ID L0IFC7_HALRX Unreviewed; 884 AA.
AC L0IFC7;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=Heavy metal translocating P-type ATPase {ECO:0000313|EMBL:AGB17464.1};
GN OrderedLocusNames=Halru_2894 {ECO:0000313|EMBL:AGB17464.1};
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:AGB17464.1, 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; AGB17464.1; -; Genomic_DNA.
DR AlphaFoldDB; L0IFC7; -.
DR STRING; 797302.Halru_2894; -.
DR KEGG; hru:Halru_2894; -.
DR eggNOG; arCOG01576; Archaea.
DR eggNOG; arCOG02764; Archaea.
DR HOGENOM; CLU_001771_0_3_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; PTHR43520; ATP7, ISOFORM B; 1.
DR PANTHER; PTHR43520:SF8; COPPER-TRANSPORTING ATPASE 2; 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 SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 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 172..191
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 211..230
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 251..269
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 275..293
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 427..445
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 457..480
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 839..865
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 87..153
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT REGION 56..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 564..658
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..73
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 618..632
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 644..658
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 884 AA; 91629 MW; F586D636C782A063 CRC64;
MSDCSLCELP TPDPPVSDPD VDGTFCCRGC LEVSRTLVDT DDLDRGDVRV RVEAARENSV
GDTAREDAAD ETASPAARTD AVPTGFETAF LAVDGMHCAT CEGFVSLLGE REPAVHTVEA
SYATDTARVV YDPDRLDHDE LPAVLSGYGY ETRLRDGTAR DARADEALVQ RLLVGGFLSM
LVMPWYVFYL YPSYVGIETG VLTTGAGSAA GSSVPLALLG VFSGGVLCYT GYPVLRGAYV
SLRVGRPNMD LLIAIAAGSA YVYSTIALVF GRTHLYYDVT VAVIMVVSLG GYYEGRIKRR
ATGLLADVTS AGVRAATRRT ADGETETVSV DRLEPGEAVV VRPGERVPVD GTVREGTAAV
DESVVTGESM PTTKRPGDAV VGGAIVTDSA LVCEVGSDAE STLDRIASLM WEIQSETPGI
QRFADRLAAV FVPLVLATAV AVTGWRVASG VSADTAVLTG LTVLVVSCPC AMGLATPLAV
ASGLRDALER GIVVANATLF ESAPAVETVV FDKTGTVTTG EMTVRTVVGE EAAIDRAAAV
ERYSTHPVAD AIVARAAAGA DFDEPAGSAN AVAPDGGTER DGEAVSDGEP VTAAGSTVLS
EESGHDAENG GHATETTALD ARDFERRPGE GVSAVVHEPA DANETGTDGV DERPTDGDRV
VVGTPELIER LVGPIPADLG DAIEDARERG RLPVVIGYAG RARAVAVVGD RPRRSWRAVL
ESVADREVVV LTGDDESATT ELREQQAVDR VFAGVPPEGK VATVRRLSAE GVTAMVGDGT
NDAPALAAAD VGIALGSGTA RATDAADAIL ADGELATVPD VFALAEGTRR RIRENVRWAL
LYNAVAIPLA AAGLINPLFA ALAMAGSSAI VVLNSSRPVL ADGS
//
