ID A0A0C7NFX5_9SACH Unreviewed; 465 AA.
AC A0A0C7NFX5;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 22-FEB-2023, entry version 29.
DE RecName: Full=V-type proton ATPase subunit H {ECO:0000256|PIRNR:PIRNR032184};
GN ORFNames=LALA0_S12e02212g {ECO:0000313|EMBL:CEP64581.1};
OS Lachancea lanzarotensis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Lachancea.
OX NCBI_TaxID=1245769 {ECO:0000313|EMBL:CEP64581.1, ECO:0000313|Proteomes:UP000054304};
RN [1] {ECO:0000313|EMBL:CEP64581.1, ECO:0000313|Proteomes:UP000054304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 12615 {ECO:0000313|EMBL:CEP64581.1,
RC ECO:0000313|Proteomes:UP000054304};
RA Neuveglise Cecile;
RL Submitted (DEC-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}.
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DR EMBL; LN736371; CEP64581.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C7NFX5; -.
DR STRING; 1245769.A0A0C7NFX5; -.
DR HOGENOM; CLU_025709_4_0_1; -.
DR OrthoDB; 176803at2759; -.
DR Proteomes; UP000054304; 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:UP000054304};
KW Transport {ECO:0000256|PIRNR:PIRNR032184}.
FT DOMAIN 343..463
FT /note="ATPase V1 complex subunit H C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11698"
SQ SEQUENCE 465 AA; 52081 MW; CFCF7445FB3FE669 CRC64;
MTVSKHAKLL LDSTHFSDIR STVRSRSIAW DALARTAEIS EADATSAKKL ESALIKHSKI
AITPAESIPA AIHIIQTVQN AEVKKFVYNL LAELLSSEEY ADATFDYFTN NPRALVDLFE
ASVSGDDQSI LLSSFNVVSL LIQPGFHNPD LVASLLGNER FVAVLQNTDH MDTSYVCIRL
LQELSALQEY RSIVWSAQSS FMPTLLGVIH NALDNNSSTR VAPTNSNNLS IQVQYYSLLT
LWLLTFDHQI SSEFASKYLS DFLNLLKLVK ITIKEKLSRL SIAIVLNCVA PHVKGHKATI
RQLLLLGNAL PILQSLSERK YSDDELRQDL STLKELLEKT YQELTSFDEY EAEVNSKLLV
WSPPHVDNGF WSENIDKFKD DNWKLFKKLV AILTVPNNEP STKIALQVAL SDITHVVELL
PESVEVLSKL NGKVLIMELL NHPDSKVKYE ALKATQAFVA HTFSK
//
