ID A0A0B2WVX7_METAS Unreviewed; 792 AA.
AC A0A0B2WVX7;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
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=MAM_02225 {ECO:0000313|EMBL:KHO00302.1};
OS Metarhizium album (strain ARSEF 1941).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=1081103 {ECO:0000313|EMBL:KHO00302.1, ECO:0000313|Proteomes:UP000030816};
RN [1] {ECO:0000313|EMBL:KHO00302.1, ECO:0000313|Proteomes:UP000030816}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 1941 {ECO:0000313|EMBL:KHO00302.1,
RC ECO:0000313|Proteomes:UP000030816};
RX PubMed=25368161; DOI=10.1073/pnas.1412662111;
RA Hu X., Xiao G., Zheng P., Shang Y., Su Y., Zhang X., Liu X., Zhan S.,
RA St Leger R.J., Wang C.;
RT "Trajectory and genomic determinants of fungal-pathogen speciation and host
RT adaptation.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:16796-16801(2014).
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:KHO00302.1}.
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DR EMBL; AZHE01000003; KHO00302.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B2WVX7; -.
DR STRING; 1081103.A0A0B2WVX7; -.
DR HOGENOM; CLU_008162_3_0_1; -.
DR OrthoDB; 5473187at2759; -.
DR Proteomes; UP000030816; 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; 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.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000030816};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 203..265
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02874"
FT DOMAIN 281..402
FT /note="ATPsynthase alpha/beta subunit N-terminal extension"
FT /evidence="ECO:0000259|Pfam:PF16886"
FT DOMAIN 411..635
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit
FT nucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF00006"
FT REGION 22..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..164
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 792 AA; 84861 MW; 1BF3FB6782F0E5D7 CRC64;
MQPGLRPRLK ARPSLLDLVR HRSNSFSSSR AGTSDSASAV ELPLPASPGA GAGAGVGVGG
AWSWSPAGSR RGSLLAASAL GPAASPASPS PSVVEVEAPA PAAAPTGAPA VGSPLAPASA
TSSPPPSPPG TELPLNSPFS PSPPLPASPS PSTSTPPSPP RPSPVSQRSS SAHQEPEPTS
SNPPKMPSKT KNAGDEAIHY GKIYSISGPV IVAEDMIGVA MYELVKVGHD NLVGEVIRIN
GDQASIQVYE ETAGVKVGDP VARSGKPLSV ELGPGLLNGI YDGIQRPLEE ISKVSKTIYI
PRGISVPALD RKKKWQFTPA KKVGDHIAGG DVWGNVFENS FISNHRILFP PRARGIITKI
APKGEYTVAE NILEVEFDGK KTEYPMMQSW PVRVPRPTTE KLAADQPFLV GQRVLDALFP
SVQGGTVAIP GAFGCGKTVI SQSVSKFSNS DVIVYVGCGE RGNEMAEVLK DFPELSIDVD
GRKEPIMKRT TLIANTSNMP VAAREASIYT GITVAEYFRD QGLDVAMMAD STSRWAEALR
ELSGRLGEMP ADQGFPAYLS AKLASFYERA GKVQSLGSPE RHGSVSIVGA VSPPGGDFSD
PVTTSTLGIV QVFWGLDKKL AQRKHFPSIN TSVSYTKYTT VLDKFYEKDY PEFPRLRDRI
KQLISDSEEL DQVVQLVGKS ALSDPDKITL DLAALIKEDF LQQNGYSDYD QFCPIWKTEW
MMKLMVGFHD ESQKAIAQGQ SWGKVREATG DLQAKLKQLK FELPSDGQEV VTKKYEAIQQ
EMMDRFASVI DE
//
