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Database: UniProt
Entry: A0A3B0JXF0_DROGU
LinkDB: A0A3B0JXF0_DROGU
Original site: A0A3B0JXF0_DROGU 
ID   A0A3B0JXF0_DROGU        Unreviewed;      1418 AA.
AC   A0A3B0JXF0;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   08-NOV-2023, entry version 20.
DE   SubName: Full=Blast:Breakpoint cluster region protein {ECO:0000313|EMBL:SPP86734.1};
GN   ORFNames=DGUA_6G008997 {ECO:0000313|EMBL:SPP86734.1};
OS   Drosophila guanche (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7266 {ECO:0000313|EMBL:SPP86734.1, ECO:0000313|Proteomes:UP000268350};
RN   [1] {ECO:0000313|Proteomes:UP000268350}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Alioto T., Alioto T.;
RL   Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cell projection, axon
CC       {ECO:0000256|ARBA:ARBA00004489}. Cell projection, dendritic spine
CC       {ECO:0000256|ARBA:ARBA00004552}. Synapse
CC       {ECO:0000256|ARBA:ARBA00034103}.
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DR   EMBL; OUUW01000011; SPP86734.1; -; Genomic_DNA.
DR   Proteomes; UP000268350; Unassembled WGS sequence.
DR   GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR   GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:InterPro.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0016043; P:cellular component organization; IEA:UniProt.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   CDD; cd13368; PH_BCR_arthropod; 1.
DR   CDD; cd00160; RhoGEF; 1.
DR   Gene3D; 4.10.280.30; Bcr-Abl oncoprotein oligomerisation domain; 1.
DR   Gene3D; 2.60.40.150; C2 domain; 1.
DR   Gene3D; 1.20.900.10; Dbl homology (DH) 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; IPR037769; Abr/Bcr.
DR   InterPro; IPR036481; Bcr-Abl_oncoprot_oligo_sf.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR035899; DBL_dom_sf.
DR   InterPro; IPR000219; DH-domain.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   PANTHER; PTHR23182; BREAKPOINT CLUSTER REGION PROTEIN BCR; 1.
DR   PANTHER; PTHR23182:SF1; RHO GTPASE ACTIVATING PROTEIN AT 1A, ISOFORM E; 1.
DR   Pfam; PF19057; PH_19; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   Pfam; PF00621; RhoGEF; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00324; RhoGAP; 1.
DR   SMART; SM00325; RhoGEF; 1.
DR   SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR   SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR   SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS50010; DH_2; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
PE   4: Predicted;
KW   Guanine-nucleotide releasing factor {ECO:0000256|ARBA:ARBA00022658}.
FT   DOMAIN          692..880
FT                   /note="DH"
FT                   /evidence="ECO:0000259|PROSITE:PS50010"
FT   DOMAIN          893..1046
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          1075..1198
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          1220..1418
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   REGION          112..205
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          218..628
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          646..682
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        133..148
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        158..174
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        184..203
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        269..283
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        329..379
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        422..438
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        439..464
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        472..512
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        523..560
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        590..628
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        666..682
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1418 AA;  154827 MW;  0BBEB81085F3722B CRC64;
     MSVFDDFQRL WMQRFPQSSL SDAWEQDVRA SLERHRVKIT ELGKELEQET LYVEYLERLL
     SDVEKYRASG GDPTALFEAA SGSGSVSGSS SNGATTTAAA VEKEFKSSLN LRESSSLSVA
     GGKDKDRLSL NTDNKYTHTS NAAGSGSRAG GSASGGAVVG NGNGNGSGGS SGLNSAPIAG
     DKRGLEPSFE REDRDKDSGN EKDANGALHQ CITELAASIN SGGGVKRPEA VEAERESSAR
     QPVRKTTSQY VTVIQVKEAK DKDGDEASSG NDQQPTPPST FSRYAPGAGS GLGAEPSAPP
     LSPSLSSYME AKKKMPPRPP PKNIRRVEPP TIPSQQHHQL SSSPKRETAA YAGSTMPLPS
     SSVGSGSLSS DSPGNSLERN IKPSDILRQK SSENLDAKYA NNRKTTPELG KFVTNPELME
     ELGRKMVGKM DSLEHAKRSD ASSSAASGGS SSLGRTSSTP GRPLNPGRTG AGTVGASPTG
     SLNKTAKLAV ADSSSTSSLE KKSRTSLQAS DAEGGAGSGG GAATQRSAGS KESLASQGIS
     EVIKSYESVS SLSSESAKAA AHQSPADHEP YYDSVPLDNG DGEYVFIKPG RTGSSSSRDD
     LSTPGSSTLP MAQGLSSQTS VVDPESPGRT SNYVNIDYFL QQSNETRSSS LDSDGEYEGP
     PILRTISHDE QTTSQTTPGA LRKVSGNARG AKIRSILSSI IHSETIYVEC LNKMMQYKKA
     IHATLGTSQP VIKEEEENTM FFKIDELFEV HTAFLSDLKT IVSHEGGDVL IGEAFKRLAD
     MFELYSAFLH NYGQAIETVK KCSASNPQFK KIVATIVVNL QTEQSLTLED LLHKPVARVQ
     INAMVFNDLL RETPANHPDH QPLRQAQKII QMFLNQFNVC QRLPTESNRN LRRMVRNSFI
     VELVDGHRKL RHLFLFNDVI ACAKYKALGR DRIDYELKWF IPLKDITVYE EADSAAELKE
     SSPANISQVK RNLRSVRDQL ILEANGVRTG DKYRRKLADL ESQLVLATPN LVLRLGNKAN
     NKAVTFFLSS DFERSQWIDS ITSLKQKCNL PGANTINSLE VTAFIVAMQK GMKTEMGSYL
     MRNTNDESLL VGDLHMSIQG LAGLEKPSDL YTCVEVDSYG HYFRKATTKI ICRSQTPVWN
     ESFMLELEGS QNVRILLYEA KDRPLLRAKH ILKLSHSWLT ETQQMRTIKL SETLELSCSF
     RFVPGELCRA TTKPGALFGV KMSQVLKREK RDIPFIISAC IREVERRGML EVGCYRVSGS
     ASDLSKLKKA FESDAYEAEQ LLREVDIHSV TGILKTFLRE LPEALFTDQL YPRFFDTFST
     LSNNNEATRI NELLKVFDEL PQANKASICL ILDHLIRVHE KEADNKMSLH NLAMVFGPTL
     LRPGQTQVKQ KDPLAASTVD VMAQAGILYC FLQARIKN
//
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