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Database: UniProt
Entry: G3JD62_CORMM
LinkDB: G3JD62_CORMM
Original site: G3JD62_CORMM 
ID   G3JD62_CORMM            Unreviewed;       838 AA.
AC   G3JD62;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   SubName: Full=Rho-GTPase-activating protein 8 {ECO:0000313|EMBL:EGX92537.1};
GN   ORFNames=CCM_03910 {ECO:0000313|EMBL:EGX92537.1};
OS   Cordyceps militaris (strain CM01) (Caterpillar fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Cordycipitaceae; Cordyceps.
OX   NCBI_TaxID=983644 {ECO:0000313|EMBL:EGX92537.1, ECO:0000313|Proteomes:UP000001610};
RN   [1] {ECO:0000313|EMBL:EGX92537.1, ECO:0000313|Proteomes:UP000001610}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CM01 {ECO:0000313|EMBL:EGX92537.1,
RC   ECO:0000313|Proteomes:UP000001610};
RX   PubMed=22112802; DOI=10.1186/gb-2011-12-11-r116;
RA   Zheng P., Xia Y., Xiao G., Xiong C., Hu X., Zhang S., Zheng H., Huang Y.,
RA   Zhou Y., Wang S., Zhao G.P., Liu X., St Leger R.J., Wang C.;
RT   "Genome sequence of the insect pathogenic fungus Cordyceps militaris, a
RT   valued traditional Chinese medicine.";
RL   Genome Biol. 12:RESEARCH116.1-RESEARCH116.21(2011).
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DR   EMBL; JH126401; EGX92537.1; -; Genomic_DNA.
DR   RefSeq; XP_006669121.1; XM_006669058.1.
DR   AlphaFoldDB; G3JD62; -.
DR   STRING; 983644.G3JD62; -.
DR   GeneID; 18165933; -.
DR   KEGG; cmt:CCM_03910; -.
DR   VEuPathDB; FungiDB:CCM_03910; -.
DR   eggNOG; ENOG502QQWB; Eukaryota.
DR   HOGENOM; CLU_008201_1_0_1; -.
DR   InParanoid; G3JD62; -.
DR   OMA; WSQKQPE; -.
DR   OrthoDB; 1328399at2759; -.
DR   Proteomes; UP000001610; Unassembled WGS sequence.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProt.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   CDD; cd04399; RhoGAP_fRGD2; 1.
DR   Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 2.
DR   Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR027267; AH/BAR_dom_sf.
DR   InterPro; IPR000591; DEP_dom.
DR   InterPro; IPR031160; F_BAR.
DR   InterPro; IPR001060; FCH_dom.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR23065; PROLINE-SERINE-THREONINE PHOSPHATASE INTERACTING PROTEIN 1; 1.
DR   PANTHER; PTHR23065:SF17; RHO-GTPASE-ACTIVATING PROTEIN RGD2; 1.
DR   Pfam; PF00610; DEP; 1.
DR   Pfam; PF00611; FCH; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   SMART; SM00049; DEP; 1.
DR   SMART; SM00055; FCH; 1.
DR   SMART; SM00324; RhoGAP; 1.
DR   SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR   SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS50186; DEP; 1.
DR   PROSITE; PS51741; F_BAR; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|PROSITE-ProRule:PRU01077};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001610};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          2..435
FT                   /note="F-BAR"
FT                   /evidence="ECO:0000259|PROSITE:PS51741"
FT   DOMAIN          216..293
FT                   /note="DEP"
FT                   /evidence="ECO:0000259|PROSITE:PS50186"
FT   DOMAIN          469..667
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   REGION          340..359
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          677..702
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          714..759
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          774..838
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        677..691
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        740..759
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        792..806
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   838 AA;  93837 MW;  EE379A3F44C39AF3 CRC64;
     MPGFADSFWS NDYAGGLGVL FGKLQQGVME DRQILTLARL RAEAEDVYGQ RLADIAPAVD
     RVSGGFSRDD GATVRKAYDG MRTEMQDAAK SHQRIAQNIR DLVVNPFARW CDAHEARIQD
     SQDDLQARTK AHDRQAETVK KLRSNYFNKC RLVEDLEEEN KLAFQEPELS PKNGTQIPEI
     KVQPHKEEES REDEEVFEIG DEIYQPDQLR KIISHMLSNI KIGETKVPIL GTYLNTSAGS
     DIVEYLQRTM AISSISYAER IGQDLISNGL LRLIGNVGST FANSSKMFYQ WRPKSFRLAG
     IPEKKQSLNR TFSLPISESS DSPVVGTVSE YLANWNVLNN SHPNETPTQR LQREGRESDE
     KYKSAVKKLD QLRCDLEQAI FLHLKFLEQC ELDRLKAIKT VILDFSGTIS NVIPSLQSTV
     DKMMLFQETV QPLGDLRYLL ETYRTGGFVP RVAVYENYYN KVDDQIFGVD LEARARADKK
     RVPVVVTAIL TYLDHHYPDL EGDEARRGVW LVDVPLAQTH RLRAKLNNDG AISQEVFSDF
     DIPTVASLLK LYLLELPDSL VSTHVYEIVR TIYTTPAAEG TEASRVAVLQ QTLSQLRLSN
     IATLDACMNH FTRLIDLTSA DDAYVASLAA TLSRCILRPR AETSLTMEEK HAIRLVRDLF
     AHKDAIFSEL KRMSTLSHSS SVGSNNRPRA VSTDESNRKN LVEERNRVIL EKATAIRGRA
     TSPAPGTNRH RRDRSTGGPE TRFPIQTSPT TNDRHRSSLG SGLASAVNRL SLEVPADGTM
     TPPETLNGAP VGENTRECTD SLTKGTPTRF VGGRRVPNSP PSEEISRGVT LEDKPMDD
//
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