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Conserved domains on  [gi|2563897125|gb|WLV75449|]
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60 kDa chaperonin, partial [Microbacterium sp.]

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 ...
 1-184 3.17e-100

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: 298.96  E-value: 3.17e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563897125   1 ATVLAQALVKEGLRNVAAGADPISLKKGIEKAVAAISAELLASAKPVESKEQIAATASI-SAADPEIGALIAEAIDKVGK 79
Cdd:PRK00013   91 ATVLAQAIVREGLKNVAAGANPMDLKRGIDKAVEAAVEELKKISKPVEDKEEIAQVATIsANGDEEIGKLIAEAMEKVGK 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563897125  80 EGVVTVEESQTFGTELELTEGMRFDKGYINPYFVTDPERQEAVFEDPYILIANQKISNIKDLLPIVDKVIQEGKELVIIA 159
Cdd:PRK00013  171 EGVITVEESKGFETELEVVEGMQFDRGYLSPYFVTDPEKMEAELENPYILITDKKISNIQDLLPVLEQVAQSGKPLLIIA 250

                         170       180
                  ....*....|....*....|....*
gi 2563897125 160 EDVEGEALATLVLNKIRGIFKSVAV 184
Cdd:PRK00013  251 EDVEGEALATLVVNKLRGTLKVVAV 275
 
Name Accession Description Interval E-value
groEL PRK00013
chaperonin GroEL; Reviewed
 1-184 3.17e-100

chaperonin GroEL; Reviewed


Pssm-ID: 234573  Cd Length: 542  Bit Score: 298.96  E-value: 3.17e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563897125   1 ATVLAQALVKEGLRNVAAGADPISLKKGIEKAVAAISAELLASAKPVESKEQIAATASI-SAADPEIGALIAEAIDKVGK 79
Cdd:PRK00013   91 ATVLAQAIVREGLKNVAAGANPMDLKRGIDKAVEAAVEELKKISKPVEDKEEIAQVATIsANGDEEIGKLIAEAMEKVGK 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563897125  80 EGVVTVEESQTFGTELELTEGMRFDKGYINPYFVTDPERQEAVFEDPYILIANQKISNIKDLLPIVDKVIQEGKELVIIA 159
Cdd:PRK00013  171 EGVITVEESKGFETELEVVEGMQFDRGYLSPYFVTDPEKMEAELENPYILITDKKISNIQDLLPVLEQVAQSGKPLLIIA 250

                         170       180
                  ....*....|....*....|....*
gi 2563897125 160 EDVEGEALATLVLNKIRGIFKSVAV 184
Cdd:PRK00013  251 EDVEGEALATLVVNKLRGTLKVVAV 275
GroEL cd03344
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ...
 1-184 5.68e-89

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: 269.71  E-value: 5.68e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563897125   1 ATVLAQALVKEGLRNVAAGADPISLKKGIEKAVAAISAELLASAKPVESKEQIAATASISA-ADPEIGALIAEAIDKVGK 79
Cdd:cd03344    89 ATVLARAIIKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKPVKTKEEIAQVATISAnGDEEIGELIAEAMEKVGK 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563897125  80 EGVVTVEESQTFGTELELTEGMRFDKGYINPYFVTDPERQEAVFEDPYILIANQKISNIKDLLPIVDKVIQEGKELVIIA 159
Cdd:cd03344   169 DGVITVEEGKTLETELEVVEGMQFDRGYLSPYFVTDPEKMEVELENPYILLTDKKISSIQELLPILELVAKAGRPLLIIA 248

                         170       180
                  ....*....|....*....|....*
gi 2563897125 160 EDVEGEALATLVLNKIRGIFKSVAV 184
Cdd:cd03344   249 EDVEGEALATLVVNKLRGGLKVCAV 273
GroEL TIGR02348
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ...
 1-184 5.01e-87

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: 264.93  E-value: 5.01e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563897125   1 ATVLAQALVKEGLRNVAAGADPISLKKGIEKAVAAISAELLASAKPVESKEQIAATASISA-ADPEIGALIAEAIDKVGK 79
Cdd:TIGR02348  90 ATVLAQAIVKEGLKNVAAGANPIELKRGIEKAVEAVVEELKKLSKPVKGKKEIAQVATISAnNDEEIGSLIAEAMEKVGK 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563897125  80 EGVVTVEESQTFGTELELTEGMRFDKGYINPYFVTDPERQEAVFEDPYILIANQKISNIKDLLPIVDKVIQEGKELVIIA 159
Cdd:TIGR02348 170 DGVITVEESKSLETELEVVEGMQFDRGYISPYFVTDAEKMEVELENPYILITDKKISNIKDLLPLLEKVAQSGKPLLIIA 249

