAPGRELAGRVVVADIGIPRDIQPDPAAWLATEGVIAAIPPRAAGDDKYAAGGVLAIAGAPGMSGAARLCTRAAMRAGAGIVAACVPHEVRVEVAIGAPEVMVTGVAGGAGMSLDALDAIMHQSARVGAVVLGPGLGRDAGTTSLVNAVLEGVALPMVLDADGLWHLGDDPAALRERPAATVITPHAGEAARLLGTTRAEVEARRLDAARELCARSGAVALLKGPGTIICAPGSLPVVIEDGTPALATAGSGDVLSGVIAALLARGMDAADAATCAAALHARAGIAAGRGDGIIASDIIEALPEVLIAARAAAGGARTASRADGAAGGAGEGA | 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: 530
Sequence Mass (Da): 51669
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U3U5U7 | MTQYYNCKNWVIWLSFCIALILQSISYPQEIHMFRPFWCLLILIYWVLIIPHQINVGSGFLLGVVIDLLEGSTLGIHALSFSIIAYVVAFKNNAFKTLALWQQALIVSLLSILEKIIVFSSEFLVVNLTFQPEMLLSSVINGILWPWIFLLLSKILHRYNLY | Function: Involved in formation of the rod shape of the cell. May also contribute to regulation of formation of penicillin-binding proteins.
Subcellular Location: Cell inner membrane
Sequence Length: 162
Sequence Mass (Da): 18768
Location Topology: Multi-pass membrane protein
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V6LZD9 | MTINKQQIISLKMSKMEKYAISAVSLLFVTTPNIMKLGNLHIFLNGQIVIGAKFQQAIYSMIGLLSPVLISIFSWAFLYNIQDASNIFIYRGACEAFITITCILCVFALFSVFITAFTDPGIIPGKELLESFTATLNEKIQSKSNTIRALPQTQKDLKISSNCQSQLPSESSMTLTILSSLHKPETPLKFQLKGYSFNSKYCSTCRFYRPLRATHASISNVCIQRYDHFCAWIGTDVALHNHGLFYLMLFIVFIQLSVMILINLTIIIYSIQAFVNIDVIPANLKGLGIFGMIMMLTLLGGAGYIIFSLCQLMQYHVNLLKTGTLTKEDSGVNNAQVSGPFSYFNLWLNFKLCFKGLTQKRLLKNAIIQQNYIINLVEKNPYIVNLDSLGRILLMNGYQQFMSTNIALSEEDQVKAQSFKHFYDESQQKNQLINNQLTYLQILTIRDGVEFGLLRSRDQVIQTKEDFDSIKDTRPDLFVEKESKRDMLSLVKVCQKKIKDNGRVDQKQEIAVAQI | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 515
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 58439
Location Topology: Multi-pass membrane protein
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Q08MQ6 | MKAIVTGASGTIGSKLCAHLRCQGHDVVPWDRRQVPVNDYGAMERFVREVAPDVVFHLGAISQPSEWSDEGWGSNYAWASELAWLTRTLGVRFLFSSTSMVFSNSARGPFTRSSQPDASEGYGYAKRLAEERVLSQNPEARVVRLGWQIGEQPTGNNMVAFLEERMRQEGRVAASTQWFPSCVMLEDTVRLLPALAWAEPGVSMLDANERWSFHEIALALNALHGGRWRVEASEHPVLDQRMRDDRVAVPSLKERLPGLL | Pathway: Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.
Function: Catalyzes the reduction of dTDP-6-deoxy-L-lyxo-4-hexulose to yield dTDP-L-rhamnose.
EC: 1.1.1.133
Catalytic Activity: dTDP-beta-L-rhamnose + NADP(+) = dTDP-4-dehydro-beta-L-rhamnose + H(+) + NADPH
Sequence Length: 260
Sequence Mass (Da): 29079
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V6LUD3 | MLDQIIQIYNIKQTQRTGWVHNSILNPETVGSHSFGVAFLAFQLCPKTLCRSKVVEMALMHDIQESMVGDITPNCGVSVEDKHEKELQAIKIISEKLNNADYVKFFTDYEDGITQEAKFVKNCDKLDMFIQALIYERQGHNLDQFYSQMRVTEFEEINMIITQIQNYRKGQQSNK | Function: Catalyzes the dephosphorylation of the nucleoside 5'-monophosphates deoxyadenosine monophosphate (dAMP), deoxycytidine monophosphate (dCMP), deoxyguanosine monophosphate (dGMP) and deoxythymidine monophosphate (dTMP).
