groEL protein, partial [Rahnella aquatilis CIP 78.65 = ATCC 33071]
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
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 ... |
1-271 | 0e+00 | |||||
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: 535.86 E-value: 0e+00
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| Name | Accession | Description | Interval | E-value | |||||
| groEL | PRK00013 | chaperonin GroEL; Reviewed |
1-271 | 0e+00 | |||||
chaperonin GroEL; Reviewed Pssm-ID: 234573 Cd Length: 542 Bit Score: 535.86 E-value: 0e+00
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| GroEL | cd03344 | GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ... |
1-271 | 5.99e-175 | |||||
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: 492.36 E-value: 5.99e-175
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| GroEL | TIGR02348 | chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ... |
1-271 | 3.71e-170 | |||||
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: 480.64 E-value: 3.71e-170
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| GroEL | COG0459 | Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ... |
1-271 | 1.03e-162 | |||||
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440227 Cd Length: 497 Bit Score: 460.70 E-value: 1.03e-162
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| Cpn60_TCP1 | pfam00118 | TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ... |
15-265 | 1.48e-41 | |||||
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: 148.89 E-value: 1.48e-41
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| Name | Accession | Description | Interval | E-value | |||||
| groEL | PRK00013 | chaperonin GroEL; Reviewed |
1-271 | 0e+00 | |||||
chaperonin GroEL; Reviewed Pssm-ID: 234573 Cd Length: 542 Bit Score: 535.86 E-value: 0e+00
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| GroEL | cd03344 | GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ... |
1-271 | 5.99e-175 | |||||
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: 492.36 E-value: 5.99e-175
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| groEL | PRK12849 | chaperonin GroEL; Reviewed |
1-271 | 1.82e-173 | |||||
chaperonin GroEL; Reviewed Pssm-ID: 237230 Cd Length: 542 Bit Score: 489.70 E-value: 1.82e-173
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| GroEL | TIGR02348 | chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ... |
1-271 | 3.71e-170 | |||||
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: 480.64 E-value: 3.71e-170
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| GroEL | COG0459 | Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ... |
1-271 | 1.03e-162 | |||||
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440227 Cd Length: 497 Bit Score: 460.70 E-value: 1.03e-162
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| groEL | PRK12850 | chaperonin GroEL; Reviewed |
3-271 | 4.25e-161 | |||||
chaperonin GroEL; Reviewed Pssm-ID: 237231 Cd Length: 544 Bit Score: 458.41 E-value: 4.25e-161
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| groEL | PRK12852 | chaperonin GroEL; Reviewed |
3-271 | 1.30e-149 | |||||
chaperonin GroEL; Reviewed Pssm-ID: 237232 Cd Length: 545 Bit Score: 429.26 E-value: 1.30e-149
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| groEL | PRK12851 | chaperonin GroEL; Reviewed |
2-271 | 4.62e-147 | |||||
chaperonin GroEL; Reviewed Pssm-ID: 171770 Cd Length: 541 Bit Score: 422.61 E-value: 4.62e-147
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| PTZ00114 | PTZ00114 | Heat shock protein 60; Provisional |
1-271 | 1.75e-144 | |||||
Heat shock protein 60; Provisional Pssm-ID: 185455 Cd Length: 555 Bit Score: 416.24 E-value: 1.75e-144
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| groEL | CHL00093 | chaperonin GroEL |
3-271 | 4.86e-125 | |||||
chaperonin GroEL Pssm-ID: 177025 Cd Length: 529 Bit Score: 365.97 E-value: 4.86e-125
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| PRK14104 | PRK14104 | chaperonin GroEL; Provisional |
1-271 | 8.13e-125 | |||||
chaperonin GroEL; Provisional Pssm-ID: 172594 Cd Length: 546 Bit Score: 365.89 E-value: 8.13e-125
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| PLN03167 | PLN03167 | Chaperonin-60 beta subunit; Provisional |
7-271 | 1.25e-100 | |||||
Chaperonin-60 beta subunit; Provisional Pssm-ID: 215611 [Multi-domain] Cd Length: 600 Bit Score: 305.70 E-value: 1.25e-100
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| chaperonin_type_I_II | cd00309 | chaperonin families, type I and type II. Chaperonins are involved in productive folding of ... |
1-270 | 9.74e-84 | |||||
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: 258.13 E-value: 9.74e-84
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| Cpn60_TCP1 | pfam00118 | TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ... |
15-265 | 1.48e-41 | |||||
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: 148.89 E-value: 1.48e-41
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| chaperonin_like | cd03333 | chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ... |
134-270 | 4.70e-17 | |||||
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: 77.51 E-value: 4.70e-17
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| cpn60 | cd03343 | cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ... |
1-161 | 3.40e-15 | |||||
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: 74.99 E-value: 3.40e-15
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| TCP1_beta | cd03336 | TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ... |
1-135 | 7.60e-13 | |||||
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: 67.74 E-value: 7.60e-13
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| TCP1_delta | cd03338 | TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ... |
15-146 | 7.37e-12 | |||||
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta 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: 239454 [Multi-domain] Cd Length: 515 Bit Score: 65.00 E-value: 7.37e-12
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| chap_CCT_eta | TIGR02345 | T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ... |
9-134 | 1.87e-11 | |||||
T-complex protein 1, eta 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 eta chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes. Pssm-ID: 274086 [Multi-domain] Cd Length: 523 Bit Score: 63.62 E-value: 1.87e-11
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| TCP1_eta | cd03340 | TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ... |
14-129 | 2.31e-11 | |||||
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: 63.46 E-value: 2.31e-11
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| chap_CCT_epsi | TIGR02343 | T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ... |
1-133 | 2.62e-11 | |||||
T-complex protein 1, epsilon 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 epsilon chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes. Pssm-ID: 274084 [Multi-domain] Cd Length: 532 Bit Score: 63.28 E-value: 2.62e-11
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| PTZ00212 | PTZ00212 | T-complex protein 1 subunit beta; Provisional |
1-128 | 4.95e-11 | |||||
T-complex protein 1 subunit beta; Provisional Pssm-ID: 185514 Cd Length: 533 Bit Score: 62.35 E-value: 4.95e-11
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| chap_CCT_beta | TIGR02341 | T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ... |
1-135 | 6.49e-11 | |||||
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: 62.18 E-value: 6.49e-11
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| chap_CCT_delta | TIGR02342 | T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ... |
2-146 | 8.06e-11 | |||||
T-complex protein 1, delta 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 delta chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes. Pssm-ID: 274083 Cd Length: 517 Bit Score: 61.72 E-value: 8.06e-11
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| TCP1_epsilon | cd03339 | TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ... |
3-134 | 1.32e-09 | |||||
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon 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: 239455 Cd Length: 526 Bit Score: 58.08 E-value: 1.32e-09
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| chap_CCT_alpha | TIGR02340 | T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ... |
1-125 | 8.45e-09 | |||||
T-complex protein 1, alpha 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 alpha chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes. Pssm-ID: 274081 [Multi-domain] Cd Length: 536 Bit Score: 55.88 E-value: 8.45e-09
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| chap_CCT_zeta | TIGR02347 | T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ... |
15-128 | 1.15e-07 | |||||
T-complex protein 1, zeta 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 zeta chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes. Pssm-ID: 274088 [Multi-domain] Cd Length: 531 Bit Score: 52.43 E-value: 1.15e-07
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| TCP1_zeta | cd03342 | TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
15-129 | 2.35e-07 | |||||
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: 51.49 E-value: 2.35e-07
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| TCP1_gamma | cd03337 | TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ... |
15-164 | 2.43e-07 | |||||
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma 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: 239453 [Multi-domain] Cd Length: 480 Bit Score: 51.14 E-value: 2.43e-07
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| chap_CCT_gamma | TIGR02344 | T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ... |
15-216 | 3.76e-07 | |||||
T-complex protein 1, gamma 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 gamma chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes. Pssm-ID: 274085 [Multi-domain] Cd Length: 524 Bit Score: 50.89 E-value: 3.76e-07
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| TCP1_alpha | cd03335 | TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ... |
1-161 | 1.39e-06 | |||||
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha 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: 239451 Cd Length: 527 Bit Score: 49.20 E-value: 1.39e-06
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| chap_CCT_theta | TIGR02346 | T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ... |
3-128 | 8.16e-06 | |||||
T-complex protein 1, theta 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 alpha chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes. Pssm-ID: 274087 [Multi-domain] Cd Length: 531 Bit Score: 46.63 E-value: 8.16e-06
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| TCP1_theta | cd03341 | TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ... |
15-128 | 4.91e-05 | |||||
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta 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: 239457 [Multi-domain] Cd Length: 472 Bit Score: 44.13 E-value: 4.91e-05
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| Blast search parameters | ||||
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