MULTISPECIES: copper chaperone CopZ [Enterococcus]
List of domain hits
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 ... |
2-69 | 4.66e-31 | ||
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: 102.80 E-value: 4.66e-31
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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 ... |
2-69 | 4.66e-31 | ||
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: 102.80 E-value: 4.66e-31
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CopZ | COG2608 | Copper chaperone CopZ [Inorganic ion transport and metabolism]; |
1-68 | 1.18e-22 | ||
Copper chaperone CopZ [Inorganic ion transport and metabolism]; Pssm-ID: 442020 [Multi-domain] Cd Length: 71 Bit Score: 81.87 E-value: 1.18e-22
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chaper_CopZ_Bs | NF033795 | copper chaperone CopZ; This model describes CopZ, a small copper chaperone, as found in ... |
2-64 | 1.06e-16 | ||
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: 66.35 E-value: 1.06e-16
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HMA | cd00371 | Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ... |
7-67 | 1.70e-14 | ||
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: 60.70 E-value: 1.70e-14
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PRK13748 | PRK13748 | putative mercuric reductase; Provisional |
6-69 | 1.76e-14 | ||
putative mercuric reductase; Provisional Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 65.56 E-value: 1.76e-14
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TIGR00003 | TIGR00003 | copper ion binding protein; This model describes an apparently copper-specific subfamily of ... |
2-66 | 9.82e-13 | ||
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: 56.40 E-value: 9.82e-13
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HMA | pfam00403 | Heavy-metal-associated domain; |
4-59 | 5.61e-12 | ||
Heavy-metal-associated domain; Pssm-ID: 459804 [Multi-domain] Cd Length: 58 Bit Score: 54.16 E-value: 5.61e-12
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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 ... |
2-69 | 4.66e-31 | ||
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: 102.80 E-value: 4.66e-31
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CopZ | COG2608 | Copper chaperone CopZ [Inorganic ion transport and metabolism]; |
1-68 | 1.18e-22 | ||
Copper chaperone CopZ [Inorganic ion transport and metabolism]; Pssm-ID: 442020 [Multi-domain] Cd Length: 71 Bit Score: 81.87 E-value: 1.18e-22
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ZntA | COG2217 | Cation-transporting P-type ATPase [Inorganic ion transport and metabolism]; |
1-69 | 1.14e-19 | ||
Cation-transporting P-type ATPase [Inorganic ion transport and metabolism]; Pssm-ID: 441819 [Multi-domain] Cd Length: 717 Bit Score: 80.57 E-value: 1.14e-19
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chaper_CopZ_Bs | NF033795 | copper chaperone CopZ; This model describes CopZ, a small copper chaperone, as found in ... |
2-64 | 1.06e-16 | ||
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: 66.35 E-value: 1.06e-16
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HMA | cd00371 | Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ... |
7-67 | 1.70e-14 | ||
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: 60.70 E-value: 1.70e-14
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PRK13748 | PRK13748 | putative mercuric reductase; Provisional |
6-69 | 1.76e-14 | ||
putative mercuric reductase; Provisional Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 65.56 E-value: 1.76e-14
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TIGR00003 | TIGR00003 | copper ion binding protein; This model describes an apparently copper-specific subfamily of ... |
2-66 | 9.82e-13 | ||
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: 56.40 E-value: 9.82e-13
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copA | PRK10671 | copper-exporting P-type ATPase CopA; |
7-66 | 3.89e-12 | ||
copper-exporting P-type ATPase CopA; Pssm-ID: 182635 [Multi-domain] Cd Length: 834 Bit Score: 58.98 E-value: 3.89e-12
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HMA | pfam00403 | Heavy-metal-associated domain; |
4-59 | 5.61e-12 | ||
Heavy-metal-associated domain; Pssm-ID: 459804 [Multi-domain] Cd Length: 58 Bit Score: 54.16 E-value: 5.61e-12
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copA | PRK10671 | copper-exporting P-type ATPase CopA; |
7-67 | 3.07e-09 | ||
copper-exporting P-type ATPase CopA; Pssm-ID: 182635 [Multi-domain] Cd Length: 834 Bit Score: 50.90 E-value: 3.07e-09
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MerP | TIGR02052 | mercuric transport protein periplasmic component; This model represents the periplasmic ... |
7-69 | 1.74e-07 | ||
mercuric transport protein periplasmic component; This model represents the periplasmic mercury (II) binding protein of the bacterial mercury detoxification system which passes mercuric ion to the MerT transporter for subsequent reduction to Hg(0) by the mercuric reductase MerA. MerP contains a distinctive GMTCXXC motif associated with metal binding. MerP is related to a larger family of metal binding proteins (pfam00403). [Cellular processes, Detoxification] Pssm-ID: 131107 [Multi-domain] Cd Length: 92 Bit Score: 43.87 E-value: 1.74e-07
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zntA | PRK11033 | zinc/cadmium/mercury/lead-transporting ATPase; Provisional |
7-65 | 1.11e-06 | ||
zinc/cadmium/mercury/lead-transporting ATPase; Provisional Pssm-ID: 236827 [Multi-domain] Cd Length: 741 Bit Score: 43.44 E-value: 1.11e-06
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PLN02957 | PLN02957 | copper, zinc superoxide dismutase |
10-66 | 6.27e-05 | ||
copper, zinc superoxide dismutase Pssm-ID: 215516 [Multi-domain] Cd Length: 238 Bit Score: 38.58 E-value: 6.27e-05
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Blast search parameters | ||||
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