EC: 3.1.3.89
Catalytic Activity: a 2'-deoxyribonucleoside 5'-phosphate + H2O = a 2'-deoxyribonucleoside + phosphate
Sequence Length: 175
Sequence Mass (Da): 20304
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Q096B1 | MSGLGAFKGRWFVVKIGGELAADRPKLAGSVGAAVRAFLDAGVRVAVIHGGGPQATELTNKLGLTPRMVAGRRVTDEATLEVVKMTLAGQVSVDVAAAFRLAGVPALCTTGVSAGLIDARKRPPKVITGAGPEPIDLGLVGDVTDVNTALFERLSEAGLVPVLGSLSGDAQGQVFNINADTVATRVAAKLRAAKLFLVSNVPGVLADKNDPSTRIPTLTPAEAQEKIALGVIQGGMIPKVEESLSMLEEGIEAIHIVGISPAHALLGEAQGAGSFGTAFLRNR | Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4.
Function: Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate.
Catalytic Activity: ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate
EC: 2.7.2.8
Subcellular Location: Cytoplasm
Sequence Length: 283
Sequence Mass (Da): 28950
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A0A968F844 | MFKTGIGIEMRPFVKGRRLILGGAKIDYPMGLEGNSDADVLCHAIIDALLGASNLGEMHELFPEDDIKYKDISGLRLLELVNLKLARISFAVENIDVILACSEIDLAPYKTYMLLNLSHALKIDSSMISLKQSNSFFHLVPQFGDGISAFAVCTLIDISEPAEEEEEAGSEEEYYE | Cofactor: Binds 1 divalent metal cation per subunit.
Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 4/6.
Function: Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP).
EC: 4.6.1.12
Catalytic Activity: 4-CDP-2-C-methyl-D-erythritol 2-phosphate = 2-C-methyl-D-erythritol 2,4-cyclic diphosphate + CMP
Sequence Length: 176
Sequence Mass (Da): 19462
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D2T034 | MVGTALSLLIRAELGQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVETGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGISSILGAINFITTAINMKPPALSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFSATQKST | 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: 217
Sequence Mass (Da): 23197
Location Topology: Multi-pass membrane protein
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A0A3N5J2S7 | MNERIIFHLDMDQFFAAVEMLHQPHLRGLPIAVGGNPSGRGVVVTASYEARRFGIRSGMPAAEALRLCPQIVFVHSSVSKYCDVSARIFKSLLEFTDRVEPVSVDEAYMDVTDTVWKDGGVQGLAMKIKRRIVESEGLTSTIGAGPNRLVAKIASGMNKPDGFTYIPADRVEDMFRDMPVGDLHGVGKATQRTLESFGIRTAGQLAEFPVDILKRRMGKFGEELVRIARGEGSDKVLVPDEQPEEKSMGHEHTFSQDISDPVLLLGRLHLLCEKVARRLRSARMAGCTVAVRIRYRGFETVLHGCKLKRFVQHEMDIYPVVEKLFHESYRRGEPVRLTGVHVAELISVSELRQQELFVVPAEPDDLSQACDEIRDLYGERAIGFASGVFFSGGRPISNSRRTHFYSAFSRGSWLR | 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: 415
Sequence Mass (Da): 46409
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A0A7J3LWH5 | MKLSDLGERKLIEIASSILEQDPDEILGLGVDDAAAKPICEDLYLVMHTDVVVESTDRLPGQSYRDLAWKAVTANISDIAAKGAKPYALLSAIGIPGIYSLEVFEELMAGLRDSSSTYGCYIVGGDLSSSRELFIALAILGLTHRDRIMGRRGAKPGDLVCITGEIGYTSLAYRVLFDEWCIDSDLRRIVLDRAYRPIARLKEGLALASTGVVSSCMDISDGLAISLNTLSEVNNVSIIIDHIPIPREVLEAVGRYSVDPIDLVLYGGGEEYELLFTVKPDGLKLVEDKLSSLKSSFTVIGRVSEGAGVYFTSGRRVEARGWQHFLDWGSKPTS | Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine diphosphate from thiamine phosphate: step 1/1.
Function: Catalyzes the ATP-dependent phosphorylation of thiamine-monophosphate (TMP) to form thiamine-pyrophosphate (TPP), the active form of vitamin B1.
