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Conserved domains on  [gi|253722779]
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Chain A, Copper chaperone

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
chaper_CopZ_Eh super family cl41439
copper chaperone CopZ; Copper chaperone CopZ, as the name is used in Enterococcus hirae and ...
 2-68 8.76e-25

copper chaperone CopZ; Copper chaperone CopZ, as the name is used in Enterococcus hirae and related species, is a small copper-binding protein with close homology to domains found, sometimes in multiple copies, in various copper-translocating copper-translocating P-type ATPases, and to distinct families of other small copper chaperones that also named CopZ.


The actual alignment was detected with superfamily member NF033794:

Pssm-ID: 411374 [Multi-domain]  Cd Length: 68  Bit Score: 87.00  E-value: 8.76e-25
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 253722779  2 QEFSVKGMSCNHCVARIEEAVGRISGVKKVKVQLKKEKAVVKFDEANVQATEICQAINELGYQAEVI 68
Cdd:NF033794  2 QTFSIKGMSCNHCVARVEKAVNELPGVKKVKVNLKKENGVVKFDETQVTAEKIAQAVNELGYQAEVV 68
 
Name Accession Description Interval E-value
chaper_CopZ_Eh NF033794
copper chaperone CopZ; Copper chaperone CopZ, as the name is used in Enterococcus hirae and ...
 2-68 8.76e-25

copper chaperone CopZ; Copper chaperone CopZ, as the name is used in Enterococcus hirae and related species, is a small copper-binding protein with close homology to domains found, sometimes in multiple copies, in various copper-translocating copper-translocating P-type ATPases, and to distinct families of other small copper chaperones that also named CopZ.


Pssm-ID: 411374 [Multi-domain]  Cd Length: 68  Bit Score: 87.00  E-value: 8.76e-25
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 253722779  2 QEFSVKGMSCNHCVARIEEAVGRISGVKKVKVQLKKEKAVVKFDEANVQATEICQAINELGYQAEVI 68
Cdd:NF033794  2 QTFSIKGMSCNHCVARVEKAVNELPGVKKVKVNLKKENGVVKFDETQVTAEKIAQAVNELGYQAEVV 68
TIGR00003 TIGR00003
copper ion binding protein; This model describes an apparently copper-specific subfamily of ...
 2-66 1.31e-20

copper ion binding protein; This model describes an apparently copper-specific subfamily of the metal-binding domain HMA (pfam00403). Closely related sequences outside this model include mercury resistance proteins and repeated domains of eukaryotic eukaryotic copper transport proteins. Members of this family are strictly prokaryotic. The model identifies both small proteins consisting of just this domain and N-terminal regions of cation (probably copper) transporting ATPases. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 188014 [Multi-domain]  Cd Length: 66  Bit Score: 76.43  E-value: 1.31e-20
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 253722779   2 QEFSVKGMSCNHCVARIEEAVGRISGVKKVKVQLKKEKAVVKFDEANVQATEICQAINELGYQAE 66
Cdd:TIGR00003  2 QTFQVKGMSCNHCVDKIEKFVGEIEGVSKVKVQLEKEKVVVEFDAPNVSATEICEAILDAGYEVE 66
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
3-68 7.37e-14

Copper chaperone CopZ [Inorganic ion transport and metabolism];


Pssm-ID: 442020 [Multi-domain]  Cd Length: 71  Bit Score: 59.53  E-value: 7.37e-14
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 253722779  3 EFSVKGMSCNHCVARIEEAVGRISGVKKVKVQLKKEKAVVKFDEANVQATEICQAINELGYQAEVI 68
Cdd:COG2608   5 TLKVEGMTCGHCVARVEKALKALDGVASVEVDLATGTATVTYDPEKVSLEDIKAAIEEAGYEVEKA 70
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
 3-66 4.09e-10

Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid residues found in a number of proteins that transport or detoxify heavy metals, for example, the CPx-type heavy metal ATPases and copper chaperones. HMA domain contains two cysteine residues that are important in binding and transfer of metal ions, such as copper, cadmium, cobalt and zinc. In the case of copper, stoichiometry of binding is one Cu+ ion per binding domain. Repeats of the HMA domain in copper chaperone has been associated with Menkes/Wilson disease due to binding of multiple copper ions.


Pssm-ID: 238219 [Multi-domain]  Cd Length: 63  Bit Score: 49.53  E-value: 4.09e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 253722779  3 EFSVKGMSCNHCVARIEEAVGRISGVKKVKVQLKKEKAVVKFDEAnVQATEICQAINELGYQAE 66
Cdd:cd00371   1 ELSVEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDPE-VSPEELLEAIEDAGYKAR 63
chaper_CopZ_Bs NF033795
copper chaperone CopZ; This model describes CopZ, a small copper chaperone, as found in ...
 6-63 9.66e-09

copper chaperone CopZ; This model describes CopZ, a small copper chaperone, as found in Bacillus subtilis and related species. A number of longer protein, such as copper-translocating P-type ATPases, contain multiple CopZ-like domains, with its signature invariant CxxC motif. CopZ from other species may be more different in sequence from this family than some of those domains of longer proteins.


Pssm-ID: 411375 [Multi-domain]  Cd Length: 66  Bit Score: 46.32  E-value: 9.66e-09
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 253722779  6 VKGMSCNHCVARIEEAVGRISGVKKVKVQLKKEKAVVKFDEANVQATEICQAINELGY 63
Cdd:NF033795  6 VEGMSCGHCVKAVEGALGELNGVSSVKVNLEEGKVDVEFDESKVTLDQIKEAIEDQGY 63
PRK13748 PRK13748
putative mercuric reductase; Provisional
 1-67 8.66e-07

putative mercuric reductase; Provisional


Pssm-ID: 184298 [Multi-domain]  Cd Length: 561  Bit Score: 43.99  E-value: 8.66e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 253722779   1 AQEFSVKGMSCNHCVARIEEAVGRISGVKKVKVQLKKEKAVVKFDeANVQATEICQAINELGYQAEV 67
Cdd:PRK13748   1 MTTLKITGMTCDSCAAHVKDALEKVPGVQSADVSYPKGSAQLAIE-VGTSPDALTAAVAGLGYRATL 66
HMA pfam00403
Heavy-metal-associated domain;
4-58 1.11e-04

Heavy-metal-associated domain;


Pssm-ID: 459804 [Multi-domain]  Cd Length: 58  Bit Score: 35.67  E-value: 1.11e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 253722779   4 FSVKGMSCNHCVARIEEAVGRISGVKKVKVQLKKEKAVVKFDEANVQATEICQAI 58
Cdd:pfam00403  2 FRVSGMHCGGCAAKVEKALSELPGVLSVSVDLATKTVTVTGDAESTKLEKLVEAI 56
 
Name Accession Description Interval E-value
chaper_CopZ_Eh NF033794
copper chaperone CopZ; Copper chaperone CopZ, as the name is used in Enterococcus hirae and ...
 2-68 8.76e-25

copper chaperone CopZ; Copper chaperone CopZ, as the name is used in Enterococcus hirae and related species, is a small copper-binding protein with close homology to domains found, sometimes in multiple copies, in various copper-translocating copper-translocating P-type ATPases, and to distinct families of other small copper chaperones that also named CopZ.


Pssm-ID: 411374 [Multi-domain]  Cd Length: 68  Bit Score: 87.00  E-value: 8.76e-25
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 253722779  2 QEFSVKGMSCNHCVARIEEAVGRISGVKKVKVQLKKEKAVVKFDEANVQATEICQAINELGYQAEVI 68
Cdd:NF033794  2 QTFSIKGMSCNHCVARVEKAVNELPGVKKVKVNLKKENGVVKFDETQVTAEKIAQAVNELGYQAEVV 68
TIGR00003 TIGR00003
copper ion binding protein; This model describes an apparently copper-specific subfamily of ...
 2-66 1.31e-20

copper ion binding protein; This model describes an apparently copper-specific subfamily of the metal-binding domain HMA (pfam00403). Closely related sequences outside this model include mercury resistance proteins and repeated domains of eukaryotic eukaryotic copper transport proteins. Members of this family are strictly prokaryotic. The model identifies both small proteins consisting of just this domain and N-terminal regions of cation (probably copper) transporting ATPases. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 188014 [Multi-domain]  Cd Length: 66  Bit Score: 76.43  E-value: 1.31e-20
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 253722779   2 QEFSVKGMSCNHCVARIEEAVGRISGVKKVKVQLKKEKAVVKFDEANVQATEICQAINELGYQAE 66
Cdd:TIGR00003  2 QTFQVKGMSCNHCVDKIEKFVGEIEGVSKVKVQLEKEKVVVEFDAPNVSATEICEAILDAGYEVE 66
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
3-68 7.37e-14

Copper chaperone CopZ [Inorganic ion transport and metabolism];


Pssm-ID: 442020 [Multi-domain]  Cd Length: 71  Bit Score: 59.53  E-value: 7.37e-14
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 253722779  3 EFSVKGMSCNHCVARIEEAVGRISGVKKVKVQLKKEKAVVKFDEANVQATEICQAINELGYQAEVI 68
Cdd:COG2608   5 TLKVEGMTCGHCVARVEKALKALDGVASVEVDLATGTATVTYDPEKVSLEDIKAAIEEAGYEVEKA 70
ZntA COG2217
Cation-transporting P-type ATPase [Inorganic ion transport and metabolism];
3-68 1.70e-10

Cation-transporting P-type ATPase [Inorganic ion transport and metabolism];


Pssm-ID: 441819 [Multi-domain]  Cd Length: 717  Bit Score: 54.38  E-value: 1.70e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 253722779   3 EFSVKGMSCNHCVARIEEAVGRISGVKKVKVQLKKEKAVVKFDEANVQATEICQAINELGYQAEVI 68
Cdd:COG2217    4 RLRIEGMTCAACAWLIEKALRKLPGVLSARVNLATERARVEYDPGKVSLEELIAAVEKAGYEAEPA 69
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
 3-66 4.09e-10

Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid residues found in a number of proteins that transport or detoxify heavy metals, for example, the CPx-type heavy metal ATPases and copper chaperones. HMA domain contains two cysteine residues that are important in binding and transfer of metal ions, such as copper, cadmium, cobalt and zinc. In the case of copper, stoichiometry of binding is one Cu+ ion per binding domain. Repeats of the HMA domain in copper chaperone has been associated with Menkes/Wilson disease due to binding of multiple copper ions.


Pssm-ID: 238219 [Multi-domain]  Cd Length: 63  Bit Score: 49.53  E-value: 4.09e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 253722779  3 EFSVKGMSCNHCVARIEEAVGRISGVKKVKVQLKKEKAVVKFDEAnVQATEICQAINELGYQAE 66
Cdd:cd00371   1 ELSVEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDPE-VSPEELLEAIEDAGYKAR 63
chaper_CopZ_Bs NF033795
copper chaperone CopZ; This model describes CopZ, a small copper chaperone, as found in ...
 6-63 9.66e-09

copper chaperone CopZ; This model describes CopZ, a small copper chaperone, as found in Bacillus subtilis and related species. A number of longer protein, such as copper-translocating P-type ATPases, contain multiple CopZ-like domains, with its signature invariant CxxC motif. CopZ from other species may be more different in sequence from this family than some of those domains of longer proteins.


Pssm-ID: 411375 [Multi-domain]  Cd Length: 66  Bit Score: 46.32  E-value: 9.66e-09
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 253722779  6 VKGMSCNHCVARIEEAVGRISGVKKVKVQLKKEKAVVKFDEANVQATEICQAINELGY 63
Cdd:NF033795  6 VEGMSCGHCVKAVEGALGELNGVSSVKVNLEEGKVDVEFDESKVTLDQIKEAIEDQGY 63
PRK13748 PRK13748
putative mercuric reductase; Provisional
 1-67 8.66e-07

putative mercuric reductase; Provisional


Pssm-ID: 184298 [Multi-domain]  Cd Length: 561  Bit Score: 43.99  E-value: 8.66e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 253722779   1 AQEFSVKGMSCNHCVARIEEAVGRISGVKKVKVQLKKEKAVVKFDeANVQATEICQAINELGYQAEV 67
Cdd:PRK13748   1 MTTLKITGMTCDSCAAHVKDALEKVPGVQSADVSYPKGSAQLAIE-VGTSPDALTAAVAGLGYRATL 66
HMA pfam00403
Heavy-metal-associated domain;
4-58 1.11e-04

Heavy-metal-associated domain;


Pssm-ID: 459804 [Multi-domain]  Cd Length: 58  Bit Score: 35.67  E-value: 1.11e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 253722779   4 FSVKGMSCNHCVARIEEAVGRISGVKKVKVQLKKEKAVVKFDEANVQATEICQAI 58
Cdd:pfam00403  2 FRVSGMHCGGCAAKVEKALSELPGVLSVSVDLATKTVTVTGDAESTKLEKLVEAI 56
copA PRK10671
copper-exporting P-type ATPase CopA;
1-68 2.69e-04

copper-exporting P-type ATPase CopA;


Pssm-ID: 182635 [Multi-domain]  Cd Length: 834  Bit Score: 37.03  E-value: 2.69e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 253722779   1 AQEFSVKGMSCNHCVARIEEAVGRISGVKKVKVQLKKEKAVVKfdeANVQATEICQAINELGYQAEVI 68
Cdd:PRK10671 100 SQQLLLSGMSCASCVSRVQNALQSVPGVTQARVNLAERTALVM---GSASPQDLVQAVEKAGYGAEAI 164
copA PRK10671
copper-exporting P-type ATPase CopA;
4-66 1.21e-03

copper-exporting P-type ATPase CopA;


Pssm-ID: 182635 [Multi-domain]  Cd Length: 834  Bit Score: 35.10  E-value: 1.21e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 253722779   4 FSVKGMSCNHCVARIEEAVGRISGvkkvkvqlkKEKAVVKFDEANV----QATEICQAINELGYQAE 66
Cdd:PRK10671   7 LTLDGLSCGHCVKRVKESLEQRPD---------VEQADVSITEAHVtgtaSAEALIETIKQAGYDAS 64
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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