ID   A0A094D7Z6_9PEZI        Unreviewed;       411 AA.
AC   A0A094D7Z6;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Peptidase M20 domain-containing protein 2 {ECO:0000256|PIRNR:PIRNR037226};
GN   ORFNames=V493_01535 {ECO:0000313|EMBL:KFY30937.1};
OS   Pseudogymnoascus sp. VKM F-4281 (FW-2241).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420906 {ECO:0000313|EMBL:KFY30937.1, ECO:0000313|Proteomes:UP000029327};
RN   [1] {ECO:0000313|EMBL:KFY30937.1, ECO:0000313|Proteomes:UP000029327}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4281 (FW-2241) {ECO:0000313|Proteomes:UP000029327};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
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:KFY30937.1}.
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DR   EMBL; JPJV01000569; KFY30937.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A094D7Z6; -.
DR   HOGENOM; CLU_031812_1_2_1; -.
DR   OrthoDB; 1074531at2759; -.
DR   Proteomes; UP000029327; 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:SF8; PEPTIDASE M20 DOMAIN-CONTAINING PROTEIN 2; 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:UP000029327};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT   DOMAIN          194..283
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   411 AA;  43638 MW;  241E3393925F29BB CRC64;
     MGGDSSAFAG DIKVEVDAAI DGLNQRLRQV NRQIWENPEL GEHEFMAHET LCSFFEEQGY
     AVTRSAYGRP TAFEVLSGSG GRLVNFNAEY DCLPGIGHAC GHNLIATSSV AAFLGLSMSL
     KKLGIPGRVQ LLGTPDEEGS GAKIKLLDAG AYKGVDASLM AHPFAGDITG NESVQNDGVA
     GMRMVARQYL SAEYRGKNAH AGGNPWNGIN ALDSAVSAYN SISLLRQQME PDERVHNVML
     ESEKTVNVIP AYAKAAYQAR SPRLAGVKAL TSRVVNCINA AALATGTEVK IEYGALYADV
     VLNETICGLY TSHTARYGHE VTKISPIIVT GSTDQGNVSQ VMPALHTMFS IPTEGNVGPH
     NAGFAKAAGT DVAHDKAIIV GKTMALVGFD ILTKDDVYES VKADWEKAMA A
//