ID A0A0D0BB57_9AGAR Unreviewed; 2313 AA.
AC A0A0D0BB57;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 13-SEP-2023, entry version 40.
DE RecName: Full=Ras GEF {ECO:0008006|Google:ProtNLM};
GN ORFNames=GYMLUDRAFT_43514 {ECO:0000313|EMBL:KIK60980.1};
OS Collybiopsis luxurians FD-317 M1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Omphalotaceae; Collybiopsis;
OC Collybiopsis luxurians.
OX NCBI_TaxID=944289 {ECO:0000313|EMBL:KIK60980.1, ECO:0000313|Proteomes:UP000053593};
RN [1] {ECO:0000313|EMBL:KIK60980.1, ECO:0000313|Proteomes:UP000053593}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FD-317 M1 {ECO:0000313|EMBL:KIK60980.1,
RC ECO:0000313|Proteomes:UP000053593};
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 (APR-2014) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KN834773; KIK60980.1; -; Genomic_DNA.
DR HOGENOM; CLU_001922_0_0_1; -.
DR OrthoDB; 1359393at2759; -.
DR Proteomes; UP000053593; Unassembled WGS sequence.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProt.
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; cd00821; PH; 1.
DR CDD; cd00159; RhoGAP; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 1.10.840.10; Ras guanine-nucleotide exchange factors catalytic domain; 1.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR Gene3D; 1.20.870.10; Son of sevenless (SoS) protein Chain: S domain 1; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
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 InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR PANTHER; PTHR23176:SF129; RHO GTPASE ACTIVATING PROTEIN AT 16F, ISOFORM E-RELATED; 1.
DR PANTHER; PTHR23176; RHO/RAC/CDC GTPASE-ACTIVATING PROTEIN; 1.
DR Pfam; PF00617; RasGEF; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00147; RasGEF; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF48366; Ras GEF; 2.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50212; RASGEF_NTER; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 4: Predicted;
KW Guanine-nucleotide releasing factor {ECO:0000256|PROSITE-ProRule:PRU00135};
KW Reference proteome {ECO:0000313|Proteomes:UP000053593}.
FT DOMAIN 1352..1508
FT /note="N-terminal Ras-GEF"
FT /evidence="ECO:0000259|PROSITE:PS50212"
FT DOMAIN 2004..2038
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 2077..2271
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 19..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 305..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 598..629
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 722..769
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 828..867
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1266..1346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1528..1565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1901..1942
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2275..2313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..76
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..102
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..129
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..261
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..290
