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Conserved domains on  [gi|55724965|emb|CAI05830|]
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60 kDa heat shock protein, partial [Enterobacter ludwigii]

Protein Classification

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 ...
 1-90 1.47e-43

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: 147.58  E-value: 1.47e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55724965    1 KLAGLTAQNEDQNVGIKVALRAMEAPLRQIVSNAGEEPSVVANMVKAGEG-NYGYNAATEEYGNMIDFGILDPTKVTRSA 79
Cdd:PRK00013 424 ALEALKGLNGDEATGINIVLRALEAPLRQIAENAGLEGSVVVEKVKNGKGkGYGYNAATGEYVDMIEAGIIDPTKVTRSA 503

                         90
                 ....*....|.
gi 55724965   80 LQYAASVAGLM 90
Cdd:PRK00013 504 LQNAASVAGLL 514
 
Name Accession Description Interval E-value
groEL PRK00013
chaperonin GroEL; Reviewed
 1-90 1.47e-43

chaperonin GroEL; Reviewed


Pssm-ID: 234573  Cd Length: 542  Bit Score: 147.58  E-value: 1.47e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55724965    1 KLAGLTAQNEDQNVGIKVALRAMEAPLRQIVSNAGEEPSVVANMVKAGEG-NYGYNAATEEYGNMIDFGILDPTKVTRSA 79
Cdd:PRK00013 424 ALEALKGLNGDEATGINIVLRALEAPLRQIAENAGLEGSVVVEKVKNGKGkGYGYNAATGEYVDMIEAGIIDPTKVTRSA 503

                         90
                 ....*....|.
gi 55724965   80 LQYAASVAGLM 90
Cdd:PRK00013 504 LQNAASVAGLL 514
GroEL TIGR02348
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ...
 1-90 9.08e-40

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: 137.04  E-value: 9.08e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55724965     1 KLAGLTAQNEDQNVGIKVALRAMEAPLRQIVSNAGEEPSVVANMVKAGEGNYGYNAATEEYGNMIDFGILDPTKVTRSAL 80
Cdd:TIGR02348 423 ALEGLKGDGEDEAIGIDIVKRALEAPLRQIAENAGLDGAVVAEKVKELKGNFGFNAATGEYEDLVEAGIIDPTKVTRSAL 502

                          90
                  ....*....|
gi 55724965    81 QYAASVAGLM 90
Cdd:TIGR02348 503 QNAASIAGLL 512
GroEL cd03344
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ...
 1-90 4.03e-39

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: 135.28  E-value: 4.03e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55724965   1 KLAGLTAQNEDQNVGIKVALRAMEAPLRQIVSNAGEEPSVVANMVKAGEGNYGYNAATEEYGNMIDFGILDPTKVTRSAL 80
Cdd:cd03344 422 ALDKLKALNGDEKLGIEIVRRALEAPLRQIAENAGVDGSVVVEKVLESPDGFGYDAATGEYVDMIEAGIIDPTKVVRSAL 501

                        90
                ....*....|
gi 55724965  81 QYAASVAGLM 90
Cdd:cd03344 502 QNAASVASLL 511
GroEL COG0459
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ...
 11-90 3.16e-33

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


Pssm-ID: 440227  Cd Length: 497  Bit Score: 119.03  E-value: 3.16e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55724965  11 DQNVGIKVALRAMEAPLRQIVSNAGEEPSVVANMVKAGE-GNYGYNAATEEYGNMIDFGILDPTKVTRSALQYAASVAGL 89
Cdd:COG0459 400 DEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKVRAAKdKGFGFDAATGEYVDMLEAGVIDPAKVKRSALQNAASVAGL 479


                .
gi 55724965  90 M 90
Cdd:COG0459 480 I 480
Cpn60_TCP1 pfam00118
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ...
 15-90 6.19e-14

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


Pssm-ID: 395068 [Multi-domain]  Cd Length: 489  Bit Score: 65.30  E-value: 6.19e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55724965    15 GIKVALRAMEAPLRQIVSNAGEEP-SVVANMVKA---GEGNYGYNAATEEYGNMIDFGILDPTKVTRSALQYAASVAGLM 90
Cdd:pfam00118 400 AIEAFAEALEVIPKTLAENAGLDPiEVLAELRAAhasGEKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKSATEAASTI 479
 
Name Accession Description Interval E-value
groEL PRK00013
chaperonin GroEL; Reviewed
 1-90 1.47e-43

chaperonin GroEL; Reviewed


Pssm-ID: 234573  Cd Length: 542  Bit Score: 147.58  E-value: 1.47e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55724965    1 KLAGLTAQNEDQNVGIKVALRAMEAPLRQIVSNAGEEPSVVANMVKAGEG-NYGYNAATEEYGNMIDFGILDPTKVTRSA 79
Cdd:PRK00013 424 ALEALKGLNGDEATGINIVLRALEAPLRQIAENAGLEGSVVVEKVKNGKGkGYGYNAATGEYVDMIEAGIIDPTKVTRSA 503

