|
Name |
Accession |
Description |
Interval |
E-value |
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
2-529 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 986.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 2 AAKDVVFGDSARAKMVEGVNILANAVKVTLGPKGRNVVLERSFGGPTVTKDGVSVAKEIELKDKLQNMGAQMVKEVASKT 81
Cdd:PRK00013 1 MAKDIKFGEDARRKLLRGVNKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDPFENMGAQLVKEVASKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 82 SDNAGDGTTTATVLAQSIVREGMKYVASGMNPMDLKRGIDKAVAAAIEELRKISKPCTTNKEIAQVGAISANSDTSIGDR 161
Cdd:PRK00013 81 NDVAGDGTTTATVLAQAIVREGLKNVAAGANPMDLKRGIDKAVEAAVEELKKISKPVEDKEEIAQVATISANGDEEIGKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 162 IAEAMDKVGKEGVITVEDGKSLQDELDVVEGMQFDRGYLSPYFINNPDKQVAVLDNPFVLLHDKKVSNIRDLLPILEQVA 241
Cdd:PRK00013 161 IAEAMEKVGKEGVITVEESKGFETELEVVEGMQFDRGYLSPYFVTDPEKMEAELENPYILITDKKISNIQDLLPVLEQVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 242 KAGRPLLIIAEDVEGEALATLVVNNIRGILKTVAVKAPGFGDRRKAMLEDIAILTGGQVIAEETGLTLEKATLNELGQAK 321
Cdd:PRK00013 241 QSGKPLLIIAEDVEGEALATLVVNKLRGTLKVVAVKAPGFGDRRKAMLEDIAILTGGTVISEELGLKLEDATLEDLGQAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 322 RIEVGKENTTIIDGAGEAASIEARVKQVRTQIEEATSDYDREKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVEDALH 401
Cdd:PRK00013 321 KVVVTKDNTTIVDGAGDKEAIKARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATEVEMKEKKDRVEDALH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 402 ATRAAVEEGIVAGGGVALIRARSAIGSVKGDNPDQDAGIKIVLRAMEEPLRQIVTNGGEEASVVVAAVAAGTG-NYGYNA 480
Cdd:PRK00013 401 ATRAAVEEGIVPGGGVALLRAAPALEALKGLNGDEATGINIVLRALEAPLRQIAENAGLEGSVVVEKVKNGKGkGYGYNA 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1878327742 481 ATGEYGDLVEAGVVDPTKVTRTALQNAASVAGLLLTTDAAVCELPKEDA 529
Cdd:PRK00013 481 ATGEYVDMIEAGIIDPTKVTRSALQNAASVAGLLLTTEAVVADKPEKKA 529
|
|
| groEL |
PRK12849 |
chaperonin GroEL; Reviewed |
2-529 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237230 Cd Length: 542 Bit Score: 901.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 2 AAKDVVFGDSARAKMVEGVNILANAVKVTLGPKGRNVVLERSFGGPTVTKDGVSVAKEIELKDKLQNMGAQMVKEVASKT 81
Cdd:PRK12849 1 MAKIIKFDEEARRALERGVNKLADAVKVTLGPKGRNVVIDKSFGAPTITKDGVSIAKEIELEDPFENLGAQLVKEVASKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 82 SDNAGDGTTTATVLAQSIVREGMKYVASGMNPMDLKRGIDKAVAAAIEELRKISKPCTTNKEIAQVGAISANSDTSIGDR 161
Cdd:PRK12849 81 NDVAGDGTTTATVLAQALVQEGLKNVAAGANPMDLKRGIDKAVEAVVEELKALARPVSGSEEIAQVATISANGDEEIGEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 162 IAEAMDKVGKEGVITVEDGKSLQDELDVVEGMQFDRGYLSPYFINNPDKQVAVLDNPFVLLHDKKVSNIRDLLPILEQVA 241
Cdd:PRK12849 161 IAEAMEKVGKDGVITVEESKTLETELEVTEGMQFDRGYLSPYFVTDPERMEAVLEDPLILLTDKKISSLQDLLPLLEKVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 242 KAGRPLLIIAEDVEGEALATLVVNNIRGILKTVAVKAPGFGDRRKAMLEDIAILTGGQVIAEETGLTLEKATLNELGQAK 321
Cdd:PRK12849 241 QSGKPLLIIAEDVEGEALATLVVNKLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGLKLEEVTLDDLGRAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 322 RIEVGKENTTIIDGAGEAASIEARVKQVRTQIEEATSDYDREKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVEDALH 401
