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
//