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Database: UniProt
Entry: A0A1V6RI92_9EURO
LinkDB: A0A1V6RI92_9EURO
Original site: A0A1V6RI92_9EURO 
ID   A0A1V6RI92_9EURO        Unreviewed;       454 AA.
AC   A0A1V6RI92;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=SAM-dependent methyltransferase Erg6/SMT-type domain-containing protein {ECO:0000259|PROSITE:PS51685};
GN   ORFNames=PENSOL_c004G10161 {ECO:0000313|EMBL:OQE01326.1};
OS   Penicillium solitum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=60172 {ECO:0000313|EMBL:OQE01326.1, ECO:0000313|Proteomes:UP000191612};
RN   [1] {ECO:0000313|Proteomes:UP000191612}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 29525 {ECO:0000313|Proteomes:UP000191612};
RX   PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA   Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA   Frisvad J.C., Workman M., Nielsen J.;
RT   "Global analysis of biosynthetic gene clusters reveals vast potential of
RT   secondary metabolite production in Penicillium species.";
RL   Nat. Microbiol. 2:17044-17044(2017).
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:OQE01326.1}.
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DR   EMBL; MDYO01000004; OQE01326.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V6RI92; -.
DR   STRING; 60172.A0A1V6RI92; -.
DR   OrthoDB; 5473013at2759; -.
DR   Proteomes; UP000191612; 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:1901617; P:organic hydroxy compound biosynthetic process; IEA:UniProt.
DR   GO; GO:0006694; P:steroid biosynthetic process; IEA:InterPro.
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   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU01022}; Reference proteome {ECO:0000313|Proteomes:UP000191612};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|PROSITE-ProRule:PRU01022};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW   ProRule:PRU01022}.
FT   DOMAIN          80..375
FT                   /note="SAM-dependent methyltransferase Erg6/SMT-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51685"
SQ   SEQUENCE   454 AA;  50786 MW;  3AED0D966A2E9892 CRC64;
     MTPATLEHED VARDAAFNKA LHGKSAKVNG GLAAMRGKDA TAQKAAIDEY FKHWDNKATD
     ETNAIREARK AEYATLTRHY YNLATDFYEY GWSTSFHFCR FAYGEPFHQA IARHEHYLAL
     QAGITKDMNV LDVGCGVGGP AREIVKFTGA NITGLNNNDY QIDRATYYAQ KQGLSDKMVF
     VKGDFMQMKF PDNSFDAVYV IEATVHAPDL EGVYKEIFRV LKPGGKFAVY EWFMTDDYDN
     DDPEHRRIRL GIEQGNGISN MVKVSEGLTA LRNAGFSLTH HEDMAARPDP IPWYYPLAGS
     FKHMGSVWDF FLIARMTWWG RGIAHRFIGA GETIGLFPKG SQKTGDSLSL GANCLVEGAQ
     KKLFTPMYLM VGQKPDMYSQ NSSHKNITMA GCQTSGSDTT LLRASACPIE KEYEWVVSVV
     IDRLHLQSKI RRHNAIYHTS SLGSARFAGL LAFA
//
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