NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1123885116|gb|APQ31210|]
View 

chaperone GroEL, partial [Tsukamurella inchonensis]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 1-225 6.95e-131

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: 379.08  E-value: 6.95e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123885116   1 MLQDMAILTGGQVISEEIGLSLDTAGLEVLGQARQVVVTKDETTIVDGAGSKEQIEGRVSQIRAEIENSDSDYDREKLQE 80
Cdd:PRK00013  287 MLEDIAILTGGTVISEELGLKLEDATLEDLGQAKKVVVTKDNTTIVDGAGDKEAIKARVAQIKAQIEETTSDYDREKLQE 366

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123885116  81 RLAKLAGGVAVIKAGAATEVELKERKHRIEDAVRNAKAAVEEGIVAGGGAALAQSGAVFESL-ALEGDEATGANIVKVAL 159
Cdd:PRK00013  367 RLAKLAGGVAVIKVGAATEVEMKEKKDRVEDALHATRAAVEEGIVPGGGVALLRAAPALEALkGLNGDEATGINIVLRAL 446

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1123885116 160 DAPVKQIAVNAGLEPGVVAEKVRNS-PAGTGLNAATGVYEDLLAAGINDPVKVTRSALQNAASIAAL 225
Cdd:PRK00013  447 EAPLRQIAENAGLEGSVVVEKVKNGkGKGYGYNAATGEYVDMIEAGIIDPTKVTRSALQNAASVAGL 513
 
Name Accession Description Interval E-value
groEL PRK00013
chaperonin GroEL; Reviewed
 1-225 6.95e-131

chaperonin GroEL; Reviewed


Pssm-ID: 234573  Cd Length: 542  Bit Score: 379.08  E-value: 6.95e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123885116   1 MLQDMAILTGGQVISEEIGLSLDTAGLEVLGQARQVVVTKDETTIVDGAGSKEQIEGRVSQIRAEIENSDSDYDREKLQE 80
Cdd:PRK00013  287 MLEDIAILTGGTVISEELGLKLEDATLEDLGQAKKVVVTKDNTTIVDGAGDKEAIKARVAQIKAQIEETTSDYDREKLQE 366

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123885116  81 RLAKLAGGVAVIKAGAATEVELKERKHRIEDAVRNAKAAVEEGIVAGGGAALAQSGAVFESL-ALEGDEATGANIVKVAL 159
Cdd:PRK00013  367 RLAKLAGGVAVIKVGAATEVEMKEKKDRVEDALHATRAAVEEGIVPGGGVALLRAAPALEALkGLNGDEATGINIVLRAL 446

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1123885116 160 DAPVKQIAVNAGLEPGVVAEKVRNS-PAGTGLNAATGVYEDLLAAGINDPVKVTRSALQNAASIAAL 225
Cdd:PRK00013  447 EAPLRQIAENAGLEGSVVVEKVKNGkGKGYGYNAATGEYVDMIEAGIIDPTKVTRSALQNAASVAGL 513
GroEL cd03344
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ...
 1-225 9.12e-116

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: 339.82  E-value: 9.12e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123885116   1 MLQDMAILTGGQVISEEIGLSLDTAGLEVLGQARQVVVTKDETTIVDGAGSKEQIEGRVSQIRAEIENSDSDYDREKLQE 80
Cdd:cd03344   285 MLEDIAILTGGTVISEELGLKLEDVTLEDLGRAKKVVVTKDDTTIIGGAGDKAAIKARIAQIRKQIEETTSDYDKEKLQE 364

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123885116  81 RLAKLAGGVAVIKAGAATEVELKERKHRIEDAVRNAKAAVEEGIVAGGGAALAQSGAVFESL-ALEGDEATGANIVKVAL 159
Cdd:cd03344   365 RLAKLSGGVAVIKVGGATEVELKEKKDRVEDALNATRAAVEEGIVPGGGVALLRASPALDKLkALNGDEKLGIEIVRRAL 444

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1123885116 160 DAPVKQIAVNAGLEPGVVAEKVRNSPAGTGLNAATGVYEDLLAAGINDPVKVTRSALQNAASIAAL 225
Cdd:cd03344   445 EAPLRQIAENAGVDGSVVVEKVLESPDGFGYDAATGEYVDMIEAGIIDPTKVVRSALQNAASVASL 510
GroEL TIGR02348
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ...
 1-225 7.78e-113

