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Conserved domains on  [gi|63086916|emb|CAH04520|]
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Cpn20 protein, partial [Toxoplasma gondii]

Protein Classification

co-chaperone GroES family protein( domain architecture ID 10085313)

co-chaperone GroES family protein such as human 10 kDa heat shock protein (Hsp10, Cpn10) that binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
cpn10 cd00320
Chaperonin 10 Kd subunit (cpn10 or GroES); Cpn10 cooperates with chaperonin 60 (cpn60 or GroEL) ...
 11-104 2.07e-26

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: 97.19  E-value: 2.07e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63086916  11 PIKPLRGMVLLERREAVEKSAGGVYLPIESKAKQVIAKVIEVGPGEVNrETGARIPVDVAIGDWTIISRHTYESFKYNGK 90
Cdd:cd00320   1 KIKPLGDRVLVKRIEAEEKTKGGIILPDSAKEKPQEGKVVAVGPGRRN-ENGERVPLSVKVGDKVLFPKYAGTEVKLDGE 79

                        90
                ....*....|....
gi 63086916  91 DCVLVEARDIIAKV 104
Cdd:cd00320  80 EYLILRESDILAVI 93
cpn10 cd00320
Chaperonin 10 Kd subunit (cpn10 or GroES); Cpn10 cooperates with chaperonin 60 (cpn60 or GroEL) ...
 118-216 4.77e-25

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: 93.73  E-value: 4.77e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63086916 118 ILPLGDTILVKLVKQAQRTASGLYLQPTGSERdrgqgVKRAQVVAVGLGRYNRNGERVPNDVVPGDEVLFPAYSQdePEM 197
Cdd:cd00320   2 IKPLGDRVLVKRIEAEEKTKGGIILPDSAKEK-----PQEGKVVAVGPGRRNENGERVPLSVKVGDKVLFPKYAG--TEV 74

                        90
                ....*....|....*....
gi 63086916 198 KYGGESYAFVRAADLLAKW 216
Cdd:cd00320  75 KLDGEEYLILRESDILAVI 93
 
Name Accession Description Interval E-value
cpn10 cd00320
Chaperonin 10 Kd subunit (cpn10 or GroES); Cpn10 cooperates with chaperonin 60 (cpn60 or GroEL) ...
 11-104 2.07e-26

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: 97.19  E-value: 2.07e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63086916  11 PIKPLRGMVLLERREAVEKSAGGVYLPIESKAKQVIAKVIEVGPGEVNrETGARIPVDVAIGDWTIISRHTYESFKYNGK 90
Cdd:cd00320   1 KIKPLGDRVLVKRIEAEEKTKGGIILPDSAKEKPQEGKVVAVGPGRRN-ENGERVPLSVKVGDKVLFPKYAGTEVKLDGE 79

                        90
                ....*....|....
gi 63086916  91 DCVLVEARDIIAKV 104
Cdd:cd00320  80 EYLILRESDILAVI 93
cpn10 cd00320
Chaperonin 10 Kd subunit (cpn10 or GroES); Cpn10 cooperates with chaperonin 60 (cpn60 or GroEL) ...
 118-216 4.77e-25

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: 93.73  E-value: 4.77e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63086916 118 ILPLGDTILVKLVKQAQRTASGLYLQPTGSERdrgqgVKRAQVVAVGLGRYNRNGERVPNDVVPGDEVLFPAYSQdePEM 197
Cdd:cd00320   2 IKPLGDRVLVKRIEAEEKTKGGIILPDSAKEK-----PQEGKVVAVGPGRRNENGERVPLSVKVGDKVLFPKYAG--TEV 74

                        90
                ....*....|....*....
gi 63086916 198 KYGGESYAFVRAADLLAKW 216
Cdd:cd00320  75 KLDGEEYLILRESDILAVI 93
Cpn10 smart00883
Chaperonin 10 Kd subunit; The chaperonins are 'helper' molecules required for correct folding ...
 118-215 3.19e-21

