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Conserved domains on  [gi|168419935|gb|ACA23881|]
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Hsp65, partial [Mycobacterium sp. Environmental_263]

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 ...
 1-122 2.04e-65

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: 206.51  E-value: 2.04e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168419935   1 IGAELVKEVAKKTDDVAGDGTTTATVLAQALVREGLRNVAAGANPLGLKRGIEKAVEKVTETLLKSAKEVETKDQIAATA 80
Cdd:PRK00013  68 MGAQLVKEVASKTNDVAGDGTTTATVLAQAIVREGLKNVAAGANPMDLKRGIDKAVEAAVEELKKISKPVEDKEEIAQVA 147

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 168419935  81 AISA-GDQSIGDLIAEAMDKVGNEGVITVEESNTFGLQLELTE 122
Cdd:PRK00013 148 TISAnGDEEIGKLIAEAMEKVGKEGVITVEESKGFETELEVVE 190
 
Name Accession Description Interval E-value
groEL PRK00013
chaperonin GroEL; Reviewed
 1-122 2.04e-65

chaperonin GroEL; Reviewed


Pssm-ID: 234573  Cd Length: 542  Bit Score: 206.51  E-value: 2.04e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168419935   1 IGAELVKEVAKKTDDVAGDGTTTATVLAQALVREGLRNVAAGANPLGLKRGIEKAVEKVTETLLKSAKEVETKDQIAATA 80
Cdd:PRK00013  68 MGAQLVKEVASKTNDVAGDGTTTATVLAQAIVREGLKNVAAGANPMDLKRGIDKAVEAAVEELKKISKPVEDKEEIAQVA 147

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 168419935  81 AISA-GDQSIGDLIAEAMDKVGNEGVITVEESNTFGLQLELTE 122
Cdd:PRK00013 148 TISAnGDEEIGKLIAEAMEKVGKEGVITVEESKGFETELEVVE 190
GroEL cd03344
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ...
 1-122 1.16e-55

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: 180.73  E-value: 1.16e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168419935   1 IGAELVKEVAKKTDDVAGDGTTTATVLAQALVREGLRNVAAGANPLGLKRGIEKAVEKVTETLLKSAKEVETKDQIAATA 80
Cdd:cd03344   66 MGAQLVKEVASKTNDVAGDGTTTATVLARAIIKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKPVKTKEEIAQVA 145

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 168419935  81 AISA-GDQSIGDLIAEAMDKVGNEGVITVEESNTFGLQLELTE 122
Cdd:cd03344  146 TISAnGDEEIGELIAEAMEKVGKDGVITVEEGKTLETELEVVE 188
GroEL COG0459
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ...
 1-122 2.49e-55

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


Pssm-ID: 440227  Cd Length: 497  Bit Score: 179.12  E-value: 2.49e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168419935   1 IGAELVKEVAKKTDDVAGDGTTTATVLAQALVREGLRNVAAGANPLGLKRGIEKAVEKVTETLLKSAKEVETKDQIAATA 80
Cdd:COG0459   68 MGAQLVKEVASKTNDEAGDGTTTATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPVDDKEELAQVA 147

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 168419935  81 AISA-GDQSIGDLIAEAMDKVGNEGVITVEESNTFGLQLELTE 122
Cdd:COG0459  148 TISAnGDEEIGELIAEAMEKVGKDGVITVEEGKGLETELEVVE 190
GroEL TIGR02348
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ...
 1-122 8.74e-55

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: 178.26  E-value: 8.74e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168419935    1 IGAELVKEVAKKTDDVAGDGTTTATVLAQALVREGLRNVAAGANPLGLKRGIEKAVEKVTETLLKSAKEVETKDQIAATA 80
Cdd:TIGR02348  67 MGAQLVKEVASKTNDVAGDGTTTATVLAQAIVKEGLKNVAAGANPIELKRGIEKAVEAVVEELKKLSKPVKGKKEIAQVA 146