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: 332.72  E-value: 7.78e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123885116   1 MLQDMAILTGGQVISEEIGLSLDTAGLEVLGQARQVVVTKDETTIVDGAGSKEQIEGRVSQIRAEIENSDSDYDREKLQE 80
Cdd:TIGR02348 286 MLEDIAILTGGQVISEELGLKLEEVTLDDLGKAKKVTVDKDNTTIVEGAGDKAAIKARVAQIKAQIEETTSDYDREKLQE 365

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123885116  81 RLAKLAGGVAVIKAGAATEVELKERKHRIEDAVRNAKAAVEEGIVAGGGAALAQSGAVFESLALEG-DEATGANIVKVAL 159
Cdd:TIGR02348 366 RLAKLAGGVAVIKVGAATETEMKEKKLRIEDALNATRAAVEEGIVPGGGVALLRAAAALEGLKGDGeDEAIGIDIVKRAL 445

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1123885116 160 DAPVKQIAVNAGLEPGVVAEKVRNSPAGTGLNAATGVYEDLLAAGINDPVKVTRSALQNAASIAAL 225
Cdd:TIGR02348 446 EAPLRQIAENAGLDGAVVAEKVKELKGNFGFNAATGEYEDLVEAGIIDPTKVTRSALQNAASIAGL 511
GroEL COG0459
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ...
 1-225 1.64e-79

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


Pssm-ID: 440227  Cd Length: 497  Bit Score: 246.53  E-value: 1.64e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123885116   1 MLQDMAILTGGQVISEEIGLSLDTAGLEVLGQARQVVVTKDETTIVDGAGSKEQIegrvsqiraeiensdsdydreklqe 80
Cdd:COG0459   287 MLEDIAILTGGRVISEDLGLKLEDVTLDDLGRAKRVEVDKDNTTIVEGAGNPKAI------------------------- 341

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123885116  81 rlaklaggvaVIKAGAATEVELKERKHRIEDAVRNAKAAVEEGIVAGGGAALAQSGAVFESLA--LEGDEATGANIVKVA 158
Cdd:COG0459   342 ----------VILVGAATEVEVKERKRRVEDALHATRAAVEEGIVPGGGAALLRAARALRELAakLEGDEQLGIEIVARA 411

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1123885116 159 LDAPVKQIAVNAGLEPGVVAEKVRNSP-AGTGLNAATGVYEDLLAAGINDPVKVTRSALQNAASIAAL 225
Cdd:COG0459   412 LEAPLRQIAENAGLDGSVVVEKVRAAKdKGFGFDAATGEYVDMLEAGVIDPAKVKRSALQNAASVAGL 479
Cpn60_TCP1 pfam00118
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ...
 1-225 1.18e-24

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: 100.74  E-value: 1.18e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123885116   1 MLQDMAILTGGQVISeeiglSLDTAGLEVLGQA---RQVVVTKDETTIVDGAGSkeqiegrvsqiraeiensdsdydrek 77
Cdd:pfam00118 284 DLERLAKATGARAVS-----SLDDLTPDDLGTAgkvEEEKIGDEKYTFIEGCKS-------------------------- 332

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123885116  78 lqerlaklaGGVAVIKAGAATEVELKERKHRIEDAVRNAKAAVEEG-IVAGGGAALAQSGAVFESLA--LEGDEATGANI 154
Cdd:pfam00118 333 ---------PKAATILLRGATDHVLDEIERSIHDALCVVKNAIEDPrVVPGGGAVEMELARALREYAksVSGKEQLAIEA 403

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1123885116 155 VKVALDAPVKQIAVNAGLEPGVVAEKVRNSPAG----TGLNAATGVYEDLLAAGINDPVKVTRSALQNAASIAAL 225
Cdd:pfam00118 404 FAEALEVIPKTLAENAGLDPIEVLAELRAAHASgekhAGIDVETGEIIDMKEAGVVDPLKVKRQALKSATEAAST 478
 
Name Accession Description Interval E-value
groEL PRK00013
chaperonin GroEL; Reviewed
 1-225 6.95e-131

chaperonin GroEL; Reviewed


Pssm-ID: 234573  Cd Length: 542  Bit Score: 379.08  E-value: 6.95e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123885116   1 MLQDMAILTGGQVISEEIGLSLDTAGLEVLGQARQVVVTKDETTIVDGAGSKEQIEGRVSQIRAEIENSDSDYDREKLQE 80
Cdd:PRK00013  287 MLEDIAILTGGTVISEELGLKLEDATLEDLGQAKKVVVTKDNTTIVDGAGDKEAIKARVAQIKAQIEETTSDYDREKLQE 366

