ID A0A2T1DSB0_9CYAN Unreviewed; 656 AA.
AC A0A2T1DSB0;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Cadmium-translocating P-type ATPase {ECO:0000313|EMBL:PSB23311.1};
GN Name=cadA {ECO:0000313|EMBL:PSB23311.1};
GN ORFNames=C7B76_00160 {ECO:0000313|EMBL:PSB23311.1};
OS filamentous cyanobacterium CCP2.
OC Bacteria; Cyanobacteriota.
OX NCBI_TaxID=2107700 {ECO:0000313|EMBL:PSB23311.1, ECO:0000313|Proteomes:UP000239512};
RN [1] {ECO:0000313|EMBL:PSB23311.1, ECO:0000313|Proteomes:UP000239512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCP2 {ECO:0000313|EMBL:PSB23311.1,
RC ECO:0000313|Proteomes:UP000239512};
RA Moore K.R., Magnabosco C., Momper L., Gold D.A., Bosak T., Fournier G.P.;
RT "The ancient ancestry and fast evolution of plastids.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PSB23311.1, ECO:0000313|Proteomes:UP000239512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCP2 {ECO:0000313|EMBL:PSB23311.1,
RC ECO:0000313|Proteomes:UP000239512};
RA Keele B.F.;
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU362081}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IB subfamily. {ECO:0000256|ARBA:ARBA00006024,
CC ECO:0000256|RuleBase:RU362081}.
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:PSB23311.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; PVWD01000001; PSB23311.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T1DSB0; -.
DR OrthoDB; 438550at2; -.
DR Proteomes; UP000239512; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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:UniProtKB-KW.
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; IPR027256; P-typ_ATPase_IB.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01512; ATPase-IB2_Cd; 1.
DR NCBIfam; TIGR01525; ATPase-IB_hvy; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 1.
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; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00941; CDATPASE.
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 PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU362081};
KW Cell membrane {ECO:0000256|RuleBase:RU362081};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362081};
KW Metal-binding {ECO:0000256|RuleBase:RU362081};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362081};
KW Reference proteome {ECO:0000313|Proteomes:UP000239512};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362081};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362081}.
FT TRANSMEM 43..60
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 67..85
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 105..130
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 271..289
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 301..325
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 609..635
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 656 AA; 70290 MW; AD7AF0DD13F9A4D4 CRC64;
MSSDEERRAL QLQQADNHNH DTDQDDDDDV EGFEGPWYAF PPIRNALIAG ALLVTGWLVS
QFQVPVYVPY SIFGLAILIG AYYWAREGWE EFVEEREIGI EALMAFATLG AVILGQWFEA
AFLVFLYAGA ESIEEYTFAR TRTAIRALLD LVPETAALLT DAGEVQISAK ELEAGNLFLV
RPGERIPTDG EIIEGASSID EAAVTGESVP VEKALGDKVF AGTINTTGIL KVRATTSFAS
NSLQKIIQTV EEAQGVKSSA QRWIDRFGRR YSPAVLVVAL LLVVIPFLLK ANFALWSVRA
VVLLVAAAPC ALVISTPVAI SAAIGRSGRE GVLIKGGIHL ENLAKIRVVA FDKTGTLTRG
KPIVTNVLST TNETASLLRQ AASIEHLSEH PLAKAIVENA QAEGIAIAAV QNFQSLTGAG
AKADIDGQTI YIGSPGLFRQ LRVPLERLEP EIERLQVEGK TVVLVGTQDR IEGLFAIRDE
PRPEAKRAIQ QLHKMQVKVA MLTGDNARTA KAIAAELGID EVRADLKPDD KVKAIQELEQ
QYGPVAMTGD GINDAPALAT ATVGLAMGTA GTDAAIEAAD IALMGDDPSR VAYALKLAKA
SQRISFQNIV FSILVLVILI PGAILGLLGI TAAVFAHEAS ELLAIANGLR ITRQQV
//
