ID   ERG6_CANGA              Reviewed;         372 AA.
AC   Q6FRZ7; Q56J90;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Sterol 24-C-methyltransferase;
DE            EC=2.1.1.41;
DE   AltName: Full=Delta(24)-sterol C-methyltransferase;
GN   Name=ERG6; OrderedLocusNames=CAGL0H04653g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=IHEM 21231;
RA   Vandeputte P., Bouchara J.-P.;
RT   "Polyene resistance in Candida glabrata.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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; AY942653; AAX73200.1; -; Genomic_DNA.
DR   EMBL; CR380954; CAG59930.1; -; Genomic_DNA.
DR   RefSeq; XP_446997.1; XM_446997.1.
DR   AlphaFoldDB; Q6FRZ7; -.
DR   SMR; Q6FRZ7; -.
DR   STRING; 5478.XP_446997.1; -.
DR   EnsemblFungi; CAG59930; CAG59930; CAGL0H04653g.
DR   GeneID; 2888522; -.
DR   KEGG; cgr:CAGL0H04653g; -.
DR   CGD; CAL0131698; ERG6.
DR   VEuPathDB; FungiDB:CAGL0H04653g; -.
DR   eggNOG; KOG1269; Eukaryota.
DR   HOGENOM; CLU_039068_5_3_1; -.
DR   InParanoid; Q6FRZ7; -.
DR   OMA; NTFDKVY; -.
DR   UniPathway; UPA00768; UER00760.
DR   Proteomes; UP000002428; Chromosome H.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:EnsemblFungi.
DR   GO; GO:0005811; C:lipid droplet; IEA:EnsemblFungi.
DR   GO; GO:0042802; F:identical protein binding; IEA:EnsemblFungi.
DR   GO; GO:0003838; F:sterol 24-C-methyltransferase activity; IMP:CGD.
DR   GO; GO:0006696; P:ergosterol biosynthetic process; IMP:CGD.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.150; -; 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   Pfam; PF08241; Methyltransf_11; 1.
DR   Pfam; PF08498; Sterol_MT_C; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS51685; SAM_MT_ERG6_SMT; 1.
PE   3: Inferred from homology;
KW   Lipid biosynthesis; Lipid metabolism; Methyltransferase;
KW   Reference proteome; S-adenosyl-L-methionine; Steroid biosynthesis;
KW   Steroid metabolism; Sterol biosynthesis; Sterol metabolism; Transferase.
FT   CHAIN           1..372
FT                   /note="Sterol 24-C-methyltransferase"
FT                   /id="PRO_0000124790"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..22
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   372 AA;  42440 MW;  4B0180321C688B80 CRC64;
     MSESELRQRQ AEFTKELHGE GAESRTGLTA LLSKNRNAQR EAVSKYLRHW DGKTDKEAED
     RRLEDYNEAT HSYYNVVTDF YEYGWGSSFH FSRFYKGENF QAAMARHEQY LAYMAGIKKG
     DLVLDVGCGV GGPARTIARF TGCNIIGLNN NDYQIQKAKY YAKKYNLQDH MDFVKGDFMN
     MEFEPNSFDK VYAIEATCHA PKLEGVYGEI YKVLKPGGTF AVYEWVMTEN YDENNEEHRK
     IAYEIELGDG IPKMFTVDVA KQALKNVGFE VEVSKDLADE DDEIPWYYPL TGEWKYVQSL
     SDIATFFRTS YFGRKFTNCM VSIMEKVGVA PQGSVEVTAA LENAAVGLVE GGRKKLFTPM
     FLFVAKKPED AK