NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1120517796|ref|WP_073376999|]
View 

MULTISPECIES: co-chaperone GroES [Nocardiopsis]

Protein Classification

GroES family protein( domain architecture ID 10785100)

GroES family protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
GroES COG0234
Co-chaperonin GroES (HSP10) [Posttranslational modification, protein turnover, chaperones];
9-103 6.73e-53

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


:

Pssm-ID: 440004  Cd Length: 95  Bit Score: 160.21  E-value: 6.73e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120517796   9 LKPLEDRVVVKALEAEQTTASGLVIPDTAKEKPQEGEVLAVGPGRWDDEGdKRIPLDVKVGDVVLYSKYGGTEVKYDGQE 88
Cdd:COG0234     2 IKPLGDRVLVKRIEAEEKTAGGIVLPDTAKEKPQEGEVVAVGPGKLLDNG-KRVPLDVKVGDKVLFGKYAGTEVKIDGEE 80

                          90
                  ....*....|....*
gi 1120517796  89 YLVLSARDLLAVVEK 103
Cdd:COG0234    81 YLILRESDILAVVEE 95
 
Name Accession Description Interval E-value
GroES COG0234
Co-chaperonin GroES (HSP10) [Posttranslational modification, protein turnover, chaperones];
9-103 6.73e-53

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


Pssm-ID: 440004  Cd Length: 95  Bit Score: 160.21  E-value: 6.73e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120517796   9 LKPLEDRVVVKALEAEQTTASGLVIPDTAKEKPQEGEVLAVGPGRWDDEGdKRIPLDVKVGDVVLYSKYGGTEVKYDGQE 88
Cdd:COG0234     2 IKPLGDRVLVKRIEAEEKTAGGIVLPDTAKEKPQEGEVVAVGPGKLLDNG-KRVPLDVKVGDKVLFGKYAGTEVKIDGEE 80

                          90
                  ....*....|....*
gi 1120517796  89 YLVLSARDLLAVVEK 103
Cdd:COG0234    81 YLILRESDILAVVEE 95
groES PRK00364
co-chaperonin GroES; Reviewed
 9-102 2.80e-51

co-chaperonin GroES; Reviewed


Pssm-ID: 178988 [Multi-domain]  Cd Length: 95  Bit Score: 156.04  E-value: 2.80e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120517796   9 LKPLEDRVVVKALEAEQTTASGLVIPDTAKEKPQEGEVLAVGPGRWDDEGdKRIPLDVKVGDVVLYSKYGGTEVKYDGQE 88
Cdd:PRK00364    3 LKPLGDRVLVKRLEEEEKTAGGIVLPDSAKEKPQEGEVVAVGPGRRLDNG-ERVPLDVKVGDKVLFGKYAGTEVKIDGEE 81

                          90
                  ....*....|....
gi 1120517796  89 YLVLSARDLLAVVE 102
Cdd:PRK00364   82 YLILRESDILAIVE 95
Cpn10 smart00883
Chaperonin 10 Kd subunit; The chaperonins are 'helper' molecules required for correct folding ...
 9-101 1.61e-46

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: 144.11  E-value: 1.61e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120517796    9 LKPLEDRVVVKALEAEQTTASGLVIPDTAKEKPQEGEVLAVGPGRWDDEGDkRIPLDVKVGDVVLYSKYGGTEVKYDGQE 88
Cdd:smart00883   2 IKPLGDRVLVKRIEEEEKTAGGIVIPDTAKEKPQEGEVVAVGPGKRLENGE-RVPLDVKVGDKVLFGKYAGTEVKLDGEE 80

                           90
                   ....*....|...
gi 1120517796   89 YLVLSARDLLAVV 101
Cdd:smart00883  81 YLILRESDILAVI 93
cpn10 cd00320
Chaperonin 10 Kd subunit (cpn10 or GroES); Cpn10 cooperates with chaperonin 60 (cpn60 or GroEL) ...
 9-101 4.29e-41

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: 130.32  E-value: 4.29e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120517796   9 LKPLEDRVVVKALEAEQTTASGLVIPDTAKEKPQEGEVLAVGPGRWDDEGdKRIPLDVKVGDVVLYSKYGGTEVKYDGQE 88
Cdd:cd00320     2 IKPLGDRVLVKRIEAEEKTKGGIILPDSAKEKPQEGKVVAVGPGRRNENG-ERVPLSVKVGDKVLFPKYAGTEVKLDGEE 80

                          90
                  ....*....|...
gi 1120517796  89 YLVLSARDLLAVV 101
Cdd:cd00320    81 YLILRESDILAVI 93
Cpn10 pfam00166
Chaperonin 10 Kd subunit; This family contains GroES and Gp31-like chaperonins. Gp31 is a ...
 9-101 1.94e-37

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: 121.18  E-value: 1.94e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120517796   9 LKPLEDRVVVKALEAEQTTASGLVIPDTAKEKPQEGEVLAVGPGRWDDegDKRIPLDVKVGDVVLYSKYGGTEVKYDGQE 88
Cdd:pfam00166   2 IKPLGDRVLVKRVEEEEKTAGGIILPDSAKEKPQQGEVVAVGPGARNN--GNDVPLEVKVGDKVLFPKYAGTEVKVDGKE 79

                          90
                  ....*....|...
gi 1120517796  89 YLVLSARDLLAVV 101
Cdd:pfam00166  80 YLILKESDILAVI 92
 
Name Accession Description Interval E-value
GroES COG0234
Co-chaperonin GroES (HSP10) [Posttranslational modification, protein turnover, chaperones];
9-103 6.73e-53