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: 84.02  E-value: 3.19e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63086916    118 ILPLGDTILVKLVKQAQRTASGLYLQPTGSERdrgqgVKRAQVVAVGLGRYNRNGERVPNDVVPGDEVLFPAYSQDepEM 197
Cdd:smart00883   2 IKPLGDRVLVKRIEEEEKTAGGIVIPDTAKEK-----PQEGEVVAVGPGKRLENGERVPLDVKVGDKVLFGKYAGT--EV 74

                           90
                   ....*....|....*...
gi 63086916    198 KYGGESYAFVRAADLLAK 215
Cdd:smart00883  75 KLDGEEYLILRESDILAV 92
GroES COG0234
Co-chaperonin GroES (HSP10) [Posttranslational modification, protein turnover, chaperones];
118-215 1.45e-20

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


Pssm-ID: 440004  Cd Length: 95  Bit Score: 82.40  E-value: 1.45e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63086916 118 ILPLGDTILVKLVKQAQRTASGLYLQPTGSERdrgqgVKRAQVVAVGLGRYNRNGERVPNDVVPGDEVLFPAYSQDepEM 197
Cdd:COG0234   2 IKPLGDRVLVKRIEAEEKTAGGIVLPDTAKEK-----PQEGEVVAVGPGKLLDNGKRVPLDVKVGDKVLFGKYAGT--EV 74

                        90
                ....*....|....*...
gi 63086916 198 KYGGESYAFVRAADLLAK 215
Cdd:COG0234  75 KIDGEEYLILRESDILAV 92
Cpn10 smart00883
Chaperonin 10 Kd subunit; The chaperonins are 'helper' molecules required for correct folding ...
 11-104 4.60e-20

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: 80.94  E-value: 4.60e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63086916     11 PIKPLRGMVLLERREAVEKSAGGVYLPIESKAKQVIAKVIEVGPGEVNrETGARIPVDVAIGDWTIISRHTYESFKYNGK 90
Cdd:smart00883   1 KIKPLGDRVLVKRIEEEEKTAGGIVIPDTAKEKPQEGEVVAVGPGKRL-ENGERVPLDVKVGDKVLFGKYAGTEVKLDGE 79

                           90
                   ....*....|....
gi 63086916     91 DCVLVEARDIIAKV 104
Cdd:smart00883  80 EYLILRESDILAVI 93
groES PRK00364
co-chaperonin GroES; Reviewed
 120-214 3.32e-19

co-chaperonin GroES; Reviewed


Pssm-ID: 178988 [Multi-domain]  Cd Length: 95  Bit Score: 78.62  E-value: 3.32e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63086916  120 PLGDTILVKLVKQAQRTASGLYLQPTGSERDrgqgvKRAQVVAVGLGRYNRNGERVPNDVVPGDEVLFPAYSQDepEMKY 199
Cdd:PRK00364   5 PLGDRVLVKRLEEEEKTAGGIVLPDSAKEKP-----QEGEVVAVGPGRRLDNGERVPLDVKVGDKVLFGKYAGT--EVKI 77

                         90
                 ....*....|....*
gi 63086916  200 GGESYAFVRAADLLA 214
Cdd:PRK00364  78 DGEEYLILRESDILA 92
groES PRK00364
co-chaperonin GroES; Reviewed
 12-104 4.34e-18

co-chaperonin GroES; Reviewed


Pssm-ID: 178988 [Multi-domain]  Cd Length: 95  Bit Score: 75.92  E-value: 4.34e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63086916   12 IKPLRGMVLLERREAVEKSAGGVYLPIESKAKQVIAKVIEVGPGEVNrETGARIPVDVAIGDWTIISRHTYESFKYNGKD 91
Cdd:PRK00364   3 LKPLGDRVLVKRLEEEEKTAGGIVLPDSAKEKPQEGEVVAVGPGRRL-DNGERVPLDVKVGDKVLFGKYAGTEVKIDGEE 81

