ID   Y5023_MYCGI             Reviewed;         307 AA.
AC   A4TED9;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Putative S-adenosyl-L-methionine-dependent methyltransferase Mflv_5023;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=Mflv_5023;
OS   Mycolicibacterium gilvum (strain PYR-GCK) (Mycobacterium gilvum (strain
OS   PYR-GCK)).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=350054;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PYR-GCK;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Miller C., Richardson P.;
RT   "Complete sequence of chromosome of Mycobacterium gilvum PYR-GCK.";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000656; ABP47489.1; -; Genomic_DNA.
DR   RefSeq; WP_011895851.1; NC_009338.1.
DR   AlphaFoldDB; A4TED9; -.
DR   SMR; A4TED9; -.
DR   STRING; 350054.Mflv_5023; -.
DR   EnsemblBacteria; ABP47489; ABP47489; Mflv_5023.
DR   KEGG; mgi:Mflv_5023; -.
DR   eggNOG; COG3315; Bacteria.
DR   HOGENOM; CLU_056160_2_1_11; -.
DR   OMA; DFFTRWV; -.
DR   OrthoDB; 847145at2; -.
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..307
FT                   /note="Putative S-adenosyl-L-methionine-dependent
FT                   methyltransferase Mflv_5023"
FT                   /id="PRO_0000361155"
FT   REGION          213..234
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         133
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         162..163
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   307 AA;  33375 MW;  1CCB2E3F70D9B17B CRC64;
     MPRTENDTWD LASSVGATAT MVAAARAVAT RAEDPVIDDP YAEPLVRAVG IDFFAKLASG
     ELTPEDLDVS GDESPVGMSR FADGMAARTR FFDDFFTDAC AAGVRQAVIL ASGLDARGYR
     LTWPEGMTLF EIDQPEVIEF KRTTLAGLGA TPSTHLATVA IDLREDWPTA LRDAGFDPSV
     PTAWIAEGLL GYLPPDAQDR LLDTIGELSA SGSRLAVESV PSQQSADQDE MREKMKDSTD
     RWRSHGFDLD FSELVFLGER ANVPDYLRER GWAVTATPTN DLLTRYGLAP LDTDEGFAEV
     VYVNAAR