ID A0A010QN95_9PEZI Unreviewed; 479 AA.
AC A0A010QN95;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=V-type proton ATPase subunit H {ECO:0000256|PIRNR:PIRNR032184};
GN ORFNames=CFIO01_12764 {ECO:0000313|EMBL:EXF78190.1};
OS Colletotrichum fioriniae PJ7.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum acutatum species complex.
OX NCBI_TaxID=1445577 {ECO:0000313|EMBL:EXF78190.1, ECO:0000313|Proteomes:UP000020467};
RN [1] {ECO:0000313|EMBL:EXF78190.1, ECO:0000313|Proteomes:UP000020467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PJ7 {ECO:0000313|EMBL:EXF78190.1,
RC ECO:0000313|Proteomes:UP000020467};
RA Baroncelli R., Thon M.R.;
RT "The genome sequence of Colletotrichum fioriniae PJ7.";
RL Submitted (FEB-2014) 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:PIRNR032184}.
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:PIRNR032184}.
CC -!- SIMILARITY: Belongs to the V-ATPase H subunit family.
CC {ECO:0000256|ARBA:ARBA00008613, ECO:0000256|PIRNR:PIRNR032184}.
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:EXF78190.1}.
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DR EMBL; JARH01000658; EXF78190.1; -; Genomic_DNA.
DR RefSeq; XP_007598172.1; XM_007598110.1.
DR AlphaFoldDB; A0A010QN95; -.
DR STRING; 1445577.A0A010QN95; -.
DR KEGG; cfj:CFIO01_12764; -.
DR eggNOG; KOG2759; Eukaryota.
DR HOGENOM; CLU_025709_4_0_1; -.
DR OrthoDB; 176803at2759; -.
DR Proteomes; UP000020467; Unassembled WGS sequence.
DR GO; GO:0000221; C:vacuolar proton-transporting V-type ATPase, V1 domain; IEA:UniProtKB-UniRule.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:UniProtKB-UniRule.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR Gene3D; 1.25.40.150; V-type ATPase, subunit H, C-terminal domain; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR004908; ATPase_V1-cplx_hsu.
DR InterPro; IPR011987; ATPase_V1-cplx_hsu_C.
DR InterPro; IPR038497; ATPase_V1-cplx_hsu_C_sf.
DR PANTHER; PTHR10698; V-TYPE PROTON ATPASE SUBUNIT H; 1.
DR PANTHER; PTHR10698:SF0; V-TYPE PROTON ATPASE SUBUNIT H; 1.
DR Pfam; PF11698; V-ATPase_H_C; 1.
DR Pfam; PF03224; V-ATPase_H_N; 1.
DR PIRSF; PIRSF032184; ATPase_V1_H; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
PE 3: Inferred from homology;
KW Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781,
KW ECO:0000256|PIRNR:PIRNR032184};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW ECO:0000256|PIRNR:PIRNR032184};
KW Reference proteome {ECO:0000313|Proteomes:UP000020467};
KW Transport {ECO:0000256|PIRNR:PIRNR032184}.
FT DOMAIN 359..477
FT /note="ATPase V1 complex subunit H C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11698"
SQ SEQUENCE 479 AA; 53058 MW; 299F3447382357E2 CRC64;
MSLDPPTYLA SLQNNIRQRP IPWDGAVRAG TITEDHLARI RAVDKAKKPE ARKEIVEGDL
DGYRSLFVGE SGKPSVLESA GKQANVVQYI LVLLADLLPS VPSLSKAIFK NTDPYKHFLP
LLAHSNNTED PIPLLTSTAL TKLMSLSLNE SQATRNAIPV LLSYLSGLAK SSDAGLQDIA
VQEYSSILYG HAARQQFWNQ RSETIAPLID ILRTAAGIGS NGSSSASIWS GTAPTRNAGF
EGSLGGGVGL QLLYHVLLVI WQMSFEAEDI GDELNDEYDI VLLYTQLLRL SPKEKTTRLV
VSTLYNLLSK NQKSLLPTAV LARLPALLDN LSGRHLTDPD LLEDAQSLKE LLEEYTKTKT
TFDEYVAEVE SGHLRWSPPH RSQVFWAENA RKILEHENGA IARQLAEIMK KPWENDKAVL
AIACNDVGAL VKEVPEMRYK LEKLGLKTRV MELMGESDEN VRWESLKALG GWLKYSFDN
//