RACC_ENTHI
ID RACC_ENTHI Reviewed; 194 AA.
AC Q24816;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Rho-related protein racC;
DE Flags: Precursor;
GN Name=RACC;
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=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; U29722; AAC47298.1; -; Genomic_DNA.
DR PIR; JC4932; JC4932.
DR PDB; 4MIT; X-ray; 2.35 A; A/B/C/D=1-183.
DR PDBsum; 4MIT; -.
DR AlphaFoldDB; Q24816; -.
DR SMR; Q24816; -.
DR DIP; DIP-60102N; -.
DR IntAct; Q24816; 1.
DR STRING; 5759.rna_EHI_070730-1; -.
DR VEuPathDB; AmoebaDB:EHI5A_060860; -.
DR VEuPathDB; AmoebaDB:EHI7A_090820; -.
DR VEuPathDB; AmoebaDB:EHI8A_093900; -.
DR VEuPathDB; AmoebaDB:EHI_070730; -.
DR VEuPathDB; AmoebaDB:KM1_331620; -.
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 1: Evidence at protein level;
KW 3D-structure; Cell membrane; GTP-binding; Lipoprotein; Membrane;
KW Methylation; Nucleotide-binding; Prenylation.
FT CHAIN 1..191
FT /note="Rho-related protein racC"
FT /id="PRO_0000198912"
FT PROPEP 192..194
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000281260"
FT MOTIF 36..44
FT /note="Effector region"
FT /evidence="ECO:0000255"
FT BINDING 14..21
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 61..65
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 119..122
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 191
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 191
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT STRAND 6..15
FT /evidence="ECO:0007829|PDB:4MIT"
FT HELIX 20..29
FT /evidence="ECO:0007829|PDB:4MIT"
FT STRAND 40..50
FT /evidence="ECO:0007829|PDB:4MIT"
FT STRAND 53..62
FT /evidence="ECO:0007829|PDB:4MIT"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:4MIT"
FT TURN 69..71
FT /evidence="ECO:0007829|PDB:4MIT"
FT HELIX 72..75
FT /evidence="ECO:0007829|PDB:4MIT"
FT STRAND 80..87
FT /evidence="ECO:0007829|PDB:4MIT"
FT HELIX 91..99
FT /evidence="ECO:0007829|PDB:4MIT"
FT HELIX 101..108
FT /evidence="ECO:0007829|PDB:4MIT"
FT STRAND 114..119
FT /evidence="ECO:0007829|PDB:4MIT"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:4MIT"
FT HELIX 127..135
FT /evidence="ECO:0007829|PDB:4MIT"
FT HELIX 143..152
FT /evidence="ECO:0007829|PDB:4MIT"
FT STRAND 156..160
FT /evidence="ECO:0007829|PDB:4MIT"
FT TURN 163..165
FT /evidence="ECO:0007829|PDB:4MIT"
FT HELIX 169..181
FT /evidence="ECO:0007829|PDB:4MIT"
SQ SEQUENCE 194 AA; 21595 MW; 8D1DCD5D64F16696 CRC64;
MSEKPTSIKL VVVGDGAVGK TCLLICYTTN EFPKDYIPTV FDNYVVSLTA GTRQIQLALW
DTAGQEEYDQ LRPLSYSSAS IFLICFSVTS SVSYDNVITK WHPEVIHFAP KVPIILVGTK
LDTRNDPAIV KRLTEQGMTV INTAKGEELK NRIKAVKYIE CSAKTSENLK TVFDEAVKTV
LMNKPQQRSK CALL