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Conserved domains on  [gi|33313014|gb|AAQ04160|]
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60 kDa heat shock protein, partial [Lacticaseibacillus rhamnosus]

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 2.10e-119

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: 348.27  E-value: 2.10e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33313014    1 ATVLAQSIIREGMKNVTAGANPVGIRTGIEKATKAAVDELHKISHKVNGKKEIAQVASVSSSN-EEVGNLIADAMEKVGH 79
Cdd:PRK00013  91 ATVLAQAIVREGLKNVAAGANPMDLKRGIDKAVEAAVEELKKISKPVEDKEEIAQVATISANGdEEIGKLIAEAMEKVGK 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33313014   80 DGVITIEESKGIDTELSVVEGMQFDRGYLSQYMVTDNDKMEADLDDPYILITDKKISNIQDILPLLQEIVQQGKALLIIA 159
Cdd:PRK00013 171 EGVITVEESKGFETELEVVEGMQFDRGYLSPYFVTDPEKMEAELENPYILITDKKISNIQDLLPVLEQVAQSGKPLLIIA 250

                        170       180
                 ....*....|....*....|....*
gi 33313014  160 DDVAGEALPTLVLNKIRGTFNVVAV 184
Cdd:PRK00013 251 EDVEGEALATLVVNKLRGTLKVVAV 275
 
Name Accession Description Interval E-value
groEL PRK00013
chaperonin GroEL; Reviewed
 1-184 2.10e-119

chaperonin GroEL; Reviewed


Pssm-ID: 234573  Cd Length: 542  Bit Score: 348.27  E-value: 2.10e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33313014    1 ATVLAQSIIREGMKNVTAGANPVGIRTGIEKATKAAVDELHKISHKVNGKKEIAQVASVSSSN-EEVGNLIADAMEKVGH 79
Cdd:PRK00013  91 ATVLAQAIVREGLKNVAAGANPMDLKRGIDKAVEAAVEELKKISKPVEDKEEIAQVATISANGdEEIGKLIAEAMEKVGK 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33313014   80 DGVITIEESKGIDTELSVVEGMQFDRGYLSQYMVTDNDKMEADLDDPYILITDKKISNIQDILPLLQEIVQQGKALLIIA 159
Cdd:PRK00013 171 EGVITVEESKGFETELEVVEGMQFDRGYLSPYFVTDPEKMEAELENPYILITDKKISNIQDLLPVLEQVAQSGKPLLIIA 250

                        170       180
                 ....*....|....*....|....*
gi 33313014  160 DDVAGEALPTLVLNKIRGTFNVVAV 184
Cdd:PRK00013 251 EDVEGEALATLVVNKLRGTLKVVAV 275
GroEL TIGR02348
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ...
 1-184 5.35e-103

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: 305.76  E-value: 5.35e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33313014     1 ATVLAQSIIREGMKNVTAGANPVGIRTGIEKATKAAVDELHKISHKVNGKKEIAQVASVSSSN-EEVGNLIADAMEKVGH 79
Cdd:TIGR02348  90 ATVLAQAIVKEGLKNVAAGANPIELKRGIEKAVEAVVEELKKLSKPVKGKKEIAQVATISANNdEEIGSLIAEAMEKVGK 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33313014    80 DGVITIEESKGIDTELSVVEGMQFDRGYLSQYMVTDNDKMEADLDDPYILITDKKISNIQDILPLLQEIVQQGKALLIIA 159
Cdd:TIGR02348 170 DGVITVEESKSLETELEVVEGMQFDRGYISPYFVTDAEKMEVELENPYILITDKKISNIKDLLPLLEKVAQSGKPLLIIA 249

                         170       180
                  ....*....|....*....|....*
gi 33313014   160 DDVAGEALPTLVLNKIRGTFNVVAV 184
Cdd:TIGR02348 250 EDVEGEALATLVVNKLRGTLNVCAV 274
GroEL cd03344
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ...
 1-184 7.51e-102

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: 302.45  E-value: 7.51e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33313014   1 ATVLAQSIIREGMKNVTAGANPVGIRTGIEKATKAAVDELHKISHKVNGKKEIAQVASVSSSN-EEVGNLIADAMEKVGH 79
Cdd:cd03344  89 ATVLARAIIKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKPVKTKEEIAQVATISANGdEEIGELIAEAMEKVGK 168

