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Conserved domains on  [gi|1800412289|gb|QHO60916|]
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chaperonin GroEL, partial [Limosilactobacillus fermentum]

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 ...
 1-153 3.14e-96

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: 287.40  E-value: 3.14e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800412289   1 LQSVVQEGRALLIIADDITGEALPTLVLNKIRGTFNVVAVKAPGFGDRRKAQLEDIAVLTGGTVISDDLGMQLKDATIDQ 80
Cdd:PRK00013  236 LEQVAQSGKPLLIIAEDVEGEALATLVVNKLRGTLKVVAVKAPGFGDRRKAMLEDIAILTGGTVISEELGLKLEDATLED 315

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1800412289  81 LGSANKVTITKDATTIVDGSGNKEAIAERVDQIKKAIAETTSDFDKEKLQERLAKLAGGVAVVKVGAATETEL 153
Cdd:PRK00013  316 LGQAKKVVVTKDNTTIVDGAGDKEAIKARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATEVEM 388
 
Name Accession Description Interval E-value
groEL PRK00013
chaperonin GroEL; Reviewed
 1-153 3.14e-96

chaperonin GroEL; Reviewed


Pssm-ID: 234573  Cd Length: 542  Bit Score: 287.40  E-value: 3.14e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800412289   1 LQSVVQEGRALLIIADDITGEALPTLVLNKIRGTFNVVAVKAPGFGDRRKAQLEDIAVLTGGTVISDDLGMQLKDATIDQ 80
Cdd:PRK00013  236 LEQVAQSGKPLLIIAEDVEGEALATLVVNKLRGTLKVVAVKAPGFGDRRKAMLEDIAILTGGTVISEELGLKLEDATLED 315

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1800412289  81 LGSANKVTITKDATTIVDGSGNKEAIAERVDQIKKAIAETTSDFDKEKLQERLAKLAGGVAVVKVGAATETEL 153
Cdd:PRK00013  316 LGQAKKVVVTKDNTTIVDGAGDKEAIKARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATEVEM 388
GroEL cd03344
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ...
 1-153 3.10e-86

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: 261.24  E-value: 3.10e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800412289   1 LQSVVQEGRALLIIADDITGEALPTLVLNKIRGTFNVVAVKAPGFGDRRKAQLEDIAVLTGGTVISDDLGMQLKDATIDQ 80
Cdd:cd03344   234 LELVAKAGRPLLIIAEDVEGEALATLVVNKLRGGLKVCAVKAPGFGDRRKAMLEDIAILTGGTVISEELGLKLEDVTLED 313

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1800412289  81 LGSANKVTITKDATTIVDGSGNKEAIAERVDQIKKAIAETTSDFDKEKLQERLAKLAGGVAVVKVGAATETEL 153
Cdd:cd03344   314 LGRAKKVVVTKDDTTIIGGAGDKAAIKARIAQIRKQIEETTSDYDKEKLQERLAKLSGGVAVIKVGGATEVEL 386
GroEL TIGR02348
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ...
 1-153 7.04e-83

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: 252.60  E-value: 7.04e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800412289   1 LQSVVQEGRALLIIADDITGEALPTLVLNKIRGTFNVVAVKAPGFGDRRKAQLEDIAVLTGGTVISDDLGMQLKDATIDQ 80
Cdd:TIGR02348 235 LEKVAQSGKPLLIIAEDVEGEALATLVVNKLRGTLNVCAVKAPGFGDRRKAMLEDIAILTGGQVISEELGLKLEEVTLDD 314

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1800412289  81 LGSANKVTITKDATTIVDGSGNKEAIAERVDQIKKAIAETTSDFDKEKLQERLAKLAGGVAVVKVGAATETEL 153
Cdd:TIGR02348 315 LGKAKKVTVDKDNTTIVEGAGDKAAIKARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATETEM 387
GroEL COG0459
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ...
 1-153 7.83e-52

