ID I0A2E9_FERFK Unreviewed; 826 AA.
AC I0A2E9;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 64.
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=FFONT_1168 {ECO:0000313|EMBL:AFH43156.1};
OS Fervidicoccus fontis (strain DSM 19380 / JCM 18336 / VKM B-2539 / Kam940).
OC Archaea; Thermoproteota; Thermoprotei; Fervidicoccales; Fervidicoccaceae;
OC Fervidicoccus.
OX NCBI_TaxID=1163730 {ECO:0000313|EMBL:AFH43156.1, ECO:0000313|Proteomes:UP000007391};
RN [1] {ECO:0000313|Proteomes:UP000007391}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19380 / VKM B-2539 / Kam940
RC {ECO:0000313|Proteomes:UP000007391};
RA Lebedinsky A.V., Mardanov A.V., Gumerov V.M., Beletsky A.V., Kublanov I.V.,
RA Perevalova A.A., Bonch-Osmolovskaya E.A., Ravin N.V., Skryabin K.G.;
RT "Fervidicoccus fontis complete genome analysis confirms its distinct
RT phylogenetic position and predicts its environmental function.";
RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AFH43156.1, ECO:0000313|Proteomes:UP000007391}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19380 / VKM B-2539 / Kam940
RC {ECO:0000313|Proteomes:UP000007391};
RX PubMed=24366681; DOI=10.1007/s00792-013-0616-7;
RA Lebedinsky A.V., Mardanov A.V., Kublanov I.V., Gumerov V.M., Beletsky A.V.,
RA Perevalova A.A., Bidzhieva S.Kh., Bonch-Osmolovskaya E.A., Skryabin K.G.,
RA Ravin N.V.;
RT "Analysis of the complete genome of Fervidococcus fontis confirms the
RT distinct phylogenetic position of the order Fervidicoccales and suggests
RT its environmental function.";
RL Extremophiles 18:295-309(2014).
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; CP003423; AFH43156.1; -; Genomic_DNA.
DR AlphaFoldDB; I0A2E9; -.
DR STRING; 1163730.FFONT_1168; -.
DR KEGG; ffo:FFONT_1168; -.
DR eggNOG; arCOG01951; Archaea.
DR HOGENOM; CLU_004652_1_0_2; -.
DR InParanoid; I0A2E9; -.
DR OrthoDB; 312894at2157; -.
DR Proteomes; UP000007391; 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:0006364; P:rRNA processing; IEA:UniProtKB-KW.
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 InterPro; IPR027992; tRNA_bind_dom.
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 Pfam; PF13725; tRNA_bind_2; 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}; Reference proteome {ECO:0000313|Proteomes:UP000007391};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_01886}; rRNA processing {ECO:0000256|ARBA:ARBA00022552};
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 31..214
FT /note="tRNA(Met) cytidine acetyltransferase TmcA N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08351"
FT DOMAIN 284..463
FT /note="Helicase"
FT /evidence="ECO:0000259|Pfam:PF05127"
FT DOMAIN 503..618
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|Pfam:PF13718"
FT DOMAIN 619..671
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|Pfam:PF13718"
FT DOMAIN 722..811
FT /note="Possible tRNA binding"
FT /evidence="ECO:0000259|Pfam:PF13725"
FT BINDING 263
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01886"
FT BINDING 445
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01886"
FT BINDING 597..599
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01886"
SQ SEQUENCE 826 AA; 95893 MW; A120F691B4F591CC CRC64;
MKREEIEAIA SDYIKTIGKE PPHEIKKFAR RLRDNTEKYV KLKYRRLVVV SGGDEKKQGF
ISGYITYHYL LELSRLRGGK KLKLLYMYHD EYEEARIRKE TFRQFMKMAR KKLQNIERNI
DVYEKSDRYL GTSYDVLILD LTNDLRPNDI GKLVEIVNGG GLIIFLTPDL EKWDRWMTAF
KQKLVVPGFN EPRHIFIRWF KETILDSDST YVYDAEKDQL VKKFYVQRVK GEEKKSEVVR
EKGLKEKHIF DERLYSLALT EDQQKVLEVM EELLGKTKKK KVLVITSNRG RGKSSVLGIG
VIALANHMSQ FKHKVRILVT APEITNVQSL FDLAYLSAKS IGLNVKLLKK GGMIIEIQGQ
NFSIEYWEPI NIPKIKGDVV VVDEASGISV PLLLKILKTH KRLIFSATIH GYEGAGRGFS
VRFLGSLRKD PNVELSTCEM KTPIRYGEGD PIEKWLYRAL LLDAEPTDLS DDDLTKIKNQ
ELEYVYLDPA ELFKKENEEL LRQLFGIFVL AHYRNQPDDL AMMADAPHHM IRAVMIKGTN
KIVCSLQIAV EGGLDSQTVD TLLRGNKIQG NIIPDRIIKH LRIWEMGWLR GYRIVRIATH
PEVQNLGIGS FALERLYEEA RQKSFDWIGS GFGANYSLLN FWIKNKFIPV HISPDKNPIS
GEYTVIVIRP INHIAEKITR EGQIYLRKKI VKGMRDVYKE MEQDLALLIL NSIEKMEIEI
PKLHPIDVDR LWIYVYGPMT YEAISDVFLD LAIYYFLGDM EKLVELNNEE KIILLAKVLQ
GKDWSEMSKM LRRRRIDLML ILKDIAKRML NSYYNKNLES SVGYHI
//