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..331
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 608..629
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1266..1294
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1323..1346
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1528..1551
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1901..1924
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1928..1942
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2276..2302
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2313 AA; 249221 MW; 389216EA911C5EBD CRC64;
MDLPSRNPNS LDLTAALSFN AASQPSSPSS PIHRSTPLGD LRAISRRAWS RSADDLSKIP
PSSSISASTD VSSGPSPPLT MEAKIAQYRN RSNSNSDALL FNSGKGMPSA PPVIQRNHSQ
GQGQGQGQPF PSMAMGGGGG GGLDTSASSS SSSPTPTVSI SISAPAVDDP SPSSSAPSSS
SKPPSSSSAP SSTHVHTRSH SFTPKLASKL SAPRFMPPSP KRKGSAGSEV DGNGSGGGIP
PSPSLPASTS GSTSSSRGGF PFSMGMGSGR SAHTDSSSTT TQLSSSPHRT TTVINSLLAP
PPNIIEASFD SSSSSSMSGP SSAGLGSSPK RSSQIVYNSG FINKFADSSS SGSGHWNGSG
NANAYNNSDM NLSSAKAWKP FKVELKGTKL FFYKPPSDRV GGVKELFPVG LVGPGVGDGE
GEEGEYGEGG ASAGTGTGLA AGAGVGVGTG AGGGEGGEFG SVDGLGVGLG GEDDPFAAAS
NTRMVVDIRA RRESSTLLAV QRKKRAFWGR RTHPDLVRDL EGGKGIEKGT FEALTHEAVF
GTIFFGGGGG EGEGDPMEQW KAFASSVLLS LPHLVDQGKF EAELMRCCEF LVTGAPEPEV
EPEVQSEVDG EGEGKTEGEG EGEGKMVKRG EEEKKRVVWL VKEYLGYHGR VLEFPDWPEW
KEMAGDAGLG PNSTSLSSSS SVASPHVSMF SPRPEDVNKV SLFDVFGEST TGTGVGVGVG
AGVGTPPSTK PGPGPSPIAT PTSYFDLNPK SPGQHRNTPP PHLSPSASSS GMMIPWASAL
DREGLSRDVL LLIDPHVIAR SLSAFHVAAV QQLPEQLTAE FVLRGGEQQQ TQTQTQTHLH
QSQYSNPHQH QYPSQSQYHQ GTTLISPTSN SLASSSFAPL FGSDDHPHWL TKLLLVQILG
ADTSTGYANV SNRNPGLGTS GIGGGGVGGI VTPAGITTVA AGASRRSDDR GAGMSAATSR
THSRSEVISA WIKIGEVCRL NGDECSWRAI VGAICSMPVA RLEKAWKRVE PQAVGVVEGW
VQLVKGSGDG VALAGEGIKE PRITPWGGNM RGLIREELGR AMVPGASGDV LVVRALDRVR
VLFEGFRTAV SSCPRSNVNA VGGGSGGFAE EKGKGKEEEV QKLVSYWKDI VADGGMGGGL
AMKFQRVDQF MSLSLAAEPK RKGLYEPFYW TKAGGHSSST APLLPLLFPE PLPTITLLDR
SQLARGRVDS EPADIQHLRA IDGHLRPEDR KPISGADGAF AVLNHGGTTI PVYNGDLLLV
VQNSSVESSS TGGSRPSSLV RSRPPSSADM DTSFLDGNKS EKPVGRTPSI RVKPGSSAGL
ERKSSVAKRS SLPSLSQRQP LTLAENSSEP PLRVLVRAGT LDRLVYVLVH GLHSVSVSVA
DDNGEMSLRV GMTRELLLDH KEFSRVWWNV FRSFVTPLIF FELLRKNYIK SQPSGSPPLP
DQYLSTISSK SQVLETIKIW LTKGGGAQDV LDDPQLFQAL RAFFASSSDH IIHSSPATFE
DSDVRQAWDA LTESRQAVER LLRTQTMRPS NSRTMPVSRN TVTTSESRVR NLSTREPPDI
DRMSPEEFVD NIDGMAFAAF NNVTEEDLYI TSDLLEVQTA DRIGWFPQRE APTLEDHVEI
QTIHSYMQEV EPSSLISELS PESLYRLLPP GIRSCIRAHS ILRKWIISKV VAPRLGLYTR
QARLEFLLQV IEVTRLRNAE PSSFSSVSEQ ACVRSFVEAT VTSAILSPEC RLHQRAWQNI
AASRGCNFET LAQLLARPNT KSVVSKDPLT VDMGWLIERI LDVIAMPDLV ESHSDEGQNL
VNFDKRRNLC NFISNAPSLL TRRLARQSDI NRRGFERLNN IEREIFPIQF DLRGIKDEAY
RESTAAGSAG TPSRNRISRP FQKLIALQLD KQRRDKNLRV RLQKEKMQEQ SRNEKREEQL
NRAMRGGRRP TSVSQKQHRN KKSMSALFSF MRPISSAFGA DTSHTPTLKR TASELDFVPS
GKPTLVLNLT DSHVAHFINN DRSFTFQLDT EDGGHYLLQA MSKRDMNKWI EILSQVSKTA
AKRRLTYIGN SPKPQVADHL HDHPATATKD PTAVFGVELN FLLQRESGGN PVSPGTIPSV
VERCIAEVET RGLTEVGIYR MAGASSEIAY LKEAFNRGED PLDVSTDIHA ICDLVKSWFR
ILPEPLFPPS SYHEAIDTMK LENLDDRLTN IRKIIHNLPR ANFDLLKRIS EHLDKVTDFE
EQNQMTAEAL SIVFSPNLLR APQNDFLMVL SNMPFAHKLV KTLITHYHVL FDESDADAEA
DPEDELDSPI AEANEDDEEA EGAFTNYLPT SPS
//