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123885116  81 RLAKLAGGVAVIKAGAATEVELKERKHRIEDAVRNAKAAVEEGIVAGGGAALAQSGAVFESL-ALEGDEATGANIVKVAL 159
Cdd:PRK00013  367 RLAKLAGGVAVIKVGAATEVEMKEKKDRVEDALHATRAAVEEGIVPGGGVALLRAAPALEALkGLNGDEATGINIVLRAL 446

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1123885116 160 DAPVKQIAVNAGLEPGVVAEKVRNS-PAGTGLNAATGVYEDLLAAGINDPVKVTRSALQNAASIAAL 225
Cdd:PRK00013  447 EAPLRQIAENAGLEGSVVVEKVKNGkGKGYGYNAATGEYVDMIEAGIIDPTKVTRSALQNAASVAGL 513
groEL PRK12849
chaperonin GroEL; Reviewed
 1-225 6.25e-119

chaperonin GroEL; Reviewed


Pssm-ID: 237230  Cd Length: 542  Bit Score: 348.72  E-value: 6.25e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123885116   1 MLQDMAILTGGQVISEEIGLSLDTAGLEVLGQARQVVVTKDETTIVDGAGSKEQIEGRVSQIRAEIENSDSDYDREKLQE 80
Cdd:PRK12849  287 MLEDIAILTGGTVISEDLGLKLEEVTLDDLGRAKRVTITKDNTTIVDGAGDKEAIEARVAQIRRQIEETTSDYDREKLQE 366

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123885116  81 RLAKLAGGVAVIKAGAATEVELKERKHRIEDAVRNAKAAVEEGIVAGGGAALAQSGAVFESLA-LEGDEATGANIVKVAL 159
Cdd:PRK12849  367 RLAKLAGGVAVIKVGAATEVELKERKDRVEDALNATRAAVEEGIVPGGGVALLRAAKALDELAgLNGDQAAGVEIVRRAL 446

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1123885116 160 DAPVKQIAVNAGLEPGVVAEKVRNSPAGTGLNAATGVYEDLLAAGINDPVKVTRSALQNAASIAAL 225
Cdd:PRK12849  447 EAPLRQIAENAGLDGSVVVAKVLELEDGFGFNAATGEYGDLIAAGIIDPVKVTRSALQNAASVAGL 512
GroEL cd03344
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ...
 1-225 9.12e-116

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: 339.82  E-value: 9.12e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123885116   1 MLQDMAILTGGQVISEEIGLSLDTAGLEVLGQARQVVVTKDETTIVDGAGSKEQIEGRVSQIRAEIENSDSDYDREKLQE 80
Cdd:cd03344   285 MLEDIAILTGGTVISEELGLKLEDVTLEDLGRAKKVVVTKDDTTIIGGAGDKAAIKARIAQIRKQIEETTSDYDKEKLQE 364

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123885116  81 RLAKLAGGVAVIKAGAATEVELKERKHRIEDAVRNAKAAVEEGIVAGGGAALAQSGAVFESL-ALEGDEATGANIVKVAL 159
Cdd:cd03344   365 RLAKLSGGVAVIKVGGATEVELKEKKDRVEDALNATRAAVEEGIVPGGGVALLRASPALDKLkALNGDEKLGIEIVRRAL 444

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1123885116 160 DAPVKQIAVNAGLEPGVVAEKVRNSPAGTGLNAATGVYEDLLAAGINDPVKVTRSALQNAASIAAL 225
Cdd:cd03344   445 EAPLRQIAENAGVDGSVVVEKVLESPDGFGYDAATGEYVDMIEAGIIDPTKVVRSALQNAASVASL 510
GroEL TIGR02348
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ...
 1-225 7.78e-113

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: 332.72  E-value: 7.78e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123885116   1 MLQDMAILTGGQVISEEIGLSLDTAGLEVLGQARQVVVTKDETTIVDGAGSKEQIEGRVSQIRAEIENSDSDYDREKLQE 80
Cdd:TIGR02348 286 MLEDIAILTGGQVISEELGLKLEEVTLDDLGKAKKVTVDKDNTTIVEGAGDKAAIKARVAQIKAQIEETTSDYDREKLQE 365

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123885116  81 RLAKLAGGVAVIKAGAATEVELKERKHRIEDAVRNAKAAVEEGIVAGGGAALAQSGAVFESLALEG-DEATGANIVKVAL 159
Cdd:TIGR02348 366 RLAKLAGGVAVIKVGAATETEMKEKKLRIEDALNATRAAVEEGIVPGGGVALLRAAAALEGLKGDGeDEAIGIDIVKRAL 445

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1123885116 160 DAPVKQIAVNAGLEPGVVAEKVRNSPAGTGLNAATGVYEDLLAAGINDPVKVTRSALQNAASIAAL 225
Cdd:TIGR02348 446 EAPLRQIAENAGLDGAVVAEKVKELKGNFGFNAATGEYEDLVEAGIIDPTKVTRSALQNAASIAGL 511
groEL PRK12850
chaperonin GroEL; Reviewed
 1-225 2.17e-103

chaperonin GroEL; Reviewed


Pssm-ID: 237231  Cd Length: 544  Bit Score: 309.34  E-value: 2.17e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123885116   1 MLQDMAILTGGQVISEEIGLSLDTAGLEVLGQARQVVVTKDETTIVDGAGSKEQIEGRVSQIRAEIENSDSDYDREKLQE 80
Cdd:PRK12850  288 MLEDIAVLTGGQVISEDLGIKLENVTLDMLGRAKRVLITKENTTIIDGAGDKKNIEARVKQIRAQIEETTSDYDREKLQE 367

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123885116  81 RLAKLAGGVAVIKAGAATEVELKERKHRIEDAVRNAKAAVEEGIVAGGGAALAQ-SGAVFESLALEGDEATGANIVKVAL 159
Cdd:PRK12850  368 RLAKLAGGVAVIRVGGATEVEVKEKKDRVDDALHATRAAVEEGIVPGGGVALLRaRSALRGLKGANADETAGIDIVRRAL 447

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1123885116 160 DAPVKQIAVNAGLEPGVVAEKVRNSPAGTGLNAATGVYEDLLAAGINDPVKVTRSALQNAASIAAL 225
Cdd:PRK12850  448 EEPLRQIATNAGFEGSVVVGKVAELPGNFGFNAQTGEYGDMVEAGIIDPAKVTRTALQDAASIAAL 513
groEL PRK12851
chaperonin GroEL; Reviewed
 1-225 1.77e-98

chaperonin GroEL; Reviewed


Pssm-ID: 171770  Cd Length: 541  Bit Score: 296.65  E-value: 1.77e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123885116   1 MLQDMAILTGGQVISEEIGLSLDTAGLEVLGQARQVVVTKDETTIVDGAGSKEQIEGRVSQIRAEIENSDSDYDREKLQE 80
Cdd:PRK12851  288 MLEDIAILTGGTVISEDLGIKLENVTLEQLGRAKKVVVEKENTTIIDGAGSKTEIEGRVAQIRAQIEETTSDYDREKLQE 367

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123885116  81 RLAKLAGGVAVIKAGAATEVELKERKHRIEDAVRNAKAAVEEGIVAGGGAALAQ-SGAVFESLALEGDEATGANIVKVAL 159
Cdd:PRK12851  368 RLAKLAGGVAVIRVGASTEVEVKEKKDRVDDALHATRAAVEEGIVPGGGVALLRaVKALDKLETANGDQRTGVEIVRRAL 447

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1123885116 160 DAPVKQIAVNAGLEPGVVAEKVRNSPAGTGLNAATGVYEDLLAAGINDPVKVTRSALQNAASIAAL 225
Cdd:PRK12851  448 EAPVRQIAENAGAEGSVVVGKLREKPGGYGFNAATNEYGDLYAQGVIDPVKVVRTALQNAASVAGL 513
groEL CHL00093
chaperonin GroEL
 1-225 8.56e-90

chaperonin GroEL


Pssm-ID: 177025  Cd Length: 529  Bit Score: 273.90  E-value: 8.56e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123885116   1 MLQDMAILTGGQVISEEIGLSLDTAGLEVLGQARQVVVTKDETTIVdGAGSKEQIEGRVSQIRAEIENSDSDYDREKLQE 80
Cdd:CHL00093  288 MLEDIAILTGGQVITEDAGLSLETIQLDLLGQARRIIVTKDSTTII-ADGNEEQVKARCEQLRKQIEIADSSYEKEKLQE 366

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123885116  81 RLAKLAGGVAVIKAGAATEVELKERKHRIEDAVRNAKAAVEEGIVAGGGAALAQSGAVFESLA---LEGDEATGANIVKV 157
Cdd:CHL00093  367 RLAKLSGGVAVIKVGAATETEMKDKKLRLEDAINATKAAVEEGIVPGGGATLVHLSENLKTWAknnLKEDELIGALIVAR 446

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1123885116 158 ALDAPVKQIAVNAGLEPGVVAEKVRNSPAGTGLNAATGVYEDLLAAGINDPVKVTRSALQNAASIAAL 225
Cdd:CHL00093  447 AILAPLKRIAENAGKNGSVIIEKVQEQDFEIGYNAANNKFVNMYEAGIIDPAKVTRSALQNAASIASM 514
PTZ00114 PTZ00114
Heat shock protein 60; Provisional
 1-225 2.27e-84

Heat shock protein 60; Provisional


Pssm-ID: 185455  Cd Length: 555  Bit Score: 260.62  E-value: 2.27e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123885116   1 MLQDMAILTGGQVISEE-IGLSLDTAGLEVLGQARQVVVTKDETTIVDGAGSKEQIEGRVSQIRAEIENSDSDYDREKLQ 79
Cdd:PTZ00114  299 ILQDIAVLTGATVVSEDnVGLKLDDFDPSMLGSAKKVTVTKDETVILTGGGDKAEIKERVELLRSQIERTTSEYDKEKLK 378

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123885116  80 ERLAKLAGGVAVIKAGAATEVELKERKHRIEDAVRNAKAAVEEGIVAGGGAALAQSGAVFESLA----LEGDEATGANIV 155
Cdd:PTZ00114  379 ERLAKLSGGVAVIKVGGASEVEVNEKKDRIEDALNATRAAVEEGIVPGGGVALLRASKLLDKLEedneLTPDQRTGVKIV 458

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1123885116 156 KVALDAPVKQIAVNAGLEPGVVAEKV-RNSPAGTGLNAATGVYEDLLAAGINDPVKVTRSALQNAASIAAL 225
Cdd:PTZ00114  459 RNALRLPTKQIAENAGVEGAVVVEKIlEKKDPSFGYDAQTGEYVNMFEAGIIDPTKVVRSALVDAASVASL 529
groEL PRK12852
chaperonin GroEL; Reviewed
 1-225 5.04e-81

chaperonin GroEL; Reviewed


Pssm-ID: 237232  Cd Length: 545  Bit Score: 251.69  E-value: 5.04e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123885116   1 MLQDMAILTGGQVISEEIGLSLDTAGLEVLGQARQVVVTKDETTIVDGAGSKEQIEGRVSQIRAEIENSDSDYDREKLQE 80
Cdd:PRK12852  288 MLEDIAILTGGQLISEDLGIKLENVTLKMLGRAKKVVIDKENTTIVNGAGKKADIEARVGQIKAQIEETTSDYDREKLQE 367

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123885116  81 RLAKLAGGVAVIKAGAATEVELKERKHRIEDAVRNAKAAVEEGIVAGGGAALAQSGAVFESLALEGDEAT-GANIVKVAL 159
Cdd:PRK12852  368 RLAKLAGGVAVIRVGGATEVEVKEKKDRVEDALNATRAAVQEGIVPGGGVALLRAKKAVGRINNDNADVQaGINIVLKAL 447

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1123885116 160 DAPVKQIAVNAGLEPGVVAEKVRNSPAGT-GLNAATGVYEDLLAAGINDPVKVTRSALQNAASIAAL 225
Cdd:PRK12852  448 EAPIRQIAENAGVEGSIVVGKILENKSETfGFDAQTEEYVDMVAKGIIDPAKVVRTALQDAASVAGL 514
GroEL COG0459
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ...
 1-225 1.64e-79

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


Pssm-ID: 440227  Cd Length: 497  Bit Score: 246.53  E-value: 1.64e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123885116   1 MLQDMAILTGGQVISEEIGLSLDTAGLEVLGQARQVVVTKDETTIVDGAGSKEQIegrvsqiraeiensdsdydreklqe 80
Cdd:COG0459   287 MLEDIAILTGGRVISEDLGLKLEDVTLDDLGRAKRVEVDKDNTTIVEGAGNPKAI------------------------- 341

