ID D5GA41_TUBMM Unreviewed; 867 AA.
AC D5GA41;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE SubName: Full=(Perigord truffle) hypothetical protein {ECO:0000313|EMBL:CAZ81384.1};
GN ORFNames=GSTUM_00003554001 {ECO:0000313|EMBL:CAZ81384.1};
OS Tuber melanosporum (strain Mel28) (Perigord black truffle).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC Pezizales; Tuberaceae; Tuber.
OX NCBI_TaxID=656061 {ECO:0000313|EMBL:CAZ81384.1, ECO:0000313|Proteomes:UP000006911};
RN [1] {ECO:0000313|EMBL:CAZ81384.1, ECO:0000313|Proteomes:UP000006911}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mel28 {ECO:0000313|EMBL:CAZ81384.1,
RC ECO:0000313|Proteomes:UP000006911};
RX PubMed=20348908; DOI=10.1038/nature08867;
RA Martin F., Kohler A., Murat C., Balestrini R., Coutinho P.M., Jaillon O.,
RA Montanini B., Morin E., Noel B., Percudani R., Porcel B., Rubini A.,
RA Amicucci A., Amselem J., Anthouard V., Arcioni S., Artiguenave F.,
RA Aury J.M., Ballario P., Bolchi A., Brenna A., Brun A., Buee M.,
RA Cantarel B., Chevalier G., Couloux A., Da Silva C., Denoeud F.,
RA Duplessis S., Ghignone S., Hilselberger B., Iotti M., Marcais B., Mello A.,
RA Miranda M., Pacioni G., Quesneville H., Riccioni C., Ruotolo R.,
RA Splivallo R., Stocchi V., Tisserant E., Viscomi A.R., Zambonelli A.,
RA Zampieri E., Henrissat B., Lebrun M.H., Paolocci F., Bonfante P.,
RA Ottonello S., Wincker P.;
RT "Perigord black truffle genome uncovers evolutionary origins and mechanisms
RT of symbiosis.";
RL Nature 464:1033-1038(2010).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the peptidase M20A family.
CC {ECO:0000256|ARBA:ARBA00006247}.
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DR EMBL; FN430073; CAZ81384.1; -; Genomic_DNA.
DR RefSeq; XP_002837193.1; XM_002837147.1.
DR AlphaFoldDB; D5GA41; -.
DR STRING; 656061.D5GA41; -.
DR EnsemblFungi; CAZ81384; CAZ81384; GSTUM_00003554001.
DR GeneID; 9187091; -.
DR KEGG; tml:GSTUM_00003554001; -.
DR eggNOG; KOG2276; Eukaryota.
DR HOGENOM; CLU_008535_1_0_1; -.
DR InParanoid; D5GA41; -.
DR OMA; HATVCVD; -.
DR OrthoDB; 177966at2759; -.
DR Proteomes; UP000006911; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:EnsemblFungi.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0061672; C:glutathione hydrolase complex; IEA:EnsemblFungi.
DR GO; GO:0034399; C:nuclear periphery; IEA:EnsemblFungi.
DR GO; GO:0036374; F:glutathione hydrolase activity; IEA:EnsemblFungi.
DR GO; GO:0042802; F:identical protein binding; IEA:EnsemblFungi.
DR GO; GO:0006751; P:glutathione catabolic process; IEA:EnsemblFungi.
DR CDD; cd05677; M20_dipept_like_DUG2_type; 1.
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; 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; 1.
DR PIRSF; PIRSF037237; Peptidase_WD_repeats_DUG2; 1.
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; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000006911};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW ProRule:PRU00221}.
FT REPEAT 92..133
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT DOMAIN 679..754
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
FT REGION 177..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..194
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 867 AA; 95406 MW; E2E525BDC648F38C CRC64;
MDGLRVLSPN NGSRVGTPLP RFLDSSGFPI NPSAKKEKEG AIEVEVPSLL HRVKHNGSIL
SFCVSDELIY AGSQSGEILV WSIETFQLVK SVHAHQGSVL CLHLSDDQSV LFSSAGDAII
NVWNAKTFEN LYSIYSTFDV GDVFCVVYSS ALQTAYFGAQ NTSIQWYDLK VKDSRPRPTL
TSHPSHRNHR FFDSKGPGGR TTPRPASKVV PPSSRLLEVD PENIVQYAHY GYVYCMLLIT
LPSGWEIKGD GGEMLLSGGG DGVVKLWTIN PVTSAITSAA NLSAGDSGVL SMAVNDTMLY
CGLTDGEICI WDLDTLQLIR SLKTHCDDVL TMSVMGNYIF SGSASGYSRK WNQRFEHMSR
WQSHSGLILA SAATKRHGRL IYITGGNDDC VAIWDTSALE QSESQILKSQ NDQLLCSLSK
LVSFRTVSSD PSYAEDCRRG ATYLKQLFKR YGATATLLPS EEGRNPIVHA RFGGCGTKGR
SKGKTILFYG HYDVIPASES AEAGWQTRPF ELTGMNGYLY GRGVSDNKGP CLAALFAAGE
LVQEQELGAD ITFLIEGEEE SGSRGFADAV RRNKEIIGDV DWILIANSYW LDDDVPCLTY
GLRGVIHATV VVGSDKPDLH SGVEGSRLNR EPTIDLVNLL ARLTSPDGKV LIPGFSEPVR
PITPAEEEMY TAITNTIVNK PDWSHLTAVQ IKDHLMSKWR FPSLTIHNVS VSGPSNAAII
PRVASASISL RIVPDQELSV IKDKLVSYLR SEYSSFNSNN KLDIKIDHEA EPWLGDPEND
AFRTLEEAVM DVWSEGNLDR VRPLYIREGG SIPTARFLEK EFGAPAAHLP CGQASDQAHL
DDERLRLVNL YKSKAILKRV FKELPRK
//