                         170       180
                  ....*....|....*....|....*
gi 2563897125 160 EDVEGEALATLVLNKIRGIFKSVAV 184
Cdd:TIGR02348 250 EDVEGEALATLVVNKLRGTLNVCAV 274
GroEL COG0459
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ...
 1-184 4.66e-86

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


Pssm-ID: 440227  Cd Length: 497  Bit Score: 261.55  E-value: 4.66e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563897125   1 ATVLAQALVKEGLRNVAAGADPISLKKGIEKAVAAISAELLASAKPVESKEQIAA-TASISAADPEIGALIAEAIDKVGK 79
Cdd:COG0459    91 ATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPVDDKEELAQvATISANGDEEIGELIAEAMEKVGK 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563897125  80 EGVVTVEESQTFGTELELTEGMRFDKGYINPYFVTDPERQEAVFEDPYILIANQKISNIKDLLPIVDKVIQEGKELVIIA 159
Cdd:COG0459   171 DGVITVEEGKGLETELEVVEGMQFDKGYLSPYFVTDPEKMPAELENAYILLTDKKISSIQDLLPLLEKVAQSGKPLLIIA 250

                         170       180
                  ....*....|....*....|....*
gi 2563897125 160 EDVEGEALATLVLNKIRGIFKSVAV 184
Cdd:COG0459   251 EDIDGEALATLVVNGIRGVLRVVAV 275
Cpn60_TCP1 pfam00118
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ...
 1-180 1.98e-15

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: 73.01  E-value: 1.98e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563897125   1 ATVLAQALVKEGLRNVAAGADPISLKKGIEKAVAaISAELLASAKPVESKEQIAATAS-----------ISAADPEIGAL 69
Cdd:pfam00118  66 VVVLAGELLEEAEKLLAAGVHPTTIIEGYEKALE-KALEILDSIISIPVEDVDREDLLkvartslsskiISRESDFLAKL 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563897125  70 IAEAI---------DKVGKEGVVTVEESQTFGTELEltEGMRFDKGYINPYFVTDperqeavFEDPYILIANQKISNIKD 140
Cdd:pfam00118 145 VVDAVlaipkndgsFDLGNIGVVKILGGSLEDSELV--DGVVLDKGPLHPDMPKR-------LENAKVLLLNCSLEYEKT 215

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2563897125 141 ------------------------LLPIVDKVIQEGKELVIIAEDVEGEALATLVLNKIRGIFK 180
Cdd:pfam00118 216 etkatvvlsdaeqlerflkaeeeqILEIVEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMALRR 279
 
Name Accession Description Interval E-value
groEL PRK00013
chaperonin GroEL; Reviewed
 1-184 3.17e-100

chaperonin GroEL; Reviewed


Pssm-ID: 234573  Cd Length: 542  Bit Score: 298.96  E-value: 3.17e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563897125   1 ATVLAQALVKEGLRNVAAGADPISLKKGIEKAVAAISAELLASAKPVESKEQIAATASI-SAADPEIGALIAEAIDKVGK 79
Cdd:PRK00013   91 ATVLAQAIVREGLKNVAAGANPMDLKRGIDKAVEAAVEELKKISKPVEDKEEIAQVATIsANGDEEIGKLIAEAMEKVGK 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563897125  80 EGVVTVEESQTFGTELELTEGMRFDKGYINPYFVTDPERQEAVFEDPYILIANQKISNIKDLLPIVDKVIQEGKELVIIA 159
Cdd:PRK00013  171 EGVITVEESKGFETELEVVEGMQFDRGYLSPYFVTDPEKMEAELENPYILITDKKISNIQDLLPVLEQVAQSGKPLLIIA 250

