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Conserved domains on  [gi|671760825|gb|AII99327|]
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GroEL, partial [Lactiplantibacillus plantarum]

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 ...
 1-149 7.56e-90

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: 270.84  E-value: 7.56e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671760825   1 RRGIEEATKTAVDSLHAMAHEVKTQEDIAQIASVSS-ASEETGKLIAEAMEKVGHDGVITIEESRGVDTSLDVVEGMQFD 79
Cdd:PRK00013 116 KRGIDKAVEAAVEELKKISKPVEDKEEIAQVATISAnGDEEIGKLIAEAMEKVGKEGVITVEESKGFETELEVVEGMQFD 195

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671760825  80 RGYLSQYMVTDNDKMEADLDNPYILITDKKISNIQDILPLLQSIVEQGKPLLIIADDISGEALPTLVLNK 149
Cdd:PRK00013 196 RGYLSPYFVTDPEKMEAELENPYILITDKKISNIQDLLPVLEQVAQSGKPLLIIAEDVEGEALATLVVNK 265
 
Name Accession Description Interval E-value
groEL PRK00013
chaperonin GroEL; Reviewed
 1-149 7.56e-90

chaperonin GroEL; Reviewed


Pssm-ID: 234573  Cd Length: 542  Bit Score: 270.84  E-value: 7.56e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671760825   1 RRGIEEATKTAVDSLHAMAHEVKTQEDIAQIASVSS-ASEETGKLIAEAMEKVGHDGVITIEESRGVDTSLDVVEGMQFD 79
Cdd:PRK00013 116 KRGIDKAVEAAVEELKKISKPVEDKEEIAQVATISAnGDEEIGKLIAEAMEKVGKEGVITVEESKGFETELEVVEGMQFD 195

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671760825  80 RGYLSQYMVTDNDKMEADLDNPYILITDKKISNIQDILPLLQSIVEQGKPLLIIADDISGEALPTLVLNK 149
Cdd:PRK00013 196 RGYLSPYFVTDPEKMEAELENPYILITDKKISNIQDLLPVLEQVAQSGKPLLIIAEDVEGEALATLVVNK 265
GroEL cd03344
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ...
 1-149 1.13e-78

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: 241.59  E-value: 1.13e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671760825   1 RRGIEEATKTAVDSLHAMAHEVKTQEDIAQIASVSSAS-EETGKLIAEAMEKVGHDGVITIEESRGVDTSLDVVEGMQFD 79
Cdd:cd03344  114 KRGIEKAVEAVVEELKKLSKPVKTKEEIAQVATISANGdEEIGELIAEAMEKVGKDGVITVEEGKTLETELEVVEGMQFD 193

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671760825  80 RGYLSQYMVTDNDKMEADLDNPYILITDKKISNIQDILPLLQSIVEQGKPLLIIADDISGEALPTLVLNK 149
Cdd:cd03344  194 RGYLSPYFVTDPEKMEVELENPYILLTDKKISSIQELLPILELVAKAGRPLLIIAEDVEGEALATLVVNK 263
GroEL TIGR02348
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ...
 1-149 5.85e-78

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: 239.89  E-value: 5.85e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671760825    1 RRGIEEATKTAVDSLHAMAHEVKTQEDIAQIASVSSAS-EETGKLIAEAMEKVGHDGVITIEESRGVDTSLDVVEGMQFD 79
Cdd:TIGR02348 115 KRGIEKAVEAVVEELKKLSKPVKGKKEIAQVATISANNdEEIGSLIAEAMEKVGKDGVITVEESKSLETELEVVEGMQFD 194

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671760825   80 RGYLSQYMVTDNDKMEADLDNPYILITDKKISNIQDILPLLQSIVEQGKPLLIIADDISGEALPTLVLNK 149
Cdd:TIGR02348 195 RGYISPYFVTDAEKMEVELENPYILITDKKISNIKDLLPLLEKVAQSGKPLLIIAEDVEGEALATLVVNK 264
GroEL COG0459
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ...
 1-149 3.16e-74

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


Pssm-ID: 440227  Cd Length: 497  Bit Score: 229.58  E-value: 3.16e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671760825   1 RRGIEEATKTAVDSLHAMAHEVKTQEDIAQIASVSSAS-EETGKLIAEAMEKVGHDGVITIEESRGVDTSLDVVEGMQFD 79
Cdd:COG0459  116 KRGIDKAVEKAVEELKKIAKPVDDKEELAQVATISANGdEEIGELIAEAMEKVGKDGVITVEEGKGLETELEVVEGMQFD 195

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671760825  80 RGYLSQYMVTDNDKMEADLDNPYILITDKKISNIQDILPLLQSIVEQGKPLLIIADDISGEALPTLVLNK 149
Cdd:COG0459  196 KGYLSPYFVTDPEKMPAELENAYILLTDKKISSIQDLLPLLEKVAQSGKPLLIIAEDIDGEALATLVVNG 265
Cpn60_TCP1 pfam00118
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ...
 1-149 2.34e-14

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: 68.77  E-value: 2.34e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671760825    1 RRGIEEATKTAV---DSLHAMAHEVKTQEDIAQIASVSSAS-------EETGKLIAEAME---------KVGHDGVITIE 61
Cdd:pfam00118  91 IEGYEKALEKALeilDSIISIPVEDVDREDLLKVARTSLSSkiisresDFLAKLVVDAVLaipkndgsfDLGNIGVVKIL 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671760825   62 ESRGVDTSLdvVEGMQFDRGYLSQymvtdndKMEADLDNPYILITDKKISNIQD------------------------IL 117
Cdd:pfam00118 171 GGSLEDSEL--VDGVVLDKGPLHP-------DMPKRLENAKVLLLNCSLEYEKTetkatvvlsdaeqlerflkaeeeqIL 241

                         170       180       190
                  ....*....|....*....|....*....|..
gi 671760825  118 PLLQSIVEQGKPLLIIADDISGEALPTLVLNK 149
Cdd:pfam00118 242 EIVEKIIDSGVNVVVCQKGIDDLALHFLAKNG 273
 
Name Accession Description Interval E-value
groEL PRK00013
chaperonin GroEL; Reviewed
 1-149 7.56e-90

chaperonin GroEL; Reviewed


Pssm-ID: 234573  Cd Length: 542  Bit Score: 270.84  E-value: 7.56e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671760825   1 RRGIEEATKTAVDSLHAMAHEVKTQEDIAQIASVSS-ASEETGKLIAEAMEKVGHDGVITIEESRGVDTSLDVVEGMQFD 79
Cdd:PRK00013 116 KRGIDKAVEAAVEELKKISKPVEDKEEIAQVATISAnGDEEIGKLIAEAMEKVGKEGVITVEESKGFETELEVVEGMQFD 195

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671760825  80 RGYLSQYMVTDNDKMEADLDNPYILITDKKISNIQDILPLLQSIVEQGKPLLIIADDISGEALPTLVLNK 149
Cdd:PRK00013 196 RGYLSPYFVTDPEKMEAELENPYILITDKKISNIQDLLPVLEQVAQSGKPLLIIAEDVEGEALATLVVNK 265
GroEL cd03344
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ...
 1-149 1.13e-78

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: 241.59  E-value: 1.13e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671760825   1 RRGIEEATKTAVDSLHAMAHEVKTQEDIAQIASVSSAS-EETGKLIAEAMEKVGHDGVITIEESRGVDTSLDVVEGMQFD 79
Cdd:cd03344  114 KRGIEKAVEAVVEELKKLSKPVKTKEEIAQVATISANGdEEIGELIAEAMEKVGKDGVITVEEGKTLETELEVVEGMQFD 193

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671760825  80 RGYLSQYMVTDNDKMEADLDNPYILITDKKISNIQDILPLLQSIVEQGKPLLIIADDISGEALPTLVLNK 149
Cdd:cd03344  194 RGYLSPYFVTDPEKMEVELENPYILLTDKKISSIQELLPILELVAKAGRPLLIIAEDVEGEALATLVVNK 263
GroEL TIGR02348
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ...
 1-149 5.85e-78

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: 239.89  E-value: 5.85e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671760825    1 RRGIEEATKTAVDSLHAMAHEVKTQEDIAQIASVSSAS-EETGKLIAEAMEKVGHDGVITIEESRGVDTSLDVVEGMQFD 79
Cdd:TIGR02348 115 KRGIEKAVEAVVEELKKLSKPVKGKKEIAQVATISANNdEEIGSLIAEAMEKVGKDGVITVEESKSLETELEVVEGMQFD 194

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671760825   80 RGYLSQYMVTDNDKMEADLDNPYILITDKKISNIQDILPLLQSIVEQGKPLLIIADDISGEALPTLVLNK 149
Cdd:TIGR02348 195 RGYISPYFVTDAEKMEVELENPYILITDKKISNIKDLLPLLEKVAQSGKPLLIIAEDVEGEALATLVVNK 264
groEL PRK12849
chaperonin GroEL; Reviewed
 1-149 9.98e-76

chaperonin GroEL; Reviewed


Pssm-ID: 237230  Cd Length: 542  Bit Score: 234.70  E-value: 9.98e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671760825   1 RRGIEEATKTAVDSLHAMAHEVKTQEDIAQIASVSSAS-EETGKLIAEAMEKVGHDGVITIEESRGVDTSLDVVEGMQFD 79
Cdd:PRK12849 116 KRGIDKAVEAVVEELKALARPVSGSEEIAQVATISANGdEEIGELIAEAMEKVGKDGVITVEESKTLETELEVTEGMQFD 195

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671760825  80 RGYLSQYMVTDNDKMEADLDNPYILITDKKISNIQDILPLLQSIVEQGKPLLIIADDISGEALPTLVLNK 149
Cdd:PRK12849 196 RGYLSPYFVTDPERMEAVLEDPLILLTDKKISSLQDLLPLLEKVAQSGKPLLIIAEDVEGEALATLVVNK 265
GroEL COG0459
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ...
 1-149 3.16e-74

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


Pssm-ID: 440227  Cd Length: 497  Bit Score: 229.58  E-value: 3.16e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671760825   1 RRGIEEATKTAVDSLHAMAHEVKTQEDIAQIASVSSAS-EETGKLIAEAMEKVGHDGVITIEESRGVDTSLDVVEGMQFD 79
Cdd:COG0459  116 KRGIDKAVEKAVEELKKIAKPVDDKEELAQVATISANGdEEIGELIAEAMEKVGKDGVITVEEGKGLETELEVVEGMQFD 195

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671760825  80 RGYLSQYMVTDNDKMEADLDNPYILITDKKISNIQDILPLLQSIVEQGKPLLIIADDISGEALPTLVLNK 149
Cdd:COG0459  196 KGYLSPYFVTDPEKMPAELENAYILLTDKKISSIQDLLPLLEKVAQSGKPLLIIAEDIDGEALATLVVNG 265
groEL PRK12850
chaperonin GroEL; Reviewed
 1-149 1.62e-69

chaperonin GroEL; Reviewed


Pssm-ID: 237231  Cd Length: 544  Bit Score: 218.43  E-value: 1.62e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671760825   1 RRGIEEATKTAVDSLHAMAHEVKTQEDIAQIASVSSASEET-GKLIAEAMEKVGHDGVITIEESRGVDTSLDVVEGMQFD 79
Cdd:PRK12850 117 KRGIDLAVAAVVDELKKIAKKVTSSKEIAQVATISANGDESiGEMIAEAMDKVGKEGVITVEEAKTLGTELDVVEGMQFD 196

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671760825  80 RGYLSQYMVTDNDKMEADLDNPYILITDKKISNIQDILPLLQSIVEQGKPLLIIADDISGEALPTLVLNK 149
Cdd:PRK12850 197 RGYLSPYFVTNPEKMRAELEDPYILLHEKKISNLQDLLPILEAVVQSGRPLLIIAEDVEGEALATLVVNK 266
groEL PRK12851
chaperonin GroEL; Reviewed
 1-149 4.16e-64

chaperonin GroEL; Reviewed


Pssm-ID: 171770  Cd Length: 541  Bit Score: 204.59  E-value: 4.16e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671760825   1 RRGIEEATKTAVDSLHAMAHEVKTQEDIAQIASVSS-ASEETGKLIAEAMEKVGHDGVITIEESRGVDTSLDVVEGMQFD 79
Cdd:PRK12851 117 KRGIDRAVAAVVEELKANARPVTTNAEIAQVATISAnGDAEIGRLVAEAMEKVGNEGVITVEESKTAETELEVVEGMQFD 196

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671760825  80 RGYLSQYMVTDNDKMEADLDNPYILITDKKISNIQDILPLLQSIVEQGKPLLIIADDISGEALPTLVLNK 149
Cdd:PRK12851 197 RGYLSPYFVTDADKMEAELEDPYILIHEKKISNLQDLLPVLEAVVQSGKPLLIIAEDVEGEALATLVVNK 266
groEL PRK12852
chaperonin GroEL; Reviewed
 1-149 1.02e-58

chaperonin GroEL; Reviewed


Pssm-ID: 237232  Cd Length: 545  Bit Score: 190.44  E-value: 1.02e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671760825   1 RRGIEEATKTAVDSLHAMAHEVKTQEDIAQIASVSS-ASEETGKLIAEAMEKVGHDGVITIEESRGVDTSLDVVEGMQFD 79
Cdd:PRK12852 117 KRGIDIAVAAVVKDIEKRAKPVASSAEIAQVGTISAnGDAAIGKMIAQAMQKVGNEGVITVEENKSLETEVDIVEGMKFD 196

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671760825  80 RGYLSQYMVTDNDKMEADLDNPYILITDKKISNIQDILPLLQSIVEQGKPLLIIADDISGEALPTLVLNK 149
Cdd:PRK12852 197 RGYLSPYFVTNAEKMTVELDDAYILLHEKKLSGLQAMLPVLEAVVQSGKPLLIIAEDVEGEALATLVVNR 266
PTZ00114 PTZ00114
Heat shock protein 60; Provisional
 1-149 3.85e-56

Heat shock protein 60; Provisional


Pssm-ID: 185455  Cd Length: 555  Bit Score: 183.96  E-value: 3.85e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671760825   1 RRGIEEATKTAVDSLHAMAHEVKTQEDIAQIASVS-SASEETGKLIAEAMEKVGHDGVITIEESRGVDTSLDVVEGMQFD 79
Cdd:PTZ00114 128 KRGIDLAVKVVLESLKEQSRPVKTKEDILNVATISaNGDVEIGSLIADAMDKVGKDGTITVEDGKTLEDELEVVEGMSFD 207

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671760825  80 RGYLSQYMVTDNDKMEADLDNPYILITDKKISNIQDILPLLQSIVEQGKPLLIIADDISGEALPTLVLNK 149
Cdd:PTZ00114 208 RGYISPYFVTNEKTQKVELENPLILVTDKKISSIQSILPILEHAVKNKRPLLIIAEDVEGEALQTLIINK 277
groEL CHL00093
chaperonin GroEL
 1-149 2.60e-54

chaperonin GroEL


Pssm-ID: 177025  Cd Length: 529  Bit Score: 178.37  E-value: 2.60e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671760825   1 RRGIEEATKTAVDSLHAMAHEVKTQEDIAQIASVSSAS-EETGKLIAEAMEKVGHDGVITIEESRGVDTSLDVVEGMQFD 79
Cdd:CHL00093 116 KRGIEKATQYVVSQIAEYARPVEDIQAITQVASISAGNdEEVGSMIADAIEKVGREGVISLEEGKSTVTELEITEGMRFE 195

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 671760825  80 RGYLSQYMVTDNDKMEADLDNPYILITDKKISNI-QDILPLLQSIVEQGKPLLIIADDISGEALPTLVLNK 149
Cdd:CHL00093 196 KGFISPYFVTDTERMEVVQENPYILLTDKKITLVqQDLLPILEQVTKTKRPLLIIAEDVEKEALATLVLNK 266
PRK14104 PRK14104
chaperonin GroEL; Provisional
 1-149 1.65e-48

chaperonin GroEL; Provisional


Pssm-ID: 172594  Cd Length: 546  Bit Score: 163.66  E-value: 1.65e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671760825   1 RRGIEEATKTAVDSLHAMAHEVKTQEDIAQIASVSS-ASEETGKLIAEAMEKVGHDGVITIEESRGVDTSLDVVEGMQFD 79
Cdd:PRK14104 117 KRGIDLAVEAVVADLVKNSKKVTSNDEIAQVGTISAnGDAEIGKFLADAMKKVGNEGVITVEEAKSLETELDVVEGMQFD 196

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671760825  80 RGYLSQYMVTDNDKMEADLDNPYILITDKKISNIQDILPLLQSIVEQGKPLLIIADDISGEALPTLVLNK 149
Cdd:PRK14104 197 RGYISPYFVTNADKMRVEMDDAYILINEKKLSSLNELLPLLEAVVQTGKPLVIVAEDVEGEALATLVVNR 266
PLN03167 PLN03167
Chaperonin-60 beta subunit; Provisional
 2-149 1.10e-43

Chaperonin-60 beta subunit; Provisional


Pssm-ID: 215611 [Multi-domain]  Cd Length: 600  Bit Score: 151.23  E-value: 1.10e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671760825   2 RGIEEATKTAVDSLHAMAHEVKTQEdIAQIASVSSASE-ETGKLIAEAMEKVGHDGVITIEESRGVDTSLDVVEGMQFDR 80
Cdd:PLN03167 173 RGIEKTAKALVKELKKMSKEVEDSE-LADVAAVSAGNNyEVGNMIAEAMSKVGRKGVVTLEEGKSAENNLYVVEGMQFDR 251

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 671760825  81 GYLSQYMVTDNDKMEADLDNPYILITDKKISNIQDILPLLQSIVEQGKPLLIIADDISGEALPTLVLNK 149
Cdd:PLN03167 252 GYISPYFVTDSEKMSVEYDNCKLLLVDKKITNARDLIGILEDAIRGGYPLLIIAEDIEQEALATLVVNK 320
chaperonin_type_I_II cd00309
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ...
 1-149 4.32e-25

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: 99.04  E-value: 4.32e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671760825   1 RRGIEEATKTAVDSLHAMA--HEVKTQEDIAQIASVSSAS-------EETGKLIAEAMEKVGHD------GVITIEESRG 65
Cdd:cd00309  110 IRGYEKAVEKALEILKEIAvpIDVEDREELLKVATTSLNSklvsggdDFLGELVVDAVLKVGKEngdvdlGVIRVEKKKG 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671760825  66 ---VDTSLdvVEGMQFDRGYLSQYmvtdndkMEADLDNPYILITDKKISNiqdilpllqsiveqgkplLIIADD-ISGEA 141
Cdd:cd00309  190 gslEDSEL--VVGMVFDKGYLSPY-------MPKRLENAKILLLDCKLEY------------------VVIAEKgIDDEA 242


                 ....*...
gi 671760825 142 LPTLVLNK 149
Cdd:cd00309  243 LHYLAKLG 250
chaperonin_like cd03333
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ...
 26-149 1.57e-16

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


Pssm-ID: 239449 [Multi-domain]  Cd Length: 209  Bit Score: 72.88  E-value: 1.57e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671760825  26 EDIAQIASVSSAS------EETGKLIAEAMEKVGHD------GVITIEESRG---VDTSLdvVEGMQFDRGYLSQYmvtd 90
Cdd:cd03333    2 ELLLQVATTSLNSklsswdDFLGKLVVDAVLKVGPDnrmddlGVIKVEKIPGgslEDSEL--VVGVVFDKGYASPY---- 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 671760825  91 ndkMEADLDNPYILITDKKISNiqdilpllqsiveqgkplLIIADD-ISGEALPTLVLNK 149
Cdd:cd03333   76 ---MPKRLENAKILLLDCPLEY------------------VVIAEKgIDDLALHYLAKAG 114
Cpn60_TCP1 pfam00118
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ...
 1-149 2.34e-14

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: 68.77  E-value: 2.34e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671760825    1 RRGIEEATKTAV---DSLHAMAHEVKTQEDIAQIASVSSAS-------EETGKLIAEAME---------KVGHDGVITIE 61
Cdd:pfam00118  91 IEGYEKALEKALeilDSIISIPVEDVDREDLLKVARTSLSSkiisresDFLAKLVVDAVLaipkndgsfDLGNIGVVKIL 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671760825   62 ESRGVDTSLdvVEGMQFDRGYLSQymvtdndKMEADLDNPYILITDKKISNIQD------------------------IL 117
Cdd:pfam00118 171 GGSLEDSEL--VDGVVLDKGPLHP-------DMPKRLENAKVLLLNCSLEYEKTetkatvvlsdaeqlerflkaeeeqIL 241

                         170       180       190
                  ....*....|....*....|....*....|..
gi 671760825  118 PLLQSIVEQGKPLLIIADDISGEALPTLVLNK 149
Cdd:pfam00118 242 EIVEKIIDSGVNVVVCQKGIDDLALHFLAKNG 273
 
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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