ID C3N0T1_SULIA Unreviewed; 770 AA.
AC C3N0T1;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=tRNA(Met) cytidine acetyltransferase TmcA {ECO:0000256|HAMAP-Rule:MF_01886};
DE EC=2.3.1.193 {ECO:0000256|HAMAP-Rule:MF_01886};
GN Name=tmcA {ECO:0000256|HAMAP-Rule:MF_01886};
GN OrderedLocusNames=M1627_2226 {ECO:0000313|EMBL:ACP56089.1};
OS Sulfolobus islandicus (strain M.16.27).
OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=427318 {ECO:0000313|EMBL:ACP56089.1, ECO:0000313|Proteomes:UP000002307};
RN [1] {ECO:0000313|EMBL:ACP56089.1, ECO:0000313|Proteomes:UP000002307}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M.16.27 {ECO:0000313|EMBL:ACP56089.1,
RC ECO:0000313|Proteomes:UP000002307};
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:0000256|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:0000256|HAMAP-Rule:MF_01886};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01886}.
CC Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604}.
CC -!- SIMILARITY: Belongs to the TmcA family. {ECO:0000256|HAMAP-
CC Rule:MF_01886}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01886}.
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DR EMBL; CP001401; ACP56089.1; -; Genomic_DNA.
DR RefSeq; WP_012719047.1; NC_012632.1.
DR AlphaFoldDB; C3N0T1; -.
DR GeneID; 84059488; -.
DR KEGG; sim:M1627_2226; -.
DR HOGENOM; CLU_004652_1_0_2; -.
DR Proteomes; UP000002307; 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 CDD; cd04301; NAT_SF; 1.
DR Gene3D; 3.40.50.11040; -; 1.
DR Gene3D; 3.40.630.30; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; N-ACETYLTRANSFERASE 10; 1.
DR PANTHER; PTHR10925:SF5; RNA CYTIDINE ACETYLTRANSFERASE; 1.
DR Pfam; PF13718; GNAT_acetyltr_2; 2.
DR Pfam; PF05127; Helicase_RecD; 1.
DR Pfam; PF08351; TmcA_N; 1.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315, ECO:0000256|HAMAP-
KW Rule:MF_01886};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01886};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01886};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01886};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_01886};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01886};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_01886};
KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555, ECO:0000256|HAMAP-
KW Rule:MF_01886}.
FT DOMAIN 458..608
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
FT BINDING 209
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01886"
FT BINDING 390
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01886"
FT BINDING 533..535
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01886"
SQ SEQUENCE 770 AA; 87750 MW; 37FF0E96871C8FCA CRC64;
MVNKEQFYDQ IRKALEDGNI RYYRNLVYIE REDYLDYVKE IINLFLKFKP DPSVAYGFVP
WASGSKERMK TIKEYFLKFD DIDYANAEYY LGNTYDLVIL DTVDNFQPIN IGRLVDLARG
GGLIIIYTNN LTKDKAFRTS ILRNGLVLDE YEKRFKRKLY EHEGIFIVDA NGYVSKPFSG
NIMLKSEKKV PRNPVMPREI HELSLSEDQN RVIENFTYLL SGGQRALVLT AARGRGKSAA
TGLSIAGLIE KLRERKGKSV RVIVTAPSIA NASQVMSFAK LGLEVLGEEL SVKVSDTGHI
KTLRGDYFKV EYVPPDAAVE DDGELLIVDE AAALGINYID LALRAWKKVA LVTTVHGYEG
SNKAFLRYLR RLIESKRIRV KWINIEQPLR YANGDPIEKW LYDALLLDAE PSEPQYLNHT
MIYEDVDKSE LANDDIKLRA IYGIMVTAHY KNNPDDLMIM LDGVHHKIKA IRIGENSYVA
ACQIAEEGEL SDNMVDIALK GGTFEGDLIP DRIIKHVRIK DFARLRGWRI VRIAVASELQ
DKGFGSELLK MIYEEAKDKG MDWVGSSFMS DQKVLNFWIK NGFAPVHISP KKNEKLGDYP
VVVIRPISDI ATKIVKISVY MLKEKLLNTL HDVYFNMNPE VVRLILKGSS IAHKTVDVNP
ILLDKTISFL QGVSPYESSA DGIHMLTLKY FWDGERDWGL TQDEELVLIA KVIQGKPWSY
VSTILNSNRT HIYELIYSAI SKIMQKYYNL TADSKVGLTL KDVMSSQQYE
//
