|
Name |
Accession |
Description |
Interval |
E-value |
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
1-184 |
3.39e-116 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 339.79 E-value: 3.39e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33313100 1 ATVLTQSIVNEGMKNVTAGANPVGIRRGIEEATKTAVDSLHAMAHEVKTQEDIAQIASVSS-ASEETGKLIAEAMEKVGH 79
Cdd:PRK00013 91 ATVLAQAIVREGLKNVAAGANPMDLKRGIDKAVEAAVEELKKISKPVEDKEEIAQVATISAnGDEEIGKLIAEAMEKVGK 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33313100 80 DGVITIEESRGVDTSLDVVEGMQFDRGYLSQYMVTDNDKMEADLDNPYILITDKKISNIQDILPLLQSIVEQGKPLLIIA 159
Cdd:PRK00013 171 EGVITVEESKGFETELEVVEGMQFDRGYLSPYFVTDPEKMEAELENPYILITDKKISNIQDLLPVLEQVAQSGKPLLIIA 250
|
170 180
....*....|....*....|....*
gi 33313100 160 DDISGEALPTLVLNKMRGTFNVVAV 184
Cdd:PRK00013 251 EDVEGEALATLVVNKLRGTLKVVAV 275
|
|
| GroEL |
cd03344 |
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ... |
1-184 |
1.19e-100 |
|
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: 299.37 E-value: 1.19e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33313100 1 ATVLTQSIVNEGMKNVTAGANPVGIRRGIEEATKTAVDSLHAMAHEVKTQEDIAQIASVSSAS-EETGKLIAEAMEKVGH 79
Cdd:cd03344 89 ATVLARAIIKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKPVKTKEEIAQVATISANGdEEIGELIAEAMEKVGK 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33313100 80 DGVITIEESRGVDTSLDVVEGMQFDRGYLSQYMVTDNDKMEADLDNPYILITDKKISNIQDILPLLQSIVEQGKPLLIIA 159
Cdd:cd03344 169 DGVITVEEGKTLETELEVVEGMQFDRGYLSPYFVTDPEKMEVELENPYILLTDKKISSIQELLPILELVAKAGRPLLIIA 248
|
170 180
....*....|....*....|....*
gi 33313100 160 DDISGEALPTLVLNKMRGTFNVVAV 184
Cdd:cd03344 249 EDVEGEALATLVVNKLRGGLKVCAV 273
|
|
| GroEL |
TIGR02348 |
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ... |
1-184 |
2.18e-100 |
|
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: 299.21 E-value: 2.18e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33313100 1 ATVLTQSIVNEGMKNVTAGANPVGIRRGIEEATKTAVDSLHAMAHEVKTQEDIAQIASVSSAS-EETGKLIAEAMEKVGH 79
Cdd:TIGR02348 90 ATVLAQAIVKEGLKNVAAGANPIELKRGIEKAVEAVVEELKKLSKPVKGKKEIAQVATISANNdEEIGSLIAEAMEKVGK 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33313100 80 DGVITIEESRGVDTSLDVVEGMQFDRGYLSQYMVTDNDKMEADLDNPYILITDKKISNIQDILPLLQSIVEQGKPLLIIA 159
Cdd:TIGR02348 170 DGVITVEESKSLETELEVVEGMQFDRGYISPYFVTDAEKMEVELENPYILITDKKISNIKDLLPLLEKVAQSGKPLLIIA 249
|
170 180
....*....|....*....|....*
gi 33313100 160 DDISGEALPTLVLNKMRGTFNVVAV 184
Cdd:TIGR02348 250 EDVEGEALATLVVNKLRGTLNVCAV 274
|
|
| GroEL |
COG0459 |
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ... |
1-184 |
1.65e-95 |
|
