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Conserved domains on  [gi|763712649|gb|AJQ30709|]
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GroEL, partial [Leuconostoc mesenteroides]

Protein Classification

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 ...
 1-107 1.18e-57

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: 185.71  E-value: 1.18e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763712649   1 LQERLAKLAGGVAVINVGAATETELKERKYRIEDALNATRAAVEEGFVAGGGTALVNVIAAVSALS-EEGDVQTGINTVI 79
Cdd:PRK00013 364 LQERLAKLAGGVAVIKVGAATEVEMKEKKDRVEDALHATRAAVEEGIVPGGGVALLRAAPALEALKgLNGDEATGINIVL 443

                         90       100
                 ....*....|....*....|....*...
gi 763712649  80 KALESPVRQIAENAGLEGSVIVNKLKEQ 107
Cdd:PRK00013 444 RALEAPLRQIAENAGLEGSVVVEKVKNG 471
 
Name Accession Description Interval E-value
groEL PRK00013
chaperonin GroEL; Reviewed
 1-107 1.18e-57

chaperonin GroEL; Reviewed


Pssm-ID: 234573  Cd Length: 542  Bit Score: 185.71  E-value: 1.18e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763712649   1 LQERLAKLAGGVAVINVGAATETELKERKYRIEDALNATRAAVEEGFVAGGGTALVNVIAAVSALS-EEGDVQTGINTVI 79
Cdd:PRK00013 364 LQERLAKLAGGVAVIKVGAATEVEMKEKKDRVEDALHATRAAVEEGIVPGGGVALLRAAPALEALKgLNGDEATGINIVL 443

                         90       100
                 ....*....|....*....|....*...
gi 763712649  80 KALESPVRQIAENAGLEGSVIVNKLKEQ 107
Cdd:PRK00013 444 RALEAPLRQIAENAGLEGSVVVEKVKNG 471
GroEL cd03344
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ...
 1-107 1.35e-50

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: 166.48  E-value: 1.35e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763712649   1 LQERLAKLAGGVAVINVGAATETELKERKYRIEDALNATRAAVEEGFVAGGGTALVNVIAAVSAL-SEEGDVQTGINTVI 79
Cdd:cd03344  362 LQERLAKLSGGVAVIKVGGATEVELKEKKDRVEDALNATRAAVEEGIVPGGGVALLRASPALDKLkALNGDEKLGIEIVR 441

                         90       100
                 ....*....|....*....|....*...
gi 763712649  80 KALESPVRQIAENAGLEGSVIVNKLKEQ 107
Cdd:cd03344  442 RALEAPLRQIAENAGVDGSVVVEKVLES 469
GroEL TIGR02348
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ...
 1-106 7.56e-48

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: 159.38  E-value: 7.56e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763712649    1 LQERLAKLAGGVAVINVGAATETELKERKYRIEDALNATRAAVEEGFVAGGGTALVNVIAAVSALSEEG-DVQTGINTVI 79
Cdd:TIGR02348 363 LQERLAKLAGGVAVIKVGAATETEMKEKKLRIEDALNATRAAVEEGIVPGGGVALLRAAAALEGLKGDGeDEAIGIDIVK 442

                          90       100
                  ....*....|....*....|....*..
gi 763712649   80 KALESPVRQIAENAGLEGSVIVNKLKE 106
Cdd:TIGR02348 443 RALEAPLRQIAENAGLDGAVVAEKVKE 469
GroEL COG0459
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ...
 13-107 1.13e-40

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


Pssm-ID: 440227  Cd Length: 497  Bit Score: 139.83  E-value: 1.13e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763712649  13 AVINVGAATETELKERKYRIEDALNATRAAVEEGFVAGGGTALVNVIAAVSALSE--EGDVQTGINTVIKALESPVRQIA 90
Cdd:COG0459  341 IVILVGAATEVEVKERKRRVEDALHATRAAVEEGIVPGGGAALLRAARALRELAAklEGDEQLGIEIVARALEAPLRQIA 420

                         90
                 ....*....|....*..
gi 763712649  91 ENAGLEGSVIVNKLKEQ 107
Cdd:COG0459  421 ENAGLDGSVVVEKVRAA 437
Cpn60_TCP1 pfam00118
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ...
 8-105 3.38e-17