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33313014  80 DGVITIEESKGIDTELSVVEGMQFDRGYLSQYMVTDNDKMEADLDDPYILITDKKISNIQDILPLLQEIVQQGKALLIIA 159
Cdd:cd03344 169 DGVITVEEGKTLETELEVVEGMQFDRGYLSPYFVTDPEKMEVELENPYILLTDKKISSIQELLPILELVAKAGRPLLIIA 248

                       170       180
                ....*....|....*....|....*
gi 33313014 160 DDVAGEALPTLVLNKIRGTFNVVAV 184
Cdd:cd03344 249 EDVEGEALATLVVNKLRGGLKVCAV 273
GroEL COG0459
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ...
 1-184 4.61e-98

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


Pssm-ID: 440227  Cd Length: 497  Bit Score: 292.37  E-value: 4.61e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33313014   1 ATVLAQSIIREGMKNVTAGANPVGIRTGIEKATKAAVDELHKISHKVNGKKEIAQVASVSSSN-EEVGNLIADAMEKVGH 79
Cdd:COG0459  91 ATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPVDDKEELAQVATISANGdEEIGELIAEAMEKVGK 170

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33313014  80 DGVITIEESKGIDTELSVVEGMQFDRGYLSQYMVTDNDKMEADLDDPYILITDKKISNIQDILPLLQEIVQQGKALLIIA 159
Cdd:COG0459 171 DGVITVEEGKGLETELEVVEGMQFDKGYLSPYFVTDPEKMPAELENAYILLTDKKISSIQDLLPLLEKVAQSGKPLLIIA 250

                       170       180
                ....*....|....*....|....*
gi 33313014 160 DDVAGEALPTLVLNKIRGTFNVVAV 184
Cdd:COG0459 251 EDIDGEALATLVVNGIRGVLRVVAV 275
Cpn60_TCP1 pfam00118
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ...
 1-181 1.23e-21

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: 90.72  E-value: 1.23e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33313014     1 ATVLAQSIIREGMKNVTAGANPVGIRTGIEKATKAAVDEL---HKISHKVNGKKEIAQVASVSSSN-------EEVGNLI 70
Cdd:pfam00118  66 VVVLAGELLEEAEKLLAAGVHPTTIIEGYEKALEKALEILdsiISIPVEDVDREDLLKVARTSLSSkiisresDFLAKLV 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33313014    71 ADAME---------KVGHDGVITIEESKGIDTELsvVEGMQFDRGYLSQymvtdndKMEADLDDPYILITDKKISNIQD- 140
Cdd:pfam00118 146 VDAVLaipkndgsfDLGNIGVVKILGGSLEDSEL--VDGVVLDKGPLHP-------DMPKRLENAKVLLLNCSLEYEKTe 216

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 33313014   141 -----------------------ILPLLQEIVQQGKALLIIADDVAGEALPTLVLNKIRGTFNV 181
Cdd:pfam00118 217 tkatvvlsdaeqlerflkaeeeqILEIVEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMALRRV 280
 
Name Accession Description Interval E-value
groEL PRK00013
chaperonin GroEL; Reviewed
 1-184 2.10e-119

chaperonin GroEL; Reviewed


Pssm-ID: 234573  Cd Length: 542  Bit Score: 348.27  E-value: 2.10e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33313014    1 ATVLAQSIIREGMKNVTAGANPVGIRTGIEKATKAAVDELHKISHKVNGKKEIAQVASVSSSN-EEVGNLIADAMEKVGH 79
Cdd:PRK00013  91 ATVLAQAIVREGLKNVAAGANPMDLKRGIDKAVEAAVEELKKISKPVEDKEEIAQVATISANGdEEIGKLIAEAMEKVGK 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33313014   80 DGVITIEESKGIDTELSVVEGMQFDRGYLSQYMVTDNDKMEADLDDPYILITDKKISNIQDILPLLQEIVQQGKALLIIA 159
Cdd:PRK00013 171 EGVITVEESKGFETELEVVEGMQFDRGYLSPYFVTDPEKMEAELENPYILITDKKISNIQDLLPVLEQVAQSGKPLLIIA 250

                        170       180
                 ....*....|....*....|....*
gi 33313014  160 DDVAGEALPTLVLNKIRGTFNVVAV 184
Cdd:PRK00013 251 EDVEGEALATLVVNKLRGTLKVVAV 275
GroEL TIGR02348
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ...
 1-184 5.35e-103

