TMCA_HALVD
ID TMCA_HALVD Reviewed; 754 AA.
AC D4GW73;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 72.
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=HVO_2736;
GN ORFNames=C498_08969;
OS Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=309800;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R.,
RA Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.;
RT "The complete genome sequence of Haloferax volcanii DS2, a model
RT archaeon.";
RL PLoS ONE 5:E9605-E9605(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=DS2 / DS70;
RX PubMed=19478918; DOI=10.1155/2009/428489;
RA El Yacoubi B., Phillips G., Blaby I.K., Haas C.E., Cruz Y., Greenberg J.,
RA de Crecy-Lagard V.;
RT "A Gateway platform for functional genomics in Haloferax volcanii: deletion
RT of three tRNA modification genes.";
RL Archaea 2:211-219(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 ECO:0000269|PubMed:19478918}.
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 -!- DISRUPTION PHENOTYPE: Mutants lack the ac(4)C modification, but do not
CC show any growth defects. {ECO:0000269|PubMed:19478918}.
CC -!- SIMILARITY: Belongs to the RNA cytidine acetyltransferase family. TmcA
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01886}.
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DR EMBL; CP001956; ADE03866.1; -; Genomic_DNA.
DR EMBL; AOHU01000047; ELY32328.1; -; Genomic_DNA.
DR RefSeq; WP_004042960.1; NZ_AOHU01000047.1.
DR AlphaFoldDB; D4GW73; -.
DR SMR; D4GW73; -.
DR IntAct; D4GW73; 3.
DR STRING; 309800.C498_08969; -.
DR EnsemblBacteria; ADE03866; ADE03866; HVO_2736.
DR EnsemblBacteria; ELY32328; ELY32328; C498_08969.
DR GeneID; 8926494; -.
DR KEGG; hvo:HVO_2736; -.
DR PATRIC; fig|309800.29.peg.1757; -.
DR eggNOG; arCOG01951; Archaea.
DR HOGENOM; CLU_004652_1_0_2; -.
DR OMA; NEPDDLG; -.
DR OrthoDB; 2707at2157; -.
DR Proteomes; UP000008243; Chromosome.
DR Proteomes; UP000011532; 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; 3.40.50.300; -; 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;
KW Reference proteome; RNA-binding; Transferase; tRNA processing;
KW tRNA-binding.
FT CHAIN 1..754
FT /note="tRNA(Met) cytidine acetyltransferase TmcA"
FT /id="PRO_0000428825"
FT DOMAIN 418..603
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01886"
FT REGION 181..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 212
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01886"
FT BINDING 236..245
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01886"
FT BINDING 383
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01886"
FT BINDING 529..531
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01886"
FT BINDING 536..542
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01886"
FT BINDING 568
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01886"
SQ SEQUENCE 754 AA; 81215 MW; 3CB2828ECF3412F9 CRC64;
MTELGDDPDV EALAAARREE ALATNQRRLL VLAGDRDAGI DAAFDAVRGA DVPDDEVTFV
TAREGFRFHR VEPKRASSLL GTTRTLVVLD AHEEFSANAL GRVAGAVDGG GLLVLLTPSL
DDWPTRRDSF DERLAVPPFS VADVTGRFRG RLVSTLRDHP GVALVDLDSG TVERDGAYRQ
GISFDAAPPR VPTEKDRRSP RRAYEDCLTA DQSEALAALE ALTEPGTAVV VEADRGRGKS
SAAGLAAGSL AAEGKDVVVT APGERNAAEV FARAERLLSE LGALRGGGAG DFDIAADRGG
RVRYVPPTEA GDAAADADAL VVDEAAALPV GLLESFLAAP AVAFCTTVRG YEGAGRGFTV
RFRDRLDDAD REVTDARLDD PIRYAAGDPV ESWTFRALLL DARPPVDQLV ADATPETVSY
RALSPDDLLA DEHLLREAFG LLVLAHYRTE PDDLARLLDA PNLTLRALTH EGRVVSVALL
AREGGLDPDT RRQMYDGGRI RGNMLPDVFT SQLRDEGAGV PVGYRVMRIA THHAVRSSGL
GSRLLTELRD EFADDADYLG VGFGATPELL SFWRDNGYGT VHLSTTRNDT SGEYSALMTR
PLSSAGRDLR DRHANWFLGR VGDVLGDALS DLDADVARAA LAAVDSFLSP DLSEYEWRVV
VGASYGPGLY TTAPGAFRRL GLAHLTNPER ASLTPREERL VVRKVLQTHP WDAVADELDF
HSTAGAMRAL GDAYEPLVDE YGTDAAREER ERFR