                         170       180
                  ....*....|....*....|....*
gi 2563897125 160 EDVEGEALATLVLNKIRGIFKSVAV 184
Cdd:PRK00013  251 EDVEGEALATLVVNKLRGTLKVVAV 275
groEL PRK12849
chaperonin GroEL; Reviewed
 1-184 5.47e-92

chaperonin GroEL; Reviewed


Pssm-ID: 237230  Cd Length: 542  Bit Score: 277.84  E-value: 5.47e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563897125   1 ATVLAQALVKEGLRNVAAGADPISLKKGIEKAVAAISAELLASAKPVESKEQIAATASISA-ADPEIGALIAEAIDKVGK 79
Cdd:PRK12849   91 ATVLAQALVQEGLKNVAAGANPMDLKRGIDKAVEAVVEELKALARPVSGSEEIAQVATISAnGDEEIGELIAEAMEKVGK 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563897125  80 EGVVTVEESQTFGTELELTEGMRFDKGYINPYFVTDPERQEAVFEDPYILIANQKISNIKDLLPIVDKVIQEGKELVIIA 159
Cdd:PRK12849  171 DGVITVEESKTLETELEVTEGMQFDRGYLSPYFVTDPERMEAVLEDPLILLTDKKISSLQDLLPLLEKVAQSGKPLLIIA 250

                         170       180
                  ....*....|....*....|....*
gi 2563897125 160 EDVEGEALATLVLNKIRGIFKSVAV 184
Cdd:PRK12849  251 EDVEGEALATLVVNKLRGGLKVAAV 275
GroEL cd03344
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ...
 1-184 5.68e-89

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: 269.71  E-value: 5.68e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563897125   1 ATVLAQALVKEGLRNVAAGADPISLKKGIEKAVAAISAELLASAKPVESKEQIAATASISA-ADPEIGALIAEAIDKVGK 79
Cdd:cd03344    89 ATVLARAIIKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKPVKTKEEIAQVATISAnGDEEIGELIAEAMEKVGK 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563897125  80 EGVVTVEESQTFGTELELTEGMRFDKGYINPYFVTDPERQEAVFEDPYILIANQKISNIKDLLPIVDKVIQEGKELVIIA 159
Cdd:cd03344   169 DGVITVEEGKTLETELEVVEGMQFDRGYLSPYFVTDPEKMEVELENPYILLTDKKISSIQELLPILELVAKAGRPLLIIA 248

                         170       180
                  ....*....|....*....|....*
gi 2563897125 160 EDVEGEALATLVLNKIRGIFKSVAV 184
Cdd:cd03344   249 EDVEGEALATLVVNKLRGGLKVCAV 273
GroEL TIGR02348
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ...
 1-184 5.01e-87

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: 264.93  E-value: 5.01e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563897125   1 ATVLAQALVKEGLRNVAAGADPISLKKGIEKAVAAISAELLASAKPVESKEQIAATASISA-ADPEIGALIAEAIDKVGK 79
Cdd:TIGR02348  90 ATVLAQAIVKEGLKNVAAGANPIELKRGIEKAVEAVVEELKKLSKPVKGKKEIAQVATISAnNDEEIGSLIAEAMEKVGK 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563897125  80 EGVVTVEESQTFGTELELTEGMRFDKGYINPYFVTDPERQEAVFEDPYILIANQKISNIKDLLPIVDKVIQEGKELVIIA 159
Cdd:TIGR02348 170 DGVITVEESKSLETELEVVEGMQFDRGYISPYFVTDAEKMEVELENPYILITDKKISNIKDLLPLLEKVAQSGKPLLIIA 249

                         170       180
                  ....*....|....*....|....*
gi 2563897125 160 EDVEGEALATLVLNKIRGIFKSVAV 184
Cdd:TIGR02348 250 EDVEGEALATLVVNKLRGTLNVCAV 274
GroEL COG0459
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ...
 1-184 4.66e-86

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


Pssm-ID: 440227  Cd Length: 497  Bit Score: 261.55  E-value: 4.66e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563897125   1 ATVLAQALVKEGLRNVAAGADPISLKKGIEKAVAAISAELLASAKPVESKEQIAA-TASISAADPEIGALIAEAIDKVGK 79
Cdd:COG0459    91 ATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPVDDKEELAQvATISANGDEEIGELIAEAMEKVGK 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563897125  80 EGVVTVEESQTFGTELELTEGMRFDKGYINPYFVTDPERQEAVFEDPYILIANQKISNIKDLLPIVDKVIQEGKELVIIA 159
Cdd:COG0459   171 DGVITVEEGKGLETELEVVEGMQFDKGYLSPYFVTDPEKMPAELENAYILLTDKKISSIQDLLPLLEKVAQSGKPLLIIA 250

