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Conserved domains on  [gi|541469458|gb|AGV23525|]
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GroEL, partial [endosymbiont of Lissorhoptrus oryzophilus]

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 ...
 1-308 0e+00

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: 566.29  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541469458   1 EVASKANDSAGDGTTTATLLAQSIVNEGLKAVAAGMNPMDLKRGIDKAVNYAIEELKRISVNCSDTKSIEQVGTISANSD 80
Cdd:PRK00013  75 EVASKTNDVAGDGTTTATVLAQAIVREGLKNVAAGANPMDLKRGIDKAVEAAVEELKKISKPVEDKEEIAQVATISANGD 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541469458  81 ETVGKLIAEAMSKVGKEGVITVEEGSGLNDELDVVEGMQFDRGYLSPYFINKTESGIVELDNPFILLVDKKITNIRELLP 160
Cdd:PRK00013 155 EEIGKLIAEAMEKVGKEGVITVEESKGFETELEVVEGMQFDRGYLSPYFVTDPEKMEAELENPYILITDKKISNIQDLLP 234

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541469458 161 ILENVAKSGKPIVIIAEDVEGEALATLVVNTMRGIVKTVAVKAPGFGDRRKSMLQDIAILTNGNVISEEIGLDLEKITLN 240
Cdd:PRK00013 235 VLEQVAQSGKPLLIIAEDVEGEALATLVVNKLRGTLKVVAVKAPGFGDRRKAMLEDIAILTGGTVISEELGLKLEDATLE 314

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 541469458 241 DLGQSKKIIINKDNTTIIDGLGSKSNISKRIIQISKEKEEATSDYDKEKLQERIAKLSGGVAVIKVGA 308
Cdd:PRK00013 315 DLGQAKKVVVTKDNTTIVDGAGDKEAIKARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIKVGA 382
 
Name Accession Description Interval E-value
groEL PRK00013
chaperonin GroEL; Reviewed
 1-308 0e+00

chaperonin GroEL; Reviewed


Pssm-ID: 234573  Cd Length: 542  Bit Score: 566.29  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541469458   1 EVASKANDSAGDGTTTATLLAQSIVNEGLKAVAAGMNPMDLKRGIDKAVNYAIEELKRISVNCSDTKSIEQVGTISANSD 80
Cdd:PRK00013  75 EVASKTNDVAGDGTTTATVLAQAIVREGLKNVAAGANPMDLKRGIDKAVEAAVEELKKISKPVEDKEEIAQVATISANGD 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541469458  81 ETVGKLIAEAMSKVGKEGVITVEEGSGLNDELDVVEGMQFDRGYLSPYFINKTESGIVELDNPFILLVDKKITNIRELLP 160
Cdd:PRK00013 155 EEIGKLIAEAMEKVGKEGVITVEESKGFETELEVVEGMQFDRGYLSPYFVTDPEKMEAELENPYILITDKKISNIQDLLP 234

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541469458 161 ILENVAKSGKPIVIIAEDVEGEALATLVVNTMRGIVKTVAVKAPGFGDRRKSMLQDIAILTNGNVISEEIGLDLEKITLN 240
Cdd:PRK00013 235 VLEQVAQSGKPLLIIAEDVEGEALATLVVNKLRGTLKVVAVKAPGFGDRRKAMLEDIAILTGGTVISEELGLKLEDATLE 314

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 541469458 241 DLGQSKKIIINKDNTTIIDGLGSKSNISKRIIQISKEKEEATSDYDKEKLQERIAKLSGGVAVIKVGA 308
Cdd:PRK00013 315 DLGQAKKVVVTKDNTTIVDGAGDKEAIKARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIKVGA 382
GroEL cd03344
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ...
 1-308 0e+00

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: 517.78  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541469458   1 EVASKANDSAGDGTTTATLLAQSIVNEGLKAVAAGMNPMDLKRGIDKAVNYAIEELKRISVNCSDTKSIEQVGTISANSD 80
Cdd:cd03344   73 EVASKTNDVAGDGTTTATVLARAIIKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKPVKTKEEIAQVATISANGD 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541469458  81 ETVGKLIAEAMSKVGKEGVITVEEGSGLNDELDVVEGMQFDRGYLSPYFINKTESGIVELDNPFILLVDKKITNIRELLP 160
Cdd:cd03344  153 EEIGELIAEAMEKVGKDGVITVEEGKTLETELEVVEGMQFDRGYLSPYFVTDPEKMEVELENPYILLTDKKISSIQELLP 232

