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Conserved domains on  [gi|733760045|gb|AJA00751|]
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heat shock protein 60, partial [Vibrio sp. PID42_41]

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 ...
 1-167 6.14e-105

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: 310.52  E-value: 6.14e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733760045   1 ATVLAQSIISEGLKAVAAGMNPMDLKRGIDKAVAAAVEELKALSVECKDTKAIAQVGTISANSDSTVGNIIAEAMEKVGR 80
Cdd:PRK00013  91 ATVLAQAIVREGLKNVAAGANPMDLKRGIDKAVEAAVEELKKISKPVEDKEEIAQVATISANGDEEIGKLIAEAMEKVGK 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733760045  81 DGVITVEEGQALQDELDVVEGMQFDRGYLSPYFINNQEAGSVDLESPFILLIDKKVSNIRELLPTLEAVAKASRPLLIIA 160
Cdd:PRK00013 171 EGVITVEESKGFETELEVVEGMQFDRGYLSPYFVTDPEKMEAELENPYILITDKKISNIQDLLPVLEQVAQSGKPLLIIA 250


                 ....*..
gi 733760045 161 EDVEGEA 167
Cdd:PRK00013 251 EDVEGEA 257
 
Name Accession Description Interval E-value
groEL PRK00013
chaperonin GroEL; Reviewed
 1-167 6.14e-105

chaperonin GroEL; Reviewed


Pssm-ID: 234573  Cd Length: 542  Bit Score: 310.52  E-value: 6.14e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733760045   1 ATVLAQSIISEGLKAVAAGMNPMDLKRGIDKAVAAAVEELKALSVECKDTKAIAQVGTISANSDSTVGNIIAEAMEKVGR 80
Cdd:PRK00013  91 ATVLAQAIVREGLKNVAAGANPMDLKRGIDKAVEAAVEELKKISKPVEDKEEIAQVATISANGDEEIGKLIAEAMEKVGK 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733760045  81 DGVITVEEGQALQDELDVVEGMQFDRGYLSPYFINNQEAGSVDLESPFILLIDKKVSNIRELLPTLEAVAKASRPLLIIA 160
Cdd:PRK00013 171 EGVITVEESKGFETELEVVEGMQFDRGYLSPYFVTDPEKMEAELENPYILITDKKISNIQDLLPVLEQVAQSGKPLLIIA 250


                 ....*..
gi 733760045 161 EDVEGEA 167
Cdd:PRK00013 251 EDVEGEA 257
GroEL cd03344
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ...
 1-167 8.19e-94

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: 281.27  E-value: 8.19e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733760045   1 ATVLAQSIISEGLKAVAAGMNPMDLKRGIDKAVAAAVEELKALSVECKDTKAIAQVGTISANSDSTVGNIIAEAMEKVGR 80
Cdd:cd03344   89 ATVLARAIIKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKPVKTKEEIAQVATISANGDEEIGELIAEAMEKVGK 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733760045  81 DGVITVEEGQALQDELDVVEGMQFDRGYLSPYFINNQEAGSVDLESPFILLIDKKVSNIRELLPTLEAVAKASRPLLIIA 160
Cdd:cd03344  169 DGVITVEEGKTLETELEVVEGMQFDRGYLSPYFVTDPEKMEVELENPYILLTDKKISSIQELLPILELVAKAGRPLLIIA 248


                 ....*..
gi 733760045 161 EDVEGEA 167
Cdd:cd03344  249 EDVEGEA 255
GroEL TIGR02348
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ...
 1-167 4.64e-92

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: 276.87  E-value: 4.64e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733760045    1 ATVLAQSIISEGLKAVAAGMNPMDLKRGIDKAVAAAVEELKALSVECKDTKAIAQVGTISANSDSTVGNIIAEAMEKVGR 80
Cdd:TIGR02348  90 ATVLAQAIVKEGLKNVAAGANPIELKRGIEKAVEAVVEELKKLSKPVKGKKEIAQVATISANNDEEIGSLIAEAMEKVGK 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733760045   81 DGVITVEEGQALQDELDVVEGMQFDRGYLSPYFINNQEAGSVDLESPFILLIDKKVSNIRELLPTLEAVAKASRPLLIIA 160
Cdd:TIGR02348 170 DGVITVEESKSLETELEVVEGMQFDRGYISPYFVTDAEKMEVELENPYILITDKKISNIKDLLPLLEKVAQSGKPLLIIA 249


                  ....*..
gi 733760045  161 EDVEGEA 167
Cdd:TIGR02348 250 EDVEGEA 256
GroEL COG0459
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ...
 1-167 6.29e-87

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


Pssm-ID: 440227  Cd Length: 497  Bit Score: 263.09  E-value: 6.29e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733760045   1 ATVLAQSIISEGLKAVAAGMNPMDLKRGIDKAVAAAVEELKALSVECKDTKAIAQVGTISANSDSTVGNIIAEAMEKVGR 80
Cdd:COG0459   91 ATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPVDDKEELAQVATISANGDEEIGELIAEAMEKVGK 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733760045  81 DGVITVEEGQALQDELDVVEGMQFDRGYLSPYFINNQEAGSVDLESPFILLIDKKVSNIRELLPTLEAVAKASRPLLIIA 160
Cdd:COG0459  171 DGVITVEEGKGLETELEVVEGMQFDKGYLSPYFVTDPEKMPAELENAYILLTDKKISSIQDLLPLLEKVAQSGKPLLIIA 250


                 ....*..
gi 733760045 161 EDVEGEA 167
Cdd:COG0459  251 EDIDGEA 257
Cpn60_TCP1 pfam00118
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ...
 1-167 1.71e-18

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: 81.48  E-value: 1.71e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733760045    1 ATVLAQSIISEGLKAVAAGMNPMDLKRGIDKAVAAAVEELK---ALSVECKDTKAIAQVGTISANSDST------VGNII 71
Cdd:pfam00118  66 VVVLAGELLEEAEKLLAAGVHPTTIIEGYEKALEKALEILDsiiSIPVEDVDREDLLKVARTSLSSKIIsresdfLAKLV 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733760045   72 AEAME---------KVGRDGVITVEEGQAlqDELDVVEGMQFDRGYLSPyfinnqeAGSVDLESPFILLIDKKVSNIRE- 141
Cdd:pfam00118 146 VDAVLaipkndgsfDLGNIGVVKILGGSL--EDSELVDGVVLDKGPLHP-------DMPKRLENAKVLLLNCSLEYEKTe 216

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 733760045  142 -----------------------LLPTLEAVAKASRPLLIIAEDVEGEA 167
Cdd:pfam00118 217 tkatvvlsdaeqlerflkaeeeqILEIVEKIIDSGVNVVVCQKGIDDLA 265
 
Name Accession Description Interval E-value
groEL PRK00013
chaperonin GroEL; Reviewed
 1-167 6.14e-105

chaperonin GroEL; Reviewed


Pssm-ID: 234573  Cd Length: 542  Bit Score: 310.52  E-value: 6.14e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733760045   1 ATVLAQSIISEGLKAVAAGMNPMDLKRGIDKAVAAAVEELKALSVECKDTKAIAQVGTISANSDSTVGNIIAEAMEKVGR 80
Cdd:PRK00013  91 ATVLAQAIVREGLKNVAAGANPMDLKRGIDKAVEAAVEELKKISKPVEDKEEIAQVATISANGDEEIGKLIAEAMEKVGK 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733760045  81 DGVITVEEGQALQDELDVVEGMQFDRGYLSPYFINNQEAGSVDLESPFILLIDKKVSNIRELLPTLEAVAKASRPLLIIA 160
Cdd:PRK00013 171 EGVITVEESKGFETELEVVEGMQFDRGYLSPYFVTDPEKMEAELENPYILITDKKISNIQDLLPVLEQVAQSGKPLLIIA 250


