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Database: UniProt
Entry: A0A369H8T6_9HYPO
LinkDB: A0A369H8T6_9HYPO
Original site: A0A369H8T6_9HYPO 
ID   A0A369H8T6_9HYPO        Unreviewed;      1092 AA.
AC   A0A369H8T6;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=Na(+)/K(+)-exchanging ATPase {ECO:0000256|ARBA:ARBA00039096};
DE            EC=7.2.2.13 {ECO:0000256|ARBA:ARBA00039096};
GN   ORFNames=CP533_6681 {ECO:0000313|EMBL:RDA91115.1};
OS   Ophiocordyceps camponoti-saundersi (nom. inval.).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX   NCBI_TaxID=2039874 {ECO:0000313|EMBL:RDA91115.1, ECO:0000313|Proteomes:UP000253071};
RN   [1] {ECO:0000313|EMBL:RDA91115.1, ECO:0000313|Proteomes:UP000253071}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BCC 79314 {ECO:0000313|EMBL:RDA91115.1,
RC   ECO:0000313|Proteomes:UP000253071};
RA   Kobmoo N., Wichadakul D., Arnamnart N., Rodriguez De La Vega R.C.,
RA   Luangsa-Ard J.-J., Giraud T.;
RT   "A genome scan of diversifying selection in the zombie-ant fungus
RT   Ophiocordyceps unilateralis complex supports a role of enterotoxins in
RT   coevolution and host-specificity.";
RL   Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
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   -!- 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:RDA91115.1}.
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DR   EMBL; PDHQ01000086; RDA91115.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A369H8T6; -.
DR   STRING; 2039874.A0A369H8T6; -.
DR   Proteomes; UP000253071; 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; 1.
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; SFLDS00003; Haloacid_Dehalogenase; 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; 1.
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:UP000253071};
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        162..185
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        197..216
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        359..381
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        393..417
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        847..869
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        875..896
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        922..947
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        985..1002
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1023..1045
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1057..1074
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          113..186
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
FT   REGION          1..68
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        6..39
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1092 AA;  119206 MW;  CC038A6DBE52E00E CRC64;
     MDDDKSDFEK ERGRAIAFDD ATARGRRARD VDGGAGGRSR SRSRFRSGSR GSSRSRAGLP
     PPSPYSGVQI EYRSLSMHVA ESTRVNNDNV DVDKNVDKNV DKDDHDAYFA RLTYHKLSPD
     ALCQQLNVSR TAGLSEEAAA RRLARDGRNA LPRAKSNYLL QLAGYLFGGF CSVLWLGVVI
     FFLCWKPLSD PPSGTNLALA ILVLIVILLQ AGFAAFQDWS TRRTMRAIVD LLPAEALVLR
     DGKPEKRPAA QLVAGDVVLL RMGDKVPADL RLLSHSGDLR FDRSVLTGEP DEIEASVDAT
     DSNILESRNM ALMGTLVVNG SGEAVVVLTG ARSVMGRIAK ATAAAGQGST LIQREVWRFV
     RIIVGLTVVL ALVILLAWLL WLRRDHPGFM GVVAMLNNVM GCVVAFIPEG MPVAVALTLM
     RVARRMKAVD VLPKGLSTVE TLGCVNVVCS DKTGTLTQNQ MVVRSVSCVE QAVSSDDGEE
     DEKQAEDEKD VPCVARLRRA ALLCNDAVFD PASLHLPIAS RPVQGNATDA AVLRFAGGTE
     TEKLPRLFQI PFNSSNKWML TLHDDGAGSS GEYRVFVKGA PDVLLPTCVS YWSRRTGVVE
     PLTLDDRAAI GRYQDKLAGR AERVIVLCEK AVRPAHALGS NDFAAEVTES AVSDLVLIGI
     LGIVDPPRPE TADTVAACRR AGARFFMVTG DYGLTAAAIA RLTGIFTSDR GLPDSAETVR
     AAVDAGEQNS TGDRSSLLLE GPTLSSLSTP AHWDIVCAYN EVVFARTSPE QKLRIVEELR
     RRGNVVAVTG DGVNDAPALR AADVGVAVVS GSDVAIEAAH LVLLDRFDSI VDAIRLGRLV
     FQNLQKVIAY LLPAGSCSEI WPVLLNVFFG VPLPLSAFLM IIICVFTDLF MSLSLIMEQE
     EFDLLSLPPR NHMRDHLINA KIYAQAYLFV GIMETCTAHA MFFLYYWREA RIPIRELFFL
     FERYTDGFHG YSAAELAKFN ATGQSVYFVT LVILQWGNIL AVRNRRLSIV QADPFTSKRR
     NPWLVLSILV SLIIAVFVTE VPGIQTLFNT ASVPIEYWLI PLPLALGLLC MDELRKLLVR
     LFPKGPLAAV AW
//
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