Cdd:PRK12849 321 RVTITKDNTTIVDGAGDKEAIEARVAQIRRQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATEVELKERKDRVEDALN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 402 ATRAAVEEGIVAGGGVALIRARSAIGSVKGDNPDQDAGIKIVLRAMEEPLRQIVTNGGEEASVVVAAVAAGTGNYGYNAA 481
Cdd:PRK12849 401 ATRAAVEEGIVPGGGVALLRAAKALDELAGLNGDQAAGVEIVRRALEAPLRQIAENAGLDGSVVVAKVLELEDGFGFNAA 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1878327742 482 TGEYGDLVEAGVVDPTKVTRTALQNAASVAGLLLTTDAAVCELPKEDA 529
Cdd:PRK12849 481 TGEYGDLIAAGIIDPVKVTRSALQNAASVAGLLLTTEALVADKPEEED 528
|
|
| GroEL |
cd03344 |
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ... |
4-523 |
0e+00 |
|
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: 887.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 4 KDVVFGDSARAKMVEGVNILANAVKVTLGPKGRNVVLERSFGGPTVTKDGVSVAKEIELKDKLQNMGAQMVKEVASKTSD 83
Cdd:cd03344 1 KDIKFGEEARKALLRGVNKLADAVKVTLGPKGRNVVIEKSFGSPKITKDGVTVAKEIELEDPFENMGAQLVKEVASKTND 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 84 NAGDGTTTATVLAQSIVREGMKYVASGMNPMDLKRGIDKAVAAAIEELRKISKPCTTNKEIAQVGAISANSDTSIGDRIA 163
Cdd:cd03344 81 VAGDGTTTATVLARAIIKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKPVKTKEEIAQVATISANGDEEIGELIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 164 EAMDKVGKEGVITVEDGKSLQDELDVVEGMQFDRGYLSPYFINNPDKQVAVLDNPFVLLHDKKVSNIRDLLPILEQVAKA 243
Cdd:cd03344 161 EAMEKVGKDGVITVEEGKTLETELEVVEGMQFDRGYLSPYFVTDPEKMEVELENPYILLTDKKISSIQELLPILELVAKA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 244 GRPLLIIAEDVEGEALATLVVNNIRGILKTVAVKAPGFGDRRKAMLEDIAILTGGQVIAEETGLTLEKATLNELGQAKRI 323
Cdd:cd03344 241 GRPLLIIAEDVEGEALATLVVNKLRGGLKVCAVKAPGFGDRRKAMLEDIAILTGGTVISEELGLKLEDVTLEDLGRAKKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 324 EVGKENTTIIDGAGEAASIEARVKQVRTQIEEATSDYDREKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVEDALHAT 403
Cdd:cd03344 321 VVTKDDTTIIGGAGDKAAIKARIAQIRKQIEETTSDYDKEKLQERLAKLSGGVAVIKVGGATEVELKEKKDRVEDALNAT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 404 RAAVEEGIVAGGGVALIRARSAIGSVKGDNPDQDAGIKIVLRAMEEPLRQIVTNGGEEASVVVAAVAAGTGNYGYNAATG 483
Cdd:cd03344 401 RAAVEEGIVPGGGVALLRASPALDKLKALNGDEKLGIEIVRRALEAPLRQIAENAGVDGSVVVEKVLESPDGFGYDAATG 480
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1878327742 484 EYGDLVEAGVVDPTKVTRTALQNAASVAGLLLTTDAAVCE 523
Cdd:cd03344 481 EYVDMIEAGIIDPTKVVRSALQNAASVASLLLTTEALVVD 520
|
|
| groEL |
PRK12850 |
chaperonin GroEL; Reviewed |
1-529 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237231 Cd Length: 544 Bit Score: 882.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 1 MAAKDVVFGDSARAKMVEGVNILANAVKVTLGPKGRNVVLERSFGGPTVTKDGVSVAKEIELKDKLQNMGAQMVKEVASK 80
Cdd:PRK12850 1 MAAKEIRFSTDARDRLLRGVNILANAVKVTLGPKGRNVVLEKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVKEVASK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 81 TSDNAGDGTTTATVLAQSIVREGMKYVASGMNPMDLKRGIDKAVAAAIEELRKISKPCTTNKEIAQVGAISANSDTSIGD 160
Cdd:PRK12850 81 TNDLAGDGTTTATVLAQAIVREGAKLVAAGMNPMDLKRGIDLAVAAVVDELKKIAKKVTSSKEIAQVATISANGDESIGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 161 RIAEAMDKVGKEGVITVEDGKSLQDELDVVEGMQFDRGYLSPYFINNPDKQVAVLDNPFVLLHDKKVSNIRDLLPILEQV 240
