(data stored in SCRATCH zone)

SWISSPROT: Q3IDD4_PSEHT

ID   Q3IDD4_PSEHT            Unreviewed;       689 AA.
AC   Q3IDD4;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   07-JUN-2017, entry version 77.
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=PSHAa0121 {ECO:0000313|EMBL:CAI85225.1};
OS   Pseudoalteromonas haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442 {ECO:0000313|EMBL:CAI85225.1, ECO:0000313|Proteomes:UP000006843};
RN   [1] {ECO:0000313|EMBL:CAI85225.1, ECO:0000313|Proteomes:UP000006843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125 {ECO:0000313|Proteomes:UP000006843};
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.,
RA   Cheung F., Cruveiller S., Damico S., Duilio A., Fang G., Feller G.,
RA   Mangenot S., Marino G., Nilsson J., Parilli E., Rocha E., Rouy Z.,
RA   Sekowska A., Tutino M.L., Vallenet D., von Heijne G., Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica
RT   bacterium Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
CC   -!- FUNCTION: Catalyzes the formation of N(4)-acetylcytidine (ac(4)C)
CC       at the wobble position of tRNA(Met), by using acetyl-CoA as an
CC       acetyl donor and ATP (or GTP). {ECO:0000256|HAMAP-Rule:MF_01886}.
CC   -!- CATALYTIC ACTIVITY: (Elongator tRNA(Met))-cytidine(34) + ATP +
CC       acetyl-CoA + H(2)O = (elongator tRNA(Met))-N(4)-acetylcytidine(34)
CC       + ADP + phosphate + CoA. {ECO:0000256|HAMAP-Rule:MF_01886}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01886}.
CC   -!- SIMILARITY: Belongs to the TmcA family. {ECO:0000256|HAMAP-
CC       Rule:MF_01886}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01886}.
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DR   EMBL; CR954246; CAI85225.1; -; Genomic_DNA.
DR   RefSeq; WP_011326843.1; NC_007481.1.
DR   STRING; 326442.PSHAa0121; -.
DR   EnsemblBacteria; CAI85225; CAI85225; PSHAa0121.
DR   KEGG; pha:PSHAa0121; -.
DR   PATRIC; fig|326442.8.peg.115; -.
DR   eggNOG; ENOG4105E0I; Bacteria.
DR   eggNOG; COG1444; LUCA.
DR   HOGENOM; HOG000131853; -.
DR   KO; K06957; -.
DR   OMA; MRIAVHP; -.
DR   OrthoDB; POG091H03ZB; -.
DR   Proteomes; UP000006843; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0051392; F:tRNA N-acetyltransferase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0051391; P:tRNA acetylation; IEA:UniProtKB-HAMAP.
DR   GO; GO:0002101; P:tRNA wobble cytosine modification; IEA:UniProtKB-HAMAP.
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; 1.
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; 2.
DR   PROSITE; PS51186; GNAT; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q3IDD4.
DR   SWISS-2DPAGE; Q3IDD4.
KW   Acyltransferase {ECO:0000256|HAMAP-Rule:MF_01886};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01886};
KW   Complete proteome {ECO:0000313|Proteomes:UP000006843};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01886};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01886};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006843};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_01886};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01886};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_01886};
KW   tRNA-binding {ECO:0000256|HAMAP-Rule:MF_01886}.
FT   DOMAIN      371    557       N-acetyltransferase.
FT                                {ECO:0000259|PROSITE:PS51186}.
FT   BINDING     177    177       ATP. {ECO:0000256|HAMAP-Rule:MF_01886}.
FT   BINDING     339    339       ATP. {ECO:0000256|HAMAP-Rule:MF_01886}.
SQ   SEQUENCE   689 AA;  77140 MW;  72E0A5CCF60886C3 CRC64;
     MQDYKLYKKQ LIQLEQQLAG AHHRQLVLVT GNDNWCYELT NSLVQNTNTL TLSKHCALKN
     AQWPAHIHQI LGQEFTHAIY DGFSGLYPDK LAAIAGTVRA GGVLFVLLPE LGNLNNWQDP
     ALKSVQSHGH SNQYSLFNQR FSSIIKSLPA LHYSEEFGCI NNNYNYVLHS NIDFEPQKNC
     VAQIVKVAHG RANRPLLINA DRGRGKSAAL GLAAAKLADK NVIICATQFR ATHSSFKHLA
     AQLNVNYDPL QKQLANMQYI APDALLNELP ECDVLLVDEA AAIPVPMLLS MLAHYPRIVF
     ASTLVGYEGN GRGYTIRFSQ YIKNHYKASK VITLDEPLRF AKHDPLEQHI RSLLALDAQY
     QETNSNKSQI PKHSEVTQQQ LVTDEALLCQ VVALLALAHY QSSVNDLRQL LDAPSQRIFI
     SKIDKQLVGV CLIAIEGGLS EELTEQVISG ERRPQGHLMA QTLAQLSFNS DFLTHLSARV
     VRIAIDPSSH NCGLGKALLS YSESQVKEQC TWFGASFGAT AQLLKFWQSL GFNAVKLGYQ
     RDKSTAEHAT LVVKSLNAPQ QSLQSLIKQF QYELFYGLLS HFKSLEWQLV STLLRSFNDE
     VIASDTLRLF TQQLSSNRFT ISPTLWRLIS QSPAAMTKLA SNQQQLLIQT VLQHHTDEQL
     IKNLNLNGKK QLEQQFRNTT NILAKQLSS
//

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