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Conserved domains on  [gi|77997928|gb|ABB16402|]
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heat-shock protein 60 kDa, partial [Pasteurella multocida]

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 ...
 1-198 1.93e-133

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: 384.48  E-value: 1.93e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77997928    1 GDGTTTATVLAQAIVNEGLKAVAAGMNPMDLKRGIDKAVTAVVTELKALSKPCETSKEIEQVGTISANSDSIVGQIIAQA 80
Cdd:PRK00013  85 GDGTTTATVLAQAIVREGLKNVAAGANPMDLKRGIDKAVEAAVEELKKISKPVEDKEEIAQVATISANGDEEIGKLIAEA 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77997928   81 MDKVGKEGVITVEDGTGLEDELAVVEGMQFDRGYLSPYFINKPETATVELDNPFILLVDKKVSNIRELLPVLEGVAKAGK 160
Cdd:PRK00013 165 MEKVGKEGVITVEESKGFETELEVVEGMQFDRGYLSPYFVTDPEKMEAELENPYILITDKKISNIQDLLPVLEQVAQSGK 244

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 77997928  161 PLLIIAEDVEGEALATLVVNTMRGIVKVAAVKAPGFGD 198
Cdd:PRK00013 245 PLLIIAEDVEGEALATLVVNKLRGTLKVVAVKAPGFGD 282
 
Name Accession Description Interval E-value
groEL PRK00013
chaperonin GroEL; Reviewed
 1-198 1.93e-133

chaperonin GroEL; Reviewed


Pssm-ID: 234573  Cd Length: 542  Bit Score: 384.48  E-value: 1.93e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77997928    1 GDGTTTATVLAQAIVNEGLKAVAAGMNPMDLKRGIDKAVTAVVTELKALSKPCETSKEIEQVGTISANSDSIVGQIIAQA 80
Cdd:PRK00013  85 GDGTTTATVLAQAIVREGLKNVAAGANPMDLKRGIDKAVEAAVEELKKISKPVEDKEEIAQVATISANGDEEIGKLIAEA 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77997928   81 MDKVGKEGVITVEDGTGLEDELAVVEGMQFDRGYLSPYFINKPETATVELDNPFILLVDKKVSNIRELLPVLEGVAKAGK 160
Cdd:PRK00013 165 MEKVGKEGVITVEESKGFETELEVVEGMQFDRGYLSPYFVTDPEKMEAELENPYILITDKKISNIQDLLPVLEQVAQSGK 244

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 77997928  161 PLLIIAEDVEGEALATLVVNTMRGIVKVAAVKAPGFGD 198
Cdd:PRK00013 245 PLLIIAEDVEGEALATLVVNKLRGTLKVVAVKAPGFGD 282
GroEL cd03344
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ...
 1-198 1.47e-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: 353.68  E-value: 1.47e-121
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77997928   1 GDGTTTATVLAQAIVNEGLKAVAAGMNPMDLKRGIDKAVTAVVTELKALSKPCETSKEIEQVGTISANSDSIVGQIIAQA 80
Cdd:cd03344  83 GDGTTTATVLARAIIKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKPVKTKEEIAQVATISANGDEEIGELIAEA 162

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77997928  81 MDKVGKEGVITVEDGTGLEDELAVVEGMQFDRGYLSPYFINKPETATVELDNPFILLVDKKVSNIRELLPVLEGVAKAGK 160
Cdd:cd03344 163 MEKVGKDGVITVEEGKTLETELEVVEGMQFDRGYLSPYFVTDPEKMEVELENPYILLTDKKISSIQELLPILELVAKAGR 242

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 77997928 161 PLLIIAEDVEGEALATLVVNTMRGIVKVAAVKAPGFGD 198
Cdd:cd03344 243 PLLIIAEDVEGEALATLVVNKLRGGLKVCAVKAPGFGD 280
GroEL TIGR02348
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ...
 1-198 5.82e-116