                         90
                 ....*....|...
gi 63086916   92 CVLVEARDIIAKV 104
Cdd:PRK00364  82 YLILRESDILAIV 94
Cpn10 pfam00166
Chaperonin 10 Kd subunit; This family contains GroES and Gp31-like chaperonins. Gp31 is a ...
 11-104 6.95e-18

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: 75.34  E-value: 6.95e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63086916    11 PIKPLRGMVLLERREAVEKSAGGVYLPIESKAKQVIAKVIEVGPGevNRETGARIPVDVAIGDWTIISRHTYESFKYNGK 90
Cdd:pfam00166   1 KIKPLGDRVLVKRVEEEEKTAGGIILPDSAKEKPQQGEVVAVGPG--ARNNGNDVPLEVKVGDKVLFPKYAGTEVKVDGK 78

                          90
                  ....*....|....
gi 63086916    91 DCVLVEARDIIAKV 104
Cdd:pfam00166  79 EYLILKESDILAVI 92
GroES COG0234
Co-chaperonin GroES (HSP10) [Posttranslational modification, protein turnover, chaperones];
12-104 7.73e-18

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


Pssm-ID: 440004  Cd Length: 95  Bit Score: 75.08  E-value: 7.73e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63086916  12 IKPLRGMVLLERREAVEKSAGGVYLPIESKAKQVIAKVIEVGPGEVNrETGARIPVDVAIGDWTIISRHTYESFKYNGKD 91
Cdd:COG0234   2 IKPLGDRVLVKRIEAEEKTAGGIVLPDTAKEKPQEGEVVAVGPGKLL-DNGKRVPLDVKVGDKVLFGKYAGTEVKIDGEE 80

                        90
                ....*....|...
gi 63086916  92 CVLVEARDIIAKV 104
Cdd:COG0234  81 YLILRESDILAVV 93
Cpn10 pfam00166
Chaperonin 10 Kd subunit; This family contains GroES and Gp31-like chaperonins. Gp31 is a ...
 118-215 6.17e-16

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: 69.95  E-value: 6.17e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63086916   118 ILPLGDTILVKLVKQAQRTASGLYLQPTGSERdrgqgVKRAQVVAVGLGRYNrNGERVPNDVVPGDEVLFPAYSQDepEM 197
Cdd:pfam00166   2 IKPLGDRVLVKRVEEEEKTAGGIILPDSAKEK-----PQQGEVVAVGPGARN-NGNDVPLEVKVGDKVLFPKYAGT--EV 73

                          90
                  ....*....|....*...
gi 63086916   198 KYGGESYAFVRAADLLAK 215
Cdd:pfam00166  74 KVDGKEYLILKESDILAV 91
 
Name Accession Description Interval E-value
cpn10 cd00320
Chaperonin 10 Kd subunit (cpn10 or GroES); Cpn10 cooperates with chaperonin 60 (cpn60 or GroEL) ...
 11-104 2.07e-26

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: 97.19  E-value: 2.07e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63086916  11 PIKPLRGMVLLERREAVEKSAGGVYLPIESKAKQVIAKVIEVGPGEVNrETGARIPVDVAIGDWTIISRHTYESFKYNGK 90
Cdd:cd00320   1 KIKPLGDRVLVKRIEAEEKTKGGIILPDSAKEKPQEGKVVAVGPGRRN-ENGERVPLSVKVGDKVLFPKYAGTEVKLDGE 79

                        90
                ....*....|....
gi 63086916  91 DCVLVEARDIIAKV 104
Cdd:cd00320  80 EYLILRESDILAVI 93
cpn10 cd00320
Chaperonin 10 Kd subunit (cpn10 or GroES); Cpn10 cooperates with chaperonin 60 (cpn60 or GroEL) ...
 118-216 4.77e-25

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: 93.73  E-value: 4.77e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63086916 118 ILPLGDTILVKLVKQAQRTASGLYLQPTGSERdrgqgVKRAQVVAVGLGRYNRNGERVPNDVVPGDEVLFPAYSQdePEM 197
Cdd:cd00320   2 IKPLGDRVLVKRIEAEEKTKGGIILPDSAKEK-----PQEGKVVAVGPGRRNENGERVPLSVKVGDKVLFPKYAG--TEV 74

