ID   Y605_RHOJR              Reviewed;         294 AA.
AC   Q0SJ46;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-JAN-2009, sequence version 2.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Putative S-adenosyl-L-methionine-dependent methyltransferase RHA1_ro00605;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=RHA1_ro00605;
OS   Rhodococcus jostii (strain RHA1).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX   NCBI_TaxID=101510;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RHA1;
RX   PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA   McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C.,
RA   Miyazawa D., Wong W., Lillquist A.L., Wang D., Dosanjh M., Hara H.,
RA   Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., Shin H.,
RA   Smailus D., Siddiqui A.S., Marra M.A., Jones S.J.M., Holt R.,
RA   Brinkman F.S.L., Miyauchi K., Fukuda M., Davies J.E., Mohn W.W.,
RA   Eltis L.D.;
RT   "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT   catabolic powerhouse.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006).
CC   -!- FUNCTION: Exhibits S-adenosyl-L-methionine-dependent methyltransferase
CC       activity. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the UPF0677 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABG92440.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000431; ABG92440.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_041810991.1; NC_008268.1.
DR   AlphaFoldDB; Q0SJ46; -.
DR   SMR; Q0SJ46; -.
DR   STRING; 101510.RHA1_ro00605; -.
DR   EnsemblBacteria; ABG92440; ABG92440; RHA1_ro00605.
DR   KEGG; rha:RHA1_ro00605; -.
DR   PATRIC; fig|101510.16.peg.630; -.
DR   eggNOG; COG3315; Bacteria.
DR   HOGENOM; CLU_056160_2_2_11; -.
DR   Proteomes; UP000008710; Chromosome.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR011610; CHP00027_methylltransferase.
DR   InterPro; IPR007213; Ppm1/Ppm2/Tcmp.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF04072; LCM; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   TIGRFAMs; TIGR00027; mthyl_TIGR00027; 1.
PE   3: Inferred from homology;
KW   Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..294
FT                   /note="Putative S-adenosyl-L-methionine-dependent
FT                   methyltransferase RHA1_ro00605"
FT                   /id="PRO_0000361262"
FT   BINDING         120
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         149..150
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   294 AA;  32042 MW;  78736F160A7F3342 CRC64;
     MRTDGDSWDI VSSVGLTALG VATFRALETV RPDALIQDDY ARWFVEAAGE PHFTGLLADP
     SLLGDMRFSG FMGSRTRFFD EFFSSATGAG VSQAVILAAG LDARAYRLDW PTGTTVFEVD
     QPQVLEFKAE VLADHGATAK ADRRPVAVDL RDDWPAALEA AGFDPGKPTA WSVEGLLAYL
     PGAAHDALFE RIDELSSPGS HVAVDNFAEG TDMQRFDAIR AKYFAENPFG DIDIAELFYG
     DERADPVQWL TGHGWSVRRS TSLELAAAYG RPVPDLPEEL VDLSERSTYL TAVK