ID A0A167FH48_9ASCO Unreviewed; 447 AA.
AC A0A167FH48;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 22-FEB-2023, entry version 23.
DE RecName: Full=V-type proton ATPase subunit H {ECO:0000256|PIRNR:PIRNR032184};
GN Name=VMA13 {ECO:0000313|EMBL:ANB15291.1};
GN ORFNames=AWJ20_2918 {ECO:0000313|EMBL:ANB15291.1};
OS Sugiyamaella lignohabitans.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Trichomonascaceae; Sugiyamaella.
OX NCBI_TaxID=796027 {ECO:0000313|EMBL:ANB15291.1, ECO:0000313|Proteomes:UP000189580};
RN [1] {ECO:0000313|EMBL:ANB15291.1, ECO:0000313|Proteomes:UP000189580}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 10342 {ECO:0000313|EMBL:ANB15291.1,
RC ECO:0000313|Proteomes:UP000189580};
RA Bellasio M., Peymann A., Valli M., Sipitzky M., Graf A., Sauer M., Marx H.,
RA Mattanovich D.;
RT "Complete genome sequence and transcriptome regulation of the pentose
RT utilising yeast Sugiyamaella lignohabitans.";
RL Submitted (FEB-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; CP014503; ANB15291.1; -; Genomic_DNA.
DR RefSeq; XP_018737768.1; XM_018879895.1.
DR AlphaFoldDB; A0A167FH48; -.
DR GeneID; 30034882; -.
DR KEGG; slb:AWJ20_2918; -.
DR OrthoDB; 176803at2759; -.
DR Proteomes; UP000189580; Chromosome b.
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:UP000189580};
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 447 AA; 50104 MW; C640EB02C1F823B8 CRC64;
MGENFGSNKA NVSLCYSSPI SSQYLEEIQS NIRVRPIPWE GYVRANLITT EEASLIKTIE
KLPKDKSVAI IAKDSDIYAA KLIGILSRIT RDDVVKYILS LVGDFASDSP EFRESLLGLK
DPQTFDVLTK LLDKPDEQTH LLSIKALITL IGQSSDDKSA VKLALAYISK KLASSPNANL
QDIAVQAYSS LLQVKKFRPL FWESRNEIVP SLIKILNASQ GNLQLQYYTL LVFWLVTFEK
QPAADVVTEF DLVPTLLNIT KNSVKEKIVR LAVATLVNTI NNASKVSVPA LLSHSCLELV
KTLAERKWTD EELIEDLDFL KTTLQEAFDS MTTFDEYGSE IIGKNLKWSP PHRSETFWKE
NIGKFKEGDW KILKALSNII TSSQDPVTLA VGSNDVSRII SELPESLKVF EKLGTKVKIM
ELMNHPDSDV RYEALKATQT FIAHSFK
//
