GenomeNet

Database: UniProt
Entry: A0A165EXQ0_EXIGL
LinkDB: A0A165EXQ0_EXIGL
Original site: A0A165EXQ0_EXIGL 
ID   A0A165EXQ0_EXIGL        Unreviewed;      1149 AA.
AC   A0A165EXQ0;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=Na(+)/K(+)-exchanging ATPase {ECO:0000256|ARBA:ARBA00039096};
DE            EC=7.2.2.13 {ECO:0000256|ARBA:ARBA00039096};
GN   ORFNames=EXIGLDRAFT_773148 {ECO:0000313|EMBL:KZV87931.1};
OS   Exidia glandulosa HHB12029.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Auriculariales; Exidiaceae; Exidia.
OX   NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZV87931.1, ECO:0000313|Proteomes:UP000077266};
RN   [1] {ECO:0000313|EMBL:KZV87931.1, ECO:0000313|Proteomes:UP000077266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB12029 {ECO:0000313|EMBL:KZV87931.1,
RC   ECO:0000313|Proteomes:UP000077266};
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., Labutti K.,
RA   Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA   Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT   "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT   Insights into the Origins of Lignocellulose Decay Capabilities.";
RL   Mol. Biol. Evol. 33:959-970(2016).
CC   -!- FUNCTION: This is the catalytic component of the active enzyme, which
CC       catalyzes the hydrolysis of ATP coupled with the exchange of sodium and
CC       potassium ions across the plasma membrane. This action creates the
CC       electrochemical gradient of sodium and potassium ions, providing the
CC       energy for active transport of various nutrients.
CC       {ECO:0000256|ARBA:ARBA00037422}.
CC   -!- SUBUNIT: The sodium/potassium-transporting ATPase is composed of a
CC       catalytic alpha subunit, an auxiliary non-catalytic beta subunit and an
CC       additional regulatory subunit. {ECO:0000256|ARBA:ARBA00038795}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KV426111; KZV87931.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A165EXQ0; -.
DR   STRING; 1314781.A0A165EXQ0; -.
DR   InParanoid; A0A165EXQ0; -.
DR   OrthoDB; 203629at2759; -.
DR   Proteomes; UP000077266; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 1.
DR   Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR   Gene3D; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 2.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR   InterPro; IPR006068; ATPase_P-typ_cation-transptr_C.
DR   InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
DR   InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR   InterPro; IPR018303; ATPase_P-typ_P_site.
DR   InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR   InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR001757; P_typ_ATPase.
DR   InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR   NCBIfam; TIGR01494; ATPase_P-type; 2.
DR   PANTHER; PTHR43294; SODIUM/POTASSIUM-TRANSPORTING ATPASE SUBUNIT ALPHA; 1.
DR   PANTHER; PTHR43294:SF13; SODIUM/POTASSIUM-TRANSPORTING ATPASE SUBUNIT ALPHA; 1.
DR   Pfam; PF13246; Cation_ATPase; 1.
DR   Pfam; PF00689; Cation_ATPase_C; 1.
DR   Pfam; PF00690; Cation_ATPase_N; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   PRINTS; PR00121; NAKATPASE.
DR   SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
DR   SFLD; SFLDF00027; p-type_atpase; 1.
DR   SMART; SM00831; Cation_ATPase_N; 1.
DR   SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR   SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 2.
DR   SUPFAM; SSF56784; HAD-like; 1.
DR   SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077266};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        147..167
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        179..197
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        341..365
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        371..396
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        849..871
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        959..981
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1029..1049
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1061..1079
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1099..1119
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          87..168
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
FT   REGION          1..62
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        47..62
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1149 AA;  126490 MW;  4D3851411C6DC21E CRC64;
     MASSPPADPP VPSPGDPHRA INFGVDHGIY LDDKTSPGLQ QGSSTRPKGH EMRRELTKED
     RELAEAGYSH LDAPGAKVES KDKSDITEHM LDLDALSSVL DTAFDAKSPN QSHGLTSAQA
     KERLERYGRN VLTPPKKKSA IMKYLECLRS LFNVLLILAG ILEYILLGIS FETSKQNEYL
     GAILIAVALL NAFIEWYQVQ KSEAILASFL AMIPPSCHVM RDGTLTSIPA ADLVSGDVVL
     IRMGNKTPAD LVLVSATDLK VDNSSLTGES EPQERRPLPN GARVRVVEAE NLVFNSTLVV
     SGEAYGVVVR TGDHTLIGQI AALTGGETGN KSPLGTEISQ FVVMISIIAI IVAIIFFAVG
     ITSVYKGNAA LTVTFAVSIL VAFVPEGLPS TVTLLLSIAA KRMAAQNVLV KDLQGVETLG
     ALTLLATDKT GTLTRNQMTV TNLWSGGRMY SAFQSNNDED ETQPFTLESP GMREMVHIAA
     LNSRIKFDKT DVPFERREIL GDATETGLTR FAGKYIEDYD KLHVQHAQVF TIPFNSTNKW
     ALVIVKKEHA DGALTSYIKG APERVLAKCS TYLVDGKPVP ITDDFKKDYD NAYSYMASRG
     HRVIACAQLL LEGEVREFSK NVEDKNGYPS EGYTFVGLVS LEDPPKHGVR EAIGTLRLAG
     IQVMMVTGDH PKTAEAIARK INLVLGDTKE SLSAKTGRPV EEIYEDEISA VVVHGDEIDG
     LHGWQWDQIF SKSEIVFART SPKHKLEIVK RAQALGHIVG VTGDGVNDSP ALKKADLGIA
     MNISGSDVSK EAANMVLLDD NFASTVKGVQ EGRLIFTNLK RSIQYTITHS TAEVIPQLLF
     VVVPIPLPIS AILILVIDLG FELFLALSFA WDVPEAKDAL MRLQPRKPVT DRSIHSLKKR
     ALQRTKTLRH DSEGRPIMPS IFRRAWSKLS IPFTRHYWEE AFEKTDEETL VDGRLLSYAY
     LEAGVIEFLA SIVSYFVVFL AKGFSPTDLR KAQHANVYFM KNSPDFVNYK GRAINGPDQV
     DALAQAQSIF YLSIFIVQCF NVFAVKARLK FPFGKRVVSN PYNFLGILFG ACLGVFIIYT
     PPLHVVFGGS FHLLPLYWLI PFAFGILLLA WASLRVVVLR RSVEDARVKE ISGLMMFPTK
     RTMSMRSRR
//
DBGET integrated database retrieval system