ID C5KY20_PERM5 Unreviewed; 965 AA.
AC C5KY20;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE SubName: Full=Copper-transporting ATPase P-type, putative {ECO:0000313|EMBL:EER10627.1};
GN ORFNames=Pmar_PMAR019004 {ECO:0000313|EMBL:EER10627.1};
OS Perkinsus marinus (strain ATCC 50983 / TXsc).
OC Eukaryota; Sar; Alveolata; Perkinsozoa; Perkinsea; Perkinsida; Perkinsidae;
OC Perkinsus.
OX NCBI_TaxID=423536 {ECO:0000313|Proteomes:UP000007800};
RN [1] {ECO:0000313|EMBL:EER10627.1, ECO:0000313|Proteomes:UP000007800}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50983 / TXsc {ECO:0000313|Proteomes:UP000007800};
RA El-Sayed N., Caler E., Inman J., Amedeo P., Hass B., Wortman J.;
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
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|RuleBase:RU362081}.
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DR EMBL; GG677298; EER10627.1; -; Genomic_DNA.
DR RefSeq; XP_002778832.1; XM_002778786.1.
DR AlphaFoldDB; C5KY20; -.
DR EnsemblProtists; EER10627; EER10627; Pmar_PMAR019004.
DR GeneID; 9038767; -.
DR OrthoDB; 5480493at2759; -.
DR Proteomes; UP000007800; 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; 2.
DR Gene3D; 3.30.70.100; -; 2.
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; 1.
DR NCBIfam; TIGR00003; copper ion binding protein; 1.
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; 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; 2.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS01047; HMA_1; 2.
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 Copper transport {ECO:0000256|ARBA:ARBA00022796};
KW Ion transport {ECO:0000256|ARBA:ARBA00022796};
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:UP000007800};
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}; Transport {ECO:0000256|ARBA:ARBA00022796}.
FT TRANSMEM 268..287
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 293..309
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 330..349
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 369..388
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 525..547
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 567..587
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 887..906
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 918..939
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 4..77
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 91..157
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
SQ SEQUENCE 965 AA; 101734 MW; CADA02A41246269E CRC64;
MQAGAVIVKV GGMTCSSCVS TVENAVKALP FVDSCSVNLV TTKAEVKIRA AAVDLKPGSE
PVEEIVDTIE GVGFDAEVIG ITKFEAKEST ETAVIRISGM SCASCVASIE RLVGNMDGVK
TIAVDLIKGM ASVTLVTGKT SAEKVAEAIE SIGYDAQVEH VVKSIPSARR SSLSGQVPTE
PTVLRVCPSS STGLVNFEDA RNILNSTDGV VGLFESSSGH AGVVQVSYVP SRDFGARDIL
AELGPQWQLA PRDPSAGYHM DPVLKHRILL AIPLAIVVEV LSMTMLGSLL GCWLPVVLLV
LSFPVQYYCG WGYHKHAFRG LAHCSLSMDF LVSFATNMAF IYSAVWVFLN LPDLVSGRMS
SDDVNMNDCM FFETTTILIT VLLLGKALES RAKASTASAL AELSSQRPTD ATIVLPDGSL
QTIDVDLLHI GDRVKVLPGG HVPADGVVVV AGSNTSCDES LLTGESRPVK KTEGDEVVGG
SICVAGGMEF TATRVGSQTA LARILQLVES AQASKPAVQR ATDKVAAVFV PAILGFCAIV
VCVWAVVAAV SPPERAADMT DSQKALMVFR FALSILMVAC PCALGLATPT AVVVATGAAA
TRLGCLVKDA QVFELAGNRK KRMAVVLDKT GTLTEGKPGV TETVGFGDFK AKMMLAAAEA
NSEHPIATAV SAWAAPNGVD SSLTVTGFEN IPGVGVKCDV DGHHVRAGGD ISWVVGSEEV
MKQEREDYVK WMQRERDDGC VVVVVAVDGR IQGCIALKDR LRPESADLIH QLRYSLDLAV
WMCSGDHEAT AKRVAADLGI DNVIGQAKPS DKMALIRRLK LNGNAVLMVG DGVNDGPALA
AADVGVAVGS GVDVSTEAAH VVIHSLRGLA PFIELSRQTL KTIWRNLFWA FIFNIIMLPL
AAGILYPSTG ITLPPEVAGA AMACSSLVVV TNSLSIQYWT KSRYGHDEQL TKAIREATSG
QAGKE
//
