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Conserved domains on  [gi|1177256150|gb|ARH02170|]
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chaperonin GroEL, partial [Leuconostoc mesenteroides]

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 ...
 1-223 9.97e-137

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: 394.11  E-value: 9.97e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177256150   1 QLEDIAILTGGTVITEDLGLNLKDVTIDQLGQASKINITKDNTTIVEGSGDKGAVSSRVDTIKQQIAETTSDFDREKLQE 80
Cdd:PRK00013  287 MLEDIAILTGGTVISEELGLKLEDATLEDLGQAKKVVVTKDNTTIVDGAGDKEAIKARVAQIKAQIEETTSDYDREKLQE 366

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177256150  81 RLAKLAGGVAVINVGAATETELKERKYRIEDALNATRAAVEEGFVAGGGTALVNVIAAVSALS-EEGDVQTGINTVIKAL 159
Cdd:PRK00013  367 RLAKLAGGVAVIKVGAATEVEMKEKKDRVEDALHATRAAVEEGIVPGGGVALLRAAPALEALKgLNGDEATGINIVLRAL 446

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1177256150 160 ESPVRQIAENAGLEGSVIVNKLKEQK-EGFGYNAATDEWVDMIAAGIVDPTKVTRSALQNAASVS 223
Cdd:PRK00013  447 EAPLRQIAENAGLEGSVVVEKVKNGKgKGYGYNAATGEYVDMIEAGIIDPTKVTRSALQNAASVA 511
 
Name Accession Description Interval E-value
groEL PRK00013
chaperonin GroEL; Reviewed
 1-223 9.97e-137

chaperonin GroEL; Reviewed


Pssm-ID: 234573  Cd Length: 542  Bit Score: 394.11  E-value: 9.97e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177256150   1 QLEDIAILTGGTVITEDLGLNLKDVTIDQLGQASKINITKDNTTIVEGSGDKGAVSSRVDTIKQQIAETTSDFDREKLQE 80
Cdd:PRK00013  287 MLEDIAILTGGTVISEELGLKLEDATLEDLGQAKKVVVTKDNTTIVDGAGDKEAIKARVAQIKAQIEETTSDYDREKLQE 366

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177256150  81 RLAKLAGGVAVINVGAATETELKERKYRIEDALNATRAAVEEGFVAGGGTALVNVIAAVSALS-EEGDVQTGINTVIKAL 159
Cdd:PRK00013  367 RLAKLAGGVAVIKVGAATEVEMKEKKDRVEDALHATRAAVEEGIVPGGGVALLRAAPALEALKgLNGDEATGINIVLRAL 446

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1177256150 160 ESPVRQIAENAGLEGSVIVNKLKEQK-EGFGYNAATDEWVDMIAAGIVDPTKVTRSALQNAASVS 223
Cdd:PRK00013  447 EAPLRQIAENAGLEGSVVVEKVKNGKgKGYGYNAATGEYVDMIEAGIIDPTKVTRSALQNAASVA 511
GroEL cd03344
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ...
 1-223 2.43e-121

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: 354.07  E-value: 2.43e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177256150   1 QLEDIAILTGGTVITEDLGLNLKDVTIDQLGQASKINITKDNTTIVEGSGDKGAVSSRVDTIKQQIAETTSDFDREKLQE 80
Cdd:cd03344   285 MLEDIAILTGGTVISEELGLKLEDVTLEDLGRAKKVVVTKDDTTIIGGAGDKAAIKARIAQIRKQIEETTSDYDKEKLQE 364

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177256150  81 RLAKLAGGVAVINVGAATETELKERKYRIEDALNATRAAVEEGFVAGGGTALVNVIAAVSAL-SEEGDVQTGINTVIKAL 159
Cdd:cd03344   365 RLAKLSGGVAVIKVGGATEVELKEKKDRVEDALNATRAAVEEGIVPGGGVALLRASPALDKLkALNGDEKLGIEIVRRAL 444

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1177256150 160 ESPVRQIAENAGLEGSVIVNKLKEQKEGFGYNAATDEWVDMIAAGIVDPTKVTRSALQNAASVS 223
Cdd:cd03344   445 EAPLRQIAENAGVDGSVVVEKVLESPDGFGYDAATGEYVDMIEAGIIDPTKVVRSALQNAASVA 508
GroEL TIGR02348
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ...
 2-222 1.56e-117

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: 344.66  E-value: 1.56e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177256150   2 LEDIAILTGGTVITEDLGLNLKDVTIDQLGQASKINITKDNTTIVEGSGDKGAVSSRVDTIKQQIAETTSDFDREKLQER 81
Cdd:TIGR02348 287 LEDIAILTGGQVISEELGLKLEEVTLDDLGKAKKVTVDKDNTTIVEGAGDKAAIKARVAQIKAQIEETTSDYDREKLQER 366

