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Database: UniProt
Entry: A0A165HTY2_9BASI
LinkDB: A0A165HTY2_9BASI
Original site: A0A165HTY2_9BASI 
ID   A0A165HTY2_9BASI        Unreviewed;       837 AA.
AC   A0A165HTY2;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   25-APR-2018, entry version 5.
DE   RecName: Full=V-type proton ATPase subunit a {ECO:0000256|RuleBase:RU361189};
GN   ORFNames=CALCODRAFT_172130 {ECO:0000313|EMBL:KZT59741.1};
OS   Calocera cornea HHB12733.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Dacrymycetes; Dacrymycetales; Dacrymycetaceae; Calocera.
OX   NCBI_TaxID=1353952 {ECO:0000313|EMBL:KZT59741.1, ECO:0000313|Proteomes:UP000076842};
RN   [1] {ECO:0000313|EMBL:KZT59741.1, ECO:0000313|Proteomes:UP000076842}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB12733 {ECO:0000313|EMBL:KZT59741.1,
RC   ECO:0000313|Proteomes:UP000076842};
RX   PubMed=26659563; DOI=10.1093/molbev/msv337;
RA   Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA   Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K.,
RA   Labutti K., Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T.,
RA   Yoshinaga Y., Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT   "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi
RT   Provides Insights into the Origins of Lignocellulose Decay
RT   Capabilities.";
RL   Mol. Biol. Evol. 33:959-970(2016).
CC   -!- FUNCTION: Essential component of the vacuolar proton pump (V-
CC       ATPase), a multimeric enzyme that catalyzes the translocation of
CC       protons across the membranes. Required for assembly and activity
CC       of the V-ATPase. {ECO:0000256|RuleBase:RU361189}.
CC   -!- SIMILARITY: Belongs to the V-ATPase 116 kDa subunit family.
CC       {ECO:0000256|RuleBase:RU361189}.
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DR   EMBL; KV423937; KZT59741.1; -; Genomic_DNA.
DR   EnsemblFungi; KZT59741; KZT59741; CALCODRAFT_172130.
DR   Proteomes; UP000076842; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000220; C:vacuolar proton-transporting V-type ATPase, V0 domain; IEA:InterPro.
DR   GO; GO:0015078; F:proton transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro.
DR   InterPro; IPR002490; V-ATPase_116kDa_su.
DR   InterPro; IPR026028; V-type_ATPase_116kDa_su_euka.
DR   PANTHER; PTHR11629; PTHR11629; 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   Complete proteome {ECO:0000313|Proteomes:UP000076842};
KW   Hydrogen ion transport {ECO:0000256|RuleBase:RU361189};
KW   Ion transport {ECO:0000256|RuleBase:RU361189};
KW   Membrane {ECO:0000256|RuleBase:RU361189};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076842};
KW   Transmembrane {ECO:0000256|RuleBase:RU361189};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU361189};
KW   Transport {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    437    454       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    466    486       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    546    565       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    577    596       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    642    664       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    765    784       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    790    810       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   COILED      102    129       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   837 AA;  94451 MW;  D60445AF19EF3832 CRC64;
     MSGYPSLFRS AAMSYVQLYI PTEVAHDTIA ELGELGKVEF KDLNPDVNAF QRAFVTEIRR
     FDEMARRVRF FETQCETASI PTRPLVDSAP IISVGPRAAQ TFDELEVTLK EHEDRLVQMN
     ESYAMLNTRS RELHEARHVL RETAVFFEKA ESQEQHDRRQ SVDEPTQPLL ASEEAEAGQY
     HPDGNGLTFD LEFVAGTIDR ARLPTFERVL WRVLRGNLYM NYTDIDEVFV DPQTGAETRK
     NVFIIFAHGA ALLAKIRRIA ESMGGTLYPI DANPDKRSEA LREVTSRLED LNTVLYNTGA
     TRRAELAKIA ESLAVWRDVV RKEKLIYETL NLFSYEARRR GFIAEGWVPT RDITPVQLAL
     RQAMEVSGTS APAILQEMRT TKTPPTYHRT NKFTEGFQTI IDSYGIATYQ EVNPGLYAVI
     TFPFLFAVMF GDLGHGFLTF CAGLAMVVFE QSLAKSDLGE IVGTFYYGRY IILLMGAFAM
     YTGMIYNDLF SFSMHLFRPG WYWPEMNGTA QAVPLGGTYI FGVDPTWHGT DNGLVFTNSY
     KMKMSIILGV IHMTFAICLQ LPNHFHFKKP LNIYAEFIPQ ILFLQSIFGY LVICIIMKWC
     TDWTNSPTSP PGLLNMLIYM FLSPGKVNPN EQLFPGQGPL QVFLLLLALI CVPWMLCMKP
     YILWQEQKKI KAQGYQGVQL GDGVSAVRES HDEEDEEEGA GVPVAEDEEG EHEDGMGDII
     IHQVIHTIEF CLGCISNTAS YLRLWALSLA HAQLSEVLFN MTIRLAFGST GISGVIFTII
     MFSVWFSGTI GILCVMEGLS AFLHALRLHW VEANGKHYMA GGYQFQPLTF ANVEGVE
//
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