ID   A0A2B7XZV8_9EURO        Unreviewed;      1010 AA.
AC   A0A2B7XZV8;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:PGH14313.1};
GN   ORFNames=AJ79_03135 {ECO:0000313|EMBL:PGH14313.1};
OS   Helicocarpus griseus UAMH5409.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Helicocarpus.
OX   NCBI_TaxID=1447875 {ECO:0000313|EMBL:PGH14313.1, ECO:0000313|Proteomes:UP000223968};
RN   [1] {ECO:0000313|EMBL:PGH14313.1, ECO:0000313|Proteomes:UP000223968}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH5409 {ECO:0000313|EMBL:PGH14313.1,
RC   ECO:0000313|Proteomes:UP000223968};
RA   Munoz J.F., Mcewen J.G., Clay O.K., Cuomo C.A.;
RT   "Comparative genomics in systemic dimorphic fungi from Ajellomycetaceae.";
RL   Submitted (OCT-2017) 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:PGH14313.1}.
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DR   EMBL; PDNB01000036; PGH14313.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2B7XZV8; -.
DR   STRING; 1447875.A0A2B7XZV8; -.
DR   OrthoDB; 177966at2759; -.
DR   Proteomes; UP000223968; 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; 6.
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:UP000223968};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW   ProRule:PRU00221}.
FT   REPEAT          89..130
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   REPEAT          245..266
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   REGION          890..929
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          986..1010
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        890..919
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        986..1003
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1010 AA;  110545 MW;  43826579FC53880A CRC64;
     MDDYSDFDGP SDIELELDRR PQFRPQHSYC DGETPPEVEL NNPCAVGHRV QAVRSVLALV
     IDEECVFAGL QGGDIVAWSL DTYELILSVR AHQESVLGLY LFEDGSLLFS SGGDSVVNVW
     STRTFERLYS IYSHHDVGDL FTVVYSSQLK TVYCGGQNTS IQWCDLQLDA QPTPPTAVHP
     SSRRHRFFDS KGPGGIVTRN PDAGEAAEKL GHGGQTLTFK RDQHKLYAHN GYIYCMLLTR
     GLEEWANGGE ILLTGSGDGS VKLWELGKGK EGAPIELAEL KNGSDSVLSI AIDGTFLYCG
     LSGGSVNIWN LDSRQIIKKL TAHTGDLWAI DVLGGVTITG DSSGVVRKLN SRFEDIGSWI
     AHEGTMLASA AGIFNGRRIY ATGGNDNTVA IWDLTEHPQD SGEIPAVGND EMVNSLAKFV
     AFKTISSRPK FAGECNQGAA FLRRHCNYLG AKTKLLATGP NTNPIVFARF NSVSKASTNK
     TILFYGHYDV VGADTNHLKW NTDPFQLSSI NGFLYGRGVS DNKGPILAAL YAAAELTQKK
     DLSCNVVFLI EGEEESGSQG FSSTVQKYKG LIGNIDWILL ANSYWLDDHI PCLTYGLRGV
     VHANFVVTSS NPDLHSGIDG SSLLDEPLKD LTMLLGTLVG PKGKINIPGF QDPVLPLTEA
     EKERYAAIAE ALLPHHPEIE NCESFIDSLM HRWREPSLTI HRVEVPGCQN TSTTISRKAR
     ATLSVRLVPN QDADQVAHDL TEFAQARFAE FDSQNTLTVE ITGKAEPWLG DPDNDIFESL
     SRAVTAAWSS TKGDRHYNYP PPNLPSQLSR RELMRTNSSD SMASHIDRII SSSSSAPKTS
     SGHRLSATSI PTSSTLAYGS ELPSIKIING TRASYKQPTS SPACEITPSA AMESEAETIQ
     QQSHTRTSTS TSQTPVSQPR PSQPLKPIYI REGGSIPTIR YLEKEFNAPA AHLPCGQASD
     HAHLDNERLR VENLYKSREI IGRVFRDLGR DKERNHNGDG NRDESEESEE
//