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MULTISPECIES: copper chaperone CopZ [Bacillus]

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 ...
 3-68 5.66e-33

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: 107.57  E-value: 5.66e-33
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500859860  3 QATLQVQGMSCGHCVKAVEGNVGELAGVESVKVHLDKGEVEVSFHPDQVTLHRISDVIEEQGYDVV 68
Cdd:NF033795  1 KVTLNVEGMSCGHCVKAVEGALGELNGVSSVKVNLEEGKVDVEFDESKVTLDQIKEAIEDQGYDVV 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 ...
 3-68 5.66e-33

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: 107.57  E-value: 5.66e-33
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500859860  3 QATLQVQGMSCGHCVKAVEGNVGELAGVESVKVHLDKGEVEVSFHPDQVTLHRISDVIEEQGYDVV 68
Cdd:NF033795  1 KVTLNVEGMSCGHCVKAVEGALGELNGVSSVKVNLEEGKVDVEFDESKVTLDQIKEAIEDQGYDVV 66
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
1-68 6.60e-22

Copper chaperone CopZ [Inorganic ion transport and metabolism];


Pssm-ID: 442020 [Multi-domain]  Cd Length: 71  Bit Score: 79.56  E-value: 6.60e-22
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500859860  1 MEQATLQVQGMSCGHCVKAVEGNVGELAGVESVKVHLDKGEVEVSFHPDQVTLHRISDVIEEQGYDVV 68
Cdd:COG2608   1 MKTVTLKVEGMTCGHCVARVEKALKALDGVASVEVDLATGTATVTYDPEKVSLEDIKAAIEEAGYEVE 68
TIGR00003 TIGR00003
copper ion binding protein; This model describes an apparently copper-specific subfamily of ...
 3-68 4.78e-17

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: 67.57  E-value: 4.78e-17
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500859860   3 QATLQVQGMSCGHCVKAVEGNVGELAGVESVKVHLDKGEVEVSFHPDQVTLHRISDVIEEQGYDVV 68
Cdd:TIGR00003  1 KQTFQVKGMSCNHCVDKIEKFVGEIEGVSKVKVQLEKEKVVVEFDAPNVSATEICEAILDAGYEVE 66
chaper_CopZ_Eh NF033794
copper chaperone CopZ; Copper chaperone CopZ, as the name is used in Enterococcus hirae and ...
 5-66 5.20e-16

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: 64.66  E-value: 5.20e-16
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500859860  5 TLQVQGMSCGHCVKAVEGNVGELAGVESVKVHLDKGEVEVSFHPDQVTLHRISDVIEEQGYD 66
Cdd:NF033794  3 TFSIKGMSCNHCVARVEKAVNELPGVKKVKVNLKKENGVVKFDETQVTAEKIAQAVNELGYQ 64
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
 5-67 3.52e-13

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: 57.62  E-value: 3.52e-13
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500859860  5 TLQVQGMSCGHCVKAVEGNVGELAGVESVKVHLDKGEVEVSFHPDqVTLHRISDVIEEQGYDV 67
Cdd:cd00371   1 ELSVEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDPE-VSPEELLEAIEDAGYKA 62
HMA pfam00403
Heavy-metal-associated domain;
5-62 2.78e-10

Heavy-metal-associated domain;


Pssm-ID: 459804 [Multi-domain]  Cd Length: 58  Bit Score: 49.93  E-value: 2.78e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 500859860   5 TLQVQGMSCGHCVKAVEGNVGELAGVESVKVHLDKGEVEVSFHPDQVTLHRISDVIEE 62
Cdd:pfam00403  1 TFRVSGMHCGGCAAKVEKALSELPGVLSVSVDLATKTVTVTGDAESTKLEKLVEAIEK 58
copA PRK10671
copper-exporting P-type ATPase CopA;
1-66 6.85e-07

copper-exporting P-type ATPase CopA;


Pssm-ID: 182635 [Multi-domain]  Cd Length: 834  Bit Score: 44.35  E-value: 6.85e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 500859860   1 MEQAT-LQVQGMSCGHCVKAVEGNVGELAGVESVKVHLDKGEVEVSfhpdqVTLHRISDVIEEQGYD 66
Cdd:PRK10671   1 MSQTIdLTLDGLSCGHCVKRVKESLEQRPDVEQADVSITEAHVTGT-----ASAEALIETIKQAGYD 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 ...
 3-68 5.66e-33

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: 107.57  E-value: 5.66e-33
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500859860  3 QATLQVQGMSCGHCVKAVEGNVGELAGVESVKVHLDKGEVEVSFHPDQVTLHRISDVIEEQGYDVV 68
Cdd:NF033795  1 KVTLNVEGMSCGHCVKAVEGALGELNGVSSVKVNLEEGKVDVEFDESKVTLDQIKEAIEDQGYDVV 66
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
1-68 6.60e-22

Copper chaperone CopZ [Inorganic ion transport and metabolism];


Pssm-ID: 442020 [Multi-domain]  Cd Length: 71  Bit Score: 79.56  E-value: 6.60e-22
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500859860  1 MEQATLQVQGMSCGHCVKAVEGNVGELAGVESVKVHLDKGEVEVSFHPDQVTLHRISDVIEEQGYDVV 68
Cdd:COG2608   1 MKTVTLKVEGMTCGHCVARVEKALKALDGVASVEVDLATGTATVTYDPEKVSLEDIKAAIEEAGYEVE 68
TIGR00003 TIGR00003
copper ion binding protein; This model describes an apparently copper-specific subfamily of ...
 3-68 4.78e-17

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: 67.57  E-value: 4.78e-17
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500859860   3 QATLQVQGMSCGHCVKAVEGNVGELAGVESVKVHLDKGEVEVSFHPDQVTLHRISDVIEEQGYDVV 68
Cdd:TIGR00003  1 KQTFQVKGMSCNHCVDKIEKFVGEIEGVSKVKVQLEKEKVVVEFDAPNVSATEICEAILDAGYEVE 66
chaper_CopZ_Eh NF033794
copper chaperone CopZ; Copper chaperone CopZ, as the name is used in Enterococcus hirae and ...
 5-66 5.20e-16

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: 64.66  E-value: 5.20e-16
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500859860  5 TLQVQGMSCGHCVKAVEGNVGELAGVESVKVHLDKGEVEVSFHPDQVTLHRISDVIEEQGYD 66
Cdd:NF033794  3 TFSIKGMSCNHCVARVEKAVNELPGVKKVKVNLKKENGVVKFDETQVTAEKIAQAVNELGYQ 64
ZntA COG2217
Cation-transporting P-type ATPase [Inorganic ion transport and metabolism];
2-68 2.09e-14

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


Pssm-ID: 441819 [Multi-domain]  Cd Length: 717  Bit Score: 65.55  E-value: 2.09e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 500859860   2 EQATLQVQGMSCGHCVKAVEGNVGELAGVESVKVHLDKGEVEVSFHPDQVTLHRISDVIEEQGYDVV 68
Cdd:COG2217    1 ERVRLRIEGMTCAACAWLIEKALRKLPGVLSARVNLATERARVEYDPGKVSLEELIAAVEKAGYEAE 67
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
 5-67 3.52e-13

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: 57.62  E-value: 3.52e-13
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500859860  5 TLQVQGMSCGHCVKAVEGNVGELAGVESVKVHLDKGEVEVSFHPDqVTLHRISDVIEEQGYDV 67
Cdd:cd00371   1 ELSVEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDPE-VSPEELLEAIEDAGYKA 62
HMA pfam00403
Heavy-metal-associated domain;
5-62 2.78e-10

Heavy-metal-associated domain;


Pssm-ID: 459804 [Multi-domain]  Cd Length: 58  Bit Score: 49.93  E-value: 2.78e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 500859860   5 TLQVQGMSCGHCVKAVEGNVGELAGVESVKVHLDKGEVEVSFHPDQVTLHRISDVIEE 62
Cdd:pfam00403  1 TFRVSGMHCGGCAAKVEKALSELPGVLSVSVDLATKTVTVTGDAESTKLEKLVEAIEK 58
copA PRK10671
copper-exporting P-type ATPase CopA;
1-66 6.85e-07

copper-exporting P-type ATPase CopA;


