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Database: UniProt
Entry: A0A177WGB8_BATDL
LinkDB: A0A177WGB8_BATDL
Original site: A0A177WGB8_BATDL 
ID   A0A177WGB8_BATDL        Unreviewed;       375 AA.
AC   A0A177WGB8;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=GTP-binding protein {ECO:0000256|RuleBase:RU367014};
GN   ORFNames=BDEG_22726 {ECO:0000313|EMBL:OAJ38826.1};
OS   Batrachochytrium dendrobatidis (strain JEL423).
OC   Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC   Chytridiomycota incertae sedis; Chytridiomycetes; Rhizophydiales;
OC   Rhizophydiales incertae sedis; Batrachochytrium.
OX   NCBI_TaxID=403673 {ECO:0000313|EMBL:OAJ38826.1, ECO:0000313|Proteomes:UP000077115};
RN   [1] {ECO:0000313|EMBL:OAJ38826.1, ECO:0000313|Proteomes:UP000077115}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JEL423 {ECO:0000313|EMBL:OAJ38826.1,
RC   ECO:0000313|Proteomes:UP000077115};
RG   The Broad Institute Genome Sequencing Platform;
RA   Birren B., Lander E., Galagan J., Cuomo C., Devon K., Jaffe D., Butler J.,
RA   Alvarez P., Gnerre S., Grabherr M., Kleber M., Mauceli E., Brockman W.,
RA   Young S., LaButti K., Sykes S., DeCaprio D., Crawford M., Koehrsen M.,
RA   Engels R., Montgomery P., Pearson M., Howarth C., Larson L., White J.,
RA   O'Leary S., Kodira C., Zeng Q., Yandava C., Alvarado L., Longcore J.,
RA   James T.;
RT   "The Genome Sequence of Batrachochytrium dendrobatidis JEL423.";
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:OAJ38826.1, ECO:0000313|Proteomes:UP000077115}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JEL423 {ECO:0000313|EMBL:OAJ38826.1,
RC   ECO:0000313|Proteomes:UP000077115};
RA   Cuomo C.A., Farrer R.A., James T., Longcore J., Birren B.;
RT   "Lineage-specific infection strategies underlie the spectrum of fungal
RT   disease in amphibians.";
RL   Submitted (MAY-2016) 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   -!- 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; DS022302; OAJ38826.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A177WGB8; -.
DR   STRING; 403673.A0A177WGB8; -.
DR   VEuPathDB; FungiDB:BDEG_22726; -.
DR   eggNOG; KOG3887; Eukaryota.
DR   Proteomes; UP000077115; Unassembled WGS sequence.
DR   GO; GO:1990131; C:Gtr1-Gtr2 GTPase complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU367014};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077115};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        356..373
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          301..321
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   375 AA;  41792 MW;  9C571F82438D48D9 CRC64;
     MATELFFNSH VSVNIRYGSS DIASAKSQSA SSTIPGQIFG SSIETPLASS GVANKPRLLI
     IGLRRSGKSS ILNVVFHKMP PNETIFLEST TVVSRYDILP FLDLQLWDFP GHVDVCDPSF
     DPVLLFQQCG AVMFVVDAQD DYLEALERLH STIFKAFRIN PDISFEIFVH KVDGLSDDHK
     IETKRDIYQR LYDDLGDVGV NAANLSFHLT SIYDHSVFEA FSKVIQKLIP QLATLENLLN
     MLCSNTGIEK AFLFDMASKI YIATDSSPVD MQSYELCSDM IDVVLDISSI YSGATVQGSV
     ASSTQSPEQP NSPLRRVNPL GDDNYQVESY ASIRLNNGMA LYLRRVNQLS VAAMSIYQYP
     AFIILLTHFF CLFRL
//
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