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227 Cd Length: 497 Bit Score: 285.82 E-value: 1.65e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33313100 1 ATVLTQSIVNEGMKNVTAGANPVGIRRGIEEATKTAVDSLHAMAHEVKTQEDIAQIASVSSAS-EETGKLIAEAMEKVGH 79
Cdd:COG0459 91 ATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPVDDKEELAQVATISANGdEEIGELIAEAMEKVGK 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33313100 80 DGVITIEESRGVDTSLDVVEGMQFDRGYLSQYMVTDNDKMEADLDNPYILITDKKISNIQDILPLLQSIVEQGKPLLIIA 159
Cdd:COG0459 171 DGVITVEEGKGLETELEVVEGMQFDKGYLSPYFVTDPEKMPAELENAYILLTDKKISSIQDLLPLLEKVAQSGKPLLIIA 250
|
170 180
....*....|....*....|....*
gi 33313100 160 DDISGEALPTLVLNKMRGTFNVVAV 184
Cdd:COG0459 251 EDIDGEALATLVVNGIRGVLRVVAV 275
|
|
| Cpn60_TCP1 |
pfam00118 |
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ... |
1-181 |
1.65e-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: 87.64 E-value: 1.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33313100 1 ATVLTQSIVNEGMKNVTAGANPVGIRRGIEEATKTAV---DSLHAMAHEVKTQEDIAQIASVSSAS-------EETGKLI 70
Cdd:pfam00118 66 VVVLAGELLEEAEKLLAAGVHPTTIIEGYEKALEKALeilDSIISIPVEDVDREDLLKVARTSLSSkiisresDFLAKLV 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33313100 71 AEAME---------KVGHDGVITIEESRGVDTSLdvVEGMQFDRGYLSQymvtdndKMEADLDNPYILITDKKISNIQD- 140
Cdd:pfam00118 146 VDAVLaipkndgsfDLGNIGVVKILGGSLEDSEL--VDGVVLDKGPLHP-------DMPKRLENAKVLLLNCSLEYEKTe 216
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 33313100 141 -----------------------ILPLLQSIVEQGKPLLIIADDISGEALPTLVLNKMRGTFNV 181
Cdd:pfam00118 217 tkatvvlsdaeqlerflkaeeeqILEIVEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMALRRV 280
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
1-184 |
3.39e-116 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 339.79 E-value: 3.39e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33313100 1 ATVLTQSIVNEGMKNVTAGANPVGIRRGIEEATKTAVDSLHAMAHEVKTQEDIAQIASVSS-ASEETGKLIAEAMEKVGH 79
Cdd:PRK00013 91 ATVLAQAIVREGLKNVAAGANPMDLKRGIDKAVEAAVEELKKISKPVEDKEEIAQVATISAnGDEEIGKLIAEAMEKVGK 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33313100 80 DGVITIEESRGVDTSLDVVEGMQFDRGYLSQYMVTDNDKMEADLDNPYILITDKKISNIQDILPLLQSIVEQGKPLLIIA 159
Cdd:PRK00013 171 EGVITVEESKGFETELEVVEGMQFDRGYLSPYFVTDPEKMEAELENPYILITDKKISNIQDLLPVLEQVAQSGKPLLIIA 250
|
170 180
....*....|....*....|....*
gi 33313100 160 DDISGEALPTLVLNKMRGTFNVVAV 184
Cdd:PRK00013 251 EDVEGEALATLVVNKLRGTLKVVAV 275
|
|
| GroEL |
cd03344 |
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ... |
1-184 |
1.19e-100 |
|
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: 299.37 E-value: 1.19e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33313100 1 ATVLTQSIVNEGMKNVTAGANPVGIRRGIEEATKTAVDSLHAMAHEVKTQEDIAQIASVSSAS-EETGKLIAEAMEKVGH 79
