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Database: UniProt
Entry: M7TAW6_BOTF1
LinkDB: M7TAW6_BOTF1
Original site: M7TAW6_BOTF1 
ID   M7TAW6_BOTF1            Unreviewed;       280 AA.
AC   M7TAW6;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Putative methyltransferase domain-containing protein {ECO:0000313|EMBL:EMR80536.1};
GN   ORFNames=BcDW1_10917 {ECO:0000313|EMBL:EMR80536.1};
OS   Botryotinia fuckeliana (strain BcDW1) (Noble rot fungus) (Botrytis
OS   cinerea).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Botrytis.
OX   NCBI_TaxID=1290391 {ECO:0000313|EMBL:EMR80536.1, ECO:0000313|Proteomes:UP000012045};
RN   [1] {ECO:0000313|Proteomes:UP000012045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BcDW1 {ECO:0000313|Proteomes:UP000012045};
RX   PubMed=23704180; DOI=10.1128/genomea.00252-13;
RA   Blanco-Ulate B., Allen G., Powell A.L., Cantu D.;
RT   "Draft genome sequence of Botrytis cinerea BcDW1, inoculum for noble rot of
RT   grape berries.";
RL   Genome Announc. 1:E0025213-E0025213(2013).
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00005179}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. {ECO:0000256|ARBA:ARBA00038314}.
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DR   EMBL; KB708120; EMR80536.1; -; Genomic_DNA.
DR   AlphaFoldDB; M7TAW6; -.
DR   STRING; 1290391.M7TAW6; -.
DR   HOGENOM; CLU_051542_0_1_1; -.
DR   Proteomes; UP000012045; Unassembled WGS sequence.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR041698; Methyltransf_25.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR35897; METHYLTRANSFERASE AUSD; 1.
DR   PANTHER; PTHR35897:SF1; METHYLTRANSFERASE AUSD; 1.
DR   Pfam; PF13649; Methyltransf_25; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000313|EMBL:EMR80536.1};
KW   Transferase {ECO:0000313|EMBL:EMR80536.1}.
FT   DOMAIN          99..201
FT                   /note="Methyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF13649"
SQ   SEQUENCE   280 AA;  32405 MW;  B63CB68602C18FF9 CRC64;
     MNNSGIEAKI EERSTHLPWY QLTVPSTKLD GAIRELLEDY AGFPSSEVEP HVYNIRNRAW
     SIFPYPCIGA FHFLDIVITS FPYYSTLLSR LASPDTKFLD LGCCFGQVMR RLVYDGALAE
     NLYGCDLRTE FFELGYDLFK DKDTFNSTLF KADIFDEDNV DLKRLEGDID VIYAGSFLHL
     YGWDDQVKIC KILARIMKKE GSVLMGRQGG GRVAKEVTFP LHEENKMFVH NAESFRKMWD
     EVSETTGTKW KVECEEIQLR DDDWKGAEGM VWIQFTIFRE
//
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