Cdd:PRK12850 161 MIAEAMDKVGKEGVITVEEAKTLGTELDVVEGMQFDRGYLSPYFVTNPEKMRAELEDPYILLHEKKISNLQDLLPILEAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 241 AKAGRPLLIIAEDVEGEALATLVVNNIRGILKTVAVKAPGFGDRRKAMLEDIAILTGGQVIAEETGLTLEKATLNELGQA 320
Cdd:PRK12850 241 VQSGRPLLIIAEDVEGEALATLVVNKLRGGLKSVAVKAPGFGDRRKAMLEDIAVLTGGQVISEDLGIKLENVTLDMLGRA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 321 KRIEVGKENTTIIDGAGEAASIEARVKQVRTQIEEATSDYDREKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVEDAL 400
Cdd:PRK12850 321 KRVLITKENTTIIDGAGDKKNIEARVKQIRAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKEKKDRVDDAL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 401 HATRAAVEEGIVAGGGVALIRARSAIGSVKGDNPDQDAGIKIVLRAMEEPLRQIVTNGGEEASVVVAAVAAGTGNYGYNA 480
Cdd:PRK12850 401 HATRAAVEEGIVPGGGVALLRARSALRGLKGANADETAGIDIVRRALEEPLRQIATNAGFEGSVVVGKVAELPGNFGFNA 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1878327742 481 ATGEYGDLVEAGVVDPTKVTRTALQNAASVAGLLLTTDAAVCELPKEDA 529
Cdd:PRK12850 481 QTGEYGDMVEAGIIDPAKVTRTALQDAASIAALLITTEAMVAEAPKKAA 529
|
|
| GroEL |
TIGR02348 |
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ... |
3-526 |
0e+00 |
|
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: 861.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 3 AKDVVFGDSARAKMVEGVNILANAVKVTLGPKGRNVVLERSFGGPTVTKDGVSVAKEIELKDKLQNMGAQMVKEVASKTS 82
Cdd:TIGR02348 1 AKQIKFDEEARKALLRGVDKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDKFENMGAQLVKEVASKTN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 83 DNAGDGTTTATVLAQSIVREGMKYVASGMNPMDLKRGIDKAVAAAIEELRKISKPCTTNKEIAQVGAISANSDTSIGDRI 162
Cdd:TIGR02348 81 DVAGDGTTTATVLAQAIVKEGLKNVAAGANPIELKRGIEKAVEAVVEELKKLSKPVKGKKEIAQVATISANNDEEIGSLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 163 AEAMDKVGKEGVITVEDGKSLQDELDVVEGMQFDRGYLSPYFINNPDKQVAVLDNPFVLLHDKKVSNIRDLLPILEQVAK 242
Cdd:TIGR02348 161 AEAMEKVGKDGVITVEESKSLETELEVVEGMQFDRGYISPYFVTDAEKMEVELENPYILITDKKISNIKDLLPLLEKVAQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 243 AGRPLLIIAEDVEGEALATLVVNNIRGILKTVAVKAPGFGDRRKAMLEDIAILTGGQVIAEETGLTLEKATLNELGQAKR 322
Cdd:TIGR02348 241 SGKPLLIIAEDVEGEALATLVVNKLRGTLNVCAVKAPGFGDRRKAMLEDIAILTGGQVISEELGLKLEEVTLDDLGKAKK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 323 IEVGKENTTIIDGAGEAASIEARVKQVRTQIEEATSDYDREKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVEDALHA 402
Cdd:TIGR02348 321 VTVDKDNTTIVEGAGDKAAIKARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATETEMKEKKLRIEDALNA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 403 TRAAVEEGIVAGGGVALIRARSAIGSVKGDNPDQDAGIKIVLRAMEEPLRQIVTNGGEEASVVVAAVAAGTGNYGYNAAT 482
Cdd:TIGR02348 401 TRAAVEEGIVPGGGVALLRAAAALEGLKGDGEDEAIGIDIVKRALEAPLRQIAENAGLDGAVVAEKVKELKGNFGFNAAT 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1878327742 483 GEYGDLVEAGVVDPTKVTRTALQNAASVAGLLLTTDAAVCELPK 526
Cdd:TIGR02348 481 GEYEDLVEAGIIDPTKVTRSALQNAASIAGLLLTTEAVVADKPE 524
|
|
| groEL |
PRK12852 |
chaperonin GroEL; Reviewed |
1-529 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237232 Cd Length: 545 Bit Score: 804.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 1 MAAKDVVFGDSARAKMVEGVNILANAVKVTLGPKGRNVVLERSFGGPTVTKDGVSVAKEIELKDKLQNMGAQMVKEVASK 80
