ID B6QQK4_TALMQ Unreviewed; 479 AA.
AC B6QQK4;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 13-SEP-2023, entry version 62.
DE RecName: Full=V-type proton ATPase subunit H {ECO:0000256|PIRNR:PIRNR032184};
GN ORFNames=PMAA_042340 {ECO:0000313|EMBL:EEA20388.1};
OS Talaromyces marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333)
OS (Penicillium marneffei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441960 {ECO:0000313|EMBL:EEA20388.1, ECO:0000313|Proteomes:UP000001294};
RN [1] {ECO:0000313|Proteomes:UP000001294}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18224 / CBS 334.59 / QM 7333
RC {ECO:0000313|Proteomes:UP000001294};
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(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}.
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DR EMBL; DS995904; EEA20388.1; -; Genomic_DNA.
DR RefSeq; XP_002151388.1; XM_002151352.1.
DR AlphaFoldDB; B6QQK4; -.
DR STRING; 441960.B6QQK4; -.
DR VEuPathDB; FungiDB:PMAA_042340; -.
DR HOGENOM; CLU_025709_4_0_1; -.
DR OrthoDB; 176803at2759; -.
DR PhylomeDB; B6QQK4; -.
DR Proteomes; UP000001294; 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:UP000001294};
KW Transport {ECO:0000256|PIRNR:PIRNR032184}.
FT DOMAIN 359..477
FT /note="ATPase V1 complex subunit H C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11698"
SQ SEQUENCE 479 AA; 53602 MW; 723546628B577650 CRC64;
MSLELPTYLN SLQNNIRARP IPWDGAVRAG NITEDQLRKI KAVDKVRTQE RKQAVEADLN
GYTTLLAGNP PDVKSVLESA SRRTDIVQYI LVLAADLIND VPALASALIS HPNPYNAFLP
FLRNLTNPED PIPLLASSFL TNLVSTALVS DQTTDAEEEA LPQLYTYLAN LTKNQDSGLQ
DIGVQGFSAL LRNKVARELF WKQRSETLDP LMGILRTAAG GKDNGSINLA TSAATSSIRT
ADISIGGGVG LQLLYHVLLV IWQLSFEGSL VGEELQSKYD IIELYTQLLR LSPKEKTTRL
LLATLNILLV ANRTLLPVAT FVRLPALLSN LSGRHLTDPD LLEDLQSLTD LLEEYTKTQT
TFDEYAAELQ SGHLRWSPPH RNPAFWRENT RRILEEERGA LPKKLAEIIA KSWENDKQVL
AIACNDVGNL VKEVPERRMQ LEKLGLKTRV MELMTDRDES VRWESLRAVG EWLRYSFDK
//