                         90
                 ....*....|.
gi 55724965   80 LQYAASVAGLM 90
Cdd:PRK00013 504 LQNAASVAGLL 514
GroEL TIGR02348
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ...
 1-90 9.08e-40

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: 137.04  E-value: 9.08e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55724965     1 KLAGLTAQNEDQNVGIKVALRAMEAPLRQIVSNAGEEPSVVANMVKAGEGNYGYNAATEEYGNMIDFGILDPTKVTRSAL 80
Cdd:TIGR02348 423 ALEGLKGDGEDEAIGIDIVKRALEAPLRQIAENAGLDGAVVAEKVKELKGNFGFNAATGEYEDLVEAGIIDPTKVTRSAL 502

                          90
                  ....*....|
gi 55724965    81 QYAASVAGLM 90
Cdd:TIGR02348 503 QNAASIAGLL 512
groEL PRK12849
chaperonin GroEL; Reviewed
 1-90 2.72e-39

chaperonin GroEL; Reviewed


Pssm-ID: 237230  Cd Length: 542  Bit Score: 136.09  E-value: 2.72e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55724965    1 KLAGLTAQNEDQNVGIKVALRAMEAPLRQIVSNAGEEPSVVANMVKAGEGNYGYNAATEEYGNMIDFGILDPTKVTRSAL 80
Cdd:PRK12849 424 ALDELAGLNGDQAAGVEIVRRALEAPLRQIAENAGLDGSVVVAKVLELEDGFGFNAATGEYGDLIAAGIIDPVKVTRSAL 503

                         90
                 ....*....|
gi 55724965   81 QYAASVAGLM 90
Cdd:PRK12849 504 QNAASVAGLL 513
GroEL cd03344
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ...
 1-90 4.03e-39

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: 135.28  E-value: 4.03e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55724965   1 KLAGLTAQNEDQNVGIKVALRAMEAPLRQIVSNAGEEPSVVANMVKAGEGNYGYNAATEEYGNMIDFGILDPTKVTRSAL 80
Cdd:cd03344 422 ALDKLKALNGDEKLGIEIVRRALEAPLRQIAENAGVDGSVVVEKVLESPDGFGYDAATGEYVDMIEAGIIDPTKVVRSAL 501

                        90
                ....*....|
gi 55724965  81 QYAASVAGLM 90
Cdd:cd03344 502 QNAASVASLL 511
groEL PRK12850
chaperonin GroEL; Reviewed
 2-90 1.96e-34

chaperonin GroEL; Reviewed


Pssm-ID: 237231  Cd Length: 544  Bit Score: 122.90  E-value: 1.96e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55724965    2 LAGLTAQNEDQNVGIKVALRAMEAPLRQIVSNAGEEPSVVANMVKAGEGNYGYNAATEEYGNMIDFGILDPTKVTRSALQ 81
Cdd:PRK12850 426 LRGLKGANADETAGIDIVRRALEEPLRQIATNAGFEGSVVVGKVAELPGNFGFNAQTGEYGDMVEAGIIDPAKVTRTALQ 505


                 ....*....
gi 55724965   82 YAASVAGLM 90
Cdd:PRK12850 506 DAASIAALL 514
GroEL COG0459
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ...
 11-90 3.16e-33

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


Pssm-ID: 440227  Cd Length: 497  Bit Score: 119.03  E-value: 3.16e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55724965  11 DQNVGIKVALRAMEAPLRQIVSNAGEEPSVVANMVKAGE-GNYGYNAATEEYGNMIDFGILDPTKVTRSALQYAASVAGL 89
Cdd:COG0459 400 DEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKVRAAKdKGFGFDAATGEYVDMLEAGVIDPAKVKRSALQNAASVAGL 479


                .
gi 55724965  90 M 90
Cdd:COG0459 480 I 480
groEL PRK12851
chaperonin GroEL; Reviewed
 2-90 6.41e-30

chaperonin GroEL; Reviewed


Pssm-ID: 171770  Cd Length: 541  Bit Score: 110.22  E-value: 6.41e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55724965    2 LAGLTAQNEDQNVGIKVALRAMEAPLRQIVSNAGEEPSVVANMVKAGEGNYGYNAATEEYGNMIDFGILDPTKVTRSALQ 81
Cdd:PRK12851 426 LDKLETANGDQRTGVEIVRRALEAPVRQIAENAGAEGSVVVGKLREKPGGYGFNAATNEYGDLYAQGVIDPVKVVRTALQ 505


                 ....*....
gi 55724965   82 YAASVAGLM 90
Cdd:PRK12851 506 NAASVAGLL 514
groEL PRK12852
chaperonin GroEL; Reviewed
 2-90 4.28e-28

chaperonin GroEL; Reviewed


Pssm-ID: 237232  Cd Length: 545  Bit Score: 105.31  E-value: 4.28e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55724965    2 LAGLTAQNEDQNVGIKVALRAMEAPLRQIVSNAGEEPSVVANMVKAGEG-NYGYNAATEEYGNMIDFGILDPTKVTRSAL 80
Cdd:PRK12852 426 VGRINNDNADVQAGINIVLKALEAPIRQIAENAGVEGSIVVGKILENKSeTFGFDAQTEEYVDMVAKGIIDPAKVVRTAL 505

