ID   SAT18_STACB             Reviewed;         401 AA.
AC   A0A084AFG7;
DT   22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT   29-OCT-2014, sequence version 1.
DT   03-AUG-2022, entry version 27.
DE   RecName: Full=O-methyltransferase SAT18 {ECO:0000303|PubMed:25015739};
DE            EC=2.1.1.- {ECO:0000255|PROSITE-ProRule:PRU01020};
DE   AltName: Full=Satratoxin biosynthesis SC3 cluster protein 186 {ECO:0000303|PubMed:25015739};
GN   Name=SAT18 {ECO:0000303|PubMed:25015739}; ORFNames=S7711_07409;
OS   Stachybotrys chartarum (strain CBS 109288 / IBT 7711) (Toxic black mold)
OS   (Stilbospora chartarum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Stachybotryaceae; Stachybotrys.
OX   NCBI_TaxID=1280523;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], IDENTIFICATION, AND
RP   FUNCTION.
RC   STRAIN=CBS 109288 / IBT 7711;
RX   PubMed=25015739; DOI=10.1186/1471-2164-15-590;
RA   Semeiks J., Borek D., Otwinowski Z., Grishin N.V.;
RT   "Comparative genome sequencing reveals chemotype-specific gene clusters in
RT   the toxigenic black mold Stachybotrys.";
RL   BMC Genomics 15:590-590(2014).
CC   -!- FUNCTION: O-methyltransferase; part of the satratoxin SC3 cluster
CC       involved in the biosynthesis of satratoxins, trichothecene mycotoxins
CC       that are associated with human food poisonings (PubMed:25015739).
CC       Satratoxins are suggested to be made by products of multiple gene
CC       clusters (SC1, SC2 and SC3) that encode 21 proteins in all, including
CC       polyketide synthases, acetyltransferases, and other enzymes expected to
CC       modify the trichothecene skeleton (PubMed:25015739). SC1 encodes 10
CC       proteins, SAT1 to SAT10 (PubMed:25015739). The largest are SAT8, which
CC       encodes a putative polyketide synthase (PKS) with a conventional non-
CC       reducing architecture, and SAT10, a putative protein containing four
CC       ankyrin repeats and thus may be involved in protein scaffolding
CC       (PubMed:25015739). The putative short-chain reductase SAT3 may assist
CC       the PKS in some capacity (PubMed:25015739). SAT6 contains a secretory
CC       lipase domain and acts probably as a trichothecene esterase
CC       (PubMed:25015739). SAT5 encodes a putative acetyltransferase, and so,
CC       with SAT6, may affect endogenous protection from toxicity
CC       (PubMed:25015739). The probable transcription factor SAT9 may regulate
CC       the expression of the SC1 cluster (PubMed:25015739). SC2 encodes
CC       proteins SAT11 to SAT16, the largest of which encodes the putative
CC       reducing PKS SAT13 (PubMed:25015739). SAT11 is a cytochrome P450
CC       monooxygenase, while SAT14 and SAT16 are probable acetyltransferases
CC       (PubMed:25015739). The SC2 cluster may be regulated by the
CC       transcription factor SAT15 (PubMed:25015739). SC3 is a small cluster
CC       that encodes 5 proteins, SAT17 to SAT21 (PubMed:25015739). SAT21 is a
CC       putative MFS-type transporter which may have a role in exporting
CC       secondary metabolites (PubMed:25015739). The four other proteins
CC       putatively encoded in SC3 include the taurine hydroxylase-like protein
CC       SAT17, the O-methyltransferase SAT18, the acetyltransferase SAT19, and
CC       the Cys6-type zinc finger SAT20, the latter being probably involved in
CC       regulation of SC3 expression (PubMed:25015739).
CC       {ECO:0000305|PubMed:25015739}.
CC   -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:25015739}.
CC   -!- MISCELLANEOUS: Trichothecenes are sesquiterpenoid toxins that act by
CC       inhibiting protein biosynthesis. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. Cation-independent O-methyltransferase family.
CC       {ECO:0000255|PROSITE-ProRule:PRU01020}.
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DR   EMBL; KL648755; KEY64046.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A084AFG7; -.
DR   SMR; A0A084AFG7; -.
DR   EnsemblFungi; KEY64046; KEY64046; S7711_07409.
DR   HOGENOM; CLU_005533_1_0_1; -.
DR   OrthoDB; 817726at2759; -.
DR   Proteomes; UP000028045; Unassembled WGS sequence.
DR   GO; GO:0008171; F:O-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.10.10; -; 1.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR016461; COMT-like.
DR   InterPro; IPR001077; O_MeTrfase_dom.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   Pfam; PF00891; Methyltransf_2; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS51683; SAM_OMT_II; 1.
PE   3: Inferred from homology;
KW   Methyltransferase; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..401
FT                   /note="O-methyltransferase SAT18"
FT                   /id="PRO_0000442408"
FT   ACT_SITE        300
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         249
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
SQ   SEQUENCE   401 AA;  44904 MW;  01D8919889A2B961 CRC64;
     MKLVEIAEDI LSKANAYTNN TGLTSSQRFQ LREEIRYQAN GILSAIDGPE QTMKAIARSY
     TTCTALKVCV DLKLASHLPL SDARSLSQLA QICGCDSLVL RPMLRLLAKN GIFEQVDAET
     WQHTELSAVM AQPPFQALEE KYRSVAHLPR LLQAVSHQFP TPGRTAFNQV YCTSLDFYTY
     SNELDHAAAR NFAFSMKELA RNQIPFVQQS YPLETIDPES HFIDVAGGVG YLSFFLAGSF
     PKATFEVQDH PFIIEEAHSV CPSELRDRIT FRAHNILHPQ PEIAKEINGR LVFLVKIILH
     DHGDDDCRLM LRNLVSVMKQ GDRILIIDTV IPETGGSLSS ANSDIIIMSM FGSGHRTLEE
     FRALIHRCGE DLVIETFASG DEEYDGMMVI EVRKAEPVLD N