ID   F0XFJ1_GROCL            Unreviewed;       124 AA.
AC   F0XFJ1;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=V-type proton ATPase subunit F {ECO:0000256|ARBA:ARBA00013430, ECO:0000256|PIRNR:PIRNR015945};
GN   ORFNames=CMQ_747 {ECO:0000313|EMBL:EFX03819.1};
OS   Grosmannia clavigera (strain kw1407 / UAMH 11150) (Blue stain fungus)
OS   (Graphiocladiella clavigera).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Leptographium.
OX   NCBI_TaxID=655863 {ECO:0000313|Proteomes:UP000007796};
RN   [1] {ECO:0000313|EMBL:EFX03819.1, ECO:0000313|Proteomes:UP000007796}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=kw1407 / UAMH 11150 {ECO:0000313|Proteomes:UP000007796};
RX   PubMed=21262841; DOI=10.1073/pnas.1011289108;
RA   DiGuistini S., Wang Y., Liao N.Y., Taylor G., Tanguay P., Feau N.,
RA   Henrissat B., Chan S.K., Hesse-Orce U., Alamouti S.M., Tsui C.K.M.,
RA   Docking R.T., Levasseur A., Haridas S., Robertson G., Birol I., Holt R.A.,
RA   Marra M.A., Hamelin R.C., Hirst M., Jones S.J.M., Bohlmann J., Breuil C.;
RT   "Genome and transcriptome analyses of the mountain pine beetle-fungal
RT   symbiont Grosmannia clavigera, a lodgepole pine pathogen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:2504-2509(2011).
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; GL629765; EFX03819.1; -; Genomic_DNA.
DR   RefSeq; XP_014173301.1; XM_014317826.1.
DR   AlphaFoldDB; F0XFJ1; -.
DR   STRING; 655863.F0XFJ1; -.
DR   GeneID; 25981017; -.
DR   eggNOG; KOG3432; Eukaryota.
DR   HOGENOM; CLU_135754_0_0_1; -.
DR   InParanoid; F0XFJ1; -.
DR   OrthoDB; 275186at2759; -.
DR   Proteomes; UP000007796; 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:UP000007796};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR015945}.
SQ   SEQUENCE   124 AA;  13954 MW;  B66171D939A7AFCF CRC64;
     MTTTQADYKD RQFLAVIGDE DSVTGLLLAG IGHVTPGADQ QKNFLVVDSK TDNAAIEAAF
     ERFSTERKDI GIILINQHIA DRIRHRIDTY TAAFPTVLEI PSKDHPYDPE KDSVLRRVRR
     LFGE
//