ID   RASX_DICDI              Reviewed;         213 AA.
AC   Q55CB8;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Ras-like protein rasX;
DE            EC=3.6.5.2 {ECO:0000250|UniProtKB:P32253};
DE   Flags: Precursor;
GN   Name=rasX; ORFNames=DDB_G0270124;
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: Ras proteins bind GDP/GTP and possess intrinsic GTPase
CC       activity. {ECO:0000250|UniProtKB:P32253}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2;
CC         Evidence={ECO:0000250|UniProtKB:P32253};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC       {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
CC       {ECO:0000305}.
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DR   EMBL; AAFI02000005; EAL72412.1; -; Genomic_DNA.
DR   RefSeq; XP_646563.1; XM_641471.1.
DR   AlphaFoldDB; Q55CB8; -.
DR   SMR; Q55CB8; -.
DR   STRING; 44689.DDB0229433; -.
DR   PaxDb; Q55CB8; -.
DR   EnsemblProtists; EAL72412; EAL72412; DDB_G0270124.
DR   GeneID; 8617531; -.
DR   KEGG; ddi:DDB_G0270124; -.
DR   dictyBase; DDB_G0270124; rasX.
DR   eggNOG; KOG0395; Eukaryota.
DR   HOGENOM; CLU_041217_9_8_1; -.
DR   InParanoid; Q55CB8; -.
DR   OMA; HYREQIR; -.
DR   PhylomeDB; Q55CB8; -.
DR   PRO; PR:Q55CB8; -.
DR   Proteomes; UP000002195; Chromosome 1.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC.
DR   GO; GO:0019003; F:GDP binding; IBA:GO_Central.
DR   GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR   GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR   GO; GO:0007265; P:Ras protein signal transduction; IBA:GO_Central.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR001806; Small_GTPase.
DR   InterPro; IPR020849; Small_GTPase_Ras-type.
DR   PANTHER; PTHR24070; PTHR24070; 1.
DR   Pfam; PF00071; Ras; 1.
DR   SMART; SM00174; RHO; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51421; RAS; 1.
PE   3: Inferred from homology;
KW   Cell membrane; GTP-binding; Hydrolase; Lipoprotein; Membrane; Methylation;
KW   Nucleotide-binding; Prenylation; Reference proteome.
FT   CHAIN           1..210
FT                   /note="Ras-like protein rasX"
FT                   /id="PRO_0000365567"
FT   PROPEP          211..213
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000365568"
FT   MOTIF           38..46
FT                   /note="Effector region"
FT   BINDING         16..23
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         63..67
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         122..125
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         210
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000250"
FT   LIPID           210
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   213 AA;  24538 MW;  D8453C36640E5441 CRC64;
     MSGYKNNNLV KLCIMGDGGV GKTAVTIQFI SNHFVHYYDP TIEDSYRKQC VIDDQVYMLD
     ILDTAGQDEL TAMRDQWIRS CEGFVLVYSV TSRSSFDQIA FFKEQINRVL DSDDVPIMMI
     GNKSDLDDER QVTYQEGKDL ARCFGMSFME VSAKTRSNIE EVFNETVRCV KRKYDLHNKD
     KSKDGKDIKK KNSIIKKLNQ KVNNTKNSIC KMM