Cdd:PRK12852 1 MAAKDVKFSGDARDRMLRGVDILANAVKVTLGPKGRNVVIEKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVREVASK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 81 TSDNAGDGTTTATVLAQSIVREGMKYVASGMNPMDLKRGIDKAVAAAIEELRKISKPCTTNKEIAQVGAISANSDTSIGD 160
Cdd:PRK12852 81 TNDLAGDGTTTATVLAQAIVREGAKAVAAGMNPMDLKRGIDIAVAAVVKDIEKRAKPVASSAEIAQVGTISANGDAAIGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 161 RIAEAMDKVGKEGVITVEDGKSLQDELDVVEGMQFDRGYLSPYFINNPDKQVAVLDNPFVLLHDKKVSNIRDLLPILEQV 240
Cdd:PRK12852 161 MIAQAMQKVGNEGVITVEENKSLETEVDIVEGMKFDRGYLSPYFVTNAEKMTVELDDAYILLHEKKLSGLQAMLPVLEAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 241 AKAGRPLLIIAEDVEGEALATLVVNNIRGILKTVAVKAPGFGDRRKAMLEDIAILTGGQVIAEETGLTLEKATLNELGQA 320
Cdd:PRK12852 241 VQSGKPLLIIAEDVEGEALATLVVNRLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGQLISEDLGIKLENVTLKMLGRA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 321 KRIEVGKENTTIIDGAGEAASIEARVKQVRTQIEEATSDYDREKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVEDAL 400
Cdd:PRK12852 321 KKVVIDKENTTIVNGAGKKADIEARVGQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKEKKDRVEDAL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 401 HATRAAVEEGIVAGGGVALIRARSAIGSVKGDNPDQDAGIKIVLRAMEEPLRQIVTNGGEEASVVVAAVAAGTG-NYGYN 479
Cdd:PRK12852 401 NATRAAVQEGIVPGGGVALLRAKKAVGRINNDNADVQAGINIVLKALEAPIRQIAENAGVEGSIVVGKILENKSeTFGFD 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1878327742 480 AATGEYGDLVEAGVVDPTKVTRTALQNAASVAGLLLTTDAAVCELPKEDA 529
Cdd:PRK12852 481 AQTEEYVDMVAKGIIDPAKVVRTALQDAASVAGLLVTTEAMVAELPKKDA 530
|
|
| groEL |
PRK12851 |
chaperonin GroEL; Reviewed |
1-529 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 171770 Cd Length: 541 Bit Score: 804.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 1 MAAKDVVFGDSARAKMVEGVNILANAVKVTLGPKGRNVVLERSFGGPTVTKDGVSVAKEIELKDKLQNMGAQMVKEVASK 80
Cdd:PRK12851 1 MAAKEVKFHVEAREKMLRGVNILADAVKVTLGPKGRNVVIDKSFGAPTITNDGVTIAKEIELEDKFENMGAQMVREVASK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 81 TSDNAGDGTTTATVLAQSIVREGMKYVASGMNPMDLKRGIDKAVAAAIEELRKISKPCTTNKEIAQVGAISANSDTSIGD 160
Cdd:PRK12851 81 TNDVAGDGTTTATVLAQAIVREGAKAVAAGANPMDLKRGIDRAVAAVVEELKANARPVTTNAEIAQVATISANGDAEIGR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 161 RIAEAMDKVGKEGVITVEDGKSLQDELDVVEGMQFDRGYLSPYFINNPDKQVAVLDNPFVLLHDKKVSNIRDLLPILEQV 240
Cdd:PRK12851 161 LVAEAMEKVGNEGVITVEESKTAETELEVVEGMQFDRGYLSPYFVTDADKMEAELEDPYILIHEKKISNLQDLLPVLEAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 241 AKAGRPLLIIAEDVEGEALATLVVNNIRGILKTVAVKAPGFGDRRKAMLEDIAILTGGQVIAEETGLTLEKATLNELGQA 320
Cdd:PRK12851 241 VQSGKPLLIIAEDVEGEALATLVVNKLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGIKLENVTLEQLGRA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 321 KRIEVGKENTTIIDGAGEAASIEARVKQVRTQIEEATSDYDREKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVEDAL 400
Cdd:PRK12851 321 KKVVVEKENTTIIDGAGSKTEIEGRVAQIRAQIEETTSDYDREKLQERLAKLAGGVAVIRVGASTEVEVKEKKDRVDDAL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 401 HATRAAVEEGIVAGGGVALIRARSAIGSVKGDNPDQDAGIKIVLRAMEEPLRQIVTNGGEEASVVVAAVAAGTGNYGYNA 480
