ID   Y5401_FRAAA             Reviewed;         306 AA.
AC   Q0RES2;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Putative S-adenosyl-L-methionine-dependent methyltransferase FRAAL5401;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=FRAAL5401;
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; CAJ64034.1; -; Genomic_DNA.
DR   RefSeq; WP_011606484.1; NC_008278.1.
DR   AlphaFoldDB; Q0RES2; -.
DR   SMR; Q0RES2; -.
DR   STRING; 326424.FRAAL5401; -.
DR   KEGG; fal:FRAAL5401; -.
DR   eggNOG; COG3315; Bacteria.
DR   HOGENOM; CLU_056160_2_1_11; -.
DR   OMA; RMADNMA; -.
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..306
FT                   /note="Putative S-adenosyl-L-methionine-dependent
FT                   methyltransferase FRAAL5401"
FT                   /id="PRO_0000361098"
FT   REGION          201..225
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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   306 AA;  33630 MW;  AC2A707107004D44 CRC64;
     MTSTRHDGDT WDLASSVGAT ATMAAVARAI ATRADRRLID DPFAAPLVRA VGIDLLTRLA
     TGDVPPDGLV EQVAIDVAKV RARFYDEFFL EATNTGITQV VILASGLDSR AYRLPWPIGT
     VVYELDQPRV VEFKTRTLAA LGAVPTADRR VAAVDLRDDW PAALRAAGFD PARPTAWSAE
     GLLGYLPPEA QDRLLDTVTE LSAPESRVAT ENRPNPKPGD EDRTKEALNR ISERWRAHSF
     DPDMARLRYY GERNETAPYL ADRGWALTGI SVRDLLAAHG LPPLRDDDLR MGDVRYVSGV
     RNKTTK