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Conserved domains on  [gi|1550139381|gb|RVO21503|]
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molecular chaperone GroEL, partial [Sinorhizobium meliloti]

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 ...
 1-127 1.66e-63

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: 202.28  E-value: 1.66e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550139381   1 AAVQEGIVPGGGVALLRSSVKI-TVKGENDDQDAGVNIVRRALQSPARQIVENAGDEASIVVGKILEKNTDDFGYNAQTG 79
Cdd:PRK00013  404 AAVEEGIVPGGGVALLRAAPALeALKGLNGDEATGINIVLRALEAPLRQIAENAGLEGSVVVEKVKNGKGKGYGYNAATG 483

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1550139381  80 EYGDMIAMGIIDPVKVVRTALQDAASVASLLITTEAMIAELPKKDAPA 127
Cdd:PRK00013  484 EYVDMIEAGIIDPTKVTRSALQNAASVAGLLLTTEAVVADKPEKKAAA 531
 
Name Accession Description Interval E-value
groEL PRK00013
chaperonin GroEL; Reviewed
 1-127 1.66e-63

chaperonin GroEL; Reviewed


Pssm-ID: 234573  Cd Length: 542  Bit Score: 202.28  E-value: 1.66e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550139381   1 AAVQEGIVPGGGVALLRSSVKI-TVKGENDDQDAGVNIVRRALQSPARQIVENAGDEASIVVGKILEKNTDDFGYNAQTG 79
Cdd:PRK00013  404 AAVEEGIVPGGGVALLRAAPALeALKGLNGDEATGINIVLRALEAPLRQIAENAGLEGSVVVEKVKNGKGKGYGYNAATG 483

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1550139381  80 EYGDMIAMGIIDPVKVVRTALQDAASVASLLITTEAMIAELPKKDAPA 127
Cdd:PRK00013  484 EYVDMIEAGIIDPTKVTRSALQNAASVAGLLLTTEAVVADKPEKKAAA 531
GroEL cd03344
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ...
 1-119 9.81e-58

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: 186.89  E-value: 9.81e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550139381   1 AAVQEGIVPGGGVALLRSSVKI-TVKGENDDQDAGVNIVRRALQSPARQIVENAGDEASIVVGKILEKNtDDFGYNAQTG 79
Cdd:cd03344   402 AAVEEGIVPGGGVALLRASPALdKLKALNGDEKLGIEIVRRALEAPLRQIAENAGVDGSVVVEKVLESP-DGFGYDAATG 480

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1550139381  80 EYGDMIAMGIIDPVKVVRTALQDAASVASLLITTEAMIAE 119
Cdd:cd03344   481 EYVDMIEAGIIDPTKVVRSALQNAASVASLLLTTEALVVD 520
GroEL COG0459
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ...
 1-127 4.82e-53

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


Pssm-ID: 440227  Cd Length: 497  Bit Score: 174.11  E-value: 4.82e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550139381   1 AAVQEGIVPGGGVALLRSSVKI---TVKGENDDQdAGVNIVRRALQSPARQIVENAGDEASIVVGKILEKNTDDFGYNAQ 77
Cdd:COG0459   369 AAVEEGIVPGGGAALLRAARALrelAAKLEGDEQ-LGIEIVARALEAPLRQIAENAGLDGSVVVEKVRAAKDKGFGFDAA 447

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1550139381  78 TGEYGDMIAMGIIDPVKVVRTALQDAASVASLLITTEAMIAELPKKDAPA 127
Cdd:COG0459   448 TGEYVDMLEAGVIDPAKVKRSALQNAASVAGLILTTEAVIADKPEKEEAA 497
GroEL TIGR02348
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ...
 1-122 4.92e-50