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: 339.27  E-value: 5.82e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77997928     1 GDGTTTATVLAQAIVNEGLKAVAAGMNPMDLKRGIDKAVTAVVTELKALSKPCETSKEIEQVGTISANSDSIVGQIIAQA 80
Cdd:TIGR02348  84 GDGTTTATVLAQAIVKEGLKNVAAGANPIELKRGIEKAVEAVVEELKKLSKPVKGKKEIAQVATISANNDEEIGSLIAEA 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77997928    81 MDKVGKEGVITVEDGTGLEDELAVVEGMQFDRGYLSPYFINKPETATVELDNPFILLVDKKVSNIRELLPVLEGVAKAGK 160
Cdd:TIGR02348 164 MEKVGKDGVITVEESKSLETELEVVEGMQFDRGYISPYFVTDAEKMEVELENPYILITDKKISNIKDLLPLLEKVAQSGK 243

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 77997928   161 PLLIIAEDVEGEALATLVVNTMRGIVKVAAVKAPGFGD 198
Cdd:TIGR02348 244 PLLIIAEDVEGEALATLVVNKLRGTLNVCAVKAPGFGD 281
GroEL COG0459
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ...
 1-198 6.60e-110

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


Pssm-ID: 440227  Cd Length: 497  Bit Score: 323.18  E-value: 6.60e-110
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77997928   1 GDGTTTATVLAQAIVNEGLKAVAAGMNPMDLKRGIDKAVTAVVTELKALSKPCETSKEIEQVGTISANSDSIVGQIIAQA 80
Cdd:COG0459  85 GDGTTTATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPVDDKEELAQVATISANGDEEIGELIAEA 164

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77997928  81 MDKVGKEGVITVEDGTGLEDELAVVEGMQFDRGYLSPYFINKPETATVELDNPFILLVDKKVSNIRELLPVLEGVAKAGK 160
Cdd:COG0459 165 MEKVGKDGVITVEEGKGLETELEVVEGMQFDKGYLSPYFVTDPEKMPAELENAYILLTDKKISSIQDLLPLLEKVAQSGK 244

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 77997928 161 PLLIIAEDVEGEALATLVVNTMRGIVKVAAVKAPGFGD 198
Cdd:COG0459 245 PLLIIAEDIDGEALATLVVNGIRGVLRVVAVKAPGFGD 282
Cpn60_TCP1 pfam00118
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ...
 1-188 3.20e-19

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: 84.56  E-value: 3.20e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77997928     1 GDGTTTATVLAQAIVNEGLKAVAAGMNPMDLKRGIDKAVTAVV---TELKALSKPCETSKEIEQVGTISANSDSI----- 72
Cdd:pfam00118  60 GDGTTTVVVLAGELLEEAEKLLAAGVHPTTIIEGYEKALEKALeilDSIISIPVEDVDREDLLKVARTSLSSKIIsresd 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77997928    73 -VGQIIAQA---------MDKVGKEGVITVEdGTGLEDeLAVVEGMQFDRGYLSPyfinkpeTATVELDNPFILLVDKKV 142
Cdd:pfam00118 140 fLAKLVVDAvlaipkndgSFDLGNIGVVKIL-GGSLED-SELVDGVVLDKGPLHP-------DMPKRLENAKVLLLNCSL 210

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77997928   143 SNIRE------------------------LLPVLEGVAKAGKPLLIIAEDVEGEALATLVVNTMRGIVKV 188
Cdd:pfam00118 211 EYEKTetkatvvlsdaeqlerflkaeeeqILEIVEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMALRRV 280
 
Name Accession Description Interval E-value
groEL PRK00013
chaperonin GroEL; Reviewed
 1-198 1.93e-133

chaperonin GroEL; Reviewed


Pssm-ID: 234573  Cd Length: 542  Bit Score: 384.48  E-value: 1.93e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77997928    1 GDGTTTATVLAQAIVNEGLKAVAAGMNPMDLKRGIDKAVTAVVTELKALSKPCETSKEIEQVGTISANSDSIVGQIIAQA 80
Cdd:PRK00013  85 GDGTTTATVLAQAIVREGLKNVAAGANPMDLKRGIDKAVEAAVEELKKISKPVEDKEEIAQVATISANGDEEIGKLIAEA 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77997928   81 MDKVGKEGVITVEDGTGLEDELAVVEGMQFDRGYLSPYFINKPETATVELDNPFILLVDKKVSNIRELLPVLEGVAKAGK 160
Cdd:PRK00013 165 MEKVGKEGVITVEESKGFETELEVVEGMQFDRGYLSPYFVTDPEKMEAELENPYILITDKKISNIQDLLPVLEQVAQSGK 244