Cdd:PRK12851 401 HATRAAVEEGIVPGGGVALLRAVKALDKLETANGDQRTGVEIVRRALEAPVRQIAENAGAEGSVVVGKLREKPGGYGFNA 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1878327742 481 ATGEYGDLVEAGVVDPTKVTRTALQNAASVAGLLLTTDAAVCELPKEDA 529
Cdd:PRK12851 481 ATNEYGDLYAQGVIDPVKVVRTALQNAASVAGLLLTTEAMVAEKPKKEP 529
|
|
| GroEL |
COG0459 |
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ... |
2-529 |
0e+00 |
|
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227 Cd Length: 497 Bit Score: 764.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 2 AAKDVVFGDSARAKMVEGVNILANAVKVTLGPKGRNVVLERSFGGPTVTKDGVSVAKEIELKDKLQNMGAQMVKEVASKT 81
Cdd:COG0459 1 MAKQILFGEDARRANIRGVKALADAVKVTLGPKGRNVMLVKSFGDPTITNDGVTIAKEIELEDPFENMGAQLVKEVASKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 82 SDNAGDGTTTATVLAQSIVREGMKYVASGMNPMDLKRGIDKAVAAAIEELRKISKPCTTNKEIAQVGAISANSDTSIGDR 161
Cdd:COG0459 81 NDEAGDGTTTATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPVDDKEELAQVATISANGDEEIGEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 162 IAEAMDKVGKEGVITVEDGKSLQDELDVVEGMQFDRGYLSPYFINNPDKQVAVLDNPFVLLHDKKVSNIRDLLPILEQVA 241
Cdd:COG0459 161 IAEAMEKVGKDGVITVEEGKGLETELEVVEGMQFDKGYLSPYFVTDPEKMPAELENAYILLTDKKISSIQDLLPLLEKVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 242 KAGRPLLIIAEDVEGEALATLVVNNIRGILKTVAVKAPGFGDRRKAMLEDIAILTGGQVIAEETGLTLEKATLNELGQAK 321
Cdd:COG0459 241 QSGKPLLIIAEDIDGEALATLVVNGIRGVLRVVAVKAPGFGDRRKAMLEDIAILTGGRVISEDLGLKLEDVTLDDLGRAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 322 RIEVGKENTTIIDGAGEAASIearvkqvrtqieeatsdydreklqervaklaggvaVIKVGAATEVEMKEKKARVEDALH 401
Cdd:COG0459 321 RVEVDKDNTTIVEGAGNPKAI-----------------------------------VILVGAATEVEVKERKRRVEDALH 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 402 ATRAAVEEGIVAGGGVALIRARSAIGSVKGD-NPDQDAGIKIVLRAMEEPLRQIVTNGGEEASVVVAAVAAGT-GNYGYN 479
Cdd:COG0459 366 ATRAAVEEGIVPGGGAALLRAARALRELAAKlEGDEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKVRAAKdKGFGFD 445
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1878327742 480 AATGEYGDLVEAGVVDPTKVTRTALQNAASVAGLLLTTDAAVCELPKEDA 529
Cdd:COG0459 446 AATGEYVDMLEAGVIDPAKVKRSALQNAASVAGLILTTEAVIADKPEKEE 495
|
|
| PTZ00114 |
PTZ00114 |
Heat shock protein 60; Provisional |
2-529 |
0e+00 |
|
Heat shock protein 60; Provisional
Pssm-ID: 185455 Cd Length: 555 Bit Score: 733.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 2 AAKDVVFGDSARAKMVEGVNILANAVKVTLGPKGRNVVLERSFGGPTVTKDGVSVAKEIELKDKLQNMGAQMVKEVASKT 81
Cdd:PTZ00114 13 KGKEIRFGDEARQSLLKGIERLADAVAVTLGPKGRNVIIEQEYGSPKITKDGVTVAKAIEFSDRFENVGAQLIRQVASKT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 82 SDNAGDGTTTATVLAQSIVREGMKYVASGMNPMDLKRGIDKAVAAAIEELRKISKPCTTNKEIAQVGAISANSDTSIGDR 161
Cdd:PTZ00114 93 NDKAGDGTTTATILARAIFREGCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQSRPVKTKEDILNVATISANGDVEIGSL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 162 IAEAMDKVGKEGVITVEDGKSLQDELDVVEGMQFDRGYLSPYFINNPDKQVAVLDNPFVLLHDKKVSNIRDLLPILEQVA 241
Cdd:PTZ00114 173 IADAMDKVGKDGTITVEDGKTLEDELEVVEGMSFDRGYISPYFVTNEKTQKVELENPLILVTDKKISSIQSILPILEHAV 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 242 KAGRPLLIIAEDVEGEALATLVVNNIRGILKTVAVKAPGFGDRRKAMLEDIAILTGGQVIAEE-TGLTLEKATLNELGQA 320
