Chain A, Uncharacterized protein Atu1203
heavy-metal-associated domain-containing protein( domain architecture ID 10006509)
heavy-metal-associated domain-containing protein may function as a heavy metal transporter and/or detoxification protein; similar to Synechocystis Pcc6803 copper chaperone Atx1, and to Salmonella enterica gold resistance metallochaperone GolB which exhibits selectivity toward the Au(I) cation
List of domain hits
Name | Accession | Description | Interval | E-value | ||
CopZ | COG2608 | Copper chaperone CopZ [Inorganic ion transport and metabolism]; |
24-85 | 1.51e-11 | ||
Copper chaperone CopZ [Inorganic ion transport and metabolism]; : Pssm-ID: 442020 [Multi-domain] Cd Length: 71 Bit Score: 54.14 E-value: 1.51e-11
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Name | Accession | Description | Interval | E-value | ||
CopZ | COG2608 | Copper chaperone CopZ [Inorganic ion transport and metabolism]; |
24-85 | 1.51e-11 | ||
Copper chaperone CopZ [Inorganic ion transport and metabolism]; Pssm-ID: 442020 [Multi-domain] Cd Length: 71 Bit Score: 54.14 E-value: 1.51e-11
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HMA | pfam00403 | Heavy-metal-associated domain; |
26-79 | 2.80e-08 | ||
Heavy-metal-associated domain; Pssm-ID: 459804 [Multi-domain] Cd Length: 58 Bit Score: 45.69 E-value: 2.80e-08
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HMA | cd00371 | Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ... |
28-85 | 1.71e-05 | ||
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: 38.74 E-value: 1.71e-05
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PRK13748 | PRK13748 | putative mercuric reductase; Provisional |
26-85 | 7.58e-04 | ||
putative mercuric reductase; Provisional Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 36.28 E-value: 7.58e-04
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chaper_CopZ_Eh | NF033794 | copper chaperone CopZ; Copper chaperone CopZ, as the name is used in Enterococcus hirae and ... |
26-85 | 1.69e-03 | ||
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: 33.46 E-value: 1.69e-03
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Name | Accession | Description | Interval | E-value | ||
CopZ | COG2608 | Copper chaperone CopZ [Inorganic ion transport and metabolism]; |
24-85 | 1.51e-11 | ||
Copper chaperone CopZ [Inorganic ion transport and metabolism]; Pssm-ID: 442020 [Multi-domain] Cd Length: 71 Bit Score: 54.14 E-value: 1.51e-11
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HMA | pfam00403 | Heavy-metal-associated domain; |
26-79 | 2.80e-08 | ||
Heavy-metal-associated domain; Pssm-ID: 459804 [Multi-domain] Cd Length: 58 Bit Score: 45.69 E-value: 2.80e-08
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ZntA | COG2217 | Cation-transporting P-type ATPase [Inorganic ion transport and metabolism]; |
24-85 | 1.38e-06 | ||
Cation-transporting P-type ATPase [Inorganic ion transport and metabolism]; Pssm-ID: 441819 [Multi-domain] Cd Length: 717 Bit Score: 43.98 E-value: 1.38e-06
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HMA | cd00371 | Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ... |
28-85 | 1.71e-05 | ||
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: 38.74 E-value: 1.71e-05
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PRK13748 | PRK13748 | putative mercuric reductase; Provisional |
26-85 | 7.58e-04 | ||
putative mercuric reductase; Provisional Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 36.28 E-value: 7.58e-04
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chaper_CopZ_Eh | NF033794 | copper chaperone CopZ; Copper chaperone CopZ, as the name is used in Enterococcus hirae and ... |
26-85 | 1.69e-03 | ||
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: 33.46 E-value: 1.69e-03
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Blast search parameters | ||||
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