RECG_ENTHI
ID RECG_ENTHI Reviewed; 199 AA.
AC O76321;
DT 27-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Rho-related protein racG;
DE Flags: Precursor;
GN Name=RACG;
OS Entamoeba histolytica.
OC Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae;
OC Entamoeba.
OX NCBI_TaxID=5759;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 30459 / HM-1:IMSS;
RX PubMed=9601102; DOI=10.1242/jcs.111.12.1729;
RA Guillen N., Boquet P., Sansonetti P.;
RT "The small GTP-binding protein RacG regulates uroid formation in the
RT protozoan parasite Entamoeba histolytica.";
RL J. Cell Sci. 111:1729-1739(1998).
CC -!- FUNCTION: Involved in cytoskeleton remodeling during capping of surface
CC receptors and uroid formation.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasm, cytoskeleton.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
CC {ECO:0000305}.
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DR EMBL; AF055340; AAC24704.1; -; Genomic_DNA.
DR AlphaFoldDB; O76321; -.
DR SMR; O76321; -.
DR STRING; 5759.rna_EHI_129750-1; -.
DR VEuPathDB; AmoebaDB:EHI5A_135270; -.
DR VEuPathDB; AmoebaDB:EHI7A_090820; -.
DR VEuPathDB; AmoebaDB:EHI8A_093900; -.
DR VEuPathDB; AmoebaDB:EHI_129750; -.
DR VEuPathDB; AmoebaDB:KM1_167560; -.
DR eggNOG; KOG0393; Eukaryota.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
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; IPR003578; Small_GTPase_Rho.
DR PANTHER; PTHR24072; PTHR24072; 1.
DR Pfam; PF00071; Ras; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51420; RHO; 1.
PE 3: Inferred from homology;
KW Cell membrane; Cytoplasm; Cytoskeleton; GTP-binding; Lipoprotein; Membrane;
KW Methylation; Nucleotide-binding; Prenylation.
FT CHAIN 1..196
FT /note="Rho-related protein racG"
FT /id="PRO_0000198914"
FT PROPEP 197..199
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000281261"
FT MOTIF 32..40
FT /note="Effector region"
FT /evidence="ECO:0000255"
FT BINDING 10..17
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 57..61
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 115..118
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 196
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 196
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 199 AA; 21926 MW; 17A202300203D510 CRC64;
MRPVKLVIVG DGAVGKTCML ISYTTNAFPN EYIPTVFENY NSSLVVDDVK INLGLWDTAG
QEDYDRLRPL SYPSTDVFLV CFSVIAPASY ENVEGKWKPE IDQHCPNVPI ILVGTKIDIR
DDPEQVKRLA EKNIVPIQPP QGDELAKKIG AVKYIECSAL TQANLKLVFE EAVRAVLAKA
AKEPTGKKEK GGKKGCSLF