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541469458 161 ILENVAKSGKPIVIIAEDVEGEALATLVVNTMRGIVKTVAVKAPGFGDRRKSMLQDIAILTNGNVISEEIGLDLEKITLN 240
Cdd:cd03344  233 ILELVAKAGRPLLIIAEDVEGEALATLVVNKLRGGLKVCAVKAPGFGDRRKAMLEDIAILTGGTVISEELGLKLEDVTLE 312

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 541469458 241 DLGQSKKIIINKDNTTIIDGLGSKSNISKRIIQISKEKEEATSDYDKEKLQERIAKLSGGVAVIKVGA 308
Cdd:cd03344  313 DLGRAKKVVVTKDDTTIIGGAGDKAAIKARIAQIRKQIEETTSDYDKEKLQERLAKLSGGVAVIKVGG 380
GroEL TIGR02348
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ...
 1-308 1.16e-179

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: 506.45  E-value: 1.16e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541469458    1 EVASKANDSAGDGTTTATLLAQSIVNEGLKAVAAGMNPMDLKRGIDKAVNYAIEELKRISVNCSDTKSIEQVGTISANSD 80
Cdd:TIGR02348  74 EVASKTNDVAGDGTTTATVLAQAIVKEGLKNVAAGANPIELKRGIEKAVEAVVEELKKLSKPVKGKKEIAQVATISANND 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541469458   81 ETVGKLIAEAMSKVGKEGVITVEEGSGLNDELDVVEGMQFDRGYLSPYFINKTESGIVELDNPFILLVDKKITNIRELLP 160
Cdd:TIGR02348 154 EEIGSLIAEAMEKVGKDGVITVEESKSLETELEVVEGMQFDRGYISPYFVTDAEKMEVELENPYILITDKKISNIKDLLP 233

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541469458  161 ILENVAKSGKPIVIIAEDVEGEALATLVVNTMRGIVKTVAVKAPGFGDRRKSMLQDIAILTNGNVISEEIGLDLEKITLN 240
Cdd:TIGR02348 234 LLEKVAQSGKPLLIIAEDVEGEALATLVVNKLRGTLNVCAVKAPGFGDRRKAMLEDIAILTGGQVISEELGLKLEEVTLD 313

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 541469458  241 DLGQSKKIIINKDNTTIIDGLGSKSNISKRIIQISKEKEEATSDYDKEKLQERIAKLSGGVAVIKVGA 308
Cdd:TIGR02348 314 DLGKAKKVTVDKDNTTIVEGAGDKAAIKARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIKVGA 381
GroEL COG0459
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ...
 1-268 1.67e-149

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


Pssm-ID: 440227  Cd Length: 497  Bit Score: 428.73  E-value: 1.67e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541469458   1 EVASKANDSAGDGTTTATLLAQSIVNEGLKAVAAGMNPMDLKRGIDKAVNYAIEELKRISVNCSDTKSIEQVGTISANSD 80
Cdd:COG0459   75 EVASKTNDEAGDGTTTATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPVDDKEELAQVATISANGD 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541469458  81 ETVGKLIAEAMSKVGKEGVITVEEGSGLNDELDVVEGMQFDRGYLSPYFINKTESGIVELDNPFILLVDKKITNIRELLP 160
Cdd:COG0459  155 EEIGELIAEAMEKVGKDGVITVEEGKGLETELEVVEGMQFDKGYLSPYFVTDPEKMPAELENAYILLTDKKISSIQDLLP 234

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541469458 161 ILENVAKSGKPIVIIAEDVEGEALATLVVNTMRGIVKTVAVKAPGFGDRRKSMLQDIAILTNGNVISEEIGLDLEKITLN 240
Cdd:COG0459  235 LLEKVAQSGKPLLIIAEDIDGEALATLVVNGIRGVLRVVAVKAPGFGDRRKAMLEDIAILTGGRVISEDLGLKLEDVTLD 314

                        250       260
                 ....*....|....*....|....*...
gi 541469458 241 DLGQSKKIIINKDNTTIIDGLGSKSNIS 268
Cdd:COG0459  315 DLGRAKRVEVDKDNTTIVEGAGNPKAIV 342
Cpn60_TCP1 pfam00118
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ...
 1-264 1.11e-31

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: 123.08  E-value: 1.11e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541469458    1 EVASKANDSAGDGTTTATLLAQSIVNEGLKAVAAGMNPMDLKRGIDKAVNYAIEELKR---ISVNCSDTKSIEQVGTISA 77
Cdd:pfam00118  50 EAAKAQDEEVGDGTTTVVVLAGELLEEAEKLLAAGVHPTTIIEGYEKALEKALEILDSiisIPVEDVDREDLLKVARTSL 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541469458   78 NSD------ETVGKLIAEAMSKVGKE---------GVITVEEGSGlnDELDVVEGMQFDRGYLSPyfinkteSGIVELDN 142
Cdd:pfam00118 130 SSKiisresDFLAKLVVDAVLAIPKNdgsfdlgniGVVKILGGSL--EDSELVDGVVLDKGPLHP-------DMPKRLEN 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541469458  143 PFILLVDKKI--------TNIR----------------ELLPILENVAKSGKPIVIIAEDVEGEALATLVVNTMRGIVKT 198
Cdd:pfam00118 201 AKVLLLNCSLeyektetkATVVlsdaeqlerflkaeeeQILEIVEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMALRRV 280

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 541469458  199 vavkapgfgdrRKSMLQDIAILTNGNVISeeiglDLEKITLNDLGQSKKI---IINKDNTTIIDGLGSK 264
Cdd:pfam00118 281 -----------KKRDLERLAKATGARAVS-----SLDDLTPDDLGTAGKVeeeKIGDEKYTFIEGCKSP 333
 
Name Accession Description Interval E-value
groEL PRK00013
chaperonin GroEL; Reviewed
 1-308 0e+00

chaperonin GroEL; Reviewed


Pssm-ID: 234573  Cd Length: 542  Bit Score: 566.29  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541469458   1 EVASKANDSAGDGTTTATLLAQSIVNEGLKAVAAGMNPMDLKRGIDKAVNYAIEELKRISVNCSDTKSIEQVGTISANSD 80
Cdd:PRK00013  75 EVASKTNDVAGDGTTTATVLAQAIVREGLKNVAAGANPMDLKRGIDKAVEAAVEELKKISKPVEDKEEIAQVATISANGD 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541469458  81 ETVGKLIAEAMSKVGKEGVITVEEGSGLNDELDVVEGMQFDRGYLSPYFINKTESGIVELDNPFILLVDKKITNIRELLP 160
Cdd:PRK00013 155 EEIGKLIAEAMEKVGKEGVITVEESKGFETELEVVEGMQFDRGYLSPYFVTDPEKMEAELENPYILITDKKISNIQDLLP 234

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541469458 161 ILENVAKSGKPIVIIAEDVEGEALATLVVNTMRGIVKTVAVKAPGFGDRRKSMLQDIAILTNGNVISEEIGLDLEKITLN 240
Cdd:PRK00013 235 VLEQVAQSGKPLLIIAEDVEGEALATLVVNKLRGTLKVVAVKAPGFGDRRKAMLEDIAILTGGTVISEELGLKLEDATLE 314

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 541469458 241 DLGQSKKIIINKDNTTIIDGLGSKSNISKRIIQISKEKEEATSDYDKEKLQERIAKLSGGVAVIKVGA 308
Cdd:PRK00013 315 DLGQAKKVVVTKDNTTIVDGAGDKEAIKARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIKVGA 382
GroEL cd03344
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ...
 1-308 0e+00

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: 517.78  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541469458   1 EVASKANDSAGDGTTTATLLAQSIVNEGLKAVAAGMNPMDLKRGIDKAVNYAIEELKRISVNCSDTKSIEQVGTISANSD 80
Cdd:cd03344   73 EVASKTNDVAGDGTTTATVLARAIIKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKPVKTKEEIAQVATISANGD 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541469458  81 ETVGKLIAEAMSKVGKEGVITVEEGSGLNDELDVVEGMQFDRGYLSPYFINKTESGIVELDNPFILLVDKKITNIRELLP 160
Cdd:cd03344  153 EEIGELIAEAMEKVGKDGVITVEEGKTLETELEVVEGMQFDRGYLSPYFVTDPEKMEVELENPYILLTDKKISSIQELLP 232

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541469458 161 ILENVAKSGKPIVIIAEDVEGEALATLVVNTMRGIVKTVAVKAPGFGDRRKSMLQDIAILTNGNVISEEIGLDLEKITLN 240
Cdd:cd03344  233 ILELVAKAGRPLLIIAEDVEGEALATLVVNKLRGGLKVCAVKAPGFGDRRKAMLEDIAILTGGTVISEELGLKLEDVTLE 312