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: 166.70  E-value: 4.92e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550139381   1 AAVQEGIVPGGGVALLRSSVKIT-VKGENDDQDAGVNIVRRALQSPARQIVENAGDEASIVVGKILEKNtDDFGYNAQTG 79
Cdd:TIGR02348 403 AAVEEGIVPGGGVALLRAAAALEgLKGDGEDEAIGIDIVKRALEAPLRQIAENAGLDGAVVAEKVKELK-GNFGFNAATG 481

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1550139381  80 EYGDMIAMGIIDPVKVVRTALQDAASVASLLITTEAMIAELPK 122
Cdd:TIGR02348 482 EYEDLVEAGIIDPTKVTRSALQNAASIAGLLLTTEAVVADKPE 524
Cpn60_TCP1 pfam00118
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ...
 5-117 7.48e-20

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: 84.18  E-value: 7.48e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550139381   5 EGIVPGGGVALLRSSVKI--TVKGENDDQDAGVNIVRRALQSPARQIVENAGDEASIVVGKIL---EKNTDDFGYNAQTG 79
Cdd:pfam00118 369 PRVVPGGGAVEMELARALreYAKSVSGKEQLAIEAFAEALEVIPKTLAENAGLDPIEVLAELRaahASGEKHAGIDVETG 448

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1550139381  80 EYGDMIAMGIIDPVKVVRTALQDAASVASLLITTEAMI 117
Cdd:pfam00118 449 EIIDMKEAGVVDPLKVKRQALKSATEAASTILRIDDII 486
 
Name Accession Description Interval E-value
groEL PRK00013
chaperonin GroEL; Reviewed
 1-127 1.66e-63

chaperonin GroEL; Reviewed


Pssm-ID: 234573  Cd Length: 542  Bit Score: 202.28  E-value: 1.66e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550139381   1 AAVQEGIVPGGGVALLRSSVKI-TVKGENDDQDAGVNIVRRALQSPARQIVENAGDEASIVVGKILEKNTDDFGYNAQTG 79
Cdd:PRK00013  404 AAVEEGIVPGGGVALLRAAPALeALKGLNGDEATGINIVLRALEAPLRQIAENAGLEGSVVVEKVKNGKGKGYGYNAATG 483

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1550139381  80 EYGDMIAMGIIDPVKVVRTALQDAASVASLLITTEAMIAELPKKDAPA 127
Cdd:PRK00013  484 EYVDMIEAGIIDPTKVTRSALQNAASVAGLLLTTEAVVADKPEKKAAA 531
groEL PRK12850
chaperonin GroEL; Reviewed
 1-127 2.49e-59

chaperonin GroEL; Reviewed


Pssm-ID: 237231  Cd Length: 544  Bit Score: 191.47  E-value: 2.49e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550139381   1 AAVQEGIVPGGGVALLRSSVKIT-VKGENDDQDAGVNIVRRALQSPARQIVENAGDEASIVVGKILEkNTDDFGYNAQTG 79
Cdd:PRK12850  405 AAVEEGIVPGGGVALLRARSALRgLKGANADETAGIDIVRRALEEPLRQIATNAGFEGSVVVGKVAE-LPGNFGFNAQTG 483

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1550139381  80 EYGDMIAMGIIDPVKVVRTALQDAASVASLLITTEAMIAELPKKDAPA 127
Cdd:PRK12850  484 EYGDMVEAGIIDPAKVTRTALQDAASIAALLITTEAMVAEAPKKAAAA 531
groEL PRK12849
chaperonin GroEL; Reviewed
 1-126 4.90e-59

chaperonin GroEL; Reviewed


Pssm-ID: 237230  Cd Length: 542  Bit Score: 190.79  E-value: 4.90e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550139381   1 AAVQEGIVPGGGVALLRSSVKIT-VKGENDDQDAGVNIVRRALQSPARQIVENAGDEASIVVGKILEKNtDDFGYNAQTG 79
Cdd:PRK12849  404 AAVEEGIVPGGGVALLRAAKALDeLAGLNGDQAAGVEIVRRALEAPLRQIAENAGLDGSVVVAKVLELE-DGFGFNAATG 482