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: 75.32  E-value: 3.38e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763712649    8 LAGGVAVINVGAATETELKERKYRIEDALNATRAAVEE-GFVAGGGTALVNVIAAVSALSE--EGDVQTGINTVIKALES 84
Cdd:pfam00118 331 KSPKAATILLRGATDHVLDEIERSIHDALCVVKNAIEDpRVVPGGGAVEMELARALREYAKsvSGKEQLAIEAFAEALEV 410

                          90       100
                  ....*....|....*....|.
gi 763712649   85 PVRQIAENAGLEGSVIVNKLK 105
Cdd:pfam00118 411 IPKTLAENAGLDPIEVLAELR 431
 
Name Accession Description Interval E-value
groEL PRK00013
chaperonin GroEL; Reviewed
 1-107 1.18e-57

chaperonin GroEL; Reviewed


Pssm-ID: 234573  Cd Length: 542  Bit Score: 185.71  E-value: 1.18e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763712649   1 LQERLAKLAGGVAVINVGAATETELKERKYRIEDALNATRAAVEEGFVAGGGTALVNVIAAVSALS-EEGDVQTGINTVI 79
Cdd:PRK00013 364 LQERLAKLAGGVAVIKVGAATEVEMKEKKDRVEDALHATRAAVEEGIVPGGGVALLRAAPALEALKgLNGDEATGINIVL 443

                         90       100
                 ....*....|....*....|....*...
gi 763712649  80 KALESPVRQIAENAGLEGSVIVNKLKEQ 107
Cdd:PRK00013 444 RALEAPLRQIAENAGLEGSVVVEKVKNG 471
GroEL cd03344
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ...
 1-107 1.35e-50

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: 166.48  E-value: 1.35e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763712649   1 LQERLAKLAGGVAVINVGAATETELKERKYRIEDALNATRAAVEEGFVAGGGTALVNVIAAVSAL-SEEGDVQTGINTVI 79
Cdd:cd03344  362 LQERLAKLSGGVAVIKVGGATEVELKEKKDRVEDALNATRAAVEEGIVPGGGVALLRASPALDKLkALNGDEKLGIEIVR 441

                         90       100
                 ....*....|....*....|....*...
gi 763712649  80 KALESPVRQIAENAGLEGSVIVNKLKEQ 107
Cdd:cd03344  442 RALEAPLRQIAENAGVDGSVVVEKVLES 469
groEL PRK12849
chaperonin GroEL; Reviewed
 1-106 2.44e-48

chaperonin GroEL; Reviewed


Pssm-ID: 237230  Cd Length: 542  Bit Score: 161.13  E-value: 2.44e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763712649   1 LQERLAKLAGGVAVINVGAATETELKERKYRIEDALNATRAAVEEGFVAGGGTALVNVIAAVSAL-SEEGDVQTGINTVI 79
Cdd:PRK12849 364 LQERLAKLAGGVAVIKVGAATEVELKERKDRVEDALNATRAAVEEGIVPGGGVALLRAAKALDELaGLNGDQAAGVEIVR 443

                         90       100
                 ....*....|....*....|....*..
gi 763712649  80 KALESPVRQIAENAGLEGSVIVNKLKE 106
Cdd:PRK12849 444 RALEAPLRQIAENAGLDGSVVVAKVLE 470
GroEL TIGR02348
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ...
 1-106 7.56e-48

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: 159.38  E-value: 7.56e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763712649    1 LQERLAKLAGGVAVINVGAATETELKERKYRIEDALNATRAAVEEGFVAGGGTALVNVIAAVSALSEEG-DVQTGINTVI 79
Cdd:TIGR02348 363 LQERLAKLAGGVAVIKVGAATETEMKEKKLRIEDALNATRAAVEEGIVPGGGVALLRAAAALEGLKGDGeDEAIGIDIVK 442

                          90       100
                  ....*....|....*....|....*..
gi 763712649   80 KALESPVRQIAENAGLEGSVIVNKLKE 106
Cdd:TIGR02348 443 RALEAPLRQIAENAGLDGAVVAEKVKE 469
groEL PRK12850
chaperonin GroEL; Reviewed
 1-106 2.19e-42

chaperonin GroEL; Reviewed


Pssm-ID: 237231  Cd Length: 544  Bit Score: 145.25  E-value: 2.19e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763712649   1 LQERLAKLAGGVAVINVGAATETELKERKYRIEDALNATRAAVEEGFVAGGGTALVNVIAAVSALSEE-GDVQTGINTVI 79
Cdd:PRK12850 365 LQERLAKLAGGVAVIRVGGATEVEVKEKKDRVDDALHATRAAVEEGIVPGGGVALLRARSALRGLKGAnADETAGIDIVR 444

                         90       100
                 ....*....|....*....|....*..
gi 763712649  80 KALESPVRQIAENAGLEGSVIVNKLKE 106
Cdd:PRK12850 445 RALEEPLRQIATNAGFEGSVVVGKVAE 471
groEL PRK12852
chaperonin GroEL; Reviewed
 1-106 4.94e-41

chaperonin GroEL; Reviewed


Pssm-ID: 237232  Cd Length: 545  Bit Score: 141.52  E-value: 4.94e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763712649   1 LQERLAKLAGGVAVINVGAATETELKERKYRIEDALNATRAAVEEGFVAGGGTALVNVIAAVSALS-EEGDVQTGINTVI 79
Cdd:PRK12852 365 LQERLAKLAGGVAVIRVGGATEVEVKEKKDRVEDALNATRAAVQEGIVPGGGVALLRAKKAVGRINnDNADVQAGINIVL 444

                         90       100
                 ....*....|....*....|....*..
gi 763712649  80 KALESPVRQIAENAGLEGSVIVNKLKE 106
Cdd:PRK12852 445 KALEAPIRQIAENAGVEGSIVVGKILE 471
GroEL COG0459
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ...
 13-107 1.13e-40

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


Pssm-ID: 440227  Cd Length: 497  Bit Score: 139.83  E-value: 1.13e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763712649  13 AVINVGAATETELKERKYRIEDALNATRAAVEEGFVAGGGTALVNVIAAVSALSE--EGDVQTGINTVIKALESPVRQIA 90
Cdd:COG0459  341 IVILVGAATEVEVKERKRRVEDALHATRAAVEEGIVPGGGAALLRAARALRELAAklEGDEQLGIEIVARALEAPLRQIA 420

                         90
                 ....*....|....*..
gi 763712649  91 ENAGLEGSVIVNKLKEQ 107
Cdd:COG0459  421 ENAGLDGSVVVEKVRAA 437
PTZ00114 PTZ00114
Heat shock protein 60; Provisional
 1-106 8.22e-40

Heat shock protein 60; Provisional


Pssm-ID: 185455  Cd Length: 555  Bit Score: 138.51  E-value: 8.22e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763712649   1 LQERLAKLAGGVAVINVGAATETELKERKYRIEDALNATRAAVEEGFVAGGGTALVNVIAAVSALSE----EGDVQTGIN 76
Cdd:PTZ00114 377 LKERLAKLSGGVAVIKVGGASEVEVNEKKDRIEDALNATRAAVEEGIVPGGGVALLRASKLLDKLEEdnelTPDQRTGVK 456

                         90       100       110
                 ....*....|....*....|....*....|
gi 763712649  77 TVIKALESPVRQIAENAGLEGSVIVNKLKE 106
Cdd:PTZ00114 457 IVRNALRLPTKQIAENAGVEGAVVVEKILE 486
groEL PRK12851
chaperonin GroEL; Reviewed
 1-106 2.28e-38

chaperonin GroEL; Reviewed


Pssm-ID: 171770  Cd Length: 541  Bit Score: 134.48  E-value: 2.28e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763712649   1 LQERLAKLAGGVAVINVGAATETELKERKYRIEDALNATRAAVEEGFVAGGGTALVNVIAAVSAL-SEEGDVQTGINTVI 79
Cdd:PRK12851 365 LQERLAKLAGGVAVIRVGASTEVEVKEKKDRVDDALHATRAAVEEGIVPGGGVALLRAVKALDKLeTANGDQRTGVEIVR 444

                         90       100
                 ....*....|....*....|....*..
gi 763712649  80 KALESPVRQIAENAGLEGSVIVNKLKE 106
Cdd:PRK12851 445 RALEAPVRQIAENAGAEGSVVVGKLRE 471
groEL CHL00093
chaperonin GroEL
 1-107 2.02e-37

chaperonin GroEL


Pssm-ID: 177025  Cd Length: 529  Bit Score: 131.77  E-value: 2.02e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763712649   1 LQERLAKLAGGVAVINVGAATETELKERKYRIEDALNATRAAVEEGFVAGGGTALVNVIAAVSALSEE---GDVQTGINT 77
Cdd:CHL00093 364 LQERLAKLSGGVAVIKVGAATETEMKDKKLRLEDAINATKAAVEEGIVPGGGATLVHLSENLKTWAKNnlkEDELIGALI 443

