ID   EASF_ARTOC              Reviewed;         340 AA.
AC   C5FTN1;
DT   15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 48.
DE   RecName: Full=4-dimethylallyltryptophan N-methyltransferase easF {ECO:0000250|UniProtKB:B6D5I7};
DE            EC=2.1.1.261 {ECO:0000250|UniProtKB:B6D5I7};
DE   AltName: Full=4-dimethylallyltryptophan methyltransferase {ECO:0000250|UniProtKB:B6D5I7};
DE   AltName: Full=Ergot alkaloid synthesis protein F {ECO:0000303|PubMed:22403186};
GN   Name=easF {ECO:0000303|PubMed:22403186}; ORFNames=MCYG_06053;
OS   Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) (Microsporum canis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Microsporum.
OX   NCBI_TaxID=554155;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4605 / CBS 113480;
RX   PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA   Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA   Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA   Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA   Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA   Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT   "Comparative genome analysis of Trichophyton rubrum and related
RT   dermatophytes reveals candidate genes involved in infection.";
RL   MBio 3:E259-E259(2012).
RN   [2]
RP   FUNCTION.
RX   PubMed=22403186; DOI=10.1099/mic.0.056796-0;
RA   Wallwey C., Heddergott C., Xie X., Brakhage A.A., Li S.M.;
RT   "Genome mining reveals the presence of a conserved gene cluster for the
RT   biosynthesis of ergot alkaloid precursors in the fungal family
RT   Arthrodermataceae.";
RL   Microbiology 158:1634-1644(2012).
CC   -!- FUNCTION: 4-dimethylallyltryptophan N-methyltransferase; part of the
CC       gene cluster that mediates the biosynthesis of fungal ergot alkaloid
CC       (PubMed:22403186). DmaW catalyzes the first step of ergot alkaloid
CC       biosynthesis by condensing dimethylallyl diphosphate (DMAP) and
CC       tryptophan to form 4-dimethylallyl-L-tryptophan (PubMed:22403186). The
CC       second step is catalyzed by the methyltransferase easF that methylates
CC       4-dimethylallyl-L-tryptophan in the presence of S-adenosyl-L-
CC       methionine, resulting in the formation of 4-dimethylallyl-L-abrine
CC       (PubMed:22403186). The catalase easC and the FAD-dependent
CC       oxidoreductase easE then transform 4-dimethylallyl-L-abrine to
CC       chanoclavine-I which is further oxidized by easD in the presence of
CC       NAD(+), resulting in the formation of chanoclavine-I aldehyde
CC       (PubMed:22403186). Chanoclavine-I aldehyde is the precursor of
CC       ergoamides and ergopeptines in Clavicipitaceae, and clavine-type
CC       alcaloids such as fumiclavine in Trichocomaceae (PubMed:22403186).
CC       However, the metabolites downstream of chanoclavine-I aldehyde in
CC       Arthrodermataceae have not been identified yet (PubMed:22403186).
CC       {ECO:0000269|PubMed:22403186}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-(3-methylbut-2-enyl)-L-tryptophan + S-adenosyl-L-methionine
CC         = 4-(3-methylbut-2-enyl)-L-abrine + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:34435, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:58209, ChEBI:CHEBI:59789, ChEBI:CHEBI:67248;
CC         EC=2.1.1.261; Evidence={ECO:0000250|UniProtKB:B6D5I7};
CC   -!- PATHWAY: Alkaloid biosynthesis; ergot alkaloid biosynthesis.
CC       {ECO:0000305|PubMed:22403186}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:B6D5I7}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC       {ECO:0000305}.
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DR   EMBL; DS995705; EEQ33234.1; -; Genomic_DNA.
DR   RefSeq; XP_002846184.1; XM_002846138.1.
DR   AlphaFoldDB; C5FTN1; -.
DR   SMR; C5FTN1; -.
DR   STRING; 63405.XP_002846184.1; -.
DR   EnsemblFungi; EEQ33234; EEQ33234; MCYG_06053.
DR   GeneID; 9227066; -.
DR   eggNOG; ENOG502SISP; Eukaryota.
DR   HOGENOM; CLU_049766_0_2_1; -.
DR   OMA; FGCSYKY; -.
DR   OrthoDB; 762504at2759; -.
DR   UniPathway; UPA00327; -.
DR   Proteomes; UP000002035; Unassembled WGS sequence.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0035835; P:indole alkaloid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR019257; MeTrfase_dom.
DR   InterPro; IPR017804; MeTrfase_EgtD-like.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR017805; SAM_MeTrfase_EasF-type_put.
DR   Pfam; PF10017; Methyltransf_33; 1.
DR   PIRSF; PIRSF018005; UCP018005; 1.
DR   TIGRFAMs; TIGR03439; methyl_EasF; 1.
PE   3: Inferred from homology;
KW   Alkaloid metabolism; Methyltransferase; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..340
FT                   /note="4-dimethylallyltryptophan N-methyltransferase easF"
FT                   /id="PRO_0000439139"
SQ   SEQUENCE   340 AA;  38134 MW;  EEDEFABEE679C6A4 CRC64;
     MGNTNPPHIL DIRRSKFEES IPKQVEAGLL SSPKTLPALL FYSTEGIQHW NRHSHAPDFY
     PRHEEIQILK EQATDMAASI ADGSVVVDLG SASLDKVIHL LEALEAAQKK VTYYALDLSF
     SELTSTLQAI PTEQFIHVQF SALHGTFEDG LHWLKETPVI QDQPHCLLLF GLTIGNFSRP
     NAAAFLRNIA SQALTGSPSQ SSILLTLDSC KVPTKVTRAY TAEGVVPFAL ESLRYANTLF
     PQDGEERVFD PHDWHFLSEW NYILGRHEAS LIPQSRDIKL GSPLDRIVVA KHEKIRFGCS
     YKYDCGERKE LFESAGLHDV KIWSKEGCDV AFYQLKCCPN