ID D5GLK9_TUBMM Unreviewed; 552 AA.
AC D5GLK9;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 22-FEB-2023, entry version 47.
DE SubName: Full=(Perigord truffle) hypothetical protein {ECO:0000313|EMBL:CAZ85402.1};
GN ORFNames=GSTUM_00010253001 {ECO:0000313|EMBL:CAZ85402.1};
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:CAZ85402.1, ECO:0000313|Proteomes:UP000006911};
RN [1] {ECO:0000313|EMBL:CAZ85402.1, ECO:0000313|Proteomes:UP000006911}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mel28 {ECO:0000313|EMBL:CAZ85402.1,
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=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; FN430349; CAZ85402.1; -; Genomic_DNA.
DR RefSeq; XP_002841211.1; XM_002841165.1.
DR AlphaFoldDB; D5GLK9; -.
DR STRING; 656061.D5GLK9; -.
DR EnsemblFungi; CAZ85402; CAZ85402; GSTUM_00010253001.
DR GeneID; 9182705; -.
DR KEGG; tml:GSTUM_00010253001; -.
DR eggNOG; KOG1158; Eukaryota.
DR HOGENOM; CLU_001570_17_5_1; -.
DR InParanoid; D5GLK9; -.
DR OMA; LCCGGGC; -.
DR OrthoDB; 9164at2759; -.
DR Proteomes; UP000006911; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR003097; CysJ-like_FAD-binding.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_alpha.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR19384:SF84; METHIONINE SYNTHASE REDUCTASE; 1.
DR PANTHER; PTHR19384; NITRIC OXIDE SYNTHASE-RELATED; 1.
DR Pfam; PF00667; FAD_binding_1; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00371; FPNCR.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 4: Predicted;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000006911}.
FT DOMAIN 141..407
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 552 AA; 61305 MW; FB6CF49198FBF35A CRC64;
MKSPILGIDF TRTGRPRRAS THLLTVGPQN VCDVINDSSA TNLVDSGCCG GGCSRLPPLP
GNSVSLDTRS RTASEFVKAP DNAAFKSLNL RLSPLTSRDR LTGITALPAQ TISIEPADEE
EKHESTVYVH PPKYVTPHPP WAVYSAKIDS TRELTKTGAP KRTYHFDLDV TDYPEEISGV
DFRVGGAIGV VAPNDFKLVA EVFDILGIDE DELDAPIQLS TQGGRWPTIW GKAKERALTT
TLRELMTWTV DIQSYPPTKN LFRLLAEYAK DEAEKTILLY LCSRQGQAAF CELRTGPYIS
LIQLLNAFPS SKPPLDHLLC NLPTLMPRFY SLSSDPRESK SKDRRIIEIA VTIHEHEEGW
RKGSRTGVGS GFFERCARRI IDEGADDIRI PMFRGLMANP LAKQFQADGP MLLIGAGVGI
APFRGFVQRR LQSANCANKV WVIQGVRDSL LDELYSGEWG EHEDKIRSVV QSRVGTGRYV
QEEVYAQADL VWSIVNSLDG RVFVCGSSKG MGEGVHESLV KVVMKKSMLG REQAEEFWEQ
KKEDGQYIAE TW
//
