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Conserved domains on  [gi|673058937|gb|AIK25077|]
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60 kDa chaperonin 2 GroEL2, partial [Mycolicibacter kumamotonensis]

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 ...
 2-142 3.03e-80

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: 245.80  E-value: 3.03e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673058937   2 VSIAKEIELEDPYEKIGAELVKEVAKKTDDVAGDGTTTATVLAQALVKEGLRNVAAGANPLALKRGIEKAVEKVSETLLK 81
Cdd:PRK00013  53 VTVAKEIELEDPFENMGAQLVKEVASKTNDVAGDGTTTATVLAQAIVREGLKNVAAGANPMDLKRGIDKAVEAAVEELKK 132

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 673058937  82 DAKEVETKEQIAATAGISA-GDQSIGDLIAEAMDKVGNEGVITVEESNTFGLQLELTEGMRF 142
Cdd:PRK00013 133 ISKPVEDKEEIAQVATISAnGDEEIGKLIAEAMEKVGKEGVITVEESKGFETELEVVEGMQF 194
 
Name Accession Description Interval E-value
groEL PRK00013
chaperonin GroEL; Reviewed
 2-142 3.03e-80

chaperonin GroEL; Reviewed


Pssm-ID: 234573  Cd Length: 542  Bit Score: 245.80  E-value: 3.03e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673058937   2 VSIAKEIELEDPYEKIGAELVKEVAKKTDDVAGDGTTTATVLAQALVKEGLRNVAAGANPLALKRGIEKAVEKVSETLLK 81
Cdd:PRK00013  53 VTVAKEIELEDPFENMGAQLVKEVASKTNDVAGDGTTTATVLAQAIVREGLKNVAAGANPMDLKRGIDKAVEAAVEELKK 132

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 673058937  82 DAKEVETKEQIAATAGISA-GDQSIGDLIAEAMDKVGNEGVITVEESNTFGLQLELTEGMRF 142
Cdd:PRK00013 133 ISKPVEDKEEIAQVATISAnGDEEIGKLIAEAMEKVGKEGVITVEESKGFETELEVVEGMQF 194
GroEL cd03344
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ...
 2-142 2.29e-69

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: 217.32  E-value: 2.29e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673058937   2 VSIAKEIELEDPYEKIGAELVKEVAKKTDDVAGDGTTTATVLAQALVKEGLRNVAAGANPLALKRGIEKAVEKVSETLLK 81
Cdd:cd03344   51 VTVAKEIELEDPFENMGAQLVKEVASKTNDVAGDGTTTATVLARAIIKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKK 130

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 673058937  82 DAKEVETKEQIAATAGISA-GDQSIGDLIAEAMDKVGNEGVITVEESNTFGLQLELTEGMRF 142
Cdd:cd03344  131 LSKPVKTKEEIAQVATISAnGDEEIGELIAEAMEKVGKDGVITVEEGKTLETELEVVEGMQF 192
GroEL COG0459
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ...
 2-142 5.94e-69

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


Pssm-ID: 440227  Cd Length: 497  Bit Score: 215.71  E-value: 5.94e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673058937   2 VSIAKEIELEDPYEKIGAELVKEVAKKTDDVAGDGTTTATVLAQALVKEGLRNVAAGANPLALKRGIEKAVEKVSETLLK 81
Cdd:COG0459   53 VTIAKEIELEDPFENMGAQLVKEVASKTNDEAGDGTTTATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKK 132

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 673058937  82 DAKEVETKEQIAATAGISA-GDQSIGDLIAEAMDKVGNEGVITVEESNTFGLQLELTEGMRF 142
Cdd:COG0459  133 IAKPVDDKEELAQVATISAnGDEEIGELIAEAMEKVGKDGVITVEEGKGLETELEVVEGMQF 194
GroEL TIGR02348
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ...
 2-142 3.62e-67

