ID A0A024U5Q7_9STRA Unreviewed; 461 AA.
AC A0A024U5Q7;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=V-type proton ATPase subunit H {ECO:0000256|PIRNR:PIRNR032184};
GN ORFNames=H310_06210 {ECO:0000313|EMBL:ETW01555.1};
OS Aphanomyces invadans.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Aphanomyces.
OX NCBI_TaxID=157072 {ECO:0000313|EMBL:ETW01555.1};
RN [1] {ECO:0000313|EMBL:ETW01555.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NJM9701 {ECO:0000313|EMBL:ETW01555.1};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., van West P., Dieguez-Uribeondo J., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L., Chapman S.B.,
RA Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C., Pearson M.,
RA Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Aphanomyces invadans NJM9701.";
RL Submitted (DEC-2013) 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; KI913962; ETW01555.1; -; Genomic_DNA.
DR RefSeq; XP_008869403.1; XM_008871181.1.
DR AlphaFoldDB; A0A024U5Q7; -.
DR STRING; 157072.A0A024U5Q7; -.
DR EnsemblFungi; H310_06210-t26_1; H310_06210-t26_1-p1; H310_06210.
DR EnsemblProtists; ETW01555; ETW01555; H310_06210.
DR GeneID; 20083260; -.
DR VEuPathDB; FungiDB:H310_06210; -.
DR eggNOG; KOG2759; Eukaryota.
DR OrthoDB; 176803at2759; -.
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; IPR000225; Armadillo.
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 SMART; SM00185; ARM; 3.
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 344..457
FT /note="ATPase V1 complex subunit H C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11698"
SQ SEQUENCE 461 AA; 51291 MW; F223565E7B229594 CRC64;
MSVSSSQVLE AVKANALDVA LAREEALAKF KDINWATYTR AGGFSLDKAE ITAIKEMETV
AKNASQNEDQ TDSLIDTFLR EYGAALGAGL LKLIKNVTEP SVLRYAFARI DDLLPDGGRS
RKRATYFVPD GTYVEAAPFL RLLRSESGYT QYAAGHILAQ FLTFRGKEQD IVSLIQWILD
AVKASAQSSD TALGATARNA ITTLMVLLRC ETARKLFTRA GGLASLADVL KNSQGKAQLA
YEVCFCLWTL SFSDEAIEAF GSSGAITALI QQVVAAPREK VVRVSLEALE NLLGKANGAY
NERMIDGGLL KTLTNLRDRK WTDEDIAKSI TAIRDVLIRE FKELNTMERY EKEVRTGSLA
WGLLHTEKFW RENVMSFEAN EFELIRLLID LLESDDPKTV SVALYDLGDF VRFYPNGKHI
AKRLGAKKVA MKLMTHENAE VQKHALTCIS KMMVNKWEFV K
//