Cdd:cd03344 89 ATVLARAIIKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKPVKTKEEIAQVATISANGdEEIGELIAEAMEKVGK 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33313100 80 DGVITIEESRGVDTSLDVVEGMQFDRGYLSQYMVTDNDKMEADLDNPYILITDKKISNIQDILPLLQSIVEQGKPLLIIA 159
Cdd:cd03344 169 DGVITVEEGKTLETELEVVEGMQFDRGYLSPYFVTDPEKMEVELENPYILLTDKKISSIQELLPILELVAKAGRPLLIIA 248
|
170 180
....*....|....*....|....*
gi 33313100 160 DDISGEALPTLVLNKMRGTFNVVAV 184
Cdd:cd03344 249 EDVEGEALATLVVNKLRGGLKVCAV 273
|
|
| GroEL |
TIGR02348 |
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ... |
1-184 |
2.18e-100 |
|
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: 299.21 E-value: 2.18e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33313100 1 ATVLTQSIVNEGMKNVTAGANPVGIRRGIEEATKTAVDSLHAMAHEVKTQEDIAQIASVSSAS-EETGKLIAEAMEKVGH 79
Cdd:TIGR02348 90 ATVLAQAIVKEGLKNVAAGANPIELKRGIEKAVEAVVEELKKLSKPVKGKKEIAQVATISANNdEEIGSLIAEAMEKVGK 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33313100 80 DGVITIEESRGVDTSLDVVEGMQFDRGYLSQYMVTDNDKMEADLDNPYILITDKKISNIQDILPLLQSIVEQGKPLLIIA 159
Cdd:TIGR02348 170 DGVITVEESKSLETELEVVEGMQFDRGYISPYFVTDAEKMEVELENPYILITDKKISNIKDLLPLLEKVAQSGKPLLIIA 249
|
170 180
....*....|....*....|....*
gi 33313100 160 DDISGEALPTLVLNKMRGTFNVVAV 184
Cdd:TIGR02348 250 EDVEGEALATLVVNKLRGTLNVCAV 274
|
|
| groEL |
PRK12849 |
chaperonin GroEL; Reviewed |
1-184 |
1.69e-97 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237230 Cd Length: 542 Bit Score: 292.10 E-value: 1.69e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33313100 1 ATVLTQSIVNEGMKNVTAGANPVGIRRGIEEATKTAVDSLHAMAHEVKTQEDIAQIASVSSAS-EETGKLIAEAMEKVGH 79
Cdd:PRK12849 91 ATVLAQALVQEGLKNVAAGANPMDLKRGIDKAVEAVVEELKALARPVSGSEEIAQVATISANGdEEIGELIAEAMEKVGK 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33313100 80 DGVITIEESRGVDTSLDVVEGMQFDRGYLSQYMVTDNDKMEADLDNPYILITDKKISNIQDILPLLQSIVEQGKPLLIIA 159
Cdd:PRK12849 171 DGVITVEESKTLETELEVTEGMQFDRGYLSPYFVTDPERMEAVLEDPLILLTDKKISSLQDLLPLLEKVAQSGKPLLIIA 250
|
170 180
....*....|....*....|....*
gi 33313100 160 DDISGEALPTLVLNKMRGTFNVVAV 184
Cdd:PRK12849 251 EDVEGEALATLVVNKLRGGLKVAAV 275
|
|
| GroEL |
COG0459 |
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ... |
1-184 |
1.65e-95 |
|
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227 Cd Length: 497 Bit Score: 285.82 E-value: 1.65e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33313100 1 ATVLTQSIVNEGMKNVTAGANPVGIRRGIEEATKTAVDSLHAMAHEVKTQEDIAQIASVSSAS-EETGKLIAEAMEKVGH 79
Cdd:COG0459 91 ATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPVDDKEELAQVATISANGdEEIGELIAEAMEKVGK 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33313100 80 DGVITIEESRGVDTSLDVVEGMQFDRGYLSQYMVTDNDKMEADLDNPYILITDKKISNIQDILPLLQSIVEQGKPLLIIA 159
