ID A0A0B7G0R1_THACB Unreviewed; 948 AA.
AC A0A0B7G0R1;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Putative di-and tripeptidase DUG2 {ECO:0000313|EMBL:CEL62689.1};
GN ORFNames=RSOLAG1IB_05045 {ECO:0000313|EMBL:CEL62689.1};
OS Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14) (Lettuce bottom
OS rot fungus) (Rhizoctonia solani).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Cantharellales; Ceratobasidiaceae; Rhizoctonia; Rhizoctonia solani AG-1.
OX NCBI_TaxID=1108050 {ECO:0000313|EMBL:CEL62689.1, ECO:0000313|Proteomes:UP000059188};
RN [1] {ECO:0000313|EMBL:CEL62689.1, ECO:0000313|Proteomes:UP000059188}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rhizoctonia solani AG1-IB 7/3/14 {ECO:0000313|EMBL:CEL62689.1};
RA Wibberg Daniel;
RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase M20A family.
CC {ECO:0000256|ARBA:ARBA00006247}.
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DR EMBL; LN679106; CEL62689.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B7G0R1; -.
DR STRING; 1108050.A0A0B7G0R1; -.
DR Proteomes; UP000059188; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
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; 1.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR017149; GSH_degradosome_Dug2.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
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; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR Pfam; PF00400; WD40; 3.
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; PS50082; WD_REPEATS_2; 2.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000059188};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW ProRule:PRU00221}.
FT REPEAT 70..111
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 434..475
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT DOMAIN 707..838
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
FT REGION 172..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 335..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..209
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..264
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 948 AA; 102226 MW; C54DED915D065412 CRC64;
MSIMLPRGPS SSLSRTPPPE AAAARLVHTL RQKESSVLSL TADERFIYSG SQGMDIYVWD
RHTFSHTASL QGHTDSVLAL IHSPERQWLF SSSGDSTVRI WCTQTLSPLY TVLPHGESGD
IFSLIYVHTP TQQRLIFGCQ NTSIQWVDLS PSTLEPPSNS CQPGVGDISP AASVYGSFSS
NTGADNGMPN RDTPGAQTPI SSSTPPKHKF FDSFPQPAGR PTAPQRPSTA VLTTSSKLSL
QRSSTPIATP EIKKPTNGDG ANTTEPTDKN EDDPRVLAVP LEHVVSSAHY GYIYCMALVR
DESGDQVRLV TGSGDEETKL WELPPDNNPV LQHSFSHDFP SPTDPSAPAP EEADEDVGGA
VLALAVRDGT IFAGGQAGRI AVWDVETATL VRVLVAAEGV DVLSLSVLGQ DLYACTADGY
VHRWSSTFQH IAVYHAHSGI ILSSIAIASC GVFVTGAGDS SVKIWDVGTA RGRRRGNSKG
VWPNEPVDDI HDGDVLGLVY EDELEAEGAD DPSNALIFAL SKFVAIPSVS SAREDCKQAA
VWLKKCFSQL GADSYLVSST ENVNSLVVAT FRGRPPAPGA PRRPRILFYG HYDVISAPPY
GWTSDPFKLS GNNGALYGRG VSDDKGPTLA VAFAVSSLLS RRMLDVDVVM LVEGEEEAGS
AGFKGLFETV KDRVGEIDCI LVSNSFWIDD VTPCVTYGLR GVVHSSIEIS SERPDVHSGV
EGGAIVEPMV DMVKVLATLA NGSKVLIPSF YDKIRPQPEE ERVLYEKIAQ VTKTTPASIA
SRWSEPSLSI HSLNVSGPGN ATVIPSSVKA KVSIRIVPDQ DTDEIAASLV KHVNDAFGEL
QSPNVLKVQI DRTADWWLGE LDDEYFHALE DAVRKEWEVE PLRIREGGSI PSVPFLEKAL
GCHALHLPMG QSSDQAHLQN ERISVNNLRK GQAVVERFLA SLGKRELS
//
