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Conserved domains on  [gi|311353288|gb|ADP93829|]
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chaperonin GroEL, partial [Clostridium perfringens]

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 ...
 1-199 1.05e-129

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: 375.23  E-value: 1.05e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311353288   1 KEVATKTNDVAGDGTTTATLLAQAIIREGLKNVTAGANPILIRNGIKTAVEKAVEEIQKISKPVNGKEDIARVAAISA-A 79
Cdd:PRK00013  74 KEVASKTNDVAGDGTTTATVLAQAIVREGLKNVAAGANPMDLKRGIDKAVEAAVEELKKISKPVEDKEEIAQVATISAnG 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311353288  80 DEKIGKLIADAMEKVGNEGVITVEESKSMGTELDVVEGMQFDRGYVSAYMVTDTEKMEAVLDNPLVLITDKKISNIQDLL 159
Cdd:PRK00013 154 DEEIGKLIAEAMEKVGKEGVITVEESKGFETELEVVEGMQFDRGYLSPYFVTDPEKMEAELENPYILITDKKISNIQDLL 233

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 311353288 160 PLLEQIVQAGKKLLIIADDIEGEAMTTLVVNKLRGTFTCV 199
Cdd:PRK00013 234 PVLEQVAQSGKPLLIIAEDVEGEALATLVVNKLRGTLKVV 273
 
Name Accession Description Interval E-value
groEL PRK00013
chaperonin GroEL; Reviewed
 1-199 1.05e-129

chaperonin GroEL; Reviewed


Pssm-ID: 234573  Cd Length: 542  Bit Score: 375.23  E-value: 1.05e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311353288   1 KEVATKTNDVAGDGTTTATLLAQAIIREGLKNVTAGANPILIRNGIKTAVEKAVEEIQKISKPVNGKEDIARVAAISA-A 79
Cdd:PRK00013  74 KEVASKTNDVAGDGTTTATVLAQAIVREGLKNVAAGANPMDLKRGIDKAVEAAVEELKKISKPVEDKEEIAQVATISAnG 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311353288  80 DEKIGKLIADAMEKVGNEGVITVEESKSMGTELDVVEGMQFDRGYVSAYMVTDTEKMEAVLDNPLVLITDKKISNIQDLL 159
Cdd:PRK00013 154 DEEIGKLIAEAMEKVGKEGVITVEESKGFETELEVVEGMQFDRGYLSPYFVTDPEKMEAELENPYILITDKKISNIQDLL 233

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 311353288 160 PLLEQIVQAGKKLLIIADDIEGEAMTTLVVNKLRGTFTCV 199
Cdd:PRK00013 234 PVLEQVAQSGKPLLIIAEDVEGEALATLVVNKLRGTLKVV 273
GroEL cd03344
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ...
 1-199 1.23e-114

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: 335.97  E-value: 1.23e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311353288   1 KEVATKTNDVAGDGTTTATLLAQAIIREGLKNVTAGANPILIRNGIKTAVEKAVEEIQKISKPVNGKEDIARVAAISA-A 79
Cdd:cd03344   72 KEVASKTNDVAGDGTTTATVLARAIIKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKPVKTKEEIAQVATISAnG 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311353288  80 DEKIGKLIADAMEKVGNEGVITVEESKSMGTELDVVEGMQFDRGYVSAYMVTDTEKMEAVLDNPLVLITDKKISNIQDLL 159
Cdd:cd03344  152 DEEIGELIAEAMEKVGKDGVITVEEGKTLETELEVVEGMQFDRGYLSPYFVTDPEKMEVELENPYILLTDKKISSIQELL 231

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 311353288 160 PLLEQIVQAGKKLLIIADDIEGEAMTTLVVNKLRGTFTCV 199
Cdd:cd03344  232 PILELVAKAGRPLLIIAEDVEGEALATLVVNKLRGGLKVC 271
GroEL COG0459
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ...
 1-199 2.37e-111

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


Pssm-ID: 440227  Cd Length: 497  Bit Score: 326.65  E-value: 2.37e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311353288   1 KEVATKTNDVAGDGTTTATLLAQAIIREGLKNVTAGANPILIRNGIKTAVEKAVEEIQKISKPVNGKEDIARVAAISAA- 79
Cdd:COG0459   74 KEVASKTNDEAGDGTTTATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPVDDKEELAQVATISANg 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311353288  80 DEKIGKLIADAMEKVGNEGVITVEESKSMGTELDVVEGMQFDRGYVSAYMVTDTEKMEAVLDNPLVLITDKKISNIQDLL 159
Cdd:COG0459  154 DEEIGELIAEAMEKVGKDGVITVEEGKGLETELEVVEGMQFDKGYLSPYFVTDPEKMPAELENAYILLTDKKISSIQDLL 233

