ID A0A2N5V960_9BASI Unreviewed; 953 AA.
AC A0A2N5V960;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Peptidase M20 dimerisation domain-containing protein {ECO:0000259|Pfam:PF07687};
GN ORFNames=PCANC_08499 {ECO:0000313|EMBL:PLW46543.1}, PCASD_07370
GN {ECO:0000313|EMBL:PLW40829.1}, PCASD_20168
GN {ECO:0000313|EMBL:PLW10979.1};
OS Puccinia coronata f. sp. avenae.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX NCBI_TaxID=200324 {ECO:0000313|EMBL:PLW46543.1, ECO:0000313|Proteomes:UP000235388};
RN [1] {ECO:0000313|Proteomes:UP000235388, ECO:0000313|Proteomes:UP000235392}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12NC29 {ECO:0000313|EMBL:PLW46543.1}, and 12SD80
RC {ECO:0000313|EMBL:PLW10979.1};
RA Miller M.E., Zhang Y., Omidvar V., Sperschneider J., Schwessinger B.,
RA Raley C., Palmer J.M., Garnica D., Upadhyaya N., Rathjen J., Taylor J.M.,
RA Park R.F., Dodds P.N., Hirsch C.D., Kianian S.F., Figueroa M.;
RT "De novo assembly and phasing of dikaryotic genomes from two isolates of
RT Puccinia coronata f. sp. avenae, the causal agent of oat crown rust.";
RL Submitted (NOV-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:PLW46543.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; PGCI01000942; PLW10979.1; -; Genomic_DNA.
DR EMBL; PGCI01000097; PLW40829.1; -; Genomic_DNA.
DR EMBL; PGCJ01000118; PLW46543.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N5V960; -.
DR STRING; 200324.A0A2N5V960; -.
DR OrthoDB; 177966at2759; -.
DR Proteomes; UP000235388; Unassembled WGS sequence.
DR Proteomes; UP000235392; 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; 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; 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; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 4.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000235388};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW ProRule:PRU00221}.
FT REPEAT 53..85
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 303..319
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 363..388
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 456..472
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT DOMAIN 691..845
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
FT REGION 141..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 953 AA; 104717 MW; E8939DEBC54C9E57 CRC64;
MESLTLLTTL SSQDKESILS LATDYQAGNV FGGSQSGDIH VWSLRTFFPV TRLVGHQSSV
LCLTISIERS LLFSSSGDNT VRIWDTNLFG HALYVVKPPI DSCGDVLSLI WCDQLSVLYL
GCQDTSIQWI YLPQLPTYRA SDPKKQDSTA PSSAAVLRPN SAAPSMEHSL SAPVKSCSTS
VGPPSPEGVN SMRTSANISP NLQSVRSPHH KFFDSLSQSE LLKAARRREC KNSQSPPHML
SFELFTEGQG KLRDPIDDIC SPEAPQREGG AEVLYIDNKD SVTYAHFGYI YCLLLICLND
QLLLISGSGD STIKVWTLDP QTGALNRKFK LLSANSSSHL APSTVSPQSS EDLGAVLTLA
AYGSTLYSGY QDGVIKIWDL DTFTCIRTLF HRGSHLSSKD SDDVLTMTVL DNGELFSGCS
SGVIIRWDSS FQRVLKWQSH EGSALASCFV LYQGKRLLLT GGSDNCIKIW DVYHTEASVP
RLVTDVPEMK DEAGTAMAFQ DRMFRHLSQF VSYRSISNEE HREECRQAAL YLKTTLVKLG
ADARLLPGDP GRNPLVLATF KGKSSSESPT SKTRRRRVLY YGHYDVVQAG DAKDWTAPAF
VMTGQNGWLY GRGVTDNKGP TLAVAYAVTA LLDQRALDVD VVMLVEGEEE AGSAGFQKAV
KENKELIGAI DVVLVSNSYW LDDETPCMTF GLRGVIHATV KVSSSQPDLH SGMHGGAVHE
PVLDLVRILG DLVGKDGKIR LDGFYKGVRP IDAEEQKHYD RIVEHISNFA NVELLKHSPT
SDIRENLIAK WRQPSLSIHK IDVTGPAHST VIPASAQSAV SIRIVPDQSL EEISSSLVSF
LHEAFRPLNS SNTLEVKINQ TADWWLGHPQ DLHSMALAEC VEEEWGMKPL WIREGGSIPS
IPFLEQEFNA TAIHLPMGSA SDSAHLPNER IKMVNLEKGN HVVAKFLKKV ALI
//
