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Database: UniProt
Entry: D4B136_ARTBC
LinkDB: D4B136_ARTBC
Original site: D4B136_ARTBC 
ID   D4B136_ARTBC            Unreviewed;       462 AA.
AC   D4B136;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   RecName: Full=GTP-binding protein {ECO:0000256|RuleBase:RU367014};
GN   ORFNames=ARB_02165 {ECO:0000313|EMBL:EFE30971.1};
OS   Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS   mentagrophytes).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=663331 {ECO:0000313|EMBL:EFE30971.1, ECO:0000313|Proteomes:UP000008866};
RN   [1] {ECO:0000313|Proteomes:UP000008866}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4681 / CBS 112371 {ECO:0000313|Proteomes:UP000008866};
RX   PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA   Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA   Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA   Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA   Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA   Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT   "Comparative and functional genomics provide insights into the
RT   pathogenicity of dermatophytic fungi.";
RL   Genome Biol. 12:R7.1-R7.16(2011).
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:EFE30971.1}.
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DR   EMBL; ABSU01000025; EFE30971.1; -; Genomic_DNA.
DR   RefSeq; XP_003011611.1; XM_003011565.1.
DR   AlphaFoldDB; D4B136; -.
DR   STRING; 663331.D4B136; -.
DR   GeneID; 9523382; -.
DR   KEGG; abe:ARB_02165; -.
DR   eggNOG; KOG3887; Eukaryota.
DR   HOGENOM; CLU_047421_2_0_1; -.
DR   OMA; ICNHQAS; -.
DR   OrthoDB; 166730at2759; -.
DR   Proteomes; UP000008866; 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:UP000008866}.
SQ   SEQUENCE   462 AA;  53769 MW;  ECB3240907C7CB89 CRC64;
     MFARETVIFF FQLGFFFLFF LVFLFFSGSA LHLLLPPPLR QGIRWNGYVP YPLDATFYSS
     RPFILRIVDW FDTSNLTVWD MLCSAVIWRY QGQERLIYSN TSLLHGHPPV IKTRAQLSLE
     ENLQANVPQS QAATRPAQIS NPKFRETRPR LLLMGLRRSG KSSIQSVVFH KMPPTETLFL
     ESTTRIQKDA IHSFMDFQIW DFPGQLEYLE PSFDQEELFS NLGALVWVID AQDDYLEAVT
     RLNKTILMIQ QYYPHINIEV FIHKVDGLSE EYRSDTFQDI VQRISDELSD AGYENAPIHY
     YLTSIYDYSV FEAFSKVIQK LIPQLSTLEN LINILSNNSG MEKTYLFDVL SKIYIASDTR
     PVDMACYEMC SDYIDVIVDI SELYSWDHPD RKAKGPQVSE AESHVILHDK CMIHLMEMNK
     YLCLVSVIKN PDAKEKKGLI DMNCRTFQDA LNEVFSRTWD QE
//
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