ID A0A0F9Y692_TRIHA Unreviewed; 858 AA.
AC A0A0F9Y692;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=V-type proton ATPase subunit a {ECO:0000256|RuleBase:RU361189};
GN ORFNames=THAR02_00268 {ECO:0000313|EMBL:KKP07593.1};
OS Trichoderma harzianum (Hypocrea lixii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=5544 {ECO:0000313|EMBL:KKP07593.1, ECO:0000313|Proteomes:UP000034112};
RN [1] {ECO:0000313|Proteomes:UP000034112}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T6776 {ECO:0000313|Proteomes:UP000034112};
RX PubMed=26067977; DOI=10.1128/genomeA.00647-15;
RA Baroncelli R., Piaggeschi G., Fiorini L., Bertolini E., Zapparata A.,
RA Pe M.E., Sarrocco S., Vannacci G.;
RT "Draft whole-genome sequence of the biocontrol agent Trichoderma harzianum
RT T6776.";
RL Genome Announc. 3:E0064715-E0064715(2015).
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:KKP07593.1}.
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DR EMBL; JOKZ01000004; KKP07593.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F9Y692; -.
DR OMA; FYLWFFL; -.
DR OrthoDB; 1967517at2759; -.
DR Proteomes; UP000034112; 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:UP000034112};
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 548..566
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 578..603
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 646..665
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 780..808
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT COILED 101..128
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 279..306
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 858 AA; 97989 MW; 0C932723313C41D8 CRC64;
MAPRKDTPFR SAEMSMVQLY VSNEIGREVV TALGELGLCQ FRDLNEDVSA FQRTFTQEIR
RLDNVERQLR YFYAQMEKAG IPLRKLDLDA EKLASPSTSE IDELAERAQK LEQRISALND
SYETLKKREG DLTEWRWVLR EAGSFFDRAH GNVDEIRAST DNDDAPLLSD IEQHNTAPDV
ERSFSGMNIG FVAGVINRDR VAAFERILWR TLRGNLYMNQ SEIPEPLIDP TNNEAIQKNV
FVIFAHGKEI LSKIRKISES MGADVYNVDE NSDLRRDQIH EVNNRLEDVQ NVLRNTQATL
EAELNQISQS LAPWTVLIAK EKAVYSTLNL LSYDSARRTL IAEAWCPTND MPLIRSTLQD
VTNRAGLSVP SIVNEIITNK KPPTYLKTNK FTEGFQTIVN AYGTATYQEV NPALPVIVTF
PFLFAVMFGD LGHAVIMLSA ALAMIYWEKS LKKVSFELFA MIFYGRYIAL VMAVFSVFTG
LMYNDIFSKS MTLWGSAWEY ERPEHWSEGT PVIATLNDEG YRYPFGLDWA WHGTENNLLF
TNSYKMKMSI ILGWAHMTYS LCFSYINARH FKKPIDIWGN FIPGMIFFQS IFGYLVVCII
YKWSVDWNAV GRAPPGLLNM LIYMFLQPGK LDERLYAGQE YVQSILLLLA FVQVPILLFL
KPFYLRWENN KTRARGYRGL GETSRVSALD GDDENEALVN GHGNSFDDGE GVAMISQNID
DDEHEEFEFS EVMIHQIIHT IEFCLNCVSH TASYLRLWAL SLAHQQLSVV LWDMTIGPCL
ATGGVLGVIM IVIGFYLWFF LTIAILVCME GTSAMLHSLR LAWVESFSKF AEFNGWPFAP
FSFNTLIEES EELKNYLE
//