ID A0A139H368_9PEZI Unreviewed; 858 AA.
AC A0A139H368;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 22-FEB-2023, entry version 14.
DE RecName: Full=V-type proton ATPase subunit a {ECO:0000256|RuleBase:RU361189};
GN ORFNames=AC578_7419 {ECO:0000313|EMBL:KXS96861.1};
OS Pseudocercospora eumusae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX NCBI_TaxID=321146 {ECO:0000313|EMBL:KXS96861.1, ECO:0000313|Proteomes:UP000070133};
RN [1] {ECO:0000313|EMBL:KXS96861.1, ECO:0000313|Proteomes:UP000070133}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 114824 {ECO:0000313|EMBL:KXS96861.1,
RC ECO:0000313|Proteomes:UP000070133};
RA Chang T.-C., Salvucci A., Crous P.W., Stergiopoulos I.;
RT "Comparative genomics of the Sigatoka disease complex on banana suggests a
RT link between parallel evolutionary changes in Pseudocercospora fijiensis
RT and Pseudocercospora eumusae and increased virulence on the banana host.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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:KXS96861.1}.
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DR EMBL; LFZN01000161; KXS96861.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A139H368; -.
DR STRING; 321146.A0A139H368; -.
DR OrthoDB; 1967517at2759; -.
DR Proteomes; UP000070133; 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:UP000070133};
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 424..449
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 470..491
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 551..569
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 581..604
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 647..668
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 760..778
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 790..812
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT COILED 101..128
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 858 AA; 97634 MW; 4AA7BA1C391757FE CRC64;
MAPNSESLFR SQDMTLTQLY VANEIGREVV SALGELGVMQ FRDLNPETTA FQRTFTQEIR
RLDNVERQLN YFRSQIEKNS IEMRSIYDFS DAIAAPSASE IDELADRSQQ LEQRIQSLNE
SYETLKKREV ELTEWRWVLR EAGGFFDRAR GQTEEIRQSI DSSDDAPLLR DVENANGSAE
GGQQSFSVMN IGFVAGVIPR ERMGAFERIL WRTLRGNLYM NQSEIPDAII DPEKNEEHHK
NVFVIFAHGK EIIAKIRKIS ESLGADIYNV DENSELRRDQ IHEVNSRLQD LGNVLGNTKR
TLDAELTQIG RSLAAWMIVI KKEKSVYQTL NRFSYDPARK TLVAEAWCPT SSLGLIKSTL
QDVNERAGLS VPTIVNQIKT SKTPPTYNKT NKFTLGFQTI IDAYGTAKYT EVNPGLPTIV
TFPFLFAVMF GDFGHGAIMT LAAIAMIIFE KPLQRGKQDE LFGMAFYGRY IMLMMGIFSM
YTGLIYCDAF SKEIPLFSSM WEWDFPDNYI PDKTTITAKR VEGYTYPFGL DWRWHDTEND
LLFSNSYKMK LSIIMGWAHM TYSLCLSYVN ARHFKSNIDI WGNFIPGMIF FQGIFGYLVL
TIVWKWCVDW YAIGEQPPNL LNMLIYMFLS PGTVEERLYS GQGGVQVILV LLAVIQVPIM
LFLKPFYLRW EHNRARAKGY RGIGETTAVS ALDDAGDHAN GDAGRPSFAE SDLDGAVITQ
DIGGDEHEEF EFSEIMIHQV IHTIEFCLNC VSHTASYLRL WALSLAHQQL SIVLWSMTLK
NAFAFEGATG IVVIFLAFVV WFALTIAVLV VMEGTSAMLH SLRLHWVEAM SKHFIGEGVA
FEPFSFKQML DDEMTELK
//