Cdd:COG0459 171 DGVITVEEGKGLETELEVVEGMQFDKGYLSPYFVTDPEKMPAELENAYILLTDKKISSIQDLLPLLEKVAQSGKPLLIIA 250
|
170 180
....*....|....*....|....*
gi 33313100 160 DDISGEALPTLVLNKMRGTFNVVAV 184
Cdd:COG0459 251 EDIDGEALATLVVNGIRGVLRVVAV 275
|
|
| groEL |
PRK12850 |
chaperonin GroEL; Reviewed |
1-184 |
7.42e-88 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237231 Cd Length: 544 Bit Score: 267.35 E-value: 7.42e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33313100 1 ATVLTQSIVNEGMKNVTAGANPVGIRRGIEEATKTAVDSLHAMAHEVKTQEDIAQIASVSSASEET-GKLIAEAMEKVGH 79
Cdd:PRK12850 92 ATVLAQAIVREGAKLVAAGMNPMDLKRGIDLAVAAVVDELKKIAKKVTSSKEIAQVATISANGDESiGEMIAEAMDKVGK 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33313100 80 DGVITIEESRGVDTSLDVVEGMQFDRGYLSQYMVTDNDKMEADLDNPYILITDKKISNIQDILPLLQSIVEQGKPLLIIA 159
Cdd:PRK12850 172 EGVITVEEAKTLGTELDVVEGMQFDRGYLSPYFVTNPEKMRAELEDPYILLHEKKISNLQDLLPILEAVVQSGRPLLIIA 251
|
170 180
....*....|....*....|....*
gi 33313100 160 DDISGEALPTLVLNKMRGTFNVVAV 184
Cdd:PRK12850 252 EDVEGEALATLVVNKLRGGLKSVAV 276
|
|
| groEL |
PRK12851 |
chaperonin GroEL; Reviewed |
1-184 |
2.54e-82 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 171770 Cd Length: 541 Bit Score: 253.13 E-value: 2.54e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33313100 1 ATVLTQSIVNEGMKNVTAGANPVGIRRGIEEATKTAVDSLHAMAHEVKTQEDIAQIASVSS-ASEETGKLIAEAMEKVGH 79
Cdd:PRK12851 92 ATVLAQAIVREGAKAVAAGANPMDLKRGIDRAVAAVVEELKANARPVTTNAEIAQVATISAnGDAEIGRLVAEAMEKVGN 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33313100 80 DGVITIEESRGVDTSLDVVEGMQFDRGYLSQYMVTDNDKMEADLDNPYILITDKKISNIQDILPLLQSIVEQGKPLLIIA 159
Cdd:PRK12851 172 EGVITVEESKTAETELEVVEGMQFDRGYLSPYFVTDADKMEAELEDPYILIHEKKISNLQDLLPVLEAVVQSGKPLLIIA 251
|
170 180
....*....|....*....|....*
gi 33313100 160 DDISGEALPTLVLNKMRGTFNVVAV 184
Cdd:PRK12851 252 EDVEGEALATLVVNKLRGGLKVAAV 276
|
|
| groEL |
CHL00093 |
chaperonin GroEL |
1-184 |
5.57e-75 |
|
chaperonin GroEL
Pssm-ID: 177025 Cd Length: 529 Bit Score: 233.84 E-value: 5.57e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33313100 1 ATVLTQSIVNEGMKNVTAGANPVGIRRGIEEATKTAVDSLHAMAHEVKTQEDIAQIASVSSAS-EETGKLIAEAMEKVGH 79
Cdd:CHL00093 91 ATVLAYAIVKQGMKNVAAGANPISLKRGIEKATQYVVSQIAEYARPVEDIQAITQVASISAGNdEEVGSMIADAIEKVGR 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33313100 80 DGVITIEESRGVDTSLDVVEGMQFDRGYLSQYMVTDNDKMEADLDNPYILITDKKISNI-QDILPLLQSIVEQGKPLLII 158
Cdd:CHL00093 171 EGVISLEEGKSTVTELEITEGMRFEKGFISPYFVTDTERMEVVQENPYILLTDKKITLVqQDLLPILEQVTKTKRPLLII 250
|
170 180
....*....|....*....|....*.
gi 33313100 159 ADDISGEALPTLVLNKMRGTFNVVAV 184
Cdd:CHL00093 251 AEDVEKEALATLVLNKLRGIVNVVAV 276
|
|
| groEL |
PRK12852 |
chaperonin GroEL; Reviewed |
1-184 |
9.22e-74 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237232 Cd Length: 545 Bit Score: 231.27 E-value: 9.22e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33313100 1 ATVLTQSIVNEGMKNVTAGANPVGIRRGIEEATKTAVDSLHAMAHEVKTQEDIAQIASVSS-ASEETGKLIAEAMEKVGH 79
Cdd:PRK12852 92 ATVLAQAIVREGAKAVAAGMNPMDLKRGIDIAVAAVVKDIEKRAKPVASSAEIAQVGTISAnGDAAIGKMIAQAMQKVGN 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33313100 80 DGVITIEESRGVDTSLDVVEGMQFDRGYLSQYMVTDNDKMEADLDNPYILITDKKISNIQDILPLLQSIVEQGKPLLIIA 159
Cdd:PRK12852 172 EGVITVEENKSLETEVDIVEGMKFDRGYLSPYFVTNAEKMTVELDDAYILLHEKKLSGLQAMLPVLEAVVQSGKPLLIIA 251
|
170 180
....*....|....*....|....*
gi 33313100 160 DDISGEALPTLVLNKMRGTFNVVAV 184
Cdd:PRK12852 252 EDVEGEALATLVVNRLRGGLKVAAV 276
|
|
| PTZ00114 |
PTZ00114 |
Heat shock protein 60; Provisional |
1-184 |
6.51e-70 |
|
Heat shock protein 60; Provisional
Pssm-ID: 185455 Cd Length: 555 Bit Score: 221.32 E-value: 6.51e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33313100 1 ATVLTQSIVNEGMKNVTAGANPVGIRRGIEEATKTAVDSLHAMAHEVKTQEDIAQIASVS-SASEETGKLIAEAMEKVGH 79
Cdd:PTZ00114 103 ATILARAIFREGCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQSRPVKTKEDILNVATISaNGDVEIGSLIADAMDKVGK 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33313100 80 DGVITIEESRGVDTSLDVVEGMQFDRGYLSQYMVTDNDKMEADLDNPYILITDKKISNIQDILPLLQSIVEQGKPLLIIA 159
Cdd:PTZ00114 183 DGTITVEDGKTLEDELEVVEGMSFDRGYISPYFVTNEKTQKVELENPLILVTDKKISSIQSILPILEHAVKNKRPLLIIA 262
|
170 180
....*....|....*....|....*
gi 33313100 160 DDISGEALPTLVLNKMRGTFNVVAV 184
Cdd:PTZ00114 263 EDVEGEALQTLIINKLRGGLKVCAV 287
|
|
| PRK14104 |
PRK14104 |
chaperonin GroEL; Provisional |
1-184 |
1.65e-61 |
|
chaperonin GroEL; Provisional
Pssm-ID: 172594 Cd Length: 546 Bit Score: 199.49 E-value: 1.65e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33313100 1 ATVLTQSIVNEGMKNVTAGANPVGIRRGIEEATKTAVDSLHAMAHEVKTQEDIAQIASVSS-ASEETGKLIAEAMEKVGH 79
Cdd:PRK14104 92 ATVLAQAIVREGAKSVAAGMNPMDLKRGIDLAVEAVVADLVKNSKKVTSNDEIAQVGTISAnGDAEIGKFLADAMKKVGN 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33313100 80 DGVITIEESRGVDTSLDVVEGMQFDRGYLSQYMVTDNDKMEADLDNPYILITDKKISNIQDILPLLQSIVEQGKPLLIIA 159
Cdd:PRK14104 172 EGVITVEEAKSLETELDVVEGMQFDRGYISPYFVTNADKMRVEMDDAYILINEKKLSSLNELLPLLEAVVQTGKPLVIVA 251
|
170 180
....*....|....*....|....*
gi 33313100 160 DDISGEALPTLVLNKMRGTFNVVAV 184
Cdd:PRK14104 252 EDVEGEALATLVVNRLRGGLKVAAV 276
|
|
| PLN03167 |
PLN03167 |
Chaperonin-60 beta subunit; Provisional |
1-184 |
2.93e-56 |
|
Chaperonin-60 beta subunit; Provisional
Pssm-ID: 215611 [Multi-domain] Cd Length: 600 Bit Score: 186.67 E-value: 2.93e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33313100 1 ATVLTQSIVNEGMKNVTAGANPVGIRRGIEEATKTAVDSLHAMAHEVKTQEdIAQIASVSSASE-ETGKLIAEAMEKVGH 79
Cdd:PLN03167 147 SVVLAQGLIAEGVKVVAAGANPVQITRGIEKTAKALVKELKKMSKEVEDSE-LADVAAVSAGNNyEVGNMIAEAMSKVGR 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33313100 80 DGVITIEESRGVDTSLDVVEGMQFDRGYLSQYMVTDNDKMEADLDNPYILITDKKISNIQDILPLLQSIVEQGKPLLIIA 159
Cdd:PLN03167 226 KGVVTLEEGKSAENNLYVVEGMQFDRGYISPYFVTDSEKMSVEYDNCKLLLVDKKITNARDLIGILEDAIRGGYPLLIIA 305
|
170 180
....*....|....*....|....*
gi 33313100 160 DDISGEALPTLVLNKMRGTFNVVAV 184
Cdd:PLN03167 306 EDIEQEALATLVVNKLRGSLKIAAL 330
|
|
| chaperonin_type_I_II |
cd00309 |
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ... |
1-174 |
5.39e-34 |
|
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: 124.85 E-value: 5.39e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33313100 1 ATVLTQSIVNEGMKNVTAGANPVGIRRGIEEATKTAVDSLHAMA--HEVKTQEDIAQIASVSSAS-------EETGKLIA 71
Cdd:cd00309 85 VVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAvpIDVEDREELLKVATTSLNSklvsggdDFLGELVV 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33313100 72 EAMEKVGHD------GVITIEESRG---VDTSLdvVEGMQFDRGYLSQYmvtdndkMEADLDNPYILITDKKISNiqdil 142
Cdd:cd00309 165 DAVLKVGKEngdvdlGVIRVEKKKGgslEDSEL--VVGMVFDKGYLSPY-------MPKRLENAKILLLDCKLEY----- 230
|
170 180 190
....*....|....*....|....*....|...
gi 33313100 143 pllqsiveqgkplLIIADD-ISGEALPTLVLNK 174
Cdd:cd00309 231 -------------VVIAEKgIDDEALHYLAKLG 250
|
|
| Cpn60_TCP1 |
pfam00118 |
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ... |
1-181 |
1.65e-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: 87.64 E-value: 1.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33313100 1 ATVLTQSIVNEGMKNVTAGANPVGIRRGIEEATKTAV---DSLHAMAHEVKTQEDIAQIASVSSAS-------EETGKLI 70
Cdd:pfam00118 66 VVVLAGELLEEAEKLLAAGVHPTTIIEGYEKALEKALeilDSIISIPVEDVDREDLLKVARTSLSSkiisresDFLAKLV 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33313100 71 AEAME---------KVGHDGVITIEESRGVDTSLdvVEGMQFDRGYLSQymvtdndKMEADLDNPYILITDKKISNIQD- 140
Cdd:pfam00118 146 VDAVLaipkndgsfDLGNIGVVKILGGSLEDSEL--VDGVVLDKGPLHP-------DMPKRLENAKVLLLNCSLEYEKTe 216
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 33313100 141 -----------------------ILPLLQSIVEQGKPLLIIADDISGEALPTLVLNKMRGTFNV 181
Cdd:pfam00118 217 tkatvvlsdaeqlerflkaeeeqILEIVEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMALRRV 280
|
|
| chaperonin_like |
cd03333 |
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ... |
51-174 |
3.57e-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: 72.88 E-value: 3.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33313100 51 EDIAQIASVSSAS------EETGKLIAEAMEKVGHD------GVITIEESRG---VDTSLdvVEGMQFDRGYLSQYmvtd 115
Cdd:cd03333 2 ELLLQVATTSLNSklsswdDFLGKLVVDAVLKVGPDnrmddlGVIKVEKIPGgslEDSEL--VVGVVFDKGYASPY---- 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 33313100 116 ndkMEADLDNPYILITDKKISNiqdilpllqsiveqgkplLIIADD-ISGEALPTLVLNK 174
Cdd:cd03333 76 ---MPKRLENAKILLLDCPLEY------------------VVIAEKgIDDLALHYLAKAG 114
|
|
|