ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
|---|---|---|
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
|
A0A024TM56 | MVNPLTRCMEDYCLPPYATFHTDDIVPAVRTALAEYALDLNALEDDLMDAGESNLCWESVMDRLEIIDDPLRRISMFLEHLRSVVDSPDLRAADAEIQPEILAMNNRRDQSDVVFQAMQRLRSRADFNTAFTTEQQRILTRKVLHATLNGAALGPCVKERFNEISVRLETLKMKFSENLMDAMNAFSRIVHDKHELQGLSDATLAHLAQNAVADGHKEATAATGPWKLSLEYPVYMPVMKQCSHRHTREILFRAFVTTASTPPFDNSPVVQEMLELRQARAQLLGFQTYAELSLQDKMAPSVEVVEDMLNDLRDKCLPLS... | 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
... |
T2MFJ3 | MFSSIYDFYKRHRKKIIFTGIFVGSTYAITKLVSWKFNEWAELKVKEMEQEAKKQYLFESNQRTCTATFLSFLPDVQEVITSKTNLDQFLEILKLNPANKIEIWENIKILSMAQMIASVLSNILLLVLLKVQLNIIGGYMFVTMMYDKEMDVSDIQKRYLSNVKVFIEQRLPLLVDDVILSVKEIIGNVSLKEKISFLKLQSLTENVIEKLKSNHLKKSVNFSHPFSWYLINNETSNTEERYRRLMFQTNETLSGDSCALVLEDCISSGLQSILNNLKDVFFGYEEDPEAITSIESCAHTSFFKEIELPMAKITPLLNQQ... | 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 Ma... |
A0A7R9Q7K4 | YYKLPNFIGILCVFGICFCALLYIKGLLLPSKGLYNRTKNPIFDYYWGIELYPHITPIISLKVWIICRFGLILWQYIVLLCWKANYETLPDGSINYSLTATTLLQTIYLMKFYYWEDGYMNTIDTSVDRFGYYVCWGCIAFVPGFYPITSVYLVDNTPYNEFGIKSLIAVLTVGLLVICLNYWADQQKLHFRATNGKCVIWGKPAKLIRAEYIDDFGKRKRSILLTSGFWGITRHMNYTFELLSTFLWCLPALYASPVPYLYLIFLTVLLIHRSVRDDNKCALKYGQYWQQYKHQVKYQMIPYVY | Pathway: Steroid biosynthesis; cholesterol biosynthesis.
Subcellular Location: Membrane
Sequence Length: 305
Sequence Mass (Da): 35911
Location Topology: Multi-pass membrane protein
|
A0A7R9L0G5 | MNKLVKKSLPLVCVVTQLMAMLLFAFSFFDVEETLFSPGSAANTGHTIGPRSAVDLIRSDVHYKQIDDYCRPRLTTTTAKPMFNKLVLVVIDALRHDFIPSIDRPPKSVQSGDRRHRHRRASGDSGGHRMPFTESIMQTNGVGLVSISATPTVTMPRIKAMISGTLPSFMDFILNLSAYRFNGENIVENAFKANKKTVFFGDDTWIQLLPKEVFAKYNGTSSFFATDYTEVDTNVTYCVRRELKALHEWDVMITHYLGVDHIGHSHGGYHSKLMPKKLLEMDAVVESIYTRVSAPDVREPYLVVITGDHGMTDIGNHGGN... | Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 658
Sequence Mass (Da): 73719
Location Topology: Multi-pass membrane protein
|
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
|
A0A072VFT5 | MGTTVDDSCATQLIDGDGVFNLTGLDNFIKTSNMANTGLSYAVVAIMGPQSSGKSTLMNHLFHTSFREMDAFRGRSQTTKGIWIAKCTGIEPCTIAMDLEGTDGRERGEDDTAFEKQSALFALAVSDIVLINMWCHDIGREQAANKPLLKTVFQVMMRLFSPRKTTLLFVIRDKTKTPLENLEPILREDIQKIWDGVPKPQAHLHTPLSEFFNVEVTALSSYEDKEEKFKEEVAQLRQRFYHSIAPGGLAGDRRGVVPASAFSLSAQHIWKVIRENKDLDLPAHKVMVATVRCEEIAYEKLSQLRSDKGWLELEEAVQSG... | 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
|
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-Y... |
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... |
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... |
