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Conserved domains on  [gi|488409200|ref|WP_002478585|]
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MULTISPECIES: copper chaperone CopZ [Staphylococcus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
chaper_CopZ_Bs NF033795
copper chaperone CopZ; This model describes CopZ, a small copper chaperone, as found in ...
 4-68 7.32e-35

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: 112.19  E-value: 7.32e-35
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488409200  4 DTLNVEGMSCEHCRNAVESALAKLNGVSSAEVDLDKGQVRVGYSEDKVTIAQMKDAIEDQGYDVK 68
Cdd:NF033795  2 VTLNVEGMSCGHCVKAVEGALGELNGVSSVKVNLEEGKVDVEFDESKVTLDQIKEAIEDQGYDVV 66
 
Name Accession Description Interval E-value
chaper_CopZ_Bs NF033795
copper chaperone CopZ; This model describes CopZ, a small copper chaperone, as found in ...
 4-68 7.32e-35

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: 112.19  E-value: 7.32e-35
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488409200  4 DTLNVEGMSCEHCRNAVESALAKLNGVSSAEVDLDKGQVRVGYSEDKVTIAQMKDAIEDQGYDVK 68
Cdd:NF033795  2 VTLNVEGMSCGHCVKAVEGALGELNGVSSVKVNLEEGKVDVEFDESKVTLDQIKEAIEDQGYDVV 66
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
1-68 2.54e-23

Copper chaperone CopZ [Inorganic ion transport and metabolism];


Pssm-ID: 442020 [Multi-domain]  Cd Length: 71  Bit Score: 83.42  E-value: 2.54e-23
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488409200  1 MKIDTLNVEGMSCEHCRNAVESALAKLNGVSSAEVDLDKGQVRVGYSEDKVTIAQMKDAIEDQGYDVK 68
Cdd:COG2608   1 MKTVTLKVEGMTCGHCVARVEKALKALDGVASVEVDLATGTATVTYDPEKVSLEDIKAAIEEAGYEVE 68
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
 5-68 4.80e-16

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: 64.55  E-value: 4.80e-16
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488409200  5 TLNVEGMSCEHCRNAVESALAKLNGVSSAEVDLDKGQVRVGYSEDkVTIAQMKDAIEDQGYDVK 68
Cdd:cd00371   1 ELSVEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDPE-VSPEELLEAIEDAGYKAR 63
TIGR00003 TIGR00003
copper ion binding protein; This model describes an apparently copper-specific subfamily of ...
 5-67 1.31e-15

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: 63.71  E-value: 1.31e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488409200   5 TLNVEGMSCEHCRNAVESALAKLNGVSSAEVDLDKGQVRVGYSEDKVTIAQMKDAIEDQGYDV 67
Cdd:TIGR00003  3 TFQVKGMSCNHCVDKIEKFVGEIEGVSKVKVQLEKEKVVVEFDAPNVSATEICEAILDAGYEV 65
HMA pfam00403
Heavy-metal-associated domain;
5-62 2.93e-14

Heavy-metal-associated domain;


Pssm-ID: 459804 [Multi-domain]  Cd Length: 58  Bit Score: 59.94  E-value: 2.93e-14
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 488409200   5 TLNVEGMSCEHCRNAVESALAKLNGVSSAEVDLDKGQVRVGYSEDKVTIAQMKDAIED 62
Cdd:pfam00403  1 TFRVSGMHCGGCAAKVEKALSELPGVLSVSVDLATKTVTVTGDAESTKLEKLVEAIEK 58
chaper_CopZ_Eh NF033794
copper chaperone CopZ; Copper chaperone CopZ, as the name is used in Enterococcus hirae and ...
 5-66 4.42e-13

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: 57.34  E-value: 4.42e-13
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488409200  5 TLNVEGMSCEHCRNAVESALAKLNGVSSAEVDLDKGQVRVGYSEDKVTIAQMKDAIEDQGYD 66
Cdd:NF033794  3 TFSIKGMSCNHCVARVEKAVNELPGVKKVKVNLKKENGVVKFDETQVTAEKIAQAVNELGYQ 64
PRK13748 PRK13748
putative mercuric reductase; Provisional
 5-65 1.67e-09

putative mercuric reductase; Provisional


Pssm-ID: 184298 [Multi-domain]  Cd Length: 561  Bit Score: 51.69  E-value: 1.67e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488409200   5 TLNVEGMSCEHCRNAVESALAKLNGVSSAEVDLDKGQVRVGySEDKVTIAQMKDAIEDQGY 65
Cdd:PRK13748   3 TLKITGMTCDSCAAHVKDALEKVPGVQSADVSYPKGSAQLA-IEVGTSPDALTAAVAGLGY 62
 
Name Accession Description Interval E-value
chaper_CopZ_Bs NF033795
copper chaperone CopZ; This model describes CopZ, a small copper chaperone, as found in ...
 4-68 7.32e-35

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: 112.19  E-value: 7.32e-35
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488409200  4 DTLNVEGMSCEHCRNAVESALAKLNGVSSAEVDLDKGQVRVGYSEDKVTIAQMKDAIEDQGYDVK 68
Cdd:NF033795  2 VTLNVEGMSCGHCVKAVEGALGELNGVSSVKVNLEEGKVDVEFDESKVTLDQIKEAIEDQGYDVV 66
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
1-68 2.54e-23

Copper chaperone CopZ [Inorganic ion transport and metabolism];


Pssm-ID: 442020 [Multi-domain]  Cd Length: 71  Bit Score: 83.42  E-value: 2.54e-23
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488409200  1 MKIDTLNVEGMSCEHCRNAVESALAKLNGVSSAEVDLDKGQVRVGYSEDKVTIAQMKDAIEDQGYDVK 68
Cdd:COG2608   1 MKTVTLKVEGMTCGHCVARVEKALKALDGVASVEVDLATGTATVTYDPEKVSLEDIKAAIEEAGYEVE 68
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
 5-68 4.80e-16

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: 64.55  E-value: 4.80e-16
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488409200  5 TLNVEGMSCEHCRNAVESALAKLNGVSSAEVDLDKGQVRVGYSEDkVTIAQMKDAIEDQGYDVK 68
Cdd:cd00371   1 ELSVEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDPE-VSPEELLEAIEDAGYKAR 63
TIGR00003 TIGR00003
copper ion binding protein; This model describes an apparently copper-specific subfamily of ...
 5-67 1.31e-15

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: 63.71  E-value: 1.31e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488409200   5 TLNVEGMSCEHCRNAVESALAKLNGVSSAEVDLDKGQVRVGYSEDKVTIAQMKDAIEDQGYDV 67
Cdd:TIGR00003  3 TFQVKGMSCNHCVDKIEKFVGEIEGVSKVKVQLEKEKVVVEFDAPNVSATEICEAILDAGYEV 65
ZntA COG2217
Cation-transporting P-type ATPase [Inorganic ion transport and metabolism];
5-67 5.53e-15

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


Pssm-ID: 441819 [Multi-domain]  Cd Length: 717  Bit Score: 67.09  E-value: 5.53e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488409200   5 TLNVEGMSCEHCRNAVESALAKLNGVSSAEVDLDKGQVRVGYSEDKVTIAQMKDAIEDQGYDV 67
Cdd:COG2217    4 RLRIEGMTCAACAWLIEKALRKLPGVLSARVNLATERARVEYDPGKVSLEELIAAVEKAGYEA 66
HMA pfam00403
Heavy-metal-associated domain;
5-62 2.93e-14

Heavy-metal-associated domain;


Pssm-ID: 459804 [Multi-domain]  Cd Length: 58  Bit Score: 59.94  E-value: 2.93e-14
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 488409200   5 TLNVEGMSCEHCRNAVESALAKLNGVSSAEVDLDKGQVRVGYSEDKVTIAQMKDAIED 62
Cdd:pfam00403  1 TFRVSGMHCGGCAAKVEKALSELPGVLSVSVDLATKTVTVTGDAESTKLEKLVEAIEK 58
chaper_CopZ_Eh NF033794
copper chaperone CopZ; Copper chaperone CopZ, as the name is used in Enterococcus hirae and ...
 5-66 4.42e-13

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: 57.34  E-value: 4.42e-13
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488409200  5 TLNVEGMSCEHCRNAVESALAKLNGVSSAEVDLDKGQVRVGYSEDKVTIAQMKDAIEDQGYD 66
Cdd:NF033794  3 TFSIKGMSCNHCVARVEKAVNELPGVKKVKVNLKKENGVVKFDETQVTAEKIAQAVNELGYQ 64
PRK13748 PRK13748
putative mercuric reductase; Provisional
 5-65 1.67e-09

putative mercuric reductase; Provisional


Pssm-ID: 184298 [Multi-domain]  Cd Length: 561  Bit Score: 51.69  E-value: 1.67e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488409200   5 TLNVEGMSCEHCRNAVESALAKLNGVSSAEVDLDKGQVRVGySEDKVTIAQMKDAIEDQGY 65
Cdd:PRK13748   3 TLKITGMTCDSCAAHVKDALEKVPGVQSADVSYPKGSAQLA-IEVGTSPDALTAAVAGLGY 62
PLN02957 PLN02957
copper, zinc superoxide dismutase
 11-66 7.63e-08

copper, zinc superoxide dismutase


Pssm-ID: 215516 [Multi-domain]  Cd Length: 238  Bit Score: 46.67  E-value: 7.63e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 488409200  11 MSCEHCRNAVESALAKLNGVSSAEVDLDKGQVRVGYSEdkvTIAQMKDAIEDQGYD 66
Cdd:PLN02957  14 MKCEGCVAAVKNKLETLEGVKAVEVDLSNQVVRVLGSS---PVKAMTAALEQTGRK 66
copA PRK10671
copper-exporting P-type ATPase CopA;
6-66 3.91e-05

copper-exporting P-type ATPase CopA;


Pssm-ID: 182635 [Multi-domain]  Cd Length: 834  Bit Score: 39.34  E-value: 3.91e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488409200   6 LNVEGMSCEHCRNAVESALAKLNGVSSAEVDLDKGQVrVGYSEDKVTIAQMKDAiedqGYD 66
Cdd:PRK10671   7 LTLDGLSCGHCVKRVKESLEQRPDVEQADVSITEAHV-TGTASAEALIETIKQA----GYD 62
copA PRK10671
copper-exporting P-type ATPase CopA;
6-37 4.14e-04

copper-exporting P-type ATPase CopA;


Pssm-ID: 182635 [Multi-domain]  Cd Length: 834  Bit Score: 36.26  E-value: 4.14e-04
                         10        20        30
                 ....*....|....*....|....*....|..
gi 488409200   6 LNVEGMSCEHCRNAVESALAKLNGVSSAEVDL 37
Cdd:PRK10671 103 LLLSGMSCASCVSRVQNALQSVPGVTQARVNL 134
 
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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