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: 211.77  E-value: 3.62e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673058937    2 VSIAKEIELEDPYEKIGAELVKEVAKKTDDVAGDGTTTATVLAQALVKEGLRNVAAGANPLALKRGIEKAVEKVSETLLK 81
Cdd:TIGR02348  52 VTVAKEIELEDKFENMGAQLVKEVASKTNDVAGDGTTTATVLAQAIVKEGLKNVAAGANPIELKRGIEKAVEAVVEELKK 131

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 673058937   82 DAKEVETKEQIAATAGISAG-DQSIGDLIAEAMDKVGNEGVITVEESNTFGLQLELTEGMRF 142
Cdd:TIGR02348 132 LSKPVKGKKEIAQVATISANnDEEIGSLIAEAMEKVGKDGVITVEESKSLETELEVVEGMQF 193
Cpn60_TCP1 pfam00118
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ...
 2-142 1.51e-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: 80.71  E-value: 1.51e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673058937    2 VSIAKEIELEDPYekigAELVKEVAKKTDDVAGDGTTTATVLAQALVKEGLRNVAAGANPLALKRGIEKAVEKVSEtLLK 81
Cdd:pfam00118  32 ATILKELEIQHPA----AKLLVEAAKAQDEEVGDGTTTVVVLAGELLEEAEKLLAAGVHPTTIIEGYEKALEKALE-ILD 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673058937   82 DAKEVETKE-------QIAATA----GISAGDQSIGDLIAEA---------MDKVGNEGVITVEESNTFGLQLEltEGMR 141
Cdd:pfam00118 107 SIISIPVEDvdredllKVARTSlsskIISRESDFLAKLVVDAvlaipkndgSFDLGNIGVVKILGGSLEDSELV--DGVV 184


                  .
gi 673058937  142 F 142
Cdd:pfam00118 185 L 185
 
Name Accession Description Interval E-value
groEL PRK00013
chaperonin GroEL; Reviewed
 2-142 3.03e-80

chaperonin GroEL; Reviewed


Pssm-ID: 234573  Cd Length: 542  Bit Score: 245.80  E-value: 3.03e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673058937   2 VSIAKEIELEDPYEKIGAELVKEVAKKTDDVAGDGTTTATVLAQALVKEGLRNVAAGANPLALKRGIEKAVEKVSETLLK 81
Cdd:PRK00013  53 VTVAKEIELEDPFENMGAQLVKEVASKTNDVAGDGTTTATVLAQAIVREGLKNVAAGANPMDLKRGIDKAVEAAVEELKK 132

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 673058937  82 DAKEVETKEQIAATAGISA-GDQSIGDLIAEAMDKVGNEGVITVEESNTFGLQLELTEGMRF 142
Cdd:PRK00013 133 ISKPVEDKEEIAQVATISAnGDEEIGKLIAEAMEKVGKEGVITVEESKGFETELEVVEGMQF 194
groEL PRK12849
chaperonin GroEL; Reviewed
 2-142 3.63e-71

chaperonin GroEL; Reviewed


Pssm-ID: 237230  Cd Length: 542  Bit Score: 222.37  E-value: 3.63e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673058937   2 VSIAKEIELEDPYEKIGAELVKEVAKKTDDVAGDGTTTATVLAQALVKEGLRNVAAGANPLALKRGIEKAVEKVSETLLK 81
Cdd:PRK12849  53 VSIAKEIELEDPFENLGAQLVKEVASKTNDVAGDGTTTATVLAQALVQEGLKNVAAGANPMDLKRGIDKAVEAVVEELKA 132

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 673058937  82 DAKEVETKEQIAATAGISA-GDQSIGDLIAEAMDKVGNEGVITVEESNTFGLQLELTEGMRF 142
Cdd:PRK12849 133 LARPVSGSEEIAQVATISAnGDEEIGELIAEAMEKVGKDGVITVEESKTLETELEVTEGMQF 194
GroEL cd03344
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ...
 2-142 2.29e-69

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: 217.32  E-value: 2.29e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673058937   2 VSIAKEIELEDPYEKIGAELVKEVAKKTDDVAGDGTTTATVLAQALVKEGLRNVAAGANPLALKRGIEKAVEKVSETLLK 81
Cdd:cd03344   51 VTVAKEIELEDPFENMGAQLVKEVASKTNDVAGDGTTTATVLARAIIKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKK 130

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 673058937  82 DAKEVETKEQIAATAGISA-GDQSIGDLIAEAMDKVGNEGVITVEESNTFGLQLELTEGMRF 142
Cdd:cd03344  131 LSKPVKTKEEIAQVATISAnGDEEIGELIAEAMEKVGKDGVITVEEGKTLETELEVVEGMQF 192
GroEL COG0459
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ...
 2-142 5.94e-69

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


Pssm-ID: 440227  Cd Length: 497  Bit Score: 215.71  E-value: 5.94e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673058937   2 VSIAKEIELEDPYEKIGAELVKEVAKKTDDVAGDGTTTATVLAQALVKEGLRNVAAGANPLALKRGIEKAVEKVSETLLK 81
Cdd:COG0459   53 VTIAKEIELEDPFENMGAQLVKEVASKTNDEAGDGTTTATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKK 132

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 673058937  82 DAKEVETKEQIAATAGISA-GDQSIGDLIAEAMDKVGNEGVITVEESNTFGLQLELTEGMRF 142
Cdd:COG0459  133 IAKPVDDKEELAQVATISAnGDEEIGELIAEAMEKVGKDGVITVEEGKGLETELEVVEGMQF 194
groEL PRK12850
chaperonin GroEL; Reviewed
 2-142 1.17e-68

chaperonin GroEL; Reviewed


Pssm-ID: 237231  Cd Length: 544  Bit Score: 216.12  E-value: 1.17e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673058937   2 VSIAKEIELEDPYEKIGAELVKEVAKKTDDVAGDGTTTATVLAQALVKEGLRNVAAGANPLALKRGIEKAVEKVSETLLK 81
Cdd:PRK12850  54 VTVAKEIELEDKFENMGAQMVKEVASKTNDLAGDGTTTATVLAQAIVREGAKLVAAGMNPMDLKRGIDLAVAAVVDELKK 133

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 673058937  82 DAKEVETKEQIAATAGISA-GDQSIGDLIAEAMDKVGNEGVITVEESNTFGLQLELTEGMRF 142
Cdd:PRK12850 134 IAKKVTSSKEIAQVATISAnGDESIGEMIAEAMDKVGKEGVITVEEAKTLGTELDVVEGMQF 195
GroEL TIGR02348
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ...
 2-142 3.62e-67

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: 211.77  E-value: 3.62e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673058937    2 VSIAKEIELEDPYEKIGAELVKEVAKKTDDVAGDGTTTATVLAQALVKEGLRNVAAGANPLALKRGIEKAVEKVSETLLK 81
Cdd:TIGR02348  52 VTVAKEIELEDKFENMGAQLVKEVASKTNDVAGDGTTTATVLAQAIVKEGLKNVAAGANPIELKRGIEKAVEAVVEELKK 131

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 673058937   82 DAKEVETKEQIAATAGISAG-DQSIGDLIAEAMDKVGNEGVITVEESNTFGLQLELTEGMRF 142
Cdd:TIGR02348 132 LSKPVKGKKEIAQVATISANnDEEIGSLIAEAMEKVGKDGVITVEESKSLETELEVVEGMQF 193
groEL PRK12851
chaperonin GroEL; Reviewed
 2-142 3.65e-61

chaperonin GroEL; Reviewed


Pssm-ID: 171770  Cd Length: 541  Bit Score: 196.50  E-value: 3.65e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673058937   2 VSIAKEIELEDPYEKIGAELVKEVAKKTDDVAGDGTTTATVLAQALVKEGLRNVAAGANPLALKRGIEKAVEKVSETLLK 81
Cdd:PRK12851  54 VTIAKEIELEDKFENMGAQMVREVASKTNDVAGDGTTTATVLAQAIVREGAKAVAAGANPMDLKRGIDRAVAAVVEELKA 133

