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Conserved domains on  [gi|30687936|ref|NP_851045|]
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chaperonin 20 [Arabidopsis thaliana]

Protein Classification

co-chaperone GroES( domain architecture ID 10791922)

co-chaperone GroES (Cpn10) binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter

CATH:  1.10.560.10
Gene Ontology:  GO:0005524|GO:0140662
PubMed:  10049801|15944406|11340060
SCOP:  4000251

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
groES PRK00364
co-chaperonin GroES; Reviewed
 61-153 3.19e-38

co-chaperonin GroES; Reviewed


:

Pssm-ID: 178988 [Multi-domain]  Cd Length: 95  Bit Score: 128.70  E-value: 3.19e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687936   61 SIKPLGDRVLVKIKEAEEKTLGGILLPSTAQSKPQGGEVVAVGEGRTIGK-NKIDITVPTGAQIIYSKYAGTEVEFNDVK 139
Cdd:PRK00364   2 NLKPLGDRVLVKRLEEEEKTAGGIVLPDSAKEKPQEGEVVAVGPGRRLDNgERVPLDVKVGDKVLFGKYAGTEVKIDGEE 81

                         90
                 ....*....|....
gi 30687936  140 HLILKEDDIVGILE 153
Cdd:PRK00364  82 YLILRESDILAIVE 95
GroES COG0234
Co-chaperonin GroES (HSP10) [Posttranslational modification, protein turnover, chaperones];
160-252 2.97e-36

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


:

Pssm-ID: 440004  Cd Length: 95  Bit Score: 123.62  E-value: 2.97e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687936 160 LKPLNDRVFIKVAEAEEKTAGGLLLTETTKEKPSIGTVIAVGPGSLDEEGKITPLPVSTGSTVLYSKYAGNDFKgKDGSN 239
Cdd:COG0234   2 IKPLGDRVLVKRIEAEEKTAGGIVLPDTAKEKPQEGEVVAVGPGKLLDNGKRVPLDVKVGDKVLFGKYAGTEVK-IDGEE 80

                        90
                ....*....|...
gi 30687936 240 YIALRASDVMAIL 252
Cdd:COG0234  81 YLILRESDILAVV 93
 
Name Accession Description Interval E-value
groES PRK00364
co-chaperonin GroES; Reviewed
 61-153 3.19e-38

co-chaperonin GroES; Reviewed


Pssm-ID: 178988 [Multi-domain]  Cd Length: 95  Bit Score: 128.70  E-value: 3.19e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687936   61 SIKPLGDRVLVKIKEAEEKTLGGILLPSTAQSKPQGGEVVAVGEGRTIGK-NKIDITVPTGAQIIYSKYAGTEVEFNDVK 139
Cdd:PRK00364   2 NLKPLGDRVLVKRLEEEEKTAGGIVLPDSAKEKPQEGEVVAVGPGRRLDNgERVPLDVKVGDKVLFGKYAGTEVKIDGEE 81

                         90
                 ....*....|....
gi 30687936  140 HLILKEDDIVGILE 153
Cdd:PRK00364  82 YLILRESDILAIVE 95
GroES COG0234
Co-chaperonin GroES (HSP10) [Posttranslational modification, protein turnover, chaperones];
61-153 5.94e-38

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


Pssm-ID: 440004  Cd Length: 95  Bit Score: 128.24  E-value: 5.94e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687936  61 SIKPLGDRVLVKIKEAEEKTLGGILLPSTAQSKPQGGEVVAVGEGRTIGK-NKIDITVPTGAQIIYSKYAGTEVEFNDVK 139
Cdd:COG0234   1 KIKPLGDRVLVKRIEAEEKTAGGIVLPDTAKEKPQEGEVVAVGPGKLLDNgKRVPLDVKVGDKVLFGKYAGTEVKIDGEE 80

                        90
                ....*....|....
gi 30687936 140 HLILKEDDIVGILE 153
Cdd:COG0234  81 YLILRESDILAVVE 94
Cpn10 smart00883
Chaperonin 10 Kd subunit; The chaperonins are 'helper' molecules required for correct folding ...
 61-152 3.88e-37

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: 126.01  E-value: 3.88e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687936     61 SIKPLGDRVLVKIKEAEEKTLGGILLPSTAQSKPQGGEVVAVGEG-RTIGKNKIDITVPTGAQIIYSKYAGTEVEFNDVK 139
Cdd:smart00883   1 KIKPLGDRVLVKRIEEEEKTAGGIVIPDTAKEKPQEGEVVAVGPGkRLENGERVPLDVKVGDKVLFGKYAGTEVKLDGEE 80