Cdd:PTZ00114 253 KNKRPLLIIAEDVEGEALQTLIINKLRGGLKVCAVKAPGFGDNRKDILQDIAVLTGATVVSEDnVGLKLDDFDPSMLGSA 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 321 KRIEVGKENTTIIDGAGEAASIEARVKQVRTQIEEATSDYDREKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVEDAL 400
Cdd:PTZ00114 333 KKVTVTKDETVILTGGGDKAEIKERVELLRSQIERTTSEYDKEKLKERLAKLSGGVAVIKVGGASEVEVNEKKDRIEDAL 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 401 HATRAAVEEGIVAGGGVALIRARSAIGSVKGDN---PDQDAGIKIVLRAMEEPLRQIVTNGGEEASVVVAA-VAAGTGNY 476
Cdd:PTZ00114 413 NATRAAVEEGIVPGGGVALLRASKLLDKLEEDNeltPDQRTGVKIVRNALRLPTKQIAENAGVEGAVVVEKiLEKKDPSF 492
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1878327742 477 GYNAATGEYGDLVEAGVVDPTKVTRTALQNAASVAGLLLTTDAAVCELPKEDA 529
Cdd:PTZ00114 493 GYDAQTGEYVNMFEAGIIDPTKVVRSALVDAASVASLMLTTEAAIVDLPKEKK 545
|
|
| groEL |
CHL00093 |
chaperonin GroEL |
3-528 |
0e+00 |
|
chaperonin GroEL
Pssm-ID: 177025 Cd Length: 529 Bit Score: 664.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 3 AKDVVFGDSARAKMVEGVNILANAVKVTLGPKGRNVVLERSFGGPTVTKDGVSVAKEIELKDKLQNMGAQMVKEVASKTS 82
Cdd:CHL00093 2 SKKILYQDNARRALERGMDILAEAVSVTLGPKGRNVVLEKKYGSPQIVNDGVTIAKEIELEDHIENTGVALIRQAASKTN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 83 DNAGDGTTTATVLAQSIVREGMKYVASGMNPMDLKRGIDKAVAAAIEELRKISKPCTTNKEIAQVGAISANSDTSIGDRI 162
Cdd:CHL00093 82 DVAGDGTTTATVLAYAIVKQGMKNVAAGANPISLKRGIEKATQYVVSQIAEYARPVEDIQAITQVASISAGNDEEVGSMI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 163 AEAMDKVGKEGVITVEDGKSLQDELDVVEGMQFDRGYLSPYFINNPDKQVAVLDNPFVLLHDKKVSNIR-DLLPILEQVA 241
Cdd:CHL00093 162 ADAIEKVGREGVISLEEGKSTVTELEITEGMRFEKGFISPYFVTDTERMEVVQENPYILLTDKKITLVQqDLLPILEQVT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 242 KAGRPLLIIAEDVEGEALATLVVNNIRGILKTVAVKAPGFGDRRKAMLEDIAILTGGQVIAEETGLTLEKATLNELGQAK 321
Cdd:CHL00093 242 KTKRPLLIIAEDVEKEALATLVLNKLRGIVNVVAVRAPGFGDRRKAMLEDIAILTGGQVITEDAGLSLETIQLDLLGQAR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 322 RIEVGKENTTIIdGAGEAASIEARVKQVRTQIEEATSDYDREKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVEDALH 401
Cdd:CHL00093 322 RIIVTKDSTTII-ADGNEEQVKARCEQLRKQIEIADSSYEKEKLQERLAKLSGGVAVIKVGAATETEMKDKKLRLEDAIN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 402 ATRAAVEEGIVAGGGVALIRARSAIGSVKGDN--PDQDAGIKIVLRAMEEPLRQIVTNGGEEASVVVAAVAAGTGNYGYN 479
Cdd:CHL00093 401 ATKAAVEEGIVPGGGATLVHLSENLKTWAKNNlkEDELIGALIVARAILAPLKRIAENAGKNGSVIIEKVQEQDFEIGYN 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1878327742 480 AATGEYGDLVEAGVVDPTKVTRTALQNAASVAGLLLTTDAAVCELPKED 528
Cdd:CHL00093 481 AANNKFVNMYEAGIIDPAKVTRSALQNAASIASMILTTECIIVDKKESS 529
|
|
| PRK14104 |
PRK14104 |
chaperonin GroEL; Provisional |
1-529 |
0e+00 |
|
chaperonin GroEL; Provisional
Pssm-ID: 172594 Cd Length: 546 Bit Score: 659.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 1 MAAKDVVFGDSARAKMVEGVNILANAVKVTLGPKGRNVVLERSFGGPTVTKDGVSVAKEIELKDKLQNMGAQMVKEVASK 80
Cdd:PRK14104 1 MSAKEVKFGVDARDRMLRGVDILANAVKVTLGPKGRNVVLDKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVREVASK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 81 TSDNAGDGTTTATVLAQSIVREGMKYVASGMNPMDLKRGIDKAVAAAIEELRKISKPCTTNKEIAQVGAISANSDTSIGD 160
Cdd:PRK14104 81 SADAAGDGTTTATVLAQAIVREGAKSVAAGMNPMDLKRGIDLAVEAVVADLVKNSKKVTSNDEIAQVGTISANGDAEIGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 161 RIAEAMDKVGKEGVITVEDGKSLQDELDVVEGMQFDRGYLSPYFINNPDKQVAVLDNPFVLLHDKKVSNIRDLLPILEQV 240
Cdd:PRK14104 161 FLADAMKKVGNEGVITVEEAKSLETELDVVEGMQFDRGYISPYFVTNADKMRVEMDDAYILINEKKLSSLNELLPLLEAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 241 AKAGRPLLIIAEDVEGEALATLVVNNIRGILKTVAVKAPGFGDRRKAMLEDIAILTGGQVIAEETGLTLEKATLNELGQA 320
Cdd:PRK14104 241 VQTGKPLVIVAEDVEGEALATLVVNRLRGGLKVAAVKAPGFGDRRKAMLQDIAILTGGQAISEDLGIKLENVTLQMLGRA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 321 KRIEVGKENTTIIDGAGEAASIEARVKQVRTQIEEATSDYDREKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVEDAL 400
Cdd:PRK14104 321 KKVMIDKENTTIVNGAGKKADIEARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKERKDRVDDAM 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 401 HATRAAVEEGIVAGGGVALIRARSAIGSVKGDNPDQDAGIKIVLRAMEEPLRQIVTNGGEEASVVVAAVAAGTG-NYGYN 479
Cdd:PRK14104 401 HATRAAVEEGIVPGGGVALLRASEQLKGIKTKNDDQKTGVEIVRKALSAPARQIAINAGEDGSVIVGKILEKEQySYGFD 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1878327742 480 AATGEYGDLVEAGVVDPTKVTRTALQNAASVAGLLLTTDAAVCELPKEDA 529
Cdd:PRK14104 481 SQTGEYGNLVSKGIIDPTKVVRTAIQNAASVAALLITTEAMVAELPKKGG 530
|
|
| PLN03167 |
PLN03167 |
Chaperonin-60 beta subunit; Provisional |
2-529 |
0e+00 |
|
Chaperonin-60 beta subunit; Provisional
Pssm-ID: 215611 [Multi-domain] Cd Length: 600 Bit Score: 535.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 2 AAKDVVFGD--SARAKMVEGVNILANAVKVTLGPKGRNVVLERSFGGPTVTKDGVSVAKEIELKDKLQNMGAQMVKEVAS 79
Cdd:PLN03167 55 AAKELHFNKdgSAIKKLQAGVNKLADLVGVTLGPKGRNVVLESKYGSPKIVNDGVTVAKEVELEDPVENIGAKLVRQAAA 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 80 KTSDNAGDGTTTATVLAQSIVREGMKYVASGMNPMDLKRGIDKAVAAAIEELRKISKPcTTNKEIAQVGAISANSDTSIG 159
Cdd:PLN03167 135 KTNDLAGDGTTTSVVLAQGLIAEGVKVVAAGANPVQITRGIEKTAKALVKELKKMSKE-VEDSELADVAAVSAGNNYEVG 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 160 DRIAEAMDKVGKEGVITVEDGKSLQDELDVVEGMQFDRGYLSPYFINNPDKQVAVLDNPFVLLHDKKVSNIRDLLPILEQ 239
Cdd:PLN03167 214 NMIAEAMSKVGRKGVVTLEEGKSAENNLYVVEGMQFDRGYISPYFVTDSEKMSVEYDNCKLLLVDKKITNARDLIGILED 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 240 VAKAGRPLLIIAEDVEGEALATLVVNNIRGILKTVAVKAPGFGDRRKAMLEDIAILTGGQVIAEETGLTLEKATLNELGQ 319
Cdd:PLN03167 294 AIRGGYPLLIIAEDIEQEALATLVVNKLRGSLKIAALKAPGFGERKSQYLDDIAILTGGTVIREEVGLSLDKVGKEVLGT 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 320 AKRIEVGKENTTIIDGAGEAASIEARVKQVRTQIEEATSDYDREKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVEDA 399
Cdd:PLN03167 374 AAKVVLTKDTTTIVGDGSTQEAVNKRVAQIKNLIEAAEQDYEKEKLNERIAKLSGGVAVIQVGAQTETELKEKKLRVEDA 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 400 LHATRAAVEEGIVAGGGVALIRARSAIGSVKG--DNPDQDAGIKIVLRAMEEPLRQIVTNGGEEASVVVAAVAAGTG-NY 476
Cdd:PLN03167 454 LNATKAAVEEGIVVGGGCTLLRLASKVDAIKDtlENDEQKVGADIVKRALSYPLKLIAKNAGVNGSVVSEKVLSNDNpKF 533
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1878327742 477 GYNAATGEYGDLVEAGVVDPTKVTRTALQNAASVAGLLLTTDAAVCELPKEDA 529
Cdd:PLN03167 534 GYNAATGKYEDLMAAGIIDPTKVVRCCLEHAASVAKTFLTSDCVVVEIKEPEP 586
|
|
| chaperonin_type_I_II |
cd00309 |
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ... |
