ID   SAT12_STACB             Reviewed;         573 AA.
AC   A0A084API2;
DT   22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT   29-OCT-2014, sequence version 1.
DT   03-AUG-2022, entry version 18.
DE   RecName: Full=Putative 15-O-acetyltransferase SAT12 {ECO:0000303|PubMed:25015739};
DE            EC=2.3.2.- {ECO:0000305|PubMed:25015739};
DE   AltName: Full=Satratoxin biosynthesis SC2 cluster protein 13 {ECO:0000303|PubMed:25015739};
GN   Name=SAT12 {ECO:0000303|PubMed:25015739}; ORFNames=S7711_09750;
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: Putative 15-O-acetyltransferase; part of the satratoxin SC2
CC       cluster involved in the biosynthesis of satratoxins, trichothecene
CC       mycotoxins that are associated with human food poisonings
CC       (PubMed:25015739). Satratoxins are suggested to be made by products of
CC       multiple gene clusters (SC1, SC2 and SC3) that encode 21 proteins in
CC       all, including polyketide synthases, acetyltransferases, and other
CC       enzymes expected to modify the trichothecene skeleton
CC       (PubMed:25015739). SC1 encodes 10 proteins, SAT1 to SAT10
CC       (PubMed:25015739). The largest are SAT8, which encodes a putative
CC       polyketide synthase (PKS) with a conventional non-reducing
CC       architecture, and SAT10, a putative protein containing four ankyrin
CC       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 trichothecene O-acetyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; KL648628; KEY67211.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A084API2; -.
DR   SMR; A0A084API2; -.
DR   EnsemblFungi; KEY67211; KEY67211; S7711_09750.
DR   HOGENOM; CLU_552125_0_0_1; -.
DR   OrthoDB; 542619at2759; -.
DR   Proteomes; UP000028045; Unassembled WGS sequence.
DR   GO; GO:0016407; F:acetyltransferase activity; IEA:InterPro.
DR   GO; GO:0043386; P:mycotoxin biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.30.559.10; -; 1.
DR   InterPro; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR009992; Tri3/Sat12/Sat16/Mac1.
DR   Pfam; PF07428; Tri3; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Transferase.
FT   CHAIN           1..573
FT                   /note="Putative 15-O-acetyltransferase SAT12"
FT                   /id="PRO_0000442394"
FT   REGION          1..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..39
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   573 AA;  63810 MW;  6E66F719509D1269 CRC64;
     MLDDDCSPTS SSEMSNASSR EASITSRSSS TSGNNSLPED RGAVVQLPTL NPSDYRWHPF
     PGDSSVLQRK AIGVEALVGI RDANSRGEYD FYNNIVLRVG NALELTLTRL KRAFVKAMLD
     ARFENPSIAC YGVWGQNKEQ YLPHIQYKSF KSQSEALAWA NNCIIIQATS LTGSELRAER
     LKKRRAQAVP QPSNPLDIII YADVANQRNR LEPGTEVNIL FLFNHLIWDG KGRYFTSELV
     QRATTILDQE KENIMPTHRW GEEKSRLDPP ILDVMLVNLD KMGPDYDLAH RKLLNSQLQV
     GLSWGLPLTR NPGEPLQIRH CISREDSTKI TDAVRARLGP KYNIGHLGHA ATVLSLLKNN
     PIPPSTQDTA FLFSPLPVDG RPYLLEERKT PRYGNAQAAA VVELQKLASW GIKSDNLNGV
     KVALDDLAKK VKEDYDYWLT NLVAWRFKSS CTSEFIAFGS AIYQTPYLDP GAPKVKVGTG
     TSTDMVFLKA FCNDGRAESI IAYTMHGPSG KELFQVDDCF GGVDVLGSNA FIRMDTWKDA
     IRLTLCYNSG CFSDAVANSF TTDVAQYMLA YSW