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Database: UniProt
Entry: A0A199VFE5_ANACO
LinkDB: A0A199VFE5_ANACO
Original site: A0A199VFE5_ANACO 
ID   A0A199VFE5_ANACO        Unreviewed;      1017 AA.
AC   A0A199VFE5;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   RecName: Full=P-type Cu(+) transporter {ECO:0000256|ARBA:ARBA00012517};
DE            EC=7.2.2.8 {ECO:0000256|ARBA:ARBA00012517};
GN   ORFNames=ACMD2_09789 {ECO:0000313|EMBL:OAY75733.1};
OS   Ananas comosus (Pineapple) (Ananas ananas).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Bromeliaceae;
OC   Bromelioideae; Ananas.
OX   NCBI_TaxID=4615 {ECO:0000313|EMBL:OAY75733.1, ECO:0000313|Proteomes:UP000092600};
RN   [1] {ECO:0000313|EMBL:OAY75733.1, ECO:0000313|Proteomes:UP000092600}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. MD2 {ECO:0000313|Proteomes:UP000092600};
RC   TISSUE=Leaf {ECO:0000313|EMBL:OAY75733.1};
RX   PubMed=27374615; DOI=10.1093/dnares/dsw026;
RA   Redwan R.M., Saidin A., Kumar S.V.;
RT   "The draft genome of MD-2 pineapple using hybrid error correction of long
RT   reads.";
RL   DNA Res. 0:0-0(2016).
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:OAY75733.1}.
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DR   EMBL; LSRQ01002021; OAY75733.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A199VFE5; -.
DR   STRING; 4615.A0A199VFE5; -.
DR   Proteomes; UP000092600; 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; 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; 3.
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; 1.
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   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:UP000092600};
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        311..332
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        352..370
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        382..401
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        421..438
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        574..596
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        616..636
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        948..967
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        979..1000
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   DOMAIN          74..140
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
FT   DOMAIN          148..214
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
FT   DOMAIN          223..289
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
FT   REGION          14..67
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1017 AA;  110025 MW;  59139CADFD9995E1 CRC64;
     MASRALLLSC INGDGASFST SRLLSPRPRY PSMPKYPKEP SSSSSSSAAA DLCGGGGDVE
     APAPDAEGEK KRRAVAVFSV TGVACAACAG SVEKAVKRLP GIHDAAVDVL NNRAQVIFYP
     AFVSVEEIRE TIEDAGFEAT LIEEDIKLVC RLQIKGMTCT SCSSAVESAL RAVPGVQKAA
     VALATEEAEI HFDSKLVKIN RLVEAVEEIG YGATVITTGE DRNRIDLKID GALDERSILM
     IKDSLQSLPG VDDTNIDRIL HKVTISYNSD QAGPRNFIEV VESAGFRASI YPEAGGREML
     RNEEIKQYYH SFLWSLVFTI PVFLISMVFM YIPGIKNVLD KKIVHMLTVG ELLRWILSTP
     VQFVIGRRFY TGSYKALRHG SANMDVLIAL GTNTAYFYSL YSIVRAAISP NFKGTDFFET
     SSMLISFILL GKYLEILAKG KTSEAIAKLM DLAPETATLL AYDGEGQVVN EREIDSRLIQ
     KNDVIKVVPG GKVASDGTVI WGQSYVNESM ITGESRPVAK RKGDDVIGGT VNENGVLHVR
     VTRVGSESAL SQIVRLVESA QMAKAPVQKL ADRISGYFVP LVIILASLTW LAWFLAGKFH
     SYPKSWIPSS TDSFQLALQF GISVMVIACP CALGLATPTA VMVGTGVGAS QGVLIKGGHA
     LEGAHKQFQS LEETKLHLLQ VNCIVFDKTG TLTTGKPILV DRKILNKMNT REFFEYVGSA
     EVNSEHPLAK AIIQYAKNIL GEEHVWPEAR DFESVTGYGV KSTVRDKEVI VGSKSWMSRL
     GIPIPTEASE FLMEAEEKAQ TGIVVLLDGE VVGVLAVSDP LKTNAREVIS LLTSMKVECI
     MVTGDNLGTA KAIAEEVGID SVVAEAKPEN KADKVKELQM SGKTVAMVGD GINDSPALVS
     ADVGIAIGAG TDIAIEAADI VLMKSNLEDV ITAIDLSRKT FSRIRMNYVW ALGYNIIGMP
     VAAGALFPST RVRLPPWVAG AAMAASSVSV VCWSLLLKYY RRPKELDRLR MEQIIIN
//
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