ID   TMCA_SULIY              Reviewed;         743 AA.
AC   C3N792;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   03-AUG-2022, entry version 65.
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=YG5714_1830;
OS   Sulfolobus islandicus (strain Y.G.57.14 / Yellowstone #1).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=439386;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y.G.57.14 / Yellowstone #1;
RX   PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA   Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT   "Biogeography of the Sulfolobus islandicus pan-genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009).
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; CP001403; ACP46086.1; -; Genomic_DNA.
DR   AlphaFoldDB; C3N792; -.
DR   SMR; C3N792; -.
DR   PRIDE; C3N792; -.
DR   EnsemblBacteria; ACP46086; ACP46086; YG5714_1830.
DR   KEGG; siy:YG5714_1830; -.
DR   HOGENOM; CLU_004652_1_0_2; -.
DR   OMA; GWRIMRI; -.
DR   Proteomes; UP000002308; 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..743
FT                   /note="tRNA(Met) cytidine acetyltransferase TmcA"
FT                   /id="PRO_0000403133"
FT   DOMAIN          420..604
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01886"
FT   BINDING         216
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01886"
FT   BINDING         241..250
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01886"
FT   BINDING         390
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01886"
FT   BINDING         531..533
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01886"
FT   BINDING         538..544
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01886"
SQ   SEQUENCE   743 AA;  84840 MW;  2A9EA5CA5048D3E5 CRC64;
     MIPGSNPGGR IHNVVKMFQS YFMDAVNGYY RHLAIIESQD YLEKVNSLVE EYLEVNKKPR
     VIYGFHPWLD NSKDRMIEFR KKFENFLDID YSNSEKYLGQ SVDLVILDAI GDFRPNYIAR
     FVDMTKGGGM AIIYSDDILR GKLYKESLTR DGVVKDLFER RFMELAKRYR GIIFLQGDRL
     TFTPYSSNET HKSHKKIPKS PKVPMQLHEL CLSSDQNKVL EESLFITSPG KRVLVVTAAR
     GRGKSASIGL FLSYLMTEEK FGNILVTSPT YYSSQEIFNF VIKGLDALNV KYKLTTSKDG
     KIMKITTGES RVKWVSPDLA RNEEGDLIVV DEAAAIGMEF LDYILQGWDK TILVTTVHGY
     EGSGKAFLKY VNRLKSKVLL KHIKMDYPIR YAKGDPIEKF MFDVFLLDAE PAEVMYNGEL
     KIEDVSQEEL FQDNNLLKSV YGILVTAHYR NSPDDLMLLG DMAFQKIVVG YSSEKPIAVC
     QVVSEGDLTD RQIEDISNGL KNEGHLIPHR LIKYMRAFDF GKLKGWRIMR IAVSPENQGK
     GIGSRIIEEV IKMAKGVDWV GSSFVADYSV LRFWIKNGFT PVYLSSIKNE ELNGYSVIVI
     RALSEKSKGF VVKLSSLLKD KLLRTSHQVY YNLNPQLIAL LMRNTYSERR REGEVPDLYV
     NKIKAYIEGK VPYNVIAETA HFLITKHFLE LKVNLSIEAE ASLVARVLQG KSWYHAGLML
     GLSSREVEER VKQGLEVLLR TYS