                         170       180
                  ....*....|....*....|....*
gi 2563897125 160 EDVEGEALATLVLNKIRGIFKSVAV 184
Cdd:COG0459   251 EDIDGEALATLVVNGIRGVLRVVAV 275
groEL PRK12850
chaperonin GroEL; Reviewed
 1-184 4.89e-86

chaperonin GroEL; Reviewed


Pssm-ID: 237231  Cd Length: 544  Bit Score: 262.73  E-value: 4.89e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563897125   1 ATVLAQALVKEGLRNVAAGADPISLKKGIEKAVAAISAELLASAKPVESKEQIAATASISAA-DPEIGALIAEAIDKVGK 79
Cdd:PRK12850   92 ATVLAQAIVREGAKLVAAGMNPMDLKRGIDLAVAAVVDELKKIAKKVTSSKEIAQVATISANgDESIGEMIAEAMDKVGK 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563897125  80 EGVVTVEESQTFGTELELTEGMRFDKGYINPYFVTDPERQEAVFEDPYILIANQKISNIKDLLPIVDKVIQEGKELVIIA 159
Cdd:PRK12850  172 EGVITVEEAKTLGTELDVVEGMQFDRGYLSPYFVTNPEKMRAELEDPYILLHEKKISNLQDLLPILEAVVQSGRPLLIIA 251

                         170       180
                  ....*....|....*....|....*
gi 2563897125 160 EDVEGEALATLVLNKIRGIFKSVAV 184
Cdd:PRK12850  252 EDVEGEALATLVVNKLRGGLKSVAV 276
groEL PRK12851
chaperonin GroEL; Reviewed
 1-184 2.21e-81

chaperonin GroEL; Reviewed


Pssm-ID: 171770  Cd Length: 541  Bit Score: 250.81  E-value: 2.21e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563897125   1 ATVLAQALVKEGLRNVAAGADPISLKKGIEKAVAAISAELLASAKPVESKEQIAATASISA-ADPEIGALIAEAIDKVGK 79
Cdd:PRK12851   92 ATVLAQAIVREGAKAVAAGANPMDLKRGIDRAVAAVVEELKANARPVTTNAEIAQVATISAnGDAEIGRLVAEAMEKVGN 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563897125  80 EGVVTVEESQTFGTELELTEGMRFDKGYINPYFVTDPERQEAVFEDPYILIANQKISNIKDLLPIVDKVIQEGKELVIIA 159
Cdd:PRK12851  172 EGVITVEESKTAETELEVVEGMQFDRGYLSPYFVTDADKMEAELEDPYILIHEKKISNLQDLLPVLEAVVQSGKPLLIIA 251

                         170       180
                  ....*....|....*....|....*
gi 2563897125 160 EDVEGEALATLVLNKIRGIFKSVAV 184
Cdd:PRK12851  252 EDVEGEALATLVVNKLRGGLKVAAV 276
groEL CHL00093
chaperonin GroEL
 1-184 4.46e-74

chaperonin GroEL


Pssm-ID: 177025  Cd Length: 529  Bit Score: 231.53  E-value: 4.46e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563897125   1 ATVLAQALVKEGLRNVAAGADPISLKKGIEKAVAAISAELLASAKPVESKEQIAATASISA-ADPEIGALIAEAIDKVGK 79
Cdd:CHL00093   91 ATVLAYAIVKQGMKNVAAGANPISLKRGIEKATQYVVSQIAEYARPVEDIQAITQVASISAgNDEEVGSMIADAIEKVGR 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563897125  80 EGVVTVEESQTFGTELELTEGMRFDKGYINPYFVTDPERQEAVFEDPYILIANQKISNIK-DLLPIVDKVIQEGKELVII 158
Cdd:CHL00093  171 EGVISLEEGKSTVTELEITEGMRFEKGFISPYFVTDTERMEVVQENPYILLTDKKITLVQqDLLPILEQVTKTKRPLLII 250