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177256150  82 LAKLAGGVAVINVGAATETELKERKYRIEDALNATRAAVEEGFVAGGGTALVNVIAAVSALSEEG-DVQTGINTVIKALE 160
Cdd:TIGR02348 367 LAKLAGGVAVIKVGAATETEMKEKKLRIEDALNATRAAVEEGIVPGGGVALLRAAAALEGLKGDGeDEAIGIDIVKRALE 446

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1177256150 161 SPVRQIAENAGLEGSVIVNKLKEQKEGFGYNAATDEWVDMIAAGIVDPTKVTRSALQNAASV 222
Cdd:TIGR02348 447 APLRQIAENAGLDGAVVAEKVKELKGNFGFNAATGEYEDLVEAGIIDPTKVTRSALQNAASI 508
GroEL COG0459
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ...
 2-223 7.82e-91

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


Pssm-ID: 440227  Cd Length: 497  Bit Score: 275.42  E-value: 7.82e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177256150   2 LEDIAILTGGTVITEDLGLNLKDVTIDQLGQASKINITKDNTTIVEGSGDKGAVssrvdtikqqiaettsdfdreklqer 81
Cdd:COG0459   288 LEDIAILTGGRVISEDLGLKLEDVTLDDLGRAKRVEVDKDNTTIVEGAGNPKAI-------------------------- 341

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177256150  82 laklaggvaVINVGAATETELKERKYRIEDALNATRAAVEEGFVAGGGTALVNVIAAVSALSE--EGDVQTGINTVIKAL 159
Cdd:COG0459   342 ---------VILVGAATEVEVKERKRRVEDALHATRAAVEEGIVPGGGAALLRAARALRELAAklEGDEQLGIEIVARAL 412

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1177256150 160 ESPVRQIAENAGLEGSVIVNKLKEQKE-GFGYNAATDEWVDMIAAGIVDPTKVTRSALQNAASVS 223
Cdd:COG0459   413 EAPLRQIAENAGLDGSVVVEKVRAAKDkGFGFDAATGEYVDMLEAGVIDPAKVKRSALQNAASVA 477
Cpn60_TCP1 pfam00118
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ...
 2-222 3.53e-32

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: 121.54  E-value: 3.53e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177256150   2 LEDIAILTGGTVITedlglNLKDVTIDQLGQASKI---NITKDNTTIVEGSGDKGAVSsrvdtikqqiaettsdfdrekl 78
Cdd:pfam00118 285 LERLAKATGARAVS-----SLDDLTPDDLGTAGKVeeeKIGDEKYTFIEGCKSPKAAT---------------------- 337

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177256150  79 qerlaklaggvavINVGAATETELKERKYRIEDALNATRAAVEEG-FVAGGGTALVNVIAAVSALSE--EGDVQTGINTV 155
Cdd:pfam00118 338 -------------ILLRGATDHVLDEIERSIHDALCVVKNAIEDPrVVPGGGAVEMELARALREYAKsvSGKEQLAIEAF 404

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1177256150 156 IKALESPVRQIAENAGLEGSVIVNKLK----EQKEGFGYNAATDEWVDMIAAGIVDPTKVTRSALQNAASV 222
Cdd:pfam00118 405 AEALEVIPKTLAENAGLDPIEVLAELRaahaSGEKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKSATEA 475
 
Name Accession Description Interval E-value
groEL PRK00013
chaperonin GroEL; Reviewed
 1-223 9.97e-137

chaperonin GroEL; Reviewed


Pssm-ID: 234573  Cd Length: 542  Bit Score: 394.11  E-value: 9.97e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177256150   1 QLEDIAILTGGTVITEDLGLNLKDVTIDQLGQASKINITKDNTTIVEGSGDKGAVSSRVDTIKQQIAETTSDFDREKLQE 80
Cdd:PRK00013  287 MLEDIAILTGGTVISEELGLKLEDATLEDLGQAKKVVVTKDNTTIVDGAGDKEAIKARVAQIKAQIEETTSDYDREKLQE 366

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177256150  81 RLAKLAGGVAVINVGAATETELKERKYRIEDALNATRAAVEEGFVAGGGTALVNVIAAVSALS-EEGDVQTGINTVIKAL 159
Cdd:PRK00013  367 RLAKLAGGVAVIKVGAATEVEMKEKKDRVEDALHATRAAVEEGIVPGGGVALLRAAPALEALKgLNGDEATGINIVLRAL 446

