ID C5KB62_PERM5 Unreviewed; 454 AA.
AC C5KB62;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=V-type proton ATPase subunit H {ECO:0000256|PIRNR:PIRNR032184};
GN ORFNames=Pmar_PMAR005299 {ECO:0000313|EMBL:EER18388.1};
OS Perkinsus marinus (strain ATCC 50983 / TXsc).
OC Eukaryota; Sar; Alveolata; Perkinsozoa; Perkinsea; Perkinsida; Perkinsidae;
OC Perkinsus.
OX NCBI_TaxID=423536 {ECO:0000313|Proteomes:UP000007800};
RN [1] {ECO:0000313|EMBL:EER18388.1, ECO:0000313|Proteomes:UP000007800}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50983 / TXsc {ECO:0000313|Proteomes:UP000007800};
RA El-Sayed N., Caler E., Inman J., Amedeo P., Hass B., Wortman J.;
RL Submitted (JUL-2008) 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; GG671811; EER18388.1; -; Genomic_DNA.
DR RefSeq; XP_002786592.1; XM_002786546.1.
DR AlphaFoldDB; C5KB62; -.
DR EnsemblProtists; EER18388; EER18388; Pmar_PMAR005299.
DR GeneID; 9049194; -.
DR InParanoid; C5KB62; -.
DR OMA; MKLCTHN; -.
DR OrthoDB; 176803at2759; -.
DR Proteomes; UP000007800; 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:UP000007800};
KW Transport {ECO:0000256|PIRNR:PIRNR032184}.
FT DOMAIN 331..446
FT /note="ATPase V1 complex subunit H C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11698"
SQ SEQUENCE 454 AA; 51147 MW; B70702ABD1DA30B9 CRC64;
MQESHQRLLE QAKAAPDDFS REAAILSSKP DWQSLENAGQ IPKGSAQWLN QIHGTSSSAV
VTLAQRNEEV ISGLLSVLKS VEDMHAVQYA FTVIYEATRY DSSFWNLLVG FARKNDIMLP
FTRFLSSDRA AEDSYSSDKA LYVLTNIMSH DGGRRFNPQE AKMIADSVAD DKNMKFKGVS
DLGRLDGFCN LLKFDGFRAV VWNNRKVQRC IMNAISGVES SDPLVLYRGV FCVWCVSFNK
ELVSTSVADM GDDLVQALLS VVANCRVEKV IRMTLAVLSN FLGDDKMCTA IVESGIIHYV
QNLEYEKWRD QELYEDVRKV AAMIASEIST HTNFERYERE LRTNKLRWGF IHSEKFWLEN
AEKFDREQFA AVKALVALLK SDSADDTTKA VACHDIGEFA RVYPTGKQVL NRLSAKPAVM
ALMTSKDRDV AREALLATQK LMLNKWQALQ QGAL
//
