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Conserved domains on  [gi|60545971|gb|AAX23053|]
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heat shock protein 60, partial [Vibrio sp. 14D09]

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 ...
 1-180 3.39e-117

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: 342.49  E-value: 3.39e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60545971    1 TTATVLAQSIIAEGLKAVAAGMNPMDLKRGIDKAVIAAVEELKNLSVPCSDTKAIAQVGTISANSDSTVGNIIAEAMEKV 80
Cdd:PRK00013  89 TTATVLAQAIVREGLKNVAAGANPMDLKRGIDKAVEAAVEELKKISKPVEDKEEIAQVATISANGDEEIGKLIAEAMEKV 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60545971   81 GRDGVITVEEGQALQDELDVVEGMQFDRGYLSPYFINNQEAGSVDLDSPFILLIDKKVSNIRELLPTLEAVAKASRPLLI 160
Cdd:PRK00013 169 GKEGVITVEESKGFETELEVVEGMQFDRGYLSPYFVTDPEKMEAELENPYILITDKKISNIQDLLPVLEQVAQSGKPLLI 248

                        170       180
                 ....*....|....*....|
gi 60545971  161 IAEDVEGEALATLVVNNMRG 180
Cdd:PRK00013 249 IAEDVEGEALATLVVNKLRG 268
 
Name Accession Description Interval E-value
groEL PRK00013
chaperonin GroEL; Reviewed
 1-180 3.39e-117

chaperonin GroEL; Reviewed


Pssm-ID: 234573  Cd Length: 542  Bit Score: 342.49  E-value: 3.39e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60545971    1 TTATVLAQSIIAEGLKAVAAGMNPMDLKRGIDKAVIAAVEELKNLSVPCSDTKAIAQVGTISANSDSTVGNIIAEAMEKV 80
Cdd:PRK00013  89 TTATVLAQAIVREGLKNVAAGANPMDLKRGIDKAVEAAVEELKKISKPVEDKEEIAQVATISANGDEEIGKLIAEAMEKV 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60545971   81 GRDGVITVEEGQALQDELDVVEGMQFDRGYLSPYFINNQEAGSVDLDSPFILLIDKKVSNIRELLPTLEAVAKASRPLLI 160
Cdd:PRK00013 169 GKEGVITVEESKGFETELEVVEGMQFDRGYLSPYFVTDPEKMEAELENPYILITDKKISNIQDLLPVLEQVAQSGKPLLI 248

                        170       180
                 ....*....|....*....|
gi 60545971  161 IAEDVEGEALATLVVNNMRG 180
Cdd:PRK00013 249 IAEDVEGEALATLVVNKLRG 268
GroEL cd03344
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ...
 1-180 7.68e-104

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: 307.46  E-value: 7.68e-104
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60545971   1 TTATVLAQSIIAEGLKAVAAGMNPMDLKRGIDKAVIAAVEELKNLSVPCSDTKAIAQVGTISANSDSTVGNIIAEAMEKV 80
Cdd:cd03344  87 TTATVLARAIIKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKPVKTKEEIAQVATISANGDEEIGELIAEAMEKV 166

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60545971  81 GRDGVITVEEGQALQDELDVVEGMQFDRGYLSPYFINNQEAGSVDLDSPFILLIDKKVSNIRELLPTLEAVAKASRPLLI 160
Cdd:cd03344 167 GKDGVITVEEGKTLETELEVVEGMQFDRGYLSPYFVTDPEKMEVELENPYILLTDKKISSIQELLPILELVAKAGRPLLI 246

                       170       180
                ....*....|....*....|
gi 60545971 161 IAEDVEGEALATLVVNNMRG 180
Cdd:cd03344 247 IAEDVEGEALATLVVNKLRG 266
GroEL TIGR02348
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ...
 1-180 4.06e-102

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: 303.45  E-value: 4.06e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60545971     1 TTATVLAQSIIAEGLKAVAAGMNPMDLKRGIDKAVIAAVEELKNLSVPCSDTKAIAQVGTISANSDSTVGNIIAEAMEKV 80
Cdd:TIGR02348  88 TTATVLAQAIVKEGLKNVAAGANPIELKRGIEKAVEAVVEELKKLSKPVKGKKEIAQVATISANNDEEIGSLIAEAMEKV 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60545971    81 GRDGVITVEEGQALQDELDVVEGMQFDRGYLSPYFINNQEAGSVDLDSPFILLIDKKVSNIRELLPTLEAVAKASRPLLI 160
Cdd:TIGR02348 168 GKDGVITVEESKSLETELEVVEGMQFDRGYISPYFVTDAEKMEVELENPYILITDKKISNIKDLLPLLEKVAQSGKPLLI 247

