ID   Y4929_FRASN             Reviewed;         310 AA.
AC   A8LHA4;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-JAN-2009, sequence version 2.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=Putative S-adenosyl-L-methionine-dependent methyltransferase Franean1_4929;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=Franean1_4929;
OS   Frankia sp. (strain EAN1pec).
OC   Bacteria; Actinobacteria; Frankiales; Frankiaceae; Frankia;
OC   unclassified Frankia.
OX   NCBI_TaxID=298653;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EAN1pec;
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABW14294.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; CP000820; ABW14294.1; ALT_FRAME; Genomic_DNA.
DR   AlphaFoldDB; A8LHA4; -.
DR   SMR; A8LHA4; -.
DR   PRIDE; A8LHA4; -.
DR   EnsemblBacteria; ABW14294; ABW14294; Franean1_4929.
DR   KEGG; fre:Franean1_4929; -.
DR   eggNOG; COG3315; Bacteria.
DR   HOGENOM; CLU_056160_2_0_11; -.
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..310
FT                   /note="Putative S-adenosyl-L-methionine-dependent
FT                   methyltransferase Franean1_4929"
FT                   /id="PRO_0000361099"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..25
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         136
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         165..166
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   310 AA;  33482 MW;  D0B51B09CBDED052 CRC64;
     MSRPSAPRGR TELRSIHERG HERGSAGVGR TALATAWIRA GESERPDRLF DDWLAPAFVA
     AAGDALPLIP PDAGGRLGAL AEMMNAYLAV RTRFFDDELL AAAEAGVRQV VLLAAGLDSR
     AFRLPWPAGT RLFEVDRPDI LAFKEQVLAA GETGPRCERH AVSADLTEDW ADEILDAGFR
     PAEPTAWLAE GIIVYLSAEE AERLLTDVTR LSAPGSRLAL EDAKGLAEEM VEEARNIPPL
     GEFADLWKGG LEGASPAWLG DHGWRGREID STTVATELRR PIPAEMPVAG YFVTAQRAVG
     ERAEGERAEG