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CDC42_COLGL
ID   CDC42_COLGL             Reviewed;         190 AA.
AC   O94103;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Cell division control protein 42 homolog;
DE   Flags: Precursor;
GN   Name=CDC42;
OS   Colletotrichum gloeosporioides (Anthracnose fungus) (Glomerella cingulata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum gloeosporioides species complex.
OX   NCBI_TaxID=474922;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Liu Z.-M., Kolattukudy P.E.;
RT   "cdc42 homolog in Colletotrichum gloeosporioides.";
RL   Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
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. CDC42
CC       subfamily. {ECO:0000305}.
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DR   EMBL; U70875; AAD00177.1; -; Genomic_DNA.
DR   AlphaFoldDB; O94103; -.
DR   SMR; O94103; -.
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:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
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 cycle; Cell division; Cell membrane; GTP-binding; Lipoprotein;
KW   Membrane; Methylation; Nucleotide-binding; Prenylation.
FT   CHAIN           1..187
FT                   /note="Cell division control protein 42 homolog"
FT                   /id="PRO_0000198953"
FT   PROPEP          188..190
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000281283"
FT   MOTIF           34..42
FT                   /note="Effector region"
FT                   /evidence="ECO:0000250"
FT   BINDING         12..19
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         59..63
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         117..120
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         187
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000250"
FT   LIPID           187
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   190 AA;  20660 MW;  A7C1E37A901A648E CRC64;
     MVVATIKCVV VGDGAVGKTC LLISYTTNKF PSEYVPTVFD NYAVTVMIGD EPYTLGLFDT
     AGQEDYDRLR PLSYPQTDVF LVCFSVTSPA SFENVARSGS RGTSPLPGVL LIVAPVTERG
     SSVREKLSKQ KMSPVRKEDG ERMAKDLGAV KYVECSALTQ FKLKDVFDEA IVAALEPPAP
     KKKSHKCLVL
 
 
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