ID L0I9V8_HALRX Unreviewed; 826 AA.
AC L0I9V8;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Heavy metal translocating P-type ATPase {ECO:0000313|EMBL:AGB15026.1};
GN OrderedLocusNames=Halru_0383 {ECO:0000313|EMBL:AGB15026.1};
OS Halovivax ruber (strain DSM 18193 / JCM 13892 / XH-70).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Halovivax.
OX NCBI_TaxID=797302 {ECO:0000313|EMBL:AGB15026.1, ECO:0000313|Proteomes:UP000010846};
RN [1] {ECO:0000313|Proteomes:UP000010846}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18193 / JCM 13892 / XH-70
RC {ECO:0000313|Proteomes:UP000010846};
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Davenport K., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Sproer C.,
RA Anderson I., Woyke T.;
RT "Complete sequence of Halovivax ruber XH-70.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP003050; AGB15026.1; -; Genomic_DNA.
DR AlphaFoldDB; L0I9V8; -.
DR STRING; 797302.Halru_0383; -.
DR KEGG; hru:Halru_0383; -.
DR eggNOG; arCOG01576; Archaea.
DR eggNOG; arCOG02764; Archaea.
DR HOGENOM; CLU_001771_6_4_2; -.
DR OrthoDB; 8588at2157; -.
DR Proteomes; UP000010846; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0019829; F:ATPase-coupled monoatomic cation transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR CDD; cd00371; HMA; 1.
DR Gene3D; 3.30.70.100; -; 1.
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; 3.40.50.1000; HAD superfamily/HAD-like; 1.
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; IPR006121; HMA_dom.
DR InterPro; IPR036163; HMA_dom_sf.
DR InterPro; IPR027256; P-typ_ATPase_IB.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01525; ATPase-IB_hvy; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR PANTHER; PTHR48085; CADMIUM/ZINC-TRANSPORTING ATPASE HMA2-RELATED; 1.
DR PANTHER; PTHR48085:SF5; CADMIUM_ZINC-TRANSPORTING ATPASE HMA2; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF00403; HMA; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR SFLD; SFLDF00027; p-type_atpase; 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; SSF55008; HMA, heavy metal-associated domain; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS50846; HMA_2; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000010846};
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 122..141
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 153..172
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 184..202
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 377..398
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 404..422
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 14..80
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT REGION 89..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 280..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 806..826
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..311
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 810..826
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 826 AA; 85883 MW; 896474FABD2EFB15 CRC64;
MTSTDEQPPD SDPAVAEFSV PEMDCPSCAG KVENALGGVE GISEADLRPT TGSVSVAYDA
ENTTDAEIAG AIEGAGYAVT DSTDERAPAA EAGAGADTTG ANDAAGDESP AIWTSSRGIK
TWISGVFVAL GLLFEFFFHG ANAQVGTLVG TDLFLADVLF LVAVAVGGQE ILRGGYYSAK
LRNLDIDFLM SAAIVGALVA SLAFGEALYF EAATLAFLFS VAELLETASM DRARNSLREL
MDLSPDEATV RRDGEEVTVP VEAVDVGDVV LVKPGEKIPT DGTVVNGERS EGSEPARANG
NSVSAVNQAP ITGESVPVDK TEGDEVYAGT INESGYLEVS VTAAAGDDTL SRIVSMVEDA
QANKTDREQF VERFADYYTP VVVAFAIVIT LASPAVLGTT WPTAVVYGLT LLVLACPCAF
VISTPVSVVS GITSAAKNGV LVKGGNHLEA MGAVDVVALD KTGTLTKGEL TVTDVVPLSD
NTEADVLRCA RGLERRSEHP IGEAIVDAAD EVGVAERDVA DFESLTGKGV RAELDGTTHF
AGKPGLFEDF GFDLSHVHAA TDGGVVTQTA RDLCDRNNCL DLLEETVPEL QAEGKTVVLV
GTEDELEGVI AVADEIRPDA KRTIQRLRDL GVERTVMLTG DNARTAATIA ERVGVDDYRA
ELLPEEKVAA IEELMDGHDD GDEHRSVATG TTGGVAMVGD GINDAPALAT ATVGVAMGAA
GTDTALETAD IALMGDDIAK LPYLYELAHD ANGVIRQNIW ASLGIKAALA VGVPFGLVPI
WLAVLAGDAG MTVGVTGNAM RLSRIEPESV EPSTVDRESG RIDTVQ
//