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


Pssm-ID: 440004  Cd Length: 95  Bit Score: 160.21  E-value: 6.73e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120517796   9 LKPLEDRVVVKALEAEQTTASGLVIPDTAKEKPQEGEVLAVGPGRWDDEGdKRIPLDVKVGDVVLYSKYGGTEVKYDGQE 88
Cdd:COG0234     2 IKPLGDRVLVKRIEAEEKTAGGIVLPDTAKEKPQEGEVVAVGPGKLLDNG-KRVPLDVKVGDKVLFGKYAGTEVKIDGEE 80

                          90
                  ....*....|....*
gi 1120517796  89 YLVLSARDLLAVVEK 103
Cdd:COG0234    81 YLILRESDILAVVEE 95
groES PRK00364
co-chaperonin GroES; Reviewed
 9-102 2.80e-51

co-chaperonin GroES; Reviewed


Pssm-ID: 178988 [Multi-domain]  Cd Length: 95  Bit Score: 156.04  E-value: 2.80e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120517796   9 LKPLEDRVVVKALEAEQTTASGLVIPDTAKEKPQEGEVLAVGPGRWDDEGdKRIPLDVKVGDVVLYSKYGGTEVKYDGQE 88
Cdd:PRK00364    3 LKPLGDRVLVKRLEEEEKTAGGIVLPDSAKEKPQEGEVVAVGPGRRLDNG-ERVPLDVKVGDKVLFGKYAGTEVKIDGEE 81

                          90
                  ....*....|....
gi 1120517796  89 YLVLSARDLLAVVE 102
Cdd:PRK00364   82 YLILRESDILAIVE 95
Cpn10 smart00883
Chaperonin 10 Kd subunit; The chaperonins are 'helper' molecules required for correct folding ...
 9-101 1.61e-46

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: 144.11  E-value: 1.61e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120517796    9 LKPLEDRVVVKALEAEQTTASGLVIPDTAKEKPQEGEVLAVGPGRWDDEGDkRIPLDVKVGDVVLYSKYGGTEVKYDGQE 88
Cdd:smart00883   2 IKPLGDRVLVKRIEEEEKTAGGIVIPDTAKEKPQEGEVVAVGPGKRLENGE-RVPLDVKVGDKVLFGKYAGTEVKLDGEE 80

                           90
                   ....*....|...
gi 1120517796   89 YLVLSARDLLAVV 101
Cdd:smart00883  81 YLILRESDILAVI 93
cpn10 cd00320
Chaperonin 10 Kd subunit (cpn10 or GroES); Cpn10 cooperates with chaperonin 60 (cpn60 or GroEL) ...
 9-101 4.29e-41

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: 130.32  E-value: 4.29e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120517796   9 LKPLEDRVVVKALEAEQTTASGLVIPDTAKEKPQEGEVLAVGPGRWDDEGdKRIPLDVKVGDVVLYSKYGGTEVKYDGQE 88
Cdd:cd00320     2 IKPLGDRVLVKRIEAEEKTKGGIILPDSAKEKPQEGKVVAVGPGRRNENG-ERVPLSVKVGDKVLFPKYAGTEVKLDGEE 80

                          90
                  ....*....|...
gi 1120517796  89 YLVLSARDLLAVV 101
Cdd:cd00320    81 YLILRESDILAVI 93
Cpn10 pfam00166
Chaperonin 10 Kd subunit; This family contains GroES and Gp31-like chaperonins. Gp31 is a ...
 9-101 1.94e-37

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: 121.18  E-value: 1.94e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120517796   9 LKPLEDRVVVKALEAEQTTASGLVIPDTAKEKPQEGEVLAVGPGRWDDegDKRIPLDVKVGDVVLYSKYGGTEVKYDGQE 88
Cdd:pfam00166   2 IKPLGDRVLVKRVEEEEKTAGGIILPDSAKEKPQQGEVVAVGPGARNN--GNDVPLEVKVGDKVLFPKYAGTEVKVDGKE 79

                          90
                  ....*....|...
gi 1120517796  89 YLVLSARDLLAVV 101
Cdd:pfam00166  80 YLILKESDILAVI 92
groES PRK14533
co-chaperonin GroES; Provisional
 9-102 2.73e-21

co-chaperonin GroES; Provisional


Pssm-ID: 184730  Cd Length: 91  Bit Score: 80.30  E-value: 2.73e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120517796   9 LKPLEDRVVVKALEAEQTTASGLVIPDTAKEKPQEGEVLAVgpGRWDDEGDkripLDVKVGDVVLYSKYGGTEVKYDGQE 88
Cdd:PRK14533    3 VIPLGERLLIKPIKEEKKTEGGIVLPDSAKEKPMKAEVVAV--GKLDDEED----FDIKVGDKVIFSKYAGTEIKIDDED 76

                          90
                  ....*....|....
gi 1120517796  89 YLVLSARDLLAVVE 102
Cdd:PRK14533   77 YIIIDVNDILAKIE 90
PTZ00414 PTZ00414
10 kDa heat shock protein; Provisional
 9-102 7.66e-14

10 kDa heat shock protein; Provisional


Pssm-ID: 173604  Cd Length: 100  Bit Score: 61.55  E-value: 7.66e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120517796   9 LKPLEDRVVVKALEAEQTTASGLVIPDTAKEKPQEGEVLAVGPGRWDdegdkRIPlDVKVGDVVLYSKYGGTEVKYDGQE 88
Cdd:PTZ00414   12 LQPLGQRVLVKRTLAAKQTKAGVLIPEQVAGKVNEGTVVAVAAATKD-----WTP-TVKVGDTVLLPEFGGSSVKVEGEE 85

                          90
                  ....*....|....
gi 1120517796  89 YLVLSARDLLAVVE 102
Cdd:PTZ00414   86 FFLYNEDSLLGVLQ 99
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH