ID A0A0N0RSQ8_9BASI Unreviewed; 490 AA.
AC A0A0N0RSQ8;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=V-type proton ATPase subunit H {ECO:0000256|PIRNR:PIRNR032184};
GN ORFNames=Malapachy_3574 {ECO:0000313|EMBL:KOS16353.1};
OS Malassezia pachydermatis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia.
OX NCBI_TaxID=77020 {ECO:0000313|EMBL:KOS16353.1, ECO:0000313|Proteomes:UP000037751};
RN [1] {ECO:0000313|EMBL:KOS16353.1, ECO:0000313|Proteomes:UP000037751}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 1879 {ECO:0000313|EMBL:KOS16353.1,
RC ECO:0000313|Proteomes:UP000037751};
RA Triana S., Ohm R., Gonzalez A., DeCock H., Restrepo S., Celis A.;
RT "Draft Genome Sequence of Malassezia furfur CBS1878 and Malassezia
RT pachydermatis CBS1879.";
RL Submitted (JUL-2015) 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}.
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:KOS16353.1}.
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DR EMBL; LGAV01000001; KOS16353.1; -; Genomic_DNA.
DR RefSeq; XP_017993985.1; XM_018138040.1.
DR AlphaFoldDB; A0A0N0RSQ8; -.
DR STRING; 77020.A0A0N0RSQ8; -.
DR GeneID; 28729916; -.
DR VEuPathDB; FungiDB:Malapachy_3574; -.
DR OrthoDB; 176803at2759; -.
DR Proteomes; UP000037751; 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:UP000037751};
KW Transport {ECO:0000256|PIRNR:PIRNR032184}.
FT DOMAIN 371..489
FT /note="ATPase V1 complex subunit H C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11698"
SQ SEQUENCE 490 AA; 53733 MW; 368EB56937DDE3B4 CRC64;
MGEDTQSDGP GVVFSTSPLL PLSNVWLKEM TEHLRGKQTA WEGYQRAQLI SADQVPLLRD
AEQAGKKGEM APIKEKGSTY AGLYMQLLDK LNRTDTIQAV LLLTDDLVQA APEHLAWFVQ
AEPYAALTKL MKMDDAFVSI KAAQFLTLCL CAHAESSDST PPHAALESLL AYIHRALSSL
NSTEAPSDGA KGNVAPIALC LAGELLRTPR FRSAIWAKDV EEKQANDDTT LVGQLVAVLG
LSFKGSGASG TNSSGRASGN TGVPQLHYLA LFGLWVLTFD EAAAKDIDTY FGVATVLVHV
AQLALKHKIV RLIVSIWRNM LSASKEANAT RLLGAKVLPL CDTLQERRYP DTELQDDLEY
VKSVLSHRME QMSSYDQYVS ELYSGHLSFD NPAHQLEEFW KENAEKMTEN DNKDLKQLIS
LLSSKSSTPD TLAAACSDLD KFVQHTEGGR RRVTSLGAKT AIMELIEHPD PNVKHQALQT
LAKLVSASWR
//
