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TMCA_PYRAB
ID   TMCA_PYRAB              Reviewed;         817 AA.
AC   Q9UZ78; G8ZH77;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=tRNA(Met) cytidine acetyltransferase TmcA {ECO:0000255|HAMAP-Rule:MF_01886};
DE            EC=2.3.1.193 {ECO:0000255|HAMAP-Rule:MF_01886};
GN   Name=tmcA {ECO:0000255|HAMAP-Rule:MF_01886}; OrderedLocusNames=PYRAB12760;
GN   ORFNames=PAB2428;
OS   Pyrococcus abyssi (strain GE5 / Orsay).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=272844;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GE5 / Orsay;
RX   PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA   Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA   Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA   Weissenbach J., Zivanovic Y., Forterre P.;
RT   "An integrated analysis of the genome of the hyperthermophilic archaeon
RT   Pyrococcus abyssi.";
RL   Mol. Microbiol. 47:1495-1512(2003).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=GE5 / Orsay;
RX   PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA   Gao J., Wang J.;
RT   "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT   Pyrococcus furiosus DSM 3638.";
RL   Curr. Microbiol. 64:118-129(2012).
CC   -!- FUNCTION: Catalyzes the formation of N(4)-acetylcytidine (ac(4)C) at
CC       the wobble position of tRNA(Met), by using acetyl-CoA as an acetyl
CC       donor and ATP (or GTP). {ECO:0000255|HAMAP-Rule:MF_01886}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + ATP + cytidine(34) in elongator tRNA(Met) + H2O =
CC         ADP + CoA + H(+) + N(4)-acetylcytidine(34) in elongator tRNA(Met) +
CC         phosphate; Xref=Rhea:RHEA:43788, Rhea:RHEA-COMP:10693, Rhea:RHEA-
CC         COMP:10694, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:74900, ChEBI:CHEBI:82748, ChEBI:CHEBI:456216;
CC         EC=2.3.1.193; Evidence={ECO:0000255|HAMAP-Rule:MF_01886};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01886}.
CC   -!- SIMILARITY: Belongs to the RNA cytidine acetyltransferase family. TmcA
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01886}.
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DR   EMBL; AJ248287; CAB50181.1; -; Genomic_DNA.
DR   EMBL; HE613800; CCE70714.1; -; Genomic_DNA.
DR   PIR; H75035; H75035.
DR   RefSeq; WP_010868389.1; NC_000868.1.
DR   AlphaFoldDB; Q9UZ78; -.
DR   SMR; Q9UZ78; -.
DR   STRING; 272844.PAB2428; -.
DR   EnsemblBacteria; CAB50181; CAB50181; PAB2428.
DR   GeneID; 1496660; -.
DR   KEGG; pab:PAB2428; -.
DR   PATRIC; fig|272844.11.peg.1357; -.
DR   eggNOG; arCOG01951; Archaea.
DR   HOGENOM; CLU_004652_1_0_2; -.
DR   OMA; NEPDDLG; -.
DR   OrthoDB; 2707at2157; -.
DR   PhylomeDB; Q9UZ78; -.
DR   Proteomes; UP000000810; Chromosome.
DR   Proteomes; UP000009139; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0051392; F:tRNA N-acetyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0051391; P:tRNA acetylation; IEA:UniProtKB-UniRule.
DR   GO; GO:0002101; P:tRNA wobble cytosine modification; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_01886; tRNA_acetyltr_TmcA; 1.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR000182; GNAT_dom.
DR   InterPro; IPR007807; Helicase_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR032672; TmcA/NAT10/Kre33.
DR   InterPro; IPR013562; TmcA_N.
DR   InterPro; IPR024914; tRNA_acetyltr_TmcA.
DR   PANTHER; PTHR10925; PTHR10925; 2.
DR   Pfam; PF08351; DUF1726; 1.
DR   Pfam; PF13718; GNAT_acetyltr_2; 1.
DR   Pfam; PF05127; Helicase_RecD; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF55729; SSF55729; 1.
DR   PROSITE; PS51186; GNAT; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; ATP-binding; Cytoplasm; Nucleotide-binding; RNA-binding;
KW   Transferase; tRNA processing; tRNA-binding.
FT   CHAIN           1..817
FT                   /note="tRNA(Met) cytidine acetyltransferase TmcA"
FT                   /id="PRO_0000403132"
FT   DOMAIN          469..664
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01886"
FT   BINDING         265
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01886"
FT   BINDING         289..298
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01886"
FT   BINDING         439
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01886"
FT   BINDING         589..591
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01886"
FT   BINDING         596..602
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01886"
FT   BINDING         629
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01886"
FT   BINDING         636
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01886"
SQ   SEQUENCE   817 AA;  94668 MW;  F058E4DE3F9BB9F7 CRC64;
     MTIKIRFPKD VREYARKEKV KESIIKLTET SLAEAITNFH RRMIILQGDT LEKAKLAGIL
     AGGVARILSE YIPEFLDRKL RDEDKIEVLY ATDALGEDTY GRKRFEEFRK HFSVLAPNAE
     LTSVTFKYSR DILGRTFDIL VLDLSYDYSP NDLGRIIETV RGGGLIFILT NPFEKWKDMW
     TGFHKSLVTP PYTIDDVKKR FNRRLIRKFT EHKGIYIVDA DKKKIERRPR KNKSQAKLPE
     REKVEIPRDI KFPRELYELC LTRGQVEVLK ALEDLIENPG MVVLTADRGR GKSVSVGIAS
     IGLAITSKKK NFRIVVTAPE LENVQSLLKF AERSLKVLGY KTKTVKESGL IKEVYAKGIG
     IRYYPPTKGY RQKADLYIVD EAAGIHVPIL HRYLEKERVV FSSTIHGYEG AGRGFSVKFL
     KKAKEKREYK EIHLSVPIRY AEGDPIERWL FDVLLLDAEP VELTEEDYEL IRKMEVYLEE
     PDLDDWFEND REDLRHFVGI YVLAHYRNRP SDVALLADAP HHEARVLRLK NGKIVTAIQI
     AKEGGIPKAV IDKMAKGYKP PGNIIPDMMV KHHYAKEFAK LRGYRIVRIA THPDAMDLGL
     GSKALELLVK EAQEKGLDWV GSGFGASEEL IRFWVRNGFA VVHLSPTRNP VSGEYTAIVI
     KPISERAKEI VKKANDEFRL RLTEWLGDTH RDLEPEIARW LFETPFGEAV NYPIHLTKVQ
     RKRLEMFIKR VLTYDTVVDA VKPLVKLYFL DGWMRPYLDD RQIALLIHRV LQAHDWKETA
     KLLNRTELYT MIELRDIVRG LWYYYKHMLK DEEKDIS
 
 
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