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 541469458 241 DLGQSKKIIINKDNTTIIDGLGSKSNISKRIIQISKEKEEATSDYDKEKLQERIAKLSGGVAVIKVGA 308
Cdd:cd03344  313 DLGRAKKVVVTKDDTTIIGGAGDKAAIKARIAQIRKQIEETTSDYDKEKLQERLAKLSGGVAVIKVGG 380
groEL PRK12849
chaperonin GroEL; Reviewed
 1-308 0e+00

chaperonin GroEL; Reviewed


Pssm-ID: 237230  Cd Length: 542  Bit Score: 517.05  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541469458   1 EVASKANDSAGDGTTTATLLAQSIVNEGLKAVAAGMNPMDLKRGIDKAVNYAIEELKRISVNCSDTKSIEQVGTISANSD 80
Cdd:PRK12849  75 EVASKTNDVAGDGTTTATVLAQALVQEGLKNVAAGANPMDLKRGIDKAVEAVVEELKALARPVSGSEEIAQVATISANGD 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541469458  81 ETVGKLIAEAMSKVGKEGVITVEEGSGLNDELDVVEGMQFDRGYLSPYFINKTESGIVELDNPFILLVDKKITNIRELLP 160
Cdd:PRK12849 155 EEIGELIAEAMEKVGKDGVITVEESKTLETELEVTEGMQFDRGYLSPYFVTDPERMEAVLEDPLILLTDKKISSLQDLLP 234

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541469458 161 ILENVAKSGKPIVIIAEDVEGEALATLVVNTMRGIVKTVAVKAPGFGDRRKSMLQDIAILTNGNVISEEIGLDLEKITLN 240
Cdd:PRK12849 235 LLEKVAQSGKPLLIIAEDVEGEALATLVVNKLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGLKLEEVTLD 314

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 541469458 241 DLGQSKKIIINKDNTTIIDGLGSKSNISKRIIQISKEKEEATSDYDKEKLQERIAKLSGGVAVIKVGA 308
Cdd:PRK12849 315 DLGRAKRVTITKDNTTIVDGAGDKEAIEARVAQIRRQIEETTSDYDREKLQERLAKLAGGVAVIKVGA 382
GroEL TIGR02348
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ...
 1-308 1.16e-179

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: 506.45  E-value: 1.16e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541469458    1 EVASKANDSAGDGTTTATLLAQSIVNEGLKAVAAGMNPMDLKRGIDKAVNYAIEELKRISVNCSDTKSIEQVGTISANSD 80
Cdd:TIGR02348  74 EVASKTNDVAGDGTTTATVLAQAIVKEGLKNVAAGANPIELKRGIEKAVEAVVEELKKLSKPVKGKKEIAQVATISANND 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541469458   81 ETVGKLIAEAMSKVGKEGVITVEEGSGLNDELDVVEGMQFDRGYLSPYFINKTESGIVELDNPFILLVDKKITNIRELLP 160
Cdd:TIGR02348 154 EEIGSLIAEAMEKVGKDGVITVEESKSLETELEVVEGMQFDRGYISPYFVTDAEKMEVELENPYILITDKKISNIKDLLP 233

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541469458  161 ILENVAKSGKPIVIIAEDVEGEALATLVVNTMRGIVKTVAVKAPGFGDRRKSMLQDIAILTNGNVISEEIGLDLEKITLN 240
Cdd:TIGR02348 234 LLEKVAQSGKPLLIIAEDVEGEALATLVVNKLRGTLNVCAVKAPGFGDRRKAMLEDIAILTGGQVISEELGLKLEEVTLD 313

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 541469458  241 DLGQSKKIIINKDNTTIIDGLGSKSNISKRIIQISKEKEEATSDYDKEKLQERIAKLSGGVAVIKVGA 308
Cdd:TIGR02348 314 DLGKAKKVTVDKDNTTIVEGAGDKAAIKARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIKVGA 381
groEL PRK12850
chaperonin GroEL; Reviewed
 1-308 1.73e-170

chaperonin GroEL; Reviewed


Pssm-ID: 237231  Cd Length: 544  Bit Score: 483.84  E-value: 1.73e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541469458   1 EVASKANDSAGDGTTTATLLAQSIVNEGLKAVAAGMNPMDLKRGIDKAVNYAIEELKRISVNCSDTKSIEQVGTISANSD 80
Cdd:PRK12850  76 EVASKTNDLAGDGTTTATVLAQAIVREGAKLVAAGMNPMDLKRGIDLAVAAVVDELKKIAKKVTSSKEIAQVATISANGD 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541469458  81 ETVGKLIAEAMSKVGKEGVITVEEGSGLNDELDVVEGMQFDRGYLSPYFINKTESGIVELDNPFILLVDKKITNIRELLP 160
Cdd:PRK12850 156 ESIGEMIAEAMDKVGKEGVITVEEAKTLGTELDVVEGMQFDRGYLSPYFVTNPEKMRAELEDPYILLHEKKISNLQDLLP 235

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541469458 161 ILENVAKSGKPIVIIAEDVEGEALATLVVNTMRGIVKTVAVKAPGFGDRRKSMLQDIAILTNGNVISEEIGLDLEKITLN 240
Cdd:PRK12850 236 ILEAVVQSGRPLLIIAEDVEGEALATLVVNKLRGGLKSVAVKAPGFGDRRKAMLEDIAVLTGGQVISEDLGIKLENVTLD 315

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 541469458 241 DLGQSKKIIINKDNTTIIDGLGSKSNISKRIIQISKEKEEATSDYDKEKLQERIAKLSGGVAVIKVGA 308
Cdd:PRK12850 316 MLGRAKRVLITKENTTIIDGAGDKKNIEARVKQIRAQIEETTSDYDREKLQERLAKLAGGVAVIRVGG 383
groEL PRK12851
chaperonin GroEL; Reviewed
 1-308 3.57e-158

chaperonin GroEL; Reviewed


Pssm-ID: 171770  Cd Length: 541  Bit Score: 452.27  E-value: 3.57e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541469458   1 EVASKANDSAGDGTTTATLLAQSIVNEGLKAVAAGMNPMDLKRGIDKAVNYAIEELKRISVNCSDTKSIEQVGTISANSD 80
Cdd:PRK12851  76 EVASKTNDVAGDGTTTATVLAQAIVREGAKAVAAGANPMDLKRGIDRAVAAVVEELKANARPVTTNAEIAQVATISANGD 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541469458  81 ETVGKLIAEAMSKVGKEGVITVEEGSGLNDELDVVEGMQFDRGYLSPYFINKTESGIVELDNPFILLVDKKITNIRELLP 160
Cdd:PRK12851 156 AEIGRLVAEAMEKVGNEGVITVEESKTAETELEVVEGMQFDRGYLSPYFVTDADKMEAELEDPYILIHEKKISNLQDLLP 235

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541469458 161 ILENVAKSGKPIVIIAEDVEGEALATLVVNTMRGIVKTVAVKAPGFGDRRKSMLQDIAILTNGNVISEEIGLDLEKITLN 240
Cdd:PRK12851 236 VLEAVVQSGKPLLIIAEDVEGEALATLVVNKLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGIKLENVTLE 315

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 541469458 241 DLGQSKKIIINKDNTTIIDGLGSKSNISKRIIQISKEKEEATSDYDKEKLQERIAKLSGGVAVIKVGA 308
Cdd:PRK12851 316 QLGRAKKVVVEKENTTIIDGAGSKTEIEGRVAQIRAQIEETTSDYDREKLQERLAKLAGGVAVIRVGA 383
groEL PRK12852
chaperonin GroEL; Reviewed
 1-308 1.37e-154

chaperonin GroEL; Reviewed


Pssm-ID: 237232  Cd Length: 545  Bit Score: 443.52  E-value: 1.37e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541469458   1 EVASKANDSAGDGTTTATLLAQSIVNEGLKAVAAGMNPMDLKRGIDKAVNYAIEELKRISVNCSDTKSIEQVGTISANSD 80
Cdd:PRK12852  76 EVASKTNDLAGDGTTTATVLAQAIVREGAKAVAAGMNPMDLKRGIDIAVAAVVKDIEKRAKPVASSAEIAQVGTISANGD 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541469458  81 ETVGKLIAEAMSKVGKEGVITVEEGSGLNDELDVVEGMQFDRGYLSPYFINKTESGIVELDNPFILLVDKKITNIRELLP 160
Cdd:PRK12852 156 AAIGKMIAQAMQKVGNEGVITVEENKSLETEVDIVEGMKFDRGYLSPYFVTNAEKMTVELDDAYILLHEKKLSGLQAMLP 235

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541469458 161 ILENVAKSGKPIVIIAEDVEGEALATLVVNTMRGIVKTVAVKAPGFGDRRKSMLQDIAILTNGNVISEEIGLDLEKITLN 240
Cdd:PRK12852 236 VLEAVVQSGKPLLIIAEDVEGEALATLVVNRLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGQLISEDLGIKLENVTLK 315

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 541469458 241 DLGQSKKIIINKDNTTIIDGLGSKSNISKRIIQISKEKEEATSDYDKEKLQERIAKLSGGVAVIKVGA 308
Cdd:PRK12852 316 MLGRAKKVVIDKENTTIVNGAGKKADIEARVGQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGG 383
GroEL COG0459
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ...
 1-268 1.67e-149

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


Pssm-ID: 440227  Cd Length: 497  Bit Score: 428.73  E-value: 1.67e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541469458   1 EVASKANDSAGDGTTTATLLAQSIVNEGLKAVAAGMNPMDLKRGIDKAVNYAIEELKRISVNCSDTKSIEQVGTISANSD 80
Cdd:COG0459   75 EVASKTNDEAGDGTTTATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPVDDKEELAQVATISANGD 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541469458  81 ETVGKLIAEAMSKVGKEGVITVEEGSGLNDELDVVEGMQFDRGYLSPYFINKTESGIVELDNPFILLVDKKITNIRELLP 160
Cdd:COG0459  155 EEIGELIAEAMEKVGKDGVITVEEGKGLETELEVVEGMQFDKGYLSPYFVTDPEKMPAELENAYILLTDKKISSIQDLLP 234

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541469458 161 ILENVAKSGKPIVIIAEDVEGEALATLVVNTMRGIVKTVAVKAPGFGDRRKSMLQDIAILTNGNVISEEIGLDLEKITLN 240
Cdd:COG0459  235 LLEKVAQSGKPLLIIAEDIDGEALATLVVNGIRGVLRVVAVKAPGFGDRRKAMLEDIAILTGGRVISEDLGLKLEDVTLD 314

                        250       260
                 ....*....|....*....|....*...
gi 541469458 241 DLGQSKKIIINKDNTTIIDGLGSKSNIS 268
Cdd:COG0459  315 DLGRAKRVEVDKDNTTIVEGAGNPKAIV 342
PTZ00114 PTZ00114
Heat shock protein 60; Provisional
 1-308 1.79e-149

Heat shock protein 60; Provisional


Pssm-ID: 185455  Cd Length: 555  Bit Score: 430.87  E-value: 1.79e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541469458   1 EVASKANDSAGDGTTTATLLAQSIVNEGLKAVAAGMNPMDLKRGIDKAVNYAIEELKRISVNCSDTKSIEQVGTISANSD 80
Cdd:PTZ00114  87 QVASKTNDKAGDGTTTATILARAIFREGCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQSRPVKTKEDILNVATISANGD 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541469458  81 ETVGKLIAEAMSKVGKEGVITVEEGSGLNDELDVVEGMQFDRGYLSPYFINKTESGIVELDNPFILLVDKKITNIRELLP 160
Cdd:PTZ00114 167 VEIGSLIADAMDKVGKDGTITVEDGKTLEDELEVVEGMSFDRGYISPYFVTNEKTQKVELENPLILVTDKKISSIQSILP 246

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541469458 161 ILENVAKSGKPIVIIAEDVEGEALATLVVNTMRGIVKTVAVKAPGFGDRRKSMLQDIAILTNGNVISEE-IGLDLEKITL 239
Cdd:PTZ00114 247 ILEHAVKNKRPLLIIAEDVEGEALQTLIINKLRGGLKVCAVKAPGFGDNRKDILQDIAVLTGATVVSEDnVGLKLDDFDP 326

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 541469458 240 NDLGQSKKIIINKDNTTIIDGLGSKSNISKRIIQISKEKEEATSDYDKEKLQERIAKLSGGVAVIKVGA 308
Cdd:PTZ00114 327 SMLGSAKKVTVTKDETVILTGGGDKAEIKERVELLRSQIERTTSEYDKEKLKERLAKLSGGVAVIKVGG 395
groEL CHL00093
chaperonin GroEL
 3-308 2.71e-145

chaperonin GroEL


Pssm-ID: 177025  Cd Length: 529  Bit Score: 419.12  E-value: 2.71e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541469458   3 ASKANDSAGDGTTTATLLAQSIVNEGLKAVAAGMNPMDLKRGIDKAVNYAIEELKRISVNCSDTKSIEQVGTISANSDET 82
Cdd:CHL00093  77 ASKTNDVAGDGTTTATVLAYAIVKQGMKNVAAGANPISLKRGIEKATQYVVSQIAEYARPVEDIQAITQVASISAGNDEE 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541469458  83 VGKLIAEAMSKVGKEGVITVEEGSGLNDELDVVEGMQFDRGYLSPYFINKTESGIVELDNPFILLVDKKITNIR-ELLPI 161
Cdd:CHL00093 157 VGSMIADAIEKVGREGVISLEEGKSTVTELEITEGMRFEKGFISPYFVTDTERMEVVQENPYILLTDKKITLVQqDLLPI 236

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541469458 162 LENVAKSGKPIVIIAEDVEGEALATLVVNTMRGIVKTVAVKAPGFGDRRKSMLQDIAILTNGNVISEEIGLDLEKITLND 241
Cdd:CHL00093 237 LEQVTKTKRPLLIIAEDVEKEALATLVLNKLRGIVNVVAVRAPGFGDRRKAMLEDIAILTGGQVITEDAGLSLETIQLDL 316

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 541469458 242 LGQSKKIIINKDNTTIIdGLGSKSNISKRIIQISKEKEEATSDYDKEKLQERIAKLSGGVAVIKVGA 308
Cdd:CHL00093 317 LGQARRIIVTKDSTTII-ADGNEEQVKARCEQLRKQIEIADSSYEKEKLQERLAKLSGGVAVIKVGA 382
PRK14104 PRK14104
chaperonin GroEL; Provisional
 1-308 1.22e-131

chaperonin GroEL; Provisional


Pssm-ID: 172594  Cd Length: 546  Bit Score: 385.15  E-value: 1.22e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541469458   1 EVASKANDSAGDGTTTATLLAQSIVNEGLKAVAAGMNPMDLKRGIDKAVNYAIEELKRISVNCSDTKSIEQVGTISANSD 80
Cdd:PRK14104  76 EVASKSADAAGDGTTTATVLAQAIVREGAKSVAAGMNPMDLKRGIDLAVEAVVADLVKNSKKVTSNDEIAQVGTISANGD 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541469458  81 ETVGKLIAEAMSKVGKEGVITVEEGSGLNDELDVVEGMQFDRGYLSPYFINKTESGIVELDNPFILLVDKKITNIRELLP 160
Cdd:PRK14104 156 AEIGKFLADAMKKVGNEGVITVEEAKSLETELDVVEGMQFDRGYISPYFVTNADKMRVEMDDAYILINEKKLSSLNELLP 235

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541469458 161 ILENVAKSGKPIVIIAEDVEGEALATLVVNTMRGIVKTVAVKAPGFGDRRKSMLQDIAILTNGNVISEEIGLDLEKITLN 240
Cdd:PRK14104 236 LLEAVVQTGKPLVIVAEDVEGEALATLVVNRLRGGLKVAAVKAPGFGDRRKAMLQDIAILTGGQAISEDLGIKLENVTLQ 315

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 541469458 241 DLGQSKKIIINKDNTTIIDGLGSKSNISKRIIQISKEKEEATSDYDKEKLQERIAKLSGGVAVIKVGA 308
Cdd:PRK14104 316 MLGRAKKVMIDKENTTIVNGAGKKADIEARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGG 383
PLN03167 PLN03167
Chaperonin-60 beta subunit; Provisional
 1-308 8.93e-109

Chaperonin-60 beta subunit; Provisional


Pssm-ID: 215611 [Multi-domain]  Cd Length: 600  Bit Score: 328.42  E-value: 8.93e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541469458   1 EVASKANDSAGDGTTTATLLAQSIVNEGLKAVAAGMNPMDLKRGIDKAVNYAIEELKRISVNCSDTKsIEQVGTISANSD 80
Cdd:PLN03167 131 QAAAKTNDLAGDGTTTSVVLAQGLIAEGVKVVAAGANPVQITRGIEKTAKALVKELKKMSKEVEDSE-LADVAAVSAGNN 209

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541469458  81 ETVGKLIAEAMSKVGKEGVITVEEGSGLNDELDVVEGMQFDRGYLSPYFINKTESGIVELDNPFILLVDKKITNIRELLP 160
Cdd:PLN03167 210 YEVGNMIAEAMSKVGRKGVVTLEEGKSAENNLYVVEGMQFDRGYISPYFVTDSEKMSVEYDNCKLLLVDKKITNARDLIG 289

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541469458 161 ILENVAKSGKPIVIIAEDVEGEALATLVVNTMRGIVKTVAVKAPGFGDRRKSMLQDIAILTNGNVISEEIGLDLEKITLN 240
Cdd:PLN03167 290 ILEDAIRGGYPLLIIAEDIEQEALATLVVNKLRGSLKIAALKAPGFGERKSQYLDDIAILTGGTVIREEVGLSLDKVGKE 369

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 541469458 241 DLGQSKKIIINKDNTTIIDGLGSKSNISKRIIQISKEKEEATSDYDKEKLQERIAKLSGGVAVIKVGA 308
Cdd:PLN03167 370 VLGTAAKVVLTKDTTTIVGDGSTQEAVNKRVAQIKNLIEAAEQDYEKEKLNERIAKLSGGVAVIQVGA 437
chaperonin_type_I_II cd00309
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ...
 1-265 1.29e-60

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: 199.96  E-value: 1.29e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541469458   1 EVASKANDSAGDGTTTATLLAQSIVNEGLKAVAAGMNPMDLKRGIDKAVNYAIEELKRISV--NCSDTKSIEQVGTISAN 78
Cdd:cd00309   69 EVAKSQDDEVGDGTTTVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVpiDVEDREELLKVATTSLN 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541469458  79 S------DETVGKLIAEAMSKVGKE------GVITVEEGSG---LNDELdvVEGMQFDRGYLSPYFinktesgIVELDNP 143
Cdd:cd00309  149 SklvsggDDFLGELVVDAVLKVGKEngdvdlGVIRVEKKKGgslEDSEL--VVGMVFDKGYLSPYM-------PKRLENA 219

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541469458 144 FILLVDKKITNirellpilenvaksgkpiVIIAED-VEGEALATLVVNtmrgivKTVAVKApgfgdRRKSMLQDIAILTN 222
Cdd:cd00309  220 KILLLDCKLEY------------------VVIAEKgIDDEALHYLAKL------GIMAVRR-----VRKEDLERIAKATG 270

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 541469458 223 GNVISEeigldLEKITLNDLGQSKKIIINK----DNTTIIDGLGSKS 265
Cdd:cd00309  271 ATIVSR-----LEDLTPEDLGTAGLVEETKigdeKYTFIEGCKGGKV 312
Cpn60_TCP1 pfam00118
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ...
 1-264 1.11e-31

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: 123.08  E-value: 1.11e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541469458    1 EVASKANDSAGDGTTTATLLAQSIVNEGLKAVAAGMNPMDLKRGIDKAVNYAIEELKR---ISVNCSDTKSIEQVGTISA 77
Cdd:pfam00118  50 EAAKAQDEEVGDGTTTVVVLAGELLEEAEKLLAAGVHPTTIIEGYEKALEKALEILDSiisIPVEDVDREDLLKVARTSL 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541469458   78 NSD------ETVGKLIAEAMSKVGKE---------GVITVEEGSGlnDELDVVEGMQFDRGYLSPyfinkteSGIVELDN 142
Cdd:pfam00118 130 SSKiisresDFLAKLVVDAVLAIPKNdgsfdlgniGVVKILGGSL--EDSELVDGVVLDKGPLHP-------DMPKRLEN 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541469458  143 PFILLVDKKI--------TNIR----------------ELLPILENVAKSGKPIVIIAEDVEGEALATLVVNTMRGIVKT 198
Cdd:pfam00118 201 AKVLLLNCSLeyektetkATVVlsdaeqlerflkaeeeQILEIVEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMALRRV 280

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 541469458  199 vavkapgfgdrRKSMLQDIAILTNGNVISeeiglDLEKITLNDLGQSKKI---IINKDNTTIIDGLGSK 264
Cdd:pfam00118 281 -----------KKRDLERLAKATGARAVS-----SLDDLTPDDLGTAGKVeeeKIGDEKYTFIEGCKSP 333
chaperonin_like cd03333
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ...
 67-265 3.50e-27

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: 105.24  E-value: 3.50e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541469458  67 KSIEQVGTISANS-----DETVGKLIAEAMSKVGKE------GVITVEEGSG---LNDELdvVEGMQFDRGYLSPYFink 132
Cdd:cd03333    2 ELLLQVATTSLNSklsswDDFLGKLVVDAVLKVGPDnrmddlGVIKVEKIPGgslEDSEL--VVGVVFDKGYASPYM--- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541469458 133 tesgIVELDNPFILLVDKKITNirellpilenvaksgkpiVIIAED-VEGEALATLVVntmRGIvktVAVKApgfgdRRK 211
Cdd:cd03333   77 ----PKRLENAKILLLDCPLEY------------------VVIAEKgIDDLALHYLAK---AGI---MAVRR-----VKK 123

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 541469458 212 SMLQDIAILTNGNVISEeigldLEKITLNDLGQSKKI----IINKDNTTIIDGLGSKS 265
Cdd:cd03333  124 EDLERIARATGATIVSS-----LEDLTPEDLGTAELVeetkIGEEKLTFIEGCKGGKA 176
TCP1_eta cd03340
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ...
 4-92 1.76e-06

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: 49.21  E-value: 1.76e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541469458   4 SKANDS-AGDGTTTATLLAQSIVNEGLKAVAAGMNPMDLKRGIDKAVNYAIEELKRISVNCSDTKSIEQvgtisansDET 82
Cdd:cd03340   79 AKSQDAeVGDGTTSVVVLAGEFLKEAKPFIEDGVHPQIIIRGYRKALQLAIEKIKEIAVNIDKEDKEEQ--------REL 150

                         90
                 ....*....|
gi 541469458  83 VGKLIAEAMS 92
Cdd:cd03340  151 LEKCAATALN 160
TCP1_delta cd03338
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ...
 4-79 4.38e-05

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: 44.97  E-value: 4.38e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 541469458   4 SKANDS-AGDGTTTATLLAQSIVNEGLKAVAAGMNPMDLKRGIDKAVNYAIEELKRISVNCS--DTKSIEQVGTISANS 79
Cdd:cd03338   71 SKAQDIeAGDGTTSVVVLAGALLSACESLLKKGIHPTVISESFQIAAKKAVEILDSMSIPVDlnDRESLIKSATTSLNS 149
 
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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