ID   VATF_NEOFI              Reviewed;         124 AA.
AC   A1DH48;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=V-type proton ATPase subunit F;
DE            Short=V-ATPase subunit F;
DE   AltName: Full=V-ATPase 14 kDa subunit;
DE   AltName: Full=Vacuolar proton pump subunit F;
GN   Name=vma7; ORFNames=NFIA_086600;
OS   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS   / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=331117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC   / WB 181;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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 (By similarity). V-ATPase is responsible for acidifying and
CC       maintaining the pH of intracellular compartments (By similarity).
CC       {ECO:0000250|UniProtKB:P39111}.
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:0000250|UniProtKB:P39111}.
CC   -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000250|UniProtKB:P39111};
CC       Peripheral membrane protein {ECO:0000305}; Cytoplasmic side
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the V-ATPase F subunit family. {ECO:0000305}.
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DR   EMBL; DS027696; EAW18705.1; -; Genomic_DNA.
DR   RefSeq; XP_001260602.1; XM_001260601.1.
DR   AlphaFoldDB; A1DH48; -.
DR   SMR; A1DH48; -.
DR   STRING; 36630.CADNFIAP00006873; -.
DR   EnsemblFungi; EAW18705; EAW18705; NFIA_086600.
DR   GeneID; 4587160; -.
DR   KEGG; nfi:NFIA_086600; -.
DR   VEuPathDB; FungiDB:NFIA_086600; -.
DR   eggNOG; KOG3432; Eukaryota.
DR   HOGENOM; CLU_135754_0_0_1; -.
DR   OMA; YTNAFPA; -.
DR   OrthoDB; 1483558at2759; -.
DR   Proteomes; UP000006702; Unassembled WGS sequence.
DR   GO; GO:0000221; C:vacuolar proton-transporting V-type ATPase, V1 domain; ISS:UniProtKB.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR   Gene3D; 3.40.50.10580; -; 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   Pfam; PF01990; ATP-synt_F; 1.
DR   PIRSF; PIRSF015945; ATPase_V1_F_euk; 1.
DR   SUPFAM; SSF159468; SSF159468; 1.
DR   TIGRFAMs; TIGR01101; V_ATP_synt_F; 1.
PE   3: Inferred from homology;
KW   Hydrogen ion transport; Ion transport; Membrane; Reference proteome;
KW   Transport; Vacuole.
FT   CHAIN           1..124
FT                   /note="V-type proton ATPase subunit F"
FT                   /id="PRO_0000406050"
SQ   SEQUENCE   124 AA;  13807 MW;  12A9AACB287533F3 CRC64;
     MAASAVSYKE RQFLAVIGDE DSVTGLLLAG IGHVTDGPDA QRNFLVVDSK TETSAIEKAF
     QNFTQERKDI AVLLINQHIA ERIRHSVDSF ADPFPAVLEI PSKDHPYDPE KDSVLKRVRR
     LFGE