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Database: UniProt
Entry: A0A0L6WGB2_9AGAR
LinkDB: A0A0L6WGB2_9AGAR
Original site: A0A0L6WGB2_9AGAR 
ID   A0A0L6WGB2_9AGAR        Unreviewed;      1122 AA.
AC   A0A0L6WGB2;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   SubName: Full=Rho-GTPase-activating protein 8 {ECO:0000313|EMBL:KNZ74555.1};
GN   ORFNames=J132_06509 {ECO:0000313|EMBL:KNZ74555.1};
OS   Termitomyces sp. J132.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Tricholomatineae; Lyophyllaceae;
OC   Termitomyces.
OX   NCBI_TaxID=1306850 {ECO:0000313|EMBL:KNZ74555.1, ECO:0000313|Proteomes:UP000053712};
RN   [1] {ECO:0000313|Proteomes:UP000053712}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J132 {ECO:0000313|Proteomes:UP000053712};
RA   Hu H., Poulsen M.;
RT   "The genome of Termitomyces.";
RL   Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KQ412647; KNZ74555.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0L6WGB2; -.
DR   STRING; 1306850.A0A0L6WGB2; -.
DR   OrthoDB; 1328399at2759; -.
DR   Proteomes; UP000053712; Unassembled WGS sequence.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProt.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
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; PF00611; FCH; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   PRINTS; PR01217; PRICHEXTENSN.
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:UP000053712}.
FT   DOMAIN          8..514
FT                   /note="F-BAR"
FT                   /evidence="ECO:0000259|PROSITE:PS51741"
FT   DOMAIN          293..373
FT                   /note="DEP"
FT                   /evidence="ECO:0000259|PROSITE:PS50186"
FT   DOMAIN          559..768
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   REGION          158..245
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          775..798
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          866..1122
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        195..226
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        229..245
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        775..794
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        866..893
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        915..932
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        958..979
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        987..1010
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1026..1045
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1054..1109
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1122 AA;  122069 MW;  FD0E80C39A993089 CRC64;
     MAVLSLPLNF TNSFWSQDYR RGLQVLFNKL DQGVAENTEI VAFIRARAIA EGHLAATLTN
     PALTGPAGTG FGADDGASLL TAFRGLQAES VIQGQAHRNI SKELGTLVVE PFEQWALGYA
     ERIKSNKVTV LDNWLRSYEQ AHAEVGKLKQ QYLAKTRRAD EAEDDAKFAP NNGGNIPDKY
     TSSPRLRPAD GRDSSPRSAS VSERITQRLK EIQTRSAGTL QSSPADDDEQ PLPKLDKGKG
     KAVDEDHLRT PFITASPPPM SPLNPPASLP PTPILLAGLA LSPASVSQLL VRAAAELPLR
     PVRFPLLGEY PDCFNGEEFV SWLNANVPGF GGNLDVAEDA ARDLTEREGL LRRIGEFGNQ
     FEHSDEAFYQ FRSKAFNLAS KAASEQDGGT LGAGAKQAEA VIKRTGGNFV NLVNKVLNNA
     NNGEPAYVKA RHEADVADNT YRKAVRKLDR HRLALEERLE EAFKLLQRWE MERLRAVKTV
     LLQYQGTLAN LPKSLEPSID RQATLVASYQ PENDLTALIE RYRTGPFRPN AQIYESVAHD
     ESDVVFGIDL RRWAEGGWHA LSTGEEKKEI VPPVLTALLE GLQEAYKRLP NDNERRKSWI
     YEVPLSAVHH LRETLNALPV DQPIPADLMV KYDAPVIAST IKLWILELDP PLALYDGWDE
     LRKLYPTVGS SATKEAEKSR EVHIQSLSAA LQRLPKVHLY VLDVVVKHLK TLIENTTVEE
     ADEIYITKLA LSVGRAVVRP KVETEISIQD RHPTLMFIDL ITHYDAILPP TISRKKRESE
     RKVPVRKRTA PVDMRLSRSR ISAGADAQQL LAAQQIAQNP SLMKSPKSPE KTSSPSIPVA
     AAAAVVPPPP LPVVPPLTLV PVPEPPAPAL SPPPPPPPVQ IPAPPPPPAV PSASGRPAFK
     EPPPEFDDQP PRPAFKEPPP EVELPRPAFK EPPPEVDFAG LVLKESPPEV DLDHRPIFVE
     PPPSPPAPAA APPTTIIPPT PHKRATGRGS ATASPSPPET PSTVTLVSRS PSPPEDIFLG
     SGRATLSRAG SGQTGTTQSG TARTPGVRGP RTVASLVSNF SNRNSVSGSS PPTPSSPSRT
     VNRLNGPGRR TSSNLYRNSG SSASFSRRTM ASDAEDDVTE KK
//
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