ID   ATR12_STAC4             Reviewed;         391 AA.
AC   A0A084R1I1;
DT   22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT   29-OCT-2014, sequence version 1.
DT   03-AUG-2022, entry version 29.
DE   RecName: Full=O-methyltransferase ATR12 {ECO:0000303|PubMed:25015739};
DE            EC=2.1.1.- {ECO:0000255|PROSITE-ProRule:PRU01020};
DE   AltName: Full=Core atranone cluster (CAC) protein 12 {ECO:0000303|PubMed:25015739};
GN   Name=ATR12 {ECO:0000303|PubMed:25015739}; ORFNames=S40285_03336;
OS   Stachybotrys chlorohalonata (strain IBT 40285).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Stachybotryaceae; Stachybotrys.
OX   NCBI_TaxID=1283841;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], IDENTIFICATION, FUNCTION,
RP   AND PATHWAY.
RC   STRAIN=IBT 40285;
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 core atranone cluster (CAC)
CC       which products are predicted to catalyze most or all steps of mycotoxin
CC       atranone synthesis, starting from geranylgeranyl pyrophosphate (GGPP)
CC       (PubMed:25015739). The initial cyclization of GGPP to dolabellane is
CC       probably performed by the terpene cyclase ATR13 (PubMed:25015739). The
CC       Baeyer-Villiger oxidation near the end of the atranone synthesis, which
CC       converts atranones D and E to atranones F and G is predicted to be
CC       catalyzed by the monooxygenase ATR8 (PubMed:25015739). Of the CAC's
CC       other predicted gene products, the reducing PKS ATR6 might synthesize a
CC       polyketide chain (PubMed:25015739). This polyketide is probably
CC       transferred onto the atranone backbone by the polyketide transferase
CC       ATR5 (By similarity). Other predicted CAC products include 4 oxygenases
CC       (ATR2, ATR3, ATR4, and ATR14), 3 short-chain reductases (ATR7, ATR9,
CC       and ATR10), and a methyltransferase (ATR12) (PubMed:25015739). These
CC       may all be involved in the various steps of atranone biosynthesis,
CC       although their specific roles must await experimental determination
CC       (PubMed:25015739). {ECO:0000250|UniProtKB:Q4WAY4,
CC       ECO:0000305|PubMed:25015739}.
CC   -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000305|PubMed:25015739}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. Cation-independent O-methyltransferase family. COMT
CC       subfamily. {ECO:0000305}.
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DR   EMBL; KL659308; KFA70066.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A084R1I1; -.
DR   SMR; A0A084R1I1; -.
DR   EnsemblFungi; KFA70066; KFA70066; S40285_03336.
DR   HOGENOM; CLU_005533_5_0_1; -.
DR   OMA; TGHMEAW; -.
DR   OrthoDB; 817726at2759; -.
DR   Proteomes; UP000028524; 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; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..391
FT                   /note="O-methyltransferase ATR12"
FT                   /id="PRO_0000442407"
FT   ACT_SITE        299
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         233..234
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:O04385"
FT   BINDING         259
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         279..280
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:O04385"
SQ   SEQUENCE   391 AA;  43506 MW;  DE6443F8FA681557 CRC64;
     MASSVATLVK SLDKINAADF ESDEAARVNA IAAAQKMIHR LQSGVERGIE LTHQRSTVFP
     IIDVFEDLGL WEAWASQGHE ISLEGLAQLS NTPLALNLLR RLCRLLTAAD IFEEKSEDCY
     TPTELSLYMG DKTKGSQVSQ GSAPGWVGSY TNLPIFLKET AYQEPLDPKK SAYSKTAGKS
     FWEELSQDPL QQENFGRFMS SWAKFKVPWP AFYDTESLVR GAEPGMPILV DIGGNDGTDV
     ERFLAKHPGV AAGSLILQDR PAALKLAKVD QKIELMPHDF FTPQPVIGSR AYFFHAVLHD
     WDDAHALDIL RNTVPAMRKG YSKLLILDIA IPRTGASLIQ AAMDISMMSL LSSLERPITT
     WEILLKKAGL KIVKFWPDPR RYETLIEAEL E