ID D5GHC4_TUBMM Unreviewed; 1063 AA.
AC D5GHC4;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 22-FEB-2023, entry version 71.
DE SubName: Full=(Perigord truffle) hypothetical protein {ECO:0000313|EMBL:CAZ83876.1};
GN ORFNames=GSTUM_00007746001 {ECO:0000313|EMBL:CAZ83876.1};
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:CAZ83876.1, ECO:0000313|Proteomes:UP000006911};
RN [1] {ECO:0000313|EMBL:CAZ83876.1, ECO:0000313|Proteomes:UP000006911}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mel28 {ECO:0000313|EMBL:CAZ83876.1,
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; FN430308; CAZ83876.1; -; Genomic_DNA.
DR RefSeq; XP_002839685.1; XM_002839639.1.
DR AlphaFoldDB; D5GHC4; -.
DR STRING; 656061.D5GHC4; -.
DR EnsemblFungi; CAZ83876; CAZ83876; GSTUM_00007746001.
DR GeneID; 9182581; -.
DR KEGG; tml:GSTUM_00007746001; -.
DR eggNOG; KOG3417; Eukaryota.
DR HOGENOM; CLU_002632_0_0_1; -.
DR InParanoid; D5GHC4; -.
DR OMA; DWPGPDS; -.
DR OrthoDB; 68574at2759; -.
DR Proteomes; UP000006911; Unassembled WGS sequence.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR CDD; cd00155; RasGEF; 1.
DR CDD; cd06224; REM; 1.
DR CDD; cd00201; WW; 1.
DR Gene3D; 2.20.70.10; -; 1.
DR Gene3D; 1.10.840.10; Ras guanine-nucleotide exchange factors catalytic domain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR Gene3D; 1.20.870.10; Son of sevenless (SoS) protein Chain: S domain 1; 1.
DR InterPro; IPR008937; Ras-like_GEF.
DR InterPro; IPR000651; Ras-like_Gua-exchang_fac_N.
DR InterPro; IPR019804; Ras_G-nucl-exch_fac_CS.
DR InterPro; IPR023578; Ras_GEF_dom_sf.
DR InterPro; IPR001895; RASGEF_cat_dom.
DR InterPro; IPR036964; RASGEF_cat_dom_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR001202; WW_dom.
DR PANTHER; PTHR23113; GUANINE NUCLEOTIDE EXCHANGE FACTOR; 1.
DR PANTHER; PTHR23113:SF341; PROTEIN SON OF SEVENLESS; 1.
DR Pfam; PF00617; RasGEF; 1.
DR Pfam; PF00618; RasGEF_N; 1.
DR Pfam; PF00018; SH3_1; 1.
DR SMART; SM00147; RasGEF; 1.
DR SMART; SM00229; RasGEFN; 1.
DR SUPFAM; SSF48366; Ras GEF; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS00720; RASGEF; 1.
DR PROSITE; PS50009; RASGEF_CAT; 1.
DR PROSITE; PS50212; RASGEF_NTER; 1.
PE 4: Predicted;
KW Guanine-nucleotide releasing factor {ECO:0000256|ARBA:ARBA00022658,
KW ECO:0000256|PROSITE-ProRule:PRU00168};
KW Reference proteome {ECO:0000313|Proteomes:UP000006911};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443}.
FT DOMAIN 643..776
FT /note="N-terminal Ras-GEF"
FT /evidence="ECO:0000259|PROSITE:PS50212"
FT DOMAIN 811..1049
FT /note="Ras-GEF"
FT /evidence="ECO:0000259|PROSITE:PS50009"
FT REGION 81..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 175..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 550..627
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..97
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..573
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 580..601
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1063 AA; 118588 MW; F0C6497FEBD2FF6C CRC64;
MYVRALYNYA SEDPTSLSFS QGDVIQVITQ LESGEGGFQA IINEMVWLRR ADDEAAFWIP
QATPDGRLYY FNMITGVTRT ELPLETPTST TESGPRDRLN FSAPEQTRPP PELMARGYER
EEPAYRDLGD DDVESASDKE GEMLVLSMHS PSRVADKTLV DRESQATLVD SVSTSIDATR
GPNGSFQPGH SRSLSVSTTA TAVNLNAGSP TINTKSTPSA YHDNGMPVPS SWDELIDNTR
LAVERYRQAV NTFDRAQYVA RAEDVSDMLR LLIAAGSATT DNHSGQPSII ISNKALNPHY
RHFMAAFSKL VLSSHVAATD CPPADAESKC LGEADEVMIG VFGFADVARA QRGEKLPRLK
PGFVYGSHAG GGWKGVGKAV VSSKISGAAA LSPAEDPLLP LTPNLIERME EVYGIVKPAL
KRLESTLENT ETVVSEYEQE IIGARVISAA QGAFDAIKRY FNLIESINMS PLSATPQHPT
LVDFSTQKQR LHDSFAELFL SCQAVTAPLA DEWAALRGEP LEERLNSVRI YVKEIESGIS
SLNFSTQLLV EERQEREPNK DIRTEDLRKP DASPIDQASR TPGPLHQRTG SRQTSRVTSS
MDRGIRPGGG GGSKAARVFG EEPPPETPSY LNCDYDSEII YGARNKVKGG TLVALVERVT
RHDMLDSNFI STFLLTYRSF TTASELFKQL VRRFTVQPPS ALSGSEFEIW TEKKQKLIRV
RVLSILKMWL EQNWMEGLDD NAKDLLKKMY LFAKDVMLPQ LSGTSQVLSL IETRLRGQEP
EMKRLILNMV VQPPPPIMPK HMKKLKFLDI DALEFARQLT IIESKSYGKL KAAECLSKGW
SKQPSSGGPD PAENIRAIIM QSNRLTNWVA EMILTQTEVR KRVVVIKHFI AVAEKCRLLN
NFSTLTAILA ALQTSSIHRL KRTWEHVPSR TNQTLEGMNT LMGATMNFAE YREMLHIVNP
PCVPFLGVYL KDLTFVADGN DDFIKGDQKL INFDKRVKTA NIIREIQQYQ SVPYPLQPVP
ELQDYIISNM QSARDVNDMY NLSLSLEPRE REDEKIARYF DFL
//