ID   A0A139HPM4_9PEZI        Unreviewed;       954 AA.
AC   A0A139HPM4;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=Peptidase M20 dimerisation domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=AC578_7944 {ECO:0000313|EMBL:KXT04332.1};
OS   Pseudocercospora eumusae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX   NCBI_TaxID=321146 {ECO:0000313|EMBL:KXT04332.1, ECO:0000313|Proteomes:UP000070133};
RN   [1] {ECO:0000313|EMBL:KXT04332.1, ECO:0000313|Proteomes:UP000070133}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 114824 {ECO:0000313|EMBL:KXT04332.1,
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   -!- SIMILARITY: Belongs to the peptidase M20A family.
CC       {ECO:0000256|ARBA:ARBA00006247}.
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:KXT04332.1}.
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DR   EMBL; LFZN01000022; KXT04332.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A139HPM4; -.
DR   STRING; 321146.A0A139HPM4; -.
DR   OrthoDB; 177966at2759; -.
DR   Proteomes; UP000070133; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006751; P:glutathione catabolic process; IEA:InterPro.
DR   Gene3D; 3.30.70.360; -; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR   Gene3D; 3.40.630.10; Zn peptidases; 2.
DR   InterPro; IPR001261; ArgE/DapE_CS.
DR   InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR   InterPro; IPR017149; GSH_degradosome_Dug2.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   InterPro; IPR001680; WD40_rpt.
DR   PANTHER; PTHR43270; BETA-ALA-HIS DIPEPTIDASE; 1.
DR   PANTHER; PTHR43270:SF8; DI- AND TRIPEPTIDASE DUG2-RELATED; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   Pfam; PF00400; WD40; 2.
DR   PIRSF; PIRSF037237; Peptidase_WD_repeats_DUG2; 1.
DR   PRINTS; PR00320; GPROTEINBRPT.
DR   SMART; SM00320; WD40; 5.
DR   SUPFAM; SSF50978; WD40 repeat-like; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR   PROSITE; PS00758; ARGE_DAPE_CPG2_1; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 2.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070133};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW   ProRule:PRU00221}.
FT   REPEAT          110..151
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   REPEAT          380..415
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   REGION          32..66
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          836..863
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        840..862
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   954 AA;  104824 MW;  C3EACECF0AAB190C CRC64;
     MPLAVRRDCS EDRSALWIES HALNDAAAAL NGSETSDLES TSLPTRESFS RQPSQDHGDP
     SNTIPSLSQR LRHTSSILAI ALTSEHIYAG TQAGEILVYD LGTYEKRAVL EGHRGSVLGL
     CLSQDQKLLF SSSGDRVVNI WDTKTLKRTS CLRSSFDVGD VFCVAHSAAL DTAYLGSQNT
     MIQWCGISPQ SIKSLPTAVR DDDRFFDSRG PGGVRTPKPA GSDVLPKHAV GGDELEIEKV
     NVKHFAHYGY VYCMLLAREG VPERYGEDTL VTGGGDGVIK LWKLDAENGG AVEELYSLDD
     GREEGHAILS LAMDGTFVYS GRSGGEVDVW DLETKQLVRN LKAHRDDVQS LAVGGGFLFS
     AAVTGYVRKF DRQYQLKTRF KAHDGRILAS AFSFHKGKPV YVTGSNDNSL AVWDVTDCIR
     LSIVPGKTSN EQLVESLRRF VAFRTVSSDQ RHKADCRRAA SYLRSVFKNF GAITEMLPAE
     DGCNPVILAR FRGNPATRAQ RKKILFYGHY DVVPANNDSG KWIVDPFAME GIDGYLYGRG
     TSDNKGPIMA AIFACAELMT KQALGSDIVF LIEGEEESGS RGFEKAVKAS KDKIGDVDWI
     LLANSYWLDD RIPCLTYGLR GVIHATVQIE SNHPDLHSGV DGSAQLDESL KDLVLLLGTL
     TGKNGEVKIP GFYDPVPEVS DTEAALYADI TNALVSRNPD LGDPEALATS LMRRWREASL
     TIHRFQTSGP DNATIIPRMA KAALSIRLVP NQEASEVAKA LQTYLESGFK QLESNNRLTV
     TIDHKAEPWL GDWTNDLFKT LEEAIMEAWG PIETQANHHR SPSKAALKLG IPRQLANGHQ
     HAKPSPTTST TLANQSVETP SPLTPMAEVA NKLEEIITAP EKKPKQRRKP LYIREGGSIP
     AIRFLEKEFN APAAHFPCGQ ASDSAHLDNE RLRLQNLYKA KDIFAKVFRD LPQK
//