ID U4L206_PYROM Unreviewed; 446 AA.
AC U4L206;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=GTP-binding protein {ECO:0000256|RuleBase:RU367014};
GN ORFNames=PCON_08474 {ECO:0000313|EMBL:CCX08881.1};
OS Pyronema omphalodes (strain CBS 100304) (Pyronema confluens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC Pezizales; Pyronemataceae; Pyronema.
OX NCBI_TaxID=1076935 {ECO:0000313|EMBL:CCX08881.1};
RN [1] {ECO:0000313|EMBL:CCX08881.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS100304 {ECO:0000313|EMBL:CCX08881.1};
RC TISSUE=Vegetative mycelium {ECO:0000313|EMBL:CCX08881.1};
RX PubMed=24068976; DOI=10.1371/journal.pgen.1003820;
RA Traeger S., Altegoer F., Freitag M., Gabaldon T., Kempken F., Kumar A.,
RA Marcet-Houben M., Poggeler S., Stajich J.E., Nowrousian M.;
RT "The genome and development-dependent transcriptomes of Pyronema confluens:
RT a window into fungal evolution.";
RL PLoS Genet. 9:E1003820-E1003820(2013).
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}.
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DR EMBL; HF935434; CCX08881.1; -; Genomic_DNA.
DR AlphaFoldDB; U4L206; -.
DR STRING; 1076935.U4L206; -.
DR eggNOG; KOG3887; Eukaryota.
DR OMA; NCRTFQE; -.
DR OrthoDB; 166730at2759; -.
DR Proteomes; UP000018144; 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}.
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 61..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 327..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 446 AA; 50347 MW; A87FC8C3BF11E90D CRC64;
MTSFYTHLPL PADPPNTSPE RRSSYSLERF LQEPEQKELS PASSIEARYL DTAEIALRHK
RMQDQQSPVN SMGAYGLPPP GQQRGRPRLL LMGQRRSGKS SISSVVFHKM PPMETLFLES
TTKIQKDPIH SFMDFQVWDF PGQLDYLDDT FDFDNIFGEL GALIWVIDAQ DEILDPLSRL
HSTIIALQRS YPMINIEVFI HKVDGLSDEY KLDTMRDIMQ RTQDELADAG FDNVQISYHL
TSIYDHSIFE AFSKVIQKLL PQLGTLENLL NVLCSNSGIE KAFLFDVLSK IYIATDSSPV
DVQSYEICSD FIDVIVDVSE IYGYDRKNPD EAAQPSPPVS PGAAPAENTQ EVSSIIKLQN
GMVLYLREIN KFLALICLMR KESIEKKGLV DYNVQIFQNA LQRVFELGGG VRVALAQGPD
EEEQQEAAHP EPWYRRLCVE GSGGAN
//
