ID   A0A316UAJ8_9BASI        Unreviewed;       378 AA.
AC   A0A316UAJ8;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=GTP-binding protein {ECO:0000256|RuleBase:RU367014};
GN   ORFNames=BCV69DRAFT_250084 {ECO:0000313|EMBL:PWN20055.1};
OS   Pseudomicrostroma glucosiphilum.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Exobasidiomycetes; Microstromatales; Microstromatales incertae sedis;
OC   Pseudomicrostroma.
OX   NCBI_TaxID=1684307 {ECO:0000313|EMBL:PWN20055.1, ECO:0000313|Proteomes:UP000245942};
RN   [1] {ECO:0000313|EMBL:PWN20055.1, ECO:0000313|Proteomes:UP000245942}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCA 4718 {ECO:0000313|EMBL:PWN20055.1,
RC   ECO:0000313|Proteomes:UP000245942};
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; KZ819329; PWN20055.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A316UAJ8; -.
DR   STRING; 1684307.A0A316UAJ8; -.
DR   OrthoDB; 33171at2759; -.
DR   Proteomes; UP000245942; 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   Gene3D; 3.30.450.190; -; 2.
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   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:UP000245942}.
FT   REGION          236..283
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        245..269
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   378 AA;  42012 MW;  0853D09E096A22EC CRC64;
     MKKKILLMGR SGCGKTSMRA LVFSSALYSN PASTQRLGPT TGMELSTFRF LKNLLINLFD
     CGGQQTYMDS YVEDKREQVF KDVGAFVYVF DMGSANNEEG EDGWQGDLRY WRDCLKILRQ
     LSPNAHVVCL LHKMDLLNSA RRQDIYTDRV KDLRGKAKEL GATELSCYGT SIWDETLYRA
     WSRIIHELIP NIATLESNLT EFTKITAATE AVIFEKTTFL VIARSGGDTV AKSVGGAADK
     AKASTGAGSS PSSKRAATTN RLSTVSSHGT LADDKERDSL LEGYPPTEAE RKALLARGEM
     HPERFEKISE LVKNLRGSCN KLQASFESFE VRGATFSAYL DVFTENTYIM VIVADPRVEL
     SAIKLNVQLG RERFEKLG
//