ID D5GF01_TUBMM Unreviewed; 1595 AA.
AC D5GF01;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE SubName: Full=(Perigord truffle) hypothetical protein {ECO:0000313|EMBL:CAZ83094.1};
GN ORFNames=GSTUM_00006678001 {ECO:0000313|EMBL:CAZ83094.1};
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:CAZ83094.1, ECO:0000313|Proteomes:UP000006911};
RN [1] {ECO:0000313|EMBL:CAZ83094.1, ECO:0000313|Proteomes:UP000006911}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mel28 {ECO:0000313|EMBL:CAZ83094.1,
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; CAZ83094.1; -; Genomic_DNA.
DR RefSeq; XP_002838903.1; XM_002838857.1.
DR STRING; 656061.D5GF01; -.
DR EnsemblFungi; CAZ83094; CAZ83094; GSTUM_00006678001.
DR GeneID; 9188632; -.
DR KEGG; tml:GSTUM_00006678001; -.
DR eggNOG; KOG3417; Eukaryota.
DR HOGENOM; CLU_001471_0_0_1; -.
DR InParanoid; D5GF01; -.
DR OMA; ICNYATM; -.
DR OrthoDB; 5476208at2759; -.
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; cd06224; REM; 1.
DR Gene3D; 1.10.840.10; Ras guanine-nucleotide exchange factors catalytic domain; 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; IPR023578; Ras_GEF_dom_sf.
DR InterPro; IPR001895; RASGEF_cat_dom.
DR InterPro; IPR036964; RASGEF_cat_dom_sf.
DR PANTHER; PTHR23113; GUANINE NUCLEOTIDE EXCHANGE FACTOR; 1.
DR PANTHER; PTHR23113:SF364; GUANINE NUCLEOTIDE EXCHANGE FACTOR LTE1; 1.
DR Pfam; PF00617; RasGEF; 1.
DR Pfam; PF00618; RasGEF_N; 1.
DR SMART; SM00147; RasGEF; 1.
DR SMART; SM00229; RasGEFN; 1.
DR SUPFAM; SSF48366; Ras GEF; 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}.
FT DOMAIN 273..399
FT /note="N-terminal Ras-GEF"
FT /evidence="ECO:0000259|PROSITE:PS50212"
FT DOMAIN 1348..1592
FT /note="Ras-GEF"
FT /evidence="ECO:0000259|PROSITE:PS50009"
FT REGION 14..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 209..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 508..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 667..706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 764..822
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 852..880
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1258..1330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..538
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 684..706
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1273..1291
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1595 AA; 174626 MW; 6CF0063E97C0141F CRC64;
MFAETLSLYR PVVRSARDIQ QFTLPPTTPP SSAEEPEGKP WQQDRRESGG RPSGKQLPLT
PPPKTPPRKR SVLSDGDALD FYMKSSPPIP RTRHRRACSC STVGENVTPY KPPDHGAFRM
KVEQVDGPSQ ERPRPRTSGH QETCRALDVQ IPDYSLGSPH FSPNGTPFLY GASSLHVPSI
QVERGSSPSL SLQADLRWLW PGADARSSTP SLVPNREASP LPSEQLPGGQ IQHAASSLSL
AGMSRLRISP EMYDILSFPP SSEDPSIVRY DKRTQEITAA VPARIISQIT SAEFVDYHLL
SDFFLTFRLF MQPPDLVAYL VARLRWAIDR EDDIGRVVRV RTFVAIRHWL LNYFADDFIP
SLPLREDFAK TLNNLSNAVR ENGQPSNMKI IRELKRCWRR TCALYWDTPT GPDVSIDQDI
LPGGPPGSRF DSYRPLSTLL HPKKSAPRLG ALFPDRDTGT EAFVQEVVGA SVAARATGGT
PLRSFSRPVS NFSNDSAKTP SLSYFSLENR SKSTPAPSTS SPLKPKPSQA TISSDEAGST
EEGGKKYRPT PHKRSGSFSD ALRDTRQPLP LPKSIARSTH LLMALPYAGS LVRGNLFPPT
PAYVQVVAPS TPVSELSSYG FLAPSDAAGG SVATQFARRT FDPNQGNKTL NGPGMKRFLG
SVRRALSGKV GNGAGPHGSG GGGSTRSPLP TARPTRSRSL GPTPDNLSLS KFMAASSSGN
KVAILENGKA ARVDLLGAGV VEAFQRAMQE ELSSDDGEWI SYNVTQGEGE EGGPWHKNQF
QLDRTGDGGL PLEVGRENAL SEDESNAPEP SENPPPSTAR QPGLRETFEQ IPNFGLAESV
ISEIANMGEA GSISDRKNLP DRGPKSSIFP GESQQARRSK SFSFETTPHL LSQHYEGMCR
KLSVSPRPGP GGKSLRPARS FSVRRVQSGV SQFSSNLDDN SETFSYISSP ESKRGNLQPA
RMLRRRPGGD LRLAATVGDL DGRPRSAGSI WTGNFSDMGA NGTPLQQRPN SICVTESIHP
QQRVPAGCSE ADAKASFEAG VQKLRDLPDF ESDDGGIEVA LMKLEGTYQK RASDISPGKE
RNPTMSFASG RSFISQDSLV IVGDAHSERT FGMDASVDDD EYMRRMKRRH KQVFDHVPLD
TPPILEGGSA GNSSTNLSTN GAVFRDESEA SGPNLERGLS VNHWNFRETV TSSNLSLPPL
ERGMSSGSSP IHRGFSEQLR DDISELSSEI SFEMVQSANK SATKFPPMQP GTIIAELGIP
SHPLRHPPSP PLTLEKTLST SPNNASPSAV RRPRSPVSPP QAETFPGSRA PGRASQDALL
GGNGPHYNDT KPTLRPTSIH LPFILAYDSE LLAKQFTLIE KDALMEVDWK ELVELKWSQT
SPAVRDWVEF LSSEGTRGVE VVIARFNLMC KWARSEIVMT KDINERAKTV VKFIHIAAHA
RRLQNFATMY QITIALLTAD VTRLRQTWSL ISPADLSTFK EMEALVQPIR NFHNLRAEMD
KVTGESGCIP FVGIFTHDLI QNAQRPLTIS TSPDSEPLIN FERHRTTASI VKRLLRLIEA
SHKYDFKAVD GVCERCLWIA SLMDEEIRDL SKSLQ
//