                        90
                ....*....|....*....
gi 63086916 198 KYGGESYAFVRAADLLAKW 216
Cdd:cd00320  75 KLDGEEYLILRESDILAVI 93
Cpn10 smart00883
Chaperonin 10 Kd subunit; The chaperonins are 'helper' molecules required for correct folding ...
 118-215 3.19e-21

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: 84.02  E-value: 3.19e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63086916    118 ILPLGDTILVKLVKQAQRTASGLYLQPTGSERdrgqgVKRAQVVAVGLGRYNRNGERVPNDVVPGDEVLFPAYSQDepEM 197
Cdd:smart00883   2 IKPLGDRVLVKRIEEEEKTAGGIVIPDTAKEK-----PQEGEVVAVGPGKRLENGERVPLDVKVGDKVLFGKYAGT--EV 74

                           90
                   ....*....|....*...
gi 63086916    198 KYGGESYAFVRAADLLAK 215
Cdd:smart00883  75 KLDGEEYLILRESDILAV 92
GroES COG0234
Co-chaperonin GroES (HSP10) [Posttranslational modification, protein turnover, chaperones];
118-215 1.45e-20

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


Pssm-ID: 440004  Cd Length: 95  Bit Score: 82.40  E-value: 1.45e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63086916 118 ILPLGDTILVKLVKQAQRTASGLYLQPTGSERdrgqgVKRAQVVAVGLGRYNRNGERVPNDVVPGDEVLFPAYSQDepEM 197
Cdd:COG0234   2 IKPLGDRVLVKRIEAEEKTAGGIVLPDTAKEK-----PQEGEVVAVGPGKLLDNGKRVPLDVKVGDKVLFGKYAGT--EV 74

                        90
                ....*....|....*...
gi 63086916 198 KYGGESYAFVRAADLLAK 215
Cdd:COG0234  75 KIDGEEYLILRESDILAV 92
Cpn10 smart00883
Chaperonin 10 Kd subunit; The chaperonins are 'helper' molecules required for correct folding ...
 11-104 4.60e-20

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: 80.94  E-value: 4.60e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63086916     11 PIKPLRGMVLLERREAVEKSAGGVYLPIESKAKQVIAKVIEVGPGEVNrETGARIPVDVAIGDWTIISRHTYESFKYNGK 90
Cdd:smart00883   1 KIKPLGDRVLVKRIEEEEKTAGGIVIPDTAKEKPQEGEVVAVGPGKRL-ENGERVPLDVKVGDKVLFGKYAGTEVKLDGE 79

                           90
                   ....*....|....
gi 63086916     91 DCVLVEARDIIAKV 104
Cdd:smart00883  80 EYLILRESDILAVI 93
groES PRK00364
co-chaperonin GroES; Reviewed
 120-214 3.32e-19

co-chaperonin GroES; Reviewed


Pssm-ID: 178988 [Multi-domain]  Cd Length: 95  Bit Score: 78.62  E-value: 3.32e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63086916  120 PLGDTILVKLVKQAQRTASGLYLQPTGSERDrgqgvKRAQVVAVGLGRYNRNGERVPNDVVPGDEVLFPAYSQDepEMKY 199
Cdd:PRK00364   5 PLGDRVLVKRLEEEEKTAGGIVLPDSAKEKP-----QEGEVVAVGPGRRLDNGERVPLDVKVGDKVLFGKYAGT--EVKI 77