                           90
                   ....*....|...
gi 30687936    140 HLILKEDDIVGIL 152
Cdd:smart00883  81 YLILRESDILAVI 93
GroES COG0234
Co-chaperonin GroES (HSP10) [Posttranslational modification, protein turnover, chaperones];
160-252 2.97e-36

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


Pssm-ID: 440004  Cd Length: 95  Bit Score: 123.62  E-value: 2.97e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687936 160 LKPLNDRVFIKVAEAEEKTAGGLLLTETTKEKPSIGTVIAVGPGSLDEEGKITPLPVSTGSTVLYSKYAGNDFKgKDGSN 239
Cdd:COG0234   2 IKPLGDRVLVKRIEAEEKTAGGIVLPDTAKEKPQEGEVVAVGPGKLLDNGKRVPLDVKVGDKVLFGKYAGTEVK-IDGEE 80

                        90
                ....*....|...
gi 30687936 240 YIALRASDVMAIL 252
Cdd:COG0234  81 YLILRESDILAVV 93
groES PRK00364
co-chaperonin GroES; Reviewed
 160-252 5.12e-36

co-chaperonin GroES; Reviewed


Pssm-ID: 178988 [Multi-domain]  Cd Length: 95  Bit Score: 123.30  E-value: 5.12e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687936  160 LKPLNDRVFIKVAEAEEKTAGGLLLTETTKEKPSIGTVIAVGPGSLDEEGKITPLPVSTGSTVLYSKYAGNDFKgKDGSN 239
Cdd:PRK00364   3 LKPLGDRVLVKRLEEEEKTAGGIVLPDSAKEKPQEGEVVAVGPGRRLDNGERVPLDVKVGDKVLFGKYAGTEVK-IDGEE 81

                         90
                 ....*....|...
gi 30687936  240 YIALRASDVMAIL 252
Cdd:PRK00364  82 YLILRESDILAIV 94
Cpn10 pfam00166
Chaperonin 10 Kd subunit; This family contains GroES and Gp31-like chaperonins. Gp31 is a ...
 61-152 5.04e-35

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: 120.41  E-value: 5.04e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687936    61 SIKPLGDRVLVKIKEAEEKTLGGILLPSTAQSKPQGGEVVAVGEGRTIGKNKIDITVPTGAQIIYSKYAGTEVEFNDVKH 140
Cdd:pfam00166   1 KIKPLGDRVLVKRVEEEEKTAGGIILPDSAKEKPQQGEVVAVGPGARNNGNDVPLEVKVGDKVLFPKYAGTEVKVDGKEY 80

                          90
                  ....*....|..
gi 30687936   141 LILKEDDIVGIL 152
Cdd:pfam00166  81 LILKESDILAVI 92
Cpn10 smart00883
Chaperonin 10 Kd subunit; The chaperonins are 'helper' molecules required for correct folding ...
 160-252 1.42e-34

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: 119.46  E-value: 1.42e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687936    160 LKPLNDRVFIKVAEAEEKTAGGLLLTETTKEKPSIGTVIAVGPGSLDEEGKITPLPVSTGSTVLYSKYAGNDFKGkDGSN 239
Cdd:smart00883   2 IKPLGDRVLVKRIEEEEKTAGGIVIPDTAKEKPQEGEVVAVGPGKRLENGERVPLDVKVGDKVLFGKYAGTEVKL-DGEE 80

                           90
                   ....*....|...
gi 30687936    240 YIALRASDVMAIL 252
Cdd:smart00883  81 YLILRESDILAVI 93
cpn10 cd00320
Chaperonin 10 Kd subunit (cpn10 or GroES); Cpn10 cooperates with chaperonin 60 (cpn60 or GroEL) ...
 61-152 3.48e-34

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: 118.38  E-value: 3.48e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687936  61 SIKPLGDRVLVKIKEAEEKTLGGILLPSTAQSKPQGGEVVAVGEGRTIGK-NKIDITVPTGAQIIYSKYAGTEVEFNDVK 139
Cdd:cd00320   1 KIKPLGDRVLVKRIEAEEKTKGGIILPDSAKEKPQEGKVVAVGPGRRNENgERVPLSVKVGDKVLFPKYAGTEVKLDGEE 80

