ID A0A0N1IIH3_LEPSE Unreviewed; 482 AA.
AC A0A0N1IIH3;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 22-FEB-2023, entry version 22.
DE RecName: Full=V-type proton ATPase subunit H {ECO:0000256|PIRNR:PIRNR032184};
GN ORFNames=ABL78_6837 {ECO:0000313|EMBL:KPI84100.1};
OS Leptomonas seymouri.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leptomonas.
OX NCBI_TaxID=5684 {ECO:0000313|EMBL:KPI84100.1, ECO:0000313|Proteomes:UP000038009};
RN [1] {ECO:0000313|EMBL:KPI84100.1, ECO:0000313|Proteomes:UP000038009}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 30220 {ECO:0000313|EMBL:KPI84100.1,
RC ECO:0000313|Proteomes:UP000038009};
RX PubMed=26317207;
RA Kraeva N., Butenko A., Hlavacova J., Kostygov A., Myskova J., Grybchuk D.,
RA Lestinova T., Votypka J., Volf P., Opperdoes F., Flegontov P., Lukes J.,
RA Yurchenko V.;
RT "Leptomonas seymouri: Adaptations to the Dixenous Life Cycle Analyzed by
RT Genome Sequencing, Transcriptome Profiling and Co-infection with Leishmania
RT donovani.";
RL PLoS Pathog. 11:E1005127-E1005127(2015).
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:KPI84100.1}.
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DR EMBL; LJSK01000289; KPI84100.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N1IIH3; -.
DR EnsemblProtists; KPI84100; KPI84100; ABL78_6837.
DR VEuPathDB; TriTrypDB:Lsey_0289_0010; -.
DR OMA; RERMIPQ; -.
DR OrthoDB; 176803at2759; -.
DR Proteomes; UP000038009; 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}; Transport {ECO:0000256|PIRNR:PIRNR032184}.
FT DOMAIN 358..476
FT /note="ATPase V1 complex subunit H C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11698"
SQ SEQUENCE 482 AA; 54233 MW; 3763530F8DCDEA62 CRC64;
MPTLSADAAD TISLVLQLQL LDENAVRLLE QLFTNRLDEE LVNSLVGGRE ESLTIAMFRV
CAGTHTERIL GYALRFLADL VYADQAIGVQ LGRNDLQNKF GGSPASLLLQ IAATHSETLG
ISNPAIYLAA IALRFGTYEG NEDAFKEFFA LARHTFSPDT LQVSDVEFTV RACVQLARRK
DYRPLFFKGN ILSCIPRLLT DIVSSDSAGI IQIIYETLLL SWLLSFEYEG IVLLVRERMI
PQLHRVLQRV QKEKCVRVTL MTLLNMVEAE RKYMNQMLNP LSDEWVDESI QVLSRLHQGN
TVEQISTFKK GPSLVAEMVS VGMIKTLSQL FRRKFGDEDI NVMVENLNLA LESSMQVLTS
FSQYRGEVLS GVLEWTPVHT SAKFWKENAE KVEGNNYEVL IALGKTLCES KNEVTLAVAC
HDLGEIIRYH PTGRNLLTLA TMSGVKERVM SLMSHTNPEV AKEALLCTQK VMVQRWEYMQ
TA
//