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 673058937  82 DAKEVETKEQIAATAGISA-GDQSIGDLIAEAMDKVGNEGVITVEESNTFGLQLELTEGMRF 142
Cdd:PRK12851 134 NARPVTTNAEIAQVATISAnGDAEIGRLVAEAMEKVGNEGVITVEESKTAETELEVVEGMQF 195
groEL CHL00093
chaperonin GroEL
 2-142 3.78e-54

chaperonin GroEL


Pssm-ID: 177025  Cd Length: 529  Bit Score: 177.99  E-value: 3.78e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673058937   2 VSIAKEIELEDPYEKIGAELVKEVAKKTDDVAGDGTTTATVLAQALVKEGLRNVAAGANPLALKRGIEKAVEKVSETLLK 81
Cdd:CHL00093  53 VTIAKEIELEDHIENTGVALIRQAASKTNDVAGDGTTTATVLAYAIVKQGMKNVAAGANPISLKRGIEKATQYVVSQIAE 132

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 673058937  82 DAKEVETKEQIAATAGISAG-DQSIGDLIAEAMDKVGNEGVITVEESNTFGLQLELTEGMRF 142
Cdd:CHL00093 133 YARPVEDIQAITQVASISAGnDEEVGSMIADAIEKVGREGVISLEEGKSTVTELEITEGMRF 194
PTZ00114 PTZ00114
Heat shock protein 60; Provisional
 2-142 4.02e-52

Heat shock protein 60; Provisional


Pssm-ID: 185455  Cd Length: 555  Bit Score: 172.79  E-value: 4.02e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673058937   2 VSIAKEIELEDPYEKIGAELVKEVAKKTDDVAGDGTTTATVLAQALVKEGLRNVAAGANPLALKRGIEKAVEKVSETLLK 81
Cdd:PTZ00114  65 VTVAKAIEFSDRFENVGAQLIRQVASKTNDKAGDGTTTATILARAIFREGCKAVAAGLNPMDLKRGIDLAVKVVLESLKE 144

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 673058937  82 DAKEVETKEQIAATAGISA-GDQSIGDLIAEAMDKVGNEGVITVEESNTFGLQLELTEGMRF 142
Cdd:PTZ00114 145 QSRPVKTKEDILNVATISAnGDVEIGSLIADAMDKVGKDGTITVEDGKTLEDELEVVEGMSF 206
groEL PRK12852
chaperonin GroEL; Reviewed
 2-142 2.29e-50

chaperonin GroEL; Reviewed


Pssm-ID: 237232  Cd Length: 545  Bit Score: 168.10  E-value: 2.29e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673058937   2 VSIAKEIELEDPYEKIGAELVKEVAKKTDDVAGDGTTTATVLAQALVKEGLRNVAAGANPLALKRGIEKAVEKVSETLLK 81
Cdd:PRK12852  54 VTVAKEIELEDKFENMGAQMVREVASKTNDLAGDGTTTATVLAQAIVREGAKAVAAGMNPMDLKRGIDIAVAAVVKDIEK 133

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 673058937  82 DAKEVETKEQIAATAGISA-GDQSIGDLIAEAMDKVGNEGVITVEESNTFGLQLELTEGMRF 142
Cdd:PRK12852 134 RAKPVASSAEIAQVGTISAnGDAAIGKMIAQAMQKVGNEGVITVEENKSLETEVDIVEGMKF 195
PRK14104 PRK14104
chaperonin GroEL; Provisional
 2-142 1.07e-43

chaperonin GroEL; Provisional


Pssm-ID: 172594  Cd Length: 546  Bit Score: 150.57  E-value: 1.07e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673058937   2 VSIAKEIELEDPYEKIGAELVKEVAKKTDDVAGDGTTTATVLAQALVKEGLRNVAAGANPLALKRGIEKAVEKVSETLLK 81
Cdd:PRK14104  54 VTVAKEIELEDKFENMGAQMVREVASKSADAAGDGTTTATVLAQAIVREGAKSVAAGMNPMDLKRGIDLAVEAVVADLVK 133

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 673058937  82 DAKEVETKEQIAATAGISA-GDQSIGDLIAEAMDKVGNEGVITVEESNTFGLQLELTEGMRF 142
Cdd:PRK14104 134 NSKKVTSNDEIAQVGTISAnGDAEIGKFLADAMKKVGNEGVITVEEAKSLETELDVVEGMQF 195
PLN03167 PLN03167
Chaperonin-60 beta subunit; Provisional
 2-142 8.78e-39

Chaperonin-60 beta subunit; Provisional


Pssm-ID: 215611 [Multi-domain]  Cd Length: 600  Bit Score: 137.75  E-value: 8.78e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673058937   2 VSIAKEIELEDPYEKIGAELVKEVAKKTDDVAGDGTTTATVLAQALVKEGLRNVAAGANPLALKRGIEKAVEKVSETLLK 81
Cdd:PLN03167 109 VTVAKEVELEDPVENIGAKLVRQAAAKTNDLAGDGTTTSVVLAQGLIAEGVKVVAAGANPVQITRGIEKTAKALVKELKK 188

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 673058937  82 DAKEVETKEqIAATAGISAGDQ-SIGDLIAEAMDKVGNEGVITVEESNTFGLQLELTEGMRF 142
Cdd:PLN03167 189 MSKEVEDSE-LADVAAVSAGNNyEVGNMIAEAMSKVGRKGVVTLEEGKSAENNLYVVEGMQF 249
chaperonin_type_I_II cd00309
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ...
 2-142 1.09e-37

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: 132.94  E-value: 1.09e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673058937   2 VSIAKEIELEDPyekiGAELVKEVAKKTDDVAGDGTTTATVLAQALVKEGLRNVAAGANPLALKRGIEKAVEKVSETL-- 79
Cdd:cd00309   51 ATILKEIEVEHP----AAKLLVEVAKSQDDEVGDGTTTVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILke 126

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 673058937  80 LKDAKEVETKEQIAATAGISAG-------DQSIGDLIAEAMDKVG------NEGVITVEESNTFGL-QLELTEGMRF 142
Cdd:cd00309  127 IAVPIDVEDREELLKVATTSLNsklvsggDDFLGELVVDAVLKVGkengdvDLGVIRVEKKKGGSLeDSELVVGMVF 203
Cpn60_TCP1 pfam00118
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ...
 2-142 1.51e-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: 80.71  E-value: 1.51e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673058937    2 VSIAKEIELEDPYekigAELVKEVAKKTDDVAGDGTTTATVLAQALVKEGLRNVAAGANPLALKRGIEKAVEKVSEtLLK 81
Cdd:pfam00118  32 ATILKELEIQHPA----AKLLVEAAKAQDEEVGDGTTTVVVLAGELLEEAEKLLAAGVHPTTIIEGYEKALEKALE-ILD 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673058937   82 DAKEVETKE-------QIAATA----GISAGDQSIGDLIAEA---------MDKVGNEGVITVEESNTFGLQLEltEGMR 141
Cdd:pfam00118 107 SIISIPVEDvdredllKVARTSlsskIISRESDFLAKLVVDAvlaipkndgSFDLGNIGVVKILGGSLEDSELV--DGVV 184


                  .
gi 673058937  142 F 142
Cdd:pfam00118 185 L 185
cpn60 cd03343
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ...
 2-111 1.07e-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: 55.35  E-value: 1.07e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673058937   2 VSIAKEIELEDPyekiGAELVKEVAKKTDDVAGDGTTTATVLAQALVKEGLRNVAAGANPLALKRGIEKAVEKVSETLLK 81
Cdd:cd03343   58 ATILKEMDIEHP----AAKMLVEVAKTQDEEVGDGTTTAVVLAGELLEKAEDLLDQNIHPTVIIEGYRLAAEKALELLDE 133

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 673058937  82 DAKEV-----ETKEQIAATAGISAGDQSIGDLIAE 111
Cdd:cd03343  134 IAIKVdpddkDTLRKIAKTSLTGKGAEAAKDKLAD 168
chap_CCT_epsi TIGR02343
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ...
 3-136 3.53e-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: 47.87  E-value: 3.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673058937    3 SIAKEIELEDPYekigAELVKEVAKKTDDVAGDGTTTATVLAQALVKEGLRNVAAGANPLALKRGIEK----AVEKVSET 78
Cdd:TIGR02343  71 TILSQMDVDNQI----AKLMVELSKSQDDEIGDGTTGVVVLAGALLEQAEELLDKGIHPIKIADGFEEaariAVEHLEEI 146

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 673058937   79 LLKDAKEVETKEQIAATAGISAGDQsIGDLIAEAMDKVGNEGVITVEESNTFGLQLEL 136
Cdd:TIGR02343 147 SDEISADNNNREPLIQAAKTSLGSK-IVSKCHRRFAEIAVDAVLNVADMERRDVDFDL 203
PTZ00212 PTZ00212
T-complex protein 1 subunit beta; Provisional
 3-83 5.65e-06

T-complex protein 1 subunit beta; Provisional


Pssm-ID: 185514  Cd Length: 533  Bit Score: 44.63  E-value: 5.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673058937   3 SIAKEIELEDPYEKIgaeLVkEVAKKTDDVAGDGTTTATVLAQALVKEGLRNVAAGANPLALKRGIEKAVEKVSETLLKD 82
Cdd:PTZ00212  71 TILKSVWLDNPAAKI---LV-DISKTQDEEVGDGTTSVVVLAGELLREAEKLLDQKIHPQTIIEGWRMALDVARKALEEI 146


                 .
gi 673058937  83 A 83
Cdd:PTZ00212 147 A 147
TCP1_beta cd03336
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ...
 4-83 7.38e-06

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: 44.24  E-value: 7.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673058937   4 IAKEIELEDPYEKIgaeLVkEVAKKTDDVAGDGTTTATVLAQALVKEGLRNVAAGANPLALKRGIEKAVEKVSETLLKDA 83
Cdd:cd03336   60 ILKSIGVDNPAAKV---LV-DISKVQDDEVGDGTTSVTVLAAELLREAEKLVAQKIHPQTIIEGYRMATAAAREALLSSA 135
TCP1_epsilon cd03339
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ...
 3-96 2.60e-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: 42.67  E-value: 2.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673058937   3 SIAKEIELEDPYekigAELVKEVAKKTDDVAGDGTTTATVLAQALVKEGLRNVAAGANPLALKRGIEKA-------VEKV 75
Cdd:cd03339   67 TILEKMDVDHQI----AKLLVELSKSQDDEIGDGTTGVVVLAGALLEQAEKLLDRGIHPIRIADGYEQAckiavehLEEI 142

                         90       100
                 ....*....|....*....|.
gi 673058937  76 SETLLKDAKEVETKEQIAATA 96
Cdd:cd03339  143 ADKIEFSPDNKEPLIQTAMTS 163
TCP1_eta cd03340
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ...
 19-96 3.32e-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: 42.27  E-value: 3.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673058937  19 AELVKEVAKKTDDVAGDGTTTATVLAQALVKEGLRNVAAGANPLALKRGIEKA----VEKVSETLLKDAKEVETK----- 89
Cdd:cd03340   72 AKTLVDIAKSQDAEVGDGTTSVVVLAGEFLKEAKPFIEDGVHPQIIIRGYRKAlqlaIEKIKEIAVNIDKEDKEEqrell 151


                 ....*..
gi 673058937  90 EQIAATA 96
Cdd:cd03340  152 EKCAATA 158
TCP1_delta cd03338
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ...
 4-96 4.03e-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: 39.19  E-value: 4.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673058937   4 IAKEIELEDPYEKIGAELvkevaKKTDDV-AGDGTTTATVLAQALVKEGLRNVAAGANPLALKRGIEKAVEKVSETLLKD 82
Cdd:cd03338   53 ILKQMSVLHPAAKMLVEL-----SKAQDIeAGDGTTSVVVLAGALLSACESLLKKGIHPTVISESFQIAAKKAVEILDSM 127

                         90
                 ....*....|....*....
gi 673058937  83 AKEVETKE-----QIAATA 96
Cdd:cd03338  128 SIPVDLNDresliKSATTS 146
chap_CCT_beta TIGR02341
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ...
 3-85 7.47e-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: 38.30  E-value: 7.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673058937    3 SIAKEIELEDPyekiGAELVKEVAKKTDDVAGDGTTTATVLAQALVKEGLRNVAAGANPLALKRGIEKAVEKVSETLLKD 82
Cdd:TIGR02341  60 TILKSIGVDNP----AAKVLVDMSKVQDDEVGDGTTSVTVLAAELLREAEKLINQKIHPQTIIAGYREATKAARDALLKS 135


                  ...
gi 673058937   83 AKE 85
Cdd:TIGR02341 136 AVD 138
chap_CCT_zeta TIGR02347
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ...
 19-79 1.02e-03

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: 37.79  E-value: 1.02e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 673058937   19 AELVKEVAKKTDDVAGDGTTTATVLAQALVKEGLRNVAAGANPLALKRGIEKAVEKVSETL 79
Cdd:TIGR02347  72 ASMIARAATAQDDITGDGTTSTVLLIGELLKQAERYILEGVHPRIITEGFEIARKEALQFL 132
chap_CCT_delta TIGR02342
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ...
 19-91 1.70e-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: 37.46  E-value: 1.70e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 673058937   19 AELVKEVAKKTDDVAGDGTTTATVLAQALVKEGLRNVAAGANPLALKRGIEKAVEKVSETLLKDAKEVETKEQ 91
Cdd:TIGR02342  65 AKMLVELSKAQDIEAGDGTTSVVILAGALLGACERLLNKGIHPTIISESFQSAADEAIKILDEMSIPVDLSDR 137
TCP1_zeta cd03342
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ...
 19-88 3.05e-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: 36.47  E-value: 3.05e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 673058937  19 AELVKEVAKKTDDVAGDGTTTATVLAQALVKEGLRNVAAGANPLALKRGIEKAVEKVSETL--LKDAKEVET 88
Cdd:cd03342   68 ASMIARAATAQDDITGDGTTSNVLLIGELLKQAERYIQEGVHPRIITEGFELAKNKALKFLesFKVPVEIDT 139
chap_CCT_alpha TIGR02340
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ...
 3-83 7.77e-03

T-complex protein 1, alpha 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 alpha chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.


Pssm-ID: 274081 [Multi-domain]  Cd Length: 536  Bit Score: 35.47  E-value: 7.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 673058937    3 SIAKEIELEDPYEKIGAELvkevAKKTDDVAGDGTTTATVLAQALVKEGLRNVAAGANP--------LALK---RGIEKA 71
Cdd:TIGR02340  56 TILKLLEVEHPAAKILVEL----AQLQDREVGDGTTSVVIIAAELLKRADELVKNKIHPtsvisgyrLACKeavKYIKEN 131

                          90
                  ....*....|..
gi 673058937   72 VEKVSETLLKDA 83
Cdd:TIGR02340 132 LSVSVDELGREA 143
 
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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