ID W9CRU6_SCLBF Unreviewed; 669 AA.
AC W9CRU6;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=V-type proton ATPase catalytic subunit A {ECO:0000256|ARBA:ARBA00018860};
DE EC=7.1.2.2 {ECO:0000256|ARBA:ARBA00012473};
GN ORFNames=SBOR_1041 {ECO:0000313|EMBL:ESZ98591.1};
OS Sclerotinia borealis (strain F-4128).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Sclerotinia.
OX NCBI_TaxID=1432307 {ECO:0000313|EMBL:ESZ98591.1, ECO:0000313|Proteomes:UP000019487};
RN [1] {ECO:0000313|EMBL:ESZ98591.1, ECO:0000313|Proteomes:UP000019487}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F-4157 {ECO:0000313|Proteomes:UP000019487};
RX PubMed=24459262; DOI=10.1128/genomeA.01175-13;
RA Mardanov A.V., Beletsky A.V., Kadnikov V.V., Ignatov A.N., Ravin N.V.;
RT "Draft genome sequence of Sclerotinia borealis, a psychrophilic plant
RT pathogenic fungus.";
RL Genome Announc. 2:E0117513-E0117513(2014).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate;
CC Xref=Rhea:RHEA:57720, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.1.2.2;
CC Evidence={ECO:0000256|ARBA:ARBA00001741};
CC -!- SUBCELLULAR LOCATION: Endomembrane system
CC {ECO:0000256|ARBA:ARBA00029433}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00029433}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00029433}. Vacuole membrane
CC {ECO:0000256|ARBA:ARBA00029427}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00029427}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00029427}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000256|ARBA:ARBA00008936}.
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:ESZ98591.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AYSA01000039; ESZ98591.1; -; Genomic_DNA.
DR AlphaFoldDB; W9CRU6; -.
DR STRING; 1432307.W9CRU6; -.
DR HOGENOM; CLU_008162_3_1_1; -.
DR OrthoDB; 5473187at2759; -.
DR Proteomes; UP000019487; Unassembled WGS sequence.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0033180; C:proton-transporting V-type ATPase, V1 domain; IEA:InterPro.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-EC.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:UniProtKB-EC.
DR CDD; cd18111; ATP-synt_V_A-type_alpha_C; 1.
DR CDD; cd18119; ATP-synt_V_A-type_alpha_N; 1.
DR CDD; cd01134; V_A-ATPase_A; 1.
DR Gene3D; 2.40.30.20; -; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_00309; ATP_synth_A_arch; 1.
DR InterPro; IPR031686; ATP-synth_a_Xtn.
DR InterPro; IPR023366; ATP_synth_asu-like_sf.
DR InterPro; IPR020003; ATPase_a/bsu_AS.
DR InterPro; IPR004100; ATPase_F1/V1/A1_a/bsu_N.
DR InterPro; IPR036121; ATPase_F1/V1/A1_a/bsu_N_sf.
DR InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR InterPro; IPR024034; ATPase_F1/V1_b/a_C.
DR InterPro; IPR005725; ATPase_V1-cplx_asu.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR022878; V-ATPase_asu.
DR NCBIfam; TIGR01042; V-ATPase_V1_A; 1.
DR PANTHER; PTHR43607; V-TYPE PROTON ATPASE CATALYTIC SUBUNIT A; 1.
DR PANTHER; PTHR43607:SF1; V-TYPE PROTON ATPASE CATALYTIC SUBUNIT A; 1.
DR Pfam; PF00006; ATP-synt_ab; 1.
DR Pfam; PF02874; ATP-synt_ab_N; 1.
DR Pfam; PF16886; ATP-synt_ab_Xtn; 1.
DR SUPFAM; SSF47917; C-terminal domain of alpha and beta subunits of F1 ATP synthase; 1.
DR SUPFAM; SSF50615; N-terminal domain of alpha and beta subunits of F1 ATP synthase; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000019487};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 80..142
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02874"
FT DOMAIN 158..279
FT /note="ATPsynthase alpha/beta subunit N-terminal extension"
FT /evidence="ECO:0000259|Pfam:PF16886"
FT DOMAIN 288..513
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit
FT nucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF00006"
SQ SEQUENCE 669 AA; 73934 MW; C347B06650D22D8C CRC64;
MSLGLRPRLK ARPSFLDLIQ IQHIDTLSIA PVELNQEPLP QLPLSPPPTT IQFAFSKSSK
EIAKMAPQRD ADGEEQFGSI YSVSGPVVVA ENMIGVAMYE LVRVGHDNLV GEVIRIEADR
ATIQVYEETA GVTVGDPVVR TGKPLSVELG PGLMETIYDG IQRPLKAIAD VSNSIYIPRG
ISAPALNREK DWDFKPIMKV GDHITGGDIW GTVYENSLLD DHKILFPPRA RGTITRIAEK
GSYKVDQKIL EAEFDGKKTE YSMMHTWPVR VPRPTTEKLA ADKPFIVGQR VLDALFPSVQ
GGTVAIPGAF GCGKTVISQS VSKFSNSDII IYVGCGERGN EMAEVLMDFP ELSIEIDGRK
EPIMKRTTLI ANTSNMPVAA REASIYTGIT VAEYFRDQGK DVAMMADSTS RWAEALREIS
GRLGEMPADQ GFPAYLGAKL ASFYERAGKV QALGSPDREG SVSIVGAVSP PGGDFSDPVT
SSTLGIVQVF WGLDKKLAQR KHFPSINTSV SYSKYTGVLD KYYEKDFPEF PRLRDRIKQL
LTDSEELDQV VQLVGKSALS DPDKITLDVA ALIKEDFLQQ NGYSDYDQFC PIWKTEWMMK
AMMGFHDEAQ KAIAQGQSWN KVREATSELQ SQLRSMKFEV PSEGEEKITK KYEDLVQAMT
DKFASVTDE
//