ID   A0A136IXL0_9PEZI        Unreviewed;       865 AA.
AC   A0A136IXL0;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   28-JUN-2023, entry version 16.
DE   RecName: Full=V-type proton ATPase subunit a {ECO:0000256|RuleBase:RU361189};
GN   ORFNames=Micbo1qcDRAFT_149255 {ECO:0000313|EMBL:KXJ89621.1};
OS   Microdochium bolleyi.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Microdochiaceae; Microdochium.
OX   NCBI_TaxID=196109 {ECO:0000313|EMBL:KXJ89621.1, ECO:0000313|Proteomes:UP000070501};
RN   [1] {ECO:0000313|Proteomes:UP000070501}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J235TASD1 {ECO:0000313|Proteomes:UP000070501};
RG   DOE Joint Genome Institute;
RA   David A.S., May G., Haridas S., Lim J., Wang M., Labutti K., Lipzen A.,
RA   Barry K., Grigoriev I.V.;
RT   "Draft genome sequence of Microdochium bolleyi, a fungal endophyte of
RT   beachgrass.";
RL   Submitted (FEB-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}.
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DR   EMBL; KQ964254; KXJ89621.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A136IXL0; -.
DR   STRING; 196109.A0A136IXL0; -.
DR   InParanoid; A0A136IXL0; -.
DR   OrthoDB; 1967517at2759; -.
DR   Proteomes; UP000070501; 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:UP000070501};
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        422..446
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361189"
FT   TRANSMEM        458..483
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361189"
FT   TRANSMEM        547..565
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361189"
FT   TRANSMEM        577..602
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361189"
FT   TRANSMEM        639..659
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361189"
FT   TRANSMEM        795..816
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361189"
FT   REGION          682..707
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          101..128
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          279..306
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        684..699
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   865 AA;  98630 MW;  CDC15293DE7F327B CRC64;
     MAPSQQSMFR SADMSLVQLY ISNEIGRECV NALGELGLVQ FRDLNKSVSA FQRTFTQEIR
     RLDNVERQLR YFHAQMDKSS IPVRKFDLDN ETLPPPTTTE IDELAERSQS LEQRIFQLND
     SYETLKKREV ELTEWRWVLR EAGGFFDRAH GNVEEIRAST EEDDAPLLRD VEQHSQAPDA
     ERSFSGMNIG FVAGVIPRDR VAAFERILWR TLRGNLYMNQ SEIPEPLANP STNETVNKNV
     FVIFAHGKEI LAKIRKISES MGAEIYTVDE NSDLRRDQVH EVNARLNDVQ NVLQNTQQTL
     EAELTQIAQS LSAWMILITK EKAAYQTLNL FSFDRQRRTL IAEAWVPKND LSRIRTVLQD
     VTNQAGLSVP SIINEIKTNK TPPTYLKTNK FTEAFQTIIN AYGTASYQEV NPALPAIVTF
     PFLFAVMFGD LGHAVIMLSS ALAMIYWEKP LKKVTFELFA MIYYGRYIAL VMSIFSVFTG
     LIYNDVFSKS LTLFETSWEW VVPDGWSEHQ PLFAQPKEGY RYPFGLDWTW HGTENALLFS
     NSYKMKMSII LGWAHMTYSL CLSYFNARHH KKPIDIWGNF IPGMIFFQSI FGYLVLCIIY
     KWSVDWLGTG RQPPGLLNML IYMFLQPGTL DVQFYSGQAG VQTCLLLLAF SQVPVMLFLK
     PFYLRWEHNK TRGRGYRGIG EPSRVSAVDD EDDGHANGRI SIDTDGGDGV ALLGHNGGAD
     DDDDEEGDGH HKEFEFSEEM IHQVIHTIEF CLNCVSHTAS YLRLWALSLA HQQLSIVLWD
     MTLKTGLVPG GVAGAIYLVI VFYMWFFLSC AILIAMEGCS AMLHSLRLQW VEAQSKYAHF
     EGHMFAPLSF ATLLEEDEGL AEFRG
//