ID D2V346_NAEGR Unreviewed; 1043 AA.
AC D2V346;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE RecName: Full=Sodium/potassium-transporting ATPase subunit alpha {ECO:0000256|RuleBase:RU362084};
GN ORFNames=NAEGRDRAFT_30663 {ECO:0000313|EMBL:EFC48712.1};
OS Naegleria gruberi (Amoeba).
OC Eukaryota; Discoba; Heterolobosea; Tetramitia; Eutetramitia;
OC Vahlkampfiidae; Naegleria.
OX NCBI_TaxID=5762 {ECO:0000313|Proteomes:UP000006671};
RN [1] {ECO:0000313|EMBL:EFC48712.1, ECO:0000313|Proteomes:UP000006671}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEG-M {ECO:0000313|EMBL:EFC48712.1,
RC ECO:0000313|Proteomes:UP000006671};
RX PubMed=20211133; DOI=10.1016/j.cell.2010.01.032;
RA Fritz-Laylin L.K., Prochnik S.E., Ginger M.L., Dacks J.B., Carpenter M.L.,
RA Field M.C., Kuo A., Paredez A., Chapman J., Pham J., Shu S., Neupane R.,
RA Cipriano M., Mancuso J., Tu H., Salamov A., Lindquist E., Shapiro H.,
RA Lucas S., Grigoriev I.V., Cande W.Z., Fulton C., Rokhsar D.S., Dawson S.C.;
RT "The genome of Naegleria gruberi illuminates early eukaryotic
RT versatility.";
RL Cell 140:631-642(2010).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU362084};
CC Multi-pass membrane protein {ECO:0000256|RuleBase:RU362084}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IIC subfamily. {ECO:0000256|ARBA:ARBA00006934,
CC ECO:0000256|RuleBase:RU362084}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU362084}.
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DR EMBL; GG738850; EFC48712.1; -; Genomic_DNA.
DR RefSeq; XP_002681456.1; XM_002681410.1.
DR AlphaFoldDB; D2V346; -.
DR EnsemblProtists; EFC48712; EFC48712; NAEGRDRAFT_30663.
DR GeneID; 8861557; -.
DR VEuPathDB; AmoebaDB:NAEGRDRAFT_30663; -.
DR eggNOG; KOG0203; Eukaryota.
DR InParanoid; D2V346; -.
DR OMA; FQDWSTK; -.
DR OrthoDB; 203629at2759; -.
DR Proteomes; UP000006671; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008556; F:P-type potassium transmembrane transporter 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; IPR005775; P-type_ATPase_IIC.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01106; ATPase-IIC_X-K; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR PANTHER; PTHR43294:SF22; P-TYPE ATPASE; 1.
DR PANTHER; PTHR43294; 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; 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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU362084};
KW Ion transport {ECO:0000256|RuleBase:RU362084};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362084};
KW Metal-binding {ECO:0000256|RuleBase:RU362084};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU362084}; Potassium {ECO:0000256|RuleBase:RU362084};
KW Potassium transport {ECO:0000256|RuleBase:RU362084};
KW Reference proteome {ECO:0000313|Proteomes:UP000006671};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362084};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362084}; Transport {ECO:0000256|RuleBase:RU362084}.
FT TRANSMEM 84..105
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 111..134
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 280..300
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 868..897
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 940..959
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 971..994
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 1006..1025
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT DOMAIN 23..104
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 1043 AA; 117033 MW; 05AA9A8D80CC6F1F CRC64;
MKQKSAKEVK FIKKSKKKAI DISEHELSVE RVCETYGTSF NQDKPEKSTG LTQQVASERL
KVNGPNQLTP PKKRPFIFKI IEQFTSLFAL LLIVAGLLSF LNVAIERTTE SYPNIFLGVI
LWFIVIMNAT ITLVQERSSE KVLQSFQQMQ SDSCMVIRDG IPQKIPVEEL VLGDLVRIEG
GDKIPADLRV VSCSQLKLDN ASLTGETEPQ SRSVEMTSKN PLETNNLVFF GTLALEGSGY
GIVIRCGNQT VIGQIALLAG ASTEKKTPLR REIDSFVRKI AVLAFTMAII FFCLGFAIGN
SWFTNFLFAI GIIISNIPQG LIPTVTVCLT VSAKRLKAVN VLVKKLEHVE TLGSTSVICS
DKTGTLTQNR MTVVELWVDG RVSSVDYQDR YMTQKPSTLT PLTSYSKEGE EQLTTDQMLR
RCSALCSKTY FVPEEDNLRK PILDRECEGD ASETALVKFI QTRTDCATIE EFRSDYTELY
SIPFNSKNKW MLSIRKNNHL PQWTTNTTDS ASTDSKVLLL MKGAPERIIQ RCSHIRVGSQ
TLPLDDNWKQ NFKDAYDFFA SKGERVLGFA QLFIDEHLVE EQLRIEKSGQ TSDQIAQSIP
MEGLCFLGMA GLTDPPKVGV PECIGQCKKA GIQVVMVTGD HPATAKAIAK QVGIIESDAR
TIDDIAEEES CDPKTIPYSR ADAIVLHGEE IDKLTSKEWK QILKKKQIVF ARTSPQQKLI
IVTKFQELGH CVAVTGDGTN DSPALKKADV GVAMNISGSA VSKEAAAIIL LDDNFASIVN
GIKEGRLIFD NLKKSIAYTV SHLSAEIFPY LVFIVFSMPL PITGLLILCV DLGTELISAV
SLAYETAESD IMSIPPRTKN QPLVSSSLLI FSYLQMGVIE TLACFTNYFL VFAYYGIPPK
YLWEATSKDY FDINSDKKLY IEETGMYLDK MYQHNVLCTA QTAFFMTIVI CQWATLFSCK
TRRLSIFTHG LLGNLMTYFG LIYSACLLVI LIYVPFIGDY IFNTRFMIID FWLYPIPWMF
LMIFYDEMRK WVIRKLNFSF LFW
//
