ID A0A367LGX0_9HYPO Unreviewed; 412 AA.
AC A0A367LGX0;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=GTP-binding protein {ECO:0000256|RuleBase:RU367014};
GN ORFNames=L249_7975 {ECO:0000313|EMBL:RCI13683.1};
OS Ophiocordyceps polyrhachis-furcata BCC 54312.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX NCBI_TaxID=1330021 {ECO:0000313|EMBL:RCI13683.1, ECO:0000313|Proteomes:UP000253664};
RN [1] {ECO:0000313|EMBL:RCI13683.1, ECO:0000313|Proteomes:UP000253664}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCC 54312 {ECO:0000313|EMBL:RCI13683.1,
RC ECO:0000313|Proteomes:UP000253664};
RX PubMed=26511477; DOI=10.1186/s12864-015-2101-4;
RA Wichadakul D., Kobmoo N., Ingsriswang S., Tangphatsornruang S.,
RA Chantasingh D., Luangsa-ard J.J., Eurwilaichitr L.;
RT "Insights from the genome of Ophiocordyceps polyrhachis-furcata to
RT pathogenicity and host specificity in insect fungi.";
RL BMC Genomics 16:881-881(2015).
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 -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC Evidence={ECO:0000256|ARBA:ARBA00001702};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000256|ARBA:ARBA00001702};
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:RCI13683.1}.
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DR EMBL; LKCN02000005; RCI13683.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A367LGX0; -.
DR STRING; 1330021.A0A367LGX0; -.
DR Proteomes; UP000253664; 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; cd11385; RagC_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; IPR039400; RagC/D.
DR PANTHER; PTHR11259:SF2; GH16429P; 1.
DR PANTHER; PTHR11259; RAS-RELATED GTP BINDING RAG/GTR YEAST; 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 Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU367014};
KW Reference proteome {ECO:0000313|Proteomes:UP000253664}.
FT REGION 50..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 412 AA; 46030 MW; D061B780CF2A1450 CRC64;
MTLNPRIRGE LPPALSDDDV ALRLPGVLTP AMLNLRRIYA QASSAAAARA PAGSRDEAPS
KQLSGEVAPL PSSSSSQPAA KGKPRLLLMG QRRSGKSSIS SVVFHKLPPN ETLFLESTAR
IQKDSMASFM DFQVWDFPGQ IDVFENPNFD MDAIFGEIGA LIWVIDAQDD YLEAVARLNS
TILALQGHYP NINIEVFIHK VDGLSDDYKL DIQRDITIRI QDELSDNGFE NAPVTFHLTS
IYNHSIFEAF SRVIQKLIPR LGTLESMLTN LCRTCRFEKA YLFDVLSKIY IATDSATADM
ASYEICSDYI DVIIDITEVY GTWHRSDASR QKLEAEPWNA KLEHQIGCST AESCLVLHDS
NKPIMLREVD RYLALVAIMK DDSYDRMPLV NMNVEAVVEG LTEFFDITKP TK
//