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Database: UniProt
Entry: A0A194VVP9_9PEZI
LinkDB: A0A194VVP9_9PEZI
Original site: A0A194VVP9_9PEZI 
ID   A0A194VVP9_9PEZI        Unreviewed;       116 AA.
AC   A0A194VVP9;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   RecName: Full=V-type proton ATPase subunit F {ECO:0000256|ARBA:ARBA00013430};
DE   AltName: Full=Vacuolar proton pump subunit F {ECO:0000256|ARBA:ARBA00030311};
GN   ORFNames=VM1G_03922 {ECO:0000313|EMBL:KUI68306.1};
OS   Valsa mali.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX   NCBI_TaxID=105487 {ECO:0000313|EMBL:KUI68306.1};
RN   [1] {ECO:0000313|EMBL:KUI68306.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=03-8 {ECO:0000313|EMBL:KUI68306.1};
RA   Yin Z., Liu H., Gao X., Li Z., Song N., Ke X., Dai Q., Wu Y., Sun Y.,
RA   Xu J.-R., Kang Z.K., Wang L., Huang L.;
RT   "Genome Sequence of Valsa Canker Pathogens Uncovers a Specific Adaption of
RT   Colonization on Woody Bark.";
RL   Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
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   -!- 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}.
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DR   EMBL; CM003101; KUI68306.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A194VVP9; -.
DR   OrthoDB; 275186at2759; -.
DR   Proteomes; UP000078559; Chromosome 4.
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   Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
SQ   SEQUENCE   116 AA;  13085 MW;  C186FB2C0B003C34 CRC64;
     MSTHADYKDR QFLAVIGDED SVTGLLLAGI GHVTAGPDAQ KNFLVVDNKT DNATIESNFD
     KFIERKDIGI IADRIRHRID TYTAAFPTIL EIPSKDHPYD PEKDSVLRRV RRLFGE
//
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