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Database: UniProt
Entry: A0A0S7DPG6_9EURO
LinkDB: A0A0S7DPG6_9EURO
Original site: A0A0S7DPG6_9EURO 
ID   A0A0S7DPG6_9EURO        Unreviewed;       124 AA.
AC   A0A0S7DPG6;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=V-type proton ATPase subunit F {ECO:0000256|ARBA:ARBA00013430, ECO:0000256|PIRNR:PIRNR015945};
GN   ORFNames=ALT_000715 {ECO:0000313|EMBL:GIM38332.1}, CNMCM8060_005754
GN   {ECO:0000313|EMBL:KAF4177164.1};
OS   Aspergillus lentulus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=293939 {ECO:0000313|EMBL:GIM38332.1};
RN   [1] {ECO:0000313|EMBL:GIM38332.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=IFM 54703 {ECO:0000313|EMBL:GIM38332.1};
RA   Kusuya Y., Sakai K., Kamei K., Takahashi H., Yaguchi T.;
RT   "Draft Genome sequence of the pathogenic filamentous fungus Aspergillus
RT   lentulus IFM 54703T.";
RL   Genome Announc. 4:e01568-15(2016).
RN   [2] {ECO:0000313|EMBL:KAF4177164.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CNM-CM8060 {ECO:0000313|EMBL:KAF4177164.1};
RA   dos Santos R.A.C., Steenwyk J.L., Rivero-Menendez O., Mead M.E.,
RA   Silva L.P., Bastos R.W., Alastruey-Izquierdo A., Goldman G.H., Rokas A.;
RT   "Genomic and phenotypic heterogeneity of clinical isolates of the human
RT   pathogens Aspergillus fumigatus, Aspergillus lentulus and Aspergillus
RT   fumigatiaffinis.";
RL   bioRxiv 0:0-0(2020).
RN   [3] {ECO:0000313|EMBL:KAF4177164.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CNM-CM8060 {ECO:0000313|EMBL:KAF4177164.1};
RA   Santos R.A.C., Steenwyk J.L., Rivero-Menendez O., Mead M.E., Silva L.P.,
RA   Bastos R.W., Alastruey-Izquierdo A., Goldman G.H., Rokas A.;
RL   Submitted (APR-2020) to the EMBL/GenBank/DDBJ databases.
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}.
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:GIM38332.1}.
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DR   EMBL; BCLY01000008; GIM38332.1; -; Genomic_DNA.
DR   EMBL; JAAAPS010000035; KAF4177164.1; -; Genomic_DNA.
DR   STRING; 293939.A0A0S7DPG6; -.
DR   VEuPathDB; FungiDB:TMP_alenIFM54703_4022; -.
DR   OrthoDB; 275186at2759; -.
DR   Proteomes; UP000713487; 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   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR015945}.
SQ   SEQUENCE   124 AA;  13807 MW;  12A9AACB287533F3 CRC64;
     MAASAVSYKE RQFLAVIGDE DSVTGLLLAG IGHVTDGPDA QRNFLVVDSK TETSAIEKAF
     QNFTQERKDI AVLLINQHIA ERIRHSVDSF ADPFPAVLEI PSKDHPYDPE KDSVLKRVRR
     LFGE
//
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