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Conserved domains on  [gi|340547694|gb|AEK52015|]
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chaperonin GroL, partial [Aeromonas sp. Ae44(2011)]

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 ...
 1-170 2.10e-109

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: 322.07  E-value: 2.10e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547694   1 DKAVVAAVAELQALSQPCADSNAIAQVGTISANSDEKVGKLIAEAMDKVGRDGVITVEDGQGLDDELAVVEGMQFDRGYL 80
Cdd:PRK00013 120 DKAVEAAVEELKKISKPVEDKEEIAQVATISANGDEEIGKLIAEAMEKVGKEGVITVEESKGFETELEVVEGMQFDRGYL 199

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547694  81 SPYFINKQETGSVELDDPFILLVDKKVSNIREMLPVLEGVAKAGKPLLIVAEDVEGEALATLVVNTMRGIVKVAAVKAPG 160
Cdd:PRK00013 200 SPYFVTDPEKMEAELENPYILITDKKISNIQDLLPVLEQVAQSGKPLLIIAEDVEGEALATLVVNKLRGTLKVVAVKAPG 279

                        170
                 ....*....|
gi 340547694 161 FGDRRKAMLQ 170
Cdd:PRK00013 280 FGDRRKAMLE 289
 
Name Accession Description Interval E-value
groEL PRK00013
chaperonin GroEL; Reviewed
 1-170 2.10e-109

chaperonin GroEL; Reviewed


Pssm-ID: 234573  Cd Length: 542  Bit Score: 322.07  E-value: 2.10e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547694   1 DKAVVAAVAELQALSQPCADSNAIAQVGTISANSDEKVGKLIAEAMDKVGRDGVITVEDGQGLDDELAVVEGMQFDRGYL 80
Cdd:PRK00013 120 DKAVEAAVEELKKISKPVEDKEEIAQVATISANGDEEIGKLIAEAMEKVGKEGVITVEESKGFETELEVVEGMQFDRGYL 199

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547694  81 SPYFINKQETGSVELDDPFILLVDKKVSNIREMLPVLEGVAKAGKPLLIVAEDVEGEALATLVVNTMRGIVKVAAVKAPG 160
Cdd:PRK00013 200 SPYFVTDPEKMEAELENPYILITDKKISNIQDLLPVLEQVAQSGKPLLIIAEDVEGEALATLVVNKLRGTLKVVAVKAPG 279

                        170
                 ....*....|
gi 340547694 161 FGDRRKAMLQ 170
Cdd:PRK00013 280 FGDRRKAMLE 289
GroEL cd03344
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ...
 1-170 1.95e-98

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: 293.21  E-value: 1.95e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547694   1 DKAVVAAVAELQALSQPCADSNAIAQVGTISANSDEKVGKLIAEAMDKVGRDGVITVEDGQGLDDELAVVEGMQFDRGYL 80
Cdd:cd03344  118 EKAVEAVVEELKKLSKPVKTKEEIAQVATISANGDEEIGELIAEAMEKVGKDGVITVEEGKTLETELEVVEGMQFDRGYL 197

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547694  81 SPYFINKQETGSVELDDPFILLVDKKVSNIREMLPVLEGVAKAGKPLLIVAEDVEGEALATLVVNTMRGIVKVAAVKAPG 160
Cdd:cd03344  198 SPYFVTDPEKMEVELENPYILLTDKKISSIQELLPILELVAKAGRPLLIIAEDVEGEALATLVVNKLRGGLKVCAVKAPG 277

                        170
                 ....*....|
gi 340547694 161 FGDRRKAMLQ 170
Cdd:cd03344  278 FGDRRKAMLE 287
GroEL TIGR02348
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ...
 1-170 1.65e-95

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: 285.73  E-value: 1.65e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547694    1 DKAVVAAVAELQALSQPCADSNAIAQVGTISANSDEKVGKLIAEAMDKVGRDGVITVEDGQGLDDELAVVEGMQFDRGYL 80
Cdd:TIGR02348 119 EKAVEAVVEELKKLSKPVKGKKEIAQVATISANNDEEIGSLIAEAMEKVGKDGVITVEESKSLETELEVVEGMQFDRGYI 198