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 168419935   81 AISAG-DQSIGDLIAEAMDKVGNEGVITVEESNTFGLQLELTE 122
Cdd:TIGR02348 147 TISANnDEEIGSLIAEAMEKVGKDGVITVEESKSLETELEVVE 189
Cpn60_TCP1 pfam00118
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ...
 3-119 8.66e-15

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: 69.15  E-value: 8.66e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168419935    3 AELVKEVAKKTDDVAGDGTTTATVLAQALVREGLRNVAAGANPLGLKRGIEKAVEKVTEtLLKSAKEVETKD-------Q 75
Cdd:pfam00118  45 AKLLVEAAKAQDEEVGDGTTTVVVLAGELLEEAEKLLAAGVHPTTIIEGYEKALEKALE-ILDSIISIPVEDvdredllK 123

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 168419935   76 IAATAA----ISAGDQSIGDLIAEA---------MDKVGNEGVITVEESNTFGLQLE 119
Cdd:pfam00118 124 VARTSLsskiISRESDFLAKLVVDAvlaipkndgSFDLGNIGVVKILGGSLEDSELV 180
 
Name Accession Description Interval E-value
groEL PRK00013
chaperonin GroEL; Reviewed
 1-122 2.04e-65

chaperonin GroEL; Reviewed


Pssm-ID: 234573  Cd Length: 542  Bit Score: 206.51  E-value: 2.04e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168419935   1 IGAELVKEVAKKTDDVAGDGTTTATVLAQALVREGLRNVAAGANPLGLKRGIEKAVEKVTETLLKSAKEVETKDQIAATA 80
Cdd:PRK00013  68 MGAQLVKEVASKTNDVAGDGTTTATVLAQAIVREGLKNVAAGANPMDLKRGIDKAVEAAVEELKKISKPVEDKEEIAQVA 147

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 168419935  81 AISA-GDQSIGDLIAEAMDKVGNEGVITVEESNTFGLQLELTE 122
Cdd:PRK00013 148 TISAnGDEEIGKLIAEAMEKVGKEGVITVEESKGFETELEVVE 190
groEL PRK12849
chaperonin GroEL; Reviewed
 1-122 1.09e-56

chaperonin GroEL; Reviewed


Pssm-ID: 237230  Cd Length: 542  Bit Score: 183.85  E-value: 1.09e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168419935   1 IGAELVKEVAKKTDDVAGDGTTTATVLAQALVREGLRNVAAGANPLGLKRGIEKAVEKVTETLLKSAKEVETKDQIAATA 80
Cdd:PRK12849  68 LGAQLVKEVASKTNDVAGDGTTTATVLAQALVQEGLKNVAAGANPMDLKRGIDKAVEAVVEELKALARPVSGSEEIAQVA 147

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 168419935  81 AISA-GDQSIGDLIAEAMDKVGNEGVITVEESNTFGLQLELTE 122
Cdd:PRK12849 148 TISAnGDEEIGELIAEAMEKVGKDGVITVEESKTLETELEVTE 190
GroEL cd03344
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ...
 1-122 1.16e-55

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: 180.73  E-value: 1.16e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168419935   1 IGAELVKEVAKKTDDVAGDGTTTATVLAQALVREGLRNVAAGANPLGLKRGIEKAVEKVTETLLKSAKEVETKDQIAATA 80
Cdd:cd03344   66 MGAQLVKEVASKTNDVAGDGTTTATVLARAIIKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKPVKTKEEIAQVA 145

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 168419935  81 AISA-GDQSIGDLIAEAMDKVGNEGVITVEESNTFGLQLELTE 122
Cdd:cd03344  146 TISAnGDEEIGELIAEAMEKVGKDGVITVEEGKTLETELEVVE 188
GroEL COG0459
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ...
 1-122 2.49e-55

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


Pssm-ID: 440227  Cd Length: 497  Bit Score: 179.12  E-value: 2.49e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168419935   1 IGAELVKEVAKKTDDVAGDGTTTATVLAQALVREGLRNVAAGANPLGLKRGIEKAVEKVTETLLKSAKEVETKDQIAATA 80
Cdd:COG0459   68 MGAQLVKEVASKTNDEAGDGTTTATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPVDDKEELAQVA 147

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 168419935  81 AISA-GDQSIGDLIAEAMDKVGNEGVITVEESNTFGLQLELTE 122
Cdd:COG0459  148 TISAnGDEEIGELIAEAMEKVGKDGVITVEEGKGLETELEVVE 190
groEL PRK12850
chaperonin GroEL; Reviewed
 1-122 3.45e-55

chaperonin GroEL; Reviewed


Pssm-ID: 237231  Cd Length: 544  Bit Score: 179.91  E-value: 3.45e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168419935   1 IGAELVKEVAKKTDDVAGDGTTTATVLAQALVREGLRNVAAGANPLGLKRGIEKAVEKVTETLLKSAKEVETKDQIAATA 80
Cdd:PRK12850  69 MGAQMVKEVASKTNDLAGDGTTTATVLAQAIVREGAKLVAAGMNPMDLKRGIDLAVAAVVDELKKIAKKVTSSKEIAQVA 148

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 168419935  81 AISA-GDQSIGDLIAEAMDKVGNEGVITVEESNTFGLQLELTE 122
Cdd:PRK12850 149 TISAnGDESIGEMIAEAMDKVGKEGVITVEEAKTLGTELDVVE 191
GroEL TIGR02348
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ...
 1-122 8.74e-55

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: 178.26  E-value: 8.74e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168419935    1 IGAELVKEVAKKTDDVAGDGTTTATVLAQALVREGLRNVAAGANPLGLKRGIEKAVEKVTETLLKSAKEVETKDQIAATA 80
Cdd:TIGR02348  67 MGAQLVKEVASKTNDVAGDGTTTATVLAQAIVKEGLKNVAAGANPIELKRGIEKAVEAVVEELKKLSKPVKGKKEIAQVA 146

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 168419935   81 AISAG-DQSIGDLIAEAMDKVGNEGVITVEESNTFGLQLELTE 122
Cdd:TIGR02348 147 TISANnDEEIGSLIAEAMEKVGKDGVITVEESKSLETELEVVE 189
groEL PRK12851
chaperonin GroEL; Reviewed
 1-122 3.09e-49

chaperonin GroEL; Reviewed


Pssm-ID: 171770  Cd Length: 541  Bit Score: 164.14  E-value: 3.09e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168419935   1 IGAELVKEVAKKTDDVAGDGTTTATVLAQALVREGLRNVAAGANPLGLKRGIEKAVEKVTETLLKSAKEVETKDQIAATA 80
Cdd:PRK12851  69 MGAQMVREVASKTNDVAGDGTTTATVLAQAIVREGAKAVAAGANPMDLKRGIDRAVAAVVEELKANARPVTTNAEIAQVA 148

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 168419935  81 AISA-GDQSIGDLIAEAMDKVGNEGVITVEESNTFGLQLELTE 122
Cdd:PRK12851 149 TISAnGDAEIGRLVAEAMEKVGNEGVITVEESKTAETELEVVE 191
PTZ00114 PTZ00114
Heat shock protein 60; Provisional
 1-122 1.41e-42

Heat shock protein 60; Provisional


Pssm-ID: 185455  Cd Length: 555  Bit Score: 146.60  E-value: 1.41e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168419935   1 IGAELVKEVAKKTDDVAGDGTTTATVLAQALVREGLRNVAAGANPLGLKRGIEKAVEKVTETLLKSAKEVETKDQIAATA 80
Cdd:PTZ00114  80 VGAQLIRQVASKTNDKAGDGTTTATILARAIFREGCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQSRPVKTKEDILNVA 159

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 168419935  81 AISA-GDQSIGDLIAEAMDKVGNEGVITVEESNTFGLQLELTE 122
Cdd:PTZ00114 160 TISAnGDVEIGSLIADAMDKVGKDGTITVEDGKTLEDELEVVE 202
groEL CHL00093
chaperonin GroEL
 2-122 2.18e-41

chaperonin GroEL


Pssm-ID: 177025  Cd Length: 529  Bit Score: 142.94  E-value: 2.18e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168419935   2 GAELVKEVAKKTDDVAGDGTTTATVLAQALVREGLRNVAAGANPLGLKRGIEKAVEKVTETLLKSAKEVETKDQIAATAA 81
Cdd:CHL00093  69 GVALIRQAASKTNDVAGDGTTTATVLAYAIVKQGMKNVAAGANPISLKRGIEKATQYVVSQIAEYARPVEDIQAITQVAS 148

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 168419935  82 ISAG-DQSIGDLIAEAMDKVGNEGVITVEESNTFGLQLELTE 122
Cdd:CHL00093 149 ISAGnDEEVGSMIADAIEKVGREGVISLEEGKSTVTELEITE 190
groEL PRK12852
chaperonin GroEL; Reviewed
 1-122 5.54e-40

chaperonin GroEL; Reviewed


Pssm-ID: 237232  Cd Length: 545  Bit Score: 139.59  E-value: 5.54e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168419935   1 IGAELVKEVAKKTDDVAGDGTTTATVLAQALVREGLRNVAAGANPLGLKRGIEKAVEKVTETLLKSAKEVETKDQIAATA 80
Cdd:PRK12852  69 MGAQMVREVASKTNDLAGDGTTTATVLAQAIVREGAKAVAAGMNPMDLKRGIDIAVAAVVKDIEKRAKPVASSAEIAQVG 148

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 168419935  81 AISA-GDQSIGDLIAEAMDKVGNEGVITVEESNTFGLQLELTE 122
Cdd:PRK12852 149 TISAnGDAAIGKMIAQAMQKVGNEGVITVEENKSLETEVDIVE 191
PRK14104 PRK14104
chaperonin GroEL; Provisional
 1-122 1.02e-34

chaperonin GroEL; Provisional


Pssm-ID: 172594  Cd Length: 546  Bit Score: 125.14  E-value: 1.02e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168419935   1 IGAELVKEVAKKTDDVAGDGTTTATVLAQALVREGLRNVAAGANPLGLKRGIEKAVEKVTETLLKSAKEVETKDQIAATA 80
Cdd:PRK14104  69 MGAQMVREVASKSADAAGDGTTTATVLAQAIVREGAKSVAAGMNPMDLKRGIDLAVEAVVADLVKNSKKVTSNDEIAQVG 148

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 168419935  81 AISA-GDQSIGDLIAEAMDKVGNEGVITVEESNTFGLQLELTE 122
Cdd:PRK14104 149 TISAnGDAEIGKFLADAMKKVGNEGVITVEEAKSLETELDVVE 191
chaperonin_type_I_II cd00309
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ...
 2-113 3.15e-32

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: 117.53  E-value: 3.15e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168419935   2 GAELVKEVAKKTDDVAGDGTTTATVLAQALVREGLRNVAAGANPLGLKRGIEKAVEKVTETLLKSAKEVETKD-----QI 76
Cdd:cd00309   63 AAKLLVEVAKSQDDEVGDGTTTVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVPIDVEDreellKV 142

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 168419935  77 AATAA----ISAGDQSIGDLIAEAMDKVG------NEGVITVEESNT 113
Cdd:cd00309  143 ATTSLnsklVSGGDDFLGELVVDAVLKVGkengdvDLGVIRVEKKKG 189
PLN03167 PLN03167
Chaperonin-60 beta subunit; Provisional
 1-110 1.25e-28

Chaperonin-60 beta subunit; Provisional


Pssm-ID: 215611 [Multi-domain]  Cd Length: 600  Bit Score: 108.47  E-value: 1.25e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168419935   1 IGAELVKEVAKKTDDVAGDGTTTATVLAQALVREGLRNVAAGANPLGLKRGIEKAVEKVTETLLKSAKEVEtKDQIAATA 80
Cdd:PLN03167 124 IGAKLVRQAAAKTNDLAGDGTTTSVVLAQGLIAEGVKVVAAGANPVQITRGIEKTAKALVKELKKMSKEVE-DSELADVA 202

                         90       100       110
                 ....*....|....*....|....*....|.
gi 168419935  81 AISAGDQ-SIGDLIAEAMDKVGNEGVITVEE 110
Cdd:PLN03167 203 AVSAGNNyEVGNMIAEAMSKVGRKGVVTLEE 233
Cpn60_TCP1 pfam00118
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ...
 3-119 8.66e-15

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: 69.15  E-value: 8.66e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168419935    3 AELVKEVAKKTDDVAGDGTTTATVLAQALVREGLRNVAAGANPLGLKRGIEKAVEKVTEtLLKSAKEVETKD-------Q 75
Cdd:pfam00118  45 AKLLVEAAKAQDEEVGDGTTTVVVLAGELLEEAEKLLAAGVHPTTIIEGYEKALEKALE-ILDSIISIPVEDvdredllK 123

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 168419935   76 IAATAA----ISAGDQSIGDLIAEA---------MDKVGNEGVITVEESNTFGLQLE 119
Cdd:pfam00118 124 VARTSLsskiISRESDFLAKLVVDAvlaipkndgSFDLGNIGVVKILGGSLEDSELV 180
cpn60 cd03343
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ...
 2-95 1.55e-07

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: 48.41  E-value: 1.55e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168419935   2 GAELVKEVAKKTDDVAGDGTTTATVLAQALVREGLRNVAAGANPLGLKRGIEKAVEKVTETLLKSAKEVETKD-----QI 76
Cdd:cd03343   70 AAKMLVEVAKTQDEEVGDGTTTAVVLAGELLEKAEDLLDQNIHPTVIIEGYRLAAEKALELLDEIAIKVDPDDkdtlrKI 149

                         90
                 ....*....|....*....
gi 168419935  77 AATAAISAGDQSIGDLIAE 95
Cdd:cd03343  150 AKTSLTGKGAEAAKDKLAD 168
chap_CCT_epsi TIGR02343
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ...
 3-71 1.24e-06

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: 45.56  E-value: 1.24e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 168419935    3 AELVKEVAKKTDDVAGDGTTTATVLAQALVREGLRNVAAGANPLGLKRGIEKAVEKVTETLLKSAKEVE 71
Cdd:TIGR02343  83 AKLMVELSKSQDDEIGDGTTGVVVLAGALLEQAEELLDKGIHPIKIADGFEEAARIAVEHLEEISDEIS 151
TCP1_beta cd03336
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ...
 3-67 1.76e-05

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: 42.32  E-value: 1.76e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 168419935   3 AELVKEVAKKTDDVAGDGTTTATVLAQALVREGLRNVAAGANPLGLKRGIEKAVEKVTETLLKSA 67
Cdd:cd03336   71 AKVLVDISKVQDDEVGDGTTSVTVLAAELLREAEKLVAQKIHPQTIIEGYRMATAAAREALLSSA 135
PTZ00212 PTZ00212
T-complex protein 1 subunit beta; Provisional
 3-67 2.15e-05

