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ENA P-type ATPase 2 (Putative Na( )/Li( )-exporting P-type ATPase isoform 1B)

 Q209Q6_HORWE            Unreviewed;      1070 AA.
Q209Q6;
18-APR-2006, integrated into UniProtKB/TrEMBL.
18-APR-2006, sequence version 1.
22-NOV-2017, entry version 79.
SubName: Full=ENA P-type ATPase 2 {ECO:0000313|EMBL:ABD64571.1};
SubName: Full=Putative Na(+)/Li(+)-exporting P-type ATPase isoform 1B {ECO:0000313|EMBL:AGT96030.1};
Name=ENA2 {ECO:0000313|EMBL:ABD64571.1};
Synonyms=ENA1B {ECO:0000313|EMBL:AGT96030.1};
Hortaea werneckii.
Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
Dothideomycetes; Dothideomycetidae; Dothideales; Hortaea.
NCBI_TaxID=91943 {ECO:0000313|EMBL:ABD64571.1};
[1] {ECO:0000313|EMBL:ABD64571.1}
NUCLEOTIDE SEQUENCE.
STRAIN=MZKI B-736 {ECO:0000313|EMBL:ABD64571.1};
PubMed=17034413; DOI=10.1111/j.1574-6968.2006.00473.x;
Gorjan A., Plemenitas A.;
"Identification and characterization of ENA ATPases HwENA1 and HwENA2
from the halophilic black yeast Hortaea werneckii.";
FEMS Microbiol. Lett. 265:41-50(2006).
[2] {ECO:0000313|EMBL:AGT96030.1}
NUCLEOTIDE SEQUENCE.
STRAIN=EXF-2000 {ECO:0000313|EMBL:AGT96030.1};
Lenassi M., Gostincar C., Plemenitas A., Gunde-Cimerman N.;
"Whole genome duplication and enrichment of metal cation transporters
revealed by de novo genome sequencing of extremely halotolerant black
yeast Hortaea werneckii.";
Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
-!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC
3.A.3) family. {ECO:0000256|SAAS:SAAS00832166}.
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EMBL; DQ401071; ABD64571.1; -; Genomic_DNA.
EMBL; KC961353; AGT96030.1; -; Genomic_DNA.
ProteinModelPortal; Q209Q6; -.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0019829; F:cation-transporting ATPase activity; IEA:InterPro.
Gene3D; 3.40.1110.10; -; 1.
Gene3D; 3.40.50.1000; -; 1.
InterPro; IPR006068; ATPase_P-typ_cation-transptr_C.
InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
InterPro; IPR018303; ATPase_P-typ_P_site.
InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
InterPro; IPR036412; HAD-like_sf.
InterPro; IPR023214; HAD_sf.
InterPro; IPR006414; P-type_ATPase_IID.
InterPro; IPR001757; P_typ_ATPase.
Pfam; PF00689; Cation_ATPase_C; 1.
Pfam; PF00690; Cation_ATPase_N; 1.
PRINTS; PR00120; HATPASE.
SMART; SM00831; Cation_ATPase_N; 1.
SUPFAM; SSF56784; SSF56784; 2.
SUPFAM; SSF81653; SSF81653; 1.
SUPFAM; SSF81660; SSF81660; 1.
SUPFAM; SSF81665; SSF81665; 3.
TIGRFAMs; TIGR01523; ATPase-IID_K-Na; 1.
TIGRFAMs; TIGR01494; ATPase_P-type; 2.
PROSITE; PS00154; ATPASE_E1_E2; 1.
3: Inferred from homology;
ATP-binding {ECO:0000256|SAAS:SAAS00832164};
Hydrolase {ECO:0000256|SAAS:SAAS00831205};
Membrane {ECO:0000256|SAAS:SAAS00832181, ECO:0000256|SAM:Phobius};
Nucleotide-binding {ECO:0000256|SAAS:SAAS00832164};
Transmembrane {ECO:0000256|SAAS:SAAS00832181,
ECO:0000256|SAM:Phobius};
Transmembrane helix {ECO:0000256|SAAS:SAAS00832181,
ECO:0000256|SAM:Phobius}.
TRANSMEM 132 151 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 157 175 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 344 366 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 372 398 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 810 831 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 847 864 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 893 911 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 942 964 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 985 1006 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 1018 1037 Helical. {ECO:0000256|SAM:Phobius}.
DOMAIN 78 152 Cation_ATPase_N.
{ECO:0000259|SMART:SM00831}.
SEQUENCE 1070 AA; 115994 MW; 0D95A356B568BE39 CRC64;
MEEAPVHAVQ KNGFASHTSR PSGSIATCED DGSSDDPPPI PCAGSSSYLT SQSVGETRLN
NPNKNHHLHH DPAEVHTLAH TLASGQVAEQ LETNVERGLT TQEATERLRQ YGHNKLETSG
GVSWWRILIR QVSNSLTFVL AIAMILSFVT LDFIEGGVIA AVICLNIVVG FVQDFRAEQT
IQSLLAMAAP VCRVIRDNGT SISINADELV PGDVVVLAVG DIVPTDVRLT STINFATDEA
LLTGESKPCT KDAEASLDDM DSPIGDRINM AYSSTNVTRG RAVGIAVSTG MKTEIGKIAE
LLKDKDATTE KEGFWLLRAG RKILFNVKSA LGLIGTPLQV KLSWFALLLF ALAILLAIIV
FSANAWDVDD ETLIYGICTA VAVIPESLIA VLTIVIAVGS KAMAKSNVIV RKMGALEAIG
GVTNICSDKT GTLTQGKMLA RKAFLPNGEH MVVQNETGPF DPTSGEIASQ GVTLTEQSAT
QNQQMRDFFH TISLCNLATV TLPSAQGDDA PSAWKATGEP TEIALQVMAM RIAYGKQQVL
DREGLSLITE HSFDSSIKRM SVIYQSHDEK HLEVFTKGAT EVLLPLTDVP VSARQTILEQ
ADSMASQGLR VLCLARRKLL ITARDSVDDR ASIEQQLTFA GLVGLYDPPR LESADAIRQC
QAAGITVHML TGDHLKTATT IAQEIGILGP HVYGSMTSSS VMVAQDFDKF TDEAIDDMKT
LPLVLARCSP STKLRMLHAL HRRGKYCVMT GDGTNDSPAL KGADVGVAMG MNGSDVSKEA
ADMVLTDDNF ASIVSAIREG RRLFDNIQKF LLHLLTSNIS QIILLLVGLA FQDRRGISVF
PLSPIEILWA NLITSSFLAI GLGLEEASAD VMLRPPHSLS TGVFTKELIV DKFIYGGITG
ILSLVCYVIV IEGVGNGDLG EDCNESYNET CDLAFKARGT AYAIMTVQIT LMALEAKHLT
LGLFNMHTEG NVFTGFFRTL YKNKFLFWSS VVGIITPFPA VFIPVVNKTV FRHLPLTWEW
ALVFGSSILF VVLVEAWKAA KRVKRSRAER RRQVVNTEKQ VERSEESSIV


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