ID   GACO_DICDI              Reviewed;         684 AA.
AC   Q55GP8;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=Rho GTPase-activating protein gacO;
DE   AltName: Full=GTPase activating factor for raC protein O;
GN   Name=gacO; ORFNames=DDB_G0267568;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
CC   -!- FUNCTION: Rho GTPase-activating protein involved in the signal
CC       transduction pathway. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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DR   EMBL; AAFI02000003; EAL73237.1; -; Genomic_DNA.
DR   RefSeq; XP_647136.1; XM_642044.1.
DR   AlphaFoldDB; Q55GP8; -.
DR   SMR; Q55GP8; -.
DR   STRING; 44689.DDB0233841; -.
DR   PaxDb; Q55GP8; -.
DR   EnsemblProtists; EAL73237; EAL73237; DDB_G0267568.
DR   GeneID; 8615939; -.
DR   KEGG; ddi:DDB_G0267568; -.
DR   dictyBase; DDB_G0267568; gacO.
DR   eggNOG; ENOG502QR6X; Eukaryota.
DR   HOGENOM; CLU_402508_0_0_1; -.
DR   InParanoid; Q55GP8; -.
DR   PRO; PR:Q55GP8; -.
DR   Proteomes; UP000002195; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   Gene3D; 1.10.555.10; -; 1.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   Pfam; PF00620; RhoGAP; 1.
DR   SMART; SM00324; RhoGAP; 1.
DR   SUPFAM; SSF48350; SSF48350; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
PE   3: Inferred from homology;
KW   Coiled coil; Cytoplasm; GTPase activation; Reference proteome.
FT   CHAIN           1..684
FT                   /note="Rho GTPase-activating protein gacO"
FT                   /id="PRO_0000380213"
FT   DOMAIN          497..684
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT   REGION          1..283
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          292..311
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          403..489
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          399..473
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        36..113
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        140..170
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        171..186
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        197..266
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        403..472
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        473..489
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   684 AA;  74889 MW;  E20062EE7C429274 CRC64;
     MSKLPPPPVQ SSPQGFQLPS LHSVQLKPVR PPPQPTQQQL ASNTSPREVG TSLSPQSPSN
     NINPSSSSSS PSSSIRQSPS SSPNVARKVP PTPTNNNGGP PTTTTTTTTT MPPPPAFIKK
     LSPSSSPILP KRIVSSPPLN GNTAPPPPPI VHLPPPPPTN LPPPPTLSPS SSTTTSPSSS
     SLNLSGGVPL PPRILRNSDG SANNNNNSNN NSNNNINSLN LSTSGGIPPP PSFFNNNNNN
     NNNSGSFVNS ASSNGSPSLQ SQNSVGYFKP PPPPVPTRSA SLDPKQMGQF IKPQQNQNNS
     NNINNINNNN NNIILPPPPN ININNNNFVP YIPSNNNQQQ STTPPPIVSI SPLKRNSIDN
     SVVNKRLSQD LNTMLVNRLQ HGLSPPVATP FFDDKILGSA SKSAELKEKR DQEERERRER
     ERIKKEKEDS EKKEKKEKKG KEEQEKKDKK KKEEQEKKDK KKKEEEEKKS KSSSSSSSSS
     KKSSSDNTIV NQNIFNNTLS QIMENQRDAQ SLSPSSLPYP LILKLLTESI MSLNGPYTEG
     IFRITGSGTE VNRLKKQINE HDFSLDTQDP HVLAGLLKLW LRELVHPIIP SELYNDAIKS
     RSKEEVSRII SLIPDQNKEV LNFLIPFLKN VSQPHYAQYS KMDIDNVAMV FSPGLLRSTV
     LTTDLLLNSQ YEKDFVKCLI EMSP