ID   Y3718_FRAAA             Reviewed;         286 AA.
AC   Q0RJF1;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Putative S-adenosyl-L-methionine-dependent methyltransferase FRAAL3718;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=FRAAL3718;
OS   Frankia alni (strain ACN14a).
OC   Bacteria; Actinobacteria; Frankiales; Frankiaceae; Frankia.
OX   NCBI_TaxID=326424;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACN14a;
RX   PubMed=17151343; DOI=10.1101/gr.5798407;
RA   Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N.,
RA   Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N., Couloux A.,
RA   Cournoyer B., Cruveiller S., Daubin V., Demange N., Francino M.P.,
RA   Goltsman E., Huang Y., Kopp O.R., Labarre L., Lapidus A., Lavire C.,
RA   Marechal J., Martinez M., Mastronunzio J.E., Mullin B.C., Niemann J.,
RA   Pujic P., Rawnsley T., Rouy Z., Schenowitz C., Sellstedt A., Tavares F.,
RA   Tomkins J.P., Vallenet D., Valverde C., Wall L.G., Wang Y., Medigue C.,
RA   Benson D.R.;
RT   "Genome characteristics of facultatively symbiotic Frankia sp. strains
RT   reflect host range and host plant biogeography.";
RL   Genome Res. 17:7-15(2007).
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; CT573213; CAJ62361.1; -; Genomic_DNA.
DR   RefSeq; WP_011604857.1; NC_008278.1.
DR   AlphaFoldDB; Q0RJF1; -.
DR   SMR; Q0RJF1; -.
DR   STRING; 326424.FRAAL3718; -.
DR   KEGG; fal:FRAAL3718; -.
DR   eggNOG; COG3315; Bacteria.
DR   HOGENOM; CLU_056160_2_0_11; -.
DR   OMA; GSAASMW; -.
DR   OrthoDB; 847145at2; -.
DR   Proteomes; UP000000657; 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..286
FT                   /note="Putative S-adenosyl-L-methionine-dependent
FT                   methyltransferase FRAAL3718"
FT                   /id="PRO_0000361096"
FT   BINDING         122
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         151..152
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   286 AA;  30536 MW;  53F0842234575AC1 CRC64;
     MTDAAGRVEP SGVWATAVGV ARVRAMETAR EQPLFRDPLA LAFATAGGRG PGTLSPPRAD
     EAARRRWLEV ALSIVIRTKF LDDLLNRAVA SGVRQVVLLG AGMDSRAFRM DWPTGTRLFE
     VDTAEPLGFK ASVLRQERAV ARCERITVPV DLREDWPGAL AAAGHDPAQP TVWIAEGLLI
     YLPADAVQSL LERVGALSAA GSRMGLTLGT RGVVERFRGD AAAGSAASMW VSEMPEDPVG
     WLDGLGWQAE TFTLRDRAAA YGRPLLTPSQ QDEGTGALVS AVRTAH