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 311353288 160 PLLEQIVQAGKKLLIIADDIEGEAMTTLVVNKLRGTFTCV 199
Cdd:COG0459  234 PLLEKVAQSGKPLLIIAEDIDGEALATLVVNGIRGVLRVV 273
GroEL TIGR02348
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ...
 1-199 9.94e-111

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: 326.17  E-value: 9.94e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311353288    1 KEVATKTNDVAGDGTTTATLLAQAIIREGLKNVTAGANPILIRNGIKTAVEKAVEEIQKISKPVNGKEDIARVAAISA-A 79
Cdd:TIGR02348  73 KEVASKTNDVAGDGTTTATVLAQAIVKEGLKNVAAGANPIELKRGIEKAVEAVVEELKKLSKPVKGKKEIAQVATISAnN 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311353288   80 DEKIGKLIADAMEKVGNEGVITVEESKSMGTELDVVEGMQFDRGYVSAYMVTDTEKMEAVLDNPLVLITDKKISNIQDLL 159
Cdd:TIGR02348 153 DEEIGSLIAEAMEKVGKDGVITVEESKSLETELEVVEGMQFDRGYISPYFVTDAEKMEVELENPYILITDKKISNIKDLL 232

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 311353288  160 PLLEQIVQAGKKLLIIADDIEGEAMTTLVVNKLRGTFTCV 199
Cdd:TIGR02348 233 PLLEKVAQSGKPLLIIAEDVEGEALATLVVNKLRGTLNVC 272
Cpn60_TCP1 pfam00118
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ...
 2-194 2.50e-28

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: 110.37  E-value: 2.50e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311353288    2 EVATKTNDVAGDGTTTATLLAQAIIREGLKNVTAGANPILIRNGIKTAVEKAVE---EIQKISKPVNGKEDIARVAAISA 78
Cdd:pfam00118  50 EAAKAQDEEVGDGTTTVVVLAGELLEEAEKLLAAGVHPTTIIEGYEKALEKALEildSIISIPVEDVDREDLLKVARTSL 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311353288   79 A-------DEKIGKLIADAME---------KVGNEGVITVEESKSMGTELdvVEGMQFDRGYVSaymvtdtEKMEAVLDN 142
Cdd:pfam00118 130 SskiisreSDFLAKLVVDAVLaipkndgsfDLGNIGVVKILGGSLEDSEL--VDGVVLDKGPLH-------PDMPKRLEN 200

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 311353288  143 PLVLITDKKISNIQD------------------------LLPLLEQIVQAGKKLLIIADDIEGEAMTTLVVNKLRG 194
Cdd:pfam00118 201 AKVLLLNCSLEYEKTetkatvvlsdaeqlerflkaeeeqILEIVEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMA 276
 
Name Accession Description Interval E-value
groEL PRK00013
chaperonin GroEL; Reviewed
 1-199 1.05e-129

chaperonin GroEL; Reviewed


Pssm-ID: 234573  Cd Length: 542  Bit Score: 375.23  E-value: 1.05e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311353288   1 KEVATKTNDVAGDGTTTATLLAQAIIREGLKNVTAGANPILIRNGIKTAVEKAVEEIQKISKPVNGKEDIARVAAISA-A 79
Cdd:PRK00013  74 KEVASKTNDVAGDGTTTATVLAQAIVREGLKNVAAGANPMDLKRGIDKAVEAAVEELKKISKPVEDKEEIAQVATISAnG 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311353288  80 DEKIGKLIADAMEKVGNEGVITVEESKSMGTELDVVEGMQFDRGYVSAYMVTDTEKMEAVLDNPLVLITDKKISNIQDLL 159
Cdd:PRK00013 154 DEEIGKLIAEAMEKVGKEGVITVEESKGFETELEVVEGMQFDRGYLSPYFVTDPEKMEAELENPYILITDKKISNIQDLL 233

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 311353288 160 PLLEQIVQAGKKLLIIADDIEGEAMTTLVVNKLRGTFTCV 199
Cdd:PRK00013 234 PVLEQVAQSGKPLLIIAEDVEGEALATLVVNKLRGTLKVV 273
GroEL cd03344
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ...
 1-199 1.23e-114

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: 335.97  E-value: 1.23e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311353288   1 KEVATKTNDVAGDGTTTATLLAQAIIREGLKNVTAGANPILIRNGIKTAVEKAVEEIQKISKPVNGKEDIARVAAISA-A 79
Cdd:cd03344   72 KEVASKTNDVAGDGTTTATVLARAIIKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKPVKTKEEIAQVATISAnG 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311353288  80 DEKIGKLIADAMEKVGNEGVITVEESKSMGTELDVVEGMQFDRGYVSAYMVTDTEKMEAVLDNPLVLITDKKISNIQDLL 159
Cdd:cd03344  152 DEEIGELIAEAMEKVGKDGVITVEEGKTLETELEVVEGMQFDRGYLSPYFVTDPEKMEVELENPYILLTDKKISSIQELL 231

