ID   A0A0B4HTB6_METMF        Unreviewed;       358 AA.
AC   A0A0B4HTB6;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=GTP-binding protein {ECO:0000256|RuleBase:RU367014};
DE   Flags: Fragment;
GN   ORFNames=MAJ_08483 {ECO:0000313|EMBL:KID95542.1};
OS   Metarhizium majus (strain ARSEF 297).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium;
OC   Metarhizium majus.
OX   NCBI_TaxID=1276143 {ECO:0000313|EMBL:KID95542.1, ECO:0000313|Proteomes:UP000031176};
RN   [1] {ECO:0000313|EMBL:KID95542.1, ECO:0000313|Proteomes:UP000031176}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ARSEF 297 {ECO:0000313|EMBL:KID95542.1,
RC   ECO:0000313|Proteomes:UP000031176};
RX   PubMed=25368161; DOI=10.1073/pnas.1412662111;
RA   Hu X., Xiao G., Zheng P., Shang Y., Su Y., Zhang X., Liu X., Zhan S.,
RA   St Leger R.J., Wang C.;
RT   "Trajectory and genomic determinants of fungal-pathogen speciation and host
RT   adaptation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:16796-16801(2014).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KID95542.1}.
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DR   EMBL; AZNE01000073; KID95542.1; -; Genomic_DNA.
DR   RefSeq; XP_014574536.1; XM_014719050.1.
DR   AlphaFoldDB; A0A0B4HTB6; -.
DR   HOGENOM; CLU_044099_0_0_1; -.
DR   OrthoDB; 33171at2759; -.
DR   Proteomes; UP000031176; 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:UP000031176}.
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KID95542.1"
SQ   SEQUENCE   358 AA;  40177 MW;  59EA5B84C756E600 CRC64;
     MTPHPDHPPA DAGPSEVRNE VKKPKKKKVL LMGKSGSGKS SMRSIIFSNY IARDTRRLGA
     TIDIDLSHVK FLGNLTLNLW DCGGQEAFME NYLSQQRVHV FSNVGVLIYV FDIESRDVDR
     DLATYVSILS ALLQYSPAAK IYILIHKMDL VVPTARETVY DERVRTVKQK TAEYINSVGG
     DTSTVELTPF ATSIWDQSLY KAWASIIHDL VPNLAVIERN LANLGVAIEA EELLLFERTS
     FLAVSSWTST EGRRNPTEDR LERMSNIMKH FKQSISRFTG TPRNAEQFIR MEHKAGTRFN
     LFILKFTTNT YLMVVLPPGE ARFNAAMLNC QIAIEHFKFL DGPAPHAVTA TVVPPASS
//