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Database: UniProt
Entry: A0A2G5EWQ2_AQUCA
LinkDB: A0A2G5EWQ2_AQUCA
Original site: A0A2G5EWQ2_AQUCA 
ID   A0A2G5EWQ2_AQUCA        Unreviewed;       887 AA.
AC   A0A2G5EWQ2;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=Rho-GAP domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=AQUCO_00400805v1 {ECO:0000313|EMBL:PIA60160.1};
OS   Aquilegia coerulea (Rocky mountain columbine).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Ranunculales; Ranunculaceae; Thalictroideae;
OC   Aquilegia.
OX   NCBI_TaxID=218851 {ECO:0000313|EMBL:PIA60160.1, ECO:0000313|Proteomes:UP000230069};
RN   [1] {ECO:0000313|EMBL:PIA60160.1, ECO:0000313|Proteomes:UP000230069}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Goldsmith {ECO:0000313|Proteomes:UP000230069};
RA   Hodges S., Kramer E., Nordborg M., Tomkins J., Borevitz J., Derieg N.,
RA   Yan J., Mihaltcheva S., Hayes R.D., Rokhsar D.;
RT   "WGS assembly of Aquilegia coerulea Goldsmith.";
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KZ305021; PIA60160.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G5EWQ2; -.
DR   STRING; 218851.A0A2G5EWQ2; -.
DR   InParanoid; A0A2G5EWQ2; -.
DR   OrthoDB; 5395569at2759; -.
DR   Proteomes; UP000230069; Unassembled WGS sequence.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   CDD; cd00821; PH; 1.
DR   CDD; cd00159; RhoGAP; 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; IPR025757; MIP1_Leuzipper.
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; PTHR46265; RHO GTPASE-ACTIVATING PROTEIN 7; 1.
DR   PANTHER; PTHR46265:SF2; RHO GTPASE-ACTIVATING PROTEIN 7; 1.
DR   Pfam; PF14389; Lzipper-MIP1; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000230069}.
FT   DOMAIN          20..127
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          173..373
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   REGION          384..438
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          506..569
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          710..731
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          779..816
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          867..887
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          622..656
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        416..430
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        506..526
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        541..569
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   887 AA;  98208 MW;  DF0126A7A6FBE1CF CRC64;
     MSGSFGPLEG PRNGVSGSNT VYKSGPLLIS SKGIGWKSWK KRWFILTRTS LVFFKNDPSE
     LPQRGGEVNL TLGGIDLNNS GSVVVREDKK LLTVLFPDGR DGRGFTLKAE SSEDLYEWKT
     ALEHALAQAP SAALVMGHGI FRNDASDTVE GSFQQWRDKH PVKSLVVGRP ILLALEDIDG
     SPSFLEKALC FLEKFGTKVE GILRQSADVE EVDRRVQEYE QGKSEFESDE DAHVVGDCVK
     HVLRELPSSP VPASCCTALL EAYRVEGKAD RVVALRSAIY DTFPEPNRRL LQRVLKMMHK
     ISAHSADNRM TPSAVAACMA PLLLRPLLAG ECELEDDFDM NGDDSAQLLA AANAANNAQA
     IVTTLLEEYD NVFPGVNLHG CSLSVDPQME NSESEDSTDD GNSNTKDISY HDAANEVNPE
     FEDDSERVLS GKLSETSGYS GSDLYDNKVC VDDLDVESPE RKHSSPRKLL SEKSVRDTNG
     IFKTHNTLKN ESEVSIKVMD SPSALVANGS HRSTGDRLTS VDTRIPSHAP SPELCLEKST
     VKPNGSKNNV KRSNFWGRSN TRRNTSVDSV DLSGDEETFQ SGFSYKLMQS RLFRLAIQRL
     EIAKNDLLNR IAKEAKGNAI LQASLERRKQ ALHERRLALE QDVSRLQEQL QAERDLRAAL
     EVGLSMSSGQ FSDSRGMDSK TRAELEEIAL AEADVAKLKQ KVTELHHQLN QQRQQHYGSL
     SDASNRHQHA QNLHSQLKFM QQDFDMNLAF CNHERKQRTE ESSLGADWKS LKAQLLSAAS
     NSKQHSRKQL ANLTSPSDSR STEASTSFSA DNFSAIDSAT MPTTSREMEG LGNQRQTAPS
     SSTLVELTTR LDFFKERRSQ LMEQLHNLDL ASSPQGMVHS PPSPSWR
//
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