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Database: UniProt
Entry: A0A1H3E8D1_9EURY
LinkDB: A0A1H3E8D1_9EURY
Original site: A0A1H3E8D1_9EURY 
ID   A0A1H3E8D1_9EURY        Unreviewed;       934 AA.
AC   A0A1H3E8D1;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Cu2+-exporting ATPase {ECO:0000313|EMBL:SDX75003.1};
GN   ORFNames=SAMN05216564_101329 {ECO:0000313|EMBL:SDX75003.1};
OS   Halopenitus persicus.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Halorubraceae; Halopenitus.
OX   NCBI_TaxID=1048396 {ECO:0000313|EMBL:SDX75003.1, ECO:0000313|Proteomes:UP000199079};
RN   [1] {ECO:0000313|EMBL:SDX75003.1, ECO:0000313|Proteomes:UP000199079}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DC30,IBRC 10041,KCTC 4046 {ECO:0000313|Proteomes:UP000199079};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FNPC01000001; SDX75003.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H3E8D1; -.
DR   OrthoDB; 8588at2157; -.
DR   Proteomes; UP000199079; Unassembled WGS sequence.
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: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; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 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; 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; IPR001757; P_typ_ATPase.
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   SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 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; PS01229; COF_2; 1.
DR   PROSITE; PS50846; HMA_2; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        194..215
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        235..261
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        273..291
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        297..315
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        470..492
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        498..524
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          84..150
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
FT   REGION          156..189
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          603..647
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          891..934
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        156..178
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        906..927
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   934 AA;  94939 MW;  C5988491F1F1B123 CRC64;
     MSDCRLCGLP TPDQPVTASD VDGAFCCRGC LEVARRLDDL DDVGGTAGGV GGTADGVGSG
     AAALEAASDG VVSDSDANAA PDAPEAYLAV EGMHCTTCEA FLRLRGDDVA GVHAVQANYG
     TETARVVYDP DEIDREALPE ALSGYGYALR FMEGERTTDG TGKRSNGDDA KPARREGDPG
     STSGRSTDPT LERLAIGGFL AMLVMPWYVL SLYPSYLGIE TNVLAIDTTT PVGRYLPLVF
     IALVTTILVA TTGAPLLRGA YVSLRARRPN MDLLVTVAAL SAYAYSTLAL ATGSTHLYYD
     VTVAVVMVVS LGRYYEGRVR SRATDLLETV TAARVESATR ITDAGRETVP IGALEPGDRI
     RVAPGERVPV DGTVIEGVAD VDQSVITGES LPVRAEPGEE VVGGARVLGD VGHGGRDAGC
     ESGDGNDDGA AGGAIAVRVG EDAESTADRL AAALWEVQTT TPGIQRFVDA LATVFVPVVL
     TLGLAVAAWQ LVAGETVAAA MLAGLTVLVV SCPCAMGLAT PLAVSGGLRD AIARGVVVTD
     GSVFESAREA ETVVFDKTGT LTAGEMRVGA VHGDDRTLAR AAAVERRADH PVADAIHEAA
     AARADGGGKS GGVVETTETG GAAASAASGT DGPTVESFTH HPGMGVSGTL VDAARDDRVI
     PSETAGTDAG GERVVVGTPD LVERECGPLP AALAERVDAA TDDGALPIAV GWGGAARGVI
     VVTDRDRAGW TAALEAFADR EVVVLTGDDG PRADRFRGHP AVDEVFAGVP PDGKLEAVRG
     FVADGTTVMV GDGTNDAPAL AAADLGIALG DGTARAVEAA DVVITGDDLR TVETVFELAA
     GTRRRIRENV AWALCYNAVA IPLAVSGALN PFFAALAMAA SSAIVVTNST RPVLDDDPAS
     EASEASEAPD SASGTSDSAS GTSDPASEAS GPAF
//
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