ID   A0A1V6QJK7_9EURO        Unreviewed;       419 AA.
AC   A0A1V6QJK7;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Peptidase M20 domain-containing protein 2 {ECO:0000256|PIRNR:PIRNR037226};
GN   ORFNames=PENANT_c002G08707 {ECO:0000313|EMBL:OQD89393.1};
OS   Penicillium antarcticum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=416450 {ECO:0000313|EMBL:OQD89393.1, ECO:0000313|Proteomes:UP000191672};
RN   [1] {ECO:0000313|Proteomes:UP000191672}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 31811 {ECO:0000313|Proteomes:UP000191672};
RX   PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA   Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA   Frisvad J.C., Workman M., Nielsen J.;
RT   "Global analysis of biosynthetic gene clusters reveals vast potential of
RT   secondary metabolite production in Penicillium species.";
RL   Nat. Microbiol. 2:17044-17044(2017).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC   -!- SIMILARITY: Belongs to the peptidase M20A family.
CC       {ECO:0000256|ARBA:ARBA00006247, ECO:0000256|PIRNR:PIRNR037226}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OQD89393.1}.
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DR   EMBL; MDYN01000002; OQD89393.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V6QJK7; -.
DR   STRING; 416450.A0A1V6QJK7; -.
DR   OrthoDB; 1074531at2759; -.
DR   Proteomes; UP000191672; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016805; F:dipeptidase activity; IEA:InterPro.
DR   CDD; cd05672; M20_ACY1L2-like; 1.
DR   Gene3D; 3.30.70.360; -; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR017439; Amidohydrolase.
DR   InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   InterPro; IPR017144; Xaa-Arg_dipeptidase.
DR   NCBIfam; TIGR01891; amidohydrolases; 1.
DR   PANTHER; PTHR30575; PEPTIDASE M20; 1.
DR   PANTHER; PTHR30575:SF0; XAA-ARG DIPEPTIDASE; 1.
DR   Pfam; PF07687; M20_dimer; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   PIRSF; PIRSF037226; Amidohydrolase_ACY1L2_prd; 1.
DR   SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000191672};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT   DOMAIN          196..288
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   419 AA;  44657 MW;  9D89023D26709B7A CRC64;
     MLTVQAQTEI IQKVHGALDK YEAKLSDINQ RIWSTPELAF KEYNAHDSIC TFFESLNDAY
     TVTRKAYGVE TALEVAYKQG NGGRIVAFNA EYDALPGMGH ACGHNLIATS SIAAFLATVE
     TMKALHSNNP KASYEVRLFG TPAEEGGGGK LLLINAGAYK PIHACFMVHP FPILSGAPEL
     LSSSSCMGQY LANDKVRVTY TGKPAHASAA PWEGVNALDA VVSAYVGISM LRQQIRPTDK
     IHGVVLRGGE RPNVIPASTT VEYYIRSGSV AELKPLTEKV VKCFEAAATA TGCSVEFEWE
     ASYKDMKINL PICDSYVSAM NAMGHSTIFD AAGQAGGLSG GSTDMGNVSY EVPSFHGGFY
     IATDGVNHTP QFTAGAGSEE GFKRSLHCAA GMAVVACRDL VDDSFAKAVE SDFGTDNTL
//