ID   RACD_ENTHI              Reviewed;         198 AA.
AC   Q24817;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Rho-related protein racD;
DE   Flags: Precursor; Fragment;
GN   Name=RACD;
OS   Entamoeba histolytica.
OC   Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae;
OC   Entamoeba.
OX   NCBI_TaxID=5759;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=ATCC 30459 / HM-1:IMSS;
RX   PubMed=8964500; DOI=10.1016/0378-1119(96)00232-6;
RA   Lohia A., Samuelson J.;
RT   "Heterogeneity of Entamoeba histolytica rac genes encoding p21rac
RT   homologues.";
RL   Gene 173:205-208(1996).
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC       {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
CC       {ECO:0000305}.
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DR   EMBL; U30148; AAC47299.1; -; mRNA.
DR   PIR; PC4201; PC4201.
DR   AlphaFoldDB; Q24817; -.
DR   SMR; Q24817; -.
DR   STRING; 5759.rna_EHI_012240-1; -.
DR   PRIDE; Q24817; -.
DR   VEuPathDB; AmoebaDB:EHI5A_020530; -.
DR   VEuPathDB; AmoebaDB:EHI7A_026510; -.
DR   VEuPathDB; AmoebaDB:EHI8A_058280; -.
DR   VEuPathDB; AmoebaDB:EHI_012240; -.
DR   VEuPathDB; AmoebaDB:KM1_058210; -.
DR   eggNOG; KOG0393; Eukaryota.
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   2: Evidence at transcript level;
KW   Cell membrane; GTP-binding; Lipoprotein; Membrane; Methylation;
KW   Nucleotide-binding; Prenylation.
FT   CHAIN           <1..195
FT                   /note="Rho-related protein racD"
FT                   /id="PRO_0000198913"
FT   PROPEP          196..198
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000281290"
FT   MOTIF           37..45
FT                   /note="Effector region"
FT                   /evidence="ECO:0000255"
FT   BINDING         15..22
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         62..66
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         120..123
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         195
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000250"
FT   LIPID           195
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   198 AA;  22041 MW;  1BF0ACCDB40CDBDD CRC64;
     AAPTDAKSVK LVVVGDGSVG KTCLLICYTT NEFPKDYVPT VFDNYMAPMT VDGEPINLGL
     WDTAGQEDSE QLRPLSYPNT DLFLLCFSVI SRTSFNNISS KWLPEIKHYE PKCKMMVVGT
     NTDCRNDEAM IRKLADENQK PITTEEGEKL AKDIKAICYM ECSALTRSGL NQVFDEAIHI
     VLNKNQSSKK SSKKCALL