4-521 |
1.19e-148 |
|
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: 434.93 E-value: 1.19e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 4 KDVVFGDSARAKMVEGVNILANAVKVTLGPKGRNVVLERSFGGPTVTKDGVSVAKEIELkdklQNMGAQMVKEVASKTSD 83
Cdd:cd00309 1 KEREFGEEARLSNINAAKALADAVKTTLGPKGMDKMLVDSLGDPTITNDGATILKEIEV----EHPAAKLLVEVAKSQDD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 84 NAGDGTTTATVLAQSIVREGMKYVASGMNPMDLKRGIDKAVAAAIEELRKISKP--CTTNKEIAQVGAISANS------D 155
Cdd:cd00309 77 EVGDGTTTVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVPidVEDREELLKVATTSLNSklvsggD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 156 TSIGDRIAEAMDKVGKE------GVITVEDGKS---LQDELdvVEGMQFDRGYLSPYFInnpdkqvAVLDNPFVLLHDKK 226
Cdd:cd00309 157 DFLGELVVDAVLKVGKEngdvdlGVIRVEKKKGgslEDSEL--VVGMVFDKGYLSPYMP-------KRLENAKILLLDCK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 227 VSNirdllpileqvakagrplLIIAED-VEGEALATLVVNNIrgilktVAVKApgfgdRRKAMLEDIAILTGGQVIAeet 305
Cdd:cd00309 228 LEY------------------VVIAEKgIDDEALHYLAKLGI------MAVRR-----VRKEDLERIAKATGATIVS--- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 306 glTLEKATLNELGQAKRIEVGK----ENTTIIDGAGeaasiearvkqvrtqieeatsdydreklqervaklaGGVAVIKV 381
Cdd:cd00309 276 --RLEDLTPEDLGTAGLVEETKigdeKYTFIEGCKG------------------------------------GKVATILL 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 382 GAATEVEMKEKKARVEDALHATRAAVEE-GIVAGGGVALIRARSAIGSV-KGDNPDQDAGIKIVLRAMEEPLRQIVTNGG 459
Cdd:cd00309 318 RGATEVELDEAERSLHDALCAVRAAVEDgGIVPGGGAAEIELSKALEELaKTLPGKEQLGIEAFADALEVIPRTLAENAG 397
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1878327742 460 EEASVV----VAAVAAGTGNYGYNAATGEYGDLVEAGVVDPTKVTRTALQNAASVAGLLLTTDAAV 521
Cdd:cd00309 398 LDPIEVvtklRAKHAEGGGNAGGDVETGEIVDMKEAGIIDPLKVKRQALKSATEAASLILTIDDII 463
|
|
| Cpn60_TCP1 |
pfam00118 |
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ... |
23-521 |
8.84e-83 |
|
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: 266.38 E-value: 8.84e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 23 LANAVKVTLGPKGRNVVLERSFGGPTVTKDGVSVAKEIELkdklQNMGAQMVKEVASKTSDNAGDGTTTATVLAQSIVRE 102
Cdd:pfam00118 1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELEI----QHPAAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 103 GMKYVASGMNPMDLKRGIDKAVAAAIEELRKI-SKPCTTN--KEIAQVGAISANSDTS------IGDRIAEA-------- 165
Cdd:pfam00118 77 AEKLLAAGVHPTTIIEGYEKALEKALEILDSIiSIPVEDVdrEDLLKVARTSLSSKIIsresdfLAKLVVDAvlaipknd 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 166 -MDKVGKEGVITVEdGKSLQDeLDVVEGMQFDRGYLSPyfinnpdKQVAVLDNPFVLLHDKKVSNIRD------------ 232
Cdd:pfam00118 157 gSFDLGNIGVVKIL-GGSLED-SELVDGVVLDKGPLHP-------DMPKRLENAKVLLLNCSLEYEKTetkatvvlsdae 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 233 ------------LLPILEQVAKAGRPLLIIAEDVEGEALATLVVNNIRGILKTvavkapgfgdrRKAMLEDIAILTGGQV 300
Cdd:pfam00118 228 qlerflkaeeeqILEIVEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMALRRV-----------KKRDLERLAKATGARA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 301 IAEETGLTLEkatlnELGQAKRIE---VGKENTTIIDGAGEaasiearvkqvrtqieeatsdydreklqervaklaGGVA 377
Cdd:pfam00118 297 VSSLDDLTPD-----DLGTAGKVEeekIGDEKYTFIEGCