ID E5A7R9_LEPMJ Unreviewed; 361 AA.
AC E5A7R9;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=GTP-binding protein {ECO:0000256|RuleBase:RU367014};
GN ORFNames=LEMA_P089030.1 {ECO:0000313|EMBL:CBX99664.1};
OS Leptosphaeria maculans (strain JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8)
OS (Blackleg fungus) (Phoma lingam).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Leptosphaeriaceae;
OC Plenodomus; Plenodomus lingam/Leptosphaeria maculans species complex.
OX NCBI_TaxID=985895 {ECO:0000313|EMBL:CBX99664.1, ECO:0000313|Proteomes:UP000002668};
RN [1] {ECO:0000313|Proteomes:UP000002668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8
RC {ECO:0000313|Proteomes:UP000002668};
RX PubMed=21326234; DOI=10.1038/ncomms1189;
RA Rouxel T., Grandaubert J., Hane J.K., Hoede C., van de Wouw A.P.,
RA Couloux A., Dominguez V., Anthouard V., Bally P., Bourras S.,
RA Cozijnsen A.J., Ciuffetti L.M., Degrave A., Dilmaghani A., Duret L.,
RA Fudal I., Goodwin S.B., Gout L., Glaser N., Linglin J., Kema G.H.J.,
RA Lapalu N., Lawrence C.B., May K., Meyer M., Ollivier B., Poulain J.,
RA Schoch C.L., Simon A., Spatafora J.W., Stachowiak A., Turgeon B.G.,
RA Tyler B.M., Vincent D., Weissenbach J., Amselem J., Quesneville H.,
RA Oliver R.P., Wincker P., Balesdent M.-H., Howlett B.J.;
RT "Effector diversification within compartments of the Leptosphaeria maculans
RT genome affected by Repeat-Induced Point mutations.";
RL Nat. Commun. 2:202-202(2011).
CC -!- FUNCTION: GTPase involved in activation of the TORC1 signaling pathway,
CC which promotes growth and represses autophagy in nutrient-rich
CC conditions. {ECO:0000256|RuleBase:RU367014}.
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;
CC Evidence={ECO:0000256|ARBA:ARBA00001702};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000256|ARBA:ARBA00001702};
CC -!- SUBUNIT: Component of the GSE complex. {ECO:0000256|RuleBase:RU367014}.
CC -!- SIMILARITY: Belongs to the GTR/RAG GTP-binding protein family.
CC {ECO:0000256|ARBA:ARBA00007756, ECO:0000256|RuleBase:RU367014}.
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DR EMBL; FP929136; CBX99664.1; -; Genomic_DNA.
DR RefSeq; XP_003843143.1; XM_003843095.1.
DR AlphaFoldDB; E5A7R9; -.
DR STRING; 985895.E5A7R9; -.
DR EnsemblFungi; CBX99664; CBX99664; LEMA_P089030.1.
DR GeneID; 13289148; -.
DR eggNOG; KOG3887; Eukaryota.
DR HOGENOM; CLU_047421_2_0_1; -.
DR InParanoid; E5A7R9; -.
DR OMA; NCRTFQE; -.
DR OrthoDB; 166730at2759; -.
DR Proteomes; UP000002668; Genome.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IEA:EnsemblFungi.
DR GO; GO:1990131; C:Gtr1-Gtr2 GTPase complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR CDD; cd11385; RagC_like; 1.
DR Gene3D; 3.30.450.190; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR006762; Gtr1_RagA.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR039400; RagC/D.
DR PANTHER; PTHR11259:SF2; GH16429P; 1.
DR PANTHER; PTHR11259; RAS-RELATED GTP BINDING RAG/GTR YEAST; 1.
DR Pfam; PF04670; Gtr1_RagA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|RuleBase:RU367014};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU367014};
KW Reference proteome {ECO:0000313|Proteomes:UP000002668}.
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 361 AA; 41140 MW; 87CD892A762F5559 CRC64;
MEDLPNAELP PSSDYPPQYH TGRVPNSKAG DGKPRLLLMG QRRSGKSSIS SVVFHKLPPS
ETLYLETTYR IKKESMHSFM DFQVWDLPGH LDYFDPAFDT DNIFEEIGAL IWVIDAQDEY
LDAIARLNMT ILNLQQSYPN INVEVFVHKV DGLSDDFRGD TFRDIIQRVQ DELSDNGYEQ
APISFYQTSI YDHSIFEAFS KVIQKLIPQL PTLEALLNNL CGACNIEKAY LFDIMSKIYI
ATDTSPTDIG SYEICSDYID VVIDVSEIYG WDRLDEEPDE SETGNNDAES LITMEKKNSR
YLYLREINKY LALVCIMGQD NPAEKKAIID YNVGVFQAGL KQVFPKSDRE AQIEIRAAND
D
//