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123885116  81 rlaklaggvaVIKAGAATEVELKERKHRIEDAVRNAKAAVEEGIVAGGGAALAQSGAVFESLA--LEGDEATGANIVKVA 158
Cdd:COG0459   342 ----------VILVGAATEVEVKERKRRVEDALHATRAAVEEGIVPGGGAALLRAARALRELAakLEGDEQLGIEIVARA 411

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1123885116 159 LDAPVKQIAVNAGLEPGVVAEKVRNSP-AGTGLNAATGVYEDLLAAGINDPVKVTRSALQNAASIAAL 225
Cdd:COG0459   412 LEAPLRQIAENAGLDGSVVVEKVRAAKdKGFGFDAATGEYVDMLEAGVIDPAKVKRSALQNAASVAGL 479
PRK14104 PRK14104
chaperonin GroEL; Provisional
 1-225 2.20e-68

chaperonin GroEL; Provisional


Pssm-ID: 172594  Cd Length: 546  Bit Score: 219.13  E-value: 2.20e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123885116   1 MLQDMAILTGGQVISEEIGLSLDTAGLEVLGQARQVVVTKDETTIVDGAGSKEQIEGRVSQIRAEIENSDSDYDREKLQE 80
Cdd:PRK14104  288 MLQDIAILTGGQAISEDLGIKLENVTLQMLGRAKKVMIDKENTTIVNGAGKKADIEARVAQIKAQIEETTSDYDREKLQE 367

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123885116  81 RLAKLAGGVAVIKAGAATEVELKERKHRIEDAVRNAKAAVEEGIVAGGGAALAQSGAVFESLALEG-DEATGANIVKVAL 159
Cdd:PRK14104  368 RLAKLAGGVAVIRVGGATEVEVKERKDRVDDAMHATRAAVEEGIVPGGGVALLRASEQLKGIKTKNdDQKTGVEIVRKAL 447

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1123885116 160 DAPVKQIAVNAGLEPGVVAEKV-RNSPAGTGLNAATGVYEDLLAAGINDPVKVTRSALQNAASIAAL 225
Cdd:PRK14104  448 SAPARQIAINAGEDGSVIVGKIlEKEQYSYGFDSQTGEYGNLVSKGIIDPTKVVRTAIQNAASVAAL 514
PLN03167 PLN03167
Chaperonin-60 beta subunit; Provisional
 2-223 2.98e-68

Chaperonin-60 beta subunit; Provisional


Pssm-ID: 215611 [Multi-domain]  Cd Length: 600  Bit Score: 219.80  E-value: 2.98e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123885116   2 LQDMAILTGGQVISEEIGLSLDTAGLEVLGQARQVVVTKDETTIVDGAGSKEQIEGRVSQIRAEIENSDSDYDREKLQER 81
Cdd:PLN03167  343 LDDIAILTGGTVIREEVGLSLDKVGKEVLGTAAKVVLTKDTTTIVGDGSTQEAVNKRVAQIKNLIEAAEQDYEKEKLNER 422

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123885116  82 LAKLAGGVAVIKAGAATEVELKERKHRIEDAVRNAKAAVEEGIVAGGGAALAQSGAVFESL--ALEGDE-ATGANIVKVA 158
Cdd:PLN03167  423 IAKLSGGVAVIQVGAQTETELKEKKLRVEDALNATKAAVEEGIVVGGGCTLLRLASKVDAIkdTLENDEqKVGADIVKRA 502

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1123885116 159 LDAPVKQIAVNAGLEPGVVAEKV-RNSPAGTGLNAATGVYEDLLAAGINDPVKVTRSALQNAASIA 223
Cdd:PLN03167  503 LSYPLKLIAKNAGVNGSVVSEKVlSNDNPKFGYNAATGKYEDLMAAGIIDPTKVVRCCLEHAASVA 568
chaperonin_type_I_II cd00309
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ...
 1-225 1.57e-46

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: 159.90  E-value: 1.57e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123885116   1 MLQDMAILTGGQVISeeiglSLDTAGLEVLGQARQVVVTK----DETTIVDGAGskeqiegrvsqiraeiensdsdydre 76
Cdd:cd00309   261 DLERIAKATGATIVS-----RLEDLTPEDLGTAGLVEETKigdeKYTFIEGCKG-------------------------- 309

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123885116  77 klqerlaklaGGVAVIKAGAATEVELKERKHRIEDAVRNAKAAVEE-GIVAGGGAALAQSGAVFESLA--LEGDEATGAN 153
Cdd:cd00309   310 ----------GKVATILLRGATEVELDEAERSLHDALCAVRAAVEDgGIVPGGGAAEIELSKALEELAktLPGKEQLGIE 379

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1123885116 154 IVKVALDAPVKQIAVNAGLEPGVVAEKVRNSPAGTGLNAA----TGVYEDLLAAGINDPVKVTRSALQNAASIAAL 225
Cdd:cd00309   380 AFADALEVIPRTLAENAGLDPIEVVTKLRAKHAEGGGNAGgdveTGEIVDMKEAGIIDPLKVKRQALKSATEAASL 455
Cpn60_TCP1 pfam00118
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ...
 1-225 1.18e-24

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: 100.74  E-value: 1.18e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123885116   1 MLQDMAILTGGQVISeeiglSLDTAGLEVLGQA---RQVVVTKDETTIVDGAGSkeqiegrvsqiraeiensdsdydrek 77
Cdd:pfam00118 284 DLERLAKATGARAVS-----SLDDLTPDDLGTAgkvEEEKIGDEKYTFIEGCKS-------------------------- 332

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123885116  78 lqerlaklaGGVAVIKAGAATEVELKERKHRIEDAVRNAKAAVEEG-IVAGGGAALAQSGAVFESLA--LEGDEATGANI 154
Cdd:pfam00118 333 ---------PKAATILLRGATDHVLDEIERSIHDALCVVKNAIEDPrVVPGGGAVEMELARALREYAksVSGKEQLAIEA 403

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1123885116 155 VKVALDAPVKQIAVNAGLEPGVVAEKVRNSPAG----TGLNAATGVYEDLLAAGINDPVKVTRSALQNAASIAAL 225
Cdd:pfam00118 404 FAEALEVIPKTLAENAGLDPIEVLAELRAAHASgekhAGIDVETGEIIDMKEAGVVDPLKVKRQALKSATEAAST 478
chaperonin_like cd03333
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ...
 1-122 1.23e-13

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: 67.11  E-value: 1.23e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123885116   1 MLQDMAILTGGQVISeeiglSLDTAGLEVLGQARQVVVTKD----ETTIVDGAGskeqiegrvsqiraeiensdsdydre 76
Cdd:cd03333   125 DLERIARATGATIVS-----SLEDLTPEDLGTAELVEETKIgeekLTFIEGCKG-------------------------- 173

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1123885116  77 klqerlaklaGGVAVIKAGAATEVELKERKHRIEDAVRNAKAAVEE 122
Cdd:cd03333   174 ----------GKAATILLRGATEVELDEVKRSLHDALCAVRAAVEE 209
cpn60 cd03343
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ...
 109-225 1.86e-08

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: 53.81  E-value: 1.86e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123885116 109 IEDAVRNAKAAVEEG-IVAGGGAALAQSGAVFESLA--LEGDEATGANIVKVALDAPVKQIAVNAGLEPGVVAEKVRNSP 185
Cdd:cd03343   383 LEDALRVVADALEDGkVVAGGGAVEIELAKRLREYArsVGGREQLAVEAFADALEEIPRTLAENAGLDPIDTLVELRAAH 462

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1123885116 186 AGT----GLNAATGVYEDLLAAGINDPVKVTRSALQNAASIAAL 225
Cdd:cd03343   463 EKGnknaGLDVYTGEVVDMLEKGVIEPLRVKKQAIKSATEAATM 506
TCP1_zeta cd03342
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ...
 108-223 1.21e-03

TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.


Pssm-ID: 239458 [Multi-domain]  Cd Length: 484  Bit Score: 39.16  E-value: 1.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123885116 108 RIEDAVRNA----KAAVEEG-IVAGGGA---ALAQSgAVFESLALEGDEATGANIVKVALDAPVKQIAVNAGLEPG---- 175
Cdd:cd03342   344 QIKDAIRDGlravKNAIEDKcVVPGAGAfevALYAH-LKEFKKSVKGKAKLGVQAFADALLVIPKTLAENSGLDVQetlv 422

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1123885116 176 VVAEKVRNSPAGTGLNAATGVYEDLLAAGINDPVKVTRSALQNAASIA 223
Cdd:cd03342   423 KLQDEYAEGGQVGGVDLDTGEPMDPESEGIWDNYSVKRQILHSATVIA 470
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH