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Database: UniProt
Entry: A0A120E936_9BASI
LinkDB: A0A120E936_9BASI
Original site: A0A120E936_9BASI 
ID   A0A120E936_9BASI        Unreviewed;       321 AA.
AC   A0A120E936;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=GTP-binding protein {ECO:0000256|RuleBase:RU367014};
GN   ORFNames=RHOSPDRAFT_28426 {ECO:0000313|EMBL:KWU46580.1};
OS   Rhodotorula sp. JG-1b.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX   NCBI_TaxID=1305733 {ECO:0000313|EMBL:KWU46580.1, ECO:0000313|Proteomes:UP000062823};
RN   [1] {ECO:0000313|EMBL:KWU46580.1, ECO:0000313|Proteomes:UP000062823}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JG-1b {ECO:0000313|EMBL:KWU46580.1,
RC   ECO:0000313|Proteomes:UP000062823};
RG   DOE Joint Genome Institute;
RA   Goordial J., Raymond-Bouchard I., Riley R., Ronholm J., Shapiro N.,
RA   Woyke T., Grigoriev I.V., Labutti K.M., Greer C., Whyte L., Bakermans C.;
RT   "Draft genome of eurypsychrophile Rhodotorula sp. JG1b isolated from
RT   permafrost in the hyper-arid Upper Elevation McMurdo Dry Valleys,
RT   Antarctica.";
RL   Submitted (DEC-2015) 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}.
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DR   EMBL; KQ954467; KWU46580.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A120E936; -.
DR   STRING; 1305733.A0A120E936; -.
DR   OrthoDB; 33171at2759; -.
DR   Proteomes; UP000062823; 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; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
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; 2.
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:UP000062823}.
FT   REGION          107..133
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   321 AA;  35068 MW;  626658ACCAB6EEEF CRC64;
     MGKSGSGKTS MRAIIFKSQL AADTRRLGAT IDVENSQIKF LGGLRLDLWD CGGQDSFMDS
     HLTAQSSTVF RSVHSLIYIF DAESPELLTS DTVYFLKCLR ALRDQNPTPS SSAASLNANG
     GPSGSTANGS TTVANDEGPT VFVLLHKMDL VPVDQQASKL AEFEGEVTKK AREGGYKGAM
     QFYGTSIWNE TLYKAWSVVM ANLMPSLSSL RTHLNHFLDL SGASEIVLFE RTTFLVISSW
     DERRFERIST MVKAFKLGCS KIRSPFSSLA VSTQHYTAVL DALSPETYIL VVAKETAALE
     LNIRLARPHF ATLEAIGMGR S
//
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