ID   A0A0D2AR20_9EURO        Unreviewed;       924 AA.
AC   A0A0D2AR20;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   13-SEP-2023, entry version 37.
DE   RecName: Full=Rho-GAP domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PV06_05950 {ECO:0000313|EMBL:KIW42391.1};
OS   Exophiala oligosperma.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=215243 {ECO:0000313|EMBL:KIW42391.1, ECO:0000313|Proteomes:UP000053342};
RN   [1] {ECO:0000313|EMBL:KIW42391.1, ECO:0000313|Proteomes:UP000053342}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 72588 {ECO:0000313|EMBL:KIW42391.1,
RC   ECO:0000313|Proteomes:UP000053342};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Exophiala oligosperma CBS72588.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KN847336; KIW42391.1; -; Genomic_DNA.
DR   RefSeq; XP_016262607.1; XM_016407003.1.
DR   AlphaFoldDB; A0A0D2AR20; -.
DR   STRING; 215243.A0A0D2AR20; -.
DR   GeneID; 27358024; -.
DR   VEuPathDB; FungiDB:PV06_05950; -.
DR   HOGENOM; CLU_008201_1_0_1; -.
DR   OrthoDB; 1328399at2759; -.
DR   Proteomes; UP000053342; 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   Reference proteome {ECO:0000313|Proteomes:UP000053342}.
FT   DOMAIN          15..446
FT                   /note="F-BAR"
FT                   /evidence="ECO:0000259|PROSITE:PS51741"
FT   DOMAIN          242..311
FT                   /note="DEP"
FT                   /evidence="ECO:0000259|PROSITE:PS50186"
FT   DOMAIN          480..687
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   REGION          692..924
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          359..386
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        706..748
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        778..832
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        899..917
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   924 AA;  102220 MW;  CE320C2ECFCDB4C8 CRC64;
     MATDNAPAPG RPKVPGFTES FWSSDYAGGL GVLFQKLQQG VIENNQILTI ASMRADAEEL
     YSDRLGDIAP SVDRMTGGFA RDDGASVRKA FEGVRSEMVE ATKNHKKIAD NIRELVVNPF
     SRWCDAHATR ISNSQEDLQS KIKAHDRQAD LVKKLRSQYF NKCRLVEDLE EENKLAFQDH
     ANGSPKPQSP PPPKIVLPED EFDELPVEIG DETYSPDRLK TLLTDMLEKI PLSEFKVPIL
     GVYQNVSAGT DIVEYIQKHM KASSVGYAEK IGQDLVDRGL LRLIGNMGNT FANSSRMKYQ
     WKTRVFQITG VPEKKKPLGR SITGSSQDGV LESPTIGNIT EAIQGWNPLN NAHPNETPAE
     RLKREAKEAD EKYKAAVRKL DLLRCNLEES MMDHLKFLER CETDRLRAIK SVILDFSGAI
     SNSIPSFQSQ VDHMMLYQET IQPLGDLRYL LENYRTGAFV PKVVPYENYY GSVEDQTFGV
     DLEARARADR KRVPIIVTSI LTFLDSHYPD LEGDEARRNV WLVDVPLAAT HHLRNQINNG
     APVPREILEK YEVPIVASVL KLYLLELPDS LVSSQVYEII KTIYATTSDA APNPISTDSV
     DSAPRIKVLQ STLGQLRLNN IATLDALATH FTRLIDLTSA DEAYVTALAQ SLAPCILRPR
     TENSLTLEER HAYRLIRDLF DHKEAIFGEL KRQSSTSLST RQRAVSTNDE RSRRANMEER
     ARAITEQRQR DKSPGPANRH RRDKSTDGSI GRFPVVASPR PEHGRNVSGV GLPSKRTSLE
     VPGSNEGSPV QARTQNQSAV DRNSTTTVQP GTGMNGQTHG QGEVSPDIMN LPSTFSGGGP
     GPHIPPPLDD DSQDSDSGPQ PAQKESDGGS RAGSLKRNAA GSGRKPVGGG GSLSRRSYQA
     YEGHPSQSQN QGVQLTDRPM DDFS
//