Q08W44 | MIRIDGSKGEGGGQVLRTSLALSLVTGTPFQLVNVRAKRAKPGLLRQHLTAVKAAAEVGAAEVEGAELGSRELTFKPRALSAGNYYFSVGTAGSATLVLQTVLPALMVASGPSTLMLEGGTHNPAAPPFDFLEKAYLPLVRRMGPRVDAVLERHGFFPAGGGKFRVNVLPAPLRPLVLLERGRVKRRQATALFSQIPFNVAQRELATVEQVLGWRPDEQRVEELKRSQGPGNALMLEVESEHVTEVFTGFGERGVRAEEVAGRAAEAAKRYLDAEVPVGENLCDQLLLLLALAKGGAFRTLPLDGHSQTQLETFAHFLEV... | 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'-pho... |
A0A7V6V2F2 | MRRKTLQIPIGNILIGSEYPIIIQSMTNTLTSDIQSTVNQCIRLFDADAKLVRITARNLKEAECLKLIKNDLINMGYELPIAADIHFNPHLAKVAANYVEKIRINPGNFVNLFPNNKSYTNEQYKLEVDAIKNEIEKLLPILVANKVAVRIGVNKGSLSQRLIDKFGNTTEALVESAIENVKIFNKLNFNNIVISIKTSSVYETIAANRLLVSKLDKLGLYYPIHLGVTEAGIDKEGIIKSSVAIGNLLLDGIGDTIRVSLTGDPVKEISVAETIIKTYQKFLPLPPMPTYSYTLENAPKIFTINDLTTEHLDLNNLFID... | 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-diphosphat... |
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 pr... |
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
|
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
|
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
|
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
S... |
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... |
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... |
A0A072TYF3 | MLKDLSQKPLISILVLIFSTVIVLSTPPEDPIKCSNSQNTTCTITNSYGMFPDRTICQASQVFYPTSEQELVSMVASASREKIKVKVATRYSHSVPKLVCPEDSNGILISTKYLNKVVKIDVEEKTITLESGVTLKQIINEASKNGLALPYTPYWYGLTIGGMIGTGAHGSTLSGKGSAVHDYVVEIRIVRPSDSDDGYAKVEILNEQNNEDFNAAKVSLGVLGVISQVTLKLEPIFKRSITYVAKSDSDLGDQVVSFGHEHEFADISWYPSQHKAMYRVDDRVPINTSGNGLYDFIPFRPTPSIALAAIRITEDLDEFT... | 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
|
A0A7M7L828 | MIEMASIIVRRSFYASASQARSVGVLGIPMWRGQKKLGTDLAPAKIREDGRLISGVETVVGKPVRDFGDLDLSSYSQCDKNVTHYMAKTAQSIRKSVIHCLRECEQLITLGGDHSIAIGTVTGHADYVKEQGRDLAVIWMDAHADINTPMTTPSGSWHGMPVSFLMHEMMAHLPRIEDFKDWPSSISAHALVYVGLRDVDPQERWFLEKLQVPNFSMRELDALGIHKVTEIALDKVDPLGRKSLHVSFDIDCLDPLVAPSTGTPVPGGMSLREVAVLAEAIASTHSLTVFDLVEVNSLIGSYEDASKTIQSAALITRWMF... | 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
|
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
Seque... |
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
|
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 ... |
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 Leng... |
T2M3R3 | MVSKVYVNGFVDCCFKKYILNQMKPNRRFFCLSSIVTNDFNEKDYKFHYLNSNVFQSKSTKDLIRSFVVLKTSSIGRFVDYSERMFLIGEKIIWAPLFRWLMKSTYYGNFAAGETVDEAKATADKLKTHNVLTMLCVPIESKKFSSNQEAEFEYEKNFNTVLRCIEETAAIESNGFAQLKITALCDKELLVNANKQLEKYQYSHNEDENWDIRTVVDLIKSCQYSKIKLSGLSDESNKKFVKLLSYLDKLAQHSAKHGVRLMVDAEQTYMQATLNYLVLVLQAKYNKERHIVYNTYQCYRKDTFKRLQADHNLAKNLGFL... | 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
|
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... |
A0A7M7MCT0 | MGLLTRLGILCLRTKQIPRLNSRGLLEEPRNSRATFIYARSTWATRTNDNVNISNQTTPKAQDIKTVSLERFVSVSPSWLQPYLRLMRIERPVGTWLTLLPSLWALTTAAPAGSLPDPRLAALFCTGALLMRGFGCTINDMWDRDIDRQVERTRQRPLAAGRLSRWDALWFAGGQAGLACLVLLHFNWNTVMLGLASVGLVVIYPVMKRFTYWPQAILAVVFNWGALLGFSAVQGADMSWTTALPMYAGAFSWTLIYDTIYAHQDKRDDLLVGMKSTALRFGARTPLWLGAFSTSMTTGLIVAGITENMGWPYYAAIAAS... | 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, ge... |
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 (D... |
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
|
A0A7R9KVR2 | MAPNIQSPIEPEISDISDGIKTRRDFKVEIVWRNVAIMSGLHLAALYGLYLCFTSAHWQTMAFAVFLYVISGLGITAGAHRLWSHRAYKAKWPMRVILTIFNTVAFQNSIYEWSRDHRVHHKYSETDADPHNANRGFFFAHCGWLLCRKHPDVIEKGRNVSCEDLLQDPLVRFQRKFYLPLVLVFCFVLPSIIPNILWGESCFNAYFVCGLLRYCWTLNMTWLVNSAAHFWGRKPYDRHISPAENKVTIIGAIGEGFHNYHHTFPWDYATSELGRDYNLTTCFIDVCAKIGWAYDRKTVSPNMIRQRKERTGDVKEKGPY... | 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
|
T2M855 | MSVLVETTLGDLVFDLYTEERPRSCMNFLKLCKIKYYNFCCFHSVRRNFIAQSGDPTETGRGGVSVYSFVYGDQAKYFELELKPRIKHRTKGTISFVNNGNDMHGSQFFITLGDGLDFLDGKHTVFGQLAEGFDVLEKLNEVICDDSHKPFQDVRITHTIVLEDPFDDPKDLPIPDKSPEPTKEVLESGRIAAGEKINDDDVSKEELLKKIEDKELAIGTKILETVGDIDDADLKPPENVLFVCKLNPVTNADDLKIIFSRFGKILSCEIIKDQKTGDSLCYGFVEFKEVEACEKAYFKMDNVLIDDRRIHVDFCQSVSK... | 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 (D... |
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-car... |
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-gly... |
A0A7M7JRE0 | MGDGWALFVLSSSMFVGCYLSGLIPVSMKLSEDKINVVSILGAGLLVGTALTVIIPEGVSTLYLSRLEKAHTDHHQEVATEARHSGHHHEAHHFDDPHSLIGITLVIGFVFMLLVDQCSKRGKSSEELLPTGPNKTGAISIWKTRPATATLGLVVHAAADGIALGAAATTTRAEIEMIVFLAIMLHKAPAAFALVSFLLHEGLDRSTIKKHLLLFSAAAPILAITTYFGISQNTKESMASMNATGIAMLFSAGTFLYVATVHVLPELAASKGNVLGNKRRRCVSPTIQRRPSFLGKYLGRFYRSESYDWKLLSENSAFLS... | 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
|
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 biosyn... |
A0A8T4Z7E4 | MVTEGFPFPTTILSEGKVRILVPRATIEGPSLKGPSSRRFPVFYNPGMALNRDLSVLALRVERRLLGREALACDAMAGCGAKGLRLAAEVEGTRILLNDINPMAVRLINYNVRLNALEERAIVRNEDARLLLLERAFREGTLDYVDVDPFGSPAVFVEAALCSLVDGGFLALTATDTAVLNGVHAEACIRKYWAKPLRCEYHHEVGARILLGYTARVAAMHGFGISPLLTERSSHYVRTIVSINRSSKSLRETMNSLGFLFHCHSCFHRHLEPYDHAHKRTGLVCSCGSKLSWAGPLWIGRLGDKAFLKSMLQESEKGAM... | 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... |
A0A7M7KLG9 | MQTSSGQRPRNGGRTSDRPRGFGGGGVNRGEGGGRGENGGRDEVTYSRFEGTIGRGFRNEGAHSRAGGSGGCGGEKGDRRRLSPSSRQQGAPGEGRGPPRMKTLPIVDTGGENTTSAVNECVVCCREILVYAVGSCDHSVCYVCSTRLRVLCKTQECPVCRATVEEVYFVKENTPFGELKEKTFNLKQKQFSIFFQDDEVQLKYEELLRHKCKECERRALIAARSGERPSALEVFPTFDDLTDHVLKEHRRHFCALCVEHLNLFTFERQAYSKNDLRRHMIEGDLDDKSHKGHPRCDFCKEHFLDKDELYRHLKVEHFTC... | 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
|
T2M3E7 | MRKKYVVFTFLLLFLAAICIYEWSTNLEEVIILPEKPVNSFNRFSLKSILLWNDLFGKENWGFPRSTNYDFKELECRVQNCFITTNRDLTLDADAVIFHISGKLNSRPKLKPVNQRWVFLMHEAPCLHNFKSLRQWNSLFNWTMTYRLDSDIPIPYVHTCKKRNSKVNLLEKDIMGKKKKLAAWMVSNCNSQSQRNQYMNELLKYIPVDIFGKCSALFGQNNKCEKNDEENCMNMISSQYKFYFSFENSFSVDYATEKFIKVLNTNAVPVVRGDANYTVLGPPNSFIDTKKFKSAKHLAEYLLRLDQNEVEYLEFLKWKE... | 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
|
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 construc... |
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-hydro... |
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 s... |
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
|
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
|
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... |
A0A7R9L7G4 | MSAKVTLVSSSGCFGGKQQVWSHDSHELKCKMNFSVYIPPKVTDGVKVPVLFWLSGLTCTEQNFIIKSGFQKYAAEEGIIVVGPDTSPRNVNIEGEDDAYDFGSGAGFYVDATQDKWKQNYRMFSYITKELPKVIDDNFPVIKDCRSVFGHSMGGHGSLICALKNPGLYKSVSVFSPIANPMVGKWGQKCLSGYLGDNQKVWEEWDATVLVKKYKGPPLHLIVEQGADDPYLADELYVQNFVDSCASAHVAVDYRLHEGYDHSFYFISTFLAQHIKHHSRILYNTVWSHDSHELKCKMNFSVYIPPKVTDGVKVPVLFWL... | 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
|
A0A072UYZ3 | MAGRFLGSSSASIDMIVTNTPSQELALTNLAFISASDLPKFAVPGHDNLYLASIGDSFVFSISYPSFTTHESIRGGHIALNSIQRRCARVSAAESVPVTRFVPPENFNLAVLQLELEFIKKAGNKNEQIDAIVLAKQLRKRFIKQVMTAGQKVLFEHQGNNYSFTVSQVTVEGQQRSSSIDRGMISEDTFIAFEASRDSGIKIINQRESTTSNIFKQKEFNLESLGIGGLGAEFADIFRRAFASRVFPPHVTSKLGIKHVKGMLLYGPPGTGKTLMARQIGKILNGKEPKIVNGPEVLSKFVGETEKNVRDLFADAEQDQ... | 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 p... |
A0A6P8ZM77 | MVTLFALVVLVTLWLARYAAGRVKVTSLLAAVPGPSYPLPLIGHLIYMFGPMDGILDRGIRLYRTYGPGPIKFWIGEWPSVQIMRPEDIEPVLNSQKEVEKPDLIYKPVRAFFGDGLITLNGDAWFKHRRALTPAFHFSVLERYAGIFTRRAAAFADLLLAEVPADKTVNIMKFHSAFVTETIMETAFGMPPASRASSVQNKEMSDLVRATEDAFGVIVHRIFHPWLLIDALFKLSHSGRVNQRAEAIITRHAKAVIAQKKLELQQRRAAGDDDDAPDADEDAGVRKKYTFLDMALGGKSDVLSDAEILEEVRTLIAVQQ... | 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
|
A0A2E4AY97 | MANFITLAVDGGAGTGKSTLSKLISSENKFMYVETGSLYRAITYLMLEMKISPIDVGSEISGKELEFTSKIIKNKYFLYVGGRDCSLLDLRTAQINKQVSDYAALPAVRSFLIEFQRSQVGVAKLNGFKGIVMEGRDIGTKILPDADLKIFLFADFETRMKRRKKDGELDEIRNRDLKDLQRKASPLQRAEDALSINTAIHNQTETYSIVNRELLRLK | Catalytic Activity: ATP + CMP = ADP + CDP
EC: 2.7.4.25
Subcellular Location: Cytoplasm
Sequence Length: 218
Sequence Mass (Da): 24554
|
