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Database: UniProt
Entry: A0A2C9KM76_BIOGL
LinkDB: A0A2C9KM76_BIOGL
Original site: A0A2C9KM76_BIOGL 
ID   A0A2C9KM76_BIOGL        Unreviewed;      1191 AA.
AC   A0A2C9KM76;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Rho-GAP domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   Name=106060028 {ECO:0000313|EnsemblMetazoa:BGLB021313-PA};
OS   Biomphalaria glabrata (Bloodfluke planorb) (Freshwater snail).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Heterobranchia; Euthyneura; Panpulmonata; Hygrophila; Lymnaeoidea;
OC   Planorbidae; Biomphalaria.
OX   NCBI_TaxID=6526 {ECO:0000313|EnsemblMetazoa:BGLB021313-PA, ECO:0000313|Proteomes:UP000076420};
RN   [1] {ECO:0000313|EnsemblMetazoa:BGLB021313-PA}
RP   IDENTIFICATION.
RC   STRAIN=BB02 {ECO:0000313|EnsemblMetazoa:BGLB021313-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
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DR   RefSeq; XP_013073206.1; XM_013217752.1.
DR   AlphaFoldDB; A0A2C9KM76; -.
DR   STRING; 6526.A0A2C9KM76; -.
DR   EnsemblMetazoa; BGLB021313-RA; BGLB021313-PA; BGLB021313.
DR   KEGG; bgt:106060028; -.
DR   VEuPathDB; VectorBase:BGLB021313; -.
DR   OrthoDB; 7959at2759; -.
DR   Proteomes; UP000076420; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   CDD; cd07595; BAR_RhoGAP_Rich-like; 1.
DR   Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR   Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR   InterPro; IPR027267; AH/BAR_dom_sf.
DR   InterPro; IPR004148; BAR_dom.
DR   InterPro; IPR047165; RHG17/44/SH3BP1-like.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   PANTHER; PTHR14130; 3BP-1 RELATED RHOGAP; 1.
DR   PANTHER; PTHR14130:SF14; RHO GTPASE-ACTIVATING PROTEIN 92B; 1.
DR   Pfam; PF03114; BAR; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   SMART; SM00721; BAR; 1.
DR   SMART; SM00324; RhoGAP; 1.
DR   SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR   SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR   PROSITE; PS51021; BAR; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT   DOMAIN          1..233
FT                   /note="BAR"
FT                   /evidence="ECO:0000259|PROSITE:PS51021"
FT   DOMAIN          239..425
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   REGION          505..543
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          614..645
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          682..802
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          889..915
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          954..1191
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          153..180
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        682..700
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        742..769
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        777..802
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        954..988
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1030..1054
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1055..1076
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1091..1164
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1170..1184
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1191 AA;  130175 MW;  9F73F0C1BB526BDA CRC64;
     FRAEKSEVLS EDQQENEKRV ELVKHAFQNV TKKAAATLQS NGTDFDKRLK KLPESGLSAA
     LLDSAQTLGT ETLLSTVCKL CGECQSNLAT EQVNYEISVE TEFINPLQTI CDVDIPSIIK
     LRKALNKSTL DMDSAKSRFS QAVRQSQVPG ANMTTAAAKA ETIKEEYEEA TLKVETIKDN
     LSIELCNFAA KESDQSQKML LLLEAQADYH RKALQAIEQF IPLVKVKIDN APCKPVYGMP
     LEEHLRLMKR DISLVIEACV TVLLECGLEE EGLFRIAGAA IKLKKLKACF DAQSLDMEEF
     SNDPHTVAGA LKQYLRELPE PLLTFAMHDE FLKAATLPLD QRLQTLWTLI QKLPVANFNN
     FRYLVKFLAK LAEKSDINKM KPSNIAIVIG PNLLWSETSN APNMLTTGTL SAIIEAIVTH
     ADWFFPGAFD FHLTALGSSP KPSTEPGLLS DSAQFVNNKT IDAPAKQDLD KKDNTAEKPL
     CSKTRTLPLE QGFIVSSSDT YPLRFPEKCD EEESSSDESN PFSEKFALKS KTGESVSEKG
     CMGKESDVQR VDLGDRKCDI SGSTNTGDYD NILYTINPLN PSARCSSMNP TDRRASADNV
     SAYGKCLPAP VPPCRPSRPT KKPLPPEKTS CMPSGPRAEV SRSVDTLPDV AQPSSRYMIG
     STPNITALPY HRNEEETYSG LQSQFWNRPN QKSNFNSLKR GSDPCIIPPP SQFNNYSTHR
     PLKLSRAHLG TPPKPGEMSR SQPASHAENS RAPYSPPQEM SQSQPAPYVE KSPYSPPHEM
     SLSQPSPSLK SPANHYNPVD KSFHQDTYNT AFALSSLGAG NKSADYLTRV RAMWDDRHQQ
     LGTKPQNASH GKREELISSS LEFTPKQHPA TSYNNTNLVG SYQKNIFSSP STTNSGSSVP
     YGRSTSCSPS QPPEFDFTTV GYHDDQETYN QSQTGTQQGS MESLQIQVTS AQSINQQPPS
     PGVTVTNTSS QTTVINTQQE SPEAVSSIQR RATRKPAPPP PPEKPFTVMV TATTALKPGS
     DMGFGEPEGN GSNAQFQTWP RSAPLASPES PSEQHKLSGG HEKRSSGERP TMPPPDRPER
     PRLPQTLNPP LGRGHQRSAS TGAVMNQTAS SFEPHVGVPN AGSLTSSSIL EGDKDIDTIN
     TGVGSETASY SQGSVAQGMS HTLGRHSSMK PRPTPPPPPP PVAKESEDTK L
//
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