ID F0ZLT3_DICPU Unreviewed; 943 AA.
AC F0ZLT3;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=HMA domain-containing protein {ECO:0000259|PROSITE:PS50846};
GN ORFNames=DICPUDRAFT_47891 {ECO:0000313|EMBL:EGC35084.1};
OS Dictyostelium purpureum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=5786 {ECO:0000313|EMBL:EGC35084.1, ECO:0000313|Proteomes:UP000001064};
RN [1] {ECO:0000313|Proteomes:UP000001064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QSDP1 {ECO:0000313|Proteomes:UP000001064};
RX PubMed=21356102; DOI=10.1186/gb-2011-12-2-r20;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Sucgang R., Kuo A., Tian X., Salerno W., Parikh A., Feasley C.L., Dalin E.,
RA Tu H., Huang E., Barry K., Lindquist E., Shapiro H., Bruce D., Schmutz J.,
RA Salamov A., Fey P., Gaudet P., Anjard C., Babu M.M., Basu S.,
RA Bushmanova Y., van der Wel H., Katoh-Kurasawa M., Dinh C., Coutinho P.M.,
RA Saito T., Elias M., Schaap P., Kay R.R., Henrissat B., Eichinger L.,
RA Rivero F., Putnam N.H., West C.M., Loomis W.F., Chisholm R.L., Shaulsky G.,
RA Strassmann J.E., Queller D.C., Kuspa A., Grigoriev I.V.;
RT "Comparative genomics of the social amoebae Dictyostelium discoideum and
RT Dictyostelium purpureum.";
RL Genome Biol. 12:R20.1-R20.23(2011).
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}.
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DR EMBL; GL871072; EGC35084.1; -; Genomic_DNA.
DR RefSeq; XP_003288391.1; XM_003288343.1.
DR AlphaFoldDB; F0ZLT3; -.
DR STRING; 5786.F0ZLT3; -.
DR EnsemblProtists; EGC35084; EGC35084; DICPUDRAFT_47891.
DR GeneID; 10501823; -.
DR KEGG; dpp:DICPUDRAFT_47891; -.
DR eggNOG; KOG0207; Eukaryota.
DR InParanoid; F0ZLT3; -.
DR OMA; WECFFDE; -.
DR OrthoDB; 7279at2759; -.
DR Proteomes; UP000001064; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0005507; F:copper ion binding; IBA:GO_Central.
DR GO; GO:0043682; F:P-type divalent copper transporter activity; IBA:GO_Central.
DR GO; GO:0055070; P:copper ion homeostasis; IBA:GO_Central.
DR CDD; cd00371; HMA; 2.
DR CDD; cd02094; P-type_ATPase_Cu-like; 1.
DR Gene3D; 3.30.70.100; -; 2.
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; 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; 2.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00943; CUATPASE.
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; 2.
DR SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS01047; HMA_1; 2.
DR PROSITE; PS50846; HMA_2; 2.
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:UP000001064};
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}; Transport {ECO:0000256|ARBA:ARBA00022796}.
FT TRANSMEM 196..219
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 225..245
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 266..288
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 308..325
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 461..483
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 503..523
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 829..852
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 858..877
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 32..98
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 106..172
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
SQ SEQUENCE 943 AA; 101996 MW; 954F33FF833CB8D0 CRC64;
MGDYIKLEVL DSKQNDNNNK NIADGASIPT SKKAIFSIQG MTCSSCVGII ESFVSNCEGV
ISIQVALLQE TAEVRFNPQI LSEDDIIEQI ETVGFEAKHL QQAENNTVTL LIGGMTCTSC
VGIIESFVSG VDGVVDIKVN LAMETARVVY DPDSTGVRDI IKAIEDVGFT AQVPSHDMDQ
SKNLQHEESE RLRKTLILSF MFTLPVFVIG MIPGFGWLFK IYVINNLNFA DFIMLLCATP
VQFFVGQRFY KNGYKSLKHG GANMDVLVAL GTSCAYFYSI MVMLMDLFDT TPPDTTAMGG
MKTFFDTSAS LITFILLGKY LEIIAKGKTS EAIKKLMSLQ ATKATLTTID ENGKILEERE
IDIDLVQRGD LLKVLPGSKI PTDGIVYQGQ SHIDESIITG ESLPVSKKKD DKVIGGTVNQ
KGVLIIKATR VGSETSLSQI IRLVEKAQTE RAPIQSLADK VSGYFVPTVI SLGFLTFFVW
LFAGMSGSID SYIDSYKTTV FQFALRNAIS VIVIACPCAL GLATPTAVMV GTGIGAQNGI
LIKGGSHLET AHKISAVIFD KTGTLTTGKP IVSTTGVFGK SFAKKTFFQL VASAEAASEH
PLAGAIVNYA FEVCDVQSTT SPTFFESVTG CGIRATVQNV EIMIGSLKWI MGEGINLHSN
PEIVDVPEIE DSVRRLESDG NTVVYVVLNH QICGFIAISD QLKPEARATV TALKKLGIFP
WLVTGDNPRT ANAIAQQVGI TQVFAEVLPS NKSKKVLELK KQGNVVAMVG DGINDSPALA
EADVGIAIGA GTDIAIEAAD IVLVKSDLRD VITAISLSKT TFQRIRFNYL WATVYNILGI
PLAAGILIPF GISIPPMMAG LAMAFSSISV VLSSLHLKTY KKPEIPIIEG SEFESNRIEN
ERQRNLFKKS KIIFEPIINS IQKDSSSNGK IEKISLLASD DMV
//
