ID A0A0M0J3R9_9EUKA Unreviewed; 1382 AA.
AC A0A0M0J3R9;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Heavy metal P-type ATPase {ECO:0000313|EMBL:KOO21211.1};
GN ORFNames=Ctob_004931 {ECO:0000313|EMBL:KOO21211.1};
OS Chrysochromulina tobinii.
OC Eukaryota; Haptista; Haptophyta; Prymnesiophyceae; Prymnesiales;
OC Chrysochromulinaceae; Chrysochromulina.
OX NCBI_TaxID=1460289 {ECO:0000313|EMBL:KOO21211.1, ECO:0000313|Proteomes:UP000037460};
RN [1] {ECO:0000313|Proteomes:UP000037460}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCMP291 {ECO:0000313|Proteomes:UP000037460};
RX PubMed=26397803; DOI=10.1371/journal.pgen.1005469;
RA Hovde B.T., Deodato C.R., Hunsperger H.M., Ryken S.A., Yost W., Jha R.K.,
RA Patterson J., Monnat R.J. Jr., Barlow S.B., Starkenburg S.R.,
RA Cattolico R.A.;
RT "Genome Sequence and Transcriptome Analyses of Chrysochromulina tobin:
RT Metabolic Tools for Enhanced Algal Fitness in the Prominent Order
RT Prymnesiales (Haptophyceae).";
RL PLoS Genet. 11:e1005469-e1005469(2015).
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}.
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:KOO21211.1}.
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DR EMBL; JWZX01003382; KOO21211.1; -; Genomic_DNA.
DR OrthoDB; 5480493at2759; -.
DR Proteomes; UP000037460; 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; 7.
DR CDD; cd02094; P-type_ATPase_Cu-like; 1.
DR Gene3D; 3.30.70.100; -; 7.
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 NCBIfam; TIGR01525; ATPase-IB_hvy; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
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; 7.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00120; HATPASE.
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; 7.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS01047; HMA_1; 4.
DR PROSITE; PS50846; HMA_2; 7.
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:UP000037460};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
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 610..631
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 643..664
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 685..706
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 718..735
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 874..896
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 983..1004
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 1288..1312
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 1318..1340
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 2..68
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 70..133
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 149..212
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 219..282
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 315..378
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 409..472
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 519..585
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT REGION 484..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 909..973
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1357..1382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 924..946
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1382 AA; 142668 MW; A9D612022568856C CRC64;
MVEQVYQVSS IVCSGCKEAV EAELSQIDGV EAARVDIPTG SVTVWGNAPF TALQVAVSKS
ERVLTPLGSF CVKLHVDGMM CGHCTAKVEQ GLQAVVGVAS VKVDLKAELA TVVGTATSAA
LIHAIETTGH AAKVVEPDKA PASPRVLPSK TTLTVRGMSC GHCSAKVEKA LHDVEGVLSA
QVDLEAALAI VVGTAPLAAL LAAVEKAGLT AASAPLRPTT TTLSVGGMMC DHCTAKVEKS
LQVIEGVIST QVDLATGLAT IVGTVPLAAL IAAVEATGHP TVVASAVASA VEAGTAGPSE
GLEGTGLTHK HAADSSVTLQ VDGMFCEACR ATIKRELSAL PGVTFVAVNL HWGIVTVRGT
SSVEELIESI SSAGRFTAHE LASGDEDFTG LAADPFAPTP AAKGGRAEKL IKLLVMDMLC
SGCKDKVDRA ARMVRGVAHV DIDLDTHVLS VSGQLATEDV LAAVKAAGYE PCLLSEDFPA
KSSEACPVPS PGASPAASLP KATEGKVPKG KKVGKDHLHE VSLTIDGMTC ASCVGAVEGG
LLSLEGVHSA TVSLMGKSGK VAYDARRVDV PAILARVVKT GYAAELQADD IEAVAAASNF
GIEIAYWWRM FAGSMVFTLP VFLISMVFRM IPSTSPGLYV DVAPGLAVSV LVNLILTTPV
QLYYGFPFHR GAYASLRRCH FTMDVLVSIG TFAAYIYSII FMFVSIGTRG EEGEDHEFFE
TAAVLITFIL LGEYLESAAK GKASNAITQL LTLVPPTALQ LASCREIDLD ATEVPVSGLR
KGDVVKVLPG AQMPADGTVL FGESAVNESM ITGESLPQPK RKNDKVVGGT INGSGVLYVL
VTAVGADTTL AQIMRIVADA QHRKPRIQAV ADRISAVFVP VVITLAIFTW AAWAIAGATG
NMPDWSGDDD LDMMSFSSPS PPNPHAGHNM PPNPPNTPPD PHASHNMPPD PHVSNNMGSG
GGSGGGGHGA MSMGVPSVED PQLLAFMFGC AVLVIACPCA LGLATPTAVM VGGGVGAAHG
ILIKGGDVLE LAAAVQTICF DKTGTLTTGK LSVARVLLWA QGVNEAILLR AAGSAERGSE
HPIAKAIINH AELFGVQTAE PADFVAAAGQ GLQCVVDGKT VLMGNRSWME ENGLKLSDVQ
EAEVAALESR GALAVADSLK PDAPAVVKQL TQLGMKVWMI SGDNERTAAH IAAQAGIDLM
YVVAGVKPAG KLAKVQELRD AGAKIAFVGD GINDAPALAA ADVGIAVGSG TDVAIEAADV
VLMKEGLQDV VTALDLSKVV MRRIRINFVW AFGFNVVGIP LAAGVLFPGL GIQLPPMFAG
GAMALSSVSV VCSSLLLRFY QPPRPLSMRR QVFSRRSAEP PVSPPKMAAL EELAGPDTAS
AV
//