ID A0A0M8PEK7_9EURO Unreviewed; 477 AA.
AC A0A0M8PEK7;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 22-FEB-2023, entry version 19.
DE RecName: Full=V-type proton ATPase subunit H {ECO:0000256|PIRNR:PIRNR032184};
GN ORFNames=ACN38_g2902 {ECO:0000313|EMBL:KOS46110.1};
OS Penicillium nordicum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=229535 {ECO:0000313|EMBL:KOS46110.1, ECO:0000313|Proteomes:UP000037696};
RN [1] {ECO:0000313|EMBL:KOS46110.1, ECO:0000313|Proteomes:UP000037696}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DAOMC 185683 {ECO:0000313|EMBL:KOS46110.1,
RC ECO:0000313|Proteomes:UP000037696};
RA Nguyen H.D., Seifert K.A.;
RT "Genome sequencing of Penicillium nordicum.";
RL Submitted (AUG-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:KOS46110.1}.
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DR EMBL; LHQQ01000033; KOS46110.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M8PEK7; -.
DR STRING; 229535.A0A0M8PEK7; -.
DR OrthoDB; 176803at2759; -.
DR Proteomes; UP000037696; 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:UP000037696};
KW Transport {ECO:0000256|PIRNR:PIRNR032184}.
FT DOMAIN 357..475
FT /note="ATPase V1 complex subunit H C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11698"
SQ SEQUENCE 477 AA; 53190 MW; DADF0D198B39CD0D CRC64;
MSLEPPTYLS SLQNNIRARP IPWEGAVRAG NITDEHLKKI KAVDKVRKDQ RRQTVEGDLA
GYTDLLAGGA QGKSVLNSAS RRTDIVQYIL VLASDLIQDV PSLANSLVSH PEPYKPFLPF
LQHSTNAEDP IPLLTSTFLT ALVSHSLVAS SKPAPRDNQA LPQLYTYLST LTKNQDSGLQ
DIGVQGFSEL LRTSRAREIF WAQRQETLTP LIDTLRAAAG AKDNVSNAST LGSSTRSVEP
GLAGGVGLQL LYRVLLVLWQ LAFEGALVGE ELQENYEIIQ LYIHLLRLSP KEKTTRLLVA
TVYSLCSSNR TTLLPIAVFL RLPALLTNLA GRHLTDPDLL EDLSALSSML EEYTKTQTTF
DEYAAEVQTG HLRWSPPHKN PTFWKDNARR IVEESNGALP KKLAEILSKS WENDKQVLAI
ACSDVGHLVK EVPERRRQLE RLGLKTRVME LMVDQDESVR WESLHAVGEW LRYTFEG
//
