ID   YPT7_MAGO7              Reviewed;         205 AA.
AC   G4MYS1;
DT   07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2011, sequence version 1.
DT   03-AUG-2022, entry version 47.
DE   RecName: Full=Ypt/Rab-type GTPase ypt7;
GN   Name=YPT7 {ECO:0000303|PubMed:25991510}; ORFNames=MGG_08144;
OS   Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS   fungus) (Pyricularia oryzae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX   NCBI_TaxID=242507;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX   PubMed=15846337; DOI=10.1038/nature03449;
RA   Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA   Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA   Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA   Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA   Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA   Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT   "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL   Nature 434:980-986(2005).
RN   [2]
RP   FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP   GLN-67.
RX   PubMed=25991510; DOI=10.1111/1462-2920.12903;
RA   Liu X.H., Chen S.M., Gao H.M., Ning G.A., Shi H.B., Wang Y., Dong B.,
RA   Qi Y.Y., Zhang D.M., Lu G.D., Wang Z.H., Zhou J., Lin F.C.;
RT   "The small GTPase MoYpt7 is required for membrane fusion in autophagy and
RT   pathogenicity of Magnaporthe oryzae.";
RL   Environ. Microbiol. 17:4495-4510(2015).
RN   [3]
RP   MUTAGENESIS OF ASN-125, AND INTERACTION WITH GDI1.
RX   PubMed=29308611; DOI=10.1631/jzus.b1700336;
RA   Huang L.Y., Wu M., Yu X.Y., Li L., Lin F.C., Liu X.H.;
RT   "Physical interactions and mutational analysis of MoYpt7 in Magnaporthe
RT   oryzae.";
RL   J. Zhejiang Univ. Sci. B 19:79-84(2018).
CC   -!- FUNCTION: Ypt/Rab-type GTPases are key regulators of membrane
CC       trafficking and intracellular vesicular transport. They act as
CC       molecular switches that convert between GTP-bound and GDP-bound states,
CC       and regulate virtually all steps of membrane traffic from the formation
CC       of the transport vesicle at the donor membrane to its fusion at the
CC       target membrane. In the GDP-bound state, Ypt proteins are predominantly
CC       cytosolic, solubilized through the interaction with a GDP dissociation
CC       inhibitor (GDI). In the GTP-bound state, the proteins are membrane
CC       bound and interact with specific effector proteins that select cargo,
CC       promote vesicle movement, or verify the correct site of fusion (By
CC       similarity). Required for fungal morphogenesis, vacuole fusion,
CC       autophagy, stress resistance and pathogenicity (PubMed:25991510).
CC       {ECO:0000250|UniProtKB:P32939, ECO:0000269|PubMed:25991510}.
CC   -!- ACTIVITY REGULATION: Rab activation is generally mediated by a guanine
CC       exchange factor (GEF), while inactivation through hydrolysis of bound
CC       GTP is catalyzed by a GTPase activating protein (GAP).
CC       {ECO:0000250|UniProtKB:P32939}.
CC   -!- SUBUNIT: Interacts with the Rab GDP dissociation inhibitor GDI1.
CC       {ECO:0000269|PubMed:29308611}.
CC   -!- SUBCELLULAR LOCATION: Vacuole {ECO:0000269|PubMed:25991510}.
CC   -!- DISRUPTION PHENOTYPE: Exhibits defects in mycelial growth and
CC       production of conidia, and consequently fails to cause disease in rice
CC       and barley. Shows impairment in autophagy, breached cell wall
CC       integrity, and higher sensitivity to both calcium and heavy metal
CC       stress. {ECO:0000269|PubMed:25991510}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC       {ECO:0000305}.
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DR   EMBL; CM001232; EHA55300.1; -; Genomic_DNA.
DR   RefSeq; XP_003715107.1; XM_003715059.1.
DR   AlphaFoldDB; G4MYS1; -.
DR   SMR; G4MYS1; -.
DR   STRING; 318829.MGG_08144T0; -.
DR   EnsemblFungi; MGG_08144T0; MGG_08144T0; MGG_08144.
DR   GeneID; 2678359; -.
DR   KEGG; mgr:MGG_08144; -.
DR   VEuPathDB; FungiDB:MGG_08144; -.
DR   eggNOG; KOG0394; Eukaryota.
DR   HOGENOM; CLU_041217_10_6_1; -.
DR   InParanoid; G4MYS1; -.
DR   OMA; IQACPRD; -.
DR   OrthoDB; 1172019at2759; -.
DR   PHI-base; PHI:4736; -.
DR   Proteomes; UP000009058; Chromosome 2.
DR   GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR001806; Small_GTPase.
DR   Pfam; PF00071; Ras; 1.
DR   SMART; SM00174; RHO; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
PE   1: Evidence at protein level;
KW   GTP-binding; Lipoprotein; Methylation; Nucleotide-binding; Prenylation;
KW   Reference proteome; Vacuole.
FT   CHAIN           1..205
FT                   /note="Ypt/Rab-type GTPase ypt7"
FT                   /id="PRO_0000451057"
FT   MOTIF           37..45
FT                   /note="Effector region"
FT                   /evidence="ECO:0000250|UniProtKB:P32939"
FT   BINDING         17..23
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P32939"
FT   BINDING         33..40
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P32939"
FT   BINDING         66
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P32939"
FT   BINDING         125..128
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P32939"
FT   BINDING         157..159
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P32939"
FT   MOD_RES         205
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000250|UniProtKB:P36586"
FT   LIPID           203
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P36586"
FT   LIPID           205
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P36586"
FT   MUTAGEN         67
FT                   /note="Q->L: Constitutively in the GTP-bound conformation.
FT                   Reduces pathogenicity and produces more appressoria-forming
FT                   single-septum conidia."
FT                   /evidence="ECO:0000269|PubMed:25991510"
FT   MUTAGEN         125
FT                   /note="N->I: Constitutively in the GDP-bound conformation.
FT                   Mislocalizes to the cytoplasm. Caused severe defects in
FT                   conidiation and pathogenicity."
FT                   /evidence="ECO:0000269|PubMed:29308611"
SQ   SEQUENCE   205 AA;  22949 MW;  379CF2ACA7DAF25C CRC64;
     MSSRKKVLLK VIILGDSGVG KTSLMNQYVN KKFSASYKAT IGADFLTREV LVDDRQVTMQ
     LWDTAGQERF QSLGVAFYRG ADCCVLVFDV NNSKSFDALD SWRDEFLIQA SPRDPDNFPF
     VVLGNKIDVE ESKRVISTKR AMTFCQSKGG IPYFETSAKE AINVEQAFEV IARNALAQEE
     SEEFSGDFQD PINIHIDNDR DGCAC