ID   VERJ_CLORO              Reviewed;         388 AA.
AC   A0A1U9YI27;
DT   17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT   17-JUN-2020, sequence version 2.
DT   03-AUG-2022, entry version 12.
DE   RecName: Full=Dipeptidase verJ {ECO:0000250|UniProtKB:Q4WMJ8};
DE            EC=3.4.13.19 {ECO:0000250|UniProtKB:Q4WMJ8};
DE   AltName: Full=Verticillin biosynthesis cluster protein J {ECO:0000303|PubMed:28376389};
DE   Flags: Fragment;
GN   Name=verJ {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: Dipeptidase; part of the gene cluster that mediates the
CC       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   -!- CATALYTIC ACTIVITY:
CC       Reaction=an L-aminoacyl-L-amino acid + H2O = 2 an L-alpha-amino acid;
CC         Xref=Rhea:RHEA:48940, ChEBI:CHEBI:15377, ChEBI:CHEBI:59869,
CC         ChEBI:CHEBI:77460; EC=3.4.13.19;
CC         Evidence={ECO:0000250|UniProtKB:Q4WMJ8};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10073};
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 metallo-dependent hydrolases superfamily.
CC       Peptidase M19 family. {ECO:0000255|PROSITE-ProRule:PRU10073}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AQZ42165.1; Type=Erroneous gene model prediction; Note=Due to a wrong gene model prediction, the N-terminal sequence was wrong and only part of the N-terminus could be recovered.; Evidence={ECO:0000305};
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DR   EMBL; KY359203; AQZ42165.1; ALT_SEQ; Genomic_DNA.
DR   AlphaFoldDB; A0A1U9YI27; -.
DR   SMR; A0A1U9YI27; -.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0070573; F:metallodipeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd01301; rDP_like; 1.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   InterPro; IPR008257; Pept_M19.
DR   PANTHER; PTHR10443; PTHR10443; 1.
DR   Pfam; PF01244; Peptidase_M19; 1.
DR   SUPFAM; SSF51556; SSF51556; 1.
DR   PROSITE; PS51365; RENAL_DIPEPTIDASE_2; 1.
PE   2: Evidence at transcript level;
KW   Dipeptidase; Hydrolase; Metal-binding; Metalloprotease; Protease; Zinc.
FT   CHAIN           <1..388
FT                   /note="Dipeptidase verJ"
FT                   /id="PRO_0000450165"
FT   BINDING         29
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10073"
FT   BINDING         31
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10073"
FT   BINDING         142
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10073"
FT   BINDING         169
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10073"
FT   BINDING         243
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10073"
FT   BINDING         300
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10073"
FT   NON_TER         1
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   388 AA;  43458 MW;  05B274E56F43227F CRC64;
     PIVSKMALLD DNLSKALKLL ADVPLIDGHN DFPYFIRGWF PEQIDSLDCR NVRIAHTDLE
     RLNQGRVGGV FWSAYVPCPD RHAKNDFVVD AQYESLRATM QQIDIIHTLI ERYSDRLGLA
     RTSSEVWEVF RSGRIASLIG VEGLHQIANS PGVMRNLYRL GVRYITLTHD SNNLYADSTN
     SSGPFHGGLS RDGISIVKEM NRIGMMVDLS HTSVATQKHV LAISKAPVIF SHSSCASVTE
     HPRNSPDDVL DMLKANGGVF MITFIRKPTD AESPTLEKVA DHVQHVGDRI GYEHVGIGSD
     FDGVMLTASG LDDVSKFPLL IAELLKRGVS DHSIKNMIGL NVLRVMDSVE EVSMKMKETG
     EEMLHEVFEE IWDEKMRDEV RKTRDIFD