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: 305.76  E-value: 5.35e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33313014     1 ATVLAQSIIREGMKNVTAGANPVGIRTGIEKATKAAVDELHKISHKVNGKKEIAQVASVSSSN-EEVGNLIADAMEKVGH 79
Cdd:TIGR02348  90 ATVLAQAIVKEGLKNVAAGANPIELKRGIEKAVEAVVEELKKLSKPVKGKKEIAQVATISANNdEEIGSLIAEAMEKVGK 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33313014    80 DGVITIEESKGIDTELSVVEGMQFDRGYLSQYMVTDNDKMEADLDDPYILITDKKISNIQDILPLLQEIVQQGKALLIIA 159
Cdd:TIGR02348 170 DGVITVEESKSLETELEVVEGMQFDRGYISPYFVTDAEKMEVELENPYILITDKKISNIKDLLPLLEKVAQSGKPLLIIA 249

                         170       180
                  ....*....|....*....|....*
gi 33313014   160 DDVAGEALPTLVLNKIRGTFNVVAV 184
Cdd:TIGR02348 250 EDVEGEALATLVVNKLRGTLNVCAV 274
GroEL cd03344
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ...
 1-184 7.51e-102

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: 302.45  E-value: 7.51e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33313014   1 ATVLAQSIIREGMKNVTAGANPVGIRTGIEKATKAAVDELHKISHKVNGKKEIAQVASVSSSN-EEVGNLIADAMEKVGH 79
Cdd:cd03344  89 ATVLARAIIKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKPVKTKEEIAQVATISANGdEEIGELIAEAMEKVGK 168

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33313014  80 DGVITIEESKGIDTELSVVEGMQFDRGYLSQYMVTDNDKMEADLDDPYILITDKKISNIQDILPLLQEIVQQGKALLIIA 159
Cdd:cd03344 169 DGVITVEEGKTLETELEVVEGMQFDRGYLSPYFVTDPEKMEVELENPYILLTDKKISSIQELLPILELVAKAGRPLLIIA 248

                       170       180
                ....*....|....*....|....*
gi 33313014 160 DDVAGEALPTLVLNKIRGTFNVVAV 184
Cdd:cd03344 249 EDVEGEALATLVVNKLRGGLKVCAV 273
groEL PRK12849
chaperonin GroEL; Reviewed
 1-184 1.30e-99

chaperonin GroEL; Reviewed


Pssm-ID: 237230  Cd Length: 542  Bit Score: 297.49  E-value: 1.30e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33313014    1 ATVLAQSIIREGMKNVTAGANPVGIRTGIEKATKAAVDELHKISHKVNGKKEIAQVASVSSSN-EEVGNLIADAMEKVGH 79
Cdd:PRK12849  91 ATVLAQALVQEGLKNVAAGANPMDLKRGIDKAVEAVVEELKALARPVSGSEEIAQVATISANGdEEIGELIAEAMEKVGK 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33313014   80 DGVITIEESKGIDTELSVVEGMQFDRGYLSQYMVTDNDKMEADLDDPYILITDKKISNIQDILPLLQEIVQQGKALLIIA 159
Cdd:PRK12849 171 DGVITVEESKTLETELEVTEGMQFDRGYLSPYFVTDPERMEAVLEDPLILLTDKKISSLQDLLPLLEKVAQSGKPLLIIA 250

                        170       180
                 ....*....|....*....|....*
gi 33313014  160 DDVAGEALPTLVLNKIRGTFNVVAV 184
Cdd:PRK12849 251 EDVEGEALATLVVNKLRGGLKVAAV 275
GroEL COG0459
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ...
 1-184 4.61e-98

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


Pssm-ID: 440227  Cd Length: 497  Bit Score: 292.37  E-value: 4.61e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33313014   1 ATVLAQSIIREGMKNVTAGANPVGIRTGIEKATKAAVDELHKISHKVNGKKEIAQVASVSSSN-EEVGNLIADAMEKVGH 79
Cdd:COG0459  91 ATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPVDDKEELAQVATISANGdEEIGELIAEAMEKVGK 170

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33313014  80 DGVITIEESKGIDTELSVVEGMQFDRGYLSQYMVTDNDKMEADLDDPYILITDKKISNIQDILPLLQEIVQQGKALLIIA 159
Cdd:COG0459 171 DGVITVEEGKGLETELEVVEGMQFDKGYLSPYFVTDPEKMPAELENAYILLTDKKISSIQDLLPLLEKVAQSGKPLLIIA 250

