ID A0A0F8WUA1_9EURO Unreviewed; 1410 AA.
AC A0A0F8WUA1;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=RhoGAP domain protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=ARAM_005224 {ECO:0000313|EMBL:KKK21175.1};
OS Aspergillus rambellii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=308745 {ECO:0000313|EMBL:KKK21175.1, ECO:0000313|Proteomes:UP000034291};
RN [1] {ECO:0000313|EMBL:KKK21175.1, ECO:0000313|Proteomes:UP000034291}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRRC1468 {ECO:0000313|EMBL:KKK21175.1,
RC ECO:0000313|Proteomes:UP000034291};
RA Moore G.G., Beltz S.B., Mack B.M.;
RT "Draft Genome Sequences of Two Closely-Related Aflatoxigenic Aspergillus
RT Species Obtained from the Cote d'Ivoire.";
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
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:KKK21175.1}.
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DR EMBL; JZBS01001836; KKK21175.1; -; Genomic_DNA.
DR STRING; 308745.A0A0F8WUA1; -.
DR OrthoDB; 25690at2759; -.
DR Proteomes; UP000034291; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProt.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd13277; PH_Bem3; 1.
DR CDD; cd06093; PX_domain; 1.
DR Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR036871; PX_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; PF00169; PH; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000034291}.
FT DOMAIN 805..921
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1099..1303
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 37..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 140..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 273..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 358..497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 532..557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 857..876
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 923..972
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..88
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..317
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..346
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..406
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..473
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 537..555
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 857..873
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 924..945
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1410 AA; 153449 MW; 965B35CD4EF0A248 CRC64;
MSQPRRQGND HIFSSLPPST AAAASPIALR PGGLALRSGS AVTDYSPRKP SLSPLHTDGR
NQSPHRTDSS LSQRTASPIS STATSPLENL STIRETAHAA FPTPLSTTGR ISIDTSSNAL
RKRALSHNEM KMADQVNEIK TRKDSDATES TLSMSPSTMS PIGSLKSISG DRPVHHRTMP
RTSSIDSAIS SLSSASQSHK ASFDANSISK ADIDNLITAA GSPEAVIIHL LKEKHHAASQ
NSQLWRLVDK QRTLILGLNK DLERAMKEKE RYKKKVKELQ SAAPPLPSTE VQPVRPPTAD
SLDTTITQIS PTNGPAKSPH PTDKPGAHPQ RLQTGDSRSS PGSTPSLQKL VESALLADEP
DLRCESQSSQ RLASIQEMST TSPTSPVSPS STIHDLASSG NKNPQVPHQI RKAPPAPLNL
TPTDRTALEI PERSDSESEY EDILAVEESP IERGRRKTRD DDDREREAVL ERDGSNALKN
IEGSGTGPYA GLAIDPAPSD SRRAVPAEAL SSTMSLRTLP SASIPERVII TGPKSPGLPL
SPRPEDRPLG SPLPRMPREM PNSFSSLTMP SGNHLSGLAL SPRVGKHPNP FVAGGHTVPS
TPTHAGIPVD SYNRRIPSID AAVKIDSPQS PEHAAIGIYQ GLKSEDYPNL LLPPNALPLI
QVKVSSSRLR PSRNSYMAMK PLEEEPVFTL SVFSRSENSE LWRVEKVIAA LPQLDQHVRQ
LSAFQGKLPD RSIFSGHSPA KIDVRRAALN SYFEALLDTP MDEKAALVIC QFLTSDAIEP
RDDELSLLKG SHQAGSEILR GPDGKPRKEG YLTKRGKNFG GWKARFFVLH GPELKYFEAP
GGAHLGTIKL HNAQIGKQSQ NTCQSNPPSQ ADDDSDNQYR HAFLILEPKK KDSSALVRHV
LCAESDEERD SWVEALLEYV EGSSENEASA SRTPSQVSTK LPTNAAAKSK LFPNGSKKAG
KGPDSPDLEI SDTVQGFSYD DAVPAEPPVL GPFDRGTPRS PMFPPGSSIE DSHAASLDPA
QISSKMISGP TNGAVIQDVG AWGNRTTSTR EKKRSIWGFR TRSSIDLASQ IQALSESPTI
QIQGPSGEKR ELVRPVFGIP LAEAVQYCAP QGANADLPAV VYRCIEYLKA KRAESEEGIF
RLSGSNIVVK ALRERFNTEG DVDFLAGDQY YDVHAVASLF KQYLRELPTT VLTRELHIEF
LRVLELNEKQ KKIVAFNSLV HRLPKPNLAL LRALVQFLII IVNNSDVNKM TVRNVGIVFA
PTLNIPAPVF SMFLTEFDEI FEGTPGSNVD AMSLTVDHSL TPEDIRSPRR QMFSEIPTPA
HHQMTFPRAG DPSDDYSAQH DTGFIPMQPS YEPYSHGTAD NFPMAMPRML APNDNSRAAK
AKRRESSMLF MEFNNENASA ASHDDHGKSL
//