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
//