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Database: UniProt
Entry: A0A0N5AB94_9BILA
LinkDB: A0A0N5AB94_9BILA
Original site: A0A0N5AB94_9BILA 
ID   A0A0N5AB94_9BILA        Unreviewed;      1008 AA.
AC   A0A0N5AB94;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   SubName: Full=Cation_ATPase_N domain-containing protein {ECO:0000313|WBParaSite:SMUV_0000142001-mRNA-1};
OS   Syphacia muris.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Oxyuridomorpha; Oxyuroidea; Oxyuridae; Syphacia.
OX   NCBI_TaxID=451379 {ECO:0000313|Proteomes:UP000046393, ECO:0000313|WBParaSite:SMUV_0000142001-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:SMUV_0000142001-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
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}.
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DR   AlphaFoldDB; A0A0N5AB94; -.
DR   STRING; 451379.A0A0N5AB94; -.
DR   WBParaSite; SMUV_0000142001-mRNA-1; SMUV_0000142001-mRNA-1; SMUV_0000142001.
DR   Proteomes; UP000046393; Unplaced.
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; 2.
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; 3.
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; 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   NCBIfam; TIGR01494; ATPase_P-type; 1.
DR   PANTHER; PTHR43294; SODIUM/POTASSIUM-TRANSPORTING ATPASE SUBUNIT ALPHA; 1.
DR   PANTHER; PTHR43294:SF13; SODIUM/POTASSIUM-TRANSPORTING ATPASE SUBUNIT ALPHA; 1.
DR   Pfam; PF00689; Cation_ATPase_C; 1.
DR   Pfam; PF00690; Cation_ATPase_N; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   PRINTS; PR00121; NAKATPASE.
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.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00023065}.
FT   TRANSMEM        97..115
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        121..142
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        286..308
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        314..345
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        577..599
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        787..808
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        848..875
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        917..935
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        947..967
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        979..999
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          32..114
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
SQ   SEQUENCE   1008 AA;  112835 MW;  30B97B80D34E8552 CRC64;
     MTLYLKFGTI CNFCFIFIPV FFKGIELSCQ FYEHTLSIEQ LNDLFPLSRI CTANPKKSRG
     FNKDEAANKL MIDGRNVICP VSGTTTFKAF LAKSLNTFRM LLLIASFMCF VTFFIDTARL
     LELYMGVTLL VILILLCLGG YWQETKAYKQ VRGFQSIIPT SCMVIRNGTI ANANAAEIVV
     GDLIWLNPGC RLPADLRLIY TDELKLETSW LTGESESLDF FDTSVNRDVG AFESQNIAFN
     GCLCQNGEGI GIVIRTGNNS VMGKLVGMIS NEKRKASRLS VEQSSFVRFV TVLAISMGII
     TFLIGLFVNH LSYVIYSFVN GFLVVVIANV PQGLPITIGA ALIIVSRRLA KKRLYMKQLD
     SVDTLGATTA LVCDKIGVFT SNEMSVISIW HDLKFYKRYS TLEEIHLNNF LNLSLNSVND
     HLSILLVAMS LCNKAQIETV TSDDYSKWNS LSVRLYTSLL GYRKSSQQVY FIFIKAFPEE
     LIQQCTSIAT AEGKAEITHE IQESFSNACN ECGALGYSLV AFAAAELEAS KDCLDIYDED
     NLLKYDLCFL SMIAMYTPQR RNIQTSIQRL RTAGSRFLDV IVLLVSAVAL VEIVLLALIS
     NDSILKLINV FKQFQLQTTT SVSGIKCFMF TTDSPSTALA TATKMGFIKS APNTSIDQYM
     QEKLIIQGNE LENMTSDDWN FILSQKNVVF TRTCPAHKLI VIKECQQRKE IVAVTGDGVL
     DAPALKKADV GIALEAIGSA FAKEAAHMVL INGDLDNIVN AVMDGRVFYE NLKKTVAYTL
     SHLIPELYSV LLTFILGFPL GLSTFQVLTI DLITELPPSI ALIWEKAERG IMQEKPRPLS
     TNLVSRSILV YSYLFAGNII AAGCIFSYIT VFWYYGISIS DLLFTWEHHW NIQALNFTSN
     GLLFTPKMQT YIRGQAAAAW HITLVVSQVF HAWICTASRV PFFQHKFTNL ALLFATLFEI
     VLLNFFIYTP GVQQWIGVYH PPSFVWLFGV CVGFLLFVYN EVSNYFIH
//
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