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Database: UniProt
Entry: I0Z7R9_COCSC
LinkDB: I0Z7R9_COCSC
Original site: I0Z7R9_COCSC 
ID   I0Z7R9_COCSC            Unreviewed;       942 AA.
AC   I0Z7R9;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   SubName: Full=Heavy metal P-type ATPase {ECO:0000313|EMBL:EIE26688.1};
GN   ORFNames=COCSUDRAFT_59206 {ECO:0000313|EMBL:EIE26688.1};
OS   Coccomyxa subellipsoidea (strain C-169) (Green microalga).
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC   Trebouxiophyceae incertae sedis; Elliptochloris clade; Coccomyxa;
OC   Coccomyxa subellipsoidea.
OX   NCBI_TaxID=574566 {ECO:0000313|EMBL:EIE26688.1, ECO:0000313|Proteomes:UP000007264};
RN   [1] {ECO:0000313|EMBL:EIE26688.1, ECO:0000313|Proteomes:UP000007264}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C-169 {ECO:0000313|EMBL:EIE26688.1,
RC   ECO:0000313|Proteomes:UP000007264};
RX   PubMed=22630137; DOI=10.1186/gb-2012-13-5-r39;
RA   Blanc G., Agarkova I., Grimwood J., Kuo A., Brueggeman A., Dunigan D.,
RA   Gurnon J., Ladunga I., Lindquist E., Lucas S., Pangilinan J., Proschold T.,
RA   Salamov A., Schmutz J., Weeks D., Yamada T., Claverie J.M., Grigoriev I.,
RA   Van Etten J., Lomsadze A., Borodovsky M.;
RT   "The genome of the polar eukaryotic microalga coccomyxa subellipsoidea
RT   reveals traits of cold adaptation.";
RL   Genome Biol. 13:R39-R39(2012).
CC   -!- SUBCELLULAR LOCATION: 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:EIE26688.1}.
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DR   EMBL; AGSI01000002; EIE26688.1; -; Genomic_DNA.
DR   RefSeq; XP_005651232.1; XM_005651175.1.
DR   AlphaFoldDB; I0Z7R9; -.
DR   STRING; 574566.I0Z7R9; -.
DR   GeneID; 17044698; -.
DR   KEGG; csl:COCSUDRAFT_59206; -.
DR   eggNOG; KOG0207; Eukaryota.
DR   OrthoDB; 7279at2759; -.
DR   Proteomes; UP000007264; Unassembled WGS sequence.
DR   GO; GO:0016020; C: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:0005507; F:copper ion binding; IEA:InterPro.
DR   CDD; cd00371; HMA; 3.
DR   CDD; cd02094; P-type_ATPase_Cu-like; 1.
DR   Gene3D; 3.30.70.100; -; 3.
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; IPR017969; Heavy-metal-associated_CS.
DR   InterPro; IPR006122; HMA_Cu_ion-bd.
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   NCBIfam; TIGR00003; copper ion binding protein; 1.
DR   PANTHER; PTHR46594; P-TYPE CATION-TRANSPORTING ATPASE; 1.
DR   PANTHER; PTHR46594:SF4; P-TYPE CATION-TRANSPORTING ATPASE; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   Pfam; PF00403; HMA; 2.
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; 3.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
DR   PROSITE; PS01047; HMA_1; 1.
DR   PROSITE; PS50846; HMA_2; 2.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU362081};
KW   Copper {ECO:0000256|ARBA:ARBA00023008};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362081};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU362081};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU362081};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007264};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
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        220..239
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        290..309
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        483..509
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        529..549
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        883..900
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        906..925
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   DOMAIN          1..58
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
FT   DOMAIN          132..198
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
SQ   SEQUENCE   942 AA;  100467 MW;  DA019DC4E0CABEB3 CRC64;
     MHCSSCSSAV ERALSSQPGV LSASVALLKE TAEVVFDDGD ITISEILKVI QDAGFMAELL
     QKQEERTRHE VAVETALGEK KGVQKALVSL TLKMAEVTHD PQVVNEAEVV ALIEEAGFEA
     RVVGRGAVPD SDSAILRVSG MTCSSCSSAV ELALLNHQGV QRAAVNLLAG KAEVQYNPDV
     TGPRHIIQAV QEAGFEAHLL RGDRPANGDQ KSELQQLRDL FFASACLTIP VFLVAMVFPM
     IPAMRPLLEA QIFDFPLDQI IKCLCATPVQ FVIGWRFHIN AWRALRNGRA NMDVLVSLGT
     NASYLYSMIS ILHHHFMNHH KTGMYRPTDF FETSAMLITF ILLGKYLEAS AKGKTSEAIG
     ALLNLTPPTA VLLEGGEDGK VEAEREVPTA LIHRGDRLKV LPGARMPVDG LVLSGKSHAD
     ESMLTGEAEP VLKVEGDAVI GGTMNMGGAL QVRATRVGKD TALAQIVQLV EAAQMSKAPI
     QAFADYVSSI FVPIVVTVAM ITCFCWYVAG KHGWFPQEWL PAGHNHFLFA LLFGIAVLVI
     ACPCALGLAT PTAVMVGTGV AASHGILIKG ADALERAHRI RTIVFDKTGT LTRGKPVVTD
     VRLYDTQASL KEVMHLAAAL EVQSEHPLAS AVINFAAEGL GIGQQQVGGG AKVTAGTKGA
     PAARRLDWVR PAKDVLSVAG KGVLGWVAVG PEISRSPIKG KEGPRDVKVI LGNKQMMADE
     GIPISKAVDD YMRDMEAKCC TCVMVALAGS IVAVLAVTDP LKPEARGVVA ALARRGLAVH
     LVTGDNWRTA RAIAEQLAII NVCAECLPGA KVDKIRGSKK VVAMVGDGVN DSPALAAADV
     GIAVGSGTDI AIEAADYVLM RDDLEDVLVA IDLSRKTFNR IRVNYFWAMG YNVVMIPFAA
     GIPPWVAGAL MVFSSVSVVC SSLLLRNYKR PKPVLRDVAV LS
//
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