ID A0A0C3ECZ0_9AGAM Unreviewed; 1077 AA.
AC A0A0C3ECZ0;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=Ras GEF {ECO:0008006|Google:ProtNLM};
GN ORFNames=SCLCIDRAFT_1211413 {ECO:0000313|EMBL:KIM66184.1};
OS Scleroderma citrinum Foug A.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Sclerodermatineae; Sclerodermataceae;
OC Scleroderma.
OX NCBI_TaxID=1036808 {ECO:0000313|EMBL:KIM66184.1, ECO:0000313|Proteomes:UP000053989};
RN [1] {ECO:0000313|EMBL:KIM66184.1, ECO:0000313|Proteomes:UP000053989}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Foug A {ECO:0000313|EMBL:KIM66184.1,
RC ECO:0000313|Proteomes:UP000053989};
RG DOE Joint Genome Institute;
RA Kuo A., Kohler A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA Hua S.X.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000053989}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Foug A {ECO:0000313|Proteomes:UP000053989};
RG DOE Joint Genome Institute;
RG Mycorrhizal Genomics Consortium;
RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KN822018; KIM66184.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C3ECZ0; -.
DR STRING; 1036808.A0A0C3ECZ0; -.
DR HOGENOM; CLU_005431_0_0_1; -.
DR InParanoid; A0A0C3ECZ0; -.
DR OrthoDB; 4819765at2759; -.
DR Proteomes; UP000053989; 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; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; IPR027417; P-loop_NTPase.
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:SF348; GUANYL-NUCLEOTIDE EXCHANGE FACTOR RASGEF, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G04700)-RELATED; 1.
DR Pfam; PF00617; RasGEF; 1.
DR Pfam; PF00618; RasGEF_N; 1.
DR SMART; SM00147; RasGEF; 1.
DR SMART; SM00229; RasGEFN; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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:UP000053989}.
FT DOMAIN 572..697
FT /note="N-terminal Ras-GEF"
FT /evidence="ECO:0000259|PROSITE:PS50212"
FT DOMAIN 806..1035
FT /note="Ras-GEF"
FT /evidence="ECO:0000259|PROSITE:PS50009"
FT REGION 1..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 458..574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 742..763
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..121
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..137
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..195
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..491
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..530
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..552
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 557..574
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1077 AA; 119497 MW; D5B5EA20ED86B9CC CRC64;
MTTEPTSSSH SLPAIPTLPP IYIPGHDDDL NASSSPRLPP VTFSPQEPTS LTTSSPILTR
KPSFTIRSSS AGSPLQHLRR SASVDSLPIR QPGDSSRSSS PTGARSTIST NTDSSHTRWP
ELSVGSRRRR EPETIPPYAR SRGHSVSTMS DGHDSAFEQD FESDSWRPLK RPVDKPRRTS
VKGSEQARPS RRPGDLKLPS RNQPPPALFN QFAHPLPRDD TRRLHSTTSL QSFPKHSSLT
DVMSGRVRSG SLGLQADPSS LGSRSLLIDV VQPKPSPREF SVAVVGTPGC GKSTFIAEDA
RAQGARNISA LSMPGNPPPR FRYTRKVDSS MLIVHEFDIT TITTPPLVDG IIVCYDYGDA
SSFSPIPNFL QLISAMKCSK ITVALKSDLE AAIDPKEVIG LLDKYHVGLV LVDNSGDAGR
MKMRKVFNFF FKSLQAPNAN LRNPASPEAA TAPVLWESRG SVSGSQSPSP VISTDTTSQD
HANSLRLSST PTLPTSPPPS NSPSRARSTS DLHLEREKIK TRESEDRKLS NARSINNLPS
ASSFQSGPPL LLQPELTNGH EDEERRLSKE KETRSAQYAT LEELLDKLLF LAVSGDDPTF
ISHFLLTYRR FAMPRSILLA MQKRMRQLDN SLGDPMLASF AQMRICHLLE TWMHNYPQDF
AVPGAAGALN AIVNSLVNKT YLLHYGCDFK PFLEYISNLV DTDATWAQKT EPLLDENEDP
YLFSDGEDLS FVATTVGSAS ASRSSVAPSN ENAVSSSSRE RKQSLPLSAK ALIMPTSAQM
ADVPEVPPKQ LLKELSKQAQ ELQTYDCAEI AEEITRNEAV LFMEIQPRHW LRYAFVPGRK
DPESDTIARF NAMSNYLADW VASLILCHDK PKNRARQIEK FVGIAHKLRA LNNYSALRAF
VAGINTSTFQ GDETMEQFKT KAPDHYKNLL SWDVLLQHRG AHQAYRMALK NTKGACIPAL
EVHISDLIRA HEGNPDFSPS EPNKIHWGKF NMLGRFIQTT MQCQIQCQTT SDYNFLERHK
IRDLVFSESI MSEGMQVSRM APVPESILDE PLKPTLPRTF PRDDTHLTQG FRRIFQR
//