A0A173YMP4 | MGNYYQPEIETMPVEKLQALQSERLVEQVKYVYDHVEFYRNKMKEAGVEPEDIKGIEDLHKLPFVTKDDLRDQYPYGFLGVPLSECVRMQSTSGTTGRRVVAFYTQEDIDVWEDCCARAIMAAGGTKDDVCHVAYGYGLFTGGAGLHGGSHRVGCMTLPMSSGNTERQIQFMEDLGSTILCCTPSYAASLGESINEGGHRENIKLKAGIFGAEPWTEEMRHNIEESLGIKAYDIYGLTEISGPGVSFECEEQKGMHIQEDHFIPEIINPDTGEVLPEGEIGELVFTCITKKAYPLLRYRTRDLCYLTRKKCSCGRTHIRM... | 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
|
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
|
N6T332 | MTEHLHDVVLPDNITEELLTSQHIDFIKKYGEEQNKFEYGMTDYLRLSGMYWGLTALELMNAGVTDTQDAIVEYIVKCQDPDSGGISACIDHDPHILHTLSGIQILAMFDKLDAIDIEGVVKYVQKLQQFDGSFSGDKWGEVDTRFSFCAVMILSILNRISAIKVQKAVKFVKSCKNFDGGFGSRPLAESHAGLTYCCVGFLSITKRFDVLDIDNLAWWLCERQNPSGGFNGRPEKLPDVCYSWWVLATLAMLGKLTWIDGAKLQTFIFACQDQETGGFSDRPKDVPDPFHTLFAVAALSLLDYENIQKVNPTYCMPQHV... | 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-ger... |
T2M6D1 | MGSIISKFQKKKSTQETLEIMEKEIDKLEENQNRNRDLQKSIVLSFLIFSVILYVLAAVIFYLWYFPKKWLQRLLYLLPFIGFPVLIFFLKKLLHFIFVTRIARNARTLANLKKEKKRILENVMETETYKVAKDILQRFDPKRKLVEQDFSIAENKTPSKDSDNKMLTTSITTSQVTPVLRNKPPQVTSNNIVNSRNGPQLVSPGQQGPTPNKFLGQQGPSPYKIAAPILPQNRSAFDKIAEYFVGDGPSNRYALICKQCFSHNGMALAEEFEFISYKCCYCNTFNQARKQRSHAPKLSQHDSDQSDSDHSKDKLNINGI... | 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 protei... |
N6TQL3 | MLIVHSMIVIIVLSFTDGARILGIFPMAAVSHHTLYSKLMKGLAEAGHDVTVVSPYRLKELPKNGKYRDVVLEGFAAEYEDKLKSLNYFELREKSLIDRYFHFTALMLPTTNHTLHNANLKKLVESNETFDALILEQMFNDNMKVYGYIFNCPVILLSPFGPNSWVNPTVGNPQPPSYVPQMNQQDFSNDLSFFNRANNLYCFIVEYLIFKYYIFPQQERMMHAIYPDAPPLDDLYSNVSLVLLSSHTSIWSPVPLVPNMVEIGGFFIDPPKKLPPDLQEFMDKATEGVIYFSMGSNLRSKNIPLEKKQAFLNVFKKLKQ... | 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
|
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:... |
H8YHY2 | MIERNPEKNWPACLEHNKPLGPLISMATPATARAFCRVESLADLQAALAWANAESLPYMVLGGGSNLLFVDDYPGLVIQPGFSQLALAPGAEGQYQLVGGAGVPWQQVVDFAVARNLWGLENLTRIPGSLGAAPIQNIGAYGVELDQVFDSLTALDVQRGEVVAFSREQCGFGYRQSVFKGDGKGRYIVLEVRLNLSAEPRPVLSYQGLEDLAGESALTPAKVAAQVAALRGQKLPDPAALPNSGSFFHNPLVSHAQADRLRARYPALVSYPQPDGRVKLAAGWLIEQAGFKGFAEQGVGVHRAQALVLVNPGRESGARV... | 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
|
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+)-... |
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 Le... |
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-cytoc... |
A0A355IKH3 | MHDDNIGKVDHQAEVDALYMRRCLQLAASGRETSQPNPMVGAVVVKDGRIIGEGWHKRVGLPHAEPMAIGAVKNQECLGQSTLYVNLEPCSHYGKTPPCVDLIISKGIPRVVIGTPDLFPLVSGRGIEKLRGAGVEVVVGVEADACRELNRHFFTFHALKRPYVTLKWAMTADGFLDYQREAGDGRVQLHISTPYTRLLTHKSRAEHAVILVGRKTALLDNPNLTVRDWYGPHPIRAVIDRQLSLPLTLNLFDGSVKTLVFTEVERQDREGVSYIRLDFSQPVIEQLLQALYERNLQTLLVEGGSTLHNAFLSSGCWDEI... | 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... |
