ID A0A1L9UH64_ASPBC Unreviewed; 850 AA.
AC A0A1L9UH64;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=V-type proton ATPase subunit a {ECO:0000256|RuleBase:RU361189};
GN ORFNames=ASPBRDRAFT_43912 {ECO:0000313|EMBL:OJJ71017.1};
OS Aspergillus brasiliensis (strain CBS 101740 / IMI 381727 / IBT 21946).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=767769 {ECO:0000313|EMBL:OJJ71017.1, ECO:0000313|Proteomes:UP000184499};
RN [1] {ECO:0000313|Proteomes:UP000184499}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101740 / IMI 381727 / IBT 21946
RC {ECO:0000313|Proteomes:UP000184499};
RX PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K., Battaglia E.,
RA Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C., Canovas D.,
RA Cerqueira G.C., Chen F., Chen W., Choi C., Clum A., Dos Santos R.A.,
RA Damasio A.R., Diallinas G., Emri T., Fekete E., Flipphi M., Freyberg S.,
RA Gallo A., Gournas C., Habgood R., Hainaut M., Harispe M.L., Henrissat B.,
RA Hilden K.S., Hope R., Hossain A., Karabika E., Karaffa L., Karanyi Z.,
RA Krasevec N., Kuo A., Kusch H., LaButti K., Lagendijk E.L., Lapidus A.,
RA Levasseur A., Lindquist E., Lipzen A., Logrieco A.F., MacCabe A.,
RA Maekelae M.R., Malavazi I., Melin P., Meyer V., Mielnichuk N., Miskei M.,
RA Molnar A.P., Mule G., Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P.,
RA Overkamp K.M., Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F.,
RA Ramon A., Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E., Sanguinetti M.,
RA Schuetze T., Sepcic K., Shelest E., Sherlock G., Sophianopoulou V.,
RA Squina F.M., Sun H., Susca A., Todd R.B., Tsang A., Unkles S.E.,
RA van de Wiele N., van Rossen-Uffink D., Oliveira J.V., Vesth T.C.,
RA Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B., Baker S.E.,
RA Benoit I., Brakhage A.A., Braus G.H., Fischer R., Frisvad J.C.,
RA Goldman G.H., Houbraken J., Oakley B., Pocsi I., Scazzocchio C.,
RA Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S., Grigoriev I.V.;
RT "Comparative genomics reveals high biological diversity and specific
RT adaptations in the industrially and medically important fungal genus
RT Aspergillus.";
RL Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(2017).
CC -!- FUNCTION: Essential component of the vacuolar proton pump (V-ATPase), a
CC multimeric enzyme that catalyzes the translocation of protons across
CC the membranes. Required for assembly and activity of the V-ATPase.
CC {ECO:0000256|RuleBase:RU361189}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the V-ATPase 116 kDa subunit family.
CC {ECO:0000256|ARBA:ARBA00009904, ECO:0000256|RuleBase:RU361189}.
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DR EMBL; KV878685; OJJ71017.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1L9UH64; -.
DR STRING; 767769.A0A1L9UH64; -.
DR VEuPathDB; FungiDB:ASPBRDRAFT_43912; -.
DR OMA; FYLWFFL; -.
DR OrthoDB; 1967517at2759; -.
DR Proteomes; UP000184499; Unassembled WGS sequence.
DR GO; GO:0000220; C:vacuolar proton-transporting V-type ATPase, V0 domain; IEA:InterPro.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR InterPro; IPR002490; V-ATPase_116kDa_su.
DR InterPro; IPR026028; V-type_ATPase_116kDa_su_euka.
DR PANTHER; PTHR11629:SF63; V-TYPE PROTON ATPASE SUBUNIT A; 1.
DR PANTHER; PTHR11629; VACUOLAR PROTON ATPASES; 1.
DR Pfam; PF01496; V_ATPase_I; 1.
DR PIRSF; PIRSF001293; ATP6V0A1; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781,
KW ECO:0000256|RuleBase:RU361189};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW ECO:0000256|RuleBase:RU361189};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361189};
KW Reference proteome {ECO:0000313|Proteomes:UP000184499};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU361189};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU361189};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU361189}.
FT TRANSMEM 425..450
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 462..482
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 547..567
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 579..602
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 644..661
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 785..806
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT COILED 100..127
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 850 AA; 96878 MW; 3FE2B2656907B6E1 CRC64;
MAPRDTLFRS SEMSLTQLYI ANEIGREVVS ALGELGQVQF RDLNPDTNAF QRTFTKEIRR
LDNVERQLRY FHAQMDKASI PMRSSSEFSD TLAAPLASEI DELAERSESL EQRIASLNDS
YETLKKREVE LTEWRWVLRE AGGFFDRAHS HTEEIRQSFD NDEAPLLRDV EQQSRGPNGD
AQGQQSFLEM NIGFVAGVIP RDRIGAFERI LWRTLRGNLY MNQSEIPEAI IDPTTNEESH
KNVFVIFAHG KSIIAKIRKI SESLGASLYN VDENSELRRD QIHEVNTRLG DVGNVLRNTK
NTLDAELTQI ARSLAAWMII VKKEKAVYDT LNKFSYDQAR KTLIAEAWCP TNSLGLIKST
LQDVNDRAGL SVPTIVNQIK TNKTPPTYMR TNKFTQAFQT IVDAYGISKY SEANPGLYTI
VTFPFLFAVM FGDFGHGALM TMAAAAMIFW ERKLAKAKLD ELTYMAFYGR YIMLMMGLFS
MYTGLLYNDV FSKSFTVFPS QWQWPDDIKQ GQTVEASLKP GYRFPFGLDW NWHEAENSLL
FTNSLKMKMS ICLGWAHMTY ALCLQYVNAR HFKSKVDVIG NFIPGMIFFQ SIFGYLVLTI
LYKWSVDWEA RGQSPPGLLN MLIFMFLSPG TVEEQLYPGQ ASVQVLLLLL AVIQVPIMLF
FKPFYLRWEH NRARALGYRG LGEPSRVSAL EDDADGGRDS MASDGEGVAM IAQDLGDEEH
EEFDFGEIMI HQVIHTIEFC LNCISHTASY LRLWALSLAH QQLSIVLWDM TIGGAFEQDS
PTMRVIMIVV TFYLWFTLTI AILCVMEGTS AMLHSLRLHW VEAMSKHFMG EGIPFTPFSF
QTLLEEDPVD
//
