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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//