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Database: UniProt
Entry: A0A162I5X9_9HYPO
LinkDB: A0A162I5X9_9HYPO
Original site: A0A162I5X9_9HYPO 
ID   A0A162I5X9_9HYPO        Unreviewed;       864 AA.
AC   A0A162I5X9;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, 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=BBO_00546 {ECO:0000313|EMBL:OAA52705.1};
OS   Beauveria brongniartii RCEF 3172.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria;
OC   Beauveria brongniartii.
OX   NCBI_TaxID=1081107 {ECO:0000313|EMBL:OAA52705.1, ECO:0000313|Proteomes:UP000076863};
RN   [1] {ECO:0000313|EMBL:OAA52705.1, ECO:0000313|Proteomes:UP000076863}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCEF 3172 {ECO:0000313|EMBL:OAA52705.1,
RC   ECO:0000313|Proteomes:UP000076863};
RX   PubMed=27071652; DOI=10.1093/gbe/evw082;
RA   Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT   "Divergent and convergent evolution of fungal pathogenicity.";
RL   Genome Biol. Evol. 8:1374-1387(2016).
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:OAA52705.1}.
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DR   EMBL; AZHA01000001; OAA52705.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A162I5X9; -.
DR   OrthoDB; 1967517at2759; -.
DR   Proteomes; UP000076863; 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   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..448
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361189"
FT   TRANSMEM        460..485
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..606
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361189"
FT   TRANSMEM        646..665
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361189"
FT   COILED          101..128
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          281..308
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   864 AA;  97945 MW;  9917D5D5867B47EE CRC64;
     MAPKQDTPFR SADMSMVQLY VSNEIGREVV TALGELGLCQ FRDLNEDVSA FQRTYTQEIR
     RLDNVERQLR YFNSQMEKTG IALRKLDLDT ESLACPSTTE IDELAERSEK LEQRVSALND
     SYETLKKREG DLTEWRWVLR EAGSFFDRAH GNVDEIRASM DNNQDDAPLL ADVEQHRAAP
     EVERSFGGMN IGFVAGVIAR DRVAAFERIL WRTLRGNLYM NQSEIPEPLI NPVNNEAVDK
     NVFVIFAHGK EIIAKIRKIS ESMGAEVYSV DENSDLRRDQ IHEVNNRLQD VQNVLQNTQA
     TLQAELNQIS QSLSAWMVLI AKEKAVYGTL NLFSYDRARR TLIAEGWCPT NDLPLIRSTL
     QDVTNRAGLS VPSIINEIRT NKKPPTYLKT NKFTEGFQTI VNAYGTATYQ EVNPAMPVIV
     TFPFLFAVMF GDFGHAVIML SAALAMIYWE RSLKKVTFEL FAMVFYGRYI ALVMAVFSLF
     TGLIYNDAFS KSMTLFDSAW EFKVPEKGFK EGQTIEGTLN GHGYRYPFGL DSAWHGTDND
     LLFSNSYKMK MSILLGWAHM TYSLIFAYVN ARHFRKPIDI WGNFVPGMIF FQSIFGYLVV
     CIIYKWTVDW EAADKPAPGL LNMLIYMFLQ PGTLAGGERL YAGQEYVQVG LLLLAFAQVP
     VLLFLKPFYL RWEHNRARAK GYRGLGETSR VSALDEDDEG EGLIHGGGHG NSIDDGEGVA
     MISQNVDEEH EEFEFSEVMI HQVIHTIEFC LNCVSHTASY LRLWALSLAH QQLSVVLWTM
     TIGLCLPMTG VVGVIAIVIG FYMWFFLTIA ILVCMEGTSA MLHSLRLAWV ESFSKFAEFA
     GWPFVPFSFA ALLEESEELK EYLG
//
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