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1177256150 160 ESPVRQIAENAGLEGSVIVNKLKEQK-EGFGYNAATDEWVDMIAAGIVDPTKVTRSALQNAASVS 223
Cdd:PRK00013  447 EAPLRQIAENAGLEGSVVVEKVKNGKgKGYGYNAATGEYVDMIEAGIIDPTKVTRSALQNAASVA 511
GroEL cd03344
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ...
 1-223 2.43e-121

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: 354.07  E-value: 2.43e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177256150   1 QLEDIAILTGGTVITEDLGLNLKDVTIDQLGQASKINITKDNTTIVEGSGDKGAVSSRVDTIKQQIAETTSDFDREKLQE 80
Cdd:cd03344   285 MLEDIAILTGGTVISEELGLKLEDVTLEDLGRAKKVVVTKDDTTIIGGAGDKAAIKARIAQIRKQIEETTSDYDKEKLQE 364

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177256150  81 RLAKLAGGVAVINVGAATETELKERKYRIEDALNATRAAVEEGFVAGGGTALVNVIAAVSAL-SEEGDVQTGINTVIKAL 159
Cdd:cd03344   365 RLAKLSGGVAVIKVGGATEVELKEKKDRVEDALNATRAAVEEGIVPGGGVALLRASPALDKLkALNGDEKLGIEIVRRAL 444

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1177256150 160 ESPVRQIAENAGLEGSVIVNKLKEQKEGFGYNAATDEWVDMIAAGIVDPTKVTRSALQNAASVS 223
Cdd:cd03344   445 EAPLRQIAENAGVDGSVVVEKVLESPDGFGYDAATGEYVDMIEAGIIDPTKVVRSALQNAASVA 508
groEL PRK12849
chaperonin GroEL; Reviewed
 2-223 1.53e-118

chaperonin GroEL; Reviewed


Pssm-ID: 237230  Cd Length: 542  Bit Score: 347.56  E-value: 1.53e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177256150   2 LEDIAILTGGTVITEDLGLNLKDVTIDQLGQASKINITKDNTTIVEGSGDKGAVSSRVDTIKQQIAETTSDFDREKLQER 81
Cdd:PRK12849  288 LEDIAILTGGTVISEDLGLKLEEVTLDDLGRAKRVTITKDNTTIVDGAGDKEAIEARVAQIRRQIEETTSDYDREKLQER 367

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177256150  82 LAKLAGGVAVINVGAATETELKERKYRIEDALNATRAAVEEGFVAGGGTALVNVIAAVSAL-SEEGDVQTGINTVIKALE 160
Cdd:PRK12849  368 LAKLAGGVAVIKVGAATEVELKERKDRVEDALNATRAAVEEGIVPGGGVALLRAAKALDELaGLNGDQAAGVEIVRRALE 447

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1177256150 161 SPVRQIAENAGLEGSVIVNKLKEQKEGFGYNAATDEWVDMIAAGIVDPTKVTRSALQNAASVS 223
Cdd:PRK12849  448 APLRQIAENAGLDGSVVVAKVLELEDGFGFNAATGEYGDLIAAGIIDPVKVTRSALQNAASVA 510
GroEL TIGR02348
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ...
 2-222 1.56e-117

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: 344.66  E-value: 1.56e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177256150   2 LEDIAILTGGTVITEDLGLNLKDVTIDQLGQASKINITKDNTTIVEGSGDKGAVSSRVDTIKQQIAETTSDFDREKLQER 81
Cdd:TIGR02348 287 LEDIAILTGGQVISEELGLKLEEVTLDDLGKAKKVTVDKDNTTIVEGAGDKAAIKARVAQIKAQIEETTSDYDREKLQER 366

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177256150  82 LAKLAGGVAVINVGAATETELKERKYRIEDALNATRAAVEEGFVAGGGTALVNVIAAVSALSEEG-DVQTGINTVIKALE 160
Cdd:TIGR02348 367 LAKLAGGVAVIKVGAATETEMKEKKLRIEDALNATRAAVEEGIVPGGGVALLRAAAALEGLKGDGeDEAIGIDIVKRALE 446

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1177256150 161 SPVRQIAENAGLEGSVIVNKLKEQKEGFGYNAATDEWVDMIAAGIVDPTKVTRSALQNAASV 222
Cdd:TIGR02348 447 APLRQIAENAGLDGAVVAEKVKELKGNFGFNAATGEYEDLVEAGIIDPTKVTRSALQNAASI 508
groEL PRK12850
chaperonin GroEL; Reviewed
 2-223 3.57e-106

chaperonin GroEL; Reviewed


Pssm-ID: 237231  Cd Length: 544  Bit Score: 316.27  E-value: 3.57e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177256150   2 LEDIAILTGGTVITEDLGLNLKDVTIDQLGQASKINITKDNTTIVEGSGDKGAVSSRVDTIKQQIAETTSDFDREKLQER 81
Cdd:PRK12850  289 LEDIAVLTGGQVISEDLGIKLENVTLDMLGRAKRVLITKENTTIIDGAGDKKNIEARVKQIRAQIEETTSDYDREKLQER 368

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177256150  82 LAKLAGGVAVINVGAATETELKERKYRIEDALNATRAAVEEGFVAGGGTALVNVIAAVSALSEE-GDVQTGINTVIKALE 160
Cdd:PRK12850  369 LAKLAGGVAVIRVGGATEVEVKEKKDRVDDALHATRAAVEEGIVPGGGVALLRARSALRGLKGAnADETAGIDIVRRALE 448

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1177256150 161 SPVRQIAENAGLEGSVIVNKLKEQKEGFGYNAATDEWVDMIAAGIVDPTKVTRSALQNAASVS 223
Cdd:PRK12850  449 EPLRQIATNAGFEGSVVVGKVAELPGNFGFNAQTGEYGDMVEAGIIDPAKVTRTALQDAASIA 511
groEL PRK12851
chaperonin GroEL; Reviewed
 2-223 3.13e-100

chaperonin GroEL; Reviewed


Pssm-ID: 171770  Cd Length: 541  Bit Score: 300.89  E-value: 3.13e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177256150   2 LEDIAILTGGTVITEDLGLNLKDVTIDQLGQASKINITKDNTTIVEGSGDKGAVSSRVDTIKQQIAETTSDFDREKLQER 81
Cdd:PRK12851  289 LEDIAILTGGTVISEDLGIKLENVTLEQLGRAKKVVVEKENTTIIDGAGSKTEIEGRVAQIRAQIEETTSDYDREKLQER 368

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177256150  82 LAKLAGGVAVINVGAATETELKERKYRIEDALNATRAAVEEGFVAGGGTALVNVIAAVSAL-SEEGDVQTGINTVIKALE 160
Cdd:PRK12851  369 LAKLAGGVAVIRVGASTEVEVKEKKDRVDDALHATRAAVEEGIVPGGGVALLRAVKALDKLeTANGDQRTGVEIVRRALE 448

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1177256150 161 SPVRQIAENAGLEGSVIVNKLKEQKEGFGYNAATDEWVDMIAAGIVDPTKVTRSALQNAASVS 223
Cdd:PRK12851  449 APVRQIAENAGAEGSVVVGKLREKPGGYGFNAATNEYGDLYAQGVIDPVKVVRTALQNAASVA 511
groEL PRK12852
chaperonin GroEL; Reviewed
 2-223 2.47e-98

chaperonin GroEL; Reviewed


Pssm-ID: 237232  Cd Length: 545  Bit Score: 295.99  E-value: 2.47e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177256150   2 LEDIAILTGGTVITEDLGLNLKDVTIDQLGQASKINITKDNTTIVEGSGDKGAVSSRVDTIKQQIAETTSDFDREKLQER 81
Cdd:PRK12852  289 LEDIAILTGGQLISEDLGIKLENVTLKMLGRAKKVVIDKENTTIVNGAGKKADIEARVGQIKAQIEETTSDYDREKLQER 368

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177256150  82 LAKLAGGVAVINVGAATETELKERKYRIEDALNATRAAVEEGFVAGGGTALVNVIAAVSALS-EEGDVQTGINTVIKALE 160
Cdd:PRK12852  369 LAKLAGGVAVIRVGGATEVEVKEKKDRVEDALNATRAAVQEGIVPGGGVALLRAKKAVGRINnDNADVQAGINIVLKALE 448

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1177256150 161 SPVRQIAENAGLEGSVIVNKLKEQK-EGFGYNAATDEWVDMIAAGIVDPTKVTRSALQNAASVS 223
Cdd:PRK12852  449 APIRQIAENAGVEGSIVVGKILENKsETFGFDAQTEEYVDMVAKGIIDPAKVVRTALQDAASVA 512
groEL CHL00093
chaperonin GroEL
 2-223 9.94e-92

chaperonin GroEL


Pssm-ID: 177025  Cd Length: 529  Bit Score: 278.53  E-value: 9.94e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177256150   2 LEDIAILTGGTVITEDLGLNLKDVTIDQLGQASKINITKDNTTIVeGSGDKGAVSSRVDTIKQQIAETTSDFDREKLQER 81
Cdd:CHL00093  289 LEDIAILTGGQVITEDAGLSLETIQLDLLGQARRIIVTKDSTTII-ADGNEEQVKARCEQLRKQIEIADSSYEKEKLQER 367

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177256150  82 LAKLAGGVAVINVGAATETELKERKYRIEDALNATRAAVEEGFVAGGGTALVNVIAAVSALSEE---GDVQTGINTVIKA 158
Cdd:CHL00093  368 LAKLSGGVAVIKVGAATETEMKDKKLRLEDAINATKAAVEEGIVPGGGATLVHLSENLKTWAKNnlkEDELIGALIVARA 447

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1177256150 159 LESPVRQIAENAGLEGSVIVNKLKEQKEGFGYNAATDEWVDMIAAGIVDPTKVTRSALQNAASVS 223
Cdd:CHL00093  448 ILAPLKRIAENAGKNGSVIIEKVQEQDFEIGYNAANNKFVNMYEAGIIDPAKVTRSALQNAASIA 512
GroEL COG0459
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ...
 2-223 7.82e-91

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


Pssm-ID: 440227  Cd Length: 497  Bit Score: 275.42  E-value: 7.82e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177256150   2 LEDIAILTGGTVITEDLGLNLKDVTIDQLGQASKINITKDNTTIVEGSGDKGAVssrvdtikqqiaettsdfdreklqer 81
Cdd:COG0459   288 LEDIAILTGGRVISEDLGLKLEDVTLDDLGRAKRVEVDKDNTTIVEGAGNPKAI-------------------------- 341

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177256150  82 laklaggvaVINVGAATETELKERKYRIEDALNATRAAVEEGFVAGGGTALVNVIAAVSALSE--EGDVQTGINTVIKAL 159
Cdd:COG0459   342 ---------VILVGAATEVEVKERKRRVEDALHATRAAVEEGIVPGGGAALLRAARALRELAAklEGDEQLGIEIVARAL 412

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1177256150 160 ESPVRQIAENAGLEGSVIVNKLKEQKE-GFGYNAATDEWVDMIAAGIVDPTKVTRSALQNAASVS 223
Cdd:COG0459   413 EAPLRQIAENAGLDGSVVVEKVRAAKDkGFGFDAATGEYVDMLEAGVIDPAKVKRSALQNAASVA 477
PTZ00114 PTZ00114
Heat shock protein 60; Provisional
 1-223 7.97e-90

Heat shock protein 60; Provisional


Pssm-ID: 185455  Cd Length: 555  Bit Score: 274.48  E-value: 7.97e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177256150   1 QLEDIAILTGGTVITED-LGLNLKDVTIDQLGQASKINITKDNTTIVEGSGDKGAVSSRVDTIKQQIAETTSDFDREKLQ 79
Cdd:PTZ00114  299 ILQDIAVLTGATVVSEDnVGLKLDDFDPSMLGSAKKVTVTKDETVILTGGGDKAEIKERVELLRSQIERTTSEYDKEKLK 378

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177256150  80 ERLAKLAGGVAVINVGAATETELKERKYRIEDALNATRAAVEEGFVAGGGTALVNVIAAVSALSE----EGDVQTGINTV 155
Cdd:PTZ00114  379 ERLAKLSGGVAVIKVGGASEVEVNEKKDRIEDALNATRAAVEEGIVPGGGVALLRASKLLDKLEEdnelTPDQRTGVKIV 458

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1177256150 156 IKALESPVRQIAENAGLEGSVIVNKLKEQKE-GFGYNAATDEWVDMIAAGIVDPTKVTRSALQNAASVS 223
Cdd:PTZ00114  459 RNALRLPTKQIAENAGVEGAVVVEKILEKKDpSFGYDAQTGEYVNMFEAGIIDPTKVVRSALVDAASVA 527
PRK14104 PRK14104
chaperonin GroEL; Provisional
 2-223 7.78e-76

chaperonin GroEL; Provisional


Pssm-ID: 172594  Cd Length: 546  Bit Score: 238.39  E-value: 7.78e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177256150   2 LEDIAILTGGTVITEDLGLNLKDVTIDQLGQASKINITKDNTTIVEGSGDKGAVSSRVDTIKQQIAETTSDFDREKLQER 81
Cdd:PRK14104  289 LQDIAILTGGQAISEDLGIKLENVTLQMLGRAKKVMIDKENTTIVNGAGKKADIEARVAQIKAQIEETTSDYDREKLQER 368

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177256150  82 LAKLAGGVAVINVGAATETELKERKYRIEDALNATRAAVEEGFVAGGGTALVNVIAAVSALSEEGDVQ-TGINTVIKALE 160
Cdd:PRK14104  369 LAKLAGGVAVIRVGGATEVEVKERKDRVDDAMHATRAAVEEGIVPGGGVALLRASEQLKGIKTKNDDQkTGVEIVRKALS 448

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1177256150 161 SPVRQIAENAGLEGSVIVNKLKEQKE-GFGYNAATDEWVDMIAAGIVDPTKVTRSALQNAASVS 223
Cdd:PRK14104  449 APARQIAINAGEDGSVIVGKILEKEQySYGFDSQTGEYGNLVSKGIIDPTKVVRTAIQNAASVA 512
PLN03167 PLN03167
Chaperonin-60 beta subunit; Provisional
 2-223 8.22e-68

Chaperonin-60 beta subunit; Provisional


Pssm-ID: 215611 [Multi-domain]  Cd Length: 600  Bit Score: 218.64  E-value: 8.22e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177256150   2 LEDIAILTGGTVITEDLGLNLKDVTIDQLGQASKINITKDNTTIVEGSGDKGAVSSRVDTIKQQIAETTSDFDREKLQER 81
Cdd:PLN03167  343 LDDIAILTGGTVIREEVGLSLDKVGKEVLGTAAKVVLTKDTTTIVGDGSTQEAVNKRVAQIKNLIEAAEQDYEKEKLNER 422

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177256150  82 LAKLAGGVAVINVGAATETELKERKYRIEDALNATRAAVEEGFVAGGGTALVNVIAAVSALSE--EGDVQ-TGINTVIKA 158
Cdd:PLN03167  423 IAKLSGGVAVIQVGAQTETELKEKKLRVEDALNATKAAVEEGIVVGGGCTLLRLASKVDAIKDtlENDEQkVGADIVKRA 502

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1177256150 159 LESPVRQIAENAGLEGSVIVNK-LKEQKEGFGYNAATDEWVDMIAAGIVDPTKVTRSALQNAASVS 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 ...
 2-223 1.53e-54

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: 180.70  E-value: 1.53e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177256150   2 LEDIAILTGGTVITEdlglnLKDVTIDQLGQASKINITK----DNTTIVEGSGdkgavssrvdtikqqiaettsdfdrek 77
Cdd:cd00309   262 LERIAKATGATIVSR-----LEDLTPEDLGTAGLVEETKigdeKYTFIEGCKG--------------------------- 309

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177256150  78 lqerlaklaGGVAVINVGAATETELKERKYRIEDALNATRAAVEE-GFVAGGGTALVNVIAAVS--ALSEEGDVQTGINT 154
Cdd:cd00309   310 ---------GKVATILLRGATEVELDEAERSLHDALCAVRAAVEDgGIVPGGGAAEIELSKALEelAKTLPGKEQLGIEA 380

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1177256150 155 VIKALESPVRQIAENAGLEGSVIVNKLKEQKEGFGYNAA----TDEWVDMIAAGIVDPTKVTRSALQNAASVS 223
Cdd:cd00309   381 FADALEVIPRTLAENAGLDPIEVVTKLRAKHAEGGGNAGgdveTGEIVDMKEAGIIDPLKVKRQALKSATEAA 453
Cpn60_TCP1 pfam00118
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ...
 2-222 3.53e-32

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: 121.54  E-value: 3.53e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177256150   2 LEDIAILTGGTVITedlglNLKDVTIDQLGQASKI---NITKDNTTIVEGSGDKGAVSsrvdtikqqiaettsdfdrekl 78
Cdd:pfam00118 285 LERLAKATGARAVS-----SLDDLTPDDLGTAGKVeeeKIGDEKYTFIEGCKSPKAAT---------------------- 337

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177256150  79 qerlaklaggvavINVGAATETELKERKYRIEDALNATRAAVEEG-FVAGGGTALVNVIAAVSALSE--EGDVQTGINTV 155
Cdd:pfam00118 338 -------------ILLRGATDHVLDEIERSIHDALCVVKNAIEDPrVVPGGGAVEMELARALREYAKsvSGKEQLAIEAF 404

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1177256150 156 IKALESPVRQIAENAGLEGSVIVNKLK----EQKEGFGYNAATDEWVDMIAAGIVDPTKVTRSALQNAASV 222
Cdd:pfam00118 405 AEALEVIPKTLAENAGLDPIEVLAELRaahaSGEKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKSATEA 475
chaperonin_like cd03333
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ...
 2-122 3.48e-15

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: 71.34  E-value: 3.48e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177256150   2 LEDIAILTGGTVITEdlglnLKDVTIDQLGQASKINITKD----NTTIVEGSGdkgavssrvdtikqqiaettsdfdrek 77
Cdd:cd03333   126 LERIARATGATIVSS-----LEDLTPEDLGTAELVEETKIgeekLTFIEGCKG--------------------------- 173

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1177256150  78 lqerlaklaGGVAVINVGAATETELKERKYRIEDALNATRAAVEE 122
Cdd:cd03333   174 ---------GKAATILLRGATEVELDEVKRSLHDALCAVRAAVEE 209
cpn60 cd03343
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ...
 2-219 1.52e-11

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: 63.05  E-value: 1.52e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177256150   2 LEDIAILTGGTVITedlglNLKDVTIDQLGQA---SKINITKDNTTIVEGSGDKGAVSsrvdtikqqiaettsdfdrekl 78
Cdd:cd03343   313 MEKLARATGAKIVT-----NIDDLTPEDLGEAelvEERKVGDDKMVFVEGCKNPKAVT---------------------- 365

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177256150  79 qerlaklaggvavINVGAATETELKERKYRIEDALNATRAAVEEG-FVAGGGTALVNVIAAVS--ALSEEGDVQTGINTV 155
Cdd:cd03343   366 -------------ILLRGGTEHVVDELERALEDALRVVADALEDGkVVAGGGAVEIELAKRLReyARSVGGREQLAVEAF 432

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1177256150 156 IKALESPVRQIAENAGLEGSVIVNKLK----EQKEGFGYNAATDEWVDMIAAGIVDPTKVTRSALQNA 219
Cdd:cd03343   433 ADALEEIPRTLAENAGLDPIDTLVELRaaheKGNKNAGLDVYTGEVVDMLEKGVIEPLRVKKQAIKSA 500
chap_CCT_eta TIGR02345
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ...
 53-221 2.77e-08

T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT eta chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.


Pssm-ID: 274086 [Multi-domain]  Cd Length: 523  Bit Score: 53.22  E-value: 2.77e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177256150  53 GAVSSRVDTIKQQIAETTSDFDREKL-QERLAKLAGG----VAVINVGAATETELKERKYRIEDALNATRAAVEEGFVAG 127
Cdd:TIGR02345 326 GSIQSTTSDLEADVLGTCALFEERQIgSERYNYFTGCphakTCTIILRGGAEQFIEEAERSLHDAIMIVRRALKNKKIVA 405

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177256150 128 GGTALVNVIAAV---SALSEEGDVQTGINTVIKALESPVRQIAENAGLEGSVIVNKLK----EQKEGFGYNAATDEWVDM 200
Cdd:TIGR02345 406 GGGAIEMELSKClrdYSKTIDGKQQLIINAFAKALEIIPRQLCENAGFDSIEILNKLRsrhaKGGKWYGVDINTEDIGDN 485

                         170       180
                  ....*....|....*....|.
gi 1177256150 201 IAAGIVDPTKVTRSALQNAAS 221
Cdd:TIGR02345 486 FEAFVWEPALVKINALKAAFE 506
TCP1_eta cd03340
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ...
 109-221 4.38e-08

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: 52.67  E-value: 4.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177256150 109 IEDALNATRAAVEEGFVAGGGTALVNVIAAV---SALSEEGDVQTGINTVIKALESPVRQIAENAGLEGSVIVNKLKEQ- 184
Cdd:cd03340   385 LHDAIMIVRRAIKNDSVVAGGGAIEMELSKYlrdYSRTIAGKQQLVINAFAKALEIIPRQLCDNAGFDATDILNKLRQKh 464

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1177256150 185 ----KEGFGYNAATDEWVDMIAAGIVDPTKVTRSALQNAAS 221
Cdd:cd03340   465 aqggGKWYGVDINNEGIADNFEAFVWEPSLVKINALTAATE 505
TCP1_delta cd03338
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ...
 102-220 3.12e-06

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: 47.28  E-value: 3.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177256150 102 LKERKYRIEDALNATRAAVEEGF-VAGGGTALVNViaaVSALSEEGDVQTGINTVI-----KALESPVRQIAENAGLEGS 175
Cdd:cd03338   375 LDEAERSLHDALCVIRCLVKKRAlIPGGGAPEIEI---ALQLSEWARTLTGVEQYCvrafaDALEVIPYTLAENAGLNPI 451

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1177256150 176 VIVNKLKEQ-KEG---FGYNAATDEWVDMIAAGIVDPTKVTRSALQNAA 220
Cdd:cd03338   452 SIVTELRNRhAQGeknAGINVRKGAITNILEENVVQPLLVSTSAITLAT 500
TCP1_beta cd03336
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ...
 86-220 5.84e-06

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


Pssm-ID: 239452 [Multi-domain]  Cd Length: 517  Bit Score: 46.55  E-value: 5.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177256150  86 AGGVAVINVGAATETELKERKYRIEDALNATRAAVEEG-FVAGGGTALVNVIAAVS--ALSEEGDVQTGINTVIKALESP 162
Cdd:cd03336   357 AGEACTIVLRGASQQILDEAERSLHDALCVLAQTVKDTrVVLGGGCSEMLMAKAVEelAKKTPGKKSLAIEAFAKALRQL 436

