ID   A0A139HGQ8_9PEZI        Unreviewed;       421 AA.
AC   A0A139HGQ8;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Peptidase M20 domain-containing protein 2 {ECO:0000256|PIRNR:PIRNR037226};
GN   ORFNames=AC578_4549 {ECO:0000313|EMBL:KXT01539.1};
OS   Pseudocercospora eumusae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX   NCBI_TaxID=321146 {ECO:0000313|EMBL:KXT01539.1, ECO:0000313|Proteomes:UP000070133};
RN   [1] {ECO:0000313|EMBL:KXT01539.1, ECO:0000313|Proteomes:UP000070133}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 114824 {ECO:0000313|EMBL:KXT01539.1,
RC   ECO:0000313|Proteomes:UP000070133};
RA   Chang T.-C., Salvucci A., Crous P.W., Stergiopoulos I.;
RT   "Comparative genomics of the Sigatoka disease complex on banana suggests a
RT   link between parallel evolutionary changes in Pseudocercospora fijiensis
RT   and Pseudocercospora eumusae and increased virulence on the banana host.";
RL   Submitted (JUL-2015) 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:KXT01539.1}.
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DR   EMBL; LFZN01000054; KXT01538.1; -; Genomic_DNA.
DR   EMBL; LFZN01000054; KXT01539.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A139HGQ8; -.
DR   OrthoDB; 1074531at2759; -.
DR   Proteomes; UP000070133; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016805; F:dipeptidase activity; IEA:InterPro.
DR   CDD; cd03887; M20_Acy1L2; 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:SF4; 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:UP000070133};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT   DOMAIN          186..279
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   421 AA;  45530 MW;  E408EFF2E7DED63E CRC64;
     MDDFIMIEHK EVDAPYLNSI SASVDALSGD LRKVSLEVHD HPELGYKEFH AHEVLTKYMS
     QQKGWKVTPS AYGIETAFVA VYRSGKPGPV VSFNAEYDAL KGIGHACGHN LICIASVGAA
     LATAKLLAHQ KLGGQVVLLG TPAEEGGGGK IKLLNAGAYK DNNVDISLIS HPGIDDDRAL
     VRTAAYASFK VEYFGKEAHA AAMPWDGINA LDALITAYNA ISVLRQQTQP GDIIQANITN
     GGLRPNIIHA YASGMFVVRS ANRARLDALK KRVFACFDAG ATATGAELKL TPKGAYDDHM
     PNHTIAARYR EAFNRLGGSI PSGDIDYLTG STMASTDQGN ISYVYPSISP NFWIRSEDEH
     GKQLGGPHTP DFEKAARTEE NHRMALRVAK ALSATAVDML TRPELLDEAK REFKDAIKRV
     P
//