ID B8NJT6_ASPFN Unreviewed; 476 AA.
AC B8NJT6;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 24-JAN-2024, entry version 75.
DE RecName: Full=V-type proton ATPase subunit H {ECO:0000256|PIRNR:PIRNR032184};
GN ORFNames=AFLA_068960 {ECO:0000313|EMBL:EED50074.1};
OS Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS / JCM 12722 / SRRC 167).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=332952 {ECO:0000313|EMBL:EED50074.1, ECO:0000313|Proteomes:UP000001875};
RN [1] {ECO:0000313|EMBL:EED50074.1, ECO:0000313|Proteomes:UP000001875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 /
RC SRRC 167 {ECO:0000313|Proteomes:UP000001875};
RX PubMed=25883274; DOI=10.1128/genomeA.00168-15;
RA Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT aflatoxin contamination of food and feed.";
RL Genome Announc. 3:E0016815-E0016815(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; EQ963479; EED50074.1; -; Genomic_DNA.
DR RefSeq; XP_002380455.1; XM_002380414.1.
DR AlphaFoldDB; B8NJT6; -.
DR STRING; 332952.B8NJT6; -.
DR EnsemblFungi; EED50074; EED50074; AFLA_068960.
DR VEuPathDB; FungiDB:AFLA_008833; -.
DR eggNOG; KOG2759; Eukaryota.
DR HOGENOM; CLU_025709_4_0_1; -.
DR OMA; DMLQEDK; -.
DR Proteomes; UP000001875; 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..474
FT /note="ATPase V1 complex subunit H C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11698"
SQ SEQUENCE 476 AA; 53059 MW; 5C91175F7A55C9B2 CRC64;
MSTMPLEPPM YLSSLQNNIR ARPIPWEGAV RAGNITDDHL KKIKAVDKVR KDQRRQTVEG
DISGYVTLLS GSADAKSVLD SASRRTDIVQ YILVLAADLI NDVPALSSAL IAHPDPYKPF
LPLLRHSTNA EDPIPLLTST FLTNLVSISL ASSSKSAARD EEALPQLYTY LSSLTQNQDS
GLQDIGVQEL SALLRTSRSR EIFWKQRGET VTPLIEILRA ATGGKDTSSS TVAGSSRAIE
PGLSGGVGLQ LLYRVLLVIW QLSFEGALIG DDLQADHEFL QLYTYLLRLS PKEKTTRLLL
ATLNNLLSSN RTTLLPVAVF VRLPALLSNL SGRHLTDPDL LEDLKTLSDM LDEYTKTQTT
FDQYAAELQS GHLRWSPPHR NPTFWKDNAR RILDDANLPR KLAEIISKEW DNDKQVLAIA
CNDVGHLVKE LPGRRAQLEK LGLKARVMEL MADKDESVRW ESLRAVGEWL RYTFDD
//