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Database: UniProt
Entry: A0A0C4DL51_MAGP6
LinkDB: A0A0C4DL51_MAGP6
Original site: A0A0C4DL51_MAGP6 
ID   A0A0C4DL51_MAGP6        Unreviewed;       123 AA.
AC   A0A0C4DL51;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=V-type proton ATPase subunit F {ECO:0000256|ARBA:ARBA00013430, ECO:0000256|PIRNR:PIRNR015945};
GN   ORFNames=MAPG_00489 {ECO:0000313|EMBL:KLU81399.1};
OS   Magnaporthiopsis poae (strain ATCC 64411 / 73-15) (Kentucky bluegrass
OS   fungus) (Magnaporthe poae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Magnaporthales; Magnaporthaceae; Magnaporthiopsis.
OX   NCBI_TaxID=644358 {ECO:0000313|EnsemblFungi:MAPG_00489T0, ECO:0000313|Proteomes:UP000011715};
RN   [1] {ECO:0000313|EMBL:KLU81399.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 64411 {ECO:0000313|EMBL:KLU81399.1};
RG   The Broad Institute Genome Sequencing Platform;
RG   Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Ma L.-J., Dead R., Young S., Zeng Q., Koehrsen M., Alvarado L., Berlin A.,
RA   Chapman S.B., Chen Z., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heilman E.R., Heiman D., Hepburn T., Howarth C., Jen D.,
RA   Larson L., Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T.,
RA   Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C.,
RA   Haas B., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Magnaporthe poae strain ATCC 64411.";
RL   Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000011715}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 64411 / 73-15 {ECO:0000313|Proteomes:UP000011715};
RA   Ma L.-J., Dead R., Young S., Zeng Q., Koehrsen M., Alvarado L., Berlin A.,
RA   Chapman S.B., Chen Z., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heilman E.R., Heiman D., Hepburn T., Howarth C., Jen D.,
RA   Larson L., Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T.,
RA   Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C.,
RA   Haas B., Nusbaum C., Birren B.;
RT   "The genome sequence of Magnaporthe poae strain ATCC 64411.";
RL   Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:KLU81399.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 64411 {ECO:0000313|EMBL:KLU81399.1};
RA   Ma L.-J., Dead R., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A.,
RA   Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M.,
RA   Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Larson L., Lui A.,
RA   MacDonald P.J.P., Mehta T., Montmayeur A., Murphy C., Neiman D.,
RA   Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P.,
RA   Stolte C., Sykes S., Yandava C., Wortman J., Nusbaum C., Birren B.;
RT   "Annotation of Magnaporthe poae ATCC 64411.";
RL   Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EnsemblFungi:MAPG_00489T0}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 64411 / 73-15 {ECO:0000313|EnsemblFungi:MAPG_00489T0};
RX   PubMed=26416668; DOI=10.1534/g3.115.020057;
RA   Okagaki L.H., Nunes C.C., Sailsbery J., Clay B., Brown D., John T., Oh Y.,
RA   Young N., Fitzgerald M., Haas B.J., Zeng Q., Young S., Adiconis X., Fan L.,
RA   Levin J.Z., Mitchell T.K., Okubara P.A., Farman M.L., Kohn L.M., Birren B.,
RA   Ma L.-J., Dean R.A.;
RT   "Genome sequences of three phytopathogenic species of the Magnaporthaceae
RT   family of fungi.";
RL   G3 (Bethesda) 5:2539-2545(2015).
RN   [5] {ECO:0000313|EnsemblFungi:MAPG_00489T0}
RP   IDENTIFICATION.
RC   STRAIN=ATCC 64411 {ECO:0000313|EnsemblFungi:MAPG_00489T0};
RG   EnsemblFungi;
RL   Submitted (JUN-2015) to UniProtKB.
CC   -!- FUNCTION: Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase),
CC       a multisubunit enzyme composed of a peripheral complex (V1) that
CC       hydrolyzes ATP and a membrane integral complex (V0) that translocates
CC       protons. V-ATPase is responsible for acidifying and maintaining the pH
CC       of intracellular compartments. {ECO:0000256|PIRNR:PIRNR015945}.
CC   -!- SUBUNIT: V-ATPase is a heteromultimeric enzyme composed of a peripheral
CC       catalytic V1 complex (components A to H) attached to an integral
CC       membrane V0 proton pore complex (components: a, c, c', c'', d, e, f and
CC       VOA1). {ECO:0000256|ARBA:ARBA00029477}.
CC   -!- SUBUNIT: V-ATPase is a heteromultimeric enzyme made up of two
CC       complexes: the ATP-hydrolytic V1 complex and the proton translocation
CC       V0 complex. {ECO:0000256|PIRNR:PIRNR015945}.
CC   -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000256|ARBA:ARBA00029427};
CC       Peripheral membrane protein {ECO:0000256|ARBA:ARBA00029427};
CC       Cytoplasmic side {ECO:0000256|ARBA:ARBA00029427}.
CC   -!- SIMILARITY: Belongs to the V-ATPase F subunit family.
CC       {ECO:0000256|ARBA:ARBA00010148, ECO:0000256|PIRNR:PIRNR015945}.
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DR   EMBL; ADBL01000115; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; GL876966; KLU81399.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C4DL51; -.
DR   STRING; 644358.A0A0C4DL51; -.
DR   EnsemblFungi; MAPG_00489T0; MAPG_00489T0; MAPG_00489.
DR   VEuPathDB; FungiDB:MAPG_00489; -.
DR   eggNOG; KOG3432; Eukaryota.
DR   OMA; FTEERKD; -.
DR   OrthoDB; 275186at2759; -.
DR   Proteomes; UP000011715; Unassembled WGS sequence.
DR   GO; GO:0033180; C:proton-transporting V-type ATPase, V1 domain; IEA:InterPro.
DR   GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR   Gene3D; 3.40.50.10580; ATPase, V1 complex, subunit F; 1.
DR   InterPro; IPR008218; ATPase_V1-cplx_f_g_su.
DR   InterPro; IPR005772; ATPase_V1-cplx_fsu_euk.
DR   InterPro; IPR036906; ATPase_V1_fsu_sf.
DR   NCBIfam; TIGR01101; V_ATP_synt_F; 1.
DR   PANTHER; PTHR13861:SF2; V-TYPE PROTON ATPASE SUBUNIT F; 1.
DR   PANTHER; PTHR13861; VACUOLAR ATP SYNTHASE SUBUNIT F; 1.
DR   Pfam; PF01990; ATP-synt_F; 1.
DR   PIRSF; PIRSF015945; ATPase_V1_F_euk; 1.
DR   SUPFAM; SSF159468; AtpF-like; 1.
PE   3: Inferred from homology;
KW   Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781,
KW   ECO:0000256|PIRNR:PIRNR015945};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW   ECO:0000256|PIRNR:PIRNR015945};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011715};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR015945}.
SQ   SEQUENCE   123 AA;  13645 MW;  1CD5207E4255BE81 CRC64;
     MTAQADSKNR EFLAVIGDED SVTGLLLAGI GHVTPAPDSQ KNFLVVDSKT ENAAIEAAFQ
     RFTTDRKDIG IVLINQHIAD RIRHTVDTYT AAFPAVLEIP SKDHPYDPEK DSVLRRVRRL
     FGE
//
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