RAS1_MAGO7
ID RAS1_MAGO7 Reviewed; 241 AA.
AC G4N1S3;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 52.
DE RecName: Full=Ras-like protein 1;
DE Flags: Precursor;
GN Name=RAS1 {ECO:0000303|PubMed:17056708, ECO:0000303|PubMed:24835254};
GN ORFNames=MGG_09499;
OS Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS fungus) (Pyricularia oryzae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX NCBI_TaxID=242507;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX PubMed=15846337; DOI=10.1038/nature03449;
RA Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL Nature 434:980-986(2005).
RN [2]
RP INTERACTION WITH MST50.
RX PubMed=17056708; DOI=10.1105/tpc.105.038422;
RA Park G., Xue C., Zhao X., Kim Y., Orbach M., Xu J.R.;
RT "Multiple upstream signals converge on the adaptor protein Mst50 in
RT Magnaporthe grisea.";
RL Plant Cell 18:2822-2835(2006).
RN [3]
RP DISRUPTION PHENOTYPE.
RX PubMed=24835254; DOI=10.1094/mpmi-02-14-0052-r;
RA Zhou X., Zhao X., Xue C., Dai Y., Xu J.R.;
RT "Bypassing both surface attachment and surface recognition requirements for
RT appressorium formation by overactive ras signaling in Magnaporthe oryzae.";
RL Mol. Plant Microbe Interact. 27:996-1004(2014).
RN [4]
RP SUBCELLULAR LOCATION, INTERACTION WITH RAM1, MUTAGENESIS OF CYS-238, AND
RP ISOPRENYLATION AT CYS-238.
RX PubMed=31250536; DOI=10.1111/mpp.12838;
RA Aboelfotoh Hendy A., Xing J., Chen X., Chen X.L.;
RT "The farnesyltransferase beta-subunit RAM1 regulates localization of RAS
RT proteins and appressorium-mediated infection in Magnaporthe oryzae.";
RL Mol. Plant Pathol. 20:1264-1278(2019).
CC -!- FUNCTION: Modulates the activity of the adenylate cyclase catalytic
CC subunit and therefore affects the biosynthesis of cyclic-AMP (By
CC similarity). Plays a role in both surface attachment and surface
CC recognition of appressoria, a highly specialized infection structure
CC for plant penetration. Regulates appressorium formation by coordinated
CC regulation of cAMP signaling and Pmk1 MAPK pathways (By similarity).
CC {ECO:0000250|UniProtKB:G4MZY8, ECO:0000250|UniProtKB:P01119}.
CC -!- ACTIVITY REGULATION: Alternates between an inactive form bound to GDP
CC and an active form bound to GTP. Activated by a guanine nucleotide-
CC exchange factor (GEF) and inactivated by a GTPase-activating protein
CC (GAP). {ECO:0000250|UniProtKB:P01119}.
CC -!- SUBUNIT: Interacts with farnesyltransferase beta subunit RAM1.
CC {ECO:0000269|PubMed:31250536}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15846337};
CC Lipid-anchor {ECO:0000269|PubMed:15846337}; Cytoplasmic side
CC {ECO:0000269|PubMed:15846337}.
CC -!- DISRUPTION PHENOTYPE: Displays slight reduction in conidiation, but
CC normal growth, appressorium formation, and plant infection.
CC {ECO:0000269|PubMed:24835254}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
CC {ECO:0000305}.
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DR EMBL; CM001233; EHA52438.1; -; Genomic_DNA.
DR RefSeq; XP_003712245.1; XM_003712197.1.
DR AlphaFoldDB; G4N1S3; -.
DR SMR; G4N1S3; -.
DR STRING; 318829.MGG_09499T0; -.
DR EnsemblFungi; MGG_09499T0; MGG_09499T0; MGG_09499.
DR GeneID; 2680536; -.
DR KEGG; mgr:MGG_09499; -.
DR VEuPathDB; FungiDB:MGG_09499; -.
DR eggNOG; KOG0395; Eukaryota.
DR HOGENOM; CLU_041217_9_8_1; -.
DR InParanoid; G4N1S3; -.
DR OMA; CYRKQWV; -.
DR OrthoDB; 1259506at2759; -.
DR Proteomes; UP000009058; Chromosome 3.
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: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 1: Evidence at protein level;
KW Cell membrane; GTP-binding; Lipoprotein; Membrane; Methylation;
KW Nucleotide-binding; Prenylation; Reference proteome.
FT CHAIN 1..241
FT /note="Ras-like protein 1"
FT /id="PRO_0000449939"
FT PROPEP 239..241
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:P01119"
FT /id="PRO_0000449940"
FT REGION 190..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 36..44
FT /note="Effector region"
FT /evidence="ECO:0000250|UniProtKB:P01119"
FT COMPBIAS 190..213
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..241
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 17..22
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P01112"
FT BINDING 33..39
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P01112"
FT BINDING 63..64
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P01112"
FT BINDING 138..141
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P01112"
FT BINDING 168..170
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P01112"
FT MOD_RES 238
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250|UniProtKB:P01119"
FT LIPID 238
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000305|PubMed:31250536"
FT MUTAGEN 238
FT /note="C->S: Prevents farnesylation and restricts
FT subcellular location to the cytoplasm in appressorium,
FT mycelium, conidium and infection hyphae."
FT /evidence="ECO:0000269|PubMed:31250536"
SQ SEQUENCE 241 AA; 26892 MW; 34EDB88C26BFF0E8 CRC64;
MTGRLQLHKL VVLGDGGVGK TALTIQLCLQ HFVETYDPTI EDSYRKQVVI DNQACMLEVL
DTAGQEEYTA LRDQWIRDGE GFVLVYSISS RSSFSRIKRF HHQIQRVKES CASSPSYPGS
PIATVTTQAP VPIMLVGNKS DRVTEREVST QEGHALAREL GCEFVEASAK NCINVEKAFY
DVVRILRRQR QQASRPSLPG NSRTKTGGMG KSESFYQSDG KRGSRKDGEK HRSKPIKCVI
L
