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