ID A0A0P9DSS2_9ARCH Unreviewed; 921 AA.
AC A0A0P9DSS2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Putative copper-exporting P-type ATPase A {ECO:0000313|EMBL:KPV63178.1};
GN Name=copA {ECO:0000313|EMBL:KPV63178.1};
GN ORFNames=AOA66_0990 {ECO:0000313|EMBL:KPV63178.1};
OS Candidatus Bathyarchaeota archaeon BA2.
OC Archaea; Candidatus Bathyarchaeota.
OX NCBI_TaxID=1700836 {ECO:0000313|EMBL:KPV63178.1, ECO:0000313|Proteomes:UP000050284};
RN [1] {ECO:0000313|EMBL:KPV63178.1, ECO:0000313|Proteomes:UP000050284}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BA2 {ECO:0000313|EMBL:KPV63178.1};
RX PubMed=26494757; DOI=10.1126/science.aac7745;
RA Evans P.N., Parks D.H., Chadwick G.L., Robbins S.J., Orphan V.J.,
RA Golding S.D., Tyson G.W.;
RT "Methane metabolism in the archaeal phylum Bathyarchaeota revealed by
RT genome-centric metagenomics.";
RL Science 350:434-438(2015).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KPV63178.1}.
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DR EMBL; LIHK01000025; KPV63178.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P9DSS2; -.
DR STRING; 1700836.AOA66_0990; -.
DR KEGG; barb:AOA66_0990; -.
DR PATRIC; fig|1700836.3.peg.1539; -.
DR Proteomes; UP000050284; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis 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; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01494; ATPase_P-type; 3.
DR PANTHER; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR42861:SF156; CALCIUM-TRANSPORTING ATPASE; 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 PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00120; HATPASE.
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 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
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 47..67
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 79..98
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 246..267
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 279..305
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 714..734
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 777..801
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 859..881
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 893..912
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 2..64
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 921 AA; 101697 MW; BA79A97D50832FB3 CRC64;
METLKASEKG LSEEEAKRRL AEYGYNELKE RKRRTALHMF LEEFKDIFIL LLIAATVFSV
IIGYYELMHK PERGFLETYA DAITIGIIVL LVAVAGFIQE YRAEKAIEAL KKLAAPKARV
LRDGKETMIF AREVVPGDLL LVESGDTVTA DARIIESVEL KTDEAILTGE STPVEKNLAT
LKPETPAADR KNMLLMATHT IYGRGKAVVV STGMNTEFGK IAELVQTAEE EETPLKRKLD
SFAKKIAKVV VAVCVIIFAL EAFKVATRGF LELERFIQAF MSSIALAISA VPEGLPAVVT
ITLALGAREF AKRNAIIRRL SSAESLGATT VICSDKTGTL TKGEMTVRRI HVNHKVVEVT
GVGYEPKGEF HQNNSLIDPQ NDQDLLLLLR IGALCNNAQL NKNEKGSWAI IGDPTEGALI
VTAVKAGFEK EELEKSYPRI GEVPFTSERK RMTTVHSTPE GEHVAYMKGA PEIVLERCSF
ILEKGEEKKL TKVKRKKILE INEKFASEAL RVLAMAYRKL PETLSEFDEK TVEDGLIFVG
LQGMIDPPRE EAIKANQTCQ KAGIKTIMIT GDHKLTAMAV AKEIGILKEG SLVLTGTEFD
KMSDEEFGKI VENVAVYARV SPEHKLRIVK ALKAKGEIVA MTGDGVNDAP AVKSADIGVA
MGISGTDVTR EASDLVLTDD NFATIVKAVE QGRVSYDNIR KYARFLISCN FDELLVIGTF
AILGGIFGSQ LFPLPLLPSM ILWINLVTDG APAVSLATDP PDEDVMTRQP RKPHEGILHG
MGAFIIVSFL LQAIGTILVF SLEYYVWPAH GFGTQETLAK ARTTAFVQAA FFELFVVWNC
RSETRSVWRM GRDSFKNKFF VVAEIISITA TLGICCIPTT AKMFGLVPLT LTDLIYVLAV
ASWGLFVLPE LFMRRKIWRW E
//