                 ....*..
gi 733760045 161 EDVEGEA 167
Cdd:PRK00013 251 EDVEGEA 257
GroEL cd03344
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ...
 1-167 8.19e-94

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: 281.27  E-value: 8.19e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733760045   1 ATVLAQSIISEGLKAVAAGMNPMDLKRGIDKAVAAAVEELKALSVECKDTKAIAQVGTISANSDSTVGNIIAEAMEKVGR 80
Cdd:cd03344   89 ATVLARAIIKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKPVKTKEEIAQVATISANGDEEIGELIAEAMEKVGK 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733760045  81 DGVITVEEGQALQDELDVVEGMQFDRGYLSPYFINNQEAGSVDLESPFILLIDKKVSNIRELLPTLEAVAKASRPLLIIA 160
Cdd:cd03344  169 DGVITVEEGKTLETELEVVEGMQFDRGYLSPYFVTDPEKMEVELENPYILLTDKKISSIQELLPILELVAKAGRPLLIIA 248


                 ....*..
gi 733760045 161 EDVEGEA 167
Cdd:cd03344  249 EDVEGEA 255
groEL PRK12849
chaperonin GroEL; Reviewed
 1-167 1.39e-92

chaperonin GroEL; Reviewed


Pssm-ID: 237230  Cd Length: 542  Bit Score: 278.61  E-value: 1.39e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733760045   1 ATVLAQSIISEGLKAVAAGMNPMDLKRGIDKAVAAAVEELKALSVECKDTKAIAQVGTISANSDSTVGNIIAEAMEKVGR 80
Cdd:PRK12849  91 ATVLAQALVQEGLKNVAAGANPMDLKRGIDKAVEAVVEELKALARPVSGSEEIAQVATISANGDEEIGELIAEAMEKVGK 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733760045  81 DGVITVEEGQALQDELDVVEGMQFDRGYLSPYFINNQEAGSVDLESPFILLIDKKVSNIRELLPTLEAVAKASRPLLIIA 160
Cdd:PRK12849 171 DGVITVEESKTLETELEVTEGMQFDRGYLSPYFVTDPERMEAVLEDPLILLTDKKISSLQDLLPLLEKVAQSGKPLLIIA 250


                 ....*..
gi 733760045 161 EDVEGEA 167
Cdd:PRK12849 251 EDVEGEA 257
GroEL TIGR02348
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ...
 1-167 4.64e-92

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: 276.87  E-value: 4.64e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733760045    1 ATVLAQSIISEGLKAVAAGMNPMDLKRGIDKAVAAAVEELKALSVECKDTKAIAQVGTISANSDSTVGNIIAEAMEKVGR 80
Cdd:TIGR02348  90 ATVLAQAIVKEGLKNVAAGANPIELKRGIEKAVEAVVEELKKLSKPVKGKKEIAQVATISANNDEEIGSLIAEAMEKVGK 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733760045   81 DGVITVEEGQALQDELDVVEGMQFDRGYLSPYFINNQEAGSVDLESPFILLIDKKVSNIRELLPTLEAVAKASRPLLIIA 160
Cdd:TIGR02348 170 DGVITVEESKSLETELEVVEGMQFDRGYISPYFVTDAEKMEVELENPYILITDKKISNIKDLLPLLEKVAQSGKPLLIIA 249


                  ....*..
gi 733760045  161 EDVEGEA 167
Cdd:TIGR02348 250 EDVEGEA 256
GroEL COG0459
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ...
 1-167 6.29e-87

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


Pssm-ID: 440227  Cd Length: 497  Bit Score: 263.09  E-value: 6.29e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733760045   1 ATVLAQSIISEGLKAVAAGMNPMDLKRGIDKAVAAAVEELKALSVECKDTKAIAQVGTISANSDSTVGNIIAEAMEKVGR 80
Cdd:COG0459   91 ATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPVDDKEELAQVATISANGDEEIGELIAEAMEKVGK 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733760045  81 DGVITVEEGQALQDELDVVEGMQFDRGYLSPYFINNQEAGSVDLESPFILLIDKKVSNIRELLPTLEAVAKASRPLLIIA 160
Cdd:COG0459  171 DGVITVEEGKGLETELEVVEGMQFDKGYLSPYFVTDPEKMPAELENAYILLTDKKISSIQDLLPLLEKVAQSGKPLLIIA 250


                 ....*..
gi 733760045 161 EDVEGEA 167
Cdd:COG0459  251 EDIDGEA 257
groEL PRK12850
chaperonin GroEL; Reviewed
 1-167 5.12e-86

chaperonin GroEL; Reviewed


Pssm-ID: 237231  Cd Length: 544  Bit Score: 261.96  E-value: 5.12e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733760045   1 ATVLAQSIISEGLKAVAAGMNPMDLKRGIDKAVAAAVEELKALSVECKDTKAIAQVGTISANSDSTVGNIIAEAMEKVGR 80
Cdd:PRK12850  92 ATVLAQAIVREGAKLVAAGMNPMDLKRGIDLAVAAVVDELKKIAKKVTSSKEIAQVATISANGDESIGEMIAEAMDKVGK 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733760045  81 DGVITVEEGQALQDELDVVEGMQFDRGYLSPYFINNQEAGSVDLESPFILLIDKKVSNIRELLPTLEAVAKASRPLLIIA 160
Cdd:PRK12850 172 EGVITVEEAKTLGTELDVVEGMQFDRGYLSPYFVTNPEKMRAELEDPYILLHEKKISNLQDLLPILEAVVQSGRPLLIIA 251


                 ....*..
gi 733760045 161 EDVEGEA 167
Cdd:PRK12850 252 EDVEGEA 258
groEL PRK12852
chaperonin GroEL; Reviewed
 1-167 3.19e-78

chaperonin GroEL; Reviewed


Pssm-ID: 237232  Cd Length: 545  Bit Score: 242.06  E-value: 3.19e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733760045   1 ATVLAQSIISEGLKAVAAGMNPMDLKRGIDKAVAAAVEELKALSVECKDTKAIAQVGTISANSDSTVGNIIAEAMEKVGR 80
Cdd:PRK12852  92 ATVLAQAIVREGAKAVAAGMNPMDLKRGIDIAVAAVVKDIEKRAKPVASSAEIAQVGTISANGDAAIGKMIAQAMQKVGN 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733760045  81 DGVITVEEGQALQDELDVVEGMQFDRGYLSPYFINNQEAGSVDLESPFILLIDKKVSNIRELLPTLEAVAKASRPLLIIA 160
Cdd:PRK12852 172 EGVITVEENKSLETEVDIVEGMKFDRGYLSPYFVTNAEKMTVELDDAYILLHEKKLSGLQAMLPVLEAVVQSGKPLLIIA 251


                 ....*..
gi 733760045 161 EDVEGEA 167
Cdd:PRK12852 252 EDVEGEA 258
groEL PRK12851
chaperonin GroEL; Reviewed
 1-167 3.22e-78

chaperonin GroEL; Reviewed


Pssm-ID: 171770  Cd Length: 541  Bit Score: 241.95  E-value: 3.22e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733760045   1 ATVLAQSIISEGLKAVAAGMNPMDLKRGIDKAVAAAVEELKALSVECKDTKAIAQVGTISANSDSTVGNIIAEAMEKVGR 80
Cdd:PRK12851  92 ATVLAQAIVREGAKAVAAGANPMDLKRGIDRAVAAVVEELKANARPVTTNAEIAQVATISANGDAEIGRLVAEAMEKVGN 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733760045  81 DGVITVEEGQALQDELDVVEGMQFDRGYLSPYFINNQEAGSVDLESPFILLIDKKVSNIRELLPTLEAVAKASRPLLIIA 160
Cdd:PRK12851 172 EGVITVEESKTAETELEVVEGMQFDRGYLSPYFVTDADKMEAELEDPYILIHEKKISNLQDLLPVLEAVVQSGKPLLIIA 251


                 ....*..
gi 733760045 161 EDVEGEA 167
Cdd:PRK12851 252 EDVEGEA 258
PTZ00114 PTZ00114
Heat shock protein 60; Provisional
 1-167 8.20e-76

Heat shock protein 60; Provisional


Pssm-ID: 185455  Cd Length: 555  Bit Score: 235.96  E-value: 8.20e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733760045   1 ATVLAQSIISEGLKAVAAGMNPMDLKRGIDKAVAAAVEELKALSVECKDTKAIAQVGTISANSDSTVGNIIAEAMEKVGR 80
Cdd:PTZ00114 103 ATILARAIFREGCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQSRPVKTKEDILNVATISANGDVEIGSLIADAMDKVGK 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733760045  81 DGVITVEEGQALQDELDVVEGMQFDRGYLSPYFINNQEAGSVDLESPFILLIDKKVSNIRELLPTLEAVAKASRPLLIIA 160
Cdd:PTZ00114 183 DGTITVEDGKTLEDELEVVEGMSFDRGYISPYFVTNEKTQKVELENPLILVTDKKISSIQSILPILEHAVKNKRPLLIIA 262


                 ....*..
gi 733760045 161 EDVEGEA 167
Cdd:PTZ00114 263 EDVEGEA 269
groEL CHL00093
chaperonin GroEL
 1-167 4.16e-66

chaperonin GroEL


Pssm-ID: 177025  Cd Length: 529  Bit Score: 209.96  E-value: 4.16e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733760045   1 ATVLAQSIISEGLKAVAAGMNPMDLKRGIDKAVAAAVEELKALSVECKDTKAIAQVGTISANSDSTVGNIIAEAMEKVGR 80
Cdd:CHL00093  91 ATVLAYAIVKQGMKNVAAGANPISLKRGIEKATQYVVSQIAEYARPVEDIQAITQVASISAGNDEEVGSMIADAIEKVGR 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733760045  81 DGVITVEEGQALQDELDVVEGMQFDRGYLSPYFINNQEAGSVDLESPFILLIDKKVSNIR-ELLPTLEAVAKASRPLLII 159
Cdd:CHL00093 171 EGVISLEEGKSTVTELEITEGMRFEKGFISPYFVTDTERMEVVQENPYILLTDKKITLVQqDLLPILEQVTKTKRPLLII 250


                 ....*...
gi 733760045 160 AEDVEGEA 167
Cdd:CHL00093 251 AEDVEKEA 258
PRK14104 PRK14104
chaperonin GroEL; Provisional
 1-167 1.66e-61

chaperonin GroEL; Provisional


Pssm-ID: 172594  Cd Length: 546  Bit Score: 198.72  E-value: 1.66e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733760045   1 ATVLAQSIISEGLKAVAAGMNPMDLKRGIDKAVAAAVEELKALSVECKDTKAIAQVGTISANSDSTVGNIIAEAMEKVGR 80
Cdd:PRK14104  92 ATVLAQAIVREGAKSVAAGMNPMDLKRGIDLAVEAVVADLVKNSKKVTSNDEIAQVGTISANGDAEIGKFLADAMKKVGN 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733760045  81 DGVITVEEGQALQDELDVVEGMQFDRGYLSPYFINNQEAGSVDLESPFILLIDKKVSNIRELLPTLEAVAKASRPLLIIA 160
Cdd:PRK14104 172 EGVITVEEAKSLETELDVVEGMQFDRGYISPYFVTNADKMRVEMDDAYILINEKKLSSLNELLPLLEAVVQTGKPLVIVA 251


                 ....*..
gi 733760045 161 EDVEGEA 167
Cdd:PRK14104 252 EDVEGEA 258
PLN03167 PLN03167
Chaperonin-60 beta subunit; Provisional
 1-167 1.90e-52

Chaperonin-60 beta subunit; Provisional


Pssm-ID: 215611 [Multi-domain]  Cd Length: 600  Bit Score: 175.50  E-value: 1.90e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733760045   1 ATVLAQSIISEGLKAVAAGMNPMDLKRGIDKAVAAAVEELKALSVECKDTKaIAQVGTISANSDSTVGNIIAEAMEKVGR 80
Cdd:PLN03167 147 SVVLAQGLIAEGVKVVAAGANPVQITRGIEKTAKALVKELKKMSKEVEDSE-LADVAAVSAGNNYEVGNMIAEAMSKVGR 225

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733760045  81 DGVITVEEGQALQDELDVVEGMQFDRGYLSPYFINNQEAGSVDLESPFILLIDKKVSNIRELLPTLEAVAKASRPLLIIA 160
Cdd:PLN03167 226 KGVVTLEEGKSAENNLYVVEGMQFDRGYISPYFVTDSEKMSVEYDNCKLLLVDKKITNARDLIGILEDAIRGGYPLLIIA 305


                 ....*..
gi 733760045 161 EDVEGEA 167
Cdd:PLN03167 306 EDIEQEA 312
chaperonin_type_I_II cd00309
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ...
 1-167 3.36e-35

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: 127.16  E-value: 3.36e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733760045   1 ATVLAQSIISEGLKAVAAGMNPMDLKRGIDKAVAAAVEELKALSV--ECKDTKAIAQVGTISANS------DSTVGNIIA 72
Cdd:cd00309   85 VVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVpiDVEDREELLKVATTSLNSklvsggDDFLGELVV 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733760045  73 EAMEKVGRD------GVITVEE---GQALQDELdvVEGMQFDRGYLSPYFInnqeagsVDLESPFILLIDKKVSNirell 143
Cdd:cd00309  165 DAVLKVGKEngdvdlGVIRVEKkkgGSLEDSEL--VVGMVFDKGYLSPYMP-------KRLENAKILLLDCKLEY----- 230

                        170       180
                 ....*....|....*....|....*
gi 733760045 144 ptleavakasrplLIIAED-VEGEA 167
Cdd:cd00309  231 -------------VVIAEKgIDDEA 242
Cpn60_TCP1 pfam00118
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ...
 1-167 1.71e-18

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: 81.48  E-value: 1.71e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733760045    1 ATVLAQSIISEGLKAVAAGMNPMDLKRGIDKAVAAAVEELK---ALSVECKDTKAIAQVGTISANSDST------VGNII 71
Cdd:pfam00118  66 VVVLAGELLEEAEKLLAAGVHPTTIIEGYEKALEKALEILDsiiSIPVEDVDREDLLKVARTSLSSKIIsresdfLAKLV 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733760045   72 AEAME---------KVGRDGVITVEEGQAlqDELDVVEGMQFDRGYLSPyfinnqeAGSVDLESPFILLIDKKVSNIRE- 141
Cdd:pfam00118 146 VDAVLaipkndgsfDLGNIGVVKILGGSL--EDSELVDGVVLDKGPLHP-------DMPKRLENAKVLLLNCSLEYEKTe 216

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 733760045  142 -----------------------LLPTLEAVAKASRPLLIIAEDVEGEA 167
Cdd:pfam00118 217 tkatvvlsdaeqlerflkaeeeqILEIVEKIIDSGVNVVVCQKGIDDLA 265
chaperonin_like cd03333
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ...
 51-167 3.21e-13

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: 64.41  E-value: 3.21e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733760045  51 KAIAQVGTISANS-----DSTVGNIIAEAMEKVGRD------GVITVEE---GQALQDELdvVEGMQFDRGYLSPYFinn 116
Cdd:cd03333    2 ELLLQVATTSLNSklsswDDFLGKLVVDAVLKVGPDnrmddlGVIKVEKipgGSLEDSEL--VVGVVFDKGYASPYM--- 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 733760045 117 qeagSVDLESPFILLIDKKVSNirellptleavakasrplLIIAED-VEGEA 167
Cdd:cd03333   77 ----PKRLENAKILLLDCPLEY------------------VVIAEKgIDDLA 106
 
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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