ID   CRL1_CANAW              Reviewed;         346 AA.
AC   P33153; C4YFB9;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   19-OCT-2011, sequence version 2.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=GTP-binding RHO-like protein;
DE   Flags: Precursor;
GN   Name=CRL1; Synonyms=RHO4; ORFNames=CAWG_01235;
OS   Candida albicans (strain WO-1) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=294748;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=WO-1;
RX   PubMed=1409649; DOI=10.1073/pnas.89.20.9410;
RA   Whiteway M., Dignard D., Thomas D.Y.;
RT   "Dominant negative selection of heterologous genes: isolation of Candida
RT   albicans genes that interfere with Saccharomyces cerevisiae mating factor-
RT   induced cell cycle arrest.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:9410-9414(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WO-1;
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA   Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA   Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA   Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA   Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA   Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA   Birren B.W., Kellis M., Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
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; M83991; AAA34337.2; -; Genomic_DNA.
DR   EMBL; CH672346; EEQ43005.1; -; Genomic_DNA.
DR   PIR; D47211; D47211.
DR   AlphaFoldDB; P33153; -.
DR   SMR; P33153; -.
DR   STRING; 5476.P33153; -.
DR   EnsemblFungi; EEQ43005; EEQ43005; CAWG_01235.
DR   VEuPathDB; FungiDB:CAWG_01235; -.
DR   HOGENOM; CLU_041217_21_1_1; -.
DR   OMA; KEIWFPE; -.
DR   Proteomes; UP000001429; Chromosome 1, Supercontig 1.1.
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; GTP-binding; Lipoprotein; Membrane; Methylation;
KW   Nucleotide-binding; Prenylation.
FT   CHAIN           1..343
FT                   /note="GTP-binding RHO-like protein"
FT                   /id="PRO_0000198950"
FT   PROPEP          344..346
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000281280"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          259..294
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           104..112
FT                   /note="Effector region"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        261..294
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         82..89
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         130..134
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         188..191
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         343
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000250"
FT   LIPID           343
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   346 AA;  39090 MW;  51555D8B5240364D CRC64;
     MTPNGSRRHS AYMGSPRSQH SSTMETGYNP YEAVQKKQEL YQNNNGNSPT VIIEEDPYIP
     NYKESSLANK KTNYNMKIVV VGDGGCGKTC LLLAYTQNKF PSIYVPTVFE NYVTAVQSPN
     GKTVELALWD TAGQEEYDRL RPLSYPDVDI LLVCFAVDNE VSLENVKDMW FPEVNHYCPG
     IPIILVGTKS DLSSDMNHDA SIRVAKEIGA IGLIFTSAKT MFNVRTVFNF ALNHFQRNME
     LQEQYEKTLG SRKRISRVLG GSNGGSGNHS RHHSRNYSNV SNNRRGHLKN TSYDSTALLD
     QPLTEDTYVK NPYGNFGYKA NVESPYNQDE FAFTRERKKK KKCVIL