                         90
                 ....*....|....*
gi 63086916  200 GGESYAFVRAADLLA 214
Cdd:PRK00364  78 DGEEYLILRESDILA 92
groES PRK00364
co-chaperonin GroES; Reviewed
 12-104 4.34e-18

co-chaperonin GroES; Reviewed


Pssm-ID: 178988 [Multi-domain]  Cd Length: 95  Bit Score: 75.92  E-value: 4.34e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63086916   12 IKPLRGMVLLERREAVEKSAGGVYLPIESKAKQVIAKVIEVGPGEVNrETGARIPVDVAIGDWTIISRHTYESFKYNGKD 91
Cdd:PRK00364   3 LKPLGDRVLVKRLEEEEKTAGGIVLPDSAKEKPQEGEVVAVGPGRRL-DNGERVPLDVKVGDKVLFGKYAGTEVKIDGEE 81

                         90
                 ....*....|...
gi 63086916   92 CVLVEARDIIAKV 104
Cdd:PRK00364  82 YLILRESDILAIV 94
Cpn10 pfam00166
Chaperonin 10 Kd subunit; This family contains GroES and Gp31-like chaperonins. Gp31 is a ...
 11-104 6.95e-18

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: 75.34  E-value: 6.95e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63086916    11 PIKPLRGMVLLERREAVEKSAGGVYLPIESKAKQVIAKVIEVGPGevNRETGARIPVDVAIGDWTIISRHTYESFKYNGK 90
Cdd:pfam00166   1 KIKPLGDRVLVKRVEEEEKTAGGIILPDSAKEKPQQGEVVAVGPG--ARNNGNDVPLEVKVGDKVLFPKYAGTEVKVDGK 78

                          90
                  ....*....|....
gi 63086916    91 DCVLVEARDIIAKV 104
Cdd:pfam00166  79 EYLILKESDILAVI 92
GroES COG0234
Co-chaperonin GroES (HSP10) [Posttranslational modification, protein turnover, chaperones];
12-104 7.73e-18

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


Pssm-ID: 440004  Cd Length: 95  Bit Score: 75.08  E-value: 7.73e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63086916  12 IKPLRGMVLLERREAVEKSAGGVYLPIESKAKQVIAKVIEVGPGEVNrETGARIPVDVAIGDWTIISRHTYESFKYNGKD 91
Cdd:COG0234   2 IKPLGDRVLVKRIEAEEKTAGGIVLPDTAKEKPQEGEVVAVGPGKLL-DNGKRVPLDVKVGDKVLFGKYAGTEVKIDGEE 80

                        90
                ....*....|...
gi 63086916  92 CVLVEARDIIAKV 104
Cdd:COG0234  81 YLILRESDILAVV 93
Cpn10 pfam00166
Chaperonin 10 Kd subunit; This family contains GroES and Gp31-like chaperonins. Gp31 is a ...
 118-215 6.17e-16

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: 69.95  E-value: 6.17e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63086916   118 ILPLGDTILVKLVKQAQRTASGLYLQPTGSERdrgqgVKRAQVVAVGLGRYNrNGERVPNDVVPGDEVLFPAYSQDepEM 197
Cdd:pfam00166   2 IKPLGDRVLVKRVEEEEKTAGGIILPDSAKEK-----PQQGEVVAVGPGARN-NGNDVPLEVKVGDKVLFPKYAGT--EV 73

                          90
                  ....*....|....*...
gi 63086916   198 KYGGESYAFVRAADLLAK 215
Cdd:pfam00166  74 KVDGKEYLILKESDILAV 91
groES PRK14533
co-chaperonin GroES; Provisional
 12-105 3.46e-07

co-chaperonin GroES; Provisional


Pssm-ID: 184730  Cd Length: 91  Bit Score: 46.78  E-value: 3.46e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63086916   12 IKPLRGMVLLERREAVEKSAGGVYLPIESKAKQVIAKVIEVGPGEVNREtgaripVDVAIGDWTIISRHTYESFKYNGKD 91
Cdd:PRK14533   3 VIPLGERLLIKPIKEEKKTEGGIVLPDSAKEKPMKAEVVAVGKLDDEED------FDIKVGDKVIFSKYAGTEIKIDDED 76

                         90
                 ....*....|....
gi 63086916   92 CVLVEARDIIAKVQ 105
Cdd:PRK14533  77 YIIIDVNDILAKIE 90
 
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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