EC: 2.7.4.16
Catalytic Activity: ATP + thiamine phosphate = ADP + thiamine diphosphate
Sequence Length: 334
Sequence Mass (Da): 36353
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A0A8W8MHS0 | MYRQCSRFSAWQVHKHFNSKVLTPNHGLIAKTRCVSSKTNLKTEDDQGTAFPEQMTHIKYASKGLEKFPQKYKQVPLTLFIKKSKTLVMLDEISEKFTVTFPKSEDTLTVDIGPEDFAKLKNMLEKDKRDSSPAHNPESITECIWQEMKTDNNKLMQYYFRLSKIRLTGLVVLTAMAGYAMAPAAFDPIGFTMVTLGTGLTSASANAINQFFEVPFDSQMNRTKNRVLVRGYLSPLHAVTFAAVSGSVGLVVLALGANPLTAALGAFNLGLYTLVYTPMKRHTILNTWVGSVVGAVPPLMGWAACTGSLDPGAWIMAAIMFCWQFPHFNALSWNLRPDYSRAGYRMMSVVDPNLCKRVALRHTVGITGLCFLAPVAGLTTPLFPVMSLPLNLYFTYLGWKFYQQGDSSSSRSLFRFSLLHIPLLILLMIVNKPSRKNDSKDSGKESVTVVQSELT | Function: Converts protoheme IX and farnesyl diphosphate to heme O.
Subcellular Location: Membrane
Sequence Length: 455
Sequence Mass (Da): 50658
Location Topology: Multi-pass membrane protein
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G7JEI3 | MRPPYQRQISQPSSPVVSSSDLTTTTVVGYLKLITGTHATPTVVNTSDVDGHELQRGVVRKTLADRVIERFEEREKEKMMKEVRGDDGVGGDGGCGRWREERECCVGSKNIALENSTSISNDITGNDKEKFLDGLLVSGFDESSCISRSQSHFYHKPSPYLLSKLGKYEENHRKCGPNTRAFNEDMKIIAKYKENGTDCAAKIKQHANTLFCYQQMDKEGLFCEPFLNSTWLLPNDSPFWDANDVKTYQSTIEMEIMSNTLNEDLPSTMYVDLRYSGTSDERFFHCDHSQFLLSKIPLLFFDAGEYFIPSFCLL | Function: May be involved in cell wall biosynthesis.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus
Sequence Length: 314
Sequence Mass (Da): 35620
Location Topology: Single-pass type II membrane protein
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A0A7R9LFC8 | MVSKMKEMDIFGLGNPLLDITATVDDDFLHKYSLPKNSAILAEPQHEAMYEEVINKYDIEYSAGGATQNTMRYCQWIIGKNNQVTTFCGSVGNDYFGKIMEKKAKTDGVNVKYMTAPDKNTGTCAILLTDGGQNRAMCAYLGIVTSISLSLYSLFSSFVF | Cofactor: Binds 3 Mg(2+) ions per subunit.
Pathway: Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenosine: step 1/1.
Function: ATP dependent phosphorylation of adenosine and other related nucleoside analogs to monophosphate derivatives.
EC: 2.7.1.20
Subcellular Location: Nucleus
Catalytic Activity: adenosine + ATP = ADP + AMP + H(+)
Sequence Length: 160
Sequence Mass (Da): 17704
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A0A7R9PTT2 | MASEDYHISGVAAIICIAIGILIFVLLFIFAKRQIMRLSLKNRFVPHIPLARDAPKVLKQRIDSKLTVVRDITYEPNLLNYLHFESNESKEKNYEHIYRMKAIDSLATLEADIVEVTADCSLKRPPGQDLRYYLLRLVKDDGPLNNCDTKLINQFVDSYNSARHEPYPHFGLDQYNQFMTLLNTIRNCITTKTSPNRKCVQKGKDTTAQMAFNGKTQVSIRQNKVDFVVTDETSV | Function: General regulator of phagocytosis. Required to uptake Gram negative bacterium by macrophages.
Subcellular Location: Golgi apparatus
Sequence Length: 235
Sequence Mass (Da): 26960
Location Topology: Single-pass membrane protein
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A0A2D1CJ24 | MSLRTLLSSSALIAMLGLGYGMWALISPGEERRRELVKNLPESNPLRMDETRKRNALVMQALKDAAETDENIASRMGRHR | Function: Required for the assembly of the ubiquinol-cytochrome c reductase complex (mitochondrial respiratory chain complex III or cytochrome b-c1 complex), mediating cytochrome b recruitment and probably stabilization within the complex. Thereby, plays an important role in ATP production by mitochondria. Cardiolipin-binding protein, it may also control the cardiolipin composition of mitochondria membranes and their morphology.
Subcellular Location: Membrane
Sequence Length: 80
Sequence Mass (Da): 9025
Location Topology: Single-pass membrane protein
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A0A173TXJ3 | MGSSDVDFFIHSYYEFKLFGVTLSINTTMVTTVIVCLILLALILFARHEIMKDYDEPNVVQNVVEMIVEKMDAMVVSNMGIHAKKYLNYVEALMAFIFLSNISGLFGLRPPTADFGTTFGLALITFVMIEYAWIKTKGFGIIKDLLDPFPVFLPINIISEFATPVSMSLRLFGNVTAGTIMLGLWYALMPWFTKIGIPAFLHAYFDFFSGAIQTYVFGMLTMVFISNRYD | Function: Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane.
Subcellular Location: Cell membrane
Sequence Length: 230
Sequence Mass (Da): 25988
Location Topology: Multi-pass membrane protein
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A0A1Q2CG59 | MRTVVSSAEMRAAEQAVFARDPEADLMGKAAAAIARIADDVAPDGAVLVVAGAGNNGGDGLFAAALLAERRPVLFWRAFRDAHAAAVAAARAAGCREVDAVGAVAALADCSLVIDAVTGLGSRPGLPLALQTLVDACDAATVPVLSVDLPSGLDADSGALHPSFSAEHTVTFGSVKPCHVQQPAASRCGRVHIVDIGVTVPDTQLRVAEAADVARWWPRPDASSDKYSRGVVLVDTGSEQYQGAAVLSCSGALHAGAGMVRYTGRAASGLILSRFPSVVVGEGRAQAIVLGSGWGDSDGGEGRVALARMHSLPAVVDADALHWLPGGRLDGWLLTPHAGELARLLGCTRAHVEAHPLSCVREAARHTGATVLLKGATQYVAEPSGRVTIAVAGPPWTAQAGSGDVLAGICGALLAAGLPAWRAGVLGASIQAMTAAANPGPYTPDELAARLPAMIAQLSSSPLAR | 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: 465
Sequence Mass (Da): 47124
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A0A2E3Z9C5 | MVAIAVPIRICCGIAVWERNNVIESLPAKNCWFLTGATAVGKTRIGLAMARRLHAEIISLDSMAIYQGMDIGTAKPTSDQQAEIPHHLIDIVPPDQEFSVACYLEAAHAKIEEIRRRGNEVLFVGGTPLYLKGLLRGLTPGPPANWKLREEIEAEVAKHGPQGLYRRLEQLDPVAASQIHPHDTRRLIRAVEVFRITGVPISHSQMQFEEEIPAEDCRVFALRRSREVQYERINERVDQMLERGLVEEVRSLIADIEELSRTARQAVGYQEVLEYLEHGDHEIMTAKIKTRTRRFAKRQETWFRSLSECRYFDLEDDCQVDDIVEQILESGENIQRE | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
EC: 2.5.1.75
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(37) in tRNA
Sequence Length: 337
Sequence Mass (Da): 38532
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A0A072TFS9 | MEFSVRAAELTTLLESRITNFYTNFQVDEIGRVVSVGDGIPRVYGLNEIQAGELVEFASGVKGIALNLENENVGIVVFGSDTSIKEGDLVKRTGSIVDVPAGKAMLGRVVDALGVPIDGRGALSDHERRRVEVKAPGIIERKSVHEPMQTGLKAVDSLVPIGRGQRELIIGDRQTGKTAIAIDTILNQKQMNSRATSESETLYCVYVAIGQKRSTVAQLVQILSEANALEYSILVAATASDPAPLQFLAPYSGCAMGEYFRDNGMHALIIYDDLSKQAVAYRQMSLLLRRPPGREAFPGDVFYLHSRLLERAAKRSDQTGAGSLTALPVIETQAGDVSAYIPTNVISITDGQICLETELFYRGIRPAINVGLSVSRVGSAAQLKAMKQVCGSLKLELAQYREVAAFAQFGSDLDAATQALLNRGARLTEVLKQPQYAPLPIEKQILVILCNILSTIKPELLESLKGGLTGERKIEPDAFLKEKGPFFLDQDSGLSFCPGGIIVYQSIMNNSKSTTTINDYSVKSSSTQGSSNVNANGIFEDHPGLNPSSERVIELQSEIHDKLGELMINKGPDDVLAAAEALHAESSDIGFLQHLLDDWKAGGIRSEAYREALNSLVTEASSDAADPLQLGFQDAATPMMQGIIDLHHDIFFFLILILVFVSRILVRALWIVHGTTIEILRTIFPSIIPMFIAIPSFALLYSMDEVVVDPAMTIKAIGHQWYRTYEYSDYNSSDEQSLTFDSYTIPEDDLELGQSRLLEVDNRVVVPAKTHLRIIVTSADVPHSWAVPSLGVKCDAVPGRLNQISISVQREGVYYGQCSEICGTNHAFTPIVVEAVPSKDYGSRVSNQLIPQTGEA | 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: 856
Sequence Mass (Da): 93237
Location Topology: Multi-pass membrane protein
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A0A3A0DI42 | MLRKQALAPNLMTVVNLLLGFLAIVSAANGDFVKSGWLIIVAAVCDVLDGKIARALHITSDFGVEFDSLADVVSFGVAPAFLIYSAQLHDLRLFGVLVCFLPLAAGAVRLARFNTTTTLLDKHHFIGMPIPAGAGLISSYVIFSHQLWESVQFPGLTIVLLLIGSTLMVSTIEFDALPRISFRRGRQNTVKLVLLALALTILAVSPSKTLFPLALGYILMQVGRAVLNSLRQDEDEDALPDISISKR | Catalytic Activity: a CDP-1,2-diacyl-sn-glycerol + L-serine = a 1,2-diacyl-sn-glycero-3-phospho-L-serine + CMP + H(+)
EC: 2.7.8.8
Subcellular Location: Membrane
Sequence Length: 247
Sequence Mass (Da): 26713
Location Topology: Multi-pass membrane protein
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A0A0K2Y9K6 | MFVDCVEITATSGKGGPGCVSFRREKFVMEGGPDGGDGGDGGGIVFKVDSNSDTLSAFRGKKHYKAQNGAPGGPKNCNGKKGQNLEIIVPPGTQVFNADTGELLCDLIESGAQTTLLKGGKGGLGNVRFKSASKQRPTYAQKGMAGVSLNLRLELKLIAHVGLVGFPNAGKSTLISVLSNARPKIAPYAFTTLIPNLGVVQAGQFKEFVMADIPGIISGASEGKGLGLDFLRHLERTKFLLFVLDTTYDIHQQYEELRHELAHFSQELSARDFGVVLNKMDIGQVYGFHAPKAQFVLPISAATTENTGQLLQLLAQALQLA | 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: 321
Sequence Mass (Da): 34135
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A0A2T9Y967 | MSSEKVRSRKQQRYYMNSEFNSASQHGSDYDFNENEKYNLANPSNDLDYVPAYQKDHAVFQSTHLNQAKLADPTSGKRFRFTKKRLIVLGLVFLMAAYFRLWKLSHPSKVVFDEVHFGKHAGLYINRTFFLDVHPPLAKMMFAAAGKIFGYDGKFDFKTIGLDYTSTNVPYASMRFMPAFLGLAMVPITYITIAAFGGSEEACLLGSLLVTFENSFMTISRLILLDSILIFFTGLTVMFWALFLREEGHPFTKTWWVYLILTGVNMGNALSSKWVGLFLVGTIGVWTIKDLWFRITDYRVTLNEVNKHFWARVLGLIVTPLTVYVFWFYIHFSVLTLSGSGNNFMSPEFQTTVGGSHLVSTMRDVYYGSKIRIRHDATNAGYLHSHASRYETGSKQQQVTLYSHRDDNNYWIIDYTLDQKKKLANSTNLNELKPIKNGDVIRLKHANTKKNLHSHNLRAPVTNKDYINEVSGYGGDDFDGDSNDDWIVRIMDGDNSVPSSFNQIVSIHSKFRLIHKNEKCALFSNRVKLPKWGFEQVEVVCMKHAKYPKSIWRIESATHEKINYDTAPKVSFKIPGFFEKFIESHVVMLRVNNGLTGSHFYDSRPFSWIYLRRGIGYWSEKGHTIYLIGNPIIWWLAFVSIVSFVAIQLVLVLRDQRGYNDQMFGYRAQYMNFTGFFGIGWAMHYFPFFLMGRQLFLHHYLPALWFGIVALASSIDIFTRKVSSKARTVIMCALLFYTLRLYFLYSPVGYGTSWTREACEKSKMLSSWDFSCKQYPSIAEKLAKQTFDKDQGKKDNEKIQEAEIVDPGQPQPIDNIDEEIRLNQPAPMINDEDKKKLESDWEKFKNEDVKGSASLQPEKKDGESNPENKNDKQDDKAGEIQNKEEKKEEQKQEEQKKEEQKKEEQKQEEPKKEEKKEEEQKKEEQKENQQVIDKKAEEPKVENENQVAKDKPAPAEPKP | Pathway: Protein modification; protein glycosylation.
Function: Transfers mannose from Dol-P-mannose to Ser or Thr residues on proteins.
Catalytic Activity: a dolichyl beta-D-mannosyl phosphate + L-seryl-[protein] = 3-O-(alpha-D-mannosyl)-L-seryl-[protein] + a dolichyl phosphate + H(+)
EC: 2.4.1.109
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 959
Sequence Mass (Da): 110976
Location Topology: Multi-pass membrane protein
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A0A7C4HE87 | MLLYALAKMGAYHKPIRVSTTTIADKIGLSQQSVSRHLISLEEKGLIHRTISKEGSLIRISKAGGDFLRCIYIDLSAIFKGGPRSITLEGEVFTGLGEGAYYVAQEGYRRQFVEKLGFDPYPGTLNLKISDGKSMMLRATLDIYPGIEIKGFRNKNRTFGPVKCFLAIIGGRERGAVVIAERSHYSENVLEVIAPIYLREKLGLKDGDKVKVEIFI | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin (CTP route): step 1/1.
Function: Catalyzes the CTP-dependent phosphorylation of riboflavin (vitamin B2) to form flavin mononucleotide (FMN).
EC: 2.7.1.161
Catalytic Activity: CTP + riboflavin = CDP + FMN + H(+)
Sequence Length: 216
Sequence Mass (Da): 23986
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A0A072UQB9 | MAETRRTSSSSTTVLDSLGEEIVRIITPVSICMFLVVILVSILNTNDSPTISTIANIAYDETTSDSSWDKFLGALLNSLSFVVVVTFATFFLVLLFYFRCITFLKLYMAFSSFVVLGFLGGEISIFLIQHFSVPVDCITFLVVLCNFAVVGVCAVFMSKMAIFVTQGYLVVIGILVAYWFTMLPEWTTWAMLVAMALYDLAAVLLPVGPLRLLVELAMSRDEEIPALVYEARPVSNDCMDPRIIEARRRLWRERRIESAILITESGNSVLGSGGLNVEQSSHSNSDANTVLSTNLNENLTPENGSNLNSSSTYGTRNLVRAEEGRARVQEIDSDLATPLIDHGVNVRVPRGEDATSNENLMLEGIGLASSGAIKLGLGDFIFYSVLVGRAAMYDFMTVYACYLAIIAGLGVTLMLLALYQKALPALPVSVALGVLFYFLTRLLLEVFVVQCSLNLLMF | Function: Probable subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors.
EC: 3.4.23.-
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 458
Domain: The PAL motif is required for normal active site conformation.
Sequence Mass (Da): 50244
Location Topology: Multi-pass membrane protein
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A0A2I5HKZ3 | MDTSIITDLLIRIALAGLLGGLIGIERQLRAKEAGLRTHVLVGIGSAMFMIVSKYGFEDIIRQNHVDLDPSRIAAQVVSGMGFLGAGTIIIQKQIVKGLTTAAGMWVTAAIGLVIGSGLYEIGIYGAFLTLIVLEVFRQLSNRLLNHHCILQMKISPDCLSMVFSVLQKRRIRFSFRSLKESASEDKAWELFLILTLRPKESVNNIAPALLCIEGVKSVNIR | Function: Virulence factor required for growth in low Mg(2+) medium and for intramacrophage survival. May be involved in regulating membrane potential by activating Na(+)/K(+)-ATPase.
Subcellular Location: Cell inner membrane
Sequence Length: 222
Sequence Mass (Da): 24333
Location Topology: Multi-pass membrane protein
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E2RZC6 | MKSIIIYINFYFCLSLSSLFFYKDISENSQLSFQESSSFFNNNLVFFHDNIMFYMLIILVIVGWILFSIIINKNYNKFLLENNFIEIIWTLIPAVILIIIAIPSLSLLYLIDENIEPSLTIKIIGHQWYWSYEYSNFFSNIEFDSYMISTNDLNKGDFRLLETDNDLVLPVNTKIKLIVSSADVIHCWTVPSLGIKIDAIP | Cofactor: Binds a copper A center.
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
Subcellular Location: Membrane
Sequence Length: 201
Sequence Mass (Da): 23472
Location Topology: Multi-pass membrane protein
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A0A7R9LIT0 | MPSNKTIETKNAIADQMDDTIDNKSDHLVTNKCLNDEELCQTDDQLMDSARLVVVDSGCDDTSGQTMTIDGQLVSEGHESAAKGETPEPMPYCSGGGAAKEPVLTYQLKWINWGSVKTPIITQNLNGPCPLLAIINVLILKRKIQLPSMMDVITDDQLMEYLGDCIISSVPKNIPEGVQLNYEQNFMDAMQILPKLPKGLDVN | Function: Hydrolase that can specifically remove 'Lys-48'-linked conjugated ubiquitin from proteins. Has exodeubiquitinase activity and has a preference for long polyubiquitin chains. May play a regulatory role at the level of protein turnover.
EC: 3.4.19.12
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).
Sequence Length: 203
Sequence Mass (Da): 22268
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A0A355G8T5 | MLRLSLLVLSLIVLCCVGCSGEVPTASDPEVPQAAEAGGKDTPSGADDYQVLLETTKGNIKLEVHPEWSPRGAERFKELVKNGFYNDTAFFRVIEGFMAQTGINGDPELHAKWRDNNIMDDPVVESNKRGYVSFAKTGMPNSRSTQFFINFGDNSNLDGMGFSPFAKVVEGMDVVDSLYNGYGEGAPQGRGPYQGKIVDEGNAYLKKEFPMLDYIKKATIVGEQPAETSEKAESKPETDNPGSEKPAAKEEEKTDAPAAEKKEDAAAKPETEKPAPATKE | 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: 280
Sequence Mass (Da): 30393
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A0A072VCD2 | MAFNQYFEEGMNQIDSLEEKSSQEMWKCASAEAISGSSGFDCNICLECVQDPVVTLCGHLYCWPCIYKWLNFHAENQEKQKEEPQCPVCKSEISKSSLVPLYGRGQTTPPSKGNDHQIGSVIPPRPLGPSWMTNLPRSLDAANVSQHNSRTYHPHYLNHSQRYASPMLNTGGSLPNPLDTSYGVFGEMIYARIFGNQVTNIYTYPNSYNLTGISNPRIRRHLMRADKSLGRICFFLLCCTVLCLLLF | Pathway: Protein modification; protein ubiquitination.
Function: E3 ubiquitin-protein ligase.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
EC: 2.3.2.27
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 247
Domain: The RING-type zinc finger domain is responsible for E3 ligase activity.
Sequence Mass (Da): 27874
Location Topology: Single-pass type IV membrane protein
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A0A7R9KUZ5 | MSSESDNTTKYLIQSLMWRQCVSEDNLKRLVTKCKRGEEAATEASNELVAEVVTRVNRQMRAYNISVSRGPNESDGTIYYALINTADNDITRMANSWSQKELLYFRKLMAAIIENKNSCIASTKMLNIGREDDIKFSLPVSETLTNKWVEQKWFEDVSDGKIAIGIRTLLEMSVYIRERFEVQDCFRCKILCIRGLNCMSCDTKLHYHCSDVQFIPDNKCPNCAKQFASTTTQNTNQSDSDSVANDSTQGVNGSAHNHRIDDSTDEETVEDLNEAIVGDSDEEPIQRRRSGRSKRSRLS | Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
EC: 2.3.2.27
Subcellular Location: Nucleus
Sequence Length: 299
Sequence Mass (Da): 33974
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A0A7R9Q094 | MRHKYELIIASNDRPVVHSLHNKNLTFYVFLLLSLIVISFVIYLCNYYDIKHTTHQPFLHRYGPLVRYKSQYFVNPKLWNTERDDNSDDVPNEVISRSDMFDMTADDVMVFLQIHNTGGNVFLNHIINDLIVDNPCNCESNRRKRCQCLRPNRHNSQWLFSRLTVGTKCGIHPDFNELIHCCDRVLDELEGDSVKRRYFYITLLRDPITRFISEYNHFRGQEANGKASRHWCGGREVMQMPECDFRADVTIDEFMDCEDNLAINRQTRMLSDSALVGCYNRSYMPSEERHIVQLRSAENNLHKMAFFGLNEFPRISQHLFEETFDLVFLDADTHGLHRYRRSLLDEFSAKTIDKIKRINSLDIKLYEFAKQLLFERFAKLKNKNSKLRDQSVSSLANDNTDITNWGDSEDKLNS | Function: 6-O-sulfation enzyme which catalyzes the transfer of sulfate from 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to position 6 of the N-sulfoglucosamine residue (GlcNS) of heparan sulfate.
Catalytic Activity: 3'-phosphoadenylyl sulfate + alpha-D-glucosaminyl-[heparan sulfate](n) = 6-sulfo-alpha-D-glucosaminyl-[heparan sulfate](n) + adenosine 3',5'-bisphosphate + H(+)
EC: 2.8.2.-
Subcellular Location: Membrane
Sequence Length: 414
Sequence Mass (Da): 48777
Location Topology: Single-pass type II membrane protein
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G7KI20 | MLSELLTNWTIYANKCEAFTSLLVGLDLAVRLLPLVDNSPTIGGFLAEVFLGLVLFHSTMTKKQRNL | EC: 3.4.21.-
Subcellular Location: Membrane
Sequence Length: 67
Sequence Mass (Da): 7439
Location Topology: Multi-pass membrane protein
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W2MAC6 | MRIAFVLLFVSAIVLVDSADALFPTAVRSERVLQGAQSGGMRSLRVHNEERGLPFFGGKSSNTKVSTTWLRDTTVYDDILTNAGFTTAFGIWKQNKYSEGKITRAMNKLGRTQDEIDRVLAGYRKFKNVKVR | Function: Effector that suppresses plant defense responses during the early stages of pathogen infection.
Subcellular Location: Secreted
Sequence Length: 132
Domain: The RxLR-dEER motif is required for the delivery of the effector to the host cell cytoplasm.
Sequence Mass (Da): 14806
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A0A832D1W3 | MGKEATIWEHLEELLIRLRKALLVFAIATLIVPFIPVSLSSYKPLIYVVPQFILDRVAPDTIEVFGHVIEIKLAQASPFGGLKILLYSAILIGFIVSSPYIAYQIYAFIEPALYPHEKRWLLVGGFVAVILFLTGVIVALLAVLPFTYRIMFIISYSVVGDKLIAFADPVDILSSALLITVATGVAFEIPLVIFFLIYLGIIEIKSLTGTYMRYLLIVSAIIAALISPDPSGLGMILVLVPYYILIVIAVIIANILKSRRK | 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.
Subcellular Location: Cell membrane
Sequence Length: 261
Sequence Mass (Da): 28838
Location Topology: Multi-pass membrane protein
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A0A072UQB7 | MTVLLLRRRLGRRNVAGRGNTRLMVTLLLVLAPVSSPVAATSAASAGDSGNADAPPKKHRGRPPGSGKKQLDALGAGGTGFTPHVILVESGEDITEKVMAFSQTGPRTVCILSAIGAISSVILRQPASGSIARYEVQLVNGQFEIVSLSGPMPLSENNGEQSRTSSLYVSVAGADGRVLGGAVAGELTAASTVQVIVGSFIVDRKKSSSSMVKSGPSSAPTSQMLNFGAPTTPTSPTSQGPSTESSEENDHNSNFSRGPGLYNNANQPVHNNMQQMYHHPLWAGQTHP | Function: Transcription factor that specifically binds AT-rich DNA sequences related to the nuclear matrix attachment regions (MARs).
Subcellular Location: Nucleus
Sequence Length: 288
Domain: The PPC domain mediates interactions between AHL proteins.
Sequence Mass (Da): 29893
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A0A158R9V1 | MAHTSIGPTYQFQIQLVLEEPHNLCVGSLSTGYLGALAEVPTRYIGGSGMREKCMRWGWETRGRSLPEGLKTTYTLQNCFSPVIRKNAINSRNDVFGRIAAWISQIPLIVGFSVLCLVFFHRDLHTIFYAVGMLANEAICKISKKIIRIPRPPTHPQSLVSSYGMPSNHATFMFFMMAYFSLFIKFRLSPRHYSTFARCFTVLFLFLISVITCYTRVYLEFHYVDQVCIGALVGSILGCLWFYVVQVILTPLFPRIVESKIGRTLMLQDFTHIPNIFTFEYNAVRASRPQ | Function: Required for efficient N-glycosylation. Necessary for maintaining optimal levels of dolichol-linked oligosaccharides. Hydrolyzes dolichyl pyrophosphate at a very high rate and dolichyl monophosphate at a much lower rate. Does not act on phosphatidate.
Catalytic Activity: a dolichyl diphosphate + H2O = a dolichyl phosphate + H(+) + phosphate
EC: 3.6.1.43
Subcellular Location: Membrane
Sequence Length: 290
Sequence Mass (Da): 33141
Location Topology: Multi-pass membrane protein
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