ID   Y5024_MYCGI             Reviewed;         301 AA.
AC   A4TEE0;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Putative S-adenosyl-L-methionine-dependent methyltransferase Mflv_5024;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=Mflv_5024;
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000656; ABP47490.1; -; Genomic_DNA.
DR   RefSeq; WP_011895852.1; NC_009338.1.
DR   AlphaFoldDB; A4TEE0; -.
DR   SMR; A4TEE0; -.
DR   STRING; 350054.Mflv_5024; -.
DR   EnsemblBacteria; ABP47490; ABP47490; Mflv_5024.
DR   KEGG; mgi:Mflv_5024; -.
DR   eggNOG; COG3315; Bacteria.
DR   HOGENOM; CLU_056160_2_1_11; -.
DR   OMA; GSAASMW; -.
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..301
FT                   /note="Putative S-adenosyl-L-methionine-dependent
FT                   methyltransferase Mflv_5024"
FT                   /id="PRO_0000361156"
FT   BINDING         129
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         158..159
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   301 AA;  32697 MW;  CCB7341DD0306942 CRC64;
     MARTDGDTWD LASSVGATAT SVAASRAFAS RGPDALIDDP YARLLVEAVG LPHFVKVARG
     EIDFDGDPLF GAQQAINQIV VRTRIFDDFL TDAGQREPQI RQAVILASGL DTRAYRLDWP
     AGTVVYEIDQ PEVIDFKTAV LTDAGVAPAA DRRTVGIDLR EDWPTALRDA GFDPDRPTAW
     IAEGLLPYLP PDAQDRLLDS ITALSAPGSR LATEHMDAKA LTGDWAKAMT ERARRHGSDI
     DLTKLFYNGE RRSATEHLGA VGWQTSVQTS NDAYIANGFG PIRDDLLAMI GDSGYLTAWR
     P