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VERM_CLORO
ID   VERM_CLORO              Reviewed;         407 AA.
AC   A0A1U9YI02;
DT   17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2017, sequence version 1.
DT   03-AUG-2022, entry version 13.
DE   RecName: Full=O-methyltransferase verK {ECO:0000250|UniProtKB:Q4WMJ5};
DE            EC=2.1.1.- {ECO:0000250|UniProtKB:Q4WMJ5};
DE   AltName: Full=Verticillin biosynthesis cluster protein M {ECO:0000303|PubMed:28376389};
GN   Name=verM {ECO:0000303|PubMed:28376389};
OS   Clonostachys rogersoniana.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Bionectriaceae; Clonostachys.
OX   NCBI_TaxID=122658;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE, AND
RP   PATHWAY.
RC   STRAIN=XZC04-CC-302;
RX   PubMed=28376389; DOI=10.1016/j.fgb.2017.03.007;
RA   Wang Y., Hu P., Pan Y., Zhu Y., Liu X., Che Y., Liu G.;
RT   "Identification and characterization of the verticillin biosynthetic gene
RT   cluster in Clonostachys rogersoniana.";
RL   Fungal Genet. Biol. 103:25-33(2017).
RN   [2]
RP   INDUCTION.
RX   PubMed=29058652; DOI=10.1099/mic.0.000557;
RA   Guo Z., Hao T., Wang Y., Pan Y., Ren F., Liu X., Che Y., Liu G.;
RT   "VerZ, a Zn(II)2Cys6 DNA-binding protein, regulates the biosynthesis of
RT   verticillin in Clonostachys rogersoniana.";
RL   Microbiology 163:1654-1663(2017).
CC   -!- FUNCTION: O-methyltransferase; part of the gene cluster that mediates
CC       the biosynthesis of 11'-deoxyverticillin A, one of the dimeric
CC       epipolythiodioxopiperazines (ETPs) from the verticillin family that act
CC       as mycotoxins (PubMed:28376389). 11'-deoxyverticillin A is required for
CC       normal conidiation (PubMed:28376389). The nonribosomal peptide
CC       synthetase verP is speculated to be responsible for condensation of
CC       amino acids to form the carbon skeleton of verticillin, whereas the
CC       cluster-specific tailoring enzymes are involved in further
CC       modifications leading to the production of 11'-deoxyverticillin A
CC       (Probable). {ECO:0000269|PubMed:28376389, ECO:0000305|PubMed:28376389}.
CC   -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:28376389}.
CC   -!- INDUCTION: Expression is regulated by the cluster-specific regulator
CC       verZ. {ECO:0000269|PubMed:29058652}.
CC   -!- DISRUPTION PHENOTYPE: Completely abolishes the 11'-deoxyverticillin A
CC       production. {ECO:0000269|PubMed:28376389}.
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; KY359203; AQZ42159.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1U9YI02; -.
DR   SMR; A0A1U9YI02; -.
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   PIRSF; PIRSF005739; O-mtase; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS51683; SAM_OMT_II; 1.
PE   2: Evidence at transcript level;
KW   Methyltransferase; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..407
FT                   /note="O-methyltransferase verK"
FT                   /id="PRO_0000450167"
FT   ACT_SITE        314
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         263
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         295..297
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
SQ   SEQUENCE   407 AA;  45770 MW;  2737458FAA991266 CRC64;
     MEAALKKLNI ALQEAIDSFE GPLNQERLNE LQTTESLPNK EVWSLASQTI DLADKIIHRL
     QPPSLQLAES FLAYLDTKCL WAAVSHDIPD LITAGGPQTV QELAKKSGLQ SIRLKQVMRV
     LHNNGIFEYK PTTQKYSNTP SSTLLAKDHW TQWHLWVDLY GNEHYKAAEG IPDAIREGQT
     RCAAQIQYDT DESMFRYFAR NGLQEKFHKT LGAGAVAQAP GMMADYNWGE LDDAVVLDIG
     GGGGDFITSL LREHPSMRGG LFELDSVIEM VRPKYRDASG EFADVGDRMV DLHVGDFRVE
     VPAYEVYTMK WCLHNWLDED VVKILSAVRR AIKVTPRARM VVVESVLKDG RSSRIWRFGD
     LTMMAGANGQ EREEEDWRGL AAKTGWNIHS ISPLRNAWAA AIDLRPC
 
 
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