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Database: UniProt
Entry: D5GEX1_TUBMM
LinkDB: D5GEX1_TUBMM
Original site: D5GEX1_TUBMM 
ID   D5GEX1_TUBMM            Unreviewed;       431 AA.
AC   D5GEX1;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   03-MAY-2023, entry version 47.
DE   SubName: Full=(Perigord truffle) hypothetical protein {ECO:0000313|EMBL:CAZ83064.1};
GN   ORFNames=GSTUM_00006628001 {ECO:0000313|EMBL:CAZ83064.1};
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:CAZ83064.1, ECO:0000313|Proteomes:UP000006911};
RN   [1] {ECO:0000313|EMBL:CAZ83064.1, ECO:0000313|Proteomes:UP000006911}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mel28 {ECO:0000313|EMBL:CAZ83064.1,
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; FN430197; CAZ83064.1; -; Genomic_DNA.
DR   RefSeq; XP_002838873.1; XM_002838827.1.
DR   AlphaFoldDB; D5GEX1; -.
DR   STRING; 656061.D5GEX1; -.
DR   EnsemblFungi; CAZ83064; CAZ83064; GSTUM_00006628001.
DR   GeneID; 9188602; -.
DR   KEGG; tml:GSTUM_00006628001; -.
DR   eggNOG; ENOG502QUQ4; Eukaryota.
DR   HOGENOM; CLU_026011_0_0_1; -.
DR   InParanoid; D5GEX1; -.
DR   OMA; WHITSAF; -.
DR   OrthoDB; 325143at2759; -.
DR   Proteomes; UP000006911; Unassembled WGS sequence.
DR   GO; GO:0051213; F:dioxygenase activity; IEA:InterPro.
DR   GO; GO:0006307; P:DNA dealkylation involved in DNA repair; IEA:InterPro.
DR   GO; GO:0035552; P:oxidative single-stranded DNA demethylation; IEA:InterPro.
DR   Gene3D; 2.60.120.590; Alpha-ketoglutarate-dependent dioxygenase AlkB-like; 1.
DR   InterPro; IPR027450; AlkB-like.
DR   InterPro; IPR037151; AlkB-like_sf.
DR   InterPro; IPR032854; ALKBH3.
DR   InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR   PANTHER; PTHR31212; ALPHA-KETOGLUTARATE-DEPENDENT DIOXYGENASE ALKB HOMOLOG 3; 1.
DR   PANTHER; PTHR31212:SF4; ALPHA-KETOGLUTARATE-DEPENDENT DIOXYGENASE ALKB HOMOLOG 3; 1.
DR   Pfam; PF13532; 2OG-FeII_Oxy_2; 1.
DR   SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR   PROSITE; PS51471; FE2OG_OXY; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000006911}.
FT   DOMAIN          252..359
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
FT   REGION          1..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          121..142
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..30
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        121..140
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   431 AA;  46805 MW;  00097635CB771DCF CRC64;
     MPPSRKKLKK PLDPSFFEPK SQRDRRGSAE NSATARAAAG GCSTAKYVSE EGDEQLDTDT
     KIAILASLHP SLSTAALIDI LLSVNGSIEA TSKLLAAGQT TPQARKPPST TNQSSLETFI
     STQGTSTTTS TTTSTPKPPP KGQTLHLYTP ASIALHTPCV LHTTFLPPPL ATTLLQELLH
     ESTTFPPPGK FNLFSRTVQS PHRSVMYTTT PATTPYYYQG LTLPPPRAFT PSMSTAAGLV
     EEHFRTLEPR GRITAALVNC YAGPQQGVGF HTDALTYIGP RAIICTLSLG VTREFRIQKQ
     PPSSHSLGTY AIHLPHNSLL VMTAGMQENW KHSIPLVQRV DRHEISGDIR IAITFRWYRD
     DYGPEVTPAC GCGGRMVLRP VWGGEKYFWS CDGEYRGVGQ GCGYFKWAVF GEGGRPVFED
     EKGKVVEGGD G
//
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