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Database: UniProt
Entry: A0A2Z6QS40_9GLOM
LinkDB: A0A2Z6QS40_9GLOM
Original site: A0A2Z6QS40_9GLOM 
ID   A0A2Z6QS40_9GLOM        Unreviewed;       827 AA.
AC   A0A2Z6QS40;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   03-MAY-2023, entry version 12.
DE   RecName: Full=V-type proton ATPase subunit a {ECO:0000256|RuleBase:RU361189};
GN   ORFNames=RclHR1_01440029 {ECO:0000313|EMBL:GBB87914.1};
OS   Rhizophagus clarus.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC   Glomeromycetes; Glomerales; Glomeraceae; Rhizophagus.
OX   NCBI_TaxID=94130 {ECO:0000313|EMBL:GBB87914.1, ECO:0000313|Proteomes:UP000247702};
RN   [1] {ECO:0000313|EMBL:GBB87914.1, ECO:0000313|Proteomes:UP000247702}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HR1 {ECO:0000313|EMBL:GBB87914.1,
RC   ECO:0000313|Proteomes:UP000247702};
RA   Kobayashi Y.;
RT   "The genome of Rhizophagus clarus HR1 reveals common genetic basis of
RT   auxotrophy among arbuscular mycorrhizal fungi.";
RL   Submitted (NOV-2017) 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:GBB87914.1}.
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DR   EMBL; BEXD01000491; GBB87914.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2Z6QS40; -.
DR   STRING; 94130.A0A2Z6QS40; -.
DR   Proteomes; UP000247702; 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:UP000247702};
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        408..432
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361189"
FT   TRANSMEM        453..471
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361189"
FT   TRANSMEM        531..552
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361189"
FT   TRANSMEM        564..584
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361189"
FT   TRANSMEM        635..655
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361189"
FT   TRANSMEM        762..783
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361189"
FT   COILED          90..138
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   827 AA;  94479 MW;  3865BEB72918925E CRC64;
     MPYSTLFRSE EMSLIQLYIP SEIAQPTVAE LGELGLIQFR DLNPDVNAFQ RAFVSEIRRY
     DEMERHLRFF EAQITKSDIP VRPLTGINAR VRNAQEVDDL EDKIREHERR ISQMNSSYET
     LQKRYLELTE ARHVLKETAV YFEEVRSLSA PLLDQDVEQG GGGNAGGGES QQMTLGFVTG
     VITRSRMQTF ERILWRALRG NLYLNSAEID ELITDPETDE VLEKNVFIIF AHGKEILNKI
     KKISESLGAT LYPVDDSSDK RQEHYREVNA RIEDLNSVLQ NTNNARRAEL LSIADELTSW
     TTLIKKEKAI YHTMNLFNYD ANRKCLIAEG WCPSNDINLI QQALRTATEE SGTTVPTILH
     ELRTSKEPPT YHRLNKFTSG FQEIVDAYGV AKYREVNPGL FTIITFPFLF AVMFGDFGHG
     IMVTLFALYL VIFEKKLASG KSRGEIFEMF FGGRYIILLM GIFSIYTGLI YNDVFSQPMH
     LAASGWKLTD DPSKPGKLIG QQTGVYPIGV DPVWHGSENF LLFTNSYKMK MSIILGVIQM
     SFGICLSVFN YVHFKKTLSI WTEFIPQMLF MQCIFGYLCF TIIYKWSIPW YETDASGNPR
     VSPPGLLNLL IYMFLQPGHV DKDVELYSGQ GTVQLALIGV AVLCIPWMLF TKPLILRREY
     KKIRAQGYHN PQADVTRIST DENNEHGGAI VAEEMHEEEE FDFGEVMIHQ VIHTIEFCLG
     CISNTASYLR LWALSLAHAQ LSAVLFDMTL KGTIHPKNAL GYILLIITAV LWFVLTVGIL
     LLMEGLSAFL HALRLHWVEF NNKFYEGTGR KFMPFSFKHI FKDSDDE
//
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