ID A0A1B1E4N6_9APIC Unreviewed; 457 AA.
AC A0A1B1E4N6;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 08-NOV-2023, entry version 21.
DE RecName: Full=V-type proton ATPase subunit H {ECO:0000256|PIRNR:PIRNR032184};
GN ORFNames=PCOAH_00037880 {ECO:0000313|EMBL:ANQ09951.1};
OS Plasmodium coatneyi.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium.
OX NCBI_TaxID=208452 {ECO:0000313|EMBL:ANQ09951.1, ECO:0000313|Proteomes:UP000092716};
RN [1] {ECO:0000313|Proteomes:UP000092716}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hackeri {ECO:0000313|Proteomes:UP000092716};
RA Chien J.-T., Pakala S.B., Geraldo J.A., Lapp S.A., Barnwell J.W.,
RA Kissinger J.C., Galinski M.R., Humphrey J.C.;
RT "First high quality genome sequence of Plasmodium coatneyi using continuous
RT long reads from single molecule, real-time sequencing.";
RL Submitted (JUN-2016) 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; CP016250; ANQ09951.1; -; Genomic_DNA.
DR RefSeq; XP_019916646.1; XM_020060579.1.
DR AlphaFoldDB; A0A1B1E4N6; -.
DR EnsemblProtists; ANQ09951; ANQ09951; PCOAH_00037880.
DR GeneID; 30910519; -.
DR VEuPathDB; PlasmoDB:PCOAH_00037880; -.
DR OrthoDB; 176803at2759; -.
DR Proteomes; UP000092716; Chromosome 12.
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}; Transport {ECO:0000256|PIRNR:PIRNR032184}.
FT DOMAIN 320..450
FT /note="ATPase V1 complex subunit H C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11698"
SQ SEQUENCE 457 AA; 53855 MW; 0E2946D478485F3F CRC64;
MAGDSGISVI SKIVESEQKS QILHDSILNK MPCYDKYEEI NILSSEDVEL LKKFHAFNKK
EKFDYFKENN TVVTVLFNCL QTDFNVHLIQ YVLTIFYEII RNDGSSYSYI LSILNDKSVY
SYLMKLCTHN DTYIADKSSF LLSGSFCYNS NNNYFSETEI KDFILKIDFF NVSEEGKMDI
YINILKIDNY RKDIYELEQF LTIINKNLDL SNNNANKQYK SVFCVWLLTF KDNFIKKLYK
NNIISVVINL FKKCRVEKIL RVSLNIIKNI MHMDDCFEII VDNNIIQTLT VLQYDKWRDN
DIYDTIVQLL HKLDQRVKNY SNFERYCHEL SKGKLKWSVL HTEKFWLENV MQFERDEFKA
IQQLADIIKS YAHNIAQKSD SMELKEEVDG VTVAVACFDI GEFARLYPNG KKICQKFRIK
ENVMILIATK DRDIVREALL CAQKIMLNNW QSISNAK
//
