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Conserved domains on  [gi|815720298|ref|WP_046451837|]
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MULTISPECIES: co-chaperone GroES family protein [Parabacteroides]

Protein Classification

GroES family protein( domain architecture ID 10785100)

GroES family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GroES COG0234
Co-chaperonin GroES (HSP10) [Posttranslational modification, protein turnover, chaperones];
12-122 1.32e-29

Co-chaperonin GroES (HSP10) [Posttranslational modification, protein turnover, chaperones];


:

Pssm-ID: 440004  Cd Length: 95  Bit Score: 102.43  E-value: 1.32e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815720298  12 KFLMVGDKVLIKPKNPQSQTKSGLYLPPTVQqEKIQSGYIIKVGPGfplpsqseehevwekKTEGEVHYLPLQAHEGDLA 91
Cdd:COG0234    1 KIKPLGDRVLVKRIEAEEKTAGGIVLPDTAK-EKPQEGEVVAVGPG---------------KLLDNGKRVPLDVKVGDKV 64

                         90       100       110
                 ....*....|....*....|....*....|.
gi 815720298  92 VFLQNAAYEINFNEEKFLIVPHSAILMLVRD 122
Cdd:COG0234   65 LFGKYAGTEVKIDGEEYLILRESDILAVVEE 95
 
Name Accession Description Interval E-value
GroES COG0234
Co-chaperonin GroES (HSP10) [Posttranslational modification, protein turnover, chaperones];
12-122 1.32e-29

Co-chaperonin GroES (HSP10) [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440004  Cd Length: 95  Bit Score: 102.43  E-value: 1.32e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815720298  12 KFLMVGDKVLIKPKNPQSQTKSGLYLPPTVQqEKIQSGYIIKVGPGfplpsqseehevwekKTEGEVHYLPLQAHEGDLA 91
Cdd:COG0234    1 KIKPLGDRVLVKRIEAEEKTAGGIVLPDTAK-EKPQEGEVVAVGPG---------------KLLDNGKRVPLDVKVGDKV 64

                         90       100       110
                 ....*....|....*....|....*....|.
gi 815720298  92 VFLQNAAYEINFNEEKFLIVPHSAILMLVRD 122
Cdd:COG0234   65 LFGKYAGTEVKIDGEEYLILRESDILAVVEE 95
cpn10 cd00320
Chaperonin 10 Kd subunit (cpn10 or GroES); Cpn10 cooperates with chaperonin 60 (cpn60 or GroEL) ...
 12-117 5.76e-17

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: 70.23  E-value: 5.76e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815720298  12 KFLMVGDKVLIKPKNPQSQTKSGLYLPPTVqQEKIQSGYIIKVGPGfplpsqseehevwekKTEGEVHYLPLQAHEGDLA 91
Cdd:cd00320    1 KIKPLGDRVLVKRIEAEEKTKGGIILPDSA-KEKPQEGKVVAVGPG---------------RRNENGERVPLSVKVGDKV 64

                         90       100
                 ....*....|....*....|....*.
gi 815720298  92 VFLQNAAYEINFNEEKFLIVPHSAIL 117
Cdd:cd00320   65 LFPKYAGTEVKLDGEEYLILRESDIL 90
Cpn10 smart00883
Chaperonin 10 Kd subunit; The chaperonins are 'helper' molecules required for correct folding ...
 12-117 1.82e-12

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: 58.60  E-value: 1.82e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815720298    12 KFLMVGDKVLIKPKNPQSQTKSGLYLPPTVQqEKIQSGYIIKVGPGfplpsqseehevweKKTE-GEVhyLPLQAHEGDL 90
Cdd:smart00883   1 KIKPLGDRVLVKRIEEEEKTAGGIVIPDTAK-EKPQEGEVVAVGPG--------------KRLEnGER--VPLDVKVGDK 63

                           90       100
                   ....*....|....*....|....*..
gi 815720298    91 AVFLQNAAYEINFNEEKFLIVPHSAIL 117
Cdd:smart00883  64 VLFGKYAGTEVKLDGEEYLILRESDIL 90
Cpn10 pfam00166
Chaperonin 10 Kd subunit; This family contains GroES and Gp31-like chaperonins. Gp31 is a ...
 12-117 2.78e-12

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: 58.00  E-value: 2.78e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815720298   12 KFLMVGDKVLIKPKNPQSQTKSGLYLPPTvQQEKIQSGYIIKVGPGfplpsqseehevweKKTEGEVhyLPLQAHEGDLA 91
Cdd:pfam00166   1 KIKPLGDRVLVKRVEEEEKTAGGIILPDS-AKEKPQQGEVVAVGPG--------------ARNNGND--VPLEVKVGDKV 63

                          90       100
                  ....*....|....*....|....*.
gi 815720298   92 VFLQNAAYEINFNEEKFLIVPHSAIL 117
Cdd:pfam00166  64 LFPKYAGTEVKVDGKEYLILKESDIL 89
groES PRK00364
co-chaperonin GroES; Reviewed
 12-117 9.80e-11

co-chaperonin GroES; Reviewed


Pssm-ID: 178988 [Multi-domain]  Cd Length: 95  Bit Score: 54.35  E-value: 9.80e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815720298  12 KFLMVGDKVLIKPKNPQSQTKSGLYLPPTVqQEKIQSGYIIKVGPGfplpsqseehevweKKTE-GEVhyLPLQAHEGDL 90
Cdd:PRK00364   2 NLKPLGDRVLVKRLEEEEKTAGGIVLPDSA-KEKPQEGEVVAVGPG--------------RRLDnGER--VPLDVKVGDK 64

                         90       100
                 ....*....|....*....|....*..
gi 815720298  91 AVFLQNAAYEINFNEEKFLIVPHSAIL 117
Cdd:PRK00364  65 VLFGKYAGTEVKIDGEEYLILRESDIL 91
 
Name Accession Description Interval E-value
GroES COG0234
Co-chaperonin GroES (HSP10) [Posttranslational modification, protein turnover, chaperones];
12-122 1.32e-29

Co-chaperonin GroES (HSP10) [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440004  Cd Length: 95  Bit Score: 102.43  E-value: 1.32e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815720298  12 KFLMVGDKVLIKPKNPQSQTKSGLYLPPTVQqEKIQSGYIIKVGPGfplpsqseehevwekKTEGEVHYLPLQAHEGDLA 91
Cdd:COG0234    1 KIKPLGDRVLVKRIEAEEKTAGGIVLPDTAK-EKPQEGEVVAVGPG---------------KLLDNGKRVPLDVKVGDKV 64

                         90       100       110
                 ....*....|....*....|....*....|.
gi 815720298  92 VFLQNAAYEINFNEEKFLIVPHSAILMLVRD 122
Cdd:COG0234   65 LFGKYAGTEVKIDGEEYLILRESDILAVVEE 95
cpn10 cd00320
Chaperonin 10 Kd subunit (cpn10 or GroES); Cpn10 cooperates with chaperonin 60 (cpn60 or GroEL) ...
 12-117 5.76e-17

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: 70.23  E-value: 5.76e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815720298  12 KFLMVGDKVLIKPKNPQSQTKSGLYLPPTVqQEKIQSGYIIKVGPGfplpsqseehevwekKTEGEVHYLPLQAHEGDLA 91
Cdd:cd00320    1 KIKPLGDRVLVKRIEAEEKTKGGIILPDSA-KEKPQEGKVVAVGPG---------------RRNENGERVPLSVKVGDKV 64

                         90       100
                 ....*....|....*....|....*.
gi 815720298  92 VFLQNAAYEINFNEEKFLIVPHSAIL 117
Cdd:cd00320   65 LFPKYAGTEVKLDGEEYLILRESDIL 90
Cpn10 smart00883
Chaperonin 10 Kd subunit; The chaperonins are 'helper' molecules required for correct folding ...
 12-117 1.82e-12

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: 58.60  E-value: 1.82e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815720298    12 KFLMVGDKVLIKPKNPQSQTKSGLYLPPTVQqEKIQSGYIIKVGPGfplpsqseehevweKKTE-GEVhyLPLQAHEGDL 90
Cdd:smart00883   1 KIKPLGDRVLVKRIEEEEKTAGGIVIPDTAK-EKPQEGEVVAVGPG--------------KRLEnGER--VPLDVKVGDK 63

                           90       100
                   ....*....|....*....|....*..
gi 815720298    91 AVFLQNAAYEINFNEEKFLIVPHSAIL 117
Cdd:smart00883  64 VLFGKYAGTEVKLDGEEYLILRESDIL 90
Cpn10 pfam00166
Chaperonin 10 Kd subunit; This family contains GroES and Gp31-like chaperonins. Gp31 is a ...
 12-117 2.78e-12

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: 58.00  E-value: 2.78e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815720298   12 KFLMVGDKVLIKPKNPQSQTKSGLYLPPTvQQEKIQSGYIIKVGPGfplpsqseehevweKKTEGEVhyLPLQAHEGDLA 91
Cdd:pfam00166   1 KIKPLGDRVLVKRVEEEEKTAGGIILPDS-AKEKPQQGEVVAVGPG--------------ARNNGND--VPLEVKVGDKV 63

                          90       100
                  ....*....|....*....|....*.
gi 815720298   92 VFLQNAAYEINFNEEKFLIVPHSAIL 117
Cdd:pfam00166  64 LFPKYAGTEVKVDGKEYLILKESDIL 89
groES PRK00364
co-chaperonin GroES; Reviewed
 12-117 9.80e-11

co-chaperonin GroES; Reviewed


Pssm-ID: 178988 [Multi-domain]  Cd Length: 95  Bit Score: 54.35  E-value: 9.80e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815720298  12 KFLMVGDKVLIKPKNPQSQTKSGLYLPPTVqQEKIQSGYIIKVGPGfplpsqseehevweKKTE-GEVhyLPLQAHEGDL 90
Cdd:PRK00364   2 NLKPLGDRVLVKRLEEEEKTAGGIVLPDSA-KEKPQEGEVVAVGPG--------------RRLDnGER--VPLDVKVGDK 64

                         90       100
                 ....*....|....*....|....*..
gi 815720298  91 AVFLQNAAYEINFNEEKFLIVPHSAIL 117
Cdd:PRK00364  65 VLFGKYAGTEVKIDGEEYLILRESDIL 91
 
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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