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Conserved domains on  [gi|1048348338|pdb|5CDJ|B]
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Chain B, RuBisCO large subunit-binding protein subunit alpha, chloroplastic

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 ...
 2-186 2.94e-99

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 cd03344:

Pssm-ID: 351886  Cd Length: 520  Bit Score: 295.90  E-value: 2.94e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5CDJ_B        2 EGMEIDRGYISPQFVTNQERLLVEYDNCRVLVTDQKIDAIRDIIPILEQVTRLNAPLLIIAEDVSGEALATLVVNKLRGV 81
Cdd:cd03344 188 EGMQFDRGYLSPYFVTDPEKMEVELENPYILLTDKKISSIQELLPILELVAKAGRPLLIIAEDVEGEALATLVVNKLRGG 267

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5CDJ_B       82 LNVCAIKAPGFGERRKSLLQDIAIVTGAEFIAKDLGMKVEQAVVEQLGVARKVTVANNTTTLIADAASKDEIEMRIAQLK 161
Cdd:cd03344 268 LKVCAVKAPGFGDRRKAMLEDIAILTGGTVISEELGLKLEDVTLEDLGRAKKVVVTKDDTTIIGGAGDKAAIKARIAQIR 347

                       170       180
                ....*....|....*....|....*
5CDJ_B      162 KELAETDSVYDTEKLSERIAKLSGG 186
Cdd:cd03344 348 KQIEETTSDYDKEKLQERLAKLSGG 372
 
Name Accession Description Interval E-value
GroEL cd03344
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ...
 2-186 2.94e-99

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: 295.90  E-value: 2.94e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5CDJ_B        2 EGMEIDRGYISPQFVTNQERLLVEYDNCRVLVTDQKIDAIRDIIPILEQVTRLNAPLLIIAEDVSGEALATLVVNKLRGV 81
Cdd:cd03344 188 EGMQFDRGYLSPYFVTDPEKMEVELENPYILLTDKKISSIQELLPILELVAKAGRPLLIIAEDVEGEALATLVVNKLRGG 267

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5CDJ_B       82 LNVCAIKAPGFGERRKSLLQDIAIVTGAEFIAKDLGMKVEQAVVEQLGVARKVTVANNTTTLIADAASKDEIEMRIAQLK 161
Cdd:cd03344 268 LKVCAVKAPGFGDRRKAMLEDIAILTGGTVISEELGLKLEDVTLEDLGRAKKVVVTKDDTTIIGGAGDKAAIKARIAQIR 347

                       170       180
                ....*....|....*....|....*
5CDJ_B      162 KELAETDSVYDTEKLSERIAKLSGG 186
Cdd:cd03344 348 KQIEETTSDYDKEKLQERLAKLSGG 372
groEL PRK00013
chaperonin GroEL; Reviewed
 2-186 5.88e-92

chaperonin GroEL; Reviewed


Pssm-ID: 234573  Cd Length: 542  Bit Score: 278.16  E-value: 5.88e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5CDJ_B         2 EGMEIDRGYISPQFVTNQERLLVEYDNCRVLVTDQKIDAIRDIIPILEQVTRLNAPLLIIAEDVSGEALATLVVNKLRGV 81
Cdd:PRK00013 190 EGMQFDRGYLSPYFVTDPEKMEAELENPYILITDKKISNIQDLLPVLEQVAQSGKPLLIIAEDVEGEALATLVVNKLRGT 269

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5CDJ_B        82 LNVCAIKAPGFGERRKSLLQDIAIVTGAEFIAKDLGMKVEQAVVEQLGVARKVTVANNTTTLIADAASKDEIEMRIAQLK 161
Cdd:PRK00013 270 LKVVAVKAPGFGDRRKAMLEDIAILTGGTVISEELGLKLEDATLEDLGQAKKVVVTKDNTTIVDGAGDKEAIKARVAQIK 349

                        170       180
                 ....*....|....*....|....*
5CDJ_B       162 KELAETDSVYDTEKLSERIAKLSGG 186
Cdd:PRK00013 350 AQIEETTSDYDREKLQERLAKLAGG 374
GroEL TIGR02348
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ...
 2-186 5.00e-86

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: 262.23  E-value: 5.00e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5CDJ_B          2 EGMEIDRGYISPQFVTNQERLLVEYDNCRVLVTDQKIDAIRDIIPILEQVTRLNAPLLIIAEDVSGEALATLVVNKLRGV 81
Cdd:TIGR02348 189 EGMQFDRGYISPYFVTDAEKMEVELENPYILITDKKISNIKDLLPLLEKVAQSGKPLLIIAEDVEGEALATLVVNKLRGT 268

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5CDJ_B         82 LNVCAIKAPGFGERRKSLLQDIAIVTGAEFIAKDLGMKVEQAVVEQLGVARKVTVANNTTTLIADAASKDEIEMRIAQLK 161
Cdd:TIGR02348 269 LNVCAVKAPGFGDRRKAMLEDIAILTGGQVISEELGLKLEEVTLDDLGKAKKVTVDKDNTTIVEGAGDKAAIKARVAQIK 348

                         170       180
                  ....*....|....*....|....*
5CDJ_B        162 KELAETDSVYDTEKLSERIAKLSGG 186
Cdd:TIGR02348 349 AQIEETTSDYDREKLQERLAKLAGG 373
GroEL COG0459
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ...
 2-157 2.58e-65

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


Pssm-ID: 440227  Cd Length: 497  Bit Score: 208.01  E-value: 2.58e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5CDJ_B        2 EGMEIDRGYISPQFVTNQERLLVEYDNCRVLVTDQKIDAIRDIIPILEQVTRLNAPLLIIAEDVSGEALATLVVNKLRGV 81
Cdd:COG0459 190 EGMQFDKGYLSPYFVTDPEKMPAELENAYILLTDKKISSIQDLLPLLEKVAQSGKPLLIIAEDIDGEALATLVVNGIRGV 269

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
5CDJ_B       82 LNVCAIKAPGFGERRKSLLQDIAIVTGAEFIAKDLGMKVEQAVVEQLGVARKVTVANNTTTLIADAASKDEIEMRI 157
Cdd:COG0459 270 LRVVAVKAPGFGDRRKAMLEDIAILTGGRVISEDLGLKLEDVTLDDLGRAKRVEVDKDNTTIVEGAGNPKAIVILV 345
Cpn60_TCP1 pfam00118
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ...
 2-157 1.38e-09

TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family and the TCP-1 (T-complex protein) family.


Pssm-ID: 395068 [Multi-domain]  Cd Length: 489  Bit Score: 56.06  E-value: 1.38e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5CDJ_B          2 EGMEIDRGYISPQFVTnqerllvEYDNCRVLVTDQKIDAIRD------------------------IIPILEQVTRLNAP 57
Cdd:pfam00118 181 DGVVLDKGPLHPDMPK-------RLENAKVLLLNCSLEYEKTetkatvvlsdaeqlerflkaeeeqILEIVEKIIDSGVN 253

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5CDJ_B         58 LLIIAEDVSGEALATLVVNKLRGVLNVcaikapgfgerRKSLLQDIAIVTGAEFIakdlgMKVEQAVVEQLGVARKV--- 134
Cdd:pfam00118 254 VVVCQKGIDDLALHFLAKNGIMALRRV-----------KKRDLERLAKATGARAV-----SSLDDLTPDDLGTAGKVeee 317

                         170       180       190
                  ....*....|....*....|....*....|....*...
5CDJ_B        135 TVANNTTTLIADAASK---------------DEIEMRI 157
Cdd:pfam00118 318 KIGDEKYTFIEGCKSPkaatillrgatdhvlDEIERSI 355
 
Name Accession Description Interval E-value
GroEL cd03344
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ...
 2-186 2.94e-99

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: 295.90  E-value: 2.94e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5CDJ_B        2 EGMEIDRGYISPQFVTNQERLLVEYDNCRVLVTDQKIDAIRDIIPILEQVTRLNAPLLIIAEDVSGEALATLVVNKLRGV 81
Cdd:cd03344 188 EGMQFDRGYLSPYFVTDPEKMEVELENPYILLTDKKISSIQELLPILELVAKAGRPLLIIAEDVEGEALATLVVNKLRGG 267

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5CDJ_B       82 LNVCAIKAPGFGERRKSLLQDIAIVTGAEFIAKDLGMKVEQAVVEQLGVARKVTVANNTTTLIADAASKDEIEMRIAQLK 161
Cdd:cd03344 268 LKVCAVKAPGFGDRRKAMLEDIAILTGGTVISEELGLKLEDVTLEDLGRAKKVVVTKDDTTIIGGAGDKAAIKARIAQIR 347

                       170       180
                ....*....|....*....|....*
5CDJ_B      162 KELAETDSVYDTEKLSERIAKLSGG 186
Cdd:cd03344 348 KQIEETTSDYDKEKLQERLAKLSGG 372
groEL PRK00013
chaperonin GroEL; Reviewed
 2-186 5.88e-92

chaperonin GroEL; Reviewed


Pssm-ID: 234573  Cd Length: 542  Bit Score: 278.16  E-value: 5.88e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5CDJ_B         2 EGMEIDRGYISPQFVTNQERLLVEYDNCRVLVTDQKIDAIRDIIPILEQVTRLNAPLLIIAEDVSGEALATLVVNKLRGV 81
Cdd:PRK00013 190 EGMQFDRGYLSPYFVTDPEKMEAELENPYILITDKKISNIQDLLPVLEQVAQSGKPLLIIAEDVEGEALATLVVNKLRGT 269

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5CDJ_B        82 LNVCAIKAPGFGERRKSLLQDIAIVTGAEFIAKDLGMKVEQAVVEQLGVARKVTVANNTTTLIADAASKDEIEMRIAQLK 161
Cdd:PRK00013 270 LKVVAVKAPGFGDRRKAMLEDIAILTGGTVISEELGLKLEDATLEDLGQAKKVVVTKDNTTIVDGAGDKEAIKARVAQIK 349

                        170       180
                 ....*....|....*....|....*
5CDJ_B       162 KELAETDSVYDTEKLSERIAKLSGG 186
Cdd:PRK00013 350 AQIEETTSDYDREKLQERLAKLAGG 374
groEL PRK12849
chaperonin GroEL; Reviewed
 2-186 8.78e-91

chaperonin GroEL; Reviewed


Pssm-ID: 237230  Cd Length: 542  Bit Score: 275.15  E-value: 8.78e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5CDJ_B         2 EGMEIDRGYISPQFVTNQERLLVEYDNCRVLVTDQKIDAIRDIIPILEQVTRLNAPLLIIAEDVSGEALATLVVNKLRGV 81
Cdd:PRK12849 190 EGMQFDRGYLSPYFVTDPERMEAVLEDPLILLTDKKISSLQDLLPLLEKVAQSGKPLLIIAEDVEGEALATLVVNKLRGG 269

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5CDJ_B        82 LNVCAIKAPGFGERRKSLLQDIAIVTGAEFIAKDLGMKVEQAVVEQLGVARKVTVANNTTTLIADAASKDEIEMRIAQLK 161
Cdd:PRK12849 270 LKVAAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGLKLEEVTLDDLGRAKRVTITKDNTTIVDGAGDKEAIEARVAQIR 349

                        170       180
                 ....*....|....*....|....*
5CDJ_B       162 KELAETDSVYDTEKLSERIAKLSGG 186
Cdd:PRK12849 350 RQIEETTSDYDREKLQERLAKLAGG 374
GroEL TIGR02348
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ...
 2-186 5.00e-86

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: 262.23  E-value: 5.00e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5CDJ_B          2 EGMEIDRGYISPQFVTNQERLLVEYDNCRVLVTDQKIDAIRDIIPILEQVTRLNAPLLIIAEDVSGEALATLVVNKLRGV 81
Cdd:TIGR02348 189 EGMQFDRGYISPYFVTDAEKMEVELENPYILITDKKISNIKDLLPLLEKVAQSGKPLLIIAEDVEGEALATLVVNKLRGT 268

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5CDJ_B         82 LNVCAIKAPGFGERRKSLLQDIAIVTGAEFIAKDLGMKVEQAVVEQLGVARKVTVANNTTTLIADAASKDEIEMRIAQLK 161
Cdd:TIGR02348 269 LNVCAVKAPGFGDRRKAMLEDIAILTGGQVISEELGLKLEEVTLDDLGKAKKVTVDKDNTTIVEGAGDKAAIKARVAQIK 348

                         170       180
                  ....*....|....*....|....*
5CDJ_B        162 KELAETDSVYDTEKLSERIAKLSGG 186
Cdd:TIGR02348 349 AQIEETTSDYDREKLQERLAKLAGG 373
groEL PRK12851
chaperonin GroEL; Reviewed
 2-186 8.59e-78

chaperonin GroEL; Reviewed


Pssm-ID: 171770  Cd Length: 541  Bit Score: 241.57  E-value: 8.59e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5CDJ_B         2 EGMEIDRGYISPQFVTNQERLLVEYDNCRVLVTDQKIDAIRDIIPILEQVTRLNAPLLIIAEDVSGEALATLVVNKLRGV 81
Cdd:PRK12851 191 EGMQFDRGYLSPYFVTDADKMEAELEDPYILIHEKKISNLQDLLPVLEAVVQSGKPLLIIAEDVEGEALATLVVNKLRGG 270

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5CDJ_B        82 LNVCAIKAPGFGERRKSLLQDIAIVTGAEFIAKDLGMKVEQAVVEQLGVARKVTVANNTTTLIADAASKDEIEMRIAQLK 161
Cdd:PRK12851 271 LKVAAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGIKLENVTLEQLGRAKKVVVEKENTTIIDGAGSKTEIEGRVAQIR 350

                        170       180
                 ....*....|....*....|....*
5CDJ_B       162 KELAETDSVYDTEKLSERIAKLSGG 186
Cdd:PRK12851 351 AQIEETTSDYDREKLQERLAKLAGG 375
groEL PRK12850
chaperonin GroEL; Reviewed
 2-186 2.98e-77

chaperonin GroEL; Reviewed


Pssm-ID: 237231  Cd Length: 544  Bit Score: 240.39  E-value: 2.98e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5CDJ_B         2 EGMEIDRGYISPQFVTNQERLLVEYDNCRVLVTDQKIDAIRDIIPILEQVTRLNAPLLIIAEDVSGEALATLVVNKLRGV 81
Cdd:PRK12850 191 EGMQFDRGYLSPYFVTNPEKMRAELEDPYILLHEKKISNLQDLLPILEAVVQSGRPLLIIAEDVEGEALATLVVNKLRGG 270

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5CDJ_B        82 LNVCAIKAPGFGERRKSLLQDIAIVTGAEFIAKDLGMKVEQAVVEQLGVARKVTVANNTTTLIADAASKDEIEMRIAQLK 161
Cdd:PRK12850 271 LKSVAVKAPGFGDRRKAMLEDIAVLTGGQVISEDLGIKLENVTLDMLGRAKRVLITKENTTIIDGAGDKKNIEARVKQIR 350

                        170       180
                 ....*....|....*....|....*
5CDJ_B       162 KELAETDSVYDTEKLSERIAKLSGG 186
Cdd:PRK12850 351 AQIEETTSDYDREKLQERLAKLAGG 375
groEL CHL00093
chaperonin GroEL
 1-186 8.53e-77

chaperonin GroEL


Pssm-ID: 177025  Cd Length: 529  Bit Score: 238.47  E-value: 8.53e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5CDJ_B         1 SEGMEIDRGYISPQFVTNQERLLVEYDNCRVLVTDQKIDAIR-DIIPILEQVTRLNAPLLIIAEDVSGEALATLVVNKLR 79
Cdd:CHL00093 189 TEGMRFEKGFISPYFVTDTERMEVVQENPYILLTDKKITLVQqDLLPILEQVTKTKRPLLIIAEDVEKEALATLVLNKLR 268

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5CDJ_B        80 GVLNVCAIKAPGFGERRKSLLQDIAIVTGAEFIAKDLGMKVEQAVVEQLGVARKVTVANNTTTLIADaASKDEIEMRIAQ 159
Cdd:CHL00093 269 GIVNVVAVRAPGFGDRRKAMLEDIAILTGGQVITEDAGLSLETIQLDLLGQARRIIVTKDSTTIIAD-GNEEQVKARCEQ 347

                        170       180
                 ....*....|....*....|....*..
5CDJ_B       160 LKKELAETDSVYDTEKLSERIAKLSGG 186
Cdd:CHL00093 348 LRKQIEIADSSYEKEKLQERLAKLSGG 374
PTZ00114 PTZ00114
Heat shock protein 60; Provisional
 2-186 7.26e-74

Heat shock protein 60; Provisional


Pssm-ID: 185455  Cd Length: 555  Bit Score: 231.73  E-value: 7.26e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5CDJ_B         2 EGMEIDRGYISPQFVTNQERLLVEYDNCRVLVTDQKIDAIRDIIPILEQVTRLNAPLLIIAEDVSGEALATLVVNKLRGV 81
Cdd:PTZ00114 202 EGMSFDRGYISPYFVTNEKTQKVELENPLILVTDKKISSIQSILPILEHAVKNKRPLLIIAEDVEGEALQTLIINKLRGG 281

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5CDJ_B        82 LNVCAIKAPGFGERRKSLLQDIAIVTGAEFIAKD-LGMKVEQAVVEQLGVARKVTVANNTTTLIADAASKDEIEMRIAQL 160
Cdd:PTZ00114 282 LKVCAVKAPGFGDNRKDILQDIAVLTGATVVSEDnVGLKLDDFDPSMLGSAKKVTVTKDETVILTGGGDKAEIKERVELL 361

                        170       180
                 ....*....|....*....|....*.
5CDJ_B       161 KKELAETDSVYDTEKLSERIAKLSGG 186
Cdd:PTZ00114 362 RSQIERTTSEYDKEKLKERLAKLSGG 387
groEL PRK12852
chaperonin GroEL; Reviewed
 2-186 2.86e-72

chaperonin GroEL; Reviewed


Pssm-ID: 237232  Cd Length: 545  Bit Score: 227.42  E-value: 2.86e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5CDJ_B         2 EGMEIDRGYISPQFVTNQERLLVEYDNCRVLVTDQKIDAIRDIIPILEQVTRLNAPLLIIAEDVSGEALATLVVNKLRGV 81
Cdd:PRK12852 191 EGMKFDRGYLSPYFVTNAEKMTVELDDAYILLHEKKLSGLQAMLPVLEAVVQSGKPLLIIAEDVEGEALATLVVNRLRGG 270

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5CDJ_B        82 LNVCAIKAPGFGERRKSLLQDIAIVTGAEFIAKDLGMKVEQAVVEQLGVARKVTVANNTTTLIADAASKDEIEMRIAQLK 161
Cdd:PRK12852 271 LKVAAVKAPGFGDRRKAMLEDIAILTGGQLISEDLGIKLENVTLKMLGRAKKVVIDKENTTIVNGAGKKADIEARVGQIK 350

                        170       180
                 ....*....|....*....|....*
5CDJ_B       162 KELAETDSVYDTEKLSERIAKLSGG 186
Cdd:PRK12852 351 AQIEETTSDYDREKLQERLAKLAGG 375
GroEL COG0459
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ...
 2-157 2.58e-65

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


Pssm-ID: 440227  Cd Length: 497  Bit Score: 208.01  E-value: 2.58e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5CDJ_B        2 EGMEIDRGYISPQFVTNQERLLVEYDNCRVLVTDQKIDAIRDIIPILEQVTRLNAPLLIIAEDVSGEALATLVVNKLRGV 81
Cdd:COG0459 190 EGMQFDKGYLSPYFVTDPEKMPAELENAYILLTDKKISSIQDLLPLLEKVAQSGKPLLIIAEDIDGEALATLVVNGIRGV 269

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
5CDJ_B       82 LNVCAIKAPGFGERRKSLLQDIAIVTGAEFIAKDLGMKVEQAVVEQLGVARKVTVANNTTTLIADAASKDEIEMRI 157
Cdd:COG0459 270 LRVVAVKAPGFGDRRKAMLEDIAILTGGRVISEDLGLKLEDVTLDDLGRAKRVEVDKDNTTIVEGAGNPKAIVILV 345
PRK14104 PRK14104
chaperonin GroEL; Provisional
 2-186 1.15e-64

chaperonin GroEL; Provisional


Pssm-ID: 172594  Cd Length: 546  Bit Score: 207.58  E-value: 1.15e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5CDJ_B         2 EGMEIDRGYISPQFVTNQERLLVEYDNCRVLVTDQKIDAIRDIIPILEQVTRLNAPLLIIAEDVSGEALATLVVNKLRGV 81
Cdd:PRK14104 191 EGMQFDRGYISPYFVTNADKMRVEMDDAYILINEKKLSSLNELLPLLEAVVQTGKPLVIVAEDVEGEALATLVVNRLRGG 270

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5CDJ_B        82 LNVCAIKAPGFGERRKSLLQDIAIVTGAEFIAKDLGMKVEQAVVEQLGVARKVTVANNTTTLIADAASKDEIEMRIAQLK 161
Cdd:PRK14104 271 LKVAAVKAPGFGDRRKAMLQDIAILTGGQAISEDLGIKLENVTLQMLGRAKKVMIDKENTTIVNGAGKKADIEARVAQIK 350

                        170       180
                 ....*....|....*....|....*
5CDJ_B       162 KELAETDSVYDTEKLSERIAKLSGG 186
Cdd:PRK14104 351 AQIEETTSDYDREKLQERLAKLAGG 375
PLN03167 PLN03167
Chaperonin-60 beta subunit; Provisional
 2-186 1.31e-63

Chaperonin-60 beta subunit; Provisional


Pssm-ID: 215611 [Multi-domain]  Cd Length: 600  Bit Score: 205.93  E-value: 1.31e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5CDJ_B         2 EGMEIDRGYISPQFVTNQERLLVEYDNCRVLVTDQKIDAIRDIIPILEQVTRLNAPLLIIAEDVSGEALATLVVNKLRGV 81
Cdd:PLN03167 245 EGMQFDRGYISPYFVTDSEKMSVEYDNCKLLLVDKKITNARDLIGILEDAIRGGYPLLIIAEDIEQEALATLVVNKLRGS 324

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5CDJ_B        82 LNVCAIKAPGFGERRKSLLQDIAIVTGAEFIAKDLGMKVEQAVVEQLGVARKVTVANNTTTLIADAASKDEIEMRIAQLK 161
Cdd:PLN03167 325 LKIAALKAPGFGERKSQYLDDIAILTGGTVIREEVGLSLDKVGKEVLGTAAKVVLTKDTTTIVGDGSTQEAVNKRVAQIK 404

                        170       180
                 ....*....|....*....|....*
5CDJ_B       162 KELAETDSVYDTEKLSERIAKLSGG 186
Cdd:PLN03167 405 NLIEAAEQDYEKEKLNERIAKLSGG 429
chaperonin_type_I_II cd00309
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ...
 2-136 3.84e-17

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: 78.24  E-value: 3.84e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5CDJ_B        2 EGMEIDRGYISPQFvtnqerlLVEYDNCRVLVTDQKIDairdiipileqvtrlnapLLIIAED-VSGEALATLVVnklrg 80
Cdd:cd00309 199 VGMVFDKGYLSPYM-------PKRLENAKILLLDCKLE------------------YVVIAEKgIDDEALHYLAK----- 248

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
5CDJ_B       81 vLNVCAIKApgfgeRRKSLLQDIAIVTGAEFIAkdlgmKVEQAVVEQLGVARKVTV 136
Cdd:cd00309 249 -LGIMAVRR-----VRKEDLERIAKATGATIVS-----RLEDLTPEDLGTAGLVEE 293
chaperonin_like cd03333
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ...
 2-136 7.50e-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: 69.42  E-value: 7.50e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5CDJ_B        2 EGMEIDRGYISPQFvtnqerlLVEYDNCRVLVTDQKIDairdiipileqvtrlnapLLIIAED-VSGEALATLVVnklrg 80
Cdd:cd03333  63 VGVVFDKGYASPYM-------PKRLENAKILLLDCPLE------------------YVVIAEKgIDDLALHYLAK----- 112

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
5CDJ_B       81 vLNVCAIKApgfgeRRKSLLQDIAIVTGAEFIAkdlgmKVEQAVVEQLGVARKVTV 136
Cdd:cd03333 113 -AGIMAVRR-----VKKEDLERIARATGATIVS-----SLEDLTPEDLGTAELVEE 157
Cpn60_TCP1 pfam00118
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ...
 2-157 1.38e-09

TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family and the TCP-1 (T-complex protein) family.


Pssm-ID: 395068 [Multi-domain]  Cd Length: 489  Bit Score: 56.06  E-value: 1.38e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5CDJ_B          2 EGMEIDRGYISPQFVTnqerllvEYDNCRVLVTDQKIDAIRD------------------------IIPILEQVTRLNAP 57
Cdd:pfam00118 181 DGVVLDKGPLHPDMPK-------RLENAKVLLLNCSLEYEKTetkatvvlsdaeqlerflkaeeeqILEIVEKIIDSGVN 253

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5CDJ_B         58 LLIIAEDVSGEALATLVVNKLRGVLNVcaikapgfgerRKSLLQDIAIVTGAEFIakdlgMKVEQAVVEQLGVARKV--- 134
Cdd:pfam00118 254 VVVCQKGIDDLALHFLAKNGIMALRRV-----------KKRDLERLAKATGARAV-----SSLDDLTPDDLGTAGKVeee 317

                         170       180       190
                  ....*....|....*....|....*....|....*...
5CDJ_B        135 TVANNTTTLIADAASK---------------DEIEMRI 157
Cdd:pfam00118 318 KIGDEKYTFIEGCKSPkaatillrgatdhvlDEIERSI 355
 
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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