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chaperonin GroES [Candidatus Electrothrix communis]
GroES family protein( domain architecture ID 10785100)
GroES family protein
List of domain hits
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Name | Accession | Description | Interval | E-value | |||
GroES | COG0234 | Co-chaperonin GroES (HSP10) [Posttranslational modification, protein turnover, chaperones]; |
2-94 | 2.77e-57 | |||
Co-chaperonin GroES (HSP10) [Posttranslational modification, protein turnover, chaperones]; : Pssm-ID: 440004 Cd Length: 95 Bit Score: 171.00 E-value: 2.77e-57
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Name | Accession | Description | Interval | E-value | |||
GroES | COG0234 | Co-chaperonin GroES (HSP10) [Posttranslational modification, protein turnover, chaperones]; |
2-94 | 2.77e-57 | |||
Co-chaperonin GroES (HSP10) [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440004 Cd Length: 95 Bit Score: 171.00 E-value: 2.77e-57
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groES | PRK00364 | co-chaperonin GroES; Reviewed |
1-95 | 4.88e-57 | |||
co-chaperonin GroES; Reviewed Pssm-ID: 178988 [Multi-domain] Cd Length: 95 Bit Score: 170.30 E-value: 4.88e-57
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Cpn10 | smart00883 | Chaperonin 10 Kd subunit; The chaperonins are 'helper' molecules required for correct folding ... |
2-94 | 6.89e-55 | |||
Chaperonin 10 Kd subunit; The chaperonins are 'helper' molecules required for correct folding and subsequent assembly of some proteins. These are required for normal cell growth, and are stress-induced, acting to stabilise or protect disassembled polypeptides under heat-shock conditions. Type I chaperonins present in eubacteria, mitochondria and chloroplasts require the concerted action of 2 proteins, chaperonin 60 (cpn60) and chaperonin 10 (cpn10). The 10 kDa chaperonin (cpn10 - or groES in bacteria) exists as a ring-shaped oligomer of between six to eight identical subunits, while the 60 kDa chaperonin (cpn60 - or groEL in bacteria) forms a structure comprising 2 stacked rings, each ring containing 7 identical subunits. These ring structures assemble by self-stimulation in the presence of Mg2+-ATP. The central cavity of the cylindrical cpn60 tetradecamer provides as isolated environment for protein folding whilst cpn-10 binds to cpn-60 and synchronizes the release of the folded protein in an Mg2+-ATP dependent manner. The binding of cpn10 to cpn60 inhibits the weak ATPase activity of cpn60. Pssm-ID: 197951 Cd Length: 93 Bit Score: 164.91 E-value: 6.89e-55
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cpn10 | cd00320 | Chaperonin 10 Kd subunit (cpn10 or GroES); Cpn10 cooperates with chaperonin 60 (cpn60 or GroEL) ... |
2-94 | 8.08e-48 | |||
Chaperonin 10 Kd subunit (cpn10 or GroES); Cpn10 cooperates with chaperonin 60 (cpn60 or GroEL), an ATPase, to assist the folding and assembly of proteins and is found in eubacterial cytosol, as well as in the matrix of mitochondria and chloroplasts. It forms heptameric rings with a dome-like structure, forming a lid to the large cavity of the tetradecameric cpn60 cylinder and thereby tightly regulating release and binding of proteins to the cpn60 surface. Pssm-ID: 238197 Cd Length: 93 Bit Score: 147.27 E-value: 8.08e-48
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Cpn10 | pfam00166 | Chaperonin 10 Kd subunit; This family contains GroES and Gp31-like chaperonins. Gp31 is a ... |
2-94 | 6.22e-46 | |||
Chaperonin 10 Kd subunit; This family contains GroES and Gp31-like chaperonins. Gp31 is a functional co-chaperonin that is required for the folding and assembly of Gp23, a major capsid protein, during phage morphogenesis. Pssm-ID: 395114 Cd Length: 92 Bit Score: 142.36 E-value: 6.22e-46
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Name | Accession | Description | Interval | E-value | |||
GroES | COG0234 | Co-chaperonin GroES (HSP10) [Posttranslational modification, protein turnover, chaperones]; |
2-94 | 2.77e-57 | |||
Co-chaperonin GroES (HSP10) [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440004 Cd Length: 95 Bit Score: 171.00 E-value: 2.77e-57
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groES | PRK00364 | co-chaperonin GroES; Reviewed |
1-95 | 4.88e-57 | |||
co-chaperonin GroES; Reviewed Pssm-ID: 178988 [Multi-domain] Cd Length: 95 Bit Score: 170.30 E-value: 4.88e-57
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Cpn10 | smart00883 | Chaperonin 10 Kd subunit; The chaperonins are 'helper' molecules required for correct folding ... |
2-94 | 6.89e-55 | |||
Chaperonin 10 Kd subunit; The chaperonins are 'helper' molecules required for correct folding and subsequent assembly of some proteins. These are required for normal cell growth, and are stress-induced, acting to stabilise or protect disassembled polypeptides under heat-shock conditions. Type I chaperonins present in eubacteria, mitochondria and chloroplasts require the concerted action of 2 proteins, chaperonin 60 (cpn60) and chaperonin 10 (cpn10). The 10 kDa chaperonin (cpn10 - or groES in bacteria) exists as a ring-shaped oligomer of between six to eight identical subunits, while the 60 kDa chaperonin (cpn60 - or groEL in bacteria) forms a structure comprising 2 stacked rings, each ring containing 7 identical subunits. These ring structures assemble by self-stimulation in the presence of Mg2+-ATP. The central cavity of the cylindrical cpn60 tetradecamer provides as isolated environment for protein folding whilst cpn-10 binds to cpn-60 and synchronizes the release of the folded protein in an Mg2+-ATP dependent manner. The binding of cpn10 to cpn60 inhibits the weak ATPase activity of cpn60. Pssm-ID: 197951 Cd Length: 93 Bit Score: 164.91 E-value: 6.89e-55
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cpn10 | cd00320 | Chaperonin 10 Kd subunit (cpn10 or GroES); Cpn10 cooperates with chaperonin 60 (cpn60 or GroEL) ... |
2-94 | 8.08e-48 | |||
Chaperonin 10 Kd subunit (cpn10 or GroES); Cpn10 cooperates with chaperonin 60 (cpn60 or GroEL), an ATPase, to assist the folding and assembly of proteins and is found in eubacterial cytosol, as well as in the matrix of mitochondria and chloroplasts. It forms heptameric rings with a dome-like structure, forming a lid to the large cavity of the tetradecameric cpn60 cylinder and thereby tightly regulating release and binding of proteins to the cpn60 surface. Pssm-ID: 238197 Cd Length: 93 Bit Score: 147.27 E-value: 8.08e-48
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Cpn10 | pfam00166 | Chaperonin 10 Kd subunit; This family contains GroES and Gp31-like chaperonins. Gp31 is a ... |
2-94 | 6.22e-46 | |||
Chaperonin 10 Kd subunit; This family contains GroES and Gp31-like chaperonins. Gp31 is a functional co-chaperonin that is required for the folding and assembly of Gp23, a major capsid protein, during phage morphogenesis. Pssm-ID: 395114 Cd Length: 92 Bit Score: 142.36 E-value: 6.22e-46
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groES | PRK14533 | co-chaperonin GroES; Provisional |
1-91 | 2.50e-25 | |||
co-chaperonin GroES; Provisional Pssm-ID: 184730 Cd Length: 91 Bit Score: 90.31 E-value: 2.50e-25
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PTZ00414 | PTZ00414 | 10 kDa heat shock protein; Provisional |
3-94 | 1.15e-18 | |||
10 kDa heat shock protein; Provisional Pssm-ID: 173604 Cd Length: 100 Bit Score: 73.49 E-value: 1.15e-18
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Blast search parameters | ||||
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