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 311353288 160 PLLEQIVQAGKKLLIIADDIEGEAMTTLVVNKLRGTFTCV 199
Cdd:cd03344  232 PILELVAKAGRPLLIIAEDVEGEALATLVVNKLRGGLKVC 271
groEL PRK12849
chaperonin GroEL; Reviewed
 1-199 2.01e-112

chaperonin GroEL; Reviewed


Pssm-ID: 237230  Cd Length: 542  Bit Score: 331.00  E-value: 2.01e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311353288   1 KEVATKTNDVAGDGTTTATLLAQAIIREGLKNVTAGANPILIRNGIKTAVEKAVEEIQKISKPVNGKEDIARVAAISA-A 79
Cdd:PRK12849  74 KEVASKTNDVAGDGTTTATVLAQALVQEGLKNVAAGANPMDLKRGIDKAVEAVVEELKALARPVSGSEEIAQVATISAnG 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311353288  80 DEKIGKLIADAMEKVGNEGVITVEESKSMGTELDVVEGMQFDRGYVSAYMVTDTEKMEAVLDNPLVLITDKKISNIQDLL 159
Cdd:PRK12849 154 DEEIGELIAEAMEKVGKDGVITVEESKTLETELEVTEGMQFDRGYLSPYFVTDPERMEAVLEDPLILLTDKKISSLQDLL 233

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 311353288 160 PLLEQIVQAGKKLLIIADDIEGEAMTTLVVNKLRGTFTCV 199
Cdd:PRK12849 234 PLLEKVAQSGKPLLIIAEDVEGEALATLVVNKLRGGLKVA 273
GroEL COG0459
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ...
 1-199 2.37e-111

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


Pssm-ID: 440227  Cd Length: 497  Bit Score: 326.65  E-value: 2.37e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311353288   1 KEVATKTNDVAGDGTTTATLLAQAIIREGLKNVTAGANPILIRNGIKTAVEKAVEEIQKISKPVNGKEDIARVAAISAA- 79
Cdd:COG0459   74 KEVASKTNDEAGDGTTTATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPVDDKEELAQVATISANg 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311353288  80 DEKIGKLIADAMEKVGNEGVITVEESKSMGTELDVVEGMQFDRGYVSAYMVTDTEKMEAVLDNPLVLITDKKISNIQDLL 159
Cdd:COG0459  154 DEEIGELIAEAMEKVGKDGVITVEEGKGLETELEVVEGMQFDKGYLSPYFVTDPEKMPAELENAYILLTDKKISSIQDLL 233

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 311353288 160 PLLEQIVQAGKKLLIIADDIEGEAMTTLVVNKLRGTFTCV 199
Cdd:COG0459  234 PLLEKVAQSGKPLLIIAEDIDGEALATLVVNGIRGVLRVV 273
GroEL TIGR02348
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ...
 1-199 9.94e-111

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: 326.17  E-value: 9.94e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311353288    1 KEVATKTNDVAGDGTTTATLLAQAIIREGLKNVTAGANPILIRNGIKTAVEKAVEEIQKISKPVNGKEDIARVAAISA-A 79
Cdd:TIGR02348  73 KEVASKTNDVAGDGTTTATVLAQAIVKEGLKNVAAGANPIELKRGIEKAVEAVVEELKKLSKPVKGKKEIAQVATISAnN 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311353288   80 DEKIGKLIADAMEKVGNEGVITVEESKSMGTELDVVEGMQFDRGYVSAYMVTDTEKMEAVLDNPLVLITDKKISNIQDLL 159
Cdd:TIGR02348 153 DEEIGSLIAEAMEKVGKDGVITVEESKSLETELEVVEGMQFDRGYISPYFVTDAEKMEVELENPYILITDKKISNIKDLL 232

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 311353288  160 PLLEQIVQAGKKLLIIADDIEGEAMTTLVVNKLRGTFTCV 199
Cdd:TIGR02348 233 PLLEKVAQSGKPLLIIAEDVEGEALATLVVNKLRGTLNVC 272
groEL PRK12850
chaperonin GroEL; Reviewed
 1-199 1.18e-103

chaperonin GroEL; Reviewed


Pssm-ID: 237231  Cd Length: 544  Bit Score: 308.57  E-value: 1.18e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311353288   1 KEVATKTNDVAGDGTTTATLLAQAIIREGLKNVTAGANPILIRNGIKTAVEKAVEEIQKISKPVNGKEDIARVAAISA-A 79
Cdd:PRK12850  75 KEVASKTNDLAGDGTTTATVLAQAIVREGAKLVAAGMNPMDLKRGIDLAVAAVVDELKKIAKKVTSSKEIAQVATISAnG 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311353288  80 DEKIGKLIADAMEKVGNEGVITVEESKSMGTELDVVEGMQFDRGYVSAYMVTDTEKMEAVLDNPLVLITDKKISNIQDLL 159
Cdd:PRK12850 155 DESIGEMIAEAMDKVGKEGVITVEEAKTLGTELDVVEGMQFDRGYLSPYFVTNPEKMRAELEDPYILLHEKKISNLQDLL 234

