ID   A0A167FHD6_9HYPO        Unreviewed;       838 AA.
AC   A0A167FHD6;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   SubName: Full=Rho-GTPase-activating protein 8 {ECO:0000313|EMBL:OAA45269.1};
GN   ORFNames=BBO_03847 {ECO:0000313|EMBL:OAA45269.1};
OS   Beauveria brongniartii RCEF 3172.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria;
OC   Beauveria brongniartii.
OX   NCBI_TaxID=1081107 {ECO:0000313|EMBL:OAA45269.1, ECO:0000313|Proteomes:UP000076863};
RN   [1] {ECO:0000313|EMBL:OAA45269.1, ECO:0000313|Proteomes:UP000076863}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCEF 3172 {ECO:0000313|EMBL:OAA45269.1,
RC   ECO:0000313|Proteomes:UP000076863};
RX   PubMed=27071652; DOI=10.1093/gbe/evw082;
RA   Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT   "Divergent and convergent evolution of fungal pathogenicity.";
RL   Genome Biol. Evol. 8:1374-1387(2016).
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OAA45269.1}.
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DR   EMBL; AZHA01000009; OAA45269.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A167FHD6; -.
DR   OrthoDB; 1328399at2759; -.
DR   Proteomes; UP000076863; 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   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; 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; 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, ECO:0000256|SAM:Coils};
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          161..194
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          676..838
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          348..375
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        676..696
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        697..711
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        738..776
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   838 AA;  93917 MW;  E688F6E0625D2BB9 CRC64;
     MPGFADSFWS NDYAGGLGVL FGKLQQGVME DRQILTLARL RAEAEDVYGQ RLADIAPAAD
     RVSGGFSRDD GATVRKAYDG MRTEMQEAAK SHQRIAQNIR DLVVHPFARW CEAHEARIQD
     SQDDLQARTK AHDRQAETVK KLRSNYFNKC RLVEDLEEEN KLAFQEPESS PKNASQIPEI
     KVQPHKEEES RDDDDVFEIG DEIYQPDQLK TILSNMLSNI KMGETKVPIL GTYLNTSAGS
     DIVEYLQRTM ATSSMSYAER IGQDLISNGL LRLIGNVGST FANSSRMFYQ WRPKAFRLAG
     VPEKKQTLSR TFSMPISESS DSPVVGTVTE YLANWNVLNN SHPNETPAQR LQREARESDE
     KYKSAVKKLD QLRCDLEQSI FIHLKFLEQC ELDRLKAIKT VILDFSGTIS NVIPSLQSTV
     DKMMLFQETV QPLGDLRYLL ETYRTGGFAP RVAVCENYYN KVDDQIFGVD LEARARADRK
     RVPVIVTAIL TYLDHHYPDL EGDEARRGVW LVDVPLMQTH RLRAKIHNDA TVSQEVFSDF
     DIPTVASLLK LYLLELPDSL VSTHVYEIVR TIYMTPAAES TDASRIAVLQ QTLSQLRLSN
     IATLDACMNH FTRLIDLTSA DDAYVTSLAT TLSRCILRPR VETSLTMEEK HAVRLVRDLF
     AHKDAIFSEL KRMSTLNHSS SVGSNRPRAI STNESNRKAL MEERNRALLE KASATRGRAT
     SPAPGTRHRR DRSSGGAETR FPIQTSPTAN NERHRSSLGS HLAGTVNRNS LEVPAEGTST
     PPEPVNGGIV DEAGDRERTD SLTKGTPTRF VGGRRVPNSP PIEEGVRGVT LEDKPMDD
//