ID   D5GG75_TUBMM            Unreviewed;       593 AA.
AC   D5GG75;
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:CAZ83518.1};
GN   ORFNames=GSTUM_00007245001 {ECO:0000313|EMBL:CAZ83518.1};
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:CAZ83518.1, ECO:0000313|Proteomes:UP000006911};
RN   [1] {ECO:0000313|EMBL:CAZ83518.1, ECO:0000313|Proteomes:UP000006911}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mel28 {ECO:0000313|EMBL:CAZ83518.1,
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).
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DR   EMBL; FN430242; CAZ83518.1; -; Genomic_DNA.
DR   RefSeq; XP_002839327.1; XM_002839281.1.
DR   AlphaFoldDB; D5GG75; -.
DR   STRING; 656061.D5GG75; -.
DR   EnsemblFungi; CAZ83518; CAZ83518; GSTUM_00007245001.
DR   GeneID; 9184580; -.
DR   KEGG; tml:GSTUM_00007245001; -.
DR   eggNOG; KOG2386; Eukaryota.
DR   HOGENOM; CLU_013931_1_0_1; -.
DR   InParanoid; D5GG75; -.
DR   OMA; PGIRHGH; -.
DR   OrthoDB; 49440at2759; -.
DR   Proteomes; UP000006911; Unassembled WGS sequence.
DR   GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   CDD; cd14502; RNA_5'-triphosphatase; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR000387; Tyr_Pase_dom.
DR   PANTHER; PTHR43798; MONOACYLGLYCEROL LIPASE; 1.
DR   PANTHER; PTHR43798:SF5; MONOACYLGLYCEROL LIPASE ABHD6; 1.
DR   Pfam; PF12697; Abhydrolase_6; 1.
DR   Pfam; PF00782; DSPc; 1.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000006911}.
FT   DOMAIN          507..567
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          25..53
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          325..351
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        325..350
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   593 AA;  65922 MW;  36A7491E010F5FD1 CRC64;
     MVGAVLCGIP LVYVGLRSLR ERRSKEEEVR SLKGAPDDGH SVHSNYESLS NASSSVSDSS
     LLRKHSENIS VTTKHYTYPA VRVFYRPHPK ASVLPPKLPL LVFLHGLGGQ MSQFQYLLEF
     FVHISHTLAI DLPGCGPSSE FSPKDWDAYT TSRLVELIAE VVNQKLEDGQ QVVLLGHSMG
     CSLAVTLIAE GGLLADRCAG LIAICPKATV SEKELKTLKT ALAFPEFMFD LFRIYDGRGG
     TTSNSVTRFV GSNSTEKVRK LQLRFNKESR TPVWRRMVNG IRLPTEEEWT SVKCPTYLLA
     ASEDKVCATK EVDLIHSWFD PAKRGGSVST TSMGGSADST PSSSLSPSPA RTRPVVKKCI
     IPDAGHGVMY ETPQVVSGLI GDFLSEYVTE VLSLGWQLLY LKEDKWLLKN LEKWTRIQSV
     SPRIGGYIDG SGGPYVKSPF RAMKTLRQND PSGHNPVEFS GKWPDVKDAI DISHEQPPYD
     PETLGDGVRY HKFPTVSKIP PTQDEVASFI ELVDSIRKER GYNDNITIAC HCHYGFNRTG
     FFVCCYLIQR LGFNVEQAIK AFKDARPPGI RHPHFINELF ERHCLGLVRA PTF
//