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Conserved domains on  [gi|298710983|emb|CBJ32290|]
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conserved unknown protein [Ectocarpus siliculosus]

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) ...
 15-109 5.25e-16

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: 68.30  E-value: 5.25e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298710983  15 KALYDMVYVERLPEEQQMTSGLFLPAKANPRMHVCKVVSIGNGREGESGNVTPNDaVKQGDLVFVKDPYGIgprDDEFAG 94
Cdd:cd00320    3 KPLGDRVLVKRIEAEEKTKGGIILPDSAKEKPQEGKVVAVGPGRRNENGERVPLS-VKVGDKVLFPKYAGT---EVKLDG 78

                         90
                 ....*....|....*
gi 298710983  95 KKFSFVRYTSICAVI 109
Cdd:cd00320   79 EEYLILRESDILAVI 93
 
Name Accession Description Interval E-value
cpn10 cd00320
Chaperonin 10 Kd subunit (cpn10 or GroES); Cpn10 cooperates with chaperonin 60 (cpn60 or GroEL) ...
 15-109 5.25e-16

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: 68.30  E-value: 5.25e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298710983  15 KALYDMVYVERLPEEQQMTSGLFLPAKANPRMHVCKVVSIGNGREGESGNVTPNDaVKQGDLVFVKDPYGIgprDDEFAG 94
Cdd:cd00320    3 KPLGDRVLVKRIEAEEKTKGGIILPDSAKEKPQEGKVVAVGPGRRNENGERVPLS-VKVGDKVLFPKYAGT---EVKLDG 78

                         90
                 ....*....|....*
gi 298710983  95 KKFSFVRYTSICAVI 109
Cdd:cd00320   79 EEYLILRESDILAVI 93
Cpn10 pfam00166
Chaperonin 10 Kd subunit; This family contains GroES and Gp31-like chaperonins. Gp31 is a ...
 15-109 4.77e-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: 4.77e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298710983   15 KALYDMVYVERLPEEQQMTSGLFLPAKANPRMHVCKVVSIGNGREGESGNVTPNdaVKQGDLVFVKDPYGIgprDDEFAG 94
Cdd:pfam00166   3 KPLGDRVLVKRVEEEEKTAGGIILPDSAKEKPQQGEVVAVGPGARNNGNDVPLE--VKVGDKVLFPKYAGT---EVKVDG 77

                          90
                  ....*....|....*
gi 298710983   95 KKFSFVRYTSICAVI 109
Cdd:pfam00166  78 KEYLILKESDILAVI 92
groES PRK00364
co-chaperonin GroES; Reviewed
 15-109 2.37e-11

co-chaperonin GroES; Reviewed


Pssm-ID: 178988 [Multi-domain]  Cd Length: 95  Bit Score: 56.28  E-value: 2.37e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298710983  15 KALYDMVYVERLPEEQQMTSGLFLPAKANPRMHVCKVVSIGNGREGESGNVTPNDaVKQGDLVFVKDPYGIgprDDEFAG 94
Cdd:PRK00364   4 KPLGDRVLVKRLEEEEKTAGGIVLPDSAKEKPQEGEVVAVGPGRRLDNGERVPLD-VKVGDKVLFGKYAGT---EVKIDG 79

                         90
                 ....*....|....*
gi 298710983  95 KKFSFVRYTSICAVI 109
Cdd:PRK00364  80 EEYLILRESDILAIV 94
GroES COG0234
Co-chaperonin GroES (HSP10) [Posttranslational modification, protein turnover, chaperones];
15-109 4.39e-10

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


Pssm-ID: 440004  Cd Length: 95  Bit Score: 52.74  E-value: 4.39e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298710983  15 KALYDMVYVERLPEEQQMTSGLFLP--AKANPRMHvcKVVSIGNGREGESGNVTPNDaVKQGDLVFVKDPYGIgprDDEF 92
Cdd:COG0234    3 KPLGDRVLVKRIEAEEKTAGGIVLPdtAKEKPQEG--EVVAVGPGKLLDNGKRVPLD-VKVGDKVLFGKYAGT---EVKI 76

                         90
                 ....*....|....*..
gi 298710983  93 AGKKFSFVRYTSICAVI 109
Cdd:COG0234   77 DGEEYLILRESDILAVV 93
 
Name Accession Description Interval E-value
cpn10 cd00320
Chaperonin 10 Kd subunit (cpn10 or GroES); Cpn10 cooperates with chaperonin 60 (cpn60 or GroEL) ...
 15-109 5.25e-16

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: 68.30  E-value: 5.25e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298710983  15 KALYDMVYVERLPEEQQMTSGLFLPAKANPRMHVCKVVSIGNGREGESGNVTPNDaVKQGDLVFVKDPYGIgprDDEFAG 94
Cdd:cd00320    3 KPLGDRVLVKRIEAEEKTKGGIILPDSAKEKPQEGKVVAVGPGRRNENGERVPLS-VKVGDKVLFPKYAGT---EVKLDG 78

                         90
                 ....*....|....*
gi 298710983  95 KKFSFVRYTSICAVI 109
Cdd:cd00320   79 EEYLILRESDILAVI 93
Cpn10 pfam00166
Chaperonin 10 Kd subunit; This family contains GroES and Gp31-like chaperonins. Gp31 is a ...
 15-109 4.77e-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: 4.77e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298710983   15 KALYDMVYVERLPEEQQMTSGLFLPAKANPRMHVCKVVSIGNGREGESGNVTPNdaVKQGDLVFVKDPYGIgprDDEFAG 94
Cdd:pfam00166   3 KPLGDRVLVKRVEEEEKTAGGIILPDSAKEKPQQGEVVAVGPGARNNGNDVPLE--VKVGDKVLFPKYAGT---EVKVDG 77

                          90
                  ....*....|....*
gi 298710983   95 KKFSFVRYTSICAVI 109
Cdd:pfam00166  78 KEYLILKESDILAVI 92
groES PRK00364
co-chaperonin GroES; Reviewed
 15-109 2.37e-11

co-chaperonin GroES; Reviewed


Pssm-ID: 178988 [Multi-domain]  Cd Length: 95  Bit Score: 56.28  E-value: 2.37e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298710983  15 KALYDMVYVERLPEEQQMTSGLFLPAKANPRMHVCKVVSIGNGREGESGNVTPNDaVKQGDLVFVKDPYGIgprDDEFAG 94
Cdd:PRK00364   4 KPLGDRVLVKRLEEEEKTAGGIVLPDSAKEKPQEGEVVAVGPGRRLDNGERVPLD-VKVGDKVLFGKYAGT---EVKIDG 79

                         90
                 ....*....|....*
gi 298710983  95 KKFSFVRYTSICAVI 109
Cdd:PRK00364  80 EEYLILRESDILAIV 94
GroES COG0234
Co-chaperonin GroES (HSP10) [Posttranslational modification, protein turnover, chaperones];
15-109 4.39e-10

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


Pssm-ID: 440004  Cd Length: 95  Bit Score: 52.74  E-value: 4.39e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298710983  15 KALYDMVYVERLPEEQQMTSGLFLP--AKANPRMHvcKVVSIGNGREGESGNVTPNDaVKQGDLVFVKDPYGIgprDDEF 92
Cdd:COG0234    3 KPLGDRVLVKRIEAEEKTAGGIVLPdtAKEKPQEG--EVVAVGPGKLLDNGKRVPLD-VKVGDKVLFGKYAGT---EVKI 76

                         90
                 ....*....|....*..
gi 298710983  93 AGKKFSFVRYTSICAVI 109
Cdd:COG0234   77 DGEEYLILRESDILAVV 93
 
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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