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Conserved domains on  [gi|1121615408|gb|APP89782|]
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chaperonin protein, partial [Clostridium perfringens]

Protein Classification

TCP-1/cpn60 chaperonin family protein( domain architecture ID 16)

TCP-1/cpn60 chaperonin family protein similar to mycobacterial 60 kDa chaperonin (GroEL) that together with its co-chaperonin GroES, plays an essential role in assisting protein folding

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
chaperonin_like super family cl02777
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ...
 1-190 6.31e-123

chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings, each composed of 7-9 subunits. There are 2 main chaperonin groups. The symmetry of type I is seven-fold and they are found in eubacteria (GroEL) and in organelles of eubacterial descent (hsp60 and RBP). The symmetry of type II is eight- or nine-fold and they are found in archea (thermosome), thermophilic bacteria (TF55) and in the eukaryotic cytosol (CTT). Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. This superfamily also contains related domains from Fab1-like phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinases that only contain the intermediate and apical domains.


The actual alignment was detected with superfamily member PRK00013:

Pssm-ID: 351886  Cd Length: 542  Bit Score: 357.51  E-value: 6.31e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121615408   1 TLLAQAIIREGLKNVTAGANPILIRNGIKTAVEKAVEEIQKISKPVNGKEDIARVAAISA-ADEKIGKLIADAMEKVGNE 79
Cdd:PRK00013   92 TVLAQAIVREGLKNVAAGANPMDLKRGIDKAVEAAVEELKKISKPVEDKEEIAQVATISAnGDEEIGKLIAEAMEKVGKE 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121615408  80 GVITVEESKSMGTELDVVEGMQFDRGYVSAYMVTDTEKMEAVLDNPLVLITDKKISNIQDLLPLLEQIVQAGKKLLIIAD 159
Cdd:PRK00013  172 GVITVEESKGFETELEVVEGMQFDRGYLSPYFVTDPEKMEAELENPYILITDKKISNIQDLLPVLEQVAQSGKPLLIIAE 251

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1121615408 160 DIEGEAMTTLVVNKLRGTFTCVGVKAPGFGD 190
Cdd:PRK00013  252 DVEGEALATLVVNKLRGTLKVVAVKAPGFGD 282
 
Name Accession Description Interval E-value
groEL PRK00013
chaperonin GroEL; Reviewed
 1-190 6.31e-123

chaperonin GroEL; Reviewed


Pssm-ID: 234573  Cd Length: 542  Bit Score: 357.51  E-value: 6.31e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121615408   1 TLLAQAIIREGLKNVTAGANPILIRNGIKTAVEKAVEEIQKISKPVNGKEDIARVAAISA-ADEKIGKLIADAMEKVGNE 79
Cdd:PRK00013   92 TVLAQAIVREGLKNVAAGANPMDLKRGIDKAVEAAVEELKKISKPVEDKEEIAQVATISAnGDEEIGKLIAEAMEKVGKE 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121615408  80 GVITVEESKSMGTELDVVEGMQFDRGYVSAYMVTDTEKMEAVLDNPLVLITDKKISNIQDLLPLLEQIVQAGKKLLIIAD 159
Cdd:PRK00013  172 GVITVEESKGFETELEVVEGMQFDRGYLSPYFVTDPEKMEAELENPYILITDKKISNIQDLLPVLEQVAQSGKPLLIIAE 251

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1121615408 160 DIEGEAMTTLVVNKLRGTFTCVGVKAPGFGD 190
Cdd:PRK00013  252 DVEGEALATLVVNKLRGTLKVVAVKAPGFGD 282
GroEL cd03344
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ...
 1-190 5.95e-108

GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings, each composed of 7-9 subunits. The symmetry of type I is seven-fold and they are found in eubacteria (GroEL) and in organelles of eubacterial descent (hsp60 and RBP). With the aid of cochaperonin GroES, GroEL encapsulates non-native substrate proteins inside the cavity of the GroEL-ES complex and promotes folding by using energy derived from ATP hydrolysis.


Pssm-ID: 239460  Cd Length: 520  Bit Score: 318.63  E-value: 5.95e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121615408   1 TLLAQAIIREGLKNVTAGANPILIRNGIKTAVEKAVEEIQKISKPVNGKEDIARVAAISA-ADEKIGKLIADAMEKVGNE 79
Cdd:cd03344    90 TVLARAIIKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKPVKTKEEIAQVATISAnGDEEIGELIAEAMEKVGKD 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121615408  80 GVITVEESKSMGTELDVVEGMQFDRGYVSAYMVTDTEKMEAVLDNPLVLITDKKISNIQDLLPLLEQIVQAGKKLLIIAD 159
Cdd:cd03344   170 GVITVEEGKTLETELEVVEGMQFDRGYLSPYFVTDPEKMEVELENPYILLTDKKISSIQELLPILELVAKAGRPLLIIAE 249

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1121615408 160 DIEGEAMTTLVVNKLRGTFTCVGVKAPGFGD 190
Cdd:cd03344   250 DVEGEALATLVVNKLRGGLKVCAVKAPGFGD 280
GroEL TIGR02348
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ...
 1-190 2.35e-105

chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES cytosolic chaperonin. It is found in bacteria, organelles derived from bacteria, and occasionally in the Archaea. The bacterial GroEL/GroES group I chaperonin is replaced a group II chaperonin, usually called the thermosome in the Archaeota and CCT (chaperone-containing TCP) in the Eukaryota. GroEL, thermosome subunits, and CCT subunits all fall under the scope of pfam00118. [Protein fate, Protein folding and stabilization]


Pssm-ID: 274089  Cd Length: 524  Bit Score: 311.92  E-value: 2.35e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121615408   1 TLLAQAIIREGLKNVTAGANPILIRNGIKTAVEKAVEEIQKISKPVNGKEDIARVAAISA-ADEKIGKLIADAMEKVGNE 79
Cdd:TIGR02348  91 TVLAQAIVKEGLKNVAAGANPIELKRGIEKAVEAVVEELKKLSKPVKGKKEIAQVATISAnNDEEIGSLIAEAMEKVGKD 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121615408  80 GVITVEESKSMGTELDVVEGMQFDRGYVSAYMVTDTEKMEAVLDNPLVLITDKKISNIQDLLPLLEQIVQAGKKLLIIAD 159
Cdd:TIGR02348 171 GVITVEESKSLETELEVVEGMQFDRGYISPYFVTDAEKMEVELENPYILITDKKISNIKDLLPLLEKVAQSGKPLLIIAE 250

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1121615408 160 DIEGEAMTTLVVNKLRGTFTCVGVKAPGFGD 190
Cdd:TIGR02348 251 DVEGEALATLVVNKLRGTLNVCAVKAPGFGD 281
GroEL COG0459
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ...
 1-190 2.96e-104

Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440227  Cd Length: 497  Bit Score: 308.16  E-value: 2.96e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121615408   1 TLLAQAIIREGLKNVTAGANPILIRNGIKTAVEKAVEEIQKISKPVNGKEDIARVAAISAA-DEKIGKLIADAMEKVGNE 79
Cdd:COG0459    92 TVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPVDDKEELAQVATISANgDEEIGELIAEAMEKVGKD 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121615408  80 GVITVEESKSMGTELDVVEGMQFDRGYVSAYMVTDTEKMEAVLDNPLVLITDKKISNIQDLLPLLEQIVQAGKKLLIIAD 159
Cdd:COG0459   172 GVITVEEGKGLETELEVVEGMQFDKGYLSPYFVTDPEKMPAELENAYILLTDKKISSIQDLLPLLEKVAQSGKPLLIIAE 251

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1121615408 160 DIEGEAMTTLVVNKLRGTFTCVGVKAPGFGD 190
Cdd:COG0459   252 DIDGEALATLVVNGIRGVLRVVAVKAPGFGD 282
Cpn60_TCP1 pfam00118
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ...
 2-176 4.46e-21

TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family and the TCP-1 (T-complex protein) family.


Pssm-ID: 395068 [Multi-domain]  Cd Length: 489  Bit Score: 89.57  E-value: 4.46e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121615408   2 LLAQAIIREGLKNVTAGANPILIRNGIKTAVEKAVE---EIQKISKPVNGKEDIARVAAISAA-------DEKIGKLIAD 71
Cdd:pfam00118  68 VLAGELLEEAEKLLAAGVHPTTIIEGYEKALEKALEildSIISIPVEDVDREDLLKVARTSLSskiisreSDFLAKLVVD 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121615408  72 AME---------KVGNEGVITVEESKSMGTELdvVEGMQFDRGYVSaymvtdtEKMEAVLDNPLVLITDKKISNIQD--- 139
Cdd:pfam00118 148 AVLaipkndgsfDLGNIGVVKILGGSLEDSEL--VDGVVLDKGPLH-------PDMPKRLENAKVLLLNCSLEYEKTetk 218

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1121615408 140 ---------------------LLPLLEQIVQAGKKLLIIADDIEGEAMTTLVVNKLRG 176
Cdd:pfam00118 219 atvvlsdaeqlerflkaeeeqILEIVEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMA 276
 
Name Accession Description Interval E-value
groEL PRK00013
chaperonin GroEL; Reviewed
 1-190 6.31e-123

chaperonin GroEL; Reviewed


Pssm-ID: 234573  Cd Length: 542  Bit Score: 357.51  E-value: 6.31e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121615408   1 TLLAQAIIREGLKNVTAGANPILIRNGIKTAVEKAVEEIQKISKPVNGKEDIARVAAISA-ADEKIGKLIADAMEKVGNE 79
Cdd:PRK00013   92 TVLAQAIVREGLKNVAAGANPMDLKRGIDKAVEAAVEELKKISKPVEDKEEIAQVATISAnGDEEIGKLIAEAMEKVGKE 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121615408  80 GVITVEESKSMGTELDVVEGMQFDRGYVSAYMVTDTEKMEAVLDNPLVLITDKKISNIQDLLPLLEQIVQAGKKLLIIAD 159
Cdd:PRK00013  172 GVITVEESKGFETELEVVEGMQFDRGYLSPYFVTDPEKMEAELENPYILITDKKISNIQDLLPVLEQVAQSGKPLLIIAE 251

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1121615408 160 DIEGEAMTTLVVNKLRGTFTCVGVKAPGFGD 190
Cdd:PRK00013  252 DVEGEALATLVVNKLRGTLKVVAVKAPGFGD 282
GroEL cd03344
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ...
 1-190 5.95e-108

GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings, each composed of 7-9 subunits. The symmetry of type I is seven-fold and they are found in eubacteria (GroEL) and in organelles of eubacterial descent (hsp60 and RBP). With the aid of cochaperonin GroES, GroEL encapsulates non-native substrate proteins inside the cavity of the GroEL-ES complex and promotes folding by using energy derived from ATP hydrolysis.


Pssm-ID: 239460  Cd Length: 520  Bit Score: 318.63  E-value: 5.95e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121615408   1 TLLAQAIIREGLKNVTAGANPILIRNGIKTAVEKAVEEIQKISKPVNGKEDIARVAAISA-ADEKIGKLIADAMEKVGNE 79
Cdd:cd03344    90 TVLARAIIKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKPVKTKEEIAQVATISAnGDEEIGELIAEAMEKVGKD 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121615408  80 GVITVEESKSMGTELDVVEGMQFDRGYVSAYMVTDTEKMEAVLDNPLVLITDKKISNIQDLLPLLEQIVQAGKKLLIIAD 159
Cdd:cd03344   170 GVITVEEGKTLETELEVVEGMQFDRGYLSPYFVTDPEKMEVELENPYILLTDKKISSIQELLPILELVAKAGRPLLIIAE 249

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1121615408 160 DIEGEAMTTLVVNKLRGTFTCVGVKAPGFGD 190
Cdd:cd03344   250 DVEGEALATLVVNKLRGGLKVCAVKAPGFGD 280
GroEL TIGR02348
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ...
 1-190 2.35e-105

chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES cytosolic chaperonin. It is found in bacteria, organelles derived from bacteria, and occasionally in the Archaea. The bacterial GroEL/GroES group I chaperonin is replaced a group II chaperonin, usually called the thermosome in the Archaeota and CCT (chaperone-containing TCP) in the Eukaryota. GroEL, thermosome subunits, and CCT subunits all fall under the scope of pfam00118. [Protein fate, Protein folding and stabilization]


Pssm-ID: 274089  Cd Length: 524  Bit Score: 311.92  E-value: 2.35e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121615408   1 TLLAQAIIREGLKNVTAGANPILIRNGIKTAVEKAVEEIQKISKPVNGKEDIARVAAISA-ADEKIGKLIADAMEKVGNE 79
Cdd:TIGR02348  91 TVLAQAIVKEGLKNVAAGANPIELKRGIEKAVEAVVEELKKLSKPVKGKKEIAQVATISAnNDEEIGSLIAEAMEKVGKD 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121615408  80 GVITVEESKSMGTELDVVEGMQFDRGYVSAYMVTDTEKMEAVLDNPLVLITDKKISNIQDLLPLLEQIVQAGKKLLIIAD 159
Cdd:TIGR02348 171 GVITVEESKSLETELEVVEGMQFDRGYISPYFVTDAEKMEVELENPYILITDKKISNIKDLLPLLEKVAQSGKPLLIIAE 250

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1121615408 160 DIEGEAMTTLVVNKLRGTFTCVGVKAPGFGD 190
Cdd:TIGR02348 251 DVEGEALATLVVNKLRGTLNVCAVKAPGFGD 281
groEL PRK12849
chaperonin GroEL; Reviewed
 1-190 6.37e-105

chaperonin GroEL; Reviewed


Pssm-ID: 237230  Cd Length: 542  Bit Score: 311.36  E-value: 6.37e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121615408   1 TLLAQAIIREGLKNVTAGANPILIRNGIKTAVEKAVEEIQKISKPVNGKEDIARVAAISA-ADEKIGKLIADAMEKVGNE 79
Cdd:PRK12849   92 TVLAQALVQEGLKNVAAGANPMDLKRGIDKAVEAVVEELKALARPVSGSEEIAQVATISAnGDEEIGELIAEAMEKVGKD 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121615408  80 GVITVEESKSMGTELDVVEGMQFDRGYVSAYMVTDTEKMEAVLDNPLVLITDKKISNIQDLLPLLEQIVQAGKKLLIIAD 159
Cdd:PRK12849  172 GVITVEESKTLETELEVTEGMQFDRGYLSPYFVTDPERMEAVLEDPLILLTDKKISSLQDLLPLLEKVAQSGKPLLIIAE 251

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1121615408 160 DIEGEAMTTLVVNKLRGTFTCVGVKAPGFGD 190
Cdd:PRK12849  252 DVEGEALATLVVNKLRGGLKVAAVKAPGFGD 282
GroEL COG0459
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ...
 1-190 2.96e-104

Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440227  Cd Length: 497  Bit Score: 308.16  E-value: 2.96e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121615408   1 TLLAQAIIREGLKNVTAGANPILIRNGIKTAVEKAVEEIQKISKPVNGKEDIARVAAISAA-DEKIGKLIADAMEKVGNE 79
Cdd:COG0459    92 TVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPVDDKEELAQVATISANgDEEIGELIAEAMEKVGKD 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121615408  80 GVITVEESKSMGTELDVVEGMQFDRGYVSAYMVTDTEKMEAVLDNPLVLITDKKISNIQDLLPLLEQIVQAGKKLLIIAD 159
Cdd:COG0459   172 GVITVEEGKGLETELEVVEGMQFDKGYLSPYFVTDPEKMPAELENAYILLTDKKISSIQDLLPLLEKVAQSGKPLLIIAE 251

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1121615408 160 DIEGEAMTTLVVNKLRGTFTCVGVKAPGFGD 190
Cdd:COG0459   252 DIDGEALATLVVNGIRGVLRVVAVKAPGFGD 282
groEL PRK12850
chaperonin GroEL; Reviewed
 1-190 5.92e-98

chaperonin GroEL; Reviewed


Pssm-ID: 237231  Cd Length: 544  Bit Score: 293.55  E-value: 5.92e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121615408   1 TLLAQAIIREGLKNVTAGANPILIRNGIKTAVEKAVEEIQKISKPVNGKEDIARVAAISA-ADEKIGKLIADAMEKVGNE 79
Cdd:PRK12850   93 TVLAQAIVREGAKLVAAGMNPMDLKRGIDLAVAAVVDELKKIAKKVTSSKEIAQVATISAnGDESIGEMIAEAMDKVGKE 172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121615408  80 GVITVEESKSMGTELDVVEGMQFDRGYVSAYMVTDTEKMEAVLDNPLVLITDKKISNIQDLLPLLEQIVQAGKKLLIIAD 159
Cdd:PRK12850  173 GVITVEEAKTLGTELDVVEGMQFDRGYLSPYFVTNPEKMRAELEDPYILLHEKKISNLQDLLPILEAVVQSGRPLLIIAE 252

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1121615408 160 DIEGEAMTTLVVNKLRGTFTCVGVKAPGFGD 190
Cdd:PRK12850  253 DVEGEALATLVVNKLRGGLKSVAVKAPGFGD 283
groEL PRK12851
chaperonin GroEL; Reviewed
 1-190 3.81e-93

chaperonin GroEL; Reviewed


Pssm-ID: 171770  Cd Length: 541  Bit Score: 281.25  E-value: 3.81e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121615408   1 TLLAQAIIREGLKNVTAGANPILIRNGIKTAVEKAVEEIQKISKPVNGKEDIARVAAISA-ADEKIGKLIADAMEKVGNE 79
Cdd:PRK12851   93 TVLAQAIVREGAKAVAAGANPMDLKRGIDRAVAAVVEELKANARPVTTNAEIAQVATISAnGDAEIGRLVAEAMEKVGNE 172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121615408  80 GVITVEESKSMGTELDVVEGMQFDRGYVSAYMVTDTEKMEAVLDNPLVLITDKKISNIQDLLPLLEQIVQAGKKLLIIAD 159
Cdd:PRK12851  173 GVITVEESKTAETELEVVEGMQFDRGYLSPYFVTDADKMEAELEDPYILIHEKKISNLQDLLPVLEAVVQSGKPLLIIAE 252

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1121615408 160 DIEGEAMTTLVVNKLRGTFTCVGVKAPGFGD 190
Cdd:PRK12851  253 DVEGEALATLVVNKLRGGLKVAAVKAPGFGD 283
PTZ00114 PTZ00114
Heat shock protein 60; Provisional
 1-190 4.36e-82

Heat shock protein 60; Provisional


Pssm-ID: 185455  Cd Length: 555  Bit Score: 253.30  E-value: 4.36e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121615408   1 TLLAQAIIREGLKNVTAGANPILIRNGIKTAVEKAVEEIQKISKPVNGKEDIARVAAISA-ADEKIGKLIADAMEKVGNE 79
Cdd:PTZ00114  104 TILARAIFREGCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQSRPVKTKEDILNVATISAnGDVEIGSLIADAMDKVGKD 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121615408  80 GVITVEESKSMGTELDVVEGMQFDRGYVSAYMVTDTEKMEAVLDNPLVLITDKKISNIQDLLPLLEQIVQAGKKLLIIAD 159
Cdd:PTZ00114  184 GTITVEDGKTLEDELEVVEGMSFDRGYISPYFVTNEKTQKVELENPLILVTDKKISSIQSILPILEHAVKNKRPLLIIAE 263

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1121615408 160 DIEGEAMTTLVVNKLRGTFTCVGVKAPGFGD 190
Cdd:PTZ00114  264 DVEGEALQTLIINKLRGGLKVCAVKAPGFGD 294
groEL CHL00093
chaperonin GroEL
 1-190 9.74e-82

chaperonin GroEL


Pssm-ID: 177025  Cd Length: 529  Bit Score: 251.56  E-value: 9.74e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121615408   1 TLLAQAIIREGLKNVTAGANPILIRNGIKTAVEKAVEEIQKISKPVNGKEDIARVAAISAA-DEKIGKLIADAMEKVGNE 79
Cdd:CHL00093   92 TVLAYAIVKQGMKNVAAGANPISLKRGIEKATQYVVSQIAEYARPVEDIQAITQVASISAGnDEEVGSMIADAIEKVGRE 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121615408  80 GVITVEESKSMGTELDVVEGMQFDRGYVSAYMVTDTEKMEAVLDNPLVLITDKKISNI-QDLLPLLEQIVQAGKKLLIIA 158
Cdd:CHL00093  172 GVISLEEGKSTVTELEITEGMRFEKGFISPYFVTDTERMEVVQENPYILLTDKKITLVqQDLLPILEQVTKTKRPLLIIA 251

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1121615408 159 DDIEGEAMTTLVVNKLRGTFTCVGVKAPGFGD 190
Cdd:CHL00093  252 EDVEKEALATLVLNKLRGIVNVVAVRAPGFGD 283
groEL PRK12852
chaperonin GroEL; Reviewed
 1-190 3.16e-80

chaperonin GroEL; Reviewed


Pssm-ID: 237232  Cd Length: 545  Bit Score: 248.22  E-value: 3.16e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121615408   1 TLLAQAIIREGLKNVTAGANPILIRNGIKTAVEKAVEEIQKISKPVNGKEDIARVAAISA-ADEKIGKLIADAMEKVGNE 79
Cdd:PRK12852   93 TVLAQAIVREGAKAVAAGMNPMDLKRGIDIAVAAVVKDIEKRAKPVASSAEIAQVGTISAnGDAAIGKMIAQAMQKVGNE 172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121615408  80 GVITVEESKSMGTELDVVEGMQFDRGYVSAYMVTDTEKMEAVLDNPLVLITDKKISNIQDLLPLLEQIVQAGKKLLIIAD 159
Cdd:PRK12852  173 GVITVEENKSLETEVDIVEGMKFDRGYLSPYFVTNAEKMTVELDDAYILLHEKKLSGLQAMLPVLEAVVQSGKPLLIIAE 252

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1121615408 160 DIEGEAMTTLVVNKLRGTFTCVGVKAPGFGD 190
Cdd:PRK12852  253 DVEGEALATLVVNRLRGGLKVAAVKAPGFGD 283
PRK14104 PRK14104
chaperonin GroEL; Provisional
 1-190 3.61e-70

chaperonin GroEL; Provisional


Pssm-ID: 172594  Cd Length: 546  Bit Score: 222.21  E-value: 3.61e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121615408   1 TLLAQAIIREGLKNVTAGANPILIRNGIKTAVEKAVEEIQKISKPVNGKEDIARVAAISA-ADEKIGKLIADAMEKVGNE 79
Cdd:PRK14104   93 TVLAQAIVREGAKSVAAGMNPMDLKRGIDLAVEAVVADLVKNSKKVTSNDEIAQVGTISAnGDAEIGKFLADAMKKVGNE 172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121615408  80 GVITVEESKSMGTELDVVEGMQFDRGYVSAYMVTDTEKMEAVLDNPLVLITDKKISNIQDLLPLLEQIVQAGKKLLIIAD 159
Cdd:PRK14104  173 GVITVEEAKSLETELDVVEGMQFDRGYISPYFVTNADKMRVEMDDAYILINEKKLSSLNELLPLLEAVVQTGKPLVIVAE 252

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1121615408 160 DIEGEAMTTLVVNKLRGTFTCVGVKAPGFGD 190
Cdd:PRK14104  253 DVEGEALATLVVNRLRGGLKVAAVKAPGFGD 283
PLN03167 PLN03167
Chaperonin-60 beta subunit; Provisional
 2-190 5.71e-60

Chaperonin-60 beta subunit; Provisional


Pssm-ID: 215611 [Multi-domain]  Cd Length: 600  Bit Score: 196.68  E-value: 5.71e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121615408   2 LLAQAIIREGLKNVTAGANPILIRNGIKTAVEKAVEEIQKISKPVNGKEdIARVAAISAADE-KIGKLIADAMEKVGNEG 80
Cdd:PLN03167  149 VLAQGLIAEGVKVVAAGANPVQITRGIEKTAKALVKELKKMSKEVEDSE-LADVAAVSAGNNyEVGNMIAEAMSKVGRKG 227

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121615408  81 VITVEESKSMGTELDVVEGMQFDRGYVSAYMVTDTEKMEAVLDNPLVLITDKKISNIQDLLPLLEQIVQAGKKLLIIADD 160
Cdd:PLN03167  228 VVTLEEGKSAENNLYVVEGMQFDRGYISPYFVTDSEKMSVEYDNCKLLLVDKKITNARDLIGILEDAIRGGYPLLIIAED 307

                         170       180       190
                  ....*....|....*....|....*....|
gi 1121615408 161 IEGEAMTTLVVNKLRGTFTCVGVKAPGFGD 190
Cdd:PLN03167  308 IEQEALATLVVNKLRGSLKIAALKAPGFGE 337
chaperonin_type_I_II cd00309
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ...
 1-174 5.17e-38

chaperonin families, type I and type II. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings, each composed of 7-9 subunits. There are 2 main chaperonin groups. The symmetry of type I is seven-fold and they are found in eubacteria (GroEL) and in organelles of eubacterial descent (hsp60 and RBP). The symmetry of type II is eight- or nine-fold and they are found in archea (thermosome), thermophilic bacteria (TF55) and in the eukaryotic cytosol (CTT). Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis.