A0A072TRD5 | MGPISDFPLMFIPPAMPSSPSSPELVHSEPNPNPIPEPEPNPESNTSHNAPSSPPQTTTNKPPPTAAEIAARYILQSPPLSFAPKPLSTSEVTAAFGVIDDLPSLTDEEQKPLSSILTTSSGDQFSGTSWWSNQLETGISALADLADLANPSDDDFGYQGYSIHTNLASYNSRKPFEIDNGGWSPVDYGYNFNNFFATASSPRSPSLKSVGAGITNMGNTCFMSAILQCFTHTVQMFLGLRYCTHASSCDVEGFCVICAFRDHLDDALERSRSPIVPRELVKNLNYFSAGFVIGNQEDAHEFMQYALNKLKRGFPVGEEN... | 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 ... |
A0A7R9PX17 | MVRLISMFRVVYRPLRMSSTTTHTNHTWKRLQYNRMKRFVAKFQWFHVPISLVFTFIAFQQFRRIKRREEQKRYEQNPNQILAKPIYTASDLEISMYKLLPLRTVSRIWGWINSIELPLIMRSPILRSYVRAFGCNLDEADVDDLRQYKNLGEFFRRSLKPGVRPIDTTNGIVSPADGTILYFGKANEGTVEQVKGITYSLSSFLGPXILYFGKANEGTVEQVKGITYSLSSFLGPQTWRSNGARNDNYEKSLLINSTGKQSSDLYHCVIYLAPGDYHRFHSPVEWKISFRRHFPGKLLSVRPTFVSWFPNLFNVNERVS... | 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... |
A0A520KEY0 | MEEILKEVLSRIKPKDEERNKVRQIFEEIKNRIEEKAKSLGINVRVELEGSVAKDTWISTDKDIDIFILFPHGTDKEKAKEIGLEIAKYGAGENWKIAYAEHPYIKKKIDEYEVDIVPGIEIKEGERPLTAVDRTPLHTKFIKSKMNEEMKDEVRLLKQFMKGIGVYGAELKIEGFSGYLCELLVLYYKNFKNVIKNASNWRPKTIIDYMNYYKDIPCEEIFDAPLIVIDPIDRRRNVAAAVSLQSYSIFVMASKFFLEKPSIEFFFPSKLNVNLNDIINEIKKREISLVMIKMKCPKIPSDILWGEIKKTINKFVKLIE... | 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 i... |
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
|
A0A938EMP7 | MSGVPMMPGMRPLFDAAAVRDADARAIAGGIPGEVLMETAGTLATREILAAFPPGSTATVLVGPGNNGGDGMVVARLLAEAGWDVRVQAPGAREPETPDGALMTARAAEAGIGVGDVDLHELRAGRRLVVDALLGTGTAGAPRGGVADAVEALVASGAAVVALDMPTGVDGDTGAAPAPAVRADLTITFAAEKVGLRVAPGRELAGRVVVADIGIPRDIQPDPAAWLATEGVIAAIPPRAAGDDKYAAGGVLAIAGAPGMSGAARLCTRAAMRAGAGIVAACVPHEVRVEVAIGAPEVMVTGVAGGAGMSLDALDAIMHQ... | 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... |
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
|
V6LZD9 | MTINKQQIISLKMSKMEKYAISAVSLLFVTTPNIMKLGNLHIFLNGQIVIGAKFQQAIYSMIGLLSPVLISIFSWAFLYNIQDASNIFIYRGACEAFITITCILCVFALFSVFITAFTDPGIIPGKELLESFTATLNEKIQSKSNTIRALPQTQKDLKISSNCQSQLPSESSMTLTILSSLHKPETPLKFQLKGYSFNSKYCSTCRFYRPLRATHASISNVCIQRYDHFCAWIGTDVALHNHGLFYLMLFIVFIQLSVMILINLTIIIYSIQAFVNIDVIPANLKGLGIFGMIMMLTLLGGAGYIIFSLCQLMQYHVNLL... | 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
|
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
|
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'-deoxyrib... |
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... |
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... |
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-cytoc... |
