ID   A0A1C1CYT1_9EURO        Unreviewed;       765 AA.
AC   A0A1C1CYT1;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=V-type proton ATPase subunit a {ECO:0000256|RuleBase:RU361189};
GN   ORFNames=CLCR_09670 {ECO:0000313|EMBL:OCT53699.1};
OS   Cladophialophora carrionii.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC   Cladophialophora.
OX   NCBI_TaxID=86049 {ECO:0000313|EMBL:OCT53699.1, ECO:0000313|Proteomes:UP000094526};
RN   [1] {ECO:0000313|Proteomes:UP000094526}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KSF {ECO:0000313|Proteomes:UP000094526};
RA   Teixeira M.M., Souza R.C., Almeida L.G., Vicente V.A., de Hoog S.,
RA   Bocca A.L., de Almeida S.R., Vasconcelos A.T., Felipe M.S.;
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:OCT53699.1}.
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DR   EMBL; LGRB01000008; OCT53699.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1C1CYT1; -.
DR   STRING; 86049.A0A1C1CYT1; -.
DR   VEuPathDB; FungiDB:CLCR_09670; -.
DR   VEuPathDB; FungiDB:G647_00640; -.
DR   eggNOG; KOG0003; Eukaryota.
DR   eggNOG; KOG2189; Eukaryota.
DR   Proteomes; UP000094526; 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:UP000094526};
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        426..451
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361189"
FT   TRANSMEM        463..488
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361189"
FT   TRANSMEM        548..568
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361189"
FT   TRANSMEM        580..605
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361189"
FT   TRANSMEM        642..662
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361189"
FT   REGION          690..720
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          101..128
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        690..718
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   765 AA;  87316 MW;  D82D9E52FC164F76 CRC64;
     MAHKDTLFRS ASMSLTQLYI SNEIGREVVS ALGEIGVVQF RDLNSETTAF QRTFTKEIRR
     LDNVERQLRY FKSQMEKSGI EMRSHWDFDE NMLAAPQASE IDELAERSEA LEQRVSNLND
     SYETLKRREV ELTEWRWVLK EAGGFFDRAH GQTDDIRQSI DDDDAPLLRN TEAEEGRANG
     DVAQQQSFAV MNIGFVAGVI PRERLAAFER ILWRTLRGNL YMNQSEIPEP IINPENNEEI
     RKNVFVIFAH GKEIIAKIRK ISESLGADLY NVDENSDLRR DQIHEVNTRL SDLASVLRNT
     KNTLDAELSA IARSLAAWLI VIKKEKAVYN ALNMCSYDQA RKTLIAEAWC PTNTLPQIRA
     TLQDVNDRAG LSVPTIVNQI KTNKTPPTYN KTNKFTEGFQ TIINAYGTAK YQEVNPGLYT
     IVTFPFLFAV MFGDFGHGCL MAMAAAAMIY WEKPLLRSKQ DELFAMAFYG RYIMLMMGIF
     SMYTGLIYND VFSKAFTPFA SAWEYPEDGR PEVTGHLKGS YRYPFGLDWA WHGSENDLLF
     SNSLKMKLSI LMGWAHMTYA LCFSYINARH FKSPIDIWGN FVPGMIFFQA IFGYLSFCIV
     FKWSIDWPAE GRNPPSLLNM LIQMFLAPGT VEDGEQLYSG QAGVQVFLLL IAVVNVPILL
     LLKPLYLRWQ HQKTAAQGYR GIGDTSRVTH ATDLDDDDDN HHANDRHANG RPSEDDDEGA
     MITENIGDDE EEEFEFSEVM IHQTIRKPVH PLVQGLPADM FRRHD
//