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Database: UniProt
Entry: A0A1R1XTR9_9FUNG
LinkDB: A0A1R1XTR9_9FUNG
Original site: A0A1R1XTR9_9FUNG 
ID   A0A1R1XTR9_9FUNG        Unreviewed;       373 AA.
AC   A0A1R1XTR9;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Sterol 24-C-methyltransferase {ECO:0000256|RuleBase:RU362025};
DE            EC=2.1.1.- {ECO:0000256|RuleBase:RU362025};
DE   AltName: Full=Delta(24)-sterol C-methyltransferase {ECO:0000256|RuleBase:RU362025};
GN   ORFNames=AYI70_g5614 {ECO:0000313|EMBL:OMJ18016.1};
OS   Smittium culicis.
OC   Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC   Harpellomycetes; Harpellales; Legeriomycetaceae; Smittium.
OX   NCBI_TaxID=133412 {ECO:0000313|EMBL:OMJ18016.1, ECO:0000313|Proteomes:UP000187283};
RN   [1] {ECO:0000313|EMBL:OMJ18016.1, ECO:0000313|Proteomes:UP000187283}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GSMNP {ECO:0000313|EMBL:OMJ18016.1,
RC   ECO:0000313|Proteomes:UP000187283};
RA   Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL   Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the transfer of methyl groups from S-adenosyl-
CC       methionine to the C-24 of sterols. {ECO:0000256|RuleBase:RU362025}.
CC   -!- PATHWAY: Steroid metabolism. {ECO:0000256|RuleBase:RU362025}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. Erg6/SMT family. {ECO:0000256|ARBA:ARBA00038188,
CC       ECO:0000256|PROSITE-ProRule:PRU01022, ECO:0000256|RuleBase:RU362025}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OMJ18016.1}.
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DR   EMBL; LSSN01001866; OMJ18016.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1R1XTR9; -.
DR   STRING; 133412.A0A1R1XTR9; -.
DR   Proteomes; UP000187283; 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-KW.
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   3: Inferred from homology;
KW   Lipid biosynthesis {ECO:0000256|RuleBase:RU362025};
KW   Lipid metabolism {ECO:0000256|RuleBase:RU362025};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU01022}; Reference proteome {ECO:0000313|Proteomes:UP000187283};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|PROSITE-ProRule:PRU01022};
KW   Steroid biosynthesis {ECO:0000256|RuleBase:RU362025};
KW   Steroid metabolism {ECO:0000256|RuleBase:RU362025};
KW   Sterol biosynthesis {ECO:0000256|RuleBase:RU362025};
KW   Sterol metabolism {ECO:0000256|RuleBase:RU362025};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW   ProRule:PRU01022}.
FT   DOMAIN          78..371
FT                   /note="SAM-dependent methyltransferase Erg6/SMT-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51685"
SQ   SEQUENCE   373 AA;  42137 MW;  955EB0BC51F8AA29 CRC64;
     MTIAEEIQNL IDPTPEVSAK LHGESSNIPD TPSRIVKSLI SKDKAIQEES FNTYESFKNG
     GNLENNRTRL YTTMTNTFYN LATDFYEYGW GNSFHFSRRC KGELFETSIA RHENNLFRSA
     GIKEGDKVLD VGCGVGGPAR ECVRFTGAHV IGINNNDYQL EKARKYAKIS GQESNSEFVK
     GDFLNMPFPD NTFDAVYAIE ATCHAPELYS VYKEMFRVLK PGGKFAIYEW CITKDFSSDN
     KLHSSIIKRI EYGNGIPKLY STDRCLADVE KCGFKLEFSK DISEISVQGN LPWYTDLFQD
     YFNFSSFRSM AKTKLGIAAL TYMLGFLTFI KILPKSAYEV NNLLYDAAKA CVDGSANNIF
     TPMFQVVAHK PKN
//
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