ID   ERG6_PYRO3              Reviewed;         390 AA.
AC   L7IP31; A4R5U1; G4NGD4; Q5EN22;
DT   18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Sterol 24-C-methyltransferase;
DE            EC=2.1.1.41;
DE   AltName: Full=Delta(24)-sterol C-methyltransferase;
GN   Name=ERG6; ORFNames=OOU_Y34scaffold00069g5;
OS   Pyricularia oryzae (strain Y34) (Rice blast fungus) (Magnaporthe oryzae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX   NCBI_TaxID=1143189;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Y34; TISSUE=Conidium;
RA   Dong H.T., Peng Y.L., Chen B.S., Li Y.Z., Li D.B.;
RL   Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y34;
RX   PubMed=22876203; DOI=10.1371/journal.pgen.1002869;
RA   Xue M., Yang J., Li Z., Hu S., Yao N., Dean R.A., Zhao W., Shen M.,
RA   Zhang H., Li C., Liu L., Cao L., Xu X., Xing Y., Hsiang T., Zhang Z.,
RA   Xu J.-R., Peng Y.-L.;
RT   "Comparative analysis of the genomes of two field isolates of the rice
RT   blast fungus Magnaporthe oryzae.";
RL   PLoS Genet. 8:E1002869-E1002869(2012).
CC   -!- FUNCTION: Catalyzes the methyl transfer from S-adenosyl-methionine to
CC       the C-24 of zymosterol to form fecosterol. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-adenosyl-L-methionine + zymosterol = fecosterol + H(+) + S-
CC         adenosyl-L-homocysteine; Xref=Rhea:RHEA:21128, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17038, ChEBI:CHEBI:18252, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789; EC=2.1.1.41;
CC   -!- PATHWAY: Steroid metabolism; ergosterol biosynthesis; ergosterol from
CC       zymosterol: step 1/5.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. Erg6/SMT family. {ECO:0000255|PROSITE-ProRule:PRU01022}.
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DR   EMBL; AY849610; AAX07631.1; -; mRNA.
DR   EMBL; JH793273; ELQ44666.1; -; Genomic_DNA.
DR   AlphaFoldDB; L7IP31; -.
DR   SMR; L7IP31; -.
DR   UniPathway; UPA00768; UER00760.
DR   Proteomes; UP000011086; Unassembled WGS sequence.
DR   GO; GO:0003838; F:sterol 24-C-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0016126; P:sterol biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR013216; Methyltransf_11.
DR   InterPro; IPR030384; MeTrfase_SMT.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR013705; Sterol_MeTrfase_C.
DR   PANTHER; PTHR44068:SF1; HYPOTHETICAL LOC100005854; 1.
DR   PANTHER; PTHR44068; ZGC:194242; 1.
DR   Pfam; PF08241; Methyltransf_11; 1.
DR   Pfam; PF08498; Sterol_MT_C; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS51685; SAM_MT_ERG6_SMT; 1.
PE   2: Evidence at transcript level;
KW   Lipid biosynthesis; Lipid metabolism; Methyltransferase;
KW   S-adenosyl-L-methionine; Steroid biosynthesis; Steroid metabolism;
KW   Sterol biosynthesis; Sterol metabolism; Transferase.
FT   CHAIN           1..390
FT                   /note="Sterol 24-C-methyltransferase"
FT                   /id="PRO_0000423543"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        246
FT                   /note="D -> N (in Ref. 1; AAX07631)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   390 AA;  43036 MW;  4442B9609B8DA9D5 CRC64;
     MSKQQHPSSK TQITRRRDTA DMTFEQVLHK GSSANMGGLS SMLGKDREAS KTAVDQYFRH
     WDGKTAKTET TKVREERKAD YATLTRQYYN LVTDFYEYGW GQSFHFCTFA PGETFASAIT
     RYEHTLAHRI GIKKGMKVLD IGCGVGGPAR QIAKFTGANI TGITINEYQV ERARRYAEME
     GYGAGEQLKF VQGDFMALPF EKETFDAVYS IEATVHAPKL EDVYKQIFNV LKPGGIFGLY
     EWVMTDAYDE NDPHHKEIRF GIEHGGGIAN LQTAQTAIAA IKAAGFELLE SEDLADNSDR
     APWYWPLGGN AWQYASTFGD ILSTFTMTPA GRAIAHTVLG VVESIGLVPP GTKKTADSLS
     TTAAALVAGG KEGLFTPMFL MVARKPVAKE
//