RASL_COLTR
ID RASL_COLTR Reviewed; 214 AA.
AC O42785;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Ras-like protein;
DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P01116};
DE AltName: Full=Ct-Ras;
DE Flags: Precursor;
GN Name=RAS;
OS Colletotrichum trifolii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum orbiculare species complex.
OX NCBI_TaxID=5466;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Race 1;
RX PubMed=10503535; DOI=10.1007/s004380051058;
RA Truesdell G.M., Jones C., Holt T., Henderson G., Dickman M.B.;
RT "A Ras protein from a phytopathogenic fungus causes defects in hyphal
RT growth polarity, and induces tumors in mice.";
RL Mol. Gen. Genet. 262:46-54(1999).
CC -!- FUNCTION: Ras proteins bind GDP/GTP and possess intrinsic GTPase
CC activity.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2;
CC Evidence={ECO:0000250|UniProtKB:P01116};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
CC {ECO:0000305}.
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DR EMBL; AF044895; AAC03781.1; -; mRNA.
DR AlphaFoldDB; O42785; -.
DR SMR; O42785; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0007165; P: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; IPR020849; Small_GTPase_Ras-type.
DR PANTHER; PTHR24070; PTHR24070; 1.
DR Pfam; PF00071; Ras; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51421; RAS; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; GTP-binding; Hydrolase; Lipoprotein; Membrane; Methylation;
KW Nucleotide-binding; Prenylation.
FT CHAIN 1..211
FT /note="Ras-like protein"
FT /id="PRO_0000082702"
FT PROPEP 212..214
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000281356"
FT MOTIF 37..45
FT /note="Effector region"
FT /evidence="ECO:0000305"
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 121..124
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 211
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 211
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 214 AA; 24060 MW; 263328E2C9A181C5 CRC64;
MASKFLREYK LVVVGGGGVG KSCLTIQLIQ SHFVDEYDPT IEDSYRKQCV IDEEVALLDV
LDTAGQEEYS AMREQYMRTG EGFLLVYSIT SRQSFEEITT FQQQILRVKD KDYFPMVVVG
NKCDLEGERE VTRQEGEALA KSFGCKFIET SAKSRINVDK AFYDIVREIR RYNREMQGYS
TGSGGASGIN GPPKPMDVEN GEQEAGCCSK CLIM