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 77997928  161 PLLIIAEDVEGEALATLVVNTMRGIVKVAAVKAPGFGD 198
Cdd:PRK00013 245 PLLIIAEDVEGEALATLVVNKLRGTLKVVAVKAPGFGD 282
GroEL cd03344
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ...
 1-198 1.47e-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: 353.68  E-value: 1.47e-121
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77997928   1 GDGTTTATVLAQAIVNEGLKAVAAGMNPMDLKRGIDKAVTAVVTELKALSKPCETSKEIEQVGTISANSDSIVGQIIAQA 80
Cdd:cd03344  83 GDGTTTATVLARAIIKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKPVKTKEEIAQVATISANGDEEIGELIAEA 162

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77997928  81 MDKVGKEGVITVEDGTGLEDELAVVEGMQFDRGYLSPYFINKPETATVELDNPFILLVDKKVSNIRELLPVLEGVAKAGK 160
Cdd:cd03344 163 MEKVGKDGVITVEEGKTLETELEVVEGMQFDRGYLSPYFVTDPEKMEVELENPYILLTDKKISSIQELLPILELVAKAGR 242

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 77997928 161 PLLIIAEDVEGEALATLVVNTMRGIVKVAAVKAPGFGD 198
Cdd:cd03344 243 PLLIIAEDVEGEALATLVVNKLRGGLKVCAVKAPGFGD 280
groEL PRK12849
chaperonin GroEL; Reviewed
 1-198 7.09e-119

chaperonin GroEL; Reviewed


Pssm-ID: 237230  Cd Length: 542  Bit Score: 347.56  E-value: 7.09e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77997928    1 GDGTTTATVLAQAIVNEGLKAVAAGMNPMDLKRGIDKAVTAVVTELKALSKPCETSKEIEQVGTISANSDSIVGQIIAQA 80
Cdd:PRK12849  85 GDGTTTATVLAQALVQEGLKNVAAGANPMDLKRGIDKAVEAVVEELKALARPVSGSEEIAQVATISANGDEEIGELIAEA 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77997928   81 MDKVGKEGVITVEDGTGLEDELAVVEGMQFDRGYLSPYFINKPETATVELDNPFILLVDKKVSNIRELLPVLEGVAKAGK 160
Cdd:PRK12849 165 MEKVGKDGVITVEESKTLETELEVTEGMQFDRGYLSPYFVTDPERMEAVLEDPLILLTDKKISSLQDLLPLLEKVAQSGK 244

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 77997928  161 PLLIIAEDVEGEALATLVVNTMRGIVKVAAVKAPGFGD 198
Cdd:PRK12849 245 PLLIIAEDVEGEALATLVVNKLRGGLKVAAVKAPGFGD 282
GroEL TIGR02348
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ...
 1-198 5.82e-116

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: 339.27  E-value: 5.82e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77997928     1 GDGTTTATVLAQAIVNEGLKAVAAGMNPMDLKRGIDKAVTAVVTELKALSKPCETSKEIEQVGTISANSDSIVGQIIAQA 80
Cdd:TIGR02348  84 GDGTTTATVLAQAIVKEGLKNVAAGANPIELKRGIEKAVEAVVEELKKLSKPVKGKKEIAQVATISANNDEEIGSLIAEA 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77997928    81 MDKVGKEGVITVEDGTGLEDELAVVEGMQFDRGYLSPYFINKPETATVELDNPFILLVDKKVSNIRELLPVLEGVAKAGK 160
Cdd:TIGR02348 164 MEKVGKDGVITVEESKSLETELEVVEGMQFDRGYISPYFVTDAEKMEVELENPYILITDKKISNIKDLLPLLEKVAQSGK 243