T-complex protein 1 subunit beta; Provisional


Pssm-ID: 185514  Cd Length: 533  Bit Score: 41.94  E-value: 2.15e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 168419935   3 AELVKEVAKKTDDVAGDGTTTATVLAQALVREGLRNVAAGANPLGLKRGIEKAVEKVTETLLKSA 67
Cdd:PTZ00212  83 AKILVDISKTQDEEVGDGTTSVVVLAGELLREAEKLLDQKIHPQTIIEGWRMALDVARKALEEIA 147
TCP1_epsilon cd03339
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ...
 3-71 2.70e-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: 2.70e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 168419935   3 AELVKEVAKKTDDVAGDGTTTATVLAQALVREGLRNVAAGANPLGLKRGIEKAVEKVTETLLKSAKEVE 71
Cdd:cd03339   79 AKLLVELSKSQDDEIGDGTTGVVVLAGALLEQAEKLLDRGIHPIRIADGYEQACKIAVEHLEEIADKIE 147
TCP1_eta cd03340
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ...
 3-74 2.68e-04

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: 38.81  E-value: 2.68e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 168419935   3 AELVKEVAKKTDDVAGDGTTTATVLAQALVREGLRNVAAGANPLGLKRGIEKAVEKVTETLLKSAKEVETKD 74
Cdd:cd03340   72 AKTLVDIAKSQDAEVGDGTTSVVVLAGEFLKEAKPFIEDGVHPQIIIRGYRKALQLAIEKIKEIAVNIDKED 143
chap_CCT_delta TIGR02342
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ...
 3-75 5.37e-04

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: 38.23  E-value: 5.37e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 168419935    3 AELVKEVAKKTDDVAGDGTTTATVLAQALVREGLRNVAAGANPLGLKRGIEKAVEKVTETLLKSAKEVETKDQ 75
Cdd:TIGR02342  65 AKMLVELSKAQDIEAGDGTTSVVILAGALLGACERLLNKGIHPTIISESFQSAADEAIKILDEMSIPVDLSDR 137
TCP1_delta cd03338
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ...
 3-100 6.55e-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: 6.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168419935   3 AELVKEVAKKTDDVAGDGTTTATVLAQALVREGLRNVAAGANPLGLKRGIEKAVEKVTETLLKSAKEVETKD-----QIA 77
Cdd:cd03338   64 AKMLVELSKAQDIEAGDGTTSVVVLAGALLSACESLLKKGIHPTVISESFQIAAKKAVEILDSMSIPVDLNDresliKSA 143

                         90       100
                 ....*....|....*....|....
gi 168419935  78 ATAAISAGDQSIGDLIAE-AMDKV 100
Cdd:cd03338  144 TTSLNSKVVSQYSSLLAPiAVDAV 167
chap_CCT_beta TIGR02341
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ...
 3-69 1.19e-03

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: 37.15  E-value: 1.19e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 168419935    3 AELVKEVAKKTDDVAGDGTTTATVLAQALVREGLRNVAAGANPLGLKRGIEKAVEKVTETLLKSAKE 69
Cdd:TIGR02341  72 AKVLVDMSKVQDDEVGDGTTSVTVLAAELLREAEKLINQKIHPQTIIAGYREATKAARDALLKSAVD 138
TCP1_zeta cd03342
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ...
 3-72 2.04e-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: 2.04e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 168419935   3 AELVKEVAKKTDDVAGDGTTTATVLAQALVREGLRNVAAGANPLGLKRGIEKAVEKVTETL--LKSAKEVET 72
Cdd:cd03342   68 ASMIARAATAQDDITGDGTTSNVLLIGELLKQAERYIQEGVHPRIITEGFELAKNKALKFLesFKVPVEIDT 139
chap_CCT_zeta TIGR02347
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ...
 3-63 2.17e-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: 36.25  E-value: 2.17e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 168419935    3 AELVKEVAKKTDDVAGDGTTTATVLAQALVREGLRNVAAGANPLGLKRGIEKAVEKVTETL 63
Cdd:TIGR02347  72 ASMIARAATAQDDITGDGTTSTVLLIGELLKQAERYILEGVHPRIITEGFEIARKEALQFL 132
 
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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