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