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Y1770_MYCTO
ID   Y1770_MYCTO             Reviewed;         312 AA.
AC   P9WFH8; L0T938; P71987; Q7D825;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 33.
DE   RecName: Full=Putative S-adenosyl-L-methionine-dependent methyltransferase MT1770;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=MT1770;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(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; AE000516; AAK46042.1; -; Genomic_DNA.
DR   PIR; D70687; D70687.
DR   RefSeq; WP_003408497.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WFH8; -.
DR   SMR; P9WFH8; -.
DR   EnsemblBacteria; AAK46042; AAK46042; MT1770.
DR   KEGG; mtc:MT1770; -.
DR   PATRIC; fig|83331.31.peg.1899; -.
DR   HOGENOM; CLU_056160_2_1_11; -.
DR   Proteomes; UP000001020; 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..312
FT                   /note="Putative S-adenosyl-L-methionine-dependent
FT                   methyltransferase MT1770"
FT                   /id="PRO_0000428536"
FT   BINDING         130
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         159..160
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   312 AA;  33654 MW;  D0FA7184385E7FDE CRC64;
     MARTDDDNWD LTSSVGVTAT IVAVGRALAT KDPRGLINDP FAEPLVRAVG LDLFTKMMDG
     ELDMSTIADV SPAVAQAMVY GNAVRTKYFD DYLLNATAGG IRQVAILASG LDSRAYRLPW
     PTRTVVYEID QPKVMEFKTT TLADLGAEPS AIRRAVPIDL RADWPTALQA AGFDSAAPTA
     WLAEGLLIYL KPQTQDRLFD NITALSAPGS MVATEFVTGI ADFSAERART ISNPFRCHGV
     DVDLASLVYT GPRNHVLDYL AAKGWQPEGV SLAELFRRSG LDVRAADDDT IFISGCLTDH
     SSISPPTAAG WR
 
 
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