                         90
                 ....*....|
gi 55724965   81 QYAASVAGLM 90
Cdd:PRK12852 506 QDAASVAGLL 515
PTZ00114 PTZ00114
Heat shock protein 60; Provisional
 9-90 5.61e-27

Heat shock protein 60; Provisional


Pssm-ID: 185455  Cd Length: 555  Bit Score: 102.30  E-value: 5.61e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55724965    9 NEDQNVGIKVALRAMEAPLRQIVSNAGEEPSVVA-NMVKAGEGNYGYNAATEEYGNMIDFGILDPTKVTRSALQYAASVA 87
Cdd:PTZ00114 448 TPDQRTGVKIVRNALRLPTKQIAENAGVEGAVVVeKILEKKDPSFGYDAQTGEYVNMFEAGIIDPTKVVRSALVDAASVA 527


                 ...
gi 55724965   88 GLM 90
Cdd:PTZ00114 528 SLM 530
groEL CHL00093
chaperonin GroEL
 10-90 9.63e-25

chaperonin GroEL


Pssm-ID: 177025  Cd Length: 529  Bit Score: 95.94  E-value: 9.63e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55724965   10 EDQNVGIKVALRAMEAPLRQIVSNAGEEPSVVANMVKAGEGNYGYNAATEEYGNMIDFGILDPTKVTRSALQYAASVAGL 89
Cdd:CHL00093 435 EDELIGALIVARAILAPLKRIAENAGKNGSVIIEKVQEQDFEIGYNAANNKFVNMYEAGIIDPAKVTRSALQNAASIASM 514


                 .
gi 55724965   90 M 90
Cdd:CHL00093 515 I 515
PRK14104 PRK14104
chaperonin GroEL; Provisional
 1-90 2.54e-21

chaperonin GroEL; Provisional


Pssm-ID: 172594  Cd Length: 546  Bit Score: 86.24  E-value: 2.54e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55724965    1 KLAGLTAQNEDQNVGIKVALRAMEAPLRQIVSNAGEEPSVVANMVKAGEG-NYGYNAATEEYGNMIDFGILDPTKVTRSA 79
Cdd:PRK14104 425 QLKGIKTKNDDQKTGVEIVRKALSAPARQIAINAGEDGSVIVGKILEKEQySYGFDSQTGEYGNLVSKGIIDPTKVVRTA 504

                         90
                 ....*....|.
gi 55724965   80 LQYAASVAGLM 90
Cdd:PRK14104 505 IQNAASVAALL 515
PLN03167 PLN03167
Chaperonin-60 beta subunit; Provisional
 6-87 1.57e-16

Chaperonin-60 beta subunit; Provisional


Pssm-ID: 215611 [Multi-domain]  Cd Length: 600  Bit Score: 72.65  E-value: 1.57e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55724965    6 TAQNEDQNVGIKVALRAMEAPLRQIVSNAGEEPSVVANMVKAGEG-NYGYNAATEEYGNMIDFGILDPTKVTRSALQYAA 84
Cdd:PLN03167 486 TLENDEQKVGADIVKRALSYPLKLIAKNAGVNGSVVSEKVLSNDNpKFGYNAATGKYEDLMAAGIIDPTKVVRCCLEHAA 565


                 ...
gi 55724965   85 SVA 87
Cdd:PLN03167 566 SVA 568
Cpn60_TCP1 pfam00118
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ...
 15-90 6.19e-14

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


Pssm-ID: 395068 [Multi-domain]  Cd Length: 489  Bit Score: 65.30  E-value: 6.19e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55724965    15 GIKVALRAMEAPLRQIVSNAGEEP-SVVANMVKA---GEGNYGYNAATEEYGNMIDFGILDPTKVTRSALQYAASVAGLM 90
Cdd:pfam00118 400 AIEAFAEALEVIPKTLAENAGLDPiEVLAELRAAhasGEKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKSATEAASTI 479
PTZ00212 PTZ00212
T-complex protein 1 subunit beta; Provisional
 17-87 1.50e-03

T-complex protein 1 subunit beta; Provisional


Pssm-ID: 185514  Cd Length: 533  Bit Score: 35.77  E-value: 1.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55724965   17 KVALrAMEA---PLRQ----IVSNAGEEPSVVANMVKA----GEGNYGYNAATEEYGNMIDFGILDPTKVTRSALQYAAS 85
Cdd:PTZ00212 433 KKSL-AIEAfakALRQiptiIADNGGYDSAELVSKLRAehykGNKTAGIDMEKGTVGDMKELGITESYKVKLSQLCSATE 511


                 ..
gi 55724965   86 VA 87
Cdd:PTZ00212 512 AA 513
 
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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