                       170       180
                ....*....|....*....|....*
gi 33313014 160 DDVAGEALPTLVLNKIRGTFNVVAV 184
Cdd:COG0459 251 EDIDGEALATLVVNGIRGVLRVVAV 275
groEL PRK12850
chaperonin GroEL; Reviewed
 1-184 2.01e-89

chaperonin GroEL; Reviewed


Pssm-ID: 237231  Cd Length: 544  Bit Score: 271.59  E-value: 2.01e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33313014    1 ATVLAQSIIREGMKNVTAGANPVGIRTGIEKATKAAVDELHKISHKVNGKKEIAQVASVSSSNEE-VGNLIADAMEKVGH 79
Cdd:PRK12850  92 ATVLAQAIVREGAKLVAAGMNPMDLKRGIDLAVAAVVDELKKIAKKVTSSKEIAQVATISANGDEsIGEMIAEAMDKVGK 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33313014   80 DGVITIEESKGIDTELSVVEGMQFDRGYLSQYMVTDNDKMEADLDDPYILITDKKISNIQDILPLLQEIVQQGKALLIIA 159
Cdd:PRK12850 172 EGVITVEEAKTLGTELDVVEGMQFDRGYLSPYFVTNPEKMRAELEDPYILLHEKKISNLQDLLPILEAVVQSGRPLLIIA 251

                        170       180
                 ....*....|....*....|....*
gi 33313014  160 DDVAGEALPTLVLNKIRGTFNVVAV 184
Cdd:PRK12850 252 EDVEGEALATLVVNKLRGGLKSVAV 276
groEL PRK12851
chaperonin GroEL; Reviewed
 1-184 3.23e-86

chaperonin GroEL; Reviewed


Pssm-ID: 171770  Cd Length: 541  Bit Score: 263.14  E-value: 3.23e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33313014    1 ATVLAQSIIREGMKNVTAGANPVGIRTGIEKATKAAVDELHKISHKVNGKKEIAQVASVSSSN-EEVGNLIADAMEKVGH 79
Cdd:PRK12851  92 ATVLAQAIVREGAKAVAAGANPMDLKRGIDRAVAAVVEELKANARPVTTNAEIAQVATISANGdAEIGRLVAEAMEKVGN 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33313014   80 DGVITIEESKGIDTELSVVEGMQFDRGYLSQYMVTDNDKMEADLDDPYILITDKKISNIQDILPLLQEIVQQGKALLIIA 159
Cdd:PRK12851 172 EGVITVEESKTAETELEVVEGMQFDRGYLSPYFVTDADKMEAELEDPYILIHEKKISNLQDLLPVLEAVVQSGKPLLIIA 251

                        170       180
                 ....*....|....*....|....*
gi 33313014  160 DDVAGEALPTLVLNKIRGTFNVVAV 184
Cdd:PRK12851 252 EDVEGEALATLVVNKLRGGLKVAAV 276
groEL CHL00093
chaperonin GroEL
 1-184 4.28e-77

chaperonin GroEL


Pssm-ID: 177025  Cd Length: 529  Bit Score: 239.24  E-value: 4.28e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33313014    1 ATVLAQSIIREGMKNVTAGANPVGIRTGIEKATKAAVDELHKISHKVNGKKEIAQVASVSSSN-EEVGNLIADAMEKVGH 79
Cdd:CHL00093  91 ATVLAYAIVKQGMKNVAAGANPISLKRGIEKATQYVVSQIAEYARPVEDIQAITQVASISAGNdEEVGSMIADAIEKVGR 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33313014   80 DGVITIEESKGIDTELSVVEGMQFDRGYLSQYMVTDNDKMEADLDDPYILITDKKISNI-QDILPLLQEIVQQGKALLII 158
Cdd:CHL00093 171 EGVISLEEGKSTVTELEITEGMRFEKGFISPYFVTDTERMEVVQENPYILLTDKKITLVqQDLLPILEQVTKTKRPLLII 250