Pssm-ID: 182635 [Multi-domain]  Cd Length: 834  Bit Score: 44.35  E-value: 6.85e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 500859860   1 MEQAT-LQVQGMSCGHCVKAVEGNVGELAGVESVKVHLDKGEVEVSfhpdqVTLHRISDVIEEQGYD 66
Cdd:PRK10671   1 MSQTIdLTLDGLSCGHCVKRVKESLEQRPDVEQADVSITEAHVTGT-----ASAEALIETIKQAGYD 62
PLN02957 PLN02957
copper, zinc superoxide dismutase
 11-66 4.81e-05

copper, zinc superoxide dismutase


Pssm-ID: 215516 [Multi-domain]  Cd Length: 238  Bit Score: 38.96  E-value: 4.81e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 500859860  11 MSCGHCVKAVEGNVGELAGVESVKVHLDKGEVEV--SFHPDQVTlhrisDVIEEQGYD 66
Cdd:PLN02957  14 MKCEGCVAAVKNKLETLEGVKAVEVDLSNQVVRVlgSSPVKAMT-----AALEQTGRK 66
zntA PRK11033
zinc/cadmium/mercury/lead-transporting ATPase; Provisional
 7-35 3.91e-04

zinc/cadmium/mercury/lead-transporting ATPase; Provisional


Pssm-ID: 236827 [Multi-domain]  Cd Length: 741  Bit Score: 36.51  E-value: 3.91e-04
                         10        20
                 ....*....|....*....|....*....
gi 500859860   7 QVQGMSCGHCVKAVEGNVGELAGVESVKV 35
Cdd:PRK11033  58 KVSGMDCPSCARKVENAVRQLAGVNQVQV 86
PRK13748 PRK13748
putative mercuric reductase; Provisional
 5-49 3.80e-03

putative mercuric reductase; Provisional


Pssm-ID: 184298 [Multi-domain]  Cd Length: 561  Bit Score: 33.59  E-value: 3.80e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 500859860   5 TLQVQGMSCGHCVKAVEGNVGELAGVESVKVHLDKGEVEVSFHPD 49
Cdd:PRK13748   3 TLKITGMTCDSCAAHVKDALEKVPGVQSADVSYPKGSAQLAIEVG 47
CYP27B1 cd20648
cytochrome P450 family 27, subfamily B, polypeptide 1, also called calcidiol 1-monooxygenase; ...
 17-55 7.69e-03

cytochrome P450 family 27, subfamily B, polypeptide 1, also called calcidiol 1-monooxygenase; Cytochrome p450 27B1 (CYP27B1) is also called calcidiol 1-monooxygenase (EC 1.14.15.18), 25-hydroxyvitamin D(3) 1-alpha-hydroxylase (VD3 1A hydroxylase), 25-hydroxyvitamin D-1 alpha hydroxylase, 25-OHD-1 alpha-hydroxylase, 25-hydroxycholecalciferol 1-hydroxylase, or 25-hydroxycholecalciferol 1-monooxygenase. It catalyzes the conversion of 25-hydroxyvitamin D3 (25(OH)D3) to 1-alpha,25-dihydroxyvitamin D3 (1,25(OH)2D3 or calcitriol), and of 24,25-dihydroxyvitamin D3 (24,25(OH)(2)D3) to 1-alpha,24,25-trihydroxyvitamin D3 (1alpha,24,25(OH)(3)D3). It is also active with 25-hydroxy-24-oxo-vitamin D3, and has an important role in normal bone growth, calcium metabolism, and tissue differentiation. CYP27B1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410741 [Multi-domain]  Cd Length: 430  Bit Score: 32.80  E-value: 7.69e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 500859860  17 VKAVEGNVGEL--AGVESVKVHLDKGEVEVSFHPD-QVTLHR 55
Cdd:cd20648  232 MKSIYGNVTELllAGVDTISSTLSWSLYELSRHPDvQTALHR 273
 
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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