Y917_MYCBO
ID Y917_MYCBO Reviewed; 325 AA.
AC P64748; A0A1R3XX40; Q10552; X2BGF9;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Putative S-adenosyl-L-methionine-dependent methyltransferase Mb0917c;
DE EC=2.1.1.-;
GN OrderedLocusNames=BQ2027_MB0917C;
OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=233413;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT "The complete genome sequence of Mycobacterium bovis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA Robbe-Austerman S., Gordon S.V.;
RT "Updated reference genome sequence and annotation of Mycobacterium bovis
RT AF2122/97.";
RL Genome Announc. 5:E00157-E00157(2017).
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; LT708304; SIT99515.1; -; Genomic_DNA.
DR RefSeq; NP_854574.1; NC_002945.3.
DR RefSeq; WP_003404654.1; NC_002945.4.
DR AlphaFoldDB; P64748; -.
DR SMR; P64748; -.
DR EnsemblBacteria; SIT99515; SIT99515; BQ2027_MB0917C.
DR PATRIC; fig|233413.5.peg.998; -.
DR OMA; NWDINTS; -.
DR Proteomes; UP000001419; 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; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..325
FT /note="Putative S-adenosyl-L-methionine-dependent
FT methyltransferase Mb0917c"
FT /id="PRO_0000103734"
FT BINDING 126
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 155..156
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
SQ SEQUENCE 325 AA; 36073 MW; 6280F61020906EDE CRC64;
MRTEDDSWDV TTSVGSTGLL VAAARALETQ KADPLAIDPY AEVFCRAAGG EWADVLDGKL
PDHYLTTGDF GEHFVNFQGA RTRYFDEYFS RATAAGMKQV VILAAGLDSR AFRLQWPIGT
TIFELDRPQV LDFKNAVLAD YHIRPRAQRR SVAVDLRDEW QIALCNNGFD ANRPSAWIAE
GLLVYLSAEA QQRLFIGIDT LASPGSHVAV EEATPLDPCE FAAKLERERA ANAQGDPRRF
FQMVYNERWA RATEWFDERG WRATATPLAE YLRRVGRAVP EADTEAAPMV TAITFVSAVR
TGLVADPART SPSSTSIGFK RFEAD