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Y1595_MYCMM
ID   Y1595_MYCMM             Reviewed;         318 AA.
AC   B2HHB4;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=Putative S-adenosyl-L-methionine-dependent methyltransferase MMAR_1595;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=MMAR_1595;
OS   Mycobacterium marinum (strain ATCC BAA-535 / M).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=216594;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-535 / M;
RX   PubMed=18403782; DOI=10.1101/gr.075069.107;
RA   Stinear T.P., Seemann T., Harrison P.F., Jenkin G.A., Davies J.K.,
RA   Johnson P.D., Abdellah Z., Arrowsmith C., Chillingworth T., Churcher C.,
RA   Clarke K., Cronin A., Davis P., Goodhead I., Holroyd N., Jagels K.,
RA   Lord A., Moule S., Mungall K., Norbertczak H., Quail M.A.,
RA   Rabbinowitsch E., Walker D., White B., Whitehead S., Small P.L., Brosch R.,
RA   Ramakrishnan L., Fischbach M.A., Parkhill J., Cole S.T.;
RT   "Insights from the complete genome sequence of Mycobacterium marinum on the
RT   evolution of Mycobacterium tuberculosis.";
RL   Genome Res. 18:729-741(2008).
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; CP000854; ACC40046.1; -; Genomic_DNA.
DR   RefSeq; WP_012393429.1; NC_010612.1.
DR   AlphaFoldDB; B2HHB4; -.
DR   SMR; B2HHB4; -.
DR   STRING; 216594.MMAR_1595; -.
DR   EnsemblBacteria; ACC40046; ACC40046; MMAR_1595.
DR   GeneID; 64260295; -.
DR   KEGG; mmi:MMAR_1595; -.
DR   eggNOG; COG3315; Bacteria.
DR   HOGENOM; CLU_056160_2_1_11; -.
DR   OMA; WDINESV; -.
DR   OrthoDB; 847145at2; -.
DR   Proteomes; UP000001190; 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..318
FT                   /note="Putative S-adenosyl-L-methionine-dependent
FT                   methyltransferase MMAR_1595"
FT                   /id="PRO_0000361165"
FT   BINDING         132
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         161..162
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   318 AA;  34145 MW;  199BB29E59C4B464 CRC64;
     MSITKNAPRE GAEEVAATAL GVAAARAAET RRQRPLIVDP FAQLFVDAAG QDLWSMVASG
     AAHDELASAD PALAAVMQTS LGHIASRTKF FDEFVLAAAD AGIRQVVSLG AGLDTRAWRL
     SWPDAVTVYE LEQPNVLEFK LATLRDNGAT PAANYVDVPV DLHRCWPRSL CLAGFDPAAP
     TAWLVEGLLP FLSVAAQDLL FGDVHKLSVP GSWLAAEALS SEFLKPTTVA RQRARIRRMR
     VTAATLAGLS NVTELWDLAE GRSDVADWLR GRGWHASVLT AERLLARYHR SAPVELGDAT
     PPSLYVTARL SAESSLDA
 
 
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