(data stored in SCRATCH zone)

SWISSPROT: D1YV05_METPS

ID   D1YV05_METPS            Unreviewed;       289 AA.
AC   D1YV05;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, sequence version 1.
DT   11-DEC-2019, entry version 40.
DE   RecName: Full=tRNA(Phe) (4-demethylwyosine(37)-C(7)) aminocarboxypropyltransferase {ECO:0000256|HAMAP-Rule:MF_01922};
DE            EC=2.5.1.114 {ECO:0000256|HAMAP-Rule:MF_01922};
DE   AltName: Full=tRNA wyosine derivatives biosynthesis protein Taw2 {ECO:0000256|HAMAP-Rule:MF_01922};
GN   Name=taw2 {ECO:0000256|HAMAP-Rule:MF_01922};
GN   OrderedLocusNames=MCP_0205 {ECO:0000313|EMBL:BAI60277.1};
OS   Methanocella paludicola (strain DSM 17711 / JCM 13418 / NBRC 101707 /
OS   SANAE).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanocellales; Methanocellaceae; Methanocella.
OX   NCBI_TaxID=304371 {ECO:0000313|EMBL:BAI60277.1, ECO:0000313|Proteomes:UP000001882};
RN   [1] {ECO:0000313|Proteomes:UP000001882}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17711 / JCM 13418 / NBRC 101707 / SANAE
RC   {ECO:0000313|Proteomes:UP000001882};
RX   PubMed=21829548; DOI=10.1371/journal.pone.0022898;
RA   Sakai S., Takaki Y., Shimamura S., Sekine M., Tajima T., Kosugi H.,
RA   Ichikawa N., Tasumi E., Hiraki A.T., Shimizu A., Kato Y., Nishiko R.,
RA   Mori K., Fujita N., Imachi H., Takai K.;
RT   "Genome sequence of a mesophilic hydrogenotrophic methanogen Methanocella
RT   paludicola, the first cultivated representative of the order
RT   Methanocellales.";
RL   PLoS ONE 6:E22898-E22898(2011).
CC   -!- FUNCTION: S-adenosyl-L-methionine-dependent transferase that acts as a
CC       component of the wyosine derivatives biosynthesis pathway. Catalyzes
CC       the transfer of the alpha-amino-alpha-carboxypropyl (acp) group from S-
CC       adenosyl-L-methionine to 4-demethylwyosine (imG-14), forming 7-
CC       aminocarboxypropyl-demethylwyosine (wybutosine-86) at position 37 of
CC       tRNA(Phe). {ECO:0000256|HAMAP-Rule:MF_01922}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-demethylwyosine(37) in tRNA(Phe) + S-adenosyl-L-methionine =
CC         4-demethyl-7-[(3S)-3-amino-3-carboxypropyl]wyosine(37) in tRNA(Phe) +
CC         H(+) + S-methyl-5'-thioadenosine; Xref=Rhea:RHEA:36355, Rhea:RHEA-
CC         COMP:10164, Rhea:RHEA-COMP:10378, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17509, ChEBI:CHEBI:59789, ChEBI:CHEBI:64315,
CC         ChEBI:CHEBI:73550; EC=2.5.1.114; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01922};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01922}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. TRM5/TYW2 family. {ECO:0000256|HAMAP-Rule:MF_01922}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_01922}.
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DR   EMBL; AP011532; BAI60277.1; -; Genomic_DNA.
DR   STRING; 304371.MCP_0205; -.
DR   EnsemblBacteria; BAI60277; BAI60277; MCP_0205.
DR   KEGG; mpd:MCP_0205; -.
DR   PATRIC; fig|304371.9.peg.212; -.
DR   eggNOG; arCOG10124; Archaea.
DR   eggNOG; COG2520; LUCA.
DR   HOGENOM; HOG000222903; -.
DR   KO; K07055; -.
DR   OMA; IKKYSPG; -.
DR   Proteomes; UP000001882; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0102522; F:tRNA 4-demethylwyosine alpha-amino-alpha-carboxypropyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006400; P:tRNA modification; IEA:InterPro.
DR   HAMAP; MF_01922; TYW2_archaea; 1.
DR   InterPro; IPR030382; MeTrfase_TRM5/TYW2.
DR   InterPro; IPR029063; SAM-dependent_MTases.
DR   InterPro; IPR030867; TYW2_archaea.
DR   Pfam; PF02475; Met_10; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS51684; SAM_MT_TRM5_TYW2; 1.
PE   3: Inferred from homology;
DR   PRODOM; D1YV05.
DR   SWISS-2DPAGE; D1YV05.
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01922};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001882};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_01922};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01922};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_01922}.
FT   DOMAIN          42..289
FT                   /note="SAM_MT_TRM5_TYW2"
FT                   /evidence="ECO:0000259|PROSITE:PS51684"
FT   BINDING         122
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01922"
FT   BINDING         129
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01922"
FT   BINDING         168
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01922"
SQ   SEQUENCE   289 AA;  32728 MW;  7902C0C0668FD3B8 CRC64;
     MGKNNSKMFN KQRGIPVPAD PLATLLKDRL TPEELAVLPR GWQIIGEVLL IHIPPVLQTK
     KALIAEALLT LYPRCRTVME THRIAGEYRQ PVFERISGDG TETLHKENYV VYKLDVAKIM
     FSQGNFYERR RMGTVGKGER VVDMFAGIGY FSLPMAVHAR PGKILAIELN PESYGYLCEN
     VRLNHVEDIV EPVLGDCREK APEGWADRAI MGYVGTTQEY LPWGIRALKR GGILHYHETT
     PDKLVFDRPV QNIKDAAKEQ GRKAEILEKI KVKKYSPGVW HVVVDARIS
//

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