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Database: UniProt
Entry: A0A1J9RLJ9_9PEZI
LinkDB: A0A1J9RLJ9_9PEZI
Original site: A0A1J9RLJ9_9PEZI 
ID   A0A1J9RLJ9_9PEZI        Unreviewed;       855 AA.
AC   A0A1J9RLJ9;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   22-FEB-2023, entry version 17.
DE   RecName: Full=V-type proton ATPase subunit a {ECO:0000256|RuleBase:RU361189};
GN   ORFNames=BKCO1_1000360 {ECO:0000313|EMBL:OJD40842.1};
OS   Diplodia corticola.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC   Diplodia.
OX   NCBI_TaxID=236234 {ECO:0000313|EMBL:OJD40842.1, ECO:0000313|Proteomes:UP000183809};
RN   [1] {ECO:0000313|EMBL:OJD40842.1, ECO:0000313|Proteomes:UP000183809}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 112549 {ECO:0000313|EMBL:OJD40842.1,
RC   ECO:0000313|Proteomes:UP000183809};
RA   Fernandes I., De Jonge R., Van De Peer Y., Devreese B., Alves A.,
RA   Esteves A.C.;
RT   "Proteomics and genomics reveal pathogen-plant mechanisms compatible with a
RT   hemibiotrophic lifestyle of Diplodia corticola.";
RL   Submitted (OCT-2016) 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:OJD40842.1}.
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DR   EMBL; MNUE01000001; OJD40842.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1J9RLJ9; -.
DR   STRING; 236234.A0A1J9RLJ9; -.
DR   OrthoDB; 1967517at2759; -.
DR   Proteomes; UP000183809; 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:UP000183809};
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..448
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361189"
FT   TRANSMEM        468..487
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361189"
FT   TRANSMEM        549..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        645..665
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361189"
FT   COILED          101..128
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   855 AA;  97374 MW;  78FA8E5BC02DC7DC CRC64;
     MAPPQDTLFR SADMSLTQLY ISNEIGREVV SALGELGVMD FRDLNAETTA FQRTFTQEIR
     RLDNVERQLR YFHAQMDKSN IPMRSIYEFN NTLAAPSASE IDELADRSQS LENRIASLNE
     SYETLKKREV ELTEWRWVLR EAGGFFDRAR GQTEEIRHSM DDDPDDDAPL LADVEQRGQN
     GDAERSFSVM NIGFVSGVIP RDRIAAFERI LWRTLRGNLY MNQSEIPEPI INPETNEGIN
     KNVFVIFAHG KEIIAKIRKI SESLGADLYS VDENSDLRRD QIHEVNSRLN DLTAVLRNTK
     QTLDAELTAI GRSLAAWMVV IKKEKAVYQT LNRFSYDQQR KTLIAEAWAP TNSLGLIKST
     LQDVNDRAGL SVPTIVNQIK TTKTPPTYIK TNKFTLAFQT IIDAYGTAKY KEVNPGLPTI
     VTFPFLFAVM FGDFGHGFIM TLAALAMIKW EKQLSRGKLD ELFSMAFFGR YIMLMMGIFS
     MYTGLIYCDA FSKPLPFFKS MWEFPDDFKA GDSVEATRVE GHTYPFGLDW RWHDTENDLL
     FSNSYKMKLS ILMGWAHMTY SLCLSYINAK HFKSPIDIWG NFIPGMIFFQ SIFGYLVFAI
     VYKWSTDWYG IGQAPPGLLN MLIYMFLSPG TIEDPLYNGQ GPLQVILLLL AVIQVPIMLF
     LKPFYLRHEH NKARAHGYRG IGENSRVSAL DDDDEHGHLN GGRESFADDE EGVALISQDV
     SAGGEHEEFE FSEEMIHQVI HTIEFCLNCV SHTASYLRLW ALSLAHQRLS IVLWQMTIGI
     AFSMSGAVGI IAIVCLFYLW FVLTVMVLCI MEGTSAMLHS LRLHWVEAMS KHFIGDGVPF
     EPFSFKVLLE EEPIE
//
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