(data stored in ACNUC10043 zone)

SWISSPROT: TMCA_AERPE

ID   TMCA_AERPE              Reviewed;         716 AA.
AC   Q9YBQ6;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   11-DEC-2019, entry version 97.
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=APE_1543;
OS   Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 /
OS   K1).
OC   Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Aeropyrum.
OX   NCBI_TaxID=272557;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX   PubMed=10382966; DOI=10.1093/dnares/6.2.83;
RA   Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K.,
RA   Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A.,
RA   Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S.,
RA   Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA   Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.;
RT   "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon,
RT   Aeropyrum pernix K1.";
RL   DNA Res. 6:83-101(1999).
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   -!- 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   -!- SIMILARITY: Belongs to the RNA cytidine acetyltransferase family. TmcA
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01886}.
DR   EMBL; BA000002; BAA80542.1; -; Genomic_DNA.
DR   PIR; H72635; H72635.
DR   STRING; 272557.APE_1543; -.
DR   PRIDE; Q9YBQ6; -.
DR   EnsemblBacteria; BAA80542; BAA80542; APE_1543.
DR   KEGG; ape:APE_1543; -.
DR   eggNOG; arCOG01951; Archaea.
DR   eggNOG; COG1444; LUCA.
DR   HOGENOM; HOG000232267; -.
DR   KO; K06957; -.
DR   OMA; YVSPRYN; -.
DR   Proteomes; UP000002518; 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   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; IPR024914; tRNA_acetyltr_TmcA.
DR   PANTHER; PTHR10925; PTHR10925; 2.
DR   Pfam; PF00583; Acetyltransf_1; 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;
DR   PRODOM; Q9YBQ6.
DR   SWISS-2DPAGE; Q9YBQ6.
KW   Acyltransferase; ATP-binding; Cytoplasm; Nucleotide-binding;
KW   Reference proteome; RNA-binding; Transferase; tRNA processing;
KW   tRNA-binding.
FT   CHAIN           1..716
FT                   /note="tRNA(Met) cytidine acetyltransferase TmcA"
FT                   /id="PRO_0000403129"
FT   DOMAIN          401..567
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01886"
FT   NP_BIND         217..226
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01886"
FT   REGION          493..495
FT                   /note="Acetyl-CoA binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01886"
FT   REGION          500..506
FT                   /note="Acetyl-CoA binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01886"
FT   BINDING         192
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01886"
FT   BINDING         364
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01886"
SQ   SEQUENCE   716 AA;  77792 MW;  77A5F21B652A7503 CRC64;
     MDVELEVSGF IQRLRHSRLR GLLVVGTGDV KAWAEKLAGY AGGDCALVSP SAGRLPGICR
     SWAPPGSIER ILGGEYAAAI IAVPGLLRPS IIAGAGETVR SGGFLAIVAD PPDRWDPGPP
     RGTGLYREYL FSAIRDNPVH LWIDDESGRI VSESFLEYTG VGAQGWSPGR YKPSPGSGVP
     RRLVSACRSE SQARALESLA RFFRGRWRSA LVRGDRGRGK SYVIGLALAY AAWRRLIGRA
     VLVGPTPLSV QSVMAGLLRG LDVLGLKGHR VVRTSGGEVI RVSGPWFRIA YEQPDTAEPS
     PLVVVDEAAA VGVARVRRLS WRSGKSLVAT TIHGYEGSGR AFARLLPNIL PKPFIELELR
     EPIRYLPGDP LEEWLYTVFM LRAEPQEPGD PSAARPVEVS REVLARDREV LRSVYGILVQ
     AHYRNTPDDL LAMLESPHHR IYALEADGTP VAVADVVLEG PDVEEEARIA LERLLYMAGS
     PGSGVVSWRV SRIAVHEDLQ RRGLGSRLLR HVEAQARESG ASLVTTMFSR HDVIPFWLKN
     GFKPFYVSPR YNRVTGEKNV ALAKPLDSAG AEILEKASKT LALKLALAGS SIYRDLAAEK
     LALLLHHTPA TAPPLYLTRI QARHLEGFLK GEVMADQAFD AVYIALLSTL LATRSWNPVE
     PGLVGAVARV VQGKPYSEVA SIIGASTVDE AVGKVEEYIR GILEGARSLW SGRVIP
//

If you have problems or comments...

PBIL Back to PBIL home page