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iron-sulfur cluster co-chaperone protein HscB isoform X3 [Rattus norvegicus]
List of domain hits
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Name | Accession | Description | Interval | E-value | ||
HscB_4_cys | pfam18256 | Co-chaperone HscB tetracysteine metal binding motif; This is the N-terminal domain of human ... |
38-64 | 4.09e-11 | ||
Co-chaperone HscB tetracysteine metal binding motif; This is the N-terminal domain of human co-chaperone protein HscB (hHscB). This domain is capable of binding a metal ion through its tetracysteine metal binding motif. The metal atom is coordinated by a set of four cysteine residues (Cys41, Cys44, Cys58 and Cys61) on opposed beta-hairpins. Although the N-domain lacks any recognizable secondary structure elements, it has several distant structural homologs including C-4 zinc finger domains and rubredoxin. : Pssm-ID: 375683 Cd Length: 27 Bit Score: 54.72 E-value: 4.09e-11
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hscB super family | cl35209 | Fe-S protein assembly co-chaperone HscB; |
67-142 | 1.40e-10 | ||
Fe-S protein assembly co-chaperone HscB; The actual alignment was detected with superfamily member PRK03578: Pssm-ID: 235133 [Multi-domain] Cd Length: 176 Bit Score: 56.95 E-value: 1.40e-10
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Name | Accession | Description | Interval | E-value | ||
HscB_4_cys | pfam18256 | Co-chaperone HscB tetracysteine metal binding motif; This is the N-terminal domain of human ... |
38-64 | 4.09e-11 | ||
Co-chaperone HscB tetracysteine metal binding motif; This is the N-terminal domain of human co-chaperone protein HscB (hHscB). This domain is capable of binding a metal ion through its tetracysteine metal binding motif. The metal atom is coordinated by a set of four cysteine residues (Cys41, Cys44, Cys58 and Cys61) on opposed beta-hairpins. Although the N-domain lacks any recognizable secondary structure elements, it has several distant structural homologs including C-4 zinc finger domains and rubredoxin. Pssm-ID: 375683 Cd Length: 27 Bit Score: 54.72 E-value: 4.09e-11
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hscB | PRK03578 | Fe-S protein assembly co-chaperone HscB; |
67-142 | 1.40e-10 | ||
Fe-S protein assembly co-chaperone HscB; Pssm-ID: 235133 [Multi-domain] Cd Length: 176 Bit Score: 56.95 E-value: 1.40e-10
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DjlA | COG1076 | DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones]; |
99-140 | 7.24e-05 | ||
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440694 [Multi-domain] Cd Length: 75 Bit Score: 39.39 E-value: 7.24e-05
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hscB | TIGR00714 | Fe-S protein assembly co-chaperone HscB; This model describes the small subunit, Hsc20 (20K ... |
101-141 | 2.02e-04 | ||
Fe-S protein assembly co-chaperone HscB; This model describes the small subunit, Hsc20 (20K heat shock cognate protein) of a pair of proteins Hsc66-Hsc20, related to the DnaK-DnaJ heat shock proteins, which also serve as molecular chaperones. Hsc20, unlike DnaJ, appears not to have chaperone activity on its own, but to act solely as a regulatory subunit for Hsc66 (i.e., to be a co-chaperone). The gene for Hsc20 in E. coli, hscB, is not induced by heat shock. [Protein fate, Protein folding and stabilization] Pssm-ID: 211601 [Multi-domain] Cd Length: 155 Bit Score: 39.48 E-value: 2.02e-04
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Name | Accession | Description | Interval | E-value | ||
HscB_4_cys | pfam18256 | Co-chaperone HscB tetracysteine metal binding motif; This is the N-terminal domain of human ... |
38-64 | 4.09e-11 | ||
Co-chaperone HscB tetracysteine metal binding motif; This is the N-terminal domain of human co-chaperone protein HscB (hHscB). This domain is capable of binding a metal ion through its tetracysteine metal binding motif. The metal atom is coordinated by a set of four cysteine residues (Cys41, Cys44, Cys58 and Cys61) on opposed beta-hairpins. Although the N-domain lacks any recognizable secondary structure elements, it has several distant structural homologs including C-4 zinc finger domains and rubredoxin. Pssm-ID: 375683 Cd Length: 27 Bit Score: 54.72 E-value: 4.09e-11
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hscB | PRK03578 | Fe-S protein assembly co-chaperone HscB; |
67-142 | 1.40e-10 | ||
Fe-S protein assembly co-chaperone HscB; Pssm-ID: 235133 [Multi-domain] Cd Length: 176 Bit Score: 56.95 E-value: 1.40e-10
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hscB | PRK00294 | co-chaperone HscB; Provisional |
72-141 | 1.11e-08 | ||
co-chaperone HscB; Provisional Pssm-ID: 166894 [Multi-domain] Cd Length: 173 Bit Score: 51.78 E-value: 1.11e-08
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hscB | PRK05014 | co-chaperone HscB; Provisional |
71-140 | 3.64e-08 | ||
co-chaperone HscB; Provisional Pssm-ID: 179914 [Multi-domain] Cd Length: 171 Bit Score: 50.29 E-value: 3.64e-08
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hscB | PRK01773 | Fe-S protein assembly co-chaperone HscB; |
73-136 | 6.80e-06 | ||
Fe-S protein assembly co-chaperone HscB; Pssm-ID: 179335 [Multi-domain] Cd Length: 173 Bit Score: 43.96 E-value: 6.80e-06
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DjlA | COG1076 | DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones]; |
99-140 | 7.24e-05 | ||
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440694 [Multi-domain] Cd Length: 75 Bit Score: 39.39 E-value: 7.24e-05
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hscB | TIGR00714 | Fe-S protein assembly co-chaperone HscB; This model describes the small subunit, Hsc20 (20K ... |
101-141 | 2.02e-04 | ||
Fe-S protein assembly co-chaperone HscB; This model describes the small subunit, Hsc20 (20K heat shock cognate protein) of a pair of proteins Hsc66-Hsc20, related to the DnaK-DnaJ heat shock proteins, which also serve as molecular chaperones. Hsc20, unlike DnaJ, appears not to have chaperone activity on its own, but to act solely as a regulatory subunit for Hsc66 (i.e., to be a co-chaperone). The gene for Hsc20 in E. coli, hscB, is not induced by heat shock. [Protein fate, Protein folding and stabilization] Pssm-ID: 211601 [Multi-domain] Cd Length: 155 Bit Score: 39.48 E-value: 2.02e-04
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hscB | PRK01356 | co-chaperone HscB; Provisional |
71-141 | 1.89e-03 | ||
co-chaperone HscB; Provisional Pssm-ID: 167217 [Multi-domain] Cd Length: 166 Bit Score: 37.16 E-value: 1.89e-03
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PknG_rubred | pfam16919 | Protein kinase G rubredoxin domain; This rubredoxin domain is found at the N-terminus of ... |
40-60 | 2.16e-03 | ||
Protein kinase G rubredoxin domain; This rubredoxin domain is found at the N-terminus of protein kinase G, and is essential for kinase activity. Pssm-ID: 435653 Cd Length: 139 Bit Score: 36.64 E-value: 2.16e-03
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Blast search parameters | ||||
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