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1550139381  80 EYGDMIAMGIIDPVKVVRTALQDAASVASLLITTEAMIAELPKKDAP 126
Cdd:PRK12849  483 EYGDLIAAGIIDPVKVTRSALQNAASVAGLLLTTEALVADKPEEEDP 529
groEL PRK12852
chaperonin GroEL; Reviewed
 1-126 3.56e-58

chaperonin GroEL; Reviewed


Pssm-ID: 237232  Cd Length: 545  Bit Score: 188.52  E-value: 3.56e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550139381   1 AAVQEGIVPGGGVALLRSSVKIT-VKGENDDQDAGVNIVRRALQSPARQIVENAGDEASIVVGKILEKNTDDFGYNAQTG 79
Cdd:PRK12852  405 AAVQEGIVPGGGVALLRAKKAVGrINNDNADVQAGINIVLKALEAPIRQIAENAGVEGSIVVGKILENKSETFGFDAQTE 484

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1550139381  80 EYGDMIAMGIIDPVKVVRTALQDAASVASLLITTEAMIAELPKKDAP 126
Cdd:PRK12852  485 EYVDMVAKGIIDPAKVVRTALQDAASVAGLLVTTEAMVAELPKKDAA 531
GroEL cd03344
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ...
 1-119 9.81e-58

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: 186.89  E-value: 9.81e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550139381   1 AAVQEGIVPGGGVALLRSSVKI-TVKGENDDQDAGVNIVRRALQSPARQIVENAGDEASIVVGKILEKNtDDFGYNAQTG 79
Cdd:cd03344   402 AAVEEGIVPGGGVALLRASPALdKLKALNGDEKLGIEIVRRALEAPLRQIAENAGVDGSVVVEKVLESP-DGFGYDAATG 480

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1550139381  80 EYGDMIAMGIIDPVKVVRTALQDAASVASLLITTEAMIAE 119
Cdd:cd03344   481 EYVDMIEAGIIDPTKVVRSALQNAASVASLLLTTEALVVD 520
PTZ00114 PTZ00114
Heat shock protein 60; Provisional
 1-126 1.35e-53

Heat shock protein 60; Provisional


Pssm-ID: 185455  Cd Length: 555  Bit Score: 176.64  E-value: 1.35e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550139381   1 AAVQEGIVPGGGVALLRSSVKI-TVKGEND---DQDAGVNIVRRALQSPARQIVENAGDEASIVVGKILEKNTDDFGYNA 76
Cdd:PTZ00114  417 AAVEEGIVPGGGVALLRASKLLdKLEEDNEltpDQRTGVKIVRNALRLPTKQIAENAGVEGAVVVEKILEKKDPSFGYDA 496

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1550139381  77 QTGEYGDMIAMGIIDPVKVVRTALQDAASVASLLITTEAMIAELPKKDAP 126
Cdd:PTZ00114  497 QTGEYVNMFEAGIIDPTKVVRSALVDAASVASLMLTTEAAIVDLPKEKKK 546
GroEL COG0459
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ...
 1-127 4.82e-53

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


Pssm-ID: 440227  Cd Length: 497  Bit Score: 174.11  E-value: 4.82e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550139381   1 AAVQEGIVPGGGVALLRSSVKI---TVKGENDDQdAGVNIVRRALQSPARQIVENAGDEASIVVGKILEKNTDDFGYNAQ 77
Cdd:COG0459   369 AAVEEGIVPGGGAALLRAARALrelAAKLEGDEQ-LGIEIVARALEAPLRQIAENAGLDGSVVVEKVRAAKDKGFGFDAA 447

