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Database: UniProt
Entry: A0A200RBU8_9MAGN
LinkDB: A0A200RBU8_9MAGN
Original site: A0A200RBU8_9MAGN 
ID   A0A200RBU8_9MAGN        Unreviewed;      1266 AA.
AC   A0A200RBU8;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Cation-transporting P-type ATPase {ECO:0000313|EMBL:OVA20184.1};
GN   ORFNames=BVC80_1663g84 {ECO:0000313|EMBL:OVA20184.1};
OS   Macleaya cordata.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Ranunculales; Papaveraceae; Papaveroideae;
OC   Macleaya.
OX   NCBI_TaxID=56857 {ECO:0000313|EMBL:OVA20184.1, ECO:0000313|Proteomes:UP000195402};
RN   [1] {ECO:0000313|EMBL:OVA20184.1, ECO:0000313|Proteomes:UP000195402}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. BLH2017 {ECO:0000313|Proteomes:UP000195402};
RC   TISSUE=Root {ECO:0000313|EMBL:OVA20184.1};
RX   PubMed=28552780; DOI=.1016/j.molp.2017.05.007;
RA   Liu X., Liu Y., Huang P., Ma Y., Qing Z., Tang Q., Cao H., Cheng P.,
RA   Zheng Y., Yuan Z., Zhou Y., Liu J., Tang Z., Zhuo Y., Zhang Y., Yu L.,
RA   Huang J., Yang P., Peng Q., Zhang J., Jiang W., Zhang Z., Lin K., Ro D.K.,
RA   Chen X., Xiong X., Shang Y., Huang S., Zeng J.;
RT   "The Genome of Medicinal Plant Macleaya cordata Provides New Insights into
RT   Benzylisoquinoline Alkaloids Metabolism.";
RL   Mol. Plant 10:975-989(2017).
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:OVA20184.1}.
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DR   EMBL; MVGT01000146; OVA20184.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A200RBU8; -.
DR   STRING; 56857.A0A200RBU8; -.
DR   InParanoid; A0A200RBU8; -.
DR   OrthoDB; 731611at2759; -.
DR   Proteomes; UP000195402; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005388; F:P-type calcium transporter activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 2.
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; 2.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 2.
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; 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   PANTHER; PTHR24093:SF470; CALCIUM-TRANSPORTING ATPASE 12, PLASMA MEMBRANE-TYPE-LIKE; 1.
DR   PANTHER; PTHR24093; CATION TRANSPORTING 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   SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR   SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
DR   SUPFAM; SSF56784; HAD-like; 2.
DR   SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000195402};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        197..221
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        233..257
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        387..409
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        452..475
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1076..1094
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1100..1122
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1213..1231
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1243..1263
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          150..220
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00690"
FT   DOMAIN          1096..1265
FT                   /note="Cation-transporting P-type ATPase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00689"
FT   REGION          65..100
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        65..85
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1266 AA;  140033 MW;  70AE9BF74CF14171 CRC64;
     MNVMTISADC DHDSSIHIEL LDHSTTDHDT SSTQRSTRNL WRQVLLVFRA HARLYSIIQN
     GGNTLITTDP GVNPDESSSY TVLLSHNDDA GDDEASAQNS ATDHLDIRLD IHNSSSSNNN
     DSSSNNNNSI NVETLSSVVK EKNLDFLSEH GGVEGIAAAL DTNLENGISS EAEDVHRRQD
     AYGTNTYGEA LTSSKSFFYF FFKAAIDWTN LLLFCCAALS LGSGIKEEGL KNGWYDGTII
     FISIIVLISA TTIKNYCLSR NSKKLRNENS LVIQVLRRGQ PQSISIFDVV VGDIVFLKIG
     DLVPADGLFI KGENLKVDDD DVLHDSRIDR VENPFLYCGA KVIEGSAHML VTSVGRNTAW
     GEMMSTVNHD TRKHTLIQVR LDKLNTYLQN IGLFLAILIL VVLLLRYLMG KTDDESGYPD
     QISKRSAVGE LMKAVERFLT NPRGFRASLT TVLAILLVGI QEGLPLIITI SLSYWNGRMV
     KLHQIIIREL CGCVTMGAIT TICTNKTAEL TLDLEEVMFW VGEEEVMFWV GEEAIGRDNV
     SIISQDVLEA ICNGVATPGL VCDTSTSPTK DPLLRWAVSN LGMDMEQLKK NQTILIRETF
     SSDRKKSGLL MRKNGDAEKA IHLHWRGSAD TILAMCSDYY KSNGDIKTMD KGKRAVFQKV
     IEKMTAKGLQ SIAFAHRLIE DDGDTEDDVR KLHEDGLILL GLLGIKYSCC PEARSAVDAF
     LHAGISIKLV SPESLPVLIS IAIQYGILQS GQDLNSLVLE GEEFRKLSEA ERLEKVDQIT
     VMGSSLPSDK LLFIQCLRRR EKPSAQTEKK SGLLMRKNGN AEKAIHLHWR GSADTILAMC
     SDYYKSNGDI KTMDEGKRGV FQKVIEKMTA KGLQSIAFAH RLIEDDSDTA DDVRKLHEDG
     LILLGLLGIK YSCYPEARSA VDAFLHAGIS IKLVSPESLL VLISIAIQYG ILQSGQDLNS
     LVLEGEEFRK LSEAERLEKV DQITVMGSSL PSDKLLFIQC LRRRGQVVAV TGVTASDSPA
     LKEADVGLLM GTQNSEMAKE SSDIVIASGH LASMVTVLLF GRCAYKNIQK FIQLELTINI
     SGLLITFVTT VSLGEAPITP LQLLLVNLMV GTLAALALWT GSPTKETLKM PPVNQTESLI
     TKAMWRNIFI QVCYQAVVLL MFQFKGQILP GMNWKLKKSM ILNGFILCQV FNQFNARESE
     KKNVFKGILN NHWFLVAVGA PIVLQVVVVE FATSLSCTER LNWLQWLACI LFAIMSWPID
     YVVKCI
//
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