ID C1GRQ6_PARBA Unreviewed; 1020 AA.
AC C1GRQ6;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 2.
DT 08-NOV-2023, entry version 71.
DE SubName: Full=WD repeat-containing protein {ECO:0000313|EMBL:EEH38280.2};
GN ORFNames=PAAG_01201 {ECO:0000313|EMBL:EEH38280.2};
OS Paracoccidioides lutzii (strain ATCC MYA-826 / Pb01) (Paracoccidioides
OS brasiliensis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX NCBI_TaxID=502779 {ECO:0000313|EMBL:EEH38280.2, ECO:0000313|Proteomes:UP000002059};
RN [1] {ECO:0000313|EMBL:EEH38280.2, ECO:0000313|Proteomes:UP000002059}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-826 / Pb01 {ECO:0000313|Proteomes:UP000002059};
RX PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT "Comparative genomic analysis of human fungal pathogens causing
RT paracoccidioidomycosis.";
RL PLoS Genet. 7:E1002345-E1002345(2011).
CC -!- SIMILARITY: Belongs to the peptidase M20A family.
CC {ECO:0000256|ARBA:ARBA00006247}.
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; KN293993; EEH38280.2; -; Genomic_DNA.
DR RefSeq; XP_015701048.1; XM_015844267.1.
DR AlphaFoldDB; C1GRQ6; -.
DR STRING; 502779.C1GRQ6; -.
DR GeneID; 9100080; -.
DR KEGG; pbl:PAAG_01201; -.
DR VEuPathDB; FungiDB:PAAG_01201; -.
DR eggNOG; KOG2276; Eukaryota.
DR HOGENOM; CLU_008535_1_0_1; -.
DR OMA; HATVCVD; -.
DR OrthoDB; 177966at2759; -.
DR Proteomes; UP000002059; Partially assembled 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; 3.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000002059};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW ProRule:PRU00221}.
FT REPEAT 88..129
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 244..265
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 375..393
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REGION 817..867
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 904..926
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 997..1020
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 817..859
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 904..925
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1002..1020
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1020 AA; 111037 MW; 205C2EAA0270DE76 CRC64;
MDDSDFDGPS DIELELDRRP QFQPQHSYCN GETPPDAQLN KPCAVGHRVQ AVRSVLALVI
DEECVFAGLQ GGDIVAWSLE TYELILSVKA HQESVLGLYL SDDGSLLFSS GGDSVVNVWS
TRTFERLYSI YSHHDVGDIF TAVYSTKLKT VYCGAQNTSI QWCDVQLEAH PTPPAGVHPS
SRRHRFFDSK GPGGTVTLNP DVSEAAAKLG HGGQTLTFKR DHHKPYAHNG YIYCMLLIRG
LEEWANGDEV LLTGSGDGSV KLWELGNGPD GSPLELAEFK NGSDSVLSIA VDGAFLYCGL
SGGAVYIWNL DSRQIIRKLT AHSGDLWAID VVGGITITGD SSGVIRKFNS RFEEIGSWVA
HEGTMLASAA GVFDDRRIYA TGGNDNTVAI WDLTEHPQDS REAPAIGNDE MVNSLAKFVS
FKTISSRPKF AGECNQGAAF LRRHCNYLGA HTKLLGTGPD TNPIVFARFD AVSKSSTSKT
LLFYGHYDVV GADTNHLKWN SDPFQLTSVN GFLYGRGVSD NKGPVLAALY AAAELSQKKA
LSCNVVFLIE GEEESGSQGF ANTVKKHKDL IGNVDWILLA NSYWLDDHIP CLTYGLRGVV
HANFVVTSSN PDLHSGIDGS SLLDEPLKDL TMLLGIIVGA KGKINIPGFH DPVLPLTEAE
KERYDAIAEA LLPHHPEIED SESFTDSLMH RWREPSLTIH RVEVPGCQNT STTISRKARA
TLSVRLVPNQ DAGKVAADLT EFAQAQFAKF DSQNTLTVEI TGKADPWLGD PENDIFKSLS
RAVTAAWSSA KGERHYNYPP VNIPNQLSRR ELLHTNSTDS MASRFDRITS SSSSAPKTSS
GHRLSTSAVP TSSTLAHGPD LPSANLPSRP RAFCRHGASS STCEISSAAA VVAAGGSMCY
RHPQVPQHSH TRTSTSTSQP PLAQPRSCQV VKPIYIREGG SIPTIRYLEK AFNAPAAHLP
CGQASDHAHL DNERLRVENL YKSREIISRV FRDLGRDDES AVVEDEGSES DREPEEDLEE
//