                         170       180
                  ....*....|....*....|
gi 60545971   161 IAEDVEGEALATLVVNNMRG 180
Cdd:TIGR02348 248 IAEDVEGEALATLVVNKLRG 267
GroEL COG0459
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ...
 1-180 1.47e-97

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


Pssm-ID: 440227  Cd Length: 497  Bit Score: 290.83  E-value: 1.47e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60545971   1 TTATVLAQSIIAEGLKAVAAGMNPMDLKRGIDKAVIAAVEELKNLSVPCSDTKAIAQVGTISANSDSTVGNIIAEAMEKV 80
Cdd:COG0459  89 TTATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPVDDKEELAQVATISANGDEEIGELIAEAMEKV 168

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60545971  81 GRDGVITVEEGQALQDELDVVEGMQFDRGYLSPYFINNQEAGSVDLDSPFILLIDKKVSNIRELLPTLEAVAKASRPLLI 160
Cdd:COG0459 169 GKDGVITVEEGKGLETELEVVEGMQFDKGYLSPYFVTDPEKMPAELENAYILLTDKKISSIQDLLPLLEKVAQSGKPLLI 248

                       170       180
                ....*....|....*....|
gi 60545971 161 IAEDVEGEALATLVVNNMRG 180
Cdd:COG0459 249 IAEDIDGEALATLVVNGIRG 268
Cpn60_TCP1 pfam00118
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ...
 1-180 1.10e-19

TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family and the TCP-1 (T-complex protein) family.


Pssm-ID: 395068 [Multi-domain]  Cd Length: 489  Bit Score: 85.33  E-value: 1.10e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60545971     1 TTATVLAQSIIAEGLKAVAAGMNPMDLKRGIDKAVIAAVEELKN-LSVPCS--DTKAIAQVGTISANSDST------VGN 71
Cdd:pfam00118  64 TTVVVLAGELLEEAEKLLAAGVHPTTIIEGYEKALEKALEILDSiISIPVEdvDREDLLKVARTSLSSKIIsresdfLAK 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60545971    72 IIAEAME---------KVGRDGVITVEEGQAlqDELDVVEGMQFDRGYLSPyfinnqeAGSVDLDSPFILLIDKKVSNIR 142
Cdd:pfam00118 144 LVVDAVLaipkndgsfDLGNIGVVKILGGSL--EDSELVDGVVLDKGPLHP-------DMPKRLENAKVLLLNCSLEYEK 214

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 60545971   143 E------------------------LLPTLEAVAKASRPLLIIAEDVEGEALATLVVNNMRG 180
Cdd:pfam00118 215 TetkatvvlsdaeqlerflkaeeeqILEIVEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMA 276
 
Name Accession Description Interval E-value
groEL PRK00013
chaperonin GroEL; Reviewed
 1-180 3.39e-117

chaperonin GroEL; Reviewed


Pssm-ID: 234573  Cd Length: 542  Bit Score: 342.49  E-value: 3.39e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60545971    1 TTATVLAQSIIAEGLKAVAAGMNPMDLKRGIDKAVIAAVEELKNLSVPCSDTKAIAQVGTISANSDSTVGNIIAEAMEKV 80
Cdd:PRK00013  89 TTATVLAQAIVREGLKNVAAGANPMDLKRGIDKAVEAAVEELKKISKPVEDKEEIAQVATISANGDEEIGKLIAEAMEKV 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60545971   81 GRDGVITVEEGQALQDELDVVEGMQFDRGYLSPYFINNQEAGSVDLDSPFILLIDKKVSNIRELLPTLEAVAKASRPLLI 160
Cdd:PRK00013 169 GKEGVITVEESKGFETELEVVEGMQFDRGYLSPYFVTDPEKMEAELENPYILITDKKISNIQDLLPVLEQVAQSGKPLLI 248

                        170       180
                 ....*....|....*....|
gi 60545971  161 IAEDVEGEALATLVVNNMRG 180
Cdd:PRK00013 249 IAEDVEGEALATLVVNKLRG 268
GroEL cd03344
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ...
 1-180 7.68e-104

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: 307.46  E-value: 7.68e-104
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60545971   1 TTATVLAQSIIAEGLKAVAAGMNPMDLKRGIDKAVIAAVEELKNLSVPCSDTKAIAQVGTISANSDSTVGNIIAEAMEKV 80
Cdd:cd03344  87 TTATVLARAIIKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKPVKTKEEIAQVATISANGDEEIGELIAEAMEKV 166

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60545971  81 GRDGVITVEEGQALQDELDVVEGMQFDRGYLSPYFINNQEAGSVDLDSPFILLIDKKVSNIRELLPTLEAVAKASRPLLI 160
Cdd:cd03344 167 GKDGVITVEEGKTLETELEVVEGMQFDRGYLSPYFVTDPEKMEVELENPYILLTDKKISSIQELLPILELVAKAGRPLLI 246

                       170       180
                ....*....|....*....|
gi 60545971 161 IAEDVEGEALATLVVNNMRG 180
Cdd:cd03344 247 IAEDVEGEALATLVVNKLRG 266
groEL PRK12849
chaperonin GroEL; Reviewed
 1-180 4.68e-103

chaperonin GroEL; Reviewed


Pssm-ID: 237230  Cd Length: 542  Bit Score: 306.35  E-value: 4.68e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60545971    1 TTATVLAQSIIAEGLKAVAAGMNPMDLKRGIDKAVIAAVEELKNLSVPCSDTKAIAQVGTISANSDSTVGNIIAEAMEKV 80
Cdd:PRK12849  89 TTATVLAQALVQEGLKNVAAGANPMDLKRGIDKAVEAVVEELKALARPVSGSEEIAQVATISANGDEEIGELIAEAMEKV 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60545971   81 GRDGVITVEEGQALQDELDVVEGMQFDRGYLSPYFINNQEAGSVDLDSPFILLIDKKVSNIRELLPTLEAVAKASRPLLI 160
Cdd:PRK12849 169 GKDGVITVEESKTLETELEVTEGMQFDRGYLSPYFVTDPERMEAVLEDPLILLTDKKISSLQDLLPLLEKVAQSGKPLLI 248

                        170       180
                 ....*....|....*....|
gi 60545971  161 IAEDVEGEALATLVVNNMRG 180
Cdd:PRK12849 249 IAEDVEGEALATLVVNKLRG 268
GroEL TIGR02348
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ...
 1-180 4.06e-102

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: 303.45  E-value: 4.06e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60545971     1 TTATVLAQSIIAEGLKAVAAGMNPMDLKRGIDKAVIAAVEELKNLSVPCSDTKAIAQVGTISANSDSTVGNIIAEAMEKV 80
Cdd:TIGR02348  88 TTATVLAQAIVKEGLKNVAAGANPIELKRGIEKAVEAVVEELKKLSKPVKGKKEIAQVATISANNDEEIGSLIAEAMEKV 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60545971    81 GRDGVITVEEGQALQDELDVVEGMQFDRGYLSPYFINNQEAGSVDLDSPFILLIDKKVSNIRELLPTLEAVAKASRPLLI 160
Cdd:TIGR02348 168 GKDGVITVEESKSLETELEVVEGMQFDRGYISPYFVTDAEKMEVELENPYILITDKKISNIKDLLPLLEKVAQSGKPLLI 247

                         170       180
                  ....*....|....*....|
gi 60545971   161 IAEDVEGEALATLVVNNMRG 180
Cdd:TIGR02348 248 IAEDVEGEALATLVVNKLRG 267
GroEL COG0459
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ...
 1-180 1.47e-97

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


Pssm-ID: 440227  Cd Length: 497  Bit Score: 290.83  E-value: 1.47e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60545971   1 TTATVLAQSIIAEGLKAVAAGMNPMDLKRGIDKAVIAAVEELKNLSVPCSDTKAIAQVGTISANSDSTVGNIIAEAMEKV 80
Cdd:COG0459  89 TTATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPVDDKEELAQVATISANGDEEIGELIAEAMEKV 168

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60545971  81 GRDGVITVEEGQALQDELDVVEGMQFDRGYLSPYFINNQEAGSVDLDSPFILLIDKKVSNIRELLPTLEAVAKASRPLLI 160
Cdd:COG0459 169 GKDGVITVEEGKGLETELEVVEGMQFDKGYLSPYFVTDPEKMPAELENAYILLTDKKISSIQDLLPLLEKVAQSGKPLLI 248

                       170       180
                ....*....|....*....|
gi 60545971 161 IAEDVEGEALATLVVNNMRG 180
Cdd:COG0459 249 IAEDIDGEALATLVVNGIRG 268
groEL PRK12850
chaperonin GroEL; Reviewed
 1-180 4.76e-96

chaperonin GroEL; Reviewed


Pssm-ID: 237231  Cd Length: 544  Bit Score: 288.54  E-value: 4.76e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60545971    1 TTATVLAQSIIAEGLKAVAAGMNPMDLKRGIDKAVIAAVEELKNLSVPCSDTKAIAQVGTISANSDSTVGNIIAEAMEKV 80
Cdd:PRK12850  90 TTATVLAQAIVREGAKLVAAGMNPMDLKRGIDLAVAAVVDELKKIAKKVTSSKEIAQVATISANGDESIGEMIAEAMDKV 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60545971   81 GRDGVITVEEGQALQDELDVVEGMQFDRGYLSPYFINNQEAGSVDLDSPFILLIDKKVSNIRELLPTLEAVAKASRPLLI 160
Cdd:PRK12850 170 GKEGVITVEEAKTLGTELDVVEGMQFDRGYLSPYFVTNPEKMRAELEDPYILLHEKKISNLQDLLPILEAVVQSGRPLLI 249

                        170       180
                 ....*....|....*....|
gi 60545971  161 IAEDVEGEALATLVVNNMRG 180
Cdd:PRK12850 250 IAEDVEGEALATLVVNKLRG 269
groEL PRK12852
chaperonin GroEL; Reviewed
 1-180 1.22e-88

chaperonin GroEL; Reviewed


Pssm-ID: 237232  Cd Length: 545  Bit Score: 269.41  E-value: 1.22e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60545971    1 TTATVLAQSIIAEGLKAVAAGMNPMDLKRGIDKAVIAAVEELKNLSVPCSDTKAIAQVGTISANSDSTVGNIIAEAMEKV 80
Cdd:PRK12852  90 TTATVLAQAIVREGAKAVAAGMNPMDLKRGIDIAVAAVVKDIEKRAKPVASSAEIAQVGTISANGDAAIGKMIAQAMQKV 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60545971   81 GRDGVITVEEGQALQDELDVVEGMQFDRGYLSPYFINNQEAGSVDLDSPFILLIDKKVSNIRELLPTLEAVAKASRPLLI 160
Cdd:PRK12852 170 GNEGVITVEENKSLETEVDIVEGMKFDRGYLSPYFVTNAEKMTVELDDAYILLHEKKLSGLQAMLPVLEAVVQSGKPLLI 249

                        170       180
                 ....*....|....*....|
gi 60545971  161 IAEDVEGEALATLVVNNMRG 180
Cdd:PRK12852 250 IAEDVEGEALATLVVNRLRG 269
groEL PRK12851
chaperonin GroEL; Reviewed
 1-180 3.44e-88

chaperonin GroEL; Reviewed


Pssm-ID: 171770  Cd Length: 541  Bit Score: 268.15  E-value: 3.44e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60545971    1 TTATVLAQSIIAEGLKAVAAGMNPMDLKRGIDKAVIAAVEELKNLSVPCSDTKAIAQVGTISANSDSTVGNIIAEAMEKV 80
Cdd:PRK12851  90 TTATVLAQAIVREGAKAVAAGANPMDLKRGIDRAVAAVVEELKANARPVTTNAEIAQVATISANGDAEIGRLVAEAMEKV 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60545971   81 GRDGVITVEEGQALQDELDVVEGMQFDRGYLSPYFINNQEAGSVDLDSPFILLIDKKVSNIRELLPTLEAVAKASRPLLI 160
Cdd:PRK12851 170 GNEGVITVEESKTAETELEVVEGMQFDRGYLSPYFVTDADKMEAELEDPYILIHEKKISNLQDLLPVLEAVVQSGKPLLI 249

                        170       180
                 ....*....|....*....|
gi 60545971  161 IAEDVEGEALATLVVNNMRG 180
Cdd:PRK12851 250 IAEDVEGEALATLVVNKLRG 269
PTZ00114 PTZ00114
Heat shock protein 60; Provisional
 1-180 1.14e-83

Heat shock protein 60; Provisional


Pssm-ID: 185455  Cd Length: 555  Bit Score: 256.76  E-value: 1.14e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60545971    1 TTATVLAQSIIAEGLKAVAAGMNPMDLKRGIDKAVIAAVEELKNLSVPCSDTKAIAQVGTISANSDSTVGNIIAEAMEKV 80
Cdd:PTZ00114 101 TTATILARAIFREGCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQSRPVKTKEDILNVATISANGDVEIGSLIADAMDKV 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60545971   81 GRDGVITVEEGQALQDELDVVEGMQFDRGYLSPYFINNQEAGSVDLDSPFILLIDKKVSNIRELLPTLEAVAKASRPLLI 160
Cdd:PTZ00114 181 GKDGTITVEDGKTLEDELEVVEGMSFDRGYISPYFVTNEKTQKVELENPLILVTDKKISSIQSILPILEHAVKNKRPLLI 260

                        170       180
                 ....*....|....*....|
gi 60545971  161 IAEDVEGEALATLVVNNMRG 180
Cdd:PTZ00114 261 IAEDVEGEALQTLIINKLRG 280
groEL CHL00093
chaperonin GroEL
 1-180 2.96e-77

chaperonin GroEL


Pssm-ID: 177025  Cd Length: 529  Bit Score: 239.62  E-value: 2.96e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60545971    1 TTATVLAQSIIAEGLKAVAAGMNPMDLKRGIDKAVIAAVEELKNLSVPCSDTKAIAQVGTISANSDSTVGNIIAEAMEKV 80
Cdd:CHL00093  89 TTATVLAYAIVKQGMKNVAAGANPISLKRGIEKATQYVVSQIAEYARPVEDIQAITQVASISAGNDEEVGSMIADAIEKV 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60545971   81 GRDGVITVEEGQALQDELDVVEGMQFDRGYLSPYFINNQEAGSVDLDSPFILLIDKKVSNIR-ELLPTLEAVAKASRPLL 159
Cdd:CHL00093 169 GREGVISLEEGKSTVTELEITEGMRFEKGFISPYFVTDTERMEVVQENPYILLTDKKITLVQqDLLPILEQVTKTKRPLL 248

                        170       180
                 ....*....|....*....|.
gi 60545971  160 IIAEDVEGEALATLVVNNMRG 180
Cdd:CHL00093 249 IIAEDVEKEALATLVLNKLRG 269
PRK14104 PRK14104
chaperonin GroEL; Provisional
 1-180 2.10e-70

chaperonin GroEL; Provisional


Pssm-ID: 172594  Cd Length: 546  Bit Score: 222.21  E-value: 2.10e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60545971    1 TTATVLAQSIIAEGLKAVAAGMNPMDLKRGIDKAVIAAVEELKNLSVPCSDTKAIAQVGTISANSDSTVGNIIAEAMEKV 80
Cdd:PRK14104  90 TTATVLAQAIVREGAKSVAAGMNPMDLKRGIDLAVEAVVADLVKNSKKVTSNDEIAQVGTISANGDAEIGKFLADAMKKV 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60545971   81 GRDGVITVEEGQALQDELDVVEGMQFDRGYLSPYFINNQEAGSVDLDSPFILLIDKKVSNIRELLPTLEAVAKASRPLLI 160
Cdd:PRK14104 170 GNEGVITVEEAKSLETELDVVEGMQFDRGYISPYFVTNADKMRVEMDDAYILINEKKLSSLNELLPLLEAVVQTGKPLVI 249

                        170       180
                 ....*....|....*....|
gi 60545971  161 IAEDVEGEALATLVVNNMRG 180
Cdd:PRK14104 250 VAEDVEGEALATLVVNRLRG 269
PLN03167 PLN03167
Chaperonin-60 beta subunit; Provisional
 1-180 1.51e-60

Chaperonin-60 beta subunit; Provisional


Pssm-ID: 215611 [Multi-domain]  Cd Length: 600  Bit Score: 197.84  E-value: 1.51e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60545971    1 TTATVLAQSIIAEGLKAVAAGMNPMDLKRGIDKAVIAAVEELKNLSVPCSDTKaIAQVGTISANSDSTVGNIIAEAMEKV 80
Cdd:PLN03167 145 TTSVVLAQGLIAEGVKVVAAGANPVQITRGIEKTAKALVKELKKMSKEVEDSE-LADVAAVSAGNNYEVGNMIAEAMSKV 223

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60545971   81 GRDGVITVEEGQALQDELDVVEGMQFDRGYLSPYFINNQEAGSVDLDSPFILLIDKKVSNIRELLPTLEAVAKASRPLLI 160
Cdd:PLN03167 224 GRKGVVTLEEGKSAENNLYVVEGMQFDRGYISPYFVTDSEKMSVEYDNCKLLLVDKKITNARDLIGILEDAIRGGYPLLI 303

                        170       180
                 ....*....|....*....|
gi 60545971  161 IAEDVEGEALATLVVNNMRG 180
Cdd:PLN03167 304 IAEDIEQEALATLVVNKLRG 323
chaperonin_type_I_II cd00309
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ...
 1-177 2.81e-39

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: 138.72  E-value: 2.81e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60545971   1 TTATVLAQSIIAEGLKAVAAGMNPMDLKRGIDKAVIAAVEELKNLSVP--CSDTKAIAQVGTISANS------DSTVGNI 72
Cdd:cd00309  83 TTVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVPidVEDREELLKVATTSLNSklvsggDDFLGEL 162

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60545971  73 IAEAMEKVGR------DGVITVEE---GQALQDELdvVEGMQFDRGYLSPYFInnqeagsVDLDSPFILLIDKKVSNire 143
Cdd:cd00309 163 VVDAVLKVGKengdvdLGVIRVEKkkgGSLEDSEL--VVGMVFDKGYLSPYMP-------KRLENAKILLLDCKLEY--- 230

                       170       180       190
                ....*....|....*....|....*....|....*
gi 60545971 144 llptleavakasrplLIIAED-VEGEALATLVVNN 177
Cdd:cd00309 231 ---------------VVIAEKgIDDEALHYLAKLG 250
Cpn60_TCP1 pfam00118
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ...
 1-180 1.10e-19

TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family and the TCP-1 (T-complex protein) family.


Pssm-ID: 395068 [Multi-domain]  Cd Length: 489  Bit Score: 85.33  E-value: 1.10e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60545971     1 TTATVLAQSIIAEGLKAVAAGMNPMDLKRGIDKAVIAAVEELKN-LSVPCS--DTKAIAQVGTISANSDST------VGN 71
Cdd:pfam00118  64 TTVVVLAGELLEEAEKLLAAGVHPTTIIEGYEKALEKALEILDSiISIPVEdvDREDLLKVARTSLSSKIIsresdfLAK 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60545971    72 IIAEAME---------KVGRDGVITVEEGQAlqDELDVVEGMQFDRGYLSPyfinnqeAGSVDLDSPFILLIDKKVSNIR 142
Cdd:pfam00118 144 LVVDAVLaipkndgsfDLGNIGVVKILGGSL--EDSELVDGVVLDKGPLHP-------DMPKRLENAKVLLLNCSLEYEK 214

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 60545971   143 E------------------------LLPTLEAVAKASRPLLIIAEDVEGEALATLVVNNMRG 180
Cdd:pfam00118 215 TetkatvvlsdaeqlerflkaeeeqILEIVEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMA 276
chaperonin_like cd03333
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ...
 53-177 7.88e-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: 71.73  E-value: 7.88e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60545971  53 KAIAQVGTISANS-----DSTVGNIIAEAMEKVGRD------GVITVEE---GQALQDELdvVEGMQFDRGYLSPYFinn 118
Cdd:cd03333   2 ELLLQVATTSLNSklsswDDFLGKLVVDAVLKVGPDnrmddlGVIKVEKipgGSLEDSEL--VVGVVFDKGYASPYM--- 76

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 60545971 119 qeagSVDLDSPFILLIDKKVSNirellptleavakasrplLIIAED-VEGEALATLVVNN 177
Cdd:cd03333  77 ----PKRLENAKILLLDCPLEY------------------VVIAEKgIDDLALHYLAKAG 114
 
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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