ID D5GGU1_TUBMM Unreviewed; 415 AA.
AC D5GGU1;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 24-JAN-2024, entry version 57.
DE SubName: Full=(Perigord truffle) hypothetical protein {ECO:0000313|EMBL:CAZ83713.1};
GN ORFNames=GSTUM_00007513001 {ECO:0000313|EMBL:CAZ83713.1};
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:CAZ83713.1, ECO:0000313|Proteomes:UP000006911};
RN [1] {ECO:0000313|EMBL:CAZ83713.1, ECO:0000313|Proteomes:UP000006911}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mel28 {ECO:0000313|EMBL:CAZ83713.1,
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 -!- SIMILARITY: Belongs to the peptidase C14B family.
CC {ECO:0000256|ARBA:ARBA00009005}.
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DR EMBL; FN430275; CAZ83713.1; -; Genomic_DNA.
DR RefSeq; XP_002839522.1; XM_002839476.1.
DR AlphaFoldDB; D5GGU1; -.
DR STRING; 656061.D5GGU1; -.
DR EnsemblFungi; CAZ83713; CAZ83713; GSTUM_00007513001.
DR GeneID; 9181683; -.
DR KEGG; tml:GSTUM_00007513001; -.
DR eggNOG; KOG1546; Eukaryota.
DR HOGENOM; CLU_029389_0_2_1; -.
DR InParanoid; D5GGU1; -.
DR OMA; MHRIMVT; -.
DR OrthoDB; 1077459at2759; -.
DR Proteomes; UP000006911; Unassembled WGS sequence.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.40.50.12660; -; 1.
DR InterPro; IPR029030; Caspase-like_dom_sf.
DR InterPro; IPR011600; Pept_C14_caspase.
DR PANTHER; PTHR48104:SF30; METACASPASE-1; 1.
DR PANTHER; PTHR48104; METACASPASE-4; 1.
DR Pfam; PF00656; Peptidase_C14; 1.
DR SUPFAM; SSF52129; Caspase-like; 1.
PE 3: Inferred from homology;
KW Apoptosis {ECO:0000256|ARBA:ARBA00022703};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022807};
KW Protease {ECO:0000256|ARBA:ARBA00022807};
KW Reference proteome {ECO:0000313|Proteomes:UP000006911};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT DOMAIN 121..405
FT /note="Peptidase C14 caspase"
FT /evidence="ECO:0000259|Pfam:PF00656"
FT REGION 1..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 324..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..49
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..70
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..356
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 415 AA; 45947 MW; 85F16F58A334B723 CRC64;
MSGYNQYPGY NPYPGQQYGD QQQQPYYPPP SPQPPAGYYP PPPQQGFGYP AQPQQPQWTP
QPTSQYHGAI PPQGNHMPTG QYMYSHPPPA GAPNLPPQGV QSFHVPGAPQ IGYEFSNCTG
KRKALLIGIN YFGQRGQLRG CINDVKNMST FLHDRFSYKR EDMVILTDDQ QNPRSQPTKQ
NILQAMHWLV KDAQPNDSLF FHYSGHGGQT KDLDGDEGDG YDETIYPVDF RYNGHIVDDD
MHRIMVAPLK PGVRLTAIFD SCHSGSALDL PYLYSTRGVE KEPNIAKEAA TGLFDAMSAY
SRGDLGSVAQ SAMGIFKRAT TGRGAEERAK RTKTSAADVI QWSGSKDSQT SADATEGGEA
TGAMSYAFIR ALSKNSQQSY QQLLNSIREE LQGKYSQKPQ LSCSHPLDTR LLYVM
//
