ID A0A830FAZ6_9EURY Unreviewed; 745 AA. AC A0A830FAZ6; DT 29-SEP-2021, integrated into UniProtKB/TrEMBL. DT 29-SEP-2021, sequence version 1. DT 24-JAN-2024, entry version 9. 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=GCM10009006_09810 {ECO:0000313|EMBL:GGM30352.1}; OS Haloarcula salaria. OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales; OC Haloarculaceae; Haloarcula. OX NCBI_TaxID=575195 {ECO:0000313|EMBL:GGM30352.1, ECO:0000313|Proteomes:UP000656367}; RN [1] {ECO:0000313|EMBL:GGM30352.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=JCM 15759 {ECO:0000313|EMBL:GGM30352.1}; RX PubMed=30832757; RA Wu L., Ma J.; RT "The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing RT project: providing services to taxonomists for standard genome sequencing RT and annotation."; RL Int. J. Syst. Evol. Microbiol. 69:895-898(2019). RN [2] {ECO:0000313|EMBL:GGM30352.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=JCM 15759 {ECO:0000313|EMBL:GGM30352.1}; RA Sun Q., Ohkuma M.; RL Submitted (SEP-2020) 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}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:GGM30352.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BMON01000001; GGM30352.1; -; Genomic_DNA. DR AlphaFoldDB; A0A830FAZ6; -. DR Proteomes; UP000656367; 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 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 NCBIfam; NF041296; RNAactase_tcmA_Halo; 1. DR PANTHER; PTHR10925; N-ACETYLTRANSFERASE 10; 1. DR PANTHER; PTHR10925:SF5; RNA CYTIDINE ACETYLTRANSFERASE; 1. DR Pfam; PF13718; GNAT_acetyltr_2; 1. 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. 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 4..156 FT /note="tRNA(Met) cytidine acetyltransferase TmcA N- FT terminal" FT /evidence="ECO:0000259|Pfam:PF08351" FT DOMAIN 218..391 FT /note="Helicase" FT /evidence="ECO:0000259|Pfam:PF05127" FT DOMAIN 533..592 FT /note="N-acetyltransferase" FT /evidence="ECO:0000259|Pfam:PF13718" FT REGION 159..183 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 200 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01886" FT BINDING 373 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01886" FT BINDING 519..521 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01886" FT BINDING 558 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01886" SQ SEQUENCE 745 AA; 80825 MW; 1B284FB599B62F8E CRC64; MDIARSLRAE ASRANERRLL VLAGDPDRTR ERAAAALDAA AVPSAETTVV GPKPFLACEH HEQSRAEELL GRTRTAVILD AHEELRPDAV GRTVGAVDGG GLYVLLAPPL ETWPEERDGF DASLAVPPFD VGDVSGHFRR RFVETFRAHR GIAIVDADTG TVEQDGLTDP PPSRPVSSPT APTDAWFRSE TYAQCLTDDQ RDAVQAFESL RDDGAAIVVE ADRGRGKSSA AGLAAGNLAI GGRDVLVTAP QYRSAAEVFA RAGHLLETLG VEFARDRASN PQQLDVAGAG CVRYAPPDEA ASLPDGPDVV IVDEAAALPV RRLEQFLDAP AVAFTTTVHG YEGAGRGFSV RFRDRLAESD HAVADVTMTT PIRYGDADPV EVWAFRALLL DARPPVDQLI TDATPETVEY RRLSAADLLA DEHLLREVFG LLVLAHYRTE PSDLARLLDA PNLAVRALTH EGHVVAVALL AQEGGLSADT RATMYEGRRV RGNMLPDVLS TQLRDEAAGI PVGQRVLRIA THAAVRSRGL GSELLSEIRT EFAEQVDWLG VSYGATPELV RFWADNGYNT VHLATSRNAT SGEYSVVMLN PCSDDGVALA ARHGEWFQDR IAAVLSDPLD DCDPDVVRAV LRATDGERPV SLSEWEWRLV AGVPGGASVL DTNPKPFRQL TRQHLSDPAD ATALSPREER LLVRKVLQAH PWSAVAEELA FVSKRECMRT LGGIVERLTR LYGDPWVQEE LDRHQ //