ID F9XIP2_ZYMTI Unreviewed; 312 AA.
AC F9XIP2;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=GTP-binding protein {ECO:0000256|RuleBase:RU367014};
GN ORFNames=MYCGRDRAFT_101067 {ECO:0000313|EMBL:EGP85103.1};
OS Zymoseptoria tritici (strain CBS 115943 / IPO323) (Speckled leaf blotch
OS fungus) (Septoria tritici).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX NCBI_TaxID=336722 {ECO:0000313|EMBL:EGP85103.1, ECO:0000313|Proteomes:UP000008062};
RN [1] {ECO:0000313|EMBL:EGP85103.1, ECO:0000313|Proteomes:UP000008062}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 115943 / IPO323 {ECO:0000313|Proteomes:UP000008062};
RX PubMed=21695235; DOI=10.1371/journal.pgen.1002070;
RA Goodwin S.B., Ben M'barek S., Dhillon B., Wittenberg A.H.J., Crane C.F.,
RA Hane J.K., Foster A.J., Van der Lee T.A.J., Grimwood J., Aerts A.,
RA Antoniw J., Bailey A., Bluhm B., Bowler J., Bristow J., van der Burgt A.,
RA Canto-Canche B., Churchill A.C.L., Conde-Ferraez L., Cools H.J.,
RA Coutinho P.M., Csukai M., Dehal P., De Wit P., Donzelli B.,
RA van de Geest H.C., van Ham R.C.H.J., Hammond-Kosack K.E., Henrissat B.,
RA Kilian A., Kobayashi A.K., Koopmann E., Kourmpetis Y., Kuzniar A.,
RA Lindquist E., Lombard V., Maliepaard C., Martins N., Mehrabi R.,
RA Nap J.P.H., Ponomarenko A., Rudd J.J., Salamov A., Schmutz J.,
RA Schouten H.J., Shapiro H., Stergiopoulos I., Torriani S.F.F., Tu H.,
RA de Vries R.P., Waalwijk C., Ware S.B., Wiebenga A., Zwiers L.-H.,
RA Oliver R.P., Grigoriev I.V., Kema G.H.J.;
RT "Finished genome of the fungal wheat pathogen Mycosphaerella graminicola
RT reveals dispensome structure, chromosome plasticity, and stealth
RT pathogenesis.";
RL PLoS Genet. 7:E1002070-E1002070(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 -!- 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; CM001203; EGP85103.1; -; Genomic_DNA.
DR RefSeq; XP_003850127.1; XM_003850079.1.
DR AlphaFoldDB; F9XIP2; -.
DR STRING; 336722.F9XIP2; -.
DR EnsemblFungi; Mycgr3T101067; Mycgr3P101067; Mycgr3G101067.
DR GeneID; 13394403; -.
DR KEGG; ztr:MYCGRDRAFT_101067; -.
DR eggNOG; KOG3886; Eukaryota.
DR HOGENOM; CLU_044099_0_0_1; -.
DR InParanoid; F9XIP2; -.
DR OMA; LIPNMQD; -.
DR OrthoDB; 33171at2759; -.
DR Proteomes; UP000008062; Chromosome 8.
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 GO; GO:1904262; P:negative regulation of TORC1 signaling; IEA:EnsemblFungi.
DR GO; GO:1904263; P:positive regulation of TORC1 signaling; IEA:EnsemblFungi.
DR CDD; cd11384; RagA_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; IPR039397; RagA/B.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR11259; RAS-RELATED GTP BINDING RAG/GTR YEAST; 1.
DR PANTHER; PTHR11259:SF1; RAS-RELATED GTP-BINDING PROTEIN; 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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU367014};
KW Reference proteome {ECO:0000313|Proteomes:UP000008062}.
SQ SEQUENCE 312 AA; 35560 MW; 102C48676341D7A8 CRC64;
MSTSDRSKRH KQRKVLLMGR SGAGKSSMRS IIFSNYVAKD VRRLGATVDV EHANIKFMGN
LMLNLWDCGG QDSFVESYLT NQRSHVFTSV AVLIFVFDVS SKEAASDMLS FASTIRALKE
YSPNSKIFIL IHKMDLIRPD QKHNIYGHKM RDIRATCDDE GFHSAQVDFC PSSIWDQSLY
KAWTQVIYFL VPNANTIESM LQRLADLLDA REMILYERTT CLVVTHITRG NEERNPYTDR
FERISSILKT HKHSMSKHTG TMASEVSFAE MQIKTGSFMF FITRLTENTN LAVVMPSDEA
CFNAARNHAL VL
//
