ID H2C5Y3_9CREN Unreviewed; 726 AA.
AC H2C5Y3;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 24-JAN-2024, entry version 44.
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 ORFNames=MetMK1DRAFT_00019560 {ECO:0000313|EMBL:EHP69210.1};
OS Metallosphaera yellowstonensis MK1.
OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Metallosphaera.
OX NCBI_TaxID=671065 {ECO:0000313|EMBL:EHP69210.1, ECO:0000313|Proteomes:UP000003980};
RN [1] {ECO:0000313|EMBL:EHP69210.1, ECO:0000313|Proteomes:UP000003980}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MK1 {ECO:0000313|EMBL:EHP69210.1,
RC ECO:0000313|Proteomes:UP000003980};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Cheng J.-F., Goodwin L., Pitluck S., Peters L.,
RA Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N.,
RA Kozubal M., Macur R.E., Jay Z., Inskeep W., Woyke T.;
RT "Improved High-Quality Draft sequence of Metallosphaera yellowstonensis
RT MK1.";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
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; JH597768; EHP69210.1; -; Genomic_DNA.
DR RefSeq; WP_009073021.1; NZ_JH597768.1.
DR AlphaFoldDB; H2C5Y3; -.
DR STRING; 671065.MetMK1DRAFT_00019560; -.
DR eggNOG; arCOG01951; Archaea.
DR HOGENOM; CLU_004652_1_0_2; -.
DR OrthoDB; 312894at2157; -.
DR Proteomes; UP000003980; Unassembled WGS sequence.
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}; Reference proteome {ECO:0000313|Proteomes:UP000003980};
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 432..586
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
FT BINDING 202
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01886"
FT BINDING 377
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01886"
FT BINDING 513..515
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01886"
SQ SEQUENCE 726 AA; 81783 MW; 341D4124368D32F4 CRC64;
MKSSDEVRSA LEKGLKGFFR NLVFIEGNQF QRAVADVVKL YLDLNPRAEA AYYFHPWAPG
SKGRLRNLTS VMNSVIDIDY SSSERFLGQS FDLVLIDALD DFRPSYIMRA AETARGGGVV
IIFTDNLQTM KLYKSTLVRE GRVGDLFERR FIEKLKVHRG IIIVKDDQVT VRSYSPSETS
RPRRTRMGKH PKISEKCLTD DQVKVVDEAD LVLEEGRKLL AVTASRGRGK SASVGLALSA
LIGETKYPIS VVVTSPSYWS GREVMRFSEV GLRALGRRYK KVESKEGKLM ALEVGESRIR
WLPPDLSRDA DGDFIVVDEA AALGIETLDY LLRKWKKGIL VTTVHGYEGS SKAFLKYLSS
LEERFDVQRI RLDQPVRYSK GDPLESFLYD VMLLDAEPDI NEPPRSYGEV TPNELFEDEK
RLRRIYGILV SAHYRNTPDD LMMLGDASFQ RIFIGQPETA VAQVVEEGGL DETRLEGISE
GGENLGHLIP HRVVKFWRLK DFGKLKGWRV MRIAVAPELQ GKGVGTKLIS YVARRAVEEG
MDWVGSSFLS DIRVLRFWLK NGFIPIHLAT KKNESLGGYS LIVLRPITPE ASKYSFLLSS
YLKDKILRTA HQVYFNVNPE LLAEILYNTP STPTDEIPQV YLDKVRAYLS GNIPYNSAAE
AVHALAERHF REAKFRLEGP EAGAIIARTF QGKSWYHAGL SLGKTSKGVE EALREGMKKI
LSGYIG
//