                        170       180
                 ....*....|....*....|....*.
gi 33313014  159 ADDVAGEALPTLVLNKIRGTFNVVAV 184
Cdd:CHL00093 251 AEDVEKEALATLVLNKLRGIVNVVAV 276
groEL PRK12852
chaperonin GroEL; Reviewed
 1-184 7.23e-75

chaperonin GroEL; Reviewed


Pssm-ID: 237232  Cd Length: 545  Bit Score: 233.97  E-value: 7.23e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33313014    1 ATVLAQSIIREGMKNVTAGANPVGIRTGIEKATKAAVDELHKISHKVNGKKEIAQVASVSSS-NEEVGNLIADAMEKVGH 79
Cdd:PRK12852  92 ATVLAQAIVREGAKAVAAGMNPMDLKRGIDIAVAAVVKDIEKRAKPVASSAEIAQVGTISANgDAAIGKMIAQAMQKVGN 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33313014   80 DGVITIEESKGIDTELSVVEGMQFDRGYLSQYMVTDNDKMEADLDDPYILITDKKISNIQDILPLLQEIVQQGKALLIIA 159
Cdd:PRK12852 172 EGVITVEENKSLETEVDIVEGMKFDRGYLSPYFVTNAEKMTVELDDAYILLHEKKLSGLQAMLPVLEAVVQSGKPLLIIA 251

                        170       180
                 ....*....|....*....|....*
gi 33313014  160 DDVAGEALPTLVLNKIRGTFNVVAV 184
Cdd:PRK12852 252 EDVEGEALATLVVNRLRGGLKVAAV 276
PTZ00114 PTZ00114
Heat shock protein 60; Provisional
 1-184 8.57e-72

Heat shock protein 60; Provisional


Pssm-ID: 185455  Cd Length: 555  Bit Score: 226.33  E-value: 8.57e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33313014    1 ATVLAQSIIREGMKNVTAGANPVGIRTGIEKATKAAVDELHKISHKVNGKKEIAQVASVSSSN-EEVGNLIADAMEKVGH 79
Cdd:PTZ00114 103 ATILARAIFREGCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQSRPVKTKEDILNVATISANGdVEIGSLIADAMDKVGK 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33313014   80 DGVITIEESKGIDTELSVVEGMQFDRGYLSQYMVTDNDKMEADLDDPYILITDKKISNIQDILPLLQEIVQQGKALLIIA 159
Cdd:PTZ00114 183 DGTITVEDGKTLEDELEVVEGMSFDRGYISPYFVTNEKTQKVELENPLILVTDKKISSIQSILPILEHAVKNKRPLLIIA 262

                        170       180
                 ....*....|....*....|....*
gi 33313014  160 DDVAGEALPTLVLNKIRGTFNVVAV 184
Cdd:PTZ00114 263 EDVEGEALQTLIINKLRGGLKVCAV 287
PRK14104 PRK14104
chaperonin GroEL; Provisional
 1-184 1.50e-64

chaperonin GroEL; Provisional


Pssm-ID: 172594  Cd Length: 546  Bit Score: 207.19  E-value: 1.50e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33313014    1 ATVLAQSIIREGMKNVTAGANPVGIRTGIEKATKAAVDELHKISHKVNGKKEIAQVASVSSS-NEEVGNLIADAMEKVGH 79
Cdd:PRK14104  92 ATVLAQAIVREGAKSVAAGMNPMDLKRGIDLAVEAVVADLVKNSKKVTSNDEIAQVGTISANgDAEIGKFLADAMKKVGN 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33313014   80 DGVITIEESKGIDTELSVVEGMQFDRGYLSQYMVTDNDKMEADLDDPYILITDKKISNIQDILPLLQEIVQQGKALLIIA 159
Cdd:PRK14104 172 EGVITVEEAKSLETELDVVEGMQFDRGYISPYFVTNADKMRVEMDDAYILINEKKLSSLNELLPLLEAVVQTGKPLVIVA 251

                        170       180
                 ....*....|....*....|....*
gi 33313014  160 DDVAGEALPTLVLNKIRGTFNVVAV 184
Cdd:PRK14104 252 EDVEGEALATLVVNRLRGGLKVAAV 276
PLN03167 PLN03167
Chaperonin-60 beta subunit; Provisional
 1-184 6.11e-57

Chaperonin-60 beta subunit; Provisional


Pssm-ID: 215611 [Multi-domain]  Cd Length: 600  Bit Score: 188.21  E-value: 6.11e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33313014    1 ATVLAQSIIREGMKNVTAGANPVGIRTGIEKATKAAVDELHKISHKVNgKKEIAQVASVSS-SNEEVGNLIADAMEKVGH 79
Cdd:PLN03167 147 SVVLAQGLIAEGVKVVAAGANPVQITRGIEKTAKALVKELKKMSKEVE-DSELADVAAVSAgNNYEVGNMIAEAMSKVGR 225

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33313014   80 DGVITIEESKGIDTELSVVEGMQFDRGYLSQYMVTDNDKMEADLDDPYILITDKKISNIQDILPLLQEIVQQGKALLIIA 159
Cdd:PLN03167 226 KGVVTLEEGKSAENNLYVVEGMQFDRGYISPYFVTDSEKMSVEYDNCKLLLVDKKITNARDLIGILEDAIRGGYPLLIIA 305

                        170       180
                 ....*....|....*....|....*
gi 33313014  160 DDVAGEALPTLVLNKIRGTFNVVAV 184
Cdd:PLN03167 306 EDIEQEALATLVVNKLRGSLKIAAL 330
chaperonin_type_I_II cd00309
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ...
 1-175 7.73e-37

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: 132.55  E-value: 7.73e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33313014   1 ATVLAQSIIREGMKNVTAGANPVGIRTGIEKATKAAVDELHKIS--HKVNGKKEIAQVASVSSS-------NEEVGNLIA 71
Cdd:cd00309  85 VVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAvpIDVEDREELLKVATTSLNsklvsggDDFLGELVV 164

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33313014  72 DAMEKVGHD------GVITIEESKG---IDTELsvVEGMQFDRGYLSQYmvtdndkMEADLDDPYILITDKKISNiqdil 142
Cdd:cd00309 165 DAVLKVGKEngdvdlGVIRVEKKKGgslEDSEL--VVGMVFDKGYLSPY-------MPKRLENAKILLLDCKLEY----- 230

                       170       180       190
                ....*....|....*....|....*....|....
gi 33313014 143 pllqeivqqgkalLIIADD-VAGEALPTLVLNKI 175
Cdd:cd00309 231 -------------VVIAEKgIDDEALHYLAKLGI 251
Cpn60_TCP1 pfam00118
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ...
 1-181 1.23e-21

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: 90.72  E-value: 1.23e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33313014     1 ATVLAQSIIREGMKNVTAGANPVGIRTGIEKATKAAVDEL---HKISHKVNGKKEIAQVASVSSSN-------EEVGNLI 70
Cdd:pfam00118  66 VVVLAGELLEEAEKLLAAGVHPTTIIEGYEKALEKALEILdsiISIPVEDVDREDLLKVARTSLSSkiisresDFLAKLV 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33313014    71 ADAME---------KVGHDGVITIEESKGIDTELsvVEGMQFDRGYLSQymvtdndKMEADLDDPYILITDKKISNIQD- 140
Cdd:pfam00118 146 VDAVLaipkndgsfDLGNIGVVKILGGSLEDSEL--VDGVVLDKGPLHP-------DMPKRLENAKVLLLNCSLEYEKTe 216

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 33313014   141 -----------------------ILPLLQEIVQQGKALLIIADDVAGEALPTLVLNKIRGTFNV 181
Cdd:pfam00118 217 tkatvvlsdaeqlerflkaeeeqILEIVEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMALRRV 280
chaperonin_like cd03333
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ...
 50-175 4.08e-17

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: 75.20  E-value: 4.08e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33313014  50 KKEIAQVASVSSS------NEEVGNLIADAMEKVGHD------GVITIEESKG---IDTELsvVEGMQFDRGYLSQYmvt 114
Cdd:cd03333   1 RELLLQVATTSLNsklsswDDFLGKLVVDAVLKVGPDnrmddlGVIKVEKIPGgslEDSEL--VVGVVFDKGYASPY--- 75

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 33313014 115 dndkMEADLDDPYILITDKKISNiqdilpllqeivqqgkalLIIADD-VAGEALPTLVLNKI 175
Cdd:cd03333  76 ----MPKRLENAKILLLDCPLEY------------------VVIAEKgIDDLALHYLAKAGI 115
TCP1_epsilon cd03339
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ...
 3-100 2.36e-03

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: 37.66  E-value: 2.36e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33313014   3 VLAQSIIREGMKNVTAGANPVGIRTGIEKATKAAVDELHKISHKV----NGKKEIAQVASVSSSNEEVgNLIADAMEKVG 78
Cdd:cd03339 102 VLAGALLEQAEKLLDRGIHPIRIADGYEQACKIAVEHLEEIADKIefspDNKEPLIQTAMTSLGSKIV-SRCHRQFAEIA 180

                        90       100
                ....*....|....*....|....
gi 33313014  79 HDGVITIE--ESKGIDTELSVVEG 100
Cdd:cd03339 181 VDAVLSVAdlERKDVNFELIKVEG 204
 
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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