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Database: UniProt
Entry: K2RQ14_MACPH
LinkDB: K2RQ14_MACPH
Original site: K2RQ14_MACPH 
ID   K2RQ14_MACPH            Unreviewed;       390 AA.
AC   K2RQ14;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   RecName: Full=GTP-binding protein {ECO:0000256|RuleBase:RU367014};
GN   ORFNames=MPH_10609 {ECO:0000313|EMBL:EKG12304.1};
OS   Macrophomina phaseolina (strain MS6) (Charcoal rot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC   Macrophomina.
OX   NCBI_TaxID=1126212 {ECO:0000313|EMBL:EKG12304.1, ECO:0000313|Proteomes:UP000007129};
RN   [1] {ECO:0000313|EMBL:EKG12304.1, ECO:0000313|Proteomes:UP000007129}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MS6 {ECO:0000313|EMBL:EKG12304.1,
RC   ECO:0000313|Proteomes:UP000007129};
RX   PubMed=22992219; DOI=10.1186/1471-2164-13-493;
RA   Islam M.S., Haque M.S., Islam M.M., Emdad E.M., Halim A., Hossen Q.M.M.,
RA   Hossain M.Z., Ahmed B., Rahim S., Rahman M.S., Alam M.M., Hou S., Wan X.,
RA   Saito J.A., Alam M.;
RT   "Tools to kill: Genome of one of the most destructive plant pathogenic
RT   fungi Macrophomina phaseolina.";
RL   BMC Genomics 13:493-493(2012).
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:EKG12304.1}.
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DR   EMBL; AHHD01000453; EKG12304.1; -; Genomic_DNA.
DR   AlphaFoldDB; K2RQ14; -.
DR   STRING; 1126212.K2RQ14; -.
DR   VEuPathDB; FungiDB:MPH_10609; -.
DR   eggNOG; KOG3887; Eukaryota.
DR   HOGENOM; CLU_047421_2_0_1; -.
DR   InParanoid; K2RQ14; -.
DR   OrthoDB; 166730at2759; -.
DR   Proteomes; UP000007129; 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   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU367014};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007129}.
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          52..73
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   390 AA;  44227 MW;  E2DF18ABE3A9E6D2 CRC64;
     MTSSYLSIPA RREPPGQEMG ESHHAAFDRF KPAAKLTLMR YLQDLQNAEI PPSPVAPRYH
     TGRLPNSKAG DGKPRLLLMG QRRSGKSSIS SVVFHKLPPS ETLYLETTTR IKKESMHSFM
     DFQVWDFPGH LDYFDPAFDV DNIFDEIGAL IWVIDAQDEY LDAITRLNTT ILNLQHSYPN
     INVEVFVHKV DGLSEDYKSD TYRDIIQRVQ DELSDAGYEN APVSFYQTSI YDHSIFEAFS
     KVIQKLIPQL PTLESLLNSL CSTCRIEKAY LFDVLSKIYI ATDTSPTDIG SYEICSDYID
     VVVDVSEIYG WDRPDENGHA DGGIEETGNN DAESLITMER KGNNYLYLRE INKYLALICL
     MGEDSPAEKK ALIDYNVGVF QEALAQVFPR
//
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