ID   A0A316Z8Z6_9BASI        Unreviewed;       344 AA.
AC   A0A316Z8Z6;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=GTP-binding protein {ECO:0000256|RuleBase:RU367014};
GN   ORFNames=FA09DRAFT_343597 {ECO:0000313|EMBL:PWN97458.1};
OS   Tilletiopsis washingtonensis.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Exobasidiomycetes; Entylomatales; Entylomatales incertae sedis;
OC   Tilletiopsis.
OX   NCBI_TaxID=58919 {ECO:0000313|EMBL:PWN97458.1, ECO:0000313|Proteomes:UP000245946};
RN   [1] {ECO:0000313|EMBL:PWN97458.1, ECO:0000313|Proteomes:UP000245946}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCA 4186 {ECO:0000313|EMBL:PWN97458.1,
RC   ECO:0000313|Proteomes:UP000245946};
RX   PubMed=29771364; DOI=10.1093/molbev/msy072;
RA   Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA   Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA   Spatafora J.W., Aime M.C.;
RT   "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT   clade Ustilaginomycotina.";
RL   Mol. Biol. Evol. 0:0-0(2018).
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; KZ819295; PWN97458.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A316Z8Z6; -.
DR   STRING; 58919.A0A316Z8Z6; -.
DR   OrthoDB; 33171at2759; -.
DR   Proteomes; UP000245946; Unassembled WGS sequence.
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; 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   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:UP000245946}.
FT   REGION          225..260
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   344 AA;  38553 MW;  73E4AC999704086A CRC64;
     MKKKILLMGR SGSGKTSMRS LVFSSYRPSD TRRLGSTLDV EHSHVRFLGN LVLNLWDCGG
     QQAYMDSYLD SQRHQVFSAV GVLIYVFDLV GEDGAGEEWE KDVRYYKDCL AALRVHSPDA
     RVFCLLHKMD LVDSSRRRSV YASRVAELRR KSEGKAITPF ATSIWDETLY RAWSSIVHTL
     IPQVGVLESH LSQFAQANSA TEVVVFERST FLVISRTTQG GSTLPVGASG FARPTGLPSE
     DDDDMEGFPE ERKGDDKGRL NPERFEKISE LIKSFKLSCS KLQSTFQAIE LRTPSFSAYL
     DALTANTFIM VVVADPRIEL AAIKLNVQSA REHFEKLPAL NINR
//