ID   D5G761_TUBMM            Unreviewed;       167 AA.
AC   D5G761;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   SubName: Full=(Perigord truffle) hypothetical protein {ECO:0000313|EMBL:CAZ80354.1};
GN   ORFNames=GSTUM_00002356001 {ECO:0000313|EMBL:CAZ80354.1};
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:CAZ80354.1, ECO:0000313|Proteomes:UP000006911};
RN   [1] {ECO:0000313|EMBL:CAZ80354.1, ECO:0000313|Proteomes:UP000006911}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mel28 {ECO:0000313|EMBL:CAZ80354.1,
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
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DR   EMBL; FN430021; CAZ80354.1; -; Genomic_DNA.
DR   RefSeq; XP_002836163.1; XM_002836117.1.
DR   AlphaFoldDB; D5G761; -.
DR   STRING; 656061.D5G761; -.
DR   EnsemblFungi; CAZ80354; CAZ80354; GSTUM_00002356001.
DR   GeneID; 9185252; -.
DR   KEGG; tml:GSTUM_00002356001; -.
DR   eggNOG; KOG2839; Eukaryota.
DR   HOGENOM; CLU_037162_5_3_1; -.
DR   InParanoid; D5G761; -.
DR   OMA; EDQWPEM; -.
DR   OrthoDB; 3035837at2759; -.
DR   Proteomes; UP000006911; Unassembled WGS sequence.
DR   GO; GO:0034431; F:bis(5'-adenosyl)-hexaphosphatase activity; IEA:EnsemblFungi.
DR   GO; GO:0034432; F:bis(5'-adenosyl)-pentaphosphatase activity; IEA:EnsemblFungi.
DR   GO; GO:0008486; F:diphosphoinositol-polyphosphate diphosphatase activity; IEA:EnsemblFungi.
DR   GO; GO:0000298; F:endopolyphosphatase activity; IEA:EnsemblFungi.
DR   GO; GO:0052745; F:inositol phosphate phosphatase activity; IEA:EnsemblFungi.
DR   GO; GO:1990174; F:phosphodiesterase decapping endonuclease activity; IEA:EnsemblFungi.
DR   GO; GO:1901911; P:adenosine 5'-(hexahydrogen pentaphosphate) catabolic process; IEA:EnsemblFungi.
DR   GO; GO:1901909; P:diadenosine hexaphosphate catabolic process; IEA:EnsemblFungi.
DR   GO; GO:1901907; P:diadenosine pentaphosphate catabolic process; IEA:EnsemblFungi.
DR   GO; GO:0071545; P:inositol phosphate catabolic process; IEA:EnsemblFungi.
DR   GO; GO:0006798; P:polyphosphate catabolic process; IEA:EnsemblFungi.
DR   CDD; cd04666; Nudix_Hydrolase_9; 1.
DR   Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 1.
DR   InterPro; IPR047198; DDP-like_NUDIX.
DR   InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR   InterPro; IPR000086; NUDIX_hydrolase_dom.
DR   PANTHER; PTHR12629:SF0; APS, ISOFORM A; 1.
DR   PANTHER; PTHR12629; DIPHOSPHOINOSITOL POLYPHOSPHATE PHOSPHOHYDROLASE; 1.
DR   Pfam; PF00293; NUDIX; 1.
DR   SUPFAM; SSF55811; Nudix; 1.
DR   PROSITE; PS51462; NUDIX; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006911}.
FT   DOMAIN          22..161
FT                   /note="Nudix hydrolase"
FT                   /evidence="ECO:0000259|PROSITE:PS51462"
FT   REGION          53..72
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   167 AA;  19343 MW;  7893BB998D29F3DC CRC64;
     MAQSRSMEAR VGRVKQRYAS DGSRLVAGVV AISIDRRKVL VVESTNRDNH WVLPKGGYET
     DEPTPEDAAS REAWEEAGIT GKITRNLGEI RDPRPQNVLD AAKSNSKIPP CALYYFFEFK
     VEKEEALWPE MHKRRRRWMT YEEASQCFRE MDRPELLEAI ERSSILR
//