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Database: UniProt
Entry: A0A2K3Q7Y3_9HYPO
LinkDB: A0A2K3Q7Y3_9HYPO
Original site: A0A2K3Q7Y3_9HYPO 
ID   A0A2K3Q7Y3_9HYPO        Unreviewed;       358 AA.
AC   A0A2K3Q7Y3;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=GTP-binding protein {ECO:0000256|RuleBase:RU367014};
GN   ORFNames=TCAP_06388 {ECO:0000313|EMBL:PNY23672.1};
OS   Tolypocladium capitatum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Tolypocladium.
OX   NCBI_TaxID=45235 {ECO:0000313|EMBL:PNY23672.1, ECO:0000313|Proteomes:UP000236621};
RN   [1] {ECO:0000313|EMBL:PNY23672.1, ECO:0000313|Proteomes:UP000236621}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 113982 {ECO:0000313|EMBL:PNY23672.1,
RC   ECO:0000313|Proteomes:UP000236621};
RA   Quandt C.A., Patterson W., Spatafora J.W.;
RT   "Harnessing the power of phylogenomics to disentangle the directionality
RT   and signatures of interkingdom host jumping in the parasitic fungal genus
RT   Tolypocladium.";
RL   Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
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:PNY23672.1}.
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DR   EMBL; NRSZ01001059; PNY23672.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2K3Q7Y3; -.
DR   STRING; 45235.A0A2K3Q7Y3; -.
DR   OrthoDB; 33171at2759; -.
DR   Proteomes; UP000236621; 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:UP000236621}.
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   358 AA;  39843 MW;  5467A108176CE12C CRC64;
     MAPHSPADGP PADATPSEVR SEVKKPKKKK VLLMGKSGSG KSSMRSIIFS NYIARDTRRL
     GATIDIDLSH VKFLGNLTLN LWDCGGQEAF MENYLSQQRV HVFSNVGVLI YVFDIESRDV
     DRDLATYVSI LSALLQFSPA ANIYVLIHKM DLVVPSARES VYDERVRLVR QKTVEYVASV
     GCDASPAGLE LTPFATSIWD QSLYKAWASI IHDLVPNLSV IESNLANLGI AIEAEELLLF
     ERTSFLAVSS WTSPEGHRNP TEDRLERMSN IMKHFKQSIS RFTGTPRNAE QFIRMEHKAG
     MRFNLFILKF TTNTYLMVVL PPGEARFNAA MLNCQIAIEH FKFLDGPVSV AAPAATSA
//
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