                        90
                ....*....|...
gi 30687936 140 HLILKEDDIVGIL 152
Cdd:cd00320  81 YLILRESDILAVI 93
cpn10 cd00320
Chaperonin 10 Kd subunit (cpn10 or GroES); Cpn10 cooperates with chaperonin 60 (cpn60 or GroEL) ...
 160-252 3.53e-32

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: 113.37  E-value: 3.53e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687936 160 LKPLNDRVFIKVAEAEEKTAGGLLLTETTKEKPSIGTVIAVGPGSLDEEGKITPLPVSTGSTVLYSKYAGNDFKGkDGSN 239
Cdd:cd00320   2 IKPLGDRVLVKRIEAEEKTKGGIILPDSAKEKPQEGKVVAVGPGRRNENGERVPLSVKVGDKVLFPKYAGTEVKL-DGEE 80

                        90
                ....*....|...
gi 30687936 240 YIALRASDVMAIL 252
Cdd:cd00320  81 YLILRESDILAVI 93
Cpn10 pfam00166
Chaperonin 10 Kd subunit; This family contains GroES and Gp31-like chaperonins. Gp31 is a ...
 160-252 1.33e-28

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: 104.23  E-value: 1.33e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687936   160 LKPLNDRVFIKVAEAEEKTAGGLLLTETTKEKPSIGTVIAVGPGSLDeEGKITPLPVSTGSTVLYSKYAGNDFKgKDGSN 239
Cdd:pfam00166   2 IKPLGDRVLVKRVEEEEKTAGGIILPDSAKEKPQQGEVVAVGPGARN-NGNDVPLEVKVGDKVLFPKYAGTEVK-VDGKE 79

                          90
                  ....*....|...
gi 30687936   240 YIALRASDVMAIL 252
Cdd:pfam00166  80 YLILKESDILAVI 92
 
Name Accession Description Interval E-value
groES PRK00364
co-chaperonin GroES; Reviewed
 61-153 3.19e-38

co-chaperonin GroES; Reviewed


Pssm-ID: 178988 [Multi-domain]  Cd Length: 95  Bit Score: 128.70  E-value: 3.19e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687936   61 SIKPLGDRVLVKIKEAEEKTLGGILLPSTAQSKPQGGEVVAVGEGRTIGK-NKIDITVPTGAQIIYSKYAGTEVEFNDVK 139
Cdd:PRK00364   2 NLKPLGDRVLVKRLEEEEKTAGGIVLPDSAKEKPQEGEVVAVGPGRRLDNgERVPLDVKVGDKVLFGKYAGTEVKIDGEE 81

                         90
                 ....*....|....
gi 30687936  140 HLILKEDDIVGILE 153
Cdd:PRK00364  82 YLILRESDILAIVE 95
GroES COG0234
Co-chaperonin GroES (HSP10) [Posttranslational modification, protein turnover, chaperones];
61-153 5.94e-38

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


Pssm-ID: 440004  Cd Length: 95  Bit Score: 128.24  E-value: 5.94e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687936  61 SIKPLGDRVLVKIKEAEEKTLGGILLPSTAQSKPQGGEVVAVGEGRTIGK-NKIDITVPTGAQIIYSKYAGTEVEFNDVK 139
Cdd:COG0234   1 KIKPLGDRVLVKRIEAEEKTAGGIVLPDTAKEKPQEGEVVAVGPGKLLDNgKRVPLDVKVGDKVLFGKYAGTEVKIDGEE 80

                        90
                ....*....|....
gi 30687936 140 HLILKEDDIVGILE 153
Cdd:COG0234  81 YLILRESDILAVVE 94
Cpn10 smart00883
Chaperonin 10 Kd subunit; The chaperonins are 'helper' molecules required for correct folding ...
 61-152 3.88e-37

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: 126.01  E-value: 3.88e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687936     61 SIKPLGDRVLVKIKEAEEKTLGGILLPSTAQSKPQGGEVVAVGEG-RTIGKNKIDITVPTGAQIIYSKYAGTEVEFNDVK 139
Cdd:smart00883   1 KIKPLGDRVLVKRIEEEEKTAGGIVIPDTAKEKPQEGEVVAVGPGkRLENGERVPLDVKVGDKVLFGKYAGTEVKLDGEE 80

                           90
                   ....*....|...
gi 30687936    140 HLILKEDDIVGIL 152
Cdd:smart00883  81 YLILRESDILAVI 93
GroES COG0234
Co-chaperonin GroES (HSP10) [Posttranslational modification, protein turnover, chaperones];
160-252 2.97e-36

