ID G3YGG5_ASPNA Unreviewed; 478 AA.
AC G3YGG5;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 22-FEB-2023, entry version 45.
DE RecName: Full=V-type proton ATPase subunit H {ECO:0000256|PIRNR:PIRNR032184};
GN ORFNames=ASPNIDRAFT_55847 {ECO:0000313|EMBL:EHA17918.1};
OS Aspergillus niger (strain ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 /
OS NCTC 3858a / NRRL 328 / USDA 3528.7).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=380704 {ECO:0000313|EMBL:EHA17918.1, ECO:0000313|Proteomes:UP000009038};
RN [1] {ECO:0000313|EMBL:EHA17918.1, ECO:0000313|Proteomes:UP000009038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a /
RC NRRL 328 / USDA 3528.7 {ECO:0000313|Proteomes:UP000009038};
RX PubMed=21543515; DOI=10.1101/gr.112169.110;
RA Andersen M.R., Salazar M.P., Schaap P.J., van de Vondervoort P.J.,
RA Culley D., Thykaer J., Frisvad J.C., Nielsen K.F., Albang R., Albermann K.,
RA Berka R.M., Braus G.H., Braus-Stromeyer S.A., Corrochano L.M., Dai Z.,
RA van Dijck P.W., Hofmann G., Lasure L.L., Magnuson J.K., Menke H.,
RA Meijer M., Meijer S.L., Nielsen J.B., Nielsen M.L., van Ooyen A.J.,
RA Pel H.J., Poulsen L., Samson R.A., Stam H., Tsang A., van den Brink J.M.,
RA Atkins A., Aerts A., Shapiro H., Pangilinan J., Salamov A., Lou Y.,
RA Lindquist E., Lucas S., Grimwood J., Grigoriev I.V., Kubicek C.P.,
RA Martinez D., van Peij N.N., Roubos J.A., Nielsen J., Baker S.E.;
RT "Comparative genomics of citric-acid-producing Aspergillus niger ATCC 1015
RT versus enzyme-producing CBS 513.88.";
RL Genome Res. 21:885-897(2011).
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:EHA17918.1}.
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DR EMBL; ACJE01000021; EHA17918.1; -; Genomic_DNA.
DR AlphaFoldDB; G3YGG5; -.
DR STRING; 380704.G3YGG5; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1168662; -.
DR HOGENOM; CLU_025709_4_0_1; -.
DR Proteomes; UP000009038; 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}; Transport {ECO:0000256|PIRNR:PIRNR032184}.
FT DOMAIN 358..476
FT /note="ATPase V1 complex subunit H C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11698"
SQ SEQUENCE 478 AA; 53411 MW; E1803717690D9292 CRC64;
MSSLPLEPPT YLSSLQNNIR ARPIPWEGAV RAGNITDDHL KKIKAVDKVR KEQRRQTVEG
DLAGYVGLLS GGSEGKSVLD SASRRTDIVQ YILVLAADLI NDVPSLSTAL VAHPDPYKPF
LPLLRHSTNP EDPIPLLTST FLTNLVSVSL SSSSKPAARD DEALPQLYTY LSTLTQNQDS
GLQDIGVQEL SALLRTSRSR EIFWKQRQQT VEPLVEILRA ATGAKDSSSS TLAGSSRAIE
PGLAGGVGLQ LLYRVLLVLW QLSFEGELIG DDLQADYEFV QLYTHLLRLS PKEKTTRLLL
ATLNNLLSSN RTTLLPVAVF VRLPALLTNL AGRHLTDPDL LEDLTFLSEM LDEYTKTQTT
FDQYAAELQS GHLRWSPPHR NPTFWKDNAR RILDENNGAL PKKLSEIISK SWDNDKQVLA
IACNDVGHLV KELPERRAQL EKLGLKTRVM ELMTDKDESV RWESLRAVGE WLRYTFDD
//
