ID K1X367_MARBU Unreviewed; 406 AA.
AC K1X367;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=GTP-binding protein {ECO:0000256|RuleBase:RU367014};
GN ORFNames=MBM_02714 {ECO:0000313|EMBL:EKD19477.1};
OS Marssonina brunnea f. sp. multigermtubi (strain MB_m1) (Marssonina leaf
OS spot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Drepanopezizaceae; Drepanopeziza.
OX NCBI_TaxID=1072389 {ECO:0000313|EMBL:EKD19477.1, ECO:0000313|Proteomes:UP000006753};
RN [1] {ECO:0000313|EMBL:EKD19477.1, ECO:0000313|Proteomes:UP000006753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MB_m1 {ECO:0000313|EMBL:EKD19477.1,
RC ECO:0000313|Proteomes:UP000006753};
RX PubMed=22876864; DOI=10.1186/1471-2164-13-382;
RA Zhu S., Cao Y.-Z., Jiang C., Tan B.-Y., Wang Z., Feng S., Zhang L.,
RA Su X.-H., Brejova B., Vinar T., Xu M., Wang M.-X., Zhang S.-G.,
RA Huang M.-R., Wu R., Zhou Y.;
RT "Sequencing the genome of Marssonina brunnea reveals fungus-poplar co-
RT evolution.";
RL BMC Genomics 13:382-382(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 -!- 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; JH921431; EKD19477.1; -; Genomic_DNA.
DR RefSeq; XP_007290603.1; XM_007290541.1.
DR AlphaFoldDB; K1X367; -.
DR STRING; 1072389.K1X367; -.
DR GeneID; 18758649; -.
DR KEGG; mbe:MBM_02714; -.
DR eggNOG; KOG3886; Eukaryota.
DR HOGENOM; CLU_044099_0_0_1; -.
DR InParanoid; K1X367; -.
DR OMA; QQKDHIF; -.
DR OrthoDB; 33171at2759; -.
DR Proteomes; UP000006753; 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; cd11384; RagA_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; IPR039397; RagA/B.
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; 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:UP000006753}.
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 36..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 406 AA; 45501 MW; 2E916297BD974B4A CRC64;
MPDTNGLDPS PSERPSETPP TPFYYYHGDI ELQFYRRDPV SSLAPPQTPG PAPKTASDGD
MEKQFDNLSV QDDAGGSPSS EPRKLKKKKV LLMGKSGSGK SSMRSIIFSN YVAKDTRRLG
ATIDVDLSQV KFLGNLTLNL WDCGGQDAFM ENYLSQQRQH VFSNVGVLIY VFDIESRDLE
RDLLTYRSII IALSQFSPTS SVYVLVHKMD LVVPHQREDI YSGRVQLIQS KSDNFNPIPF
ATSIWDQSLY KAWAEIIHDL VPNLGQIEHH LGSLGKLIQA EEVLLFERSS FLVVSSWCSD
IGNENPTTDR YERLSNIIKN FKQTTSRFTG TPKSAEQFSL MELKLSNFSL FLVKFTTNTY
LAVVLPPGEE RFNAAMENCL IARAEFEDLD SPAKKGLDRG ATSTEA
//