                         170       180
                  ....*....|....*....|....*.
gi 2563897125 159 AEDVEGEALATLVLNKIRGIFKSVAV 184
Cdd:CHL00093  251 AEDVEKEALATLVLNKLRGIVNVVAV 276
groEL PRK12852
chaperonin GroEL; Reviewed
 1-184 1.51e-66

chaperonin GroEL; Reviewed


Pssm-ID: 237232  Cd Length: 545  Bit Score: 212.40  E-value: 1.51e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563897125   1 ATVLAQALVKEGLRNVAAGADPISLKKGIEKAVAAISAELLASAKPV-ESKEQIAATASISAADPEIGALIAEAIDKVGK 79
Cdd:PRK12852   92 ATVLAQAIVREGAKAVAAGMNPMDLKRGIDIAVAAVVKDIEKRAKPVaSSAEIAQVGTISANGDAAIGKMIAQAMQKVGN 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563897125  80 EGVVTVEESQTFGTELELTEGMRFDKGYINPYFVTDPERQEAVFEDPYILIANQKISNIKDLLPIVDKVIQEGKELVIIA 159
Cdd:PRK12852  172 EGVITVEENKSLETEVDIVEGMKFDRGYLSPYFVTNAEKMTVELDDAYILLHEKKLSGLQAMLPVLEAVVQSGKPLLIIA 251

                         170       180
                  ....*....|....*....|....*
gi 2563897125 160 EDVEGEALATLVLNKIRGIFKSVAV 184
Cdd:PRK12852  252 EDVEGEALATLVVNRLRGGLKVAAV 276
PTZ00114 PTZ00114
Heat shock protein 60; Provisional
 1-184 4.65e-66

Heat shock protein 60; Provisional


Pssm-ID: 185455  Cd Length: 555  Bit Score: 211.31  E-value: 4.65e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563897125   1 ATVLAQALVKEGLRNVAAGADPISLKKGIEKAVAAISAELLASAKPVESKEQIAATASISA-ADPEIGALIAEAIDKVGK 79
Cdd:PTZ00114  103 ATILARAIFREGCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQSRPVKTKEDILNVATISAnGDVEIGSLIADAMDKVGK 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563897125  80 EGVVTVEESQTFGTELELTEGMRFDKGYINPYFVTDPERQEAVFEDPYILIANQKISNIKDLLPIVDKVIQEGKELVIIA 159
Cdd:PTZ00114  183 DGTITVEDGKTLEDELEVVEGMSFDRGYISPYFVTNEKTQKVELENPLILVTDKKISSIQSILPILEHAVKNKRPLLIIA 262

                         170       180
                  ....*....|....*....|....*
gi 2563897125 160 EDVEGEALATLVLNKIRGIFKSVAV 184
Cdd:PTZ00114  263 EDVEGEALQTLIINKLRGGLKVCAV 287
PRK14104 PRK14104
chaperonin GroEL; Provisional
 1-184 3.39e-57

chaperonin GroEL; Provisional


Pssm-ID: 172594  Cd Length: 546  Bit Score: 187.93  E-value: 3.39e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563897125   1 ATVLAQALVKEGLRNVAAGADPISLKKGIEKAVAAISAELLASAKPVESKEQIAATASISAA-DPEIGALIAEAIDKVGK 79
Cdd:PRK14104   92 ATVLAQAIVREGAKSVAAGMNPMDLKRGIDLAVEAVVADLVKNSKKVTSNDEIAQVGTISANgDAEIGKFLADAMKKVGN 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563897125  80 EGVVTVEESQTFGTELELTEGMRFDKGYINPYFVTDPERQEAVFEDPYILIANQKISNIKDLLPIVDKVIQEGKELVIIA 159
Cdd:PRK14104  172 EGVITVEEAKSLETELDVVEGMQFDRGYISPYFVTNADKMRVEMDDAYILINEKKLSSLNELLPLLEAVVQTGKPLVIVA 251

                         170       180
                  ....*....|....*....|....*
gi 2563897125 160 EDVEGEALATLVLNKIRGIFKSVAV 184
Cdd:PRK14104  252 EDVEGEALATLVVNRLRGGLKVAAV 276
PLN03167 PLN03167
Chaperonin-60 beta subunit; Provisional
 1-184 6.48e-50

Chaperonin-60 beta subunit; Provisional


Pssm-ID: 215611 [Multi-domain]  Cd Length: 600  Bit Score: 169.72  E-value: 6.48e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563897125   1 ATVLAQALVKEGLRNVAAGADPISLKKGIEKAVAAISAELLASAKPVESKEQIAATASISAADPEIGALIAEAIDKVGKE 80
Cdd:PLN03167  147 SVVLAQGLIAEGVKVVAAGANPVQITRGIEKTAKALVKELKKMSKEVEDSELADVAAVSAGNNYEVGNMIAEAMSKVGRK 226

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563897125  81 GVVTVEESQTFGTELELTEGMRFDKGYINPYFVTDPERQEAVFEDPYILIANQKISNIKDLLPIVDKVIQEGKELVIIAE 160
Cdd:PLN03167  227 GVVTLEEGKSAENNLYVVEGMQFDRGYISPYFVTDSEKMSVEYDNCKLLLVDKKITNARDLIGILEDAIRGGYPLLIIAE 306

                         170       180
                  ....*....|....*....|....
gi 2563897125 161 DVEGEALATLVLNKIRGIFKSVAV 184
Cdd:PLN03167  307 DIEQEALATLVVNKLRGSLKIAAL 330
chaperonin_type_I_II cd00309
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ...
 1-175 1.46e-29

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: 112.91  E-value: 1.46e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563897125   1 ATVLAQALVKEGLRNVAAGADPISLKKGIEKAVAAISAELLASAKPVESKEQIAAT---------ASISAADPEIGALIA 71
Cdd:cd00309    85 VVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVPIDVEDREELLkvattslnsKLVSGGDDFLGELVV 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563897125  72 EAIDKVGKE------GVVTVEESQTFG-TELELTEGMRFDKGYINPYFvtdperqEAVFEDPYILIANQKIsnikdllpi 144
Cdd:cd00309   165 DAVLKVGKEngdvdlGVIRVEKKKGGSlEDSELVVGMVFDKGYLSPYM-------PKRLENAKILLLDCKL--------- 228

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2563897125 145 vdkviqegkELVIIAED-VEGEALATLVLNKI 175
Cdd:cd00309   229 ---------EYVVIAEKgIDDEALHYLAKLGI 251
Cpn60_TCP1 pfam00118
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ...
 1-180 1.98e-15

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: 73.01  E-value: 1.98e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563897125   1 ATVLAQALVKEGLRNVAAGADPISLKKGIEKAVAaISAELLASAKPVESKEQIAATAS-----------ISAADPEIGAL 69
Cdd:pfam00118  66 VVVLAGELLEEAEKLLAAGVHPTTIIEGYEKALE-KALEILDSIISIPVEDVDREDLLkvartslsskiISRESDFLAKL 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563897125  70 IAEAI---------DKVGKEGVVTVEESQTFGTELEltEGMRFDKGYINPYFVTDperqeavFEDPYILIANQKISNIKD 140
Cdd:pfam00118 145 VVDAVlaipkndgsFDLGNIGVVKILGGSLEDSELV--DGVVLDKGPLHPDMPKR-------LENAKVLLLNCSLEYEKT 215

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2563897125 141 ------------------------LLPIVDKVIQEGKELVIIAEDVEGEALATLVLNKIRGIFK 180
Cdd:pfam00118 216 etkatvvlsdaeqlerflkaeeeqILEIVEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMALRR 279
chaperonin_like cd03333
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ...
 63-175 3.04e-14

chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings, each composed of 7-9 subunits. There are 2 main chaperonin groups. The symmetry of type I is seven-fold and they are found in eubacteria (GroEL) and in organelles of eubacterial descent (hsp60 and RBP). The symmetry of type II is eight- or nine-fold and they are found in archea (thermosome), thermophilic bacteria (TF55) and in the eukaryotic cytosol (CTT). Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. This superfamily also contains related domains from Fab1-like phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinases that only contain the intermediate and apical domains.


Pssm-ID: 239449 [Multi-domain]  Cd Length: 209  Bit Score: 67.88  E-value: 3.04e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563897125  63 DPEIGALIAEAIDKVGKE------GVVTVEESQTFG-TELELTEGMRFDKGYINPYFvtdperqEAVFEDPYILIANQKI 135
Cdd:cd03333    20 DDFLGKLVVDAVLKVGPDnrmddlGVIKVEKIPGGSlEDSELVVGVVFDKGYASPYM-------PKRLENAKILLLDCPL 92

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2563897125 136 snikdllpivdkviqegkELVIIAED-VEGEALATLVLNKI 175
Cdd:cd03333    93 ------------------EYVVIAEKgIDDLALHYLAKAGI 115
 
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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