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547694   81 SPYFINKQETGSVELDDPFILLVDKKVSNIREMLPVLEGVAKAGKPLLIVAEDVEGEALATLVVNTMRGIVKVAAVKAPG 160
Cdd:TIGR02348 199 SPYFVTDAEKMEVELENPYILITDKKISNIKDLLPLLEKVAQSGKPLLIIAEDVEGEALATLVVNKLRGTLNVCAVKAPG 278

                         170
                  ....*....|
gi 340547694  161 FGDRRKAMLQ 170
Cdd:TIGR02348 279 FGDRRKAMLE 288
GroEL COG0459
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ...
 1-170 2.51e-88

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


Pssm-ID: 440227  Cd Length: 497  Bit Score: 266.56  E-value: 2.51e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547694   1 DKAVVAAVAELQALSQPCADSNAIAQVGTISANSDEKVGKLIAEAMDKVGRDGVITVEDGQGLDDELAVVEGMQFDRGYL 80
Cdd:COG0459  120 DKAVEKAVEELKKIAKPVDDKEELAQVATISANGDEEIGELIAEAMEKVGKDGVITVEEGKGLETELEVVEGMQFDKGYL 199

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547694  81 SPYFINKQETGSVELDDPFILLVDKKVSNIREMLPVLEGVAKAGKPLLIVAEDVEGEALATLVVNTMRGIVKVAAVKAPG 160
Cdd:COG0459  200 SPYFVTDPEKMPAELENAYILLTDKKISSIQDLLPLLEKVAQSGKPLLIIAEDIDGEALATLVVNGIRGVLRVVAVKAPG 279

                        170
                 ....*....|
gi 340547694 161 FGDRRKAMLQ 170
Cdd:COG0459  280 FGDRRKAMLE 289
Cpn60_TCP1 pfam00118
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ...
 20-153 1.87e-08

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: 52.59  E-value: 1.87e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547694   20 DSNAIAQVGTISANSD------EKVGKLIAEA---------MDKVGRDGVITVEDGQGLDDELavVEGMQFDRGYLSPyf 84
Cdd:pfam00118 117 DREDLLKVARTSLSSKiisresDFLAKLVVDAvlaipkndgSFDLGNIGVVKILGGSLEDSEL--VDGVVLDKGPLHP-- 192

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547694   85 inkqeTGSVELDDPFILLVDKKVSNIRE------------------------MLPVLEGVAKAGKPLLIVAEDVEGEALA 140
Cdd:pfam00118 193 -----DMPKRLENAKVLLLNCSLEYEKTetkatvvlsdaeqlerflkaeeeqILEIVEKIIDSGVNVVVCQKGIDDLALH 267

                         170
                  ....*....|...
gi 340547694  141 TLVVNTMRGIVKV 153
Cdd:pfam00118 268 FLAKNGIMALRRV 280
 
Name Accession Description Interval E-value
groEL PRK00013
chaperonin GroEL; Reviewed
 1-170 2.10e-109

chaperonin GroEL; Reviewed


Pssm-ID: 234573  Cd Length: 542  Bit Score: 322.07  E-value: 2.10e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547694   1 DKAVVAAVAELQALSQPCADSNAIAQVGTISANSDEKVGKLIAEAMDKVGRDGVITVEDGQGLDDELAVVEGMQFDRGYL 80
Cdd:PRK00013 120 DKAVEAAVEELKKISKPVEDKEEIAQVATISANGDEEIGKLIAEAMEKVGKEGVITVEESKGFETELEVVEGMQFDRGYL 199

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547694  81 SPYFINKQETGSVELDDPFILLVDKKVSNIREMLPVLEGVAKAGKPLLIVAEDVEGEALATLVVNTMRGIVKVAAVKAPG 160
Cdd:PRK00013 200 SPYFVTDPEKMEAELENPYILITDKKISNIQDLLPVLEQVAQSGKPLLIIAEDVEGEALATLVVNKLRGTLKVVAVKAPG 279

                        170
                 ....*....|
gi 340547694 161 FGDRRKAMLQ 170
Cdd:PRK00013 280 FGDRRKAMLE 289
GroEL cd03344
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ...
 1-170 1.95e-98

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: 293.21  E-value: 1.95e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547694   1 DKAVVAAVAELQALSQPCADSNAIAQVGTISANSDEKVGKLIAEAMDKVGRDGVITVEDGQGLDDELAVVEGMQFDRGYL 80
Cdd:cd03344  118 EKAVEAVVEELKKLSKPVKTKEEIAQVATISANGDEEIGELIAEAMEKVGKDGVITVEEGKTLETELEVVEGMQFDRGYL 197

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547694  81 SPYFINKQETGSVELDDPFILLVDKKVSNIREMLPVLEGVAKAGKPLLIVAEDVEGEALATLVVNTMRGIVKVAAVKAPG 160
Cdd:cd03344  198 SPYFVTDPEKMEVELENPYILLTDKKISSIQELLPILELVAKAGRPLLIIAEDVEGEALATLVVNKLRGGLKVCAVKAPG 277

                        170
                 ....*....|
gi 340547694 161 FGDRRKAMLQ 170
Cdd:cd03344  278 FGDRRKAMLE 287
GroEL TIGR02348
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ...
 1-170 1.65e-95

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: 285.73  E-value: 1.65e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547694    1 DKAVVAAVAELQALSQPCADSNAIAQVGTISANSDEKVGKLIAEAMDKVGRDGVITVEDGQGLDDELAVVEGMQFDRGYL 80
Cdd:TIGR02348 119 EKAVEAVVEELKKLSKPVKGKKEIAQVATISANNDEEIGSLIAEAMEKVGKDGVITVEESKSLETELEVVEGMQFDRGYI 198

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547694   81 SPYFINKQETGSVELDDPFILLVDKKVSNIREMLPVLEGVAKAGKPLLIVAEDVEGEALATLVVNTMRGIVKVAAVKAPG 160
Cdd:TIGR02348 199 SPYFVTDAEKMEVELENPYILITDKKISNIKDLLPLLEKVAQSGKPLLIIAEDVEGEALATLVVNKLRGTLNVCAVKAPG 278

                         170
                  ....*....|
gi 340547694  161 FGDRRKAMLQ 170
Cdd:TIGR02348 279 FGDRRKAMLE 288
groEL PRK12849
chaperonin GroEL; Reviewed
 1-170 4.91e-95

chaperonin GroEL; Reviewed


Pssm-ID: 237230  Cd Length: 542  Bit Score: 285.16  E-value: 4.91e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547694   1 DKAVVAAVAELQALSQPCADSNAIAQVGTISANSDEKVGKLIAEAMDKVGRDGVITVEDGQGLDDELAVVEGMQFDRGYL 80
Cdd:PRK12849 120 DKAVEAVVEELKALARPVSGSEEIAQVATISANGDEEIGELIAEAMEKVGKDGVITVEESKTLETELEVTEGMQFDRGYL 199

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547694  81 SPYFINKQETGSVELDDPFILLVDKKVSNIREMLPVLEGVAKAGKPLLIVAEDVEGEALATLVVNTMRGIVKVAAVKAPG 160
Cdd:PRK12849 200 SPYFVTDPERMEAVLEDPLILLTDKKISSLQDLLPLLEKVAQSGKPLLIIAEDVEGEALATLVVNKLRGGLKVAAVKAPG 279

                        170
                 ....*....|
gi 340547694 161 FGDRRKAMLQ 170
Cdd:PRK12849 280 FGDRRKAMLE 289
GroEL COG0459
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ...
 1-170 2.51e-88

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


Pssm-ID: 440227  Cd Length: 497  Bit Score: 266.56  E-value: 2.51e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547694   1 DKAVVAAVAELQALSQPCADSNAIAQVGTISANSDEKVGKLIAEAMDKVGRDGVITVEDGQGLDDELAVVEGMQFDRGYL 80
Cdd:COG0459  120 DKAVEKAVEELKKIAKPVDDKEELAQVATISANGDEEIGELIAEAMEKVGKDGVITVEEGKGLETELEVVEGMQFDKGYL 199

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547694  81 SPYFINKQETGSVELDDPFILLVDKKVSNIREMLPVLEGVAKAGKPLLIVAEDVEGEALATLVVNTMRGIVKVAAVKAPG 160
Cdd:COG0459  200 SPYFVTDPEKMPAELENAYILLTDKKISSIQDLLPLLEKVAQSGKPLLIIAEDIDGEALATLVVNGIRGVLRVVAVKAPG 279

                        170
                 ....*....|
gi 340547694 161 FGDRRKAMLQ 170
Cdd:COG0459  280 FGDRRKAMLE 289
groEL PRK12850
chaperonin GroEL; Reviewed
 1-170 3.06e-85

chaperonin GroEL; Reviewed


Pssm-ID: 237231  Cd Length: 544  Bit Score: 260.04  E-value: 3.06e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547694   1 DKAVVAAVAELQALSQPCADSNAIAQVGTISANSDEKVGKLIAEAMDKVGRDGVITVEDGQGLDDELAVVEGMQFDRGYL 80
Cdd:PRK12850 121 DLAVAAVVDELKKIAKKVTSSKEIAQVATISANGDESIGEMIAEAMDKVGKEGVITVEEAKTLGTELDVVEGMQFDRGYL 200

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547694  81 SPYFINKQETGSVELDDPFILLVDKKVSNIREMLPVLEGVAKAGKPLLIVAEDVEGEALATLVVNTMRGIVKVAAVKAPG 160
Cdd:PRK12850 201 SPYFVTNPEKMRAELEDPYILLHEKKISNLQDLLPILEAVVQSGRPLLIIAEDVEGEALATLVVNKLRGGLKSVAVKAPG 280

                        170
                 ....*....|
gi 340547694 161 FGDRRKAMLQ 170
Cdd:PRK12850 281 FGDRRKAMLE 290
groEL PRK12852
chaperonin GroEL; Reviewed
 1-170 2.85e-81

chaperonin GroEL; Reviewed


Pssm-ID: 237232  Cd Length: 545  Bit Score: 250.15  E-value: 2.85e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547694   1 DKAVVAAVAELQALSQPCADSNAIAQVGTISANSDEKVGKLIAEAMDKVGRDGVITVEDGQGLDDELAVVEGMQFDRGYL 80
Cdd:PRK12852 121 DIAVAAVVKDIEKRAKPVASSAEIAQVGTISANGDAAIGKMIAQAMQKVGNEGVITVEENKSLETEVDIVEGMKFDRGYL 200

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547694  81 SPYFINKQETGSVELDDPFILLVDKKVSNIREMLPVLEGVAKAGKPLLIVAEDVEGEALATLVVNTMRGIVKVAAVKAPG 160
Cdd:PRK12852 201 SPYFVTNAEKMTVELDDAYILLHEKKLSGLQAMLPVLEAVVQSGKPLLIIAEDVEGEALATLVVNRLRGGLKVAAVKAPG 280

                        170
                 ....*....|
gi 340547694 161 FGDRRKAMLQ 170
Cdd:PRK12852 281 FGDRRKAMLE 290
groEL PRK12851
chaperonin GroEL; Reviewed
 1-170 1.70e-79

chaperonin GroEL; Reviewed


Pssm-ID: 171770  Cd Length: 541  Bit Score: 245.42  E-value: 1.70e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547694   1 DKAVVAAVAELQALSQPCADSNAIAQVGTISANSDEKVGKLIAEAMDKVGRDGVITVEDGQGLDDELAVVEGMQFDRGYL 80
Cdd:PRK12851 121 DRAVAAVVEELKANARPVTTNAEIAQVATISANGDAEIGRLVAEAMEKVGNEGVITVEESKTAETELEVVEGMQFDRGYL 200

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547694  81 SPYFINKQETGSVELDDPFILLVDKKVSNIREMLPVLEGVAKAGKPLLIVAEDVEGEALATLVVNTMRGIVKVAAVKAPG 160
Cdd:PRK12851 201 SPYFVTDADKMEAELEDPYILIHEKKISNLQDLLPVLEAVVQSGKPLLIIAEDVEGEALATLVVNKLRGGLKVAAVKAPG 280

                        170
                 ....*....|
gi 340547694 161 FGDRRKAMLQ 170
Cdd:PRK12851 281 FGDRRKAMLE 290
PTZ00114 PTZ00114
Heat shock protein 60; Provisional
 1-170 3.06e-79

Heat shock protein 60; Provisional


Pssm-ID: 185455  Cd Length: 555  Bit Score: 244.82  E-value: 3.06e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547694   1 DKAVVAAVAELQALSQPCADSNAIAQVGTISANSDEKVGKLIAEAMDKVGRDGVITVEDGQGLDDELAVVEGMQFDRGYL 80
Cdd:PTZ00114 132 DLAVKVVLESLKEQSRPVKTKEDILNVATISANGDVEIGSLIADAMDKVGKDGTITVEDGKTLEDELEVVEGMSFDRGYI 211

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547694  81 SPYFINKQETGSVELDDPFILLVDKKVSNIREMLPVLEGVAKAGKPLLIVAEDVEGEALATLVVNTMRGIVKVAAVKAPG 160
Cdd:PTZ00114 212 SPYFVTNEKTQKVELENPLILVTDKKISSIQSILPILEHAVKNKRPLLIIAEDVEGEALQTLIINKLRGGLKVCAVKAPG 291

                        170
                 ....*....|
gi 340547694 161 FGDRRKAMLQ 170
Cdd:PTZ00114 292 FGDNRKDILQ 301
groEL CHL00093
chaperonin GroEL
 1-170 2.75e-72

chaperonin GroEL


Pssm-ID: 177025  Cd Length: 529  Bit Score: 226.14  E-value: 2.75e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547694   1 DKAVVAAVAELQALSQPCADSNAIAQVGTISANSDEKVGKLIAEAMDKVGRDGVITVEDGQGLDDELAVVEGMQFDRGYL 80
Cdd:CHL00093 120 EKATQYVVSQIAEYARPVEDIQAITQVASISAGNDEEVGSMIADAIEKVGREGVISLEEGKSTVTELEITEGMRFEKGFI 199

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547694  81 SPYFINKQETGSVELDDPFILLVDKKVSNIR-EMLPVLEGVAKAGKPLLIVAEDVEGEALATLVVNTMRGIVKVAAVKAP 159
Cdd:CHL00093 200 SPYFVTDTERMEVVQENPYILLTDKKITLVQqDLLPILEQVTKTKRPLLIIAEDVEKEALATLVLNKLRGIVNVVAVRAP 279

                        170
                 ....*....|.
gi 340547694 160 GFGDRRKAMLQ 170
Cdd:CHL00093 280 GFGDRRKAMLE 290
PRK14104 PRK14104
chaperonin GroEL; Provisional
 1-170 5.60e-66

chaperonin GroEL; Provisional


Pssm-ID: 172594  Cd Length: 546  Bit Score: 210.27  E-value: 5.60e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547694   1 DKAVVAAVAELQALSQPCADSNAIAQVGTISANSDEKVGKLIAEAMDKVGRDGVITVEDGQGLDDELAVVEGMQFDRGYL 80
Cdd:PRK14104 121 DLAVEAVVADLVKNSKKVTSNDEIAQVGTISANGDAEIGKFLADAMKKVGNEGVITVEEAKSLETELDVVEGMQFDRGYI 200

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547694  81 SPYFINKQETGSVELDDPFILLVDKKVSNIREMLPVLEGVAKAGKPLLIVAEDVEGEALATLVVNTMRGIVKVAAVKAPG 160
Cdd:PRK14104 201 SPYFVTNADKMRVEMDDAYILINEKKLSSLNELLPLLEAVVQTGKPLVIVAEDVEGEALATLVVNRLRGGLKVAAVKAPG 280

                        170
                 ....*....|
gi 340547694 161 FGDRRKAMLQ 170
Cdd:PRK14104 281 FGDRRKAMLQ 290
PLN03167 PLN03167
Chaperonin-60 beta subunit; Provisional
 1-169 8.22e-56

Chaperonin-60 beta subunit; Provisional


Pssm-ID: 215611 [Multi-domain]  Cd Length: 600  Bit Score: 184.74  E-value: 8.22e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547694   1 DKAVVAAVAELQALSQPCADSNaIAQVGTISANSDEKVGKLIAEAMDKVGRDGVITVEDGQGLDDELAVVEGMQFDRGYL 80
Cdd:PLN03167 176 EKTAKALVKELKKMSKEVEDSE-LADVAAVSAGNNYEVGNMIAEAMSKVGRKGVVTLEEGKSAENNLYVVEGMQFDRGYI 254

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547694  81 SPYFINKQETGSVELDDPFILLVDKKVSNIREMLPVLEGVAKAGKPLLIVAEDVEGEALATLVVNTMRGIVKVAAVKAPG 160
Cdd:PLN03167 255 SPYFVTDSEKMSVEYDNCKLLLVDKKITNARDLIGILEDAIRGGYPLLIIAEDIEQEALATLVVNKLRGSLKIAALKAPG 334


                 ....*....
gi 340547694 161 FGDRRKAML 169
Cdd:PLN03167 335 FGERKSQYL 343
chaperonin_type_I_II cd00309
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ...
 1-170 2.09e-27

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: 106.36  E-value: 2.09e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547694   1 DKAVVAAVAELQALSQP--CADSNAIAQVGTISANS------DEKVGKLIAEAMDKVGRD------GVITVEDGQG---L 63
Cdd:cd00309  114 EKAVEKALEILKEIAVPidVEDREELLKVATTSLNSklvsggDDFLGELVVDAVLKVGKEngdvdlGVIRVEKKKGgslE 193

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547694  64 DDELavVEGMQFDRGYLSPYFInkqetgsVELDDPFILLVDKKVSNiremlpvlegvakagkplLIVAED-VEGEALATL 142
Cdd:cd00309  194 DSEL--VVGMVFDKGYLSPYMP-------KRLENAKILLLDCKLEY------------------VVIAEKgIDDEALHYL 246

                        170       180
                 ....*....|....*....|....*...
gi 340547694 143 VVNtmrgivKVAAVKApgfgdRRKAMLQ 170
Cdd:cd00309  247 AKL------GIMAVRR-----VRKEDLE 263
chaperonin_like cd03333
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ...
 24-170 2.67e-20

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: 83.28  E-value: 2.67e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547694  24 IAQVGTISANS-----DEKVGKLIAEAMDKVGRD------GVITVEDGQG---LDDELavVEGMQFDRGYLSPYFinkqe 89
Cdd:cd03333    4 LLQVATTSLNSklsswDDFLGKLVVDAVLKVGPDnrmddlGVIKVEKIPGgslEDSEL--VVGVVFDKGYASPYM----- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547694  90 tgSVELDDPFILLVDKKVSNiremlpvlegvakagkplLIVAED-VEGEALATLVVNtmrgivKVAAVKApgfgdRRKAM 168
Cdd:cd03333   77 --PKRLENAKILLLDCPLEY------------------VVIAEKgIDDLALHYLAKA------GIMAVRR-----VKKED 125


                 ..
gi 340547694 169 LQ 170
Cdd:cd03333  126 LE 127
Cpn60_TCP1 pfam00118
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ...
 20-153 1.87e-08

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: 52.59  E-value: 1.87e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547694   20 DSNAIAQVGTISANSD------EKVGKLIAEA---------MDKVGRDGVITVEDGQGLDDELavVEGMQFDRGYLSPyf 84
Cdd:pfam00118 117 DREDLLKVARTSLSSKiisresDFLAKLVVDAvlaipkndgSFDLGNIGVVKILGGSLEDSEL--VDGVVLDKGPLHP-- 192

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340547694   85 inkqeTGSVELDDPFILLVDKKVSNIRE------------------------MLPVLEGVAKAGKPLLIVAEDVEGEALA 140
Cdd:pfam00118 193 -----DMPKRLENAKVLLLNCSLEYEKTetkatvvlsdaeqlerflkaeeeqILEIVEKIIDSGVNVVVCQKGIDDLALH 267

                         170
                  ....*....|...
gi 340547694  141 TLVVNTMRGIVKV 153
Cdd:pfam00118 268 FLAKNGIMALRRV 280
 
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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