ID   Y7813_STRCO             Reviewed;         283 AA.
AC   Q9FBX1;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Putative S-adenosyl-L-methionine-dependent methyltransferase SCO7813;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=SCO7813; ORFNames=SC8E7.10;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(2002).
CC   -!- FUNCTION: Exhibits S-adenosyl-L-methionine-dependent methyltransferase
CC       activity. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the UPF0677 family. {ECO:0000305}.
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DR   EMBL; AL939132; CAC03631.1; -; Genomic_DNA.
DR   RefSeq; NP_631842.1; NC_003888.3.
DR   RefSeq; WP_011031934.1; NC_003888.3.
DR   AlphaFoldDB; Q9FBX1; -.
DR   SMR; Q9FBX1; -.
DR   STRING; 100226.SCO7813; -.
DR   PRIDE; Q9FBX1; -.
DR   GeneID; 1103251; -.
DR   KEGG; sco:SCO7813; -.
DR   PATRIC; fig|100226.15.peg.7923; -.
DR   eggNOG; COG3315; Bacteria.
DR   HOGENOM; CLU_056160_2_0_11; -.
DR   InParanoid; Q9FBX1; -.
DR   OMA; GSAASMW; -.
DR   PhylomeDB; Q9FBX1; -.
DR   Proteomes; UP000001973; 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..283
FT                   /note="Putative S-adenosyl-L-methionine-dependent
FT                   methyltransferase SCO7813"
FT                   /id="PRO_0000361266"
FT   REGION          264..283
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         121
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         150..151
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   283 AA;  30406 MW;  2FE602E7190BB46C CRC64;
     MTGEQEWVQP SGVWATAVGV ARVRALESER EDALFRDPLA QAFAAAGGLW PSSPPLPDDE
     AARRRRLAVA FSIVVRTKFL DDLLEHATAS GVRQVVLLGA GMDSRAFRMA WPEGTRLFEV
     DTPAPLEFKA SVLRQERAVA HCERITVAVD LREDWPSALA AAGHDAAIPT AWIGEGLLIY
     LPEDAVELLL ARIGEQSASG SRMGLTLGSR GVIERFAAGA VPGSAASMWV SEMPDDPVGW
     LAGHGWEASC HTLRERAVAY GRPMSTLPQH EDGPGGLISA VRR