                         90       100       110
                 ....*....|....*....|....*....|
gi 763712649  78 VIKALESPVRQIAENAGLEGSVIVNKLKEQ 107
Cdd:CHL00093 444 VARAILAPLKRIAENAGKNGSVIIEKVQEQ 473
chaperonin_type_I_II cd00309
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ...
 10-107 4.19e-31

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: 113.68  E-value: 4.19e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763712649  10 GGVAVINVGAATETELKERKYRIEDALNATRAAVEE-GFVAGGGTALVNVIAAVS--ALSEEGDVQTGINTVIKALESPV 86
Cdd:cd00309  310 GKVATILLRGATEVELDEAERSLHDALCAVRAAVEDgGIVPGGGAAEIELSKALEelAKTLPGKEQLGIEAFADALEVIP 389

                         90       100
                 ....*....|....*....|.
gi 763712649  87 RQIAENAGLEGSVIVNKLKEQ 107
Cdd:cd00309  390 RTLAENAGLDPIEVVTKLRAK 410
PRK14104 PRK14104
chaperonin GroEL; Provisional
 1-107 1.33e-29

chaperonin GroEL; Provisional


Pssm-ID: 172594  Cd Length: 546  Bit Score: 110.51  E-value: 1.33e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763712649   1 LQERLAKLAGGVAVINVGAATETELKERKYRIEDALNATRAAVEEGFVAGGGTALVNVIAAVSALSEEGDVQ-TGINTVI 79
Cdd:PRK14104 365 LQERLAKLAGGVAVIRVGGATEVEVKERKDRVDDAMHATRAAVEEGIVPGGGVALLRASEQLKGIKTKNDDQkTGVEIVR 444

                         90       100
                 ....*....|....*....|....*...
gi 763712649  80 KALESPVRQIAENAGLEGSVIVNKLKEQ 107
Cdd:PRK14104 445 KALSAPARQIAINAGEDGSVIVGKILEK 472
PLN03167 PLN03167
Chaperonin-60 beta subunit; Provisional
 1-104 4.85e-29

Chaperonin-60 beta subunit; Provisional


Pssm-ID: 215611 [Multi-domain]  Cd Length: 600  Bit Score: 108.86  E-value: 4.85e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763712649   1 LQERLAKLAGGVAVINVGAATETELKERKYRIEDALNATRAAVEEGFVAGGGTALVNVIAAVSALSE--EGDVQ-TGINT 77
Cdd:PLN03167 419 LNERIAKLSGGVAVIQVGAQTETELKEKKLRVEDALNATKAAVEEGIVVGGGCTLLRLASKVDAIKDtlENDEQkVGADI 498

                         90       100
                 ....*....|....*....|....*..
gi 763712649  78 VIKALESPVRQIAENAGLEGSVIVNKL 104
Cdd:PLN03167 499 VKRALSYPLKLIAKNAGVNGSVVSEKV 525
Cpn60_TCP1 pfam00118
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ...
 8-105 3.38e-17

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: 75.32  E-value: 3.38e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763712649    8 LAGGVAVINVGAATETELKERKYRIEDALNATRAAVEE-GFVAGGGTALVNVIAAVSALSE--EGDVQTGINTVIKALES 84
Cdd:pfam00118 331 KSPKAATILLRGATDHVLDEIERSIHDALCVVKNAIEDpRVVPGGGAVEMELARALREYAKsvSGKEQLAIEAFAEALEV 410

                          90       100
                  ....*....|....*....|.
gi 763712649   85 PVRQIAENAGLEGSVIVNKLK 105
Cdd:pfam00118 411 IPKTLAENAGLDPIEVLAELR 431
chaperonin_like cd03333
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ...
 10-45 1.40e-09

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


Pssm-ID: 239449 [Multi-domain]  Cd Length: 209  Bit Score: 52.85  E-value: 1.40e-09
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 763712649  10 GGVAVINVGAATETELKERKYRIEDALNATRAAVEE 45
Cdd:cd03333  174 GKAATILLRGATEVELDEVKRSLHDALCAVRAAVEE 209
cpn60 cd03343
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ...
 32-96 4.57e-05

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: 40.71  E-value: 4.57e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 763712649  32 IEDALNATRAAVEEG-FVAGGGTALVNVIAAVS--ALSEEGDVQTGINTVIKALESPVRQIAENAGLE 96
Cdd:cd03343  383 LEDALRVVADALEDGkVVAGGGAVEIELAKRLReyARSVGGREQLAVEAFADALEEIPRTLAENAGLD 450
chap_CCT_eta TIGR02345
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ...
 25-105 6.16e-05

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


Pssm-ID: 274086 [Multi-domain]  Cd Length: 523  Bit Score: 40.13  E-value: 6.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763712649   25 LKERKYRIEDALNATRAAVEEGFVAGGGTALVNVIAAV---SALSEEGDVQTGINTVIKALESPVRQIAENAGLEGSVIV 101
Cdd:TIGR02345 380 IEEAERSLHDAIMIVRRALKNKKIVAGGGAIEMELSKClrdYSKTIDGKQQLIINAFAKALEIIPRQLCENAGFDSIEIL 459


                  ....
gi 763712649  102 NKLK 105
Cdd:TIGR02345 460 NKLR 463
TCP1_eta cd03340
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ...
 32-107 1.49e-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: 39.19  E-value: 1.49e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 763712649  32 IEDALNATRAAVEEGFVAGGGTALVNVIAAV---SALSEEGDVQTGINTVIKALESPVRQIAENAGLEGSVIVNKLKEQ 107
Cdd:cd03340  385 LHDAIMIVRRAIKNDSVVAGGGAIEMELSKYlrdYSRTIAGKQQLVINAFAKALEIIPRQLCDNAGFDATDILNKLRQK 463
chap_CCT_theta TIGR02346
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ...
 12-104 1.02e-03

T-complex protein 1, theta 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: 274087 [Multi-domain]  Cd Length: 531  Bit Score: 36.62  E-value: 1.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763712649   12 VAVINVGAATETELKERKYRIEDALNATRAAVEEG-FVAGGGTALVNVIAAVSALSE--EGDVQTGINTVIKALESPVRQ 88
Cdd:TIGR02346 364 ISTIILRGSTDNLLDDIERAIDDGVNTVKALVKDGrLLPGAGATEIELASRLTKYGEklPGLDQYAIKKFAEAFEIIPRT 443

                          90
                  ....*....|....*.
gi 763712649   89 IAENAGLEGSVIVNKL 104
Cdd:TIGR02346 444 LAENAGLNANEVIPKL 459
TCP1_delta cd03338
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ...
 25-106 1.93e-03

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: 36.11  E-value: 1.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763712649  25 LKERKYRIEDALNATRAAVEEGF-VAGGGTALVNViaaVSALSEEGDVQTGINTVI-----KALESPVRQIAENAGLEGS 98
Cdd:cd03338  375 LDEAERSLHDALCVIRCLVKKRAlIPGGGAPEIEI---ALQLSEWARTLTGVEQYCvrafaDALEVIPYTLAENAGLNPI 451


                 ....*...
gi 763712649  99 VIVNKLKE 106
Cdd:cd03338  452 SIVTELRN 459
TCP1_theta cd03341
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ...
 12-104 2.83e-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: 35.66  E-value: 2.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763712649  12 VAVINVGAATETELKERKYRIEDALNATRAAVEEG-FVAGGGT---ALVNVIAAVSAlSEEGDVQTGINTVIKALESPVR 87
Cdd:cd03341  316 IATIVLRGATQNILDDVERAIDDGVNVFKSLTKDGrFVPGAGAteiELAKKLKEYGE-KTPGLEQYAIKKFAEAFEVVPR 394

                         90
                 ....*....|....*..
gi 763712649  88 QIAENAGLEGSVIVNKL 104
Cdd:cd03341  395 TLAENAGLDATEVLSEL 411
TCP1_beta cd03336
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ...
 9-105 9.17e-03

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: 34.23  E-value: 9.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763712649   9 AGGVAVINVGAATETELKERKYRIEDALNATRAAVEEG-FVAGGGTALVNVIAAVS--ALSEEGDVQTGINTVIKALESP 85
Cdd:cd03336  357 AGEACTIVLRGASQQILDEAERSLHDALCVLAQTVKDTrVVLGGGCSEMLMAKAVEelAKKTPGKKSLAIEAFAKALRQL 436

                         90       100
                 ....*....|....*....|
gi 763712649  86 VRQIAENAGLEGSVIVNKLK 105
Cdd:cd03336  437 PTIIADNAGYDSAELVAQLR 456
 
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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