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Database: UniProt
Entry: B9RC99_RICCO
LinkDB: B9RC99_RICCO
Original site: B9RC99_RICCO 
ID   B9RC99_RICCO            Unreviewed;       987 AA.
AC   B9RC99;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 85.
DE   SubName: Full=Copper-transporting atpase P-type, putative {ECO:0000313|EMBL:EEF51170.1};
DE            EC=3.6.3.4 {ECO:0000313|EMBL:EEF51170.1};
GN   ORFNames=RCOM_1686400 {ECO:0000313|EMBL:EEF51170.1};
OS   Ricinus communis (Castor bean).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Euphorbiaceae; Acalyphoideae; Acalypheae;
OC   Ricinus.
OX   NCBI_TaxID=3988 {ECO:0000313|Proteomes:UP000008311};
RN   [1] {ECO:0000313|Proteomes:UP000008311}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Hale {ECO:0000313|Proteomes:UP000008311};
RX   PubMed=20729833; DOI=10.1038/nbt.1674;
RA   Chan A.P., Crabtree J., Zhao Q., Lorenzi H., Orvis J., Puiu D.,
RA   Melake-Berhan A., Jones K.M., Redman J., Chen G., Cahoon E.B., Gedil M.,
RA   Stanke M., Haas B.J., Wortman J.R., Fraser-Liggett C.M., Ravel J.,
RA   Rabinowicz P.D.;
RT   "Draft genome sequence of the oilseed species Ricinus communis.";
RL   Nat. Biotechnol. 28:951-956(2010).
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}.
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DR   EMBL; EQ973774; EEF51170.1; -; Genomic_DNA.
DR   RefSeq; XP_002509783.1; XM_002509737.2.
DR   AlphaFoldDB; B9RC99; -.
DR   STRING; 3988.B9RC99; -.
DR   GeneID; 8266455; -.
DR   KEGG; rcu:8266455; -.
DR   eggNOG; KOG0207; Eukaryota.
DR   InParanoid; B9RC99; -.
DR   OrthoDB; 7279at2759; -.
DR   Proteomes; UP000008311; 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; 2.
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; 2.
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   PRINTS; PR00942; CUATPASEI.
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; 2.
DR   PROSITE; PS50846; HMA_2; 3.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU362081};
KW   Copper {ECO:0000256|ARBA:ARBA00023008};
KW   Hydrolase {ECO:0000313|EMBL:EEF51170.1};
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:UP000008311};
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        293..314
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        326..347
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        368..386
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        398..416
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        559..578
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        598..618
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        918..938
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        944..967
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   DOMAIN          48..114
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
FT   DOMAIN          126..192
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
FT   DOMAIN          201..267
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
SQ   SEQUENCE   987 AA;  107308 MW;  C3663E2BFC5054E7 CRC64;
     MAAKLLSLAC IRNESGGHDL SPRPHYPSMP KYPKGVSVRE TTVEGSEAKA VLCVIGMTCA
     ACAGSVEKAV KRLPGIKEAA VDVLNNRAQV LFYPTFVNEE TIRETIEDAG FEATLIQDET
     NDKSAQVCRI QINGMTCTSC SSAVEQALQS IQGVQTAQVA LATEEAEIHY DPKMLSYNQL
     LEAIDNTGFE AILISTGEYI DKIQLKVDGI WTYNSMRMIE NSLQALPGVQ SIDIDPELRK
     FSLSYKPEMT GPRNFIKVIE STGTGRFKAM IFPEGGGGRE SHRKEEIKQY YRSFLWSLVF
     TVPVFLTSMI FMYIPGIKHG LDTKIVNMLT VGAILRWVLS TPVQFIIGRR FYTGAYKALR
     HGSANMDVLI ALGTNAAYFY SVYSVLRAAT SSDFMGTDFF ETSSMLISFI LLGKYLEVLA
     KGKTSEAIAK LMDLAPESAI LLTLDDKGNV IDEEEIDSRL IQKNDVIKII PGAKVASDGF
     VIWGQSHVNE SMITGEARPV AKRKGDPVIG GTVNENGVMH IKATRVGSES ALAQIVRLVE
     SAQMAKAPVQ KFADRISKYF VPLVIFLSFS TWLAWFLAGK FHGYPESWIP NSMDSFQLAL
     QFGISVMVIA CPCALGLATP TAVMVGTGVG ASQGVLIKGG QALESAHKVN CIVFDKTGTL
     TVGKPVVVNT KLFKNMVLRE FYELAAAAEV NSEHPLAKAI VEYAKKFRED EENPVWPEAK
     DFISITGHGV KAIVRNREII VGNRSLMINH NIAIPVDAEE MLAETEGMAQ TGILIAIDQE
     VIGVLAISDP LKPGVHEVIS ILRSMKVRSI MVTGDNWGTA NSIAREVGIE SVIAEAKPEQ
     KAEKVKELQA AGYVVAMVGD GINDSPALVA ADVGMAIGAG TDIAIEAADI VLMKSNLEDV
     ITAIDLSRKT FSRIRLNYIW ALGYNLLGIP IAAGALFPGT GFRLPPWIAG AAMAASSVSV
     VVCSLLLKYY KRPKMLESLE IRGIRIE
//
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