A0A3N5J2S7 | MNERIIFHLDMDQFFAAVEMLHQPHLRGLPIAVGGNPSGRGVVVTASYEARRFGIRSGMPAAEALRLCPQIVFVHSSVSKYCDVSARIFKSLLEFTDRVEPVSVDEAYMDVTDTVWKDGGVQGLAMKIKRRIVESEGLTSTIGAGPNRLVAKIASGMNKPDGFTYIPADRVEDMFRDMPVGDLHGVGKATQRTLESFGIRTAGQLAEFPVDILKRRMGKFGEELVRIARGEGSDKVLVPDEQPEEKSMGHEHTFSQDISDPVLLLGRLHLLCEKVARRLRSARMAGCTVAVRIRYRGFETVLHGCKLKRFVQHEMDIYPV... | 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'... |
A0A7J3LWH5 | MKLSDLGERKLIEIASSILEQDPDEILGLGVDDAAAKPICEDLYLVMHTDVVVESTDRLPGQSYRDLAWKAVTANISDIAAKGAKPYALLSAIGIPGIYSLEVFEELMAGLRDSSSTYGCYIVGGDLSSSRELFIALAILGLTHRDRIMGRRGAKPGDLVCITGEIGYTSLAYRVLFDEWCIDSDLRRIVLDRAYRPIARLKEGLALASTGVVSSCMDISDGLAISLNTLSEVNNVSIIIDHIPIPREVLEAVGRYSVDPIDLVLYGGGEEYELLFTVKPDGLKLVEDKLSSLKSSFTVIGRVSEGAGVYFTSGRRVEAR... | 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 + thi... |
A0A8W8MHS0 | MYRQCSRFSAWQVHKHFNSKVLTPNHGLIAKTRCVSSKTNLKTEDDQGTAFPEQMTHIKYASKGLEKFPQKYKQVPLTLFIKKSKTLVMLDEISEKFTVTFPKSEDTLTVDIGPEDFAKLKNMLEKDKRDSSPAHNPESITECIWQEMKTDNNKLMQYYFRLSKIRLTGLVVLTAMAGYAMAPAAFDPIGFTMVTLGTGLTSASANAINQFFEVPFDSQMNRTKNRVLVRGYLSPLHAVTFAAVSGSVGLVVLALGANPLTAALGAFNLGLYTLVYTPMKRHTILNTWVGSVVGAVPPLMGWAACTGSLDPGAWIMAAIM... | 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
|
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
|
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... |
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
|
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-... |
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
|
A0A1Q2CG59 | MRTVVSSAEMRAAEQAVFARDPEADLMGKAAAAIARIADDVAPDGAVLVVAGAGNNGGDGLFAAALLAERRPVLFWRAFRDAHAAAVAAARAAGCREVDAVGAVAALADCSLVIDAVTGLGSRPGLPLALQTLVDACDAATVPVLSVDLPSGLDADSGALHPSFSAEHTVTFGSVKPCHVQQPAASRCGRVHIVDIGVTVPDTQLRVAEAADVARWWPRPDASSDKYSRGVVLVDTGSEQYQGAAVLSCSGALHAGAGMVRYTGRAASGLILSRFPSVVVGEGRAQAIVLGSGWGDSDGGEGRVALARMHSLPAVVDADA... | 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... |
A0A2E3Z9C5 | MVAIAVPIRICCGIAVWERNNVIESLPAKNCWFLTGATAVGKTRIGLAMARRLHAEIISLDSMAIYQGMDIGTAKPTSDQQAEIPHHLIDIVPPDQEFSVACYLEAAHAKIEEIRRRGNEVLFVGGTPLYLKGLLRGLTPGPPANWKLREEIEAEVAKHGPQGLYRRLEQLDPVAASQIHPHDTRRLIRAVEVFRITGVPISHSQMQFEEEIPAEDCRVFALRRSREVQYERINERVDQMLERGLVEEVRSLIADIEELSRTARQAVGYQEVLEYLEHGDHEIMTAKIKTRTRRFAKRQETWFRSLSECRYFDLEDDCQV... | 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)-dimethylall... |
A0A072TFS9 | MEFSVRAAELTTLLESRITNFYTNFQVDEIGRVVSVGDGIPRVYGLNEIQAGELVEFASGVKGIALNLENENVGIVVFGSDTSIKEGDLVKRTGSIVDVPAGKAMLGRVVDALGVPIDGRGALSDHERRRVEVKAPGIIERKSVHEPMQTGLKAVDSLVPIGRGQRELIIGDRQTGKTAIAIDTILNQKQMNSRATSESETLYCVYVAIGQKRSTVAQLVQILSEANALEYSILVAATASDPAPLQFLAPYSGCAMGEYFRDNGMHALIIYDDLSKQAVAYRQMSLLLRRPPGREAFPGDVFYLHSRLLERAAKRSDQTG... | 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
|
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
|
A0A0K2Y9K6 | MFVDCVEITATSGKGGPGCVSFRREKFVMEGGPDGGDGGDGGGIVFKVDSNSDTLSAFRGKKHYKAQNGAPGGPKNCNGKKGQNLEIIVPPGTQVFNADTGELLCDLIESGAQTTLLKGGKGGLGNVRFKSASKQRPTYAQKGMAGVSLNLRLELKLIAHVGLVGFPNAGKSTLISVLSNARPKIAPYAFTTLIPNLGVVQAGQFKEFVMADIPGIISGASEGKGLGLDFLRHLERTKFLLFVLDTTYDIHQQYEELRHELAHFSQELSARDFGVVLNKMDIGQVYGFHAPKAQFVLPISAATTENTGQLLQLLAQALQL... | 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 ... |
A0A2T9Y967 | MSSEKVRSRKQQRYYMNSEFNSASQHGSDYDFNENEKYNLANPSNDLDYVPAYQKDHAVFQSTHLNQAKLADPTSGKRFRFTKKRLIVLGLVFLMAAYFRLWKLSHPSKVVFDEVHFGKHAGLYINRTFFLDVHPPLAKMMFAAAGKIFGYDGKFDFKTIGLDYTSTNVPYASMRFMPAFLGLAMVPITYITIAAFGGSEEACLLGSLLVTFENSFMTISRLILLDSILIFFTGLTVMFWALFLREEGHPFTKTWWVYLILTGVNMGNALSSKWVGLFLVGTIGVWTIKDLWFRITDYRVTLNEVNKHFWARVLGLIVTP... | 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 Locatio... |
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(... |
A0A072UQB9 | MAETRRTSSSSTTVLDSLGEEIVRIITPVSICMFLVVILVSILNTNDSPTISTIANIAYDETTSDSSWDKFLGALLNSLSFVVVVTFATFFLVLLFYFRCITFLKLYMAFSSFVVLGFLGGEISIFLIQHFSVPVDCITFLVVLCNFAVVGVCAVFMSKMAIFVTQGYLVVIGILVAYWFTMLPEWTTWAMLVAMALYDLAAVLLPVGPLRLLVELAMSRDEEIPALVYEARPVSNDCMDPRIIEARRRLWRERRIESAILITESGNSVLGSGGLNVEQSSHSNSDANTVLSTNLNENLTPENGSNLNSSSTYGTRNLVR... | 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 s... |
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
|
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 oxidoreducta... |
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, thio... |
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
|
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
Subcellul... |
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
|
A0A7R9Q094 | MRHKYELIIASNDRPVVHSLHNKNLTFYVFLLLSLIVISFVIYLCNYYDIKHTTHQPFLHRYGPLVRYKSQYFVNPKLWNTERDDNSDDVPNEVISRSDMFDMTADDVMVFLQIHNTGGNVFLNHIINDLIVDNPCNCESNRRKRCQCLRPNRHNSQWLFSRLTVGTKCGIHPDFNELIHCCDRVLDELEGDSVKRRYFYITLLRDPITRFISEYNHFRGQEANGKASRHWCGGREVMQMPECDFRADVTIDEFMDCEDNLAINRQTRMLSDSALVGCYNRSYMPSEERHIVQLRSAENNLHKMAFFGLNEFPRISQHLF... | 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-[... |
G7KI20 | MLSELLTNWTIYANKCEAFTSLLVGLDLAVRLLPLVDNSPTIGGFLAEVFLGLVLFHSTMTKKQRNL | EC: 3.4.21.-
Subcellular Location: Membrane
Sequence Length: 67
Sequence Mass (Da): 7439
Location Topology: Multi-pass membrane protein
|
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
|
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... |
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
|
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 dolic... |
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.