RASY_DICDI
ID RASY_DICDI Reviewed; 216 AA.
AC Q55CB7;
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 rasY;
DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P32253};
DE Flags: Precursor;
GN Name=rasY; ORFNames=DDB_G0270126;
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; EAL72413.1; -; Genomic_DNA.
DR RefSeq; XP_646564.1; XM_641472.1.
DR AlphaFoldDB; Q55CB7; -.
DR SMR; Q55CB7; -.
DR STRING; 44689.DDB0229434; -.
DR PaxDb; Q55CB7; -.
DR EnsemblProtists; EAL72413; EAL72413; DDB_G0270126.
DR GeneID; 8617532; -.
DR KEGG; ddi:DDB_G0270126; -.
DR dictyBase; DDB_G0270126; rasY.
DR eggNOG; KOG0395; Eukaryota.
DR HOGENOM; CLU_041217_9_8_1; -.
DR InParanoid; Q55CB7; -.
DR OMA; QFVSHRF; -.
DR PhylomeDB; Q55CB7; -.
DR PRO; PR:Q55CB7; -.
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 GO; GO:0009617; P:response to bacterium; HEP:dictyBase.
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..213
FT /note="Ras-like protein rasY"
FT /id="PRO_0000365569"
FT PROPEP 214..216
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000365570"
FT MOTIF 39..47
FT /note="Effector region"
FT BINDING 17..24
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 64..68
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 123..126
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 213
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 213
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 216 AA; 24752 MW; 8953CF1D6A3D0F8E CRC64;
MTTNKSNGNL VKLCIMGDGG VGKTSVTIQF ISNHFVHYYD PTIEDSYRKQ CLIDDQVYML
DILDTAGQDE LTAMRDQWIR SCEGFILVYS VTSRSSFDQV QFFREQIIRV LDRDDVPIMM
IGNKSDLDDE RQVTFQEGKD LARCLGMSFM EVSAKTRLNV EEVFNETVRC VKRREESLLK
KDNSKDGKGD HSKKSSIFKK LNQKVNGAKI SICKMM