Pssm-ID: 238189  Cd Length: 464  Bit Score: 135.63  E-value: 5.17e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121615408   1 TLLAQAIIREGLKNVTAGANPILIRNGIKTAVEKAVEEIQKISKP--VNGKEDIARVAAISAA-------DEKIGKLIAD 71
Cdd:cd00309    86 VVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVPidVEDREELLKVATTSLNsklvsggDDFLGELVVD 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121615408  72 AMEKVG------NEGVITVEESKSmGTELD--VVEGMQFDRGYVSAYmvtdtekMEAVLDNPLVLITDKKISNiqdllpl 143
Cdd:cd00309   166 AVLKVGkengdvDLGVIRVEKKKG-GSLEDseLVVGMVFDKGYLSPY-------MPKRLENAKILLLDCKLEY------- 230

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1121615408 144 leqivqagkklLIIADD-IEGEAMTTLVVNKL 174
Cdd:cd00309   231 -----------VVIAEKgIDDEALHYLAKLGI 251
Cpn60_TCP1 pfam00118
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ...
 2-176 4.46e-21

TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family and the TCP-1 (T-complex protein) family.


Pssm-ID: 395068 [Multi-domain]  Cd Length: 489  Bit Score: 89.57  E-value: 4.46e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121615408   2 LLAQAIIREGLKNVTAGANPILIRNGIKTAVEKAVE---EIQKISKPVNGKEDIARVAAISAA-------DEKIGKLIAD 71
Cdd:pfam00118  68 VLAGELLEEAEKLLAAGVHPTTIIEGYEKALEKALEildSIISIPVEDVDREDLLKVARTSLSskiisreSDFLAKLVVD 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121615408  72 AME---------KVGNEGVITVEESKSMGTELdvVEGMQFDRGYVSaymvtdtEKMEAVLDNPLVLITDKKISNIQD--- 139
Cdd:pfam00118 148 AVLaipkndgsfDLGNIGVVKILGGSLEDSEL--VDGVVLDKGPLH-------PDMPKRLENAKVLLLNCSLEYEKTetk 218

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1121615408 140 ---------------------LLPLLEQIVQAGKKLLIIADDIEGEAMTTLVVNKLRG 176
Cdd:pfam00118 219 atvvlsdaeqlerflkaeeeqILEIVEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMA 276
chaperonin_like cd03333
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ...
 49-173 1.86e-16

chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings, each composed of 7-9 subunits. There are 2 main chaperonin groups. The symmetry of type I is seven-fold and they are found in eubacteria (GroEL) and in organelles of eubacterial descent (hsp60 and RBP). The symmetry of type II is eight- or nine-fold and they are found in archea (thermosome), thermophilic bacteria (TF55) and in the eukaryotic cytosol (CTT). Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. This superfamily also contains related domains from Fab1-like phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinases that only contain the intermediate and apical domains.


Pssm-ID: 239449 [Multi-domain]  Cd Length: 209  Bit Score: 73.65  E-value: 1.86e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121615408  49 KEDIARVAAISAA------DEKIGKLIADAMEKVG------NEGVITVEESKSmGTELD--VVEGMQFDRGYVSAYmvtd 114
Cdd:cd03333     1 RELLLQVATTSLNsklsswDDFLGKLVVDAVLKVGpdnrmdDLGVIKVEKIPG-GSLEDseLVVGVVFDKGYASPY---- 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121615408 115 tekMEAVLDNPLVLITDKKISNiqdllplleqivqagkklLIIADD-IEGEAMTTLVVNK 173
Cdd:cd03333    76 ---MPKRLENAKILLLDCPLEY------------------VVIAEKgIDDLALHYLAKAG 114
 
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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