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


Pssm-ID: 440227  Cd Length: 497  Bit Score: 171.41  E-value: 7.83e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800412289   1 LQSVVQEGRALLIIADDITGEALPTLVLNKIRGTFNVVAVKAPGFGDRRKAQLEDIAVLTGGTVISDDLGMQLKDATIDQ 80
Cdd:COG0459   236 LEKVAQSGKPLLIIAEDIDGEALATLVVNGIRGVLRVVAVKAPGFGDRRKAMLEDIAILTGGRVISEDLGLKLEDVTLDD 315

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1800412289  81 LGSANKVTITKDATTIVDGSGNKEAIaervdqikkaiaettsdfdkeklqerlaklaggvaVVKVGAATETEL 153
Cdd:COG0459   316 LGRAKRVEVDKDNTTIVEGAGNPKAI-----------------------------------VILVGAATEVEV 353
Cpn60_TCP1 pfam00118
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ...
 1-105 9.17e-09

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: 52.97  E-value: 9.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800412289   1 LQSVVQEGRALLIIADDITGEALPTLVLNKIRGTFNVvavkapgfgdrRKAQLEDIAVLTGGTVISddlgmQLKDATIDQ 80
Cdd:pfam00118 244 VEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMALRRV-----------KKRDLERLAKATGARAVS-----SLDDLTPDD 307

                          90       100
                  ....*....|....*....|....*...
gi 1800412289  81 LGSANKV---TITKDATTIVDGSGNKEA 105
Cdd:pfam00118 308 LGTAGKVeeeKIGDEKYTFIEGCKSPKA 335
 
Name Accession Description Interval E-value
groEL PRK00013
chaperonin GroEL; Reviewed
 1-153 3.14e-96

chaperonin GroEL; Reviewed


Pssm-ID: 234573  Cd Length: 542  Bit Score: 287.40  E-value: 3.14e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800412289   1 LQSVVQEGRALLIIADDITGEALPTLVLNKIRGTFNVVAVKAPGFGDRRKAQLEDIAVLTGGTVISDDLGMQLKDATIDQ 80
Cdd:PRK00013  236 LEQVAQSGKPLLIIAEDVEGEALATLVVNKLRGTLKVVAVKAPGFGDRRKAMLEDIAILTGGTVISEELGLKLEDATLED 315

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1800412289  81 LGSANKVTITKDATTIVDGSGNKEAIAERVDQIKKAIAETTSDFDKEKLQERLAKLAGGVAVVKVGAATETEL 153
Cdd:PRK00013  316 LGQAKKVVVTKDNTTIVDGAGDKEAIKARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATEVEM 388
GroEL cd03344
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ...
 1-153 3.10e-86

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: 261.24  E-value: 3.10e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800412289   1 LQSVVQEGRALLIIADDITGEALPTLVLNKIRGTFNVVAVKAPGFGDRRKAQLEDIAVLTGGTVISDDLGMQLKDATIDQ 80
Cdd:cd03344   234 LELVAKAGRPLLIIAEDVEGEALATLVVNKLRGGLKVCAVKAPGFGDRRKAMLEDIAILTGGTVISEELGLKLEDVTLED 313

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1800412289  81 LGSANKVTITKDATTIVDGSGNKEAIAERVDQIKKAIAETTSDFDKEKLQERLAKLAGGVAVVKVGAATETEL 153
Cdd:cd03344   314 LGRAKKVVVTKDDTTIIGGAGDKAAIKARIAQIRKQIEETTSDYDKEKLQERLAKLSGGVAVIKVGGATEVEL 386
GroEL TIGR02348
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ...
 1-153 7.04e-83

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: 252.60  E-value: 7.04e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800412289   1 LQSVVQEGRALLIIADDITGEALPTLVLNKIRGTFNVVAVKAPGFGDRRKAQLEDIAVLTGGTVISDDLGMQLKDATIDQ 80
Cdd:TIGR02348 235 LEKVAQSGKPLLIIAEDVEGEALATLVVNKLRGTLNVCAVKAPGFGDRRKAMLEDIAILTGGQVISEELGLKLEEVTLDD 314

