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Conserved domains on  [gi|2054259505|gb|QWT69108|]
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65 kDa heat shock protein, partial [Mycobacterium saskatchewanense]

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 ...
 1-136 1.75e-75

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: 233.48  E-value: 1.75e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054259505   1 IAKEIELEDPYEKIGAELVKEVAKKTDDVAGDGTTTATVLAQALVKEGLRNVAAGANPLALKRGIEKAVEKVTETLLKSA 80
Cdd:PRK00013   55 VAKEIELEDPFENMGAQLVKEVASKTNDVAGDGTTTATVLAQAIVREGLKNVAAGANPMDLKRGIDKAVEAAVEELKKIS 134

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2054259505  81 KDVETKEQIAATAAISA-GDQSIGDLIAEAMDKVGNEGVITVEESNTFGLQLELTEG 136
Cdd:PRK00013  135 KPVEDKEEIAQVATISAnGDEEIGKLIAEAMEKVGKEGVITVEESKGFETELEVVEG 191
 
Name Accession Description Interval E-value
groEL PRK00013
chaperonin GroEL; Reviewed
 1-136 1.75e-75

chaperonin GroEL; Reviewed


Pssm-ID: 234573  Cd Length: 542  Bit Score: 233.48  E-value: 1.75e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054259505   1 IAKEIELEDPYEKIGAELVKEVAKKTDDVAGDGTTTATVLAQALVKEGLRNVAAGANPLALKRGIEKAVEKVTETLLKSA 80
Cdd:PRK00013   55 VAKEIELEDPFENMGAQLVKEVASKTNDVAGDGTTTATVLAQAIVREGLKNVAAGANPMDLKRGIDKAVEAAVEELKKIS 134

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2054259505  81 KDVETKEQIAATAAISA-GDQSIGDLIAEAMDKVGNEGVITVEESNTFGLQLELTEG 136
Cdd:PRK00013  135 KPVEDKEEIAQVATISAnGDEEIGKLIAEAMEKVGKEGVITVEESKGFETELEVVEG 191
GroEL COG0459
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ...
 1-136 1.57e-65

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


Pssm-ID: 440227  Cd Length: 497  Bit Score: 206.47  E-value: 1.57e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054259505   1 IAKEIELEDPYEKIGAELVKEVAKKTDDVAGDGTTTATVLAQALVKEGLRNVAAGANPLALKRGIEKAVEKVTETLLKSA 80
Cdd:COG0459    55 IAKEIELEDPFENMGAQLVKEVASKTNDEAGDGTTTATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIA 134

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2054259505  81 KDVETKEQIAATAAISA-GDQSIGDLIAEAMDKVGNEGVITVEESNTFGLQLELTEG 136
Cdd:COG0459   135 KPVDDKEELAQVATISAnGDEEIGELIAEAMEKVGKDGVITVEEGKGLETELEVVEG 191
GroEL cd03344
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ...
 1-136 3.73e-65

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: 206.15  E-value: 3.73e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054259505   1 IAKEIELEDPYEKIGAELVKEVAKKTDDVAGDGTTTATVLAQALVKEGLRNVAAGANPLALKRGIEKAVEKVTETLLKSA 80
Cdd:cd03344    53 VAKEIELEDPFENMGAQLVKEVASKTNDVAGDGTTTATVLARAIIKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLS 132

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2054259505  81 KDVETKEQIAATAAISA-GDQSIGDLIAEAMDKVGNEGVITVEESNTFGLQLELTEG 136
Cdd:cd03344   133 KPVKTKEEIAQVATISAnGDEEIGELIAEAMEKVGKDGVITVEEGKTLETELEVVEG 189
GroEL TIGR02348
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ...
 1-136 3.05e-63

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: 200.98  E-value: 3.05e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054259505   1 IAKEIELEDPYEKIGAELVKEVAKKTDDVAGDGTTTATVLAQALVKEGLRNVAAGANPLALKRGIEKAVEKVTETLLKSA 80
Cdd:TIGR02348  54 VAKEIELEDKFENMGAQLVKEVASKTNDVAGDGTTTATVLAQAIVKEGLKNVAAGANPIELKRGIEKAVEAVVEELKKLS 133

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2054259505  81 KDVETKEQIAATAAISAG-DQSIGDLIAEAMDKVGNEGVITVEESNTFGLQLELTEG 136
Cdd:TIGR02348 134 KPVKGKKEIAQVATISANnDEEIGSLIAEAMEKVGKDGVITVEESKSLETELEVVEG 190
Cpn60_TCP1 pfam00118
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ...
 1-132 3.36e-18

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: 79.17  E-value: 3.36e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054259505   1 IAKEIELEDPYekigAELVKEVAKKTDDVAGDGTTTATVLAQALVKEGLRNVAAGANPLALKRGIEKAVEKVTETLLKSA 80
Cdd:pfam00118  34 ILKELEIQHPA----AKLLVEAAKAQDEEVGDGTTTVVVLAGELLEEAEKLLAAGVHPTTIIEGYEKALEKALEILDSII 109

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2054259505  81 K------DVETKEQIAATAA----ISAGDQSIGDLIAEA---------MDKVGNEGVITVEESNTFGLQLE 132
Cdd:pfam00118 110 SipvedvDREDLLKVARTSLsskiISRESDFLAKLVVDAvlaipkndgSFDLGNIGVVKILGGSLEDSELV 180
 
Name Accession Description Interval E-value
groEL PRK00013
chaperonin GroEL; Reviewed
 1-136 1.75e-75

chaperonin GroEL; Reviewed


Pssm-ID: 234573  Cd Length: 542  Bit Score: 233.48  E-value: 1.75e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054259505   1 IAKEIELEDPYEKIGAELVKEVAKKTDDVAGDGTTTATVLAQALVKEGLRNVAAGANPLALKRGIEKAVEKVTETLLKSA 80
Cdd:PRK00013   55 VAKEIELEDPFENMGAQLVKEVASKTNDVAGDGTTTATVLAQAIVREGLKNVAAGANPMDLKRGIDKAVEAAVEELKKIS 134

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2054259505  81 KDVETKEQIAATAAISA-GDQSIGDLIAEAMDKVGNEGVITVEESNTFGLQLELTEG 136
Cdd:PRK00013  135 KPVEDKEEIAQVATISAnGDEEIGKLIAEAMEKVGKEGVITVEESKGFETELEVVEG 191
groEL PRK12849
chaperonin GroEL; Reviewed
 1-136 6.59e-67

chaperonin GroEL; Reviewed


Pssm-ID: 237230  Cd Length: 542  Bit Score: 211.20  E-value: 6.59e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054259505   1 IAKEIELEDPYEKIGAELVKEVAKKTDDVAGDGTTTATVLAQALVKEGLRNVAAGANPLALKRGIEKAVEKVTETLLKSA 80
Cdd:PRK12849   55 IAKEIELEDPFENLGAQLVKEVASKTNDVAGDGTTTATVLAQALVQEGLKNVAAGANPMDLKRGIDKAVEAVVEELKALA 134

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2054259505  81 KDVETKEQIAATAAISA-GDQSIGDLIAEAMDKVGNEGVITVEESNTFGLQLELTEG 136
Cdd:PRK12849  135 RPVSGSEEIAQVATISAnGDEEIGELIAEAMEKVGKDGVITVEESKTLETELEVTEG 191
GroEL COG0459
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ...
 1-136 1.57e-65

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


Pssm-ID: 440227  Cd Length: 497  Bit Score: 206.47  E-value: 1.57e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054259505   1 IAKEIELEDPYEKIGAELVKEVAKKTDDVAGDGTTTATVLAQALVKEGLRNVAAGANPLALKRGIEKAVEKVTETLLKSA 80
Cdd:COG0459    55 IAKEIELEDPFENMGAQLVKEVASKTNDEAGDGTTTATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIA 134

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2054259505  81 KDVETKEQIAATAAISA-GDQSIGDLIAEAMDKVGNEGVITVEESNTFGLQLELTEG 136
Cdd:COG0459   135 KPVDDKEELAQVATISAnGDEEIGELIAEAMEKVGKDGVITVEEGKGLETELEVVEG 191
GroEL cd03344
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ...
 1-136 3.73e-65

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: 206.15  E-value: 3.73e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054259505   1 IAKEIELEDPYEKIGAELVKEVAKKTDDVAGDGTTTATVLAQALVKEGLRNVAAGANPLALKRGIEKAVEKVTETLLKSA 80
Cdd:cd03344    53 VAKEIELEDPFENMGAQLVKEVASKTNDVAGDGTTTATVLARAIIKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLS 132

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2054259505  81 KDVETKEQIAATAAISA-GDQSIGDLIAEAMDKVGNEGVITVEESNTFGLQLELTEG 136
Cdd:cd03344   133 KPVKTKEEIAQVATISAnGDEEIGELIAEAMEKVGKDGVITVEEGKTLETELEVVEG 189
groEL PRK12850
chaperonin GroEL; Reviewed
 1-136 3.11e-64

chaperonin GroEL; Reviewed


Pssm-ID: 237231  Cd Length: 544  Bit Score: 204.18  E-value: 3.11e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054259505   1 IAKEIELEDPYEKIGAELVKEVAKKTDDVAGDGTTTATVLAQALVKEGLRNVAAGANPLALKRGIEKAVEKVTETLLKSA 80
Cdd:PRK12850   56 VAKEIELEDKFENMGAQMVKEVASKTNDLAGDGTTTATVLAQAIVREGAKLVAAGMNPMDLKRGIDLAVAAVVDELKKIA 135

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2054259505  81 KDVETKEQIAATAAISA-GDQSIGDLIAEAMDKVGNEGVITVEESNTFGLQLELTEG 136
Cdd:PRK12850  136 KKVTSSKEIAQVATISAnGDESIGEMIAEAMDKVGKEGVITVEEAKTLGTELDVVEG 192
GroEL TIGR02348
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ...
 1-136 3.05e-63

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: 200.98  E-value: 3.05e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054259505   1 IAKEIELEDPYEKIGAELVKEVAKKTDDVAGDGTTTATVLAQALVKEGLRNVAAGANPLALKRGIEKAVEKVTETLLKSA 80
Cdd:TIGR02348  54 VAKEIELEDKFENMGAQLVKEVASKTNDVAGDGTTTATVLAQAIVKEGLKNVAAGANPIELKRGIEKAVEAVVEELKKLS 133

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2054259505  81 KDVETKEQIAATAAISAG-DQSIGDLIAEAMDKVGNEGVITVEESNTFGLQLELTEG 136
Cdd:TIGR02348 134 KPVKGKKEIAQVATISANnDEEIGSLIAEAMEKVGKDGVITVEESKSLETELEVVEG 190
groEL PRK12851
chaperonin GroEL; Reviewed
 1-136 1.79e-56

chaperonin GroEL; Reviewed


Pssm-ID: 171770  Cd Length: 541  Bit Score: 183.79  E-value: 1.79e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054259505   1 IAKEIELEDPYEKIGAELVKEVAKKTDDVAGDGTTTATVLAQALVKEGLRNVAAGANPLALKRGIEKAVEKVTETLLKSA 80
Cdd:PRK12851   56 IAKEIELEDKFENMGAQMVREVASKTNDVAGDGTTTATVLAQAIVREGAKAVAAGANPMDLKRGIDRAVAAVVEELKANA 135

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2054259505  81 KDVETKEQIAATAAISA-GDQSIGDLIAEAMDKVGNEGVITVEESNTFGLQLELTEG 136
Cdd:PRK12851  136 RPVTTNAEIAQVATISAnGDAEIGRLVAEAMEKVGNEGVITVEESKTAETELEVVEG 192
groEL CHL00093
chaperonin GroEL
 1-136 1.94e-50

chaperonin GroEL


Pssm-ID: 177025  Cd Length: 529  Bit Score: 167.59  E-value: 1.94e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054259505   1 IAKEIELEDPYEKIGAELVKEVAKKTDDVAGDGTTTATVLAQALVKEGLRNVAAGANPLALKRGIEKAVEKVTETLLKSA 80
Cdd:CHL00093   55 IAKEIELEDHIENTGVALIRQAASKTNDVAGDGTTTATVLAYAIVKQGMKNVAAGANPISLKRGIEKATQYVVSQIAEYA 134

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2054259505  81 KDVETKEQIAATAAISAG-DQSIGDLIAEAMDKVGNEGVITVEESNTFGLQLELTEG 136
Cdd:CHL00093  135 RPVEDIQAITQVASISAGnDEEVGSMIADAIEKVGREGVISLEEGKSTVTELEITEG 191
PTZ00114 PTZ00114
Heat shock protein 60; Provisional
 1-136 6.77e-49

Heat shock protein 60; Provisional


Pssm-ID: 185455  Cd Length: 555  Bit Score: 163.93  E-value: 6.77e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054259505   1 IAKEIELEDPYEKIGAELVKEVAKKTDDVAGDGTTTATVLAQALVKEGLRNVAAGANPLALKRGIEKAVEKVTETLLKSA 80
Cdd:PTZ00114   67 VAKAIEFSDRFENVGAQLIRQVASKTNDKAGDGTTTATILARAIFREGCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQS 146

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2054259505  81 KDVETKEQIAATAAISA-GDQSIGDLIAEAMDKVGNEGVITVEESNTFGLQLELTEG 136
Cdd:PTZ00114  147 RPVKTKEDILNVATISAnGDVEIGSLIADAMDKVGKDGTITVEDGKTLEDELEVVEG 203
groEL PRK12852
chaperonin GroEL; Reviewed
 1-136 8.18e-47

chaperonin GroEL; Reviewed


Pssm-ID: 237232  Cd Length: 545  Bit Score: 158.47  E-value: 8.18e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054259505   1 IAKEIELEDPYEKIGAELVKEVAKKTDDVAGDGTTTATVLAQALVKEGLRNVAAGANPLALKRGIEKAVEKVTETLLKSA 80
Cdd:PRK12852   56 VAKEIELEDKFENMGAQMVREVASKTNDLAGDGTTTATVLAQAIVREGAKAVAAGMNPMDLKRGIDIAVAAVVKDIEKRA 135

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2054259505  81 KDVETKEQIAATAAISA-GDQSIGDLIAEAMDKVGNEGVITVEESNTFGLQLELTEG 136
Cdd:PRK12852  136 KPVASSAEIAQVGTISAnGDAAIGKMIAQAMQKVGNEGVITVEENKSLETEVDIVEG 192
PRK14104 PRK14104
chaperonin GroEL; Provisional
 1-136 7.41e-41

chaperonin GroEL; Provisional


Pssm-ID: 172594  Cd Length: 546  Bit Score: 142.48  E-value: 7.41e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054259505   1 IAKEIELEDPYEKIGAELVKEVAKKTDDVAGDGTTTATVLAQALVKEGLRNVAAGANPLALKRGIEKAVEKVTETLLKSA 80
Cdd:PRK14104   56 VAKEIELEDKFENMGAQMVREVASKSADAAGDGTTTATVLAQAIVREGAKSVAAGMNPMDLKRGIDLAVEAVVADLVKNS 135

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2054259505  81 KDVETKEQIAATAAISA-GDQSIGDLIAEAMDKVGNEGVITVEESNTFGLQLELTEG 136
Cdd:PRK14104  136 KKVTSNDEIAQVGTISAnGDAEIGKFLADAMKKVGNEGVITVEEAKSLETELDVVEG 192
chaperonin_type_I_II cd00309
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ...
 1-126 3.45e-36

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: 128.70  E-value: 3.45e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054259505   1 IAKEIELEDPyekiGAELVKEVAKKTDDVAGDGTTTATVLAQALVKEGLRNVAAGANPLALKRGIEKAVEKVTETLLKSA 80
Cdd:cd00309    53 ILKEIEVEHP----AAKLLVEVAKSQDDEVGDGTTTVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIA 128

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2054259505  81 K--DVETKEQIAATAAISAG-------DQSIGDLIAEAMDKVG------NEGVITVEESNT 126
Cdd:cd00309   129 VpiDVEDREELLKVATTSLNsklvsggDDFLGELVVDAVLKVGkengdvDLGVIRVEKKKG 189
PLN03167 PLN03167
Chaperonin-60 beta subunit; Provisional
 1-136 5.56e-36

Chaperonin-60 beta subunit; Provisional


Pssm-ID: 215611 [Multi-domain]  Cd Length: 600  Bit Score: 129.66  E-value: 5.56e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054259505   1 IAKEIELEDPYEKIGAELVKEVAKKTDDVAGDGTTTATVLAQALVKEGLRNVAAGANPLALKRGIEKAVEKVTETLLKSA 80
Cdd:PLN03167  111 VAKEVELEDPVENIGAKLVRQAAAKTNDLAGDGTTTSVVLAQGLIAEGVKVVAAGANPVQITRGIEKTAKALVKELKKMS 190

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2054259505  81 KDVETKEqIAATAAISAGDQ-SIGDLIAEAMDKVGNEGVITVEESNTFGLQLELTEG 136
Cdd:PLN03167  191 KEVEDSE-LADVAAVSAGNNyEVGNMIAEAMSKVGRKGVVTLEEGKSAENNLYVVEG 246
Cpn60_TCP1 pfam00118
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ...
 1-132 3.36e-18

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: 79.17  E-value: 3.36e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054259505   1 IAKEIELEDPYekigAELVKEVAKKTDDVAGDGTTTATVLAQALVKEGLRNVAAGANPLALKRGIEKAVEKVTETLLKSA 80
Cdd:pfam00118  34 ILKELEIQHPA----AKLLVEAAKAQDEEVGDGTTTVVVLAGELLEEAEKLLAAGVHPTTIIEGYEKALEKALEILDSII 109

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2054259505  81 K------DVETKEQIAATAA----ISAGDQSIGDLIAEA---------MDKVGNEGVITVEESNTFGLQLE 132
Cdd:pfam00118 110 SipvedvDREDLLKVARTSLsskiISRESDFLAKLVVDAvlaipkndgSFDLGNIGVVKILGGSLEDSELV 180
cpn60 cd03343
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ...
 1-108 2.13e-09

cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. Archaeal cpn60 (thermosome), together with TF55 from thermophilic bacteria and the eukaryotic cytosol chaperonin (CTT), belong to the type II group of chaperonins. Cpn60 consists of two stacked octameric rings, which are composed of one or two different subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis.


Pssm-ID: 239459 [Multi-domain]  Cd Length: 517  Bit Score: 54.19  E-value: 2.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054259505   1 IAKEIELEDPyekiGAELVKEVAKKTDDVAGDGTTTATVLAQALVKEGLRNVAAGANPLALKRGIEKAVEKVTETLLKSA 80
Cdd:cd03343    60 ILKEMDIEHP----AAKMLVEVAKTQDEEVGDGTTTAVVLAGELLEKAEDLLDQNIHPTVIIEGYRLAAEKALELLDEIA 135

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2054259505  81 KDV-----ETKEQIAATAAISAGDQSIGDLIAE 108
Cdd:cd03343   136 IKVdpddkDTLRKIAKTSLTGKGAEAAKDKLAD 168
chap_CCT_epsi TIGR02343
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ...
 1-133 1.90e-07

T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT epsilon chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.


Pssm-ID: 274084 [Multi-domain]  Cd Length: 532  Bit Score: 48.65  E-value: 1.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054259505   1 IAKEIELEDPYekigAELVKEVAKKTDDVAGDGTTTATVLAQALVKEGLRNVAAGANPLALKRGIEK----AVEKVTETL 76
Cdd:TIGR02343  72 ILSQMDVDNQI----AKLMVELSKSQDDEIGDGTTGVVVLAGALLEQAEELLDKGIHPIKIADGFEEaariAVEHLEEIS 147

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2054259505  77 LKSAKDVETKEQIAATAAISAGDQsIGDLIAEAMDKVGNEGVITVEESNTFGLQLEL 133
Cdd:TIGR02343 148 DEISADNNNREPLIQAAKTSLGSK-IVSKCHRRFAEIAVDAVLNVADMERRDVDFDL 203
TCP1_beta cd03336
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ...
 1-82 4.29e-07

TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.


Pssm-ID: 239452 [Multi-domain]  Cd Length: 517  Bit Score: 47.32  E-value: 4.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054259505   1 IAKEIELEDPYEKIgaeLVkEVAKKTDDVAGDGTTTATVLAQALVKEGLRNVAAGANPLALKRGIEKAVEKVTETLLKSA 80
Cdd:cd03336    60 ILKSIGVDNPAAKV---LV-DISKVQDDEVGDGTTSVTVLAAELLREAEKLVAQKIHPQTIIEGYRMATAAAREALLSSA 135


                  ..
gi 2054259505  81 KD 82
Cdd:cd03336   136 VD 137
PTZ00212 PTZ00212
T-complex protein 1 subunit beta; Provisional
 1-82 5.26e-07

T-complex protein 1 subunit beta; Provisional


Pssm-ID: 185514  Cd Length: 533  Bit Score: 47.33  E-value: 5.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054259505   1 IAKEIELEDPYEKIgaeLVkEVAKKTDDVAGDGTTTATVLAQALVKEGLRNVAAGANPLALKRGIEKAVEKVTETLLKSA 80
Cdd:PTZ00212   72 ILKSVWLDNPAAKI---LV-DISKTQDEEVGDGTTSVVVLAGELLREAEKLLDQKIHPQTIIEGWRMALDVARKALEEIA 147


                  ..
gi 2054259505  81 KD 82
Cdd:PTZ00212  148 FD 149
TCP1_epsilon cd03339
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ...
 16-88 3.62e-05

TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.


Pssm-ID: 239455  Cd Length: 526  Bit Score: 41.90  E-value: 3.62e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2054259505  16 AELVKEVAKKTDDVAGDGTTTATVLAQALVKEGLRNVAAGANPLALKRGIEKAVEKVTETLLKSAKDVETKEQ 88
Cdd:cd03339    79 AKLLVELSKSQDDEIGDGTTGVVVLAGALLEQAEKLLDRGIHPIRIADGYEQACKIAVEHLEEIADKIEFSPD 151
TCP1_eta cd03340
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ...
 16-93 4.13e-05

TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.


Pssm-ID: 239456 [Multi-domain]  Cd Length: 522  Bit Score: 41.89  E-value: 4.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054259505  16 AELVKEVAKKTDDVAGDGTTTATVLAQALVKEGLRNVAAGANPLALKRGIEKAVEKVTETLLKSAKDVETK--------- 86
Cdd:cd03340    72 AKTLVDIAKSQDAEVGDGTTSVVVLAGEFLKEAKPFIEDGVHPQIIIRGYRKALQLAIEKIKEIAVNIDKEdkeeqrell 151


                  ....*..
gi 2054259505  87 EQIAATA 93
Cdd:cd03340   152 EKCAATA 158
chap_CCT_beta TIGR02341
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ...
 1-82 1.35e-04

T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT beta chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.


Pssm-ID: 274082  Cd Length: 519  Bit Score: 40.23  E-value: 1.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054259505   1 IAKEIELEDPyekiGAELVKEVAKKTDDVAGDGTTTATVLAQALVKEGLRNVAAGANPLALKRGIEKAVEKVTETLLKSA 80
Cdd:TIGR02341  61 ILKSIGVDNP----AAKVLVDMSKVQDDEVGDGTTSVTVLAAELLREAEKLINQKIHPQTIIAGYREATKAARDALLKSA 136


                  ..
gi 2054259505  81 KD 82
Cdd:TIGR02341 137 VD 138
chap_CCT_zeta TIGR02347
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ...
 16-110 4.57e-04

T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT zeta chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.


Pssm-ID: 274088 [Multi-domain]  Cd Length: 531  Bit Score: 38.95  E-value: 4.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054259505  16 AELVKEVAKKTDDVAGDGTTTATVLAQALVKEGLRNVAAGANPLALKRGIEKAVEKVTETLLK------SAKDVETKEQI 89
Cdd:TIGR02347  72 ASMIARAATAQDDITGDGTTSTVLLIGELLKQAERYILEGVHPRIITEGFEIARKEALQFLDKfkvkkeDEVDREFLLNV 151

                          90       100
                  ....*....|....*....|.
gi 2054259505  90 AATAAISAGDQSIGDLIAEAM 110
Cdd:TIGR02347 152 ARTSLRTKLPADLADQLTEIV 172
TCP1_delta cd03338
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ...
 1-113 7.49e-04

TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.


Pssm-ID: 239454 [Multi-domain]  Cd Length: 515  Bit Score: 38.04  E-value: 7.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054259505   1 IAKEIELEDPYEKIGAELvkevaKKTDDV-AGDGTTTATVLAQALVKEGLRNVAAGANPLALKRGIEKAVEKVTETLLKS 79
Cdd:cd03338    53 ILKQMSVLHPAAKMLVEL-----SKAQDIeAGDGTTSVVVLAGALLSACESLLKKGIHPTVISESFQIAAKKAVEILDSM 127

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2054259505  80 AKDVETKE-----QIAATAAISAGDQSIGDLIAE-AMDKV 113
Cdd:cd03338   128 SIPVDLNDresliKSATTSLNSKVVSQYSSLLAPiAVDAV 167
chap_CCT_delta TIGR02342
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ...
 16-88 1.09e-03

T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT delta chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.


Pssm-ID: 274083  Cd Length: 517  Bit Score: 37.84  E-value: 1.09e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2054259505  16 AELVKEVAKKTDDVAGDGTTTATVLAQALVKEGLRNVAAGANPLALKRGIEKAVEKVTETLLKSAKDVETKEQ 88
Cdd:TIGR02342  65 AKMLVELSKAQDIEAGDGTTSVVILAGALLGACERLLNKGIHPTIISESFQSAADEAIKILDEMSIPVDLSDR 137
TCP1_zeta cd03342
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ...
 16-109 1.38e-03

TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.


Pssm-ID: 239458 [Multi-domain]  Cd Length: 484  Bit Score: 37.24  E-value: 1.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054259505  16 AELVKEVAKKTDDVAGDGTTTATVLAQALVKEGLRNVAAGANPLALKRGIEKAVEKVTETL------LKSAKDVETKEQI 89
Cdd:cd03342    68 ASMIARAATAQDDITGDGTTSNVLLIGELLKQAERYIQEGVHPRIITEGFELAKNKALKFLesfkvpVEIDTDRELLLSV 147

                          90       100
                  ....*....|....*....|
gi 2054259505  90 AATAAISAGDQSIGDLIAEA 109
Cdd:cd03342   148 ARTSLRTKLHADLADQLTEI 167
TCP1_theta cd03341
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ...
 1-109 1.47e-03

TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.


Pssm-ID: 239457 [Multi-domain]  Cd Length: 472  Bit Score: 37.20  E-value: 1.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054259505   1 IAKEIELEDPyekiGAELVKEVAKKTDDVAGDGTTTATVLAQALVKEGLRNVAAGANPLALKRGIEKAVEKVTETL---- 76
Cdd:cd03341    53 ILRELEVQHP----AAKLLVMASQMQEEEIGDGTNLVVVLAGELLEKAEELLRMGLHPSEIIEGYEKALKKALEILeelv 128

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2054259505  77 LKSAKDVETKEQIAAT--AAISAGDQS----IGDLIAEA 109
Cdd:cd03341   129 VYKIEDLRNKEEVSKAlkTAIASKQYGnedfLSPLVAEA 167
 
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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