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


Pssm-ID: 440004  Cd Length: 95  Bit Score: 123.62  E-value: 2.97e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687936 160 LKPLNDRVFIKVAEAEEKTAGGLLLTETTKEKPSIGTVIAVGPGSLDEEGKITPLPVSTGSTVLYSKYAGNDFKgKDGSN 239
Cdd:COG0234   2 IKPLGDRVLVKRIEAEEKTAGGIVLPDTAKEKPQEGEVVAVGPGKLLDNGKRVPLDVKVGDKVLFGKYAGTEVK-IDGEE 80

                        90
                ....*....|...
gi 30687936 240 YIALRASDVMAIL 252
Cdd:COG0234  81 YLILRESDILAVV 93
groES PRK00364
co-chaperonin GroES; Reviewed
 160-252 5.12e-36

co-chaperonin GroES; Reviewed


Pssm-ID: 178988 [Multi-domain]  Cd Length: 95  Bit Score: 123.30  E-value: 5.12e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687936  160 LKPLNDRVFIKVAEAEEKTAGGLLLTETTKEKPSIGTVIAVGPGSLDEEGKITPLPVSTGSTVLYSKYAGNDFKgKDGSN 239
Cdd:PRK00364   3 LKPLGDRVLVKRLEEEEKTAGGIVLPDSAKEKPQEGEVVAVGPGRRLDNGERVPLDVKVGDKVLFGKYAGTEVK-IDGEE 81

                         90
                 ....*....|...
gi 30687936  240 YIALRASDVMAIL 252
Cdd:PRK00364  82 YLILRESDILAIV 94
Cpn10 pfam00166
Chaperonin 10 Kd subunit; This family contains GroES and Gp31-like chaperonins. Gp31 is a ...
 61-152 5.04e-35

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: 120.41  E-value: 5.04e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687936    61 SIKPLGDRVLVKIKEAEEKTLGGILLPSTAQSKPQGGEVVAVGEGRTIGKNKIDITVPTGAQIIYSKYAGTEVEFNDVKH 140
Cdd:pfam00166   1 KIKPLGDRVLVKRVEEEEKTAGGIILPDSAKEKPQQGEVVAVGPGARNNGNDVPLEVKVGDKVLFPKYAGTEVKVDGKEY 80

                          90
                  ....*....|..
gi 30687936   141 LILKEDDIVGIL 152
Cdd:pfam00166  81 LILKESDILAVI 92
Cpn10 smart00883
Chaperonin 10 Kd subunit; The chaperonins are 'helper' molecules required for correct folding ...
 160-252 1.42e-34

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: 119.46  E-value: 1.42e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687936    160 LKPLNDRVFIKVAEAEEKTAGGLLLTETTKEKPSIGTVIAVGPGSLDEEGKITPLPVSTGSTVLYSKYAGNDFKGkDGSN 239
Cdd:smart00883   2 IKPLGDRVLVKRIEEEEKTAGGIVIPDTAKEKPQEGEVVAVGPGKRLENGERVPLDVKVGDKVLFGKYAGTEVKL-DGEE 80

                           90
                   ....*....|...
gi 30687936    240 YIALRASDVMAIL 252
Cdd:smart00883  81 YLILRESDILAVI 93
cpn10 cd00320
Chaperonin 10 Kd subunit (cpn10 or GroES); Cpn10 cooperates with chaperonin 60 (cpn60 or GroEL) ...
 61-152 3.48e-34

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: 118.38  E-value: 3.48e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687936  61 SIKPLGDRVLVKIKEAEEKTLGGILLPSTAQSKPQGGEVVAVGEGRTIGK-NKIDITVPTGAQIIYSKYAGTEVEFNDVK 139
Cdd:cd00320   1 KIKPLGDRVLVKRIEAEEKTKGGIILPDSAKEKPQEGKVVAVGPGRRNENgERVPLSVKVGDKVLFPKYAGTEVKLDGEE 80

                        90
                ....*....|...
gi 30687936 140 HLILKEDDIVGIL 152
Cdd:cd00320  81 YLILRESDILAVI 93
cpn10 cd00320
Chaperonin 10 Kd subunit (cpn10 or GroES); Cpn10 cooperates with chaperonin 60 (cpn60 or GroEL) ...
 160-252 3.53e-32

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: 113.37  E-value: 3.53e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687936 160 LKPLNDRVFIKVAEAEEKTAGGLLLTETTKEKPSIGTVIAVGPGSLDEEGKITPLPVSTGSTVLYSKYAGNDFKGkDGSN 239
Cdd:cd00320   2 IKPLGDRVLVKRIEAEEKTKGGIILPDSAKEKPQEGKVVAVGPGRRNENGERVPLSVKVGDKVLFPKYAGTEVKL-DGEE 80