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1800412289  81 LGSANKVTITKDATTIVDGSGNKEAIAERVDQIKKAIAETTSDFDKEKLQERLAKLAGGVAVVKVGAATETEL 153
Cdd:TIGR02348 315 LGKAKKVTVDKDNTTIVEGAGDKAAIKARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATETEM 387
groEL PRK12849
chaperonin GroEL; Reviewed
 1-153 3.00e-82

chaperonin GroEL; Reviewed


Pssm-ID: 237230  Cd Length: 542  Bit Score: 251.65  E-value: 3.00e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800412289   1 LQSVVQEGRALLIIADDITGEALPTLVLNKIRGTFNVVAVKAPGFGDRRKAQLEDIAVLTGGTVISDDLGMQLKDATIDQ 80
Cdd:PRK12849  236 LEKVAQSGKPLLIIAEDVEGEALATLVVNKLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGLKLEEVTLDD 315

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1800412289  81 LGSANKVTITKDATTIVDGSGNKEAIAERVDQIKKAIAETTSDFDKEKLQERLAKLAGGVAVVKVGAATETEL 153
Cdd:PRK12849  316 LGRAKRVTITKDNTTIVDGAGDKEAIEARVAQIRRQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATEVEL 388
groEL PRK12850
chaperonin GroEL; Reviewed
 1-153 5.52e-73

chaperonin GroEL; Reviewed


Pssm-ID: 237231  Cd Length: 544  Bit Score: 227.68  E-value: 5.52e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800412289   1 LQSVVQEGRALLIIADDITGEALPTLVLNKIRGTFNVVAVKAPGFGDRRKAQLEDIAVLTGGTVISDDLGMQLKDATIDQ 80
Cdd:PRK12850  237 LEAVVQSGRPLLIIAEDVEGEALATLVVNKLRGGLKSVAVKAPGFGDRRKAMLEDIAVLTGGQVISEDLGIKLENVTLDM 316

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1800412289  81 LGSANKVTITKDATTIVDGSGNKEAIAERVDQIKKAIAETTSDFDKEKLQERLAKLAGGVAVVKVGAATETEL 153
Cdd:PRK12850  317 LGRAKRVLITKENTTIIDGAGDKKNIEARVKQIRAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEV 389
groEL PRK12851
chaperonin GroEL; Reviewed
 1-153 1.15e-70

chaperonin GroEL; Reviewed


Pssm-ID: 171770  Cd Length: 541  Bit Score: 221.54  E-value: 1.15e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800412289   1 LQSVVQEGRALLIIADDITGEALPTLVLNKIRGTFNVVAVKAPGFGDRRKAQLEDIAVLTGGTVISDDLGMQLKDATIDQ 80
Cdd:PRK12851  237 LEAVVQSGKPLLIIAEDVEGEALATLVVNKLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGIKLENVTLEQ 316

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1800412289  81 LGSANKVTITKDATTIVDGSGNKEAIAERVDQIKKAIAETTSDFDKEKLQERLAKLAGGVAVVKVGAATETEL 153
Cdd:PRK12851  317 LGRAKKVVVEKENTTIIDGAGSKTEIEGRVAQIRAQIEETTSDYDREKLQERLAKLAGGVAVIRVGASTEVEV 389
groEL PRK12852
chaperonin GroEL; Reviewed
 1-153 9.98e-68

chaperonin GroEL; Reviewed


Pssm-ID: 237232  Cd Length: 545  Bit Score: 213.94  E-value: 9.98e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800412289   1 LQSVVQEGRALLIIADDITGEALPTLVLNKIRGTFNVVAVKAPGFGDRRKAQLEDIAVLTGGTVISDDLGMQLKDATIDQ 80
Cdd:PRK12852  237 LEAVVQSGKPLLIIAEDVEGEALATLVVNRLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGQLISEDLGIKLENVTLKM 316

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1800412289  81 LGSANKVTITKDATTIVDGSGNKEAIAERVDQIKKAIAETTSDFDKEKLQERLAKLAGGVAVVKVGAATETEL 153
Cdd:PRK12852  317 LGRAKKVVIDKENTTIVNGAGKKADIEARVGQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEV 389
groEL CHL00093
chaperonin GroEL
 1-153 1.76e-67

chaperonin GroEL


Pssm-ID: 177025  Cd Length: 529  Bit Score: 213.04  E-value: 1.76e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800412289   1 LQSVVQEGRALLIIADDITGEALPTLVLNKIRGTFNVVAVKAPGFGDRRKAQLEDIAVLTGGTVISDDLGMQLKDATIDQ 80
Cdd:CHL00093  237 LEQVTKTKRPLLIIAEDVEKEALATLVLNKLRGIVNVVAVRAPGFGDRRKAMLEDIAILTGGQVITEDAGLSLETIQLDL 316

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1800412289  81 LGSANKVTITKDATTIVdGSGNKEAIAERVDQIKKAIAETTSDFDKEKLQERLAKLAGGVAVVKVGAATETEL 153
Cdd:CHL00093  317 LGQARRIIVTKDSTTII-ADGNEEQVKARCEQLRKQIEIADSSYEKEKLQERLAKLSGGVAVIKVGAATETEM 388
PTZ00114 PTZ00114
Heat shock protein 60; Provisional
 1-153 7.45e-64

Heat shock protein 60; Provisional


Pssm-ID: 185455  Cd Length: 555  Bit Score: 204.38  E-value: 7.45e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800412289   1 LQSVVQEGRALLIIADDITGEALPTLVLNKIRGTFNVVAVKAPGFGDRRKAQLEDIAVLTGGTVISDD-LGMQLKDATID 79
Cdd:PTZ00114  248 LEHAVKNKRPLLIIAEDVEGEALQTLIINKLRGGLKVCAVKAPGFGDNRKDILQDIAVLTGATVVSEDnVGLKLDDFDPS 327

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1800412289  80 QLGSANKVTITKDATTIVDGSGNKEAIAERVDQIKKAIAETTSDFDKEKLQERLAKLAGGVAVVKVGAATETEL 153
Cdd:PTZ00114  328 MLGSAKKVTVTKDETVILTGGGDKAEIKERVELLRSQIERTTSEYDKEKLKERLAKLSGGVAVIKVGGASEVEV 401
PRK14104 PRK14104
chaperonin GroEL; Provisional
 1-153 3.57e-56

chaperonin GroEL; Provisional


Pssm-ID: 172594  Cd Length: 546  Bit Score: 184.08  E-value: 3.57e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800412289   1 LQSVVQEGRALLIIADDITGEALPTLVLNKIRGTFNVVAVKAPGFGDRRKAQLEDIAVLTGGTVISDDLGMQLKDATIDQ 80
Cdd:PRK14104  237 LEAVVQTGKPLVIVAEDVEGEALATLVVNRLRGGLKVAAVKAPGFGDRRKAMLQDIAILTGGQAISEDLGIKLENVTLQM 316

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1800412289  81 LGSANKVTITKDATTIVDGSGNKEAIAERVDQIKKAIAETTSDFDKEKLQERLAKLAGGVAVVKVGAATETEL 153
Cdd:PRK14104  317 LGRAKKVMIDKENTTIVNGAGKKADIEARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEV 389
GroEL COG0459
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ...
 1-153 7.83e-52

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


Pssm-ID: 440227  Cd Length: 497  Bit Score: 171.41  E-value: 7.83e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800412289   1 LQSVVQEGRALLIIADDITGEALPTLVLNKIRGTFNVVAVKAPGFGDRRKAQLEDIAVLTGGTVISDDLGMQLKDATIDQ 80
Cdd:COG0459   236 LEKVAQSGKPLLIIAEDIDGEALATLVVNGIRGVLRVVAVKAPGFGDRRKAMLEDIAILTGGRVISEDLGLKLEDVTLDD 315

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1800412289  81 LGSANKVTITKDATTIVDGSGNKEAIaervdqikkaiaettsdfdkeklqerlaklaggvaVVKVGAATETEL 153
Cdd:COG0459   316 LGRAKRVEVDKDNTTIVEGAGNPKAI-----------------------------------VILVGAATEVEV 353
PLN03167 PLN03167
Chaperonin-60 beta subunit; Provisional
 1-153 2.23e-48

Chaperonin-60 beta subunit; Provisional


Pssm-ID: 215611 [Multi-domain]  Cd Length: 600  Bit Score: 164.33  E-value: 2.23e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800412289   1 LQSVVQEGRALLIIADDITGEALPTLVLNKIRGTFNVVAVKAPGFGDRRKAQLEDIAVLTGGTVISDDLGMQLKDATIDQ 80
Cdd:PLN03167  291 LEDAIRGGYPLLIIAEDIEQEALATLVVNKLRGSLKIAALKAPGFGERKSQYLDDIAILTGGTVIREEVGLSLDKVGKEV 370

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1800412289  81 LGSANKVTITKDATTIVDGSGNKEAIAERVDQIKKAIAETTSDFDKEKLQERLAKLAGGVAVVKVGAATETEL 153
Cdd:PLN03167  371 LGTAAKVVLTKDTTTIVGDGSTQEAVNKRVAQIKNLIEAAEQDYEKEKLNERIAKLSGGVAVIQVGAQTETEL 443
chaperonin_type_I_II cd00309
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ...
 12-153 2.18e-13

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: 66.30  E-value: 2.18e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800412289  12 LIIADD-ITGEALPTLVLNKIrgtfnvVAVKApgfgdRRKAQLEDIAVLTGGTVISDdlgmqLKDATIDQLGSANKVTIT 90
Cdd:cd00309   231 VVIAEKgIDDEALHYLAKLGI------MAVRR-----VRKEDLERIAKATGATIVSR-----LEDLTPEDLGTAGLVEET 294

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1800412289  91 K----DATTIVDGSGnkeaiaervdqikkaiaettsdfdkeklqerlaklaGGVAVVKVGAATETEL 153
Cdd:cd00309   295 KigdeKYTFIEGCKG------------------------------------GKVATILLRGATEVEL 325
chaperonin_like cd03333
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ...
 12-153 7.01e-11

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: 57.86  E-value: 7.01e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800412289  12 LIIADD-ITGEALPTLVLNKIrgtfnvVAVKApgfgdRRKAQLEDIAVLTGGTVISDdlgmqLKDATIDQLGSANKVTIT 90
Cdd:cd03333    95 VVIAEKgIDDLALHYLAKAGI------MAVRR-----VKKEDLERIARATGATIVSS-----LEDLTPEDLGTAELVEET 158

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1800412289  91 KDA----TTIVDGSGnkeaiaervdqikkaiaettsdfdkeklqerlaklaGGVAVVKVGAATETEL 153
Cdd:cd03333   159 KIGeeklTFIEGCKG------------------------------------GKAATILLRGATEVEL 189
Cpn60_TCP1 pfam00118
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ...
 1-105 9.17e-09

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: 52.97  E-value: 9.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800412289   1 LQSVVQEGRALLIIADDITGEALPTLVLNKIRGTFNVvavkapgfgdrRKAQLEDIAVLTGGTVISddlgmQLKDATIDQ 80
Cdd:pfam00118 244 VEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMALRRV-----------KKRDLERLAKATGARAVS-----SLDDLTPDD 307

                          90       100
                  ....*....|....*....|....*...
gi 1800412289  81 LGSANKV---TITKDATTIVDGSGNKEA 105
Cdd:pfam00118 308 LGTAGKVeeeKIGDEKYTFIEGCKSPKA 335
 
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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