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1177256150 163 VRQIAENAGLEGSVIVNKLKEQ----KEGFGYNAATDEWVDMIAAGIVDPTKVTRSALQNAA 220
Cdd:cd03336   437 PTIIADNAGYDSAELVAQLRAAhyngNTTAGLDMRKGTVGDMKELGITESFKVKRQVLLSAS 498
TCP1_theta cd03341
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ...
 89-223 1.40e-05

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


Pssm-ID: 239457 [Multi-domain]  Cd Length: 472  Bit Score: 45.29  E-value: 1.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177256150  89 VAVINVGAATETELKERKYRIEDALNATRAAVEEG-FVAGGGT---ALVNVIAAVSAlSEEGDVQTGINTVIKALESPVR 164
Cdd:cd03341   316 IATIVLRGATQNILDDVERAIDDGVNVFKSLTKDGrFVPGAGAteiELAKKLKEYGE-KTPGLEQYAIKKFAEAFEVVPR 394

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1177256150 165 QIAENAGLEGSVIVNKL------KEQKEGFGYNAATDEWVDMIAAGIVDPTKVTRSALQNAASVS 223
Cdd:cd03341   395 TLAENAGLDATEVLSELyaahqkGNKSAGVDIESGDEGTKDAKEAGIFDHLATKKWAIKLATEAA 459
PTZ00212 PTZ00212
T-complex protein 1 subunit beta; Provisional
 87-220 2.73e-04

T-complex protein 1 subunit beta; Provisional


Pssm-ID: 185514  Cd Length: 533  Bit Score: 41.17  E-value: 2.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177256150  87 GGVAVINVGAATETELKERKYRIEDALNATRAAVEEG-FVAGGGTALVNVIAAVS--ALSEEGDVQTGINTVIKALESPV 163
Cdd:PTZ00212  370 GEACTIVLRGASTHILDEAERSLHDALCVLSQTVKDTrVVLGGGCSEMLMANAVEelAKKVEGKKSLAIEAFAKALRQIP 449

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1177256150 164 RQIAENAGLEGSVIVNKLK-EQKEG---FGYNAATDEWVDMIAAGIVDPTKVTRSALQNAA 220
Cdd:PTZ00212  450 TIIADNGGYDSAELVSKLRaEHYKGnktAGIDMEKGTVGDMKELGITESYKVKLSQLCSAT 510
TCP1_zeta cd03342
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ...
 80-223 3.22e-04

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: 41.09  E-value: 3.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177256150  80 ERLAKLAGGVAVINV-----------GAATETELKERKY-------------------------RIEDA----LNATRAA 119
Cdd:cd03342   280 ERLTLACGGVAMNSVddlspeclgyaGLVYERTLGEEKYtfiegvknpksctilikgpndhtitQIKDAirdgLRAVKNA 359

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177256150 120 VEEGFVAGGGTALVnvIAAVSALSEE-----GDVQTGINTVIKALESPVRQIAENAGLEG-SVIVNKLKEQKEG---FGY 190
Cdd:cd03342   360 IEDKCVVPGAGAFE--VALYAHLKEFkksvkGKAKLGVQAFADALLVIPKTLAENSGLDVqETLVKLQDEYAEGgqvGGV 437

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1177256150 191 NAATDEWVDMIAAGIVDPTKVTRSALQNAASVS 223
Cdd:cd03342   438 DLDTGEPMDPESEGIWDNYSVKRQILHSATVIA 470
chap_CCT_theta TIGR02346
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ...
 89-220 6.46e-04

T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT alpha chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.


Pssm-ID: 274087 [Multi-domain]  Cd Length: 531  Bit Score: 40.08  E-value: 6.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177256150  89 VAVINVGAATETELKERKYRIEDALNATRAAVEEG-FVAGGGTALVNVIAAVSALSE--EGDVQTGINTVIKALESPVRQ 165
Cdd:TIGR02346 364 ISTIILRGSTDNLLDDIERAIDDGVNTVKALVKDGrLLPGAGATEIELASRLTKYGEklPGLDQYAIKKFAEAFEIIPRT 443

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1177256150 166 IAENAGLEGSVIVNKL----KEQKEGFGYN--AATDEWVDMIAAGIVDPTKVTRSALQNAA 220
Cdd:TIGR02346 444 LAENAGLNANEVIPKLyaahKKGNKSKGIDieAESDGVKDASEAGIYDMLATKKWAIKLAT 504
 
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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