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1550139381  78 TGEYGDMIAMGIIDPVKVVRTALQDAASVASLLITTEAMIAELPKKDAPA 127
Cdd:COG0459   448 TGEYVDMLEAGVIDPAKVKRSALQNAASVAGLILTTEAVIADKPEKEEAA 497
groEL PRK12851
chaperonin GroEL; Reviewed
 1-127 1.26e-52

chaperonin GroEL; Reviewed


Pssm-ID: 171770  Cd Length: 541  Bit Score: 173.77  E-value: 1.26e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550139381   1 AAVQEGIVPGGGVALLRSSVKI-TVKGENDDQDAGVNIVRRALQSPARQIVENAGDEASIVVGKILEKnTDDFGYNAQTG 79
Cdd:PRK12851  405 AAVEEGIVPGGGVALLRAVKALdKLETANGDQRTGVEIVRRALEAPVRQIAENAGAEGSVVVGKLREK-PGGYGFNAATN 483

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1550139381  80 EYGDMIAMGIIDPVKVVRTALQDAASVASLLITTEAMIAELPKKDAPA 127
Cdd:PRK12851  484 EYGDLYAQGVIDPVKVVRTALQNAASVAGLLLTTEAMVAEKPKKEPAP 531
GroEL TIGR02348
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ...
 1-122 4.92e-50

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: 166.70  E-value: 4.92e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550139381   1 AAVQEGIVPGGGVALLRSSVKIT-VKGENDDQDAGVNIVRRALQSPARQIVENAGDEASIVVGKILEKNtDDFGYNAQTG 79
Cdd:TIGR02348 403 AAVEEGIVPGGGVALLRAAAALEgLKGDGEDEAIGIDIVKRALEAPLRQIAENAGLDGAVVAEKVKELK-GNFGFNAATG 481

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1550139381  80 EYGDMIAMGIIDPVKVVRTALQDAASVASLLITTEAMIAELPK 122
Cdd:TIGR02348 482 EYEDLVEAGIIDPTKVTRSALQNAASIAGLLLTTEAVVADKPE 524
PRK14104 PRK14104
chaperonin GroEL; Provisional
 1-127 2.94e-48

chaperonin GroEL; Provisional


Pssm-ID: 172594  Cd Length: 546  Bit Score: 162.51  E-value: 2.94e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550139381   1 AAVQEGIVPGGGVALLRSSVKIT-VKGENDDQDAGVNIVRRALQSPARQIVENAGDEASIVVGKILEKNTDDFGYNAQTG 79
Cdd:PRK14104  405 AAVEEGIVPGGGVALLRASEQLKgIKTKNDDQKTGVEIVRKALSAPARQIAINAGEDGSVIVGKILEKEQYSYGFDSQTG 484

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1550139381  80 EYGDMIAMGIIDPVKVVRTALQDAASVASLLITTEAMIAELPKKDAPA 127
Cdd:PRK14104  485 EYGNLVSKGIIDPTKVVRTAIQNAASVAALLITTEAMVAELPKKGGAG 532
groEL CHL00093
chaperonin GroEL
 1-124 9.76e-34

chaperonin GroEL


Pssm-ID: 177025  Cd Length: 529  Bit Score: 123.29  E-value: 9.76e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550139381   1 AAVQEGIVPGGGVAL------LRSSVKITVKgenDDQDAGVNIVRRALQSPARQIVENAGDEASIVVGKILEKNTDdFGY 74
Cdd:CHL00093  404 AAVEEGIVPGGGATLvhlsenLKTWAKNNLK---EDELIGALIVARAILAPLKRIAENAGKNGSVIIEKVQEQDFE-IGY 479

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1550139381  75 NAQTGEYGDMIAMGIIDPVKVVRTALQDAASVASLLITTEAMIAELPKKD 124
Cdd:CHL00093  480 NAANNKFVNMYEAGIIDPAKVTRSALQNAASIASMILTTECIIVDKKESS 529
chaperonin_type_I_II cd00309
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ...
 1-118 2.48e-32

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: 118.68  E-value: 2.48e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550139381   1 AAVQE-GIVPGGGVALLRSSVKIT--VKGENDDQDAGVNIVRRALQSPARQIVENAGDEASIVVGKILEKNTDDFGY--- 74
Cdd:cd00309   341 AAVEDgGIVPGGGAAEIELSKALEelAKTLPGKEQLGIEAFADALEVIPRTLAENAGLDPIEVVTKLRAKHAEGGGNagg 420

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1550139381  75 NAQTGEYGDMIAMGIIDPVKVVRTALQDAASVASLLITTEAMIA 118
Cdd:cd00309   421 DVETGEIVDMKEAGIIDPLKVKRQALKSATEAASLILTIDDIIV 464
PLN03167 PLN03167
Chaperonin-60 beta subunit; Provisional
 1-125 2.22e-30

Chaperonin-60 beta subunit; Provisional


Pssm-ID: 215611 [Multi-domain]  Cd Length: 600  Bit Score: 114.25  E-value: 2.22e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550139381   1 AAVQEGIVPGGGVALLRSSVK---ITVKGENDDQDAGVNIVRRALQSPARQIVENAGDEASIVVGKILEKNTDDFGYNAQ 77
Cdd:PLN03167  459 AAVEEGIVVGGGCTLLRLASKvdaIKDTLENDEQKVGADIVKRALSYPLKLIAKNAGVNGSVVSEKVLSNDNPKFGYNAA 538

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1550139381  78 TGEYGDMIAMGIIDPVKVVRTALQDAASVASLLITTEAMIAELPKKDA 125
Cdd:PLN03167  539 TGKYEDLMAAGIIDPTKVVRCCLEHAASVAKTFLTSDCVVVEIKEPEP 586
Cpn60_TCP1 pfam00118
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ...
 5-117 7.48e-20

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: 84.18  E-value: 7.48e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550139381   5 EGIVPGGGVALLRSSVKI--TVKGENDDQDAGVNIVRRALQSPARQIVENAGDEASIVVGKIL---EKNTDDFGYNAQTG 79
Cdd:pfam00118 369 PRVVPGGGAVEMELARALreYAKSVSGKEQLAIEAFAEALEVIPKTLAENAGLDPIEVLAELRaahASGEKHAGIDVETG 448

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1550139381  80 EYGDMIAMGIIDPVKVVRTALQDAASVASLLITTEAMI 117
Cdd:pfam00118 449 EIIDMKEAGVVDPLKVKRQALKSATEAASTILRIDDII 486
cpn60 cd03343
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ...
 1-118 8.37e-06

cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. Archaeal cpn60 (thermosome), together with TF55 from thermophilic bacteria and the eukaryotic cytosol chaperonin (CTT), belong to the type II group of chaperonins. Cpn60 consists of two stacked octameric rings, which are composed of one or two different subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis.


Pssm-ID: 239459 [Multi-domain]  Cd Length: 517  Bit Score: 43.79  E-value: 8.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550139381   1 AAVQEG-IVPGGGVALLRSSVKI-----TVKGEndDQDAgVNIVRRALQSPARQIVENAG-DEASIVVG--KILEKNTDD 71
Cdd:cd03343   392 DALEDGkVVAGGGAVEIELAKRLreyarSVGGR--EQLA-VEAFADALEEIPRTLAENAGlDPIDTLVElrAAHEKGNKN 468

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1550139381  72 FGYNAQTGEYGDMIAMGIIDPVKVVRTALQDAASVASLLITTEAMIA 118
Cdd:cd03343   469 AGLDVYTGEVVDMLEKGVIEPLRVKKQAIKSATEAATMILRIDDVIA 515
TCP1_zeta cd03342
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ...
 5-118 2.64e-05

TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.


Pssm-ID: 239458 [Multi-domain]  Cd Length: 484  Bit Score: 42.63  E-value: 2.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550139381   5 EGIVPGGG---VAL---LRSSVKiTVKGENDdqdAGVNIVRRALQSPARQIVENAGDEASIVVGKILEKNTDD---FGYN 75
Cdd:cd03342   363 KCVVPGAGafeVALyahLKEFKK-SVKGKAK---LGVQAFADALLVIPKTLAENSGLDVQETLVKLQDEYAEGgqvGGVD 438

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1550139381  76 AQTGEYGDMIAMGIIDPVKVVRTALQDAASVAS-LLITTEAMIA 118
Cdd:cd03342   439 LDTGEPMDPESEGIWDNYSVKRQILHSATVIASqLLLVDEIIRA 482
TCP1_beta cd03336
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ...
 40-123 1.71e-04

TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.


Pssm-ID: 239452 [Multi-domain]  Cd Length: 517  Bit Score: 40.01  E-value: 1.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550139381  40 RALQSPARQIVENAGDEASIVVGKI---LEKNTDDFGYNAQTGEYGDMIAMGIIDPVKVVRTALQDAASVASLLITTEAM 116
Cdd:cd03336   431 KALRQLPTIIADNAGYDSAELVAQLraaHYNGNTTAGLDMRKGTVGDMKELGITESFKVKRQVLLSASEAAEMILRVDDI 510


                  ....*..
gi 1550139381 117 IAELPKK 123
Cdd:cd03336   511 IKCAPRK 517
chap_CCT_beta TIGR02341
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ...
 7-123 5.26e-04

T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT beta chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.


Pssm-ID: 274082  Cd Length: 519  Bit Score: 38.69  E-value: 5.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550139381   7 IVPGGGVALLRSSVKITVKGENDD--QDAGVNIVRRALQSPARQIVENAGDEASIVVGKILEKNTD---DFGYNAQTGEY 81
Cdd:TIGR02341 397 TVLGGGCSEMLMSKAVTQEAQRTPgkEALAVEAFARALRQLPTIIADNAGFDSAELVAQLRAAHYNgntTMGLDMNEGTI 476

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1550139381  82 GDMIAMGIIDPVKVVRTALQDAASVASLLITTEAMIAELPKK 123
Cdd:TIGR02341 477 ADMRQLGITESYKVKRAVVSSAAEAAEVILRVDNIIKAAPRK 518
PTZ00212 PTZ00212
T-complex protein 1 subunit beta; Provisional
 40-127 7.07e-04

T-complex protein 1 subunit beta; Provisional


Pssm-ID: 185514  Cd Length: 533  Bit Score: 38.47  E-value: 7.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550139381  40 RALQSPARQIVENAGDEASIVVGKI---LEKNTDDFGYNAQTGEYGDMIAMGIIDPVKVVRTALQDAASVASLLITTEAM 116
Cdd:PTZ00212  443 KALRQIPTIIADNGGYDSAELVSKLraeHYKGNKTAGIDMEKGTVGDMKELGITESYKVKLSQLCSATEAAEMILRVDDI 522

                          90
                  ....*....|.
gi 1550139381 117 IAELPKKDAPA 127
Cdd:PTZ00212  523 IRCAPRQREQV 533
TCP1_eta cd03340
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ...
 7-111 4.40e-03

TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.


Pssm-ID: 239456 [Multi-domain]  Cd Length: 522  Bit Score: 36.11  E-value: 4.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550139381   7 IVPGGGV------ALLRS-SVKITVKgenddQDAGVNIVRRALQSPARQIVENAGDEASIVVGKILEKNTDD----FGYN 75
Cdd:cd03340   401 VVAGGGAiemelsKYLRDySRTIAGK-----QQLVINAFAKALEIIPRQLCDNAGFDATDILNKLRQKHAQGggkwYGVD 475

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1550139381  76 AQTGEYGDMIAMGIIDPVKVVRTALQDAASVASLLI 111
Cdd:cd03340   476 INNEGIADNFEAFVWEPSLVKINALTAATEAACLIL 511
 
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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