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 311353288 160 PLLEQIVQAGKKLLIIADDIEGEAMTTLVVNKLRGTFTCV 199
Cdd:PRK12850 235 PILEAVVQSGRPLLIIAEDVEGEALATLVVNKLRGGLKSV 274
groEL PRK12851
chaperonin GroEL; Reviewed
 1-196 9.02e-98

chaperonin GroEL; Reviewed


Pssm-ID: 171770  Cd Length: 541  Bit Score: 293.57  E-value: 9.02e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311353288   1 KEVATKTNDVAGDGTTTATLLAQAIIREGLKNVTAGANPILIRNGIKTAVEKAVEEIQKISKPVNGKEDIARVAAISA-A 79
Cdd:PRK12851  75 REVASKTNDVAGDGTTTATVLAQAIVREGAKAVAAGANPMDLKRGIDRAVAAVVEELKANARPVTTNAEIAQVATISAnG 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311353288  80 DEKIGKLIADAMEKVGNEGVITVEESKSMGTELDVVEGMQFDRGYVSAYMVTDTEKMEAVLDNPLVLITDKKISNIQDLL 159
Cdd:PRK12851 155 DAEIGRLVAEAMEKVGNEGVITVEESKTAETELEVVEGMQFDRGYLSPYFVTDADKMEAELEDPYILIHEKKISNLQDLL 234

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 311353288 160 PLLEQIVQAGKKLLIIADDIEGEAMTTLVVNKLRGTF 196
Cdd:PRK12851 235 PVLEAVVQSGKPLLIIAEDVEGEALATLVVNKLRGGL 271
PTZ00114 PTZ00114
Heat shock protein 60; Provisional
 1-199 1.10e-87

Heat shock protein 60; Provisional


Pssm-ID: 185455  Cd Length: 555  Bit Score: 267.93  E-value: 1.10e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311353288   1 KEVATKTNDVAGDGTTTATLLAQAIIREGLKNVTAGANPILIRNGIKTAVEKAVEEIQKISKPVNGKEDIARVAAISA-A 79
Cdd:PTZ00114  86 RQVASKTNDKAGDGTTTATILARAIFREGCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQSRPVKTKEDILNVATISAnG 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311353288  80 DEKIGKLIADAMEKVGNEGVITVEESKSMGTELDVVEGMQFDRGYVSAYMVTDTEKMEAVLDNPLVLITDKKISNIQDLL 159
Cdd:PTZ00114 166 DVEIGSLIADAMDKVGKDGTITVEDGKTLEDELEVVEGMSFDRGYISPYFVTNEKTQKVELENPLILVTDKKISSIQSIL 245

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 311353288 160 PLLEQIVQAGKKLLIIADDIEGEAMTTLVVNKLRGTFTCV 199
Cdd:PTZ00114 246 PILEHAVKNKRPLLIIAEDVEGEALQTLIINKLRGGLKVC 285
groEL CHL00093
chaperonin GroEL
 1-194 1.90e-86

chaperonin GroEL


Pssm-ID: 177025  Cd Length: 529  Bit Score: 264.27  E-value: 1.90e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311353288   1 KEVATKTNDVAGDGTTTATLLAQAIIREGLKNVTAGANPILIRNGIKTAVEKAVEEIQKISKPVNGKEDIARVAAISAA- 79
Cdd:CHL00093  74 RQAASKTNDVAGDGTTTATVLAYAIVKQGMKNVAAGANPISLKRGIEKATQYVVSQIAEYARPVEDIQAITQVASISAGn 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311353288  80 DEKIGKLIADAMEKVGNEGVITVEESKSMGTELDVVEGMQFDRGYVSAYMVTDTEKMEAVLDNPLVLITDKKISNI-QDL 158
Cdd:CHL00093 154 DEEVGSMIADAIEKVGREGVISLEEGKSTVTELEITEGMRFEKGFISPYFVTDTERMEVVQENPYILLTDKKITLVqQDL 233

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 311353288 159 LPLLEQIVQAGKKLLIIADDIEGEAMTTLVVNKLRG 194
Cdd:CHL00093 234 LPILEQVTKTKRPLLIIAEDVEKEALATLVLNKLRG 269
groEL PRK12852
chaperonin GroEL; Reviewed
 1-194 1.44e-85

chaperonin GroEL; Reviewed


Pssm-ID: 237232  Cd Length: 545  Bit Score: 262.47  E-value: 1.44e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311353288   1 KEVATKTNDVAGDGTTTATLLAQAIIREGLKNVTAGANPILIRNGIKTAVEKAVEEIQKISKPVNGKEDIARVAAISA-A 79
Cdd:PRK12852  75 REVASKTNDLAGDGTTTATVLAQAIVREGAKAVAAGMNPMDLKRGIDIAVAAVVKDIEKRAKPVASSAEIAQVGTISAnG 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311353288  80 DEKIGKLIADAMEKVGNEGVITVEESKSMGTELDVVEGMQFDRGYVSAYMVTDTEKMEAVLDNPLVLITDKKISNIQDLL 159
Cdd:PRK12852 155 DAAIGKMIAQAMQKVGNEGVITVEENKSLETEVDIVEGMKFDRGYLSPYFVTNAEKMTVELDDAYILLHEKKLSGLQAML 234

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 311353288 160 PLLEQIVQAGKKLLIIADDIEGEAMTTLVVNKLRG 194
Cdd:PRK12852 235 PVLEAVVQSGKPLLIIAEDVEGEALATLVVNRLRG 269
PRK14104 PRK14104
chaperonin GroEL; Provisional
 1-194 1.20e-72

chaperonin GroEL; Provisional


Pssm-ID: 172594  Cd Length: 546  Bit Score: 229.15  E-value: 1.20e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311353288   1 KEVATKTNDVAGDGTTTATLLAQAIIREGLKNVTAGANPILIRNGIKTAVEKAVEEIQKISKPVNGKEDIARVAAISA-A 79
Cdd:PRK14104  75 REVASKSADAAGDGTTTATVLAQAIVREGAKSVAAGMNPMDLKRGIDLAVEAVVADLVKNSKKVTSNDEIAQVGTISAnG 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311353288  80 DEKIGKLIADAMEKVGNEGVITVEESKSMGTELDVVEGMQFDRGYVSAYMVTDTEKMEAVLDNPLVLITDKKISNIQDLL 159
Cdd:PRK14104 155 DAEIGKFLADAMKKVGNEGVITVEEAKSLETELDVVEGMQFDRGYISPYFVTNADKMRVEMDDAYILINEKKLSSLNELL 234

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 311353288 160 PLLEQIVQAGKKLLIIADDIEGEAMTTLVVNKLRG 194
Cdd:PRK14104 235 PLLEAVVQTGKPLVIVAEDVEGEALATLVVNRLRG 269
PLN03167 PLN03167
Chaperonin-60 beta subunit; Provisional
 1-196 2.05e-63

Chaperonin-60 beta subunit; Provisional


Pssm-ID: 215611 [Multi-domain]  Cd Length: 600  Bit Score: 205.93  E-value: 2.05e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311353288   1 KEVATKTNDVAGDGTTTATLLAQAIIREGLKNVTAGANPILIRNGIKTAVEKAVEEIQKISKPVNGKEdIARVAAISAAD 80
Cdd:PLN03167 130 RQAAAKTNDLAGDGTTTSVVLAQGLIAEGVKVVAAGANPVQITRGIEKTAKALVKELKKMSKEVEDSE-LADVAAVSAGN 208

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311353288  81 E-KIGKLIADAMEKVGNEGVITVEESKSMGTELDVVEGMQFDRGYVSAYMVTDTEKMEAVLDNPLVLITDKKISNIQDLL 159
Cdd:PLN03167 209 NyEVGNMIAEAMSKVGRKGVVTLEEGKSAENNLYVVEGMQFDRGYISPYFVTDSEKMSVEYDNCKLLLVDKKITNARDLI 288

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 311353288 160 PLLEQIVQAGKKLLIIADDIEGEAMTTLVVNKLRGTF 196
Cdd:PLN03167 289 GILEDAIRGGYPLLIIAEDIEQEALATLVVNKLRGSL 325
chaperonin_type_I_II cd00309
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ...
 1-192 8.10e-49

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: 164.91  E-value: 8.10e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311353288   1 KEVATKTNDVAGDGTTTATLLAQAIIREGLKNVTAGANPILIRNGIKTAVEKAVEEIQKISKP--VNGKEDIARVAAISA 78
Cdd:cd00309   68 VEVAKSQDDEVGDGTTTVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVPidVEDREELLKVATTSL 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311353288  79 A-------DEKIGKLIADAMEKVG------NEGVITVEESKSmGTELD--VVEGMQFDRGYVSAYmvtdtekMEAVLDNP 143
Cdd:cd00309  148 NsklvsggDDFLGELVVDAVLKVGkengdvDLGVIRVEKKKG-GSLEDseLVVGMVFDKGYLSPY-------MPKRLENA 219

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 311353288 144 LVLITDKKISNiqdllplleqivqagkklLIIADD-IEGEAMTTLVVNKL 192
Cdd:cd00309  220 KILLLDCKLEY------------------VVIAEKgIDDEALHYLAKLGI 251
Cpn60_TCP1 pfam00118
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ...
 2-194 2.50e-28

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: 110.37  E-value: 2.50e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311353288    2 EVATKTNDVAGDGTTTATLLAQAIIREGLKNVTAGANPILIRNGIKTAVEKAVE---EIQKISKPVNGKEDIARVAAISA 78
Cdd:pfam00118  50 EAAKAQDEEVGDGTTTVVVLAGELLEEAEKLLAAGVHPTTIIEGYEKALEKALEildSIISIPVEDVDREDLLKVARTSL 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311353288   79 A-------DEKIGKLIADAME---------KVGNEGVITVEESKSMGTELdvVEGMQFDRGYVSaymvtdtEKMEAVLDN 142
Cdd:pfam00118 130 SskiisreSDFLAKLVVDAVLaipkndgsfDLGNIGVVKILGGSLEDSEL--VDGVVLDKGPLH-------PDMPKRLEN 200

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 311353288  143 PLVLITDKKISNIQD------------------------LLPLLEQIVQAGKKLLIIADDIEGEAMTTLVVNKLRG 194
Cdd:pfam00118 201 AKVLLLNCSLEYEKTetkatvvlsdaeqlerflkaeeeqILEIVEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMA 276
chaperonin_like cd03333
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ...
 67-191 4.09e-16

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: 73.27  E-value: 4.09e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311353288  67 KEDIARVAAISAA------DEKIGKLIADAMEKVG------NEGVITVEESKSmGTELD--VVEGMQFDRGYVSAYmvtd 132
Cdd:cd03333    1 RELLLQVATTSLNsklsswDDFLGKLVVDAVLKVGpdnrmdDLGVIKVEKIPG-GSLEDseLVVGVVFDKGYASPY---- 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 311353288 133 tekMEAVLDNPLVLITDKKISNiqdllplleqivqagkklLIIADD-IEGEAMTTLVVNK 191
Cdd:cd03333   76 ---MPKRLENAKILLLDCPLEY------------------VVIAEKgIDDLALHYLAKAG 114
cpn60 cd03343
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ...
 2-98 1.15e-06

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: 48.03  E-value: 1.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311353288   2 EVATKTNDVAGDGTTTATLLAQAIIREGLKNVTAGANPILIRNGIKTAVEKAVEEIQKISKPVN--GKEDIARVA----- 74
Cdd:cd03343   76 EVAKTQDEEVGDGTTTAVVLAGELLEKAEDLLDQNIHPTVIIEGYRLAAEKALELLDEIAIKVDpdDKDTLRKIAktslt 155

                         90       100
                 ....*....|....*....|....*.
gi 311353288  75 --AISAADEKIGKLIADAMEKVGNEG 98
Cdd:cd03343  156 gkGAEAAKDKLADLVVDAVLQVAEKR 181
chap_CCT_epsi TIGR02343
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ...
 2-117 9.50e-06

T-complex protein 1, epsilon 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 epsilon chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.


Pssm-ID: 274084 [Multi-domain]  Cd Length: 532  Bit Score: 45.18  E-value: 9.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311353288    2 EVATKTNDVAGDGTTTATLLAQAIIREGLKNVTAGANPILIRNGIKTAVEKAVEEIQKISKPV----NGKEDIARvAAIS 77
Cdd:TIGR02343  88 ELSKSQDDEIGDGTTGVVVLAGALLEQAEELLDKGIHPIKIADGFEEAARIAVEHLEEISDEIsadnNNREPLIQ-AAKT 166

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 311353288   78 AADEKIGKLIADAMEKVGNEGVITVE--ESKSMGTELDVVEG 117
Cdd:TIGR02343 167 SLGSKIVSKCHRRFAEIAVDAVLNVAdmERRDVDFDLIKVEG 208
TCP1_eta cd03340
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ...
 12-97 7.12e-05

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: 42.66  E-value: 7.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311353288  12 GDGTTTATLLAQAIIREGLKNVTAGANPILIRNGIKTAVEKAVEEIQKISKPVNGK------EDIARVAA-------ISA 78
Cdd:cd03340   87 GDGTTSVVVLAGEFLKEAKPFIEDGVHPQIIIRGYRKALQLAIEKIKEIAVNIDKEdkeeqrELLEKCAAtalnsklIAS 166

                         90
                 ....*....|....*....
gi 311353288  79 ADEKIGKLIADAMEKVGNE 97
Cdd:cd03340  167 EKEFFAKMVVDAVLSLDDD 185
TCP1_gamma cd03337
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ...
 2-149 7.81e-05

TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma 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: 239453 [Multi-domain]  Cd Length: 480  Bit Score: 42.67  E-value: 7.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311353288   2 EVATKTNDVAGDGTTTATLLAQAIIREGLKNVTAGANPILIRNGIKTAVEKAVEEIQKISKPVNgKEDIARVAAI--SAA 79
Cdd:cd03337   77 ELSRTQDEEVGDGTTSVIILAGEILAVAEPFLERGIHPTVIIKAYRKALEDALKILEEISIPVD-VNDRAQMLKIikSCI 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311353288  80 DEKIGKLIADAMEKVGNEGVITVEESKSMG-TELDVVEGMQFDR---GYVSAYMVTD---------TEKMEAVLDNPLVL 146
Cdd:cd03337  156 GTKFVSRWSDLMCNLALDAVKTVAVEENGRkKEIDIKRYAKVEKipgGEIEDSRVLDgvmlnkdvtHPKMRRRIENPRIV 235


                 ...
gi 311353288 147 ITD 149
Cdd:cd03337  236 LLD 238
TCP1_delta cd03338
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ...
 6-122 1.40e-04

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: 41.89  E-value: 1.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311353288   6 KTNDV-AGDGTTTATLLAQAIIREGLKNVTAGANPILIRNGIKTAVEKAVEEIQKISKPVNGKE-----DIARVA----A 75
Cdd:cd03338   72 KAQDIeAGDGTTSVVVLAGALLSACESLLKKGIHPTVISESFQIAAKKAVEILDSMSIPVDLNDresliKSATTSlnskV 151

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 311353288  76 ISAADEKIGKLIADAMEKVGNEGVITVEESKSM-------GTELD--VVEGMQFDR 122
Cdd:cd03338  152 VSQYSSLLAPIAVDAVLKVIDPATATNVDLKDIrivkklgGTIEDteLVDGLVFTQ 207
TCP1_alpha cd03335
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ...
 12-94 1.41e-04

TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha 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: 239451  Cd Length: 527  Bit Score: 41.89  E-value: 1.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311353288  12 GDGTTTATLLAQAIIREGLKNVTAGANPILIRNGIKTAVEKAVEEIQK-ISKPVN--GKEDIARVAA-------ISAADE 81
Cdd:cd03335   79 GDGTTSVVIIAAELLKRANELVKQKIHPTTIISGYRLACKEAVKYIKEhLSISVDnlGKESLINVAKtsmsskiIGADSD 158

                         90
                 ....*....|...
gi 311353288  82 KIGKLIADAMEKV 94
Cdd:cd03335  159 FFANMVVDAILAV 171
TCP1_epsilon cd03339
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ...
 12-117 1.74e-04

TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon 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: 239455  Cd Length: 526  Bit Score: 41.52  E-value: 1.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311353288  12 GDGTTTATLLAQAIIREGLKNVTAGANPILIRNGIKTAVEKAVEEIQKISKPVN-GKEDIARV--AAISAADEKIGKLIA 88
Cdd:cd03339   94 GDGTTGVVVLAGALLEQAEKLLDRGIHPIRIADGYEQACKIAVEHLEEIADKIEfSPDNKEPLiqTAMTSLGSKIVSRCH 173

                         90       100       110
                 ....*....|....*....|....*....|.
gi 311353288  89 DAMEKVGNEGVITVE--ESKSMGTELDVVEG 117
Cdd:cd03339  174 RQFAEIAVDAVLSVAdlERKDVNFELIKVEG 204
chap_CCT_alpha TIGR02340
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ...
 2-94 6.27e-04

T-complex protein 1, alpha 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: 274081 [Multi-domain]  Cd Length: 536  Bit Score: 39.70  E-value: 6.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311353288    2 EVATKTNDVAGDGTTTATLLAQAIIREGLKNVTAGANPILIRNGIKTAVEKAVEEIQK-ISKPVN--GKEDIARVAAISA 78
Cdd:TIGR02340  73 ELAQLQDREVGDGTTSVVIIAAELLKRADELVKNKIHPTSVISGYRLACKEAVKYIKEnLSVSVDelGREALINVAKTSM 152

                          90       100
                  ....*....|....*....|...
gi 311353288   79 ADEKIG-------KLIADAMEKV 94
Cdd:TIGR02340 153 SSKIIGldsdffsNIVVDAVLAV 175
chap_CCT_zeta TIGR02347
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ...
 3-141 7.73e-04

T-complex protein 1, zeta 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 zeta chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.


Pssm-ID: 274088 [Multi-domain]  Cd Length: 531  Bit Score: 39.72  E-value: 7.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311353288    3 VATKTNDVAGDGTTTATLLAQAIIREGLKNVTAGANPILIRNGIKTAVEKAVEEIQ--KISKPVNGKEDIARVAAISAAD 80
Cdd:TIGR02347  78 AATAQDDITGDGTTSTVLLIGELLKQAERYILEGVHPRIITEGFEIARKEALQFLDkfKVKKEDEVDREFLLNVARTSLR 157

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 311353288   81 EKIGKLIADAMEKVGNEGVITVeesKSMGTELDV--VEGMQFDRGyvsayMVTDTEKMEA-VLD 141
Cdd:TIGR02347 158 TKLPADLADQLTEIVVDAVLAI---KKDGEDIDLfmVEIMEMKHK-----SATDTTLIRGlVLD 213
TCP1_zeta cd03342
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ...
 3-141 1.66e-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: 38.39  E-value: 1.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311353288   3 VATKTNDVAGDGTTTATLLAQAIIREGLKNVTAGANPILIRNGIKTAVEKAVE--EIQKISKPVNGKEDIARVAAISAAD 80
Cdd:cd03342   74 AATAQDDITGDGTTSNVLLIGELLKQAERYIQEGVHPRIITEGFELAKNKALKflESFKVPVEIDTDRELLLSVARTSLR 153

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 311353288  81 EKIGKLIADAMEKVGNEGVITVEESksmGTELDV--VEGMQFDRGyvsayMVTDTEKMEA-VLD 141
Cdd:cd03342  154 TKLHADLADQLTEIVVDAVLAIYKP---DEPIDLhmVEIMQMQHK-----SDSDTKLIRGlVLD 209
PTZ00212 PTZ00212
T-complex protein 1 subunit beta; Provisional
 2-98 2.19e-03

T-complex protein 1 subunit beta; Provisional


Pssm-ID: 185514  Cd Length: 533  Bit Score: 38.09  E-value: 2.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311353288   2 EVATKTNDVAGDGTTTATLLAQAIIREGLKNVTAGANPILIRNGIKTAVEKAVEEIQKIS-----KPVNGKEDIARVAA- 75
Cdd:PTZ00212  88 DISKTQDEEVGDGTTSVVVLAGELLREAEKLLDQKIHPQTIIEGWRMALDVARKALEEIAfdhgsDEEKFKEDLLNIARt 167

                         90       100
                 ....*....|....*....|....*....
gi 311353288  76 ------ISAADEKIGKLIADAMEKVGNEG 98
Cdd:PTZ00212 168 tlssklLTVEKDHFAKLAVDAVLRLKGSG 196
chap_CCT_gamma TIGR02344
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ...
 2-114 2.64e-03

T-complex protein 1, gamma 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 gamma chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.


Pssm-ID: 274085 [Multi-domain]  Cd Length: 524  Bit Score: 37.80  E-value: 2.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311353288    2 EVATKTNDVAGDGTTTATLLAQAIIREGLKNVTAGANPILIRNGIKTAVEKAVEEIQKISKPVNGKEDIARVAAISAAde 81
Cdd:TIGR02344  77 ELSRTQDEEVGDGTTSVIILAGEMLSVAEPFLEQNIHPTVIIRAYRKALDDALSVLEEISIPVDVNDDAAMLKLIQSC-- 154

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 311353288   82 kIG-KLIA---DAMEKVGNEGVITVEESKSMGTELDV 114
Cdd:TIGR02344 155 -IGtKFVSrwsDLMCDLALDAVRTVQRDENGRKEIDI 190
chap_CCT_delta TIGR02342
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ...
 5-83 3.38e-03

T-complex protein 1, delta 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 delta chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.


Pssm-ID: 274083  Cd Length: 517  Bit Score: 37.46  E-value: 3.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311353288    5 TKTNDV-AGDGTTTATLLAQAIIREGLKNVTAGANPILIRNGIKTAVEKAVEEIQKISKPVNGKEDIARV-AAISAADEK 82
Cdd:TIGR02342  72 SKAQDIeAGDGTTSVVILAGALLGACERLLNKGIHPTIISESFQSAADEAIKILDEMSIPVDLSDREQLLkSATTSLSSK 151


                  .
gi 311353288   83 I 83
Cdd:TIGR02342 152 V 152
TCP1_beta cd03336
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ...
 2-98 7.18e-03

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: 36.54  E-value: 7.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311353288   2 EVATKTNDVAGDGTTTATLLAQAIIREGLKNVTAGANPILIRNGIKTAVEKAVEEIQKI-----SKPVNGKEDIARVAA- 75
Cdd:cd03336   76 DISKVQDDEVGDGTTSVTVLAAELLREAEKLVAQKIHPQTIIEGYRMATAAAREALLSSavdhsSDEEAFREDLLNIARt 155

                         90       100
                 ....*....|....*....|....*....
gi 311353288  76 ------ISAADEKIGKLIADAMEKVGNEG 98
Cdd:cd03336  156 tlsskiLTQDKEHFAELAVDAVLRLKGSG 184
 
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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