                        90
                ....*....|...
gi 30687936 240 YIALRASDVMAIL 252
Cdd:cd00320  81 YLILRESDILAVI 93
Cpn10 pfam00166
Chaperonin 10 Kd subunit; This family contains GroES and Gp31-like chaperonins. Gp31 is a ...
 160-252 1.33e-28

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: 104.23  E-value: 1.33e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687936   160 LKPLNDRVFIKVAEAEEKTAGGLLLTETTKEKPSIGTVIAVGPGSLDeEGKITPLPVSTGSTVLYSKYAGNDFKgKDGSN 239
Cdd:pfam00166   2 IKPLGDRVLVKRVEEEEKTAGGIILPDSAKEKPQQGEVVAVGPGARN-NGNDVPLEVKVGDKVLFPKYAGTEVK-VDGKE 79

                          90
                  ....*....|...
gi 30687936   240 YIALRASDVMAIL 252
Cdd:pfam00166  80 YLILKESDILAVI 92
groES PRK14533
co-chaperonin GroES; Provisional
 62-153 2.97e-18

co-chaperonin GroES; Provisional


Pssm-ID: 184730  Cd Length: 91  Bit Score: 77.21  E-value: 2.97e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687936   62 IKPLGDRVLVKIKEAEEKTLGGILLPSTAQSKPQGGEVVAVGEgrtiGKNKIDITVPTGAQIIYSKYAGTEVEFNDVKHL 141
Cdd:PRK14533   3 VIPLGERLLIKPIKEEKKTEGGIVLPDSAKEKPMKAEVVAVGK----LDDEEDFDIKVGDKVIFSKYAGTEIKIDDEDYI 78

                         90
                 ....*....|..
gi 30687936  142 ILKEDDIVGILE 153
Cdd:PRK14533  79 IIDVNDILAKIE 90
groES PRK14533
co-chaperonin GroES; Provisional
 160-250 2.51e-11

co-chaperonin GroES; Provisional


Pssm-ID: 184730  Cd Length: 91  Bit Score: 58.34  E-value: 2.51e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687936  160 LKPLNDRVFIKVAEAEEKTAGGLLLTETTKEKPSIGTVIAVgpGSLDEEGKITplpVSTGSTVLYSKYAGNDFKGKDgSN 239
Cdd:PRK14533   3 VIPLGERLLIKPIKEEKKTEGGIVLPDSAKEKPMKAEVVAV--GKLDDEEDFD---IKVGDKVIFSKYAGTEIKIDD-ED 76

                         90
                 ....*....|.
gi 30687936  240 YIALRASDVMA 250
Cdd:PRK14533  77 YIIIDVNDILA 87
PTZ00414 PTZ00414
10 kDa heat shock protein; Provisional
 54-153 8.39e-09

10 kDa heat shock protein; Provisional


Pssm-ID: 173604  Cd Length: 100  Bit Score: 51.92  E-value: 8.39e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687936   54 VVAPKYTSIKPLGDRVLVKIKEAEEKTLGGILLPSTAQSKPQGGEVVAVGEGRTigknKIDITVPTGAQIIYSKYAGTEV 133
Cdd:PTZ00414   4 FTVPALKKLQPLGQRVLVKRTLAAKQTKAGVLIPEQVAGKVNEGTVVAVAAATK----DWTPTVKVGDTVLLPEFGGSSV 79

                         90       100
                 ....*....|....*....|
gi 30687936  134 EFNDVKHLILKEDDIVGILE 153
Cdd:PTZ00414  80 KVEGEEFFLYNEDSLLGVLQ 99
PTZ00414 PTZ00414
10 kDa heat shock protein; Provisional
 157-233 1.37e-07

10 kDa heat shock protein; Provisional


Pssm-ID: 173604  Cd Length: 100  Bit Score: 48.45  E-value: 1.37e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30687936  157 IKDLKPLNDRVFIKVAEAEEKTAGGLLLTETTKEKPSIGTVIAVGPGSLDeegkITPlPVSTGSTVLYSKYAGNDFK 233
Cdd:PTZ00414   9 LKKLQPLGQRVLVKRTLAAKQTKAGVLIPEQVAGKVNEGTVVAVAAATKD----WTP-TVKVGDTVLLPEFGGSSVK 80
 
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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