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 77997928   161 PLLIIAEDVEGEALATLVVNTMRGIVKVAAVKAPGFGD 198
Cdd:TIGR02348 244 PLLIIAEDVEGEALATLVVNKLRGTLNVCAVKAPGFGD 281
groEL PRK12850
chaperonin GroEL; Reviewed
 1-198 1.50e-110

chaperonin GroEL; Reviewed


Pssm-ID: 237231  Cd Length: 544  Bit Score: 326.29  E-value: 1.50e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77997928    1 GDGTTTATVLAQAIVNEGLKAVAAGMNPMDLKRGIDKAVTAVVTELKALSKPCETSKEIEQVGTISANSDSIVGQIIAQA 80
Cdd:PRK12850  86 GDGTTTATVLAQAIVREGAKLVAAGMNPMDLKRGIDLAVAAVVDELKKIAKKVTSSKEIAQVATISANGDESIGEMIAEA 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77997928   81 MDKVGKEGVITVEDGTGLEDELAVVEGMQFDRGYLSPYFINKPETATVELDNPFILLVDKKVSNIRELLPVLEGVAKAGK 160
Cdd:PRK12850 166 MDKVGKEGVITVEEAKTLGTELDVVEGMQFDRGYLSPYFVTNPEKMRAELEDPYILLHEKKISNLQDLLPILEAVVQSGR 245

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 77997928  161 PLLIIAEDVEGEALATLVVNTMRGIVKVAAVKAPGFGD 198
Cdd:PRK12850 246 PLLIIAEDVEGEALATLVVNKLRGGLKSVAVKAPGFGD 283
GroEL COG0459
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ...
 1-198 6.60e-110

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


Pssm-ID: 440227  Cd Length: 497  Bit Score: 323.18  E-value: 6.60e-110
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77997928   1 GDGTTTATVLAQAIVNEGLKAVAAGMNPMDLKRGIDKAVTAVVTELKALSKPCETSKEIEQVGTISANSDSIVGQIIAQA 80
Cdd:COG0459  85 GDGTTTATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPVDDKEELAQVATISANGDEEIGELIAEA 164

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77997928  81 MDKVGKEGVITVEDGTGLEDELAVVEGMQFDRGYLSPYFINKPETATVELDNPFILLVDKKVSNIRELLPVLEGVAKAGK 160
Cdd:COG0459 165 MEKVGKDGVITVEEGKGLETELEVVEGMQFDKGYLSPYFVTDPEKMPAELENAYILLTDKKISSIQDLLPLLEKVAQSGK 244

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 77997928 161 PLLIIAEDVEGEALATLVVNTMRGIVKVAAVKAPGFGD 198
Cdd:COG0459 245 PLLIIAEDIDGEALATLVVNGIRGVLRVVAVKAPGFGD 282
groEL PRK12852
chaperonin GroEL; Reviewed
 1-198 3.03e-104

chaperonin GroEL; Reviewed


Pssm-ID: 237232  Cd Length: 545  Bit Score: 310.24  E-value: 3.03e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77997928    1 GDGTTTATVLAQAIVNEGLKAVAAGMNPMDLKRGIDKAVTAVVTELKALSKPCETSKEIEQVGTISANSDSIVGQIIAQA 80
Cdd:PRK12852  86 GDGTTTATVLAQAIVREGAKAVAAGMNPMDLKRGIDIAVAAVVKDIEKRAKPVASSAEIAQVGTISANGDAAIGKMIAQA 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77997928   81 MDKVGKEGVITVEDGTGLEDELAVVEGMQFDRGYLSPYFINKPETATVELDNPFILLVDKKVSNIRELLPVLEGVAKAGK 160
Cdd:PRK12852 166 MQKVGNEGVITVEENKSLETEVDIVEGMKFDRGYLSPYFVTNAEKMTVELDDAYILLHEKKLSGLQAMLPVLEAVVQSGK 245

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 77997928  161 PLLIIAEDVEGEALATLVVNTMRGIVKVAAVKAPGFGD 198
Cdd:PRK12852 246 PLLIIAEDVEGEALATLVVNRLRGGLKVAAVKAPGFGD 283
PTZ00114 PTZ00114
Heat shock protein 60; Provisional
 1-198 1.02e-102

Heat shock protein 60; Provisional


Pssm-ID: 185455  Cd Length: 555  Bit Score: 306.45  E-value: 1.02e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77997928    1 GDGTTTATVLAQAIVNEGLKAVAAGMNPMDLKRGIDKAVTAVVTELKALSKPCETSKEIEQVGTISANSDSIVGQIIAQA 80
Cdd:PTZ00114  97 GDGTTTATILARAIFREGCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQSRPVKTKEDILNVATISANGDVEIGSLIADA 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77997928   81 MDKVGKEGVITVEDGTGLEDELAVVEGMQFDRGYLSPYFINKPETATVELDNPFILLVDKKVSNIRELLPVLEGVAKAGK 160
Cdd:PTZ00114 177 MDKVGKDGTITVEDGKTLEDELEVVEGMSFDRGYISPYFVTNEKTQKVELENPLILVTDKKISSIQSILPILEHAVKNKR 256

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 77997928  161 PLLIIAEDVEGEALATLVVNTMRGIVKVAAVKAPGFGD 198
Cdd:PTZ00114 257 PLLIIAEDVEGEALQTLIINKLRGGLKVCAVKAPGFGD 294
groEL PRK12851
chaperonin GroEL; Reviewed
 1-198 1.91e-101

chaperonin GroEL; Reviewed


Pssm-ID: 171770  Cd Length: 541  Bit Score: 302.82  E-value: 1.91e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77997928    1 GDGTTTATVLAQAIVNEGLKAVAAGMNPMDLKRGIDKAVTAVVTELKALSKPCETSKEIEQVGTISANSDSIVGQIIAQA 80
Cdd:PRK12851  86 GDGTTTATVLAQAIVREGAKAVAAGANPMDLKRGIDRAVAAVVEELKANARPVTTNAEIAQVATISANGDAEIGRLVAEA 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77997928   81 MDKVGKEGVITVEDGTGLEDELAVVEGMQFDRGYLSPYFINKPETATVELDNPFILLVDKKVSNIRELLPVLEGVAKAGK 160
Cdd:PRK12851 166 MEKVGNEGVITVEESKTAETELEVVEGMQFDRGYLSPYFVTDADKMEAELEDPYILIHEKKISNLQDLLPVLEAVVQSGK 245

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 77997928  161 PLLIIAEDVEGEALATLVVNTMRGIVKVAAVKAPGFGD 198
Cdd:PRK12851 246 PLLIIAEDVEGEALATLVVNKLRGGLKVAAVKAPGFGD 283
groEL CHL00093
chaperonin GroEL
 1-198 1.05e-92

chaperonin GroEL


Pssm-ID: 177025  Cd Length: 529  Bit Score: 280.07  E-value: 1.05e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77997928    1 GDGTTTATVLAQAIVNEGLKAVAAGMNPMDLKRGIDKAVTAVVTELKALSKPCETSKEIEQVGTISANSDSIVGQIIAQA 80
Cdd:CHL00093  85 GDGTTTATVLAYAIVKQGMKNVAAGANPISLKRGIEKATQYVVSQIAEYARPVEDIQAITQVASISAGNDEEVGSMIADA 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77997928   81 MDKVGKEGVITVEDGTGLEDELAVVEGMQFDRGYLSPYFINKPETATVELDNPFILLVDKKVSNIR-ELLPVLEGVAKAG 159
Cdd:CHL00093 165 IEKVGREGVISLEEGKSTVTELEITEGMRFEKGFISPYFVTDTERMEVVQENPYILLTDKKITLVQqDLLPILEQVTKTK 244

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 77997928  160 KPLLIIAEDVEGEALATLVVNTMRGIVKVAAVKAPGFGD 198
Cdd:CHL00093 245 RPLLIIAEDVEKEALATLVLNKLRGIVNVVAVRAPGFGD 283
PRK14104 PRK14104
chaperonin GroEL; Provisional
 1-198 3.15e-83

chaperonin GroEL; Provisional


Pssm-ID: 172594  Cd Length: 546  Bit Score: 256.50  E-value: 3.15e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77997928    1 GDGTTTATVLAQAIVNEGLKAVAAGMNPMDLKRGIDKAVTAVVTELKALSKPCETSKEIEQVGTISANSDSIVGQIIAQA 80
Cdd:PRK14104  86 GDGTTTATVLAQAIVREGAKSVAAGMNPMDLKRGIDLAVEAVVADLVKNSKKVTSNDEIAQVGTISANGDAEIGKFLADA 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77997928   81 MDKVGKEGVITVEDGTGLEDELAVVEGMQFDRGYLSPYFINKPETATVELDNPFILLVDKKVSNIRELLPVLEGVAKAGK 160
Cdd:PRK14104 166 MKKVGNEGVITVEEAKSLETELDVVEGMQFDRGYISPYFVTNADKMRVEMDDAYILINEKKLSSLNELLPLLEAVVQTGK 245

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 77997928  161 PLLIIAEDVEGEALATLVVNTMRGIVKVAAVKAPGFGD 198
Cdd:PRK14104 246 PLVIVAEDVEGEALATLVVNRLRGGLKVAAVKAPGFGD 283
PLN03167 PLN03167
Chaperonin-60 beta subunit; Provisional
 1-198 3.41e-72

Chaperonin-60 beta subunit; Provisional


Pssm-ID: 215611 [Multi-domain]  Cd Length: 600  Bit Score: 229.04  E-value: 3.41e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77997928    1 GDGTTTATVLAQAIVNEGLKAVAAGMNPMDLKRGIDKAVTAVVTELKALSKPCETSkEIEQVGTISANSDSIVGQIIAQA 80
Cdd:PLN03167 141 GDGTTTSVVLAQGLIAEGVKVVAAGANPVQITRGIEKTAKALVKELKKMSKEVEDS-ELADVAAVSAGNNYEVGNMIAEA 219

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77997928   81 MDKVGKEGVITVEDGTGLEDELAVVEGMQFDRGYLSPYFINKPETATVELDNPFILLVDKKVSNIRELLPVLEGVAKAGK 160
Cdd:PLN03167 220 MSKVGRKGVVTLEEGKSAENNLYVVEGMQFDRGYISPYFVTDSEKMSVEYDNCKLLLVDKKITNARDLIGILEDAIRGGY 299

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 77997928  161 PLLIIAEDVEGEALATLVVNTMRGIVKVAAVKAPGFGD 198
Cdd:PLN03167 300 PLLIIAEDIEQEALATLVVNKLRGSLKIAALKAPGFGE 337
chaperonin_type_I_II cd00309
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ...
 1-198 4.26e-45

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: 154.89  E-value: 4.26e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77997928   1 GDGTTTATVLAQAIVNEGLKAVAAGMNPMDLKRGIDKAVTAVVTELKALSKP--CETSKEIEQVGTISANS------DSI 72
Cdd:cd00309  79 GDGTTTVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVPidVEDREELLKVATTSLNSklvsggDDF 158

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77997928  73 VGQIIAQAMDKVGKE------GVITVEDGTG---LEDELavVEGMQFDRGYLSPYFinkpetaTVELDNPFILLVDKKVS 143
Cdd:cd00309 159 LGELVVDAVLKVGKEngdvdlGVIRVEKKKGgslEDSEL--VVGMVFDKGYLSPYM-------PKRLENAKILLLDCKLE 229

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 77997928 144 NirellpvlegvakagkplLIIAED-VEGEALATLVVNtmrgivKVAAVKAPGFGD 198
Cdd:cd00309 230 Y------------------VVIAEKgIDDEALHYLAKL------GIMAVRRVRKED 261
Cpn60_TCP1 pfam00118
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ...
 1-188 3.20e-19

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: 84.56  E-value: 3.20e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77997928     1 GDGTTTATVLAQAIVNEGLKAVAAGMNPMDLKRGIDKAVTAVV---TELKALSKPCETSKEIEQVGTISANSDSI----- 72
Cdd:pfam00118  60 GDGTTTVVVLAGELLEEAEKLLAAGVHPTTIIEGYEKALEKALeilDSIISIPVEDVDREDLLKVARTSLSSKIIsresd 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77997928    73 -VGQIIAQA---------MDKVGKEGVITVEdGTGLEDeLAVVEGMQFDRGYLSPyfinkpeTATVELDNPFILLVDKKV 142
Cdd:pfam00118 140 fLAKLVVDAvlaipkndgSFDLGNIGVVKIL-GGSLED-SELVDGVVLDKGPLHP-------DMPKRLENAKVLLLNCSL 210

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77997928   143 SNIRE------------------------LLPVLEGVAKAGKPLLIIAEDVEGEALATLVVNTMRGIVKV 188
Cdd:pfam00118 211 EYEKTetkatvvlsdaeqlerflkaeeeqILEIVEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMALRRV 280
chaperonin_like cd03333
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ...
 57-193 2.24e-18

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: 79.05  E-value: 2.24e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77997928  57 KEIEQVGTISANS-----DSIVGQIIAQAMDKVGKE------GVITVEDGTG---LEDELavVEGMQFDRGYLSPYFink 122
Cdd:cd03333   2 ELLLQVATTSLNSklsswDDFLGKLVVDAVLKVGPDnrmddlGVIKVEKIPGgslEDSEL--VVGVVFDKGYASPYM--- 76

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 77997928 123 petaTVELDNPFILLVDKKVSNirellpvlegvakagkplLIIAED-VEGEALATLVVNtmrgivKVAAVKA 193
Cdd:cd03333  77 ----PKRLENAKILLLDCPLEY------------------VVIAEKgIDDLALHYLAKA------GIMAVRR 120
TCP1_eta cd03340
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ...
 1-61 5.98e-03

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: 36.88  E-value: 5.98e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 77997928   1 GDGTTTATVLAQAIVNEGLKAVAAGMNPMDLKRGIDKAVTAVVTELKALSKPCETSKEIEQ 61
Cdd:cd03340  87 GDGTTSVVVLAGEFLKEAKPFIEDGVHPQIIIRGYRKALQLAIEKIKEIAVNIDKEDKEEQ 147
TCP1_delta cd03338
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ...
 1-112 8.07e-03

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: 36.50  E-value: 8.07e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77997928   1 GDGTTTATVLAQAIVNEGLKAVAAGMNPMDLKRGIDKAVTAVVTELKALSKPCETSKE---IEQVGT------ISANSDS 71
Cdd:cd03338  79 GDGTTSVVVLAGALLSACESLLKKGIHPTVISESFQIAAKKAVEILDSMSIPVDLNDReslIKSATTslnskvVSQYSSL 158

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 77997928  72 IVgQIIAQAMDKVGKEGVITVED-----------GTGLEDELavVEGMQFDR 112
Cdd:cd03338 159 LA-PIAVDAVLKVIDPATATNVDlkdirivkklgGTIEDTEL--VDGLVFTQ 207
chap_CCT_epsi TIGR02343
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ...
 1-94 8.45e-03

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: 36.32  E-value: 8.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77997928     1 GDGTTTATVLAQAIVNEGLKAVAAGMNPMDLKRGIDKAVTAVVTELKALSKPCETSKEIEQVgTISANSDSIVGQIIAQA 80
Cdd:TIGR02343  98 GDGTTGVVVLAGALLEQAEELLDKGIHPIKIADGFEEAARIAVEHLEEISDEISADNNNREP-LIQAAKTSLGSKIVSKC 176

                          90
                  ....*....|....*..
gi 77997928    81 MDKVGK---EGVITVED 94
Cdd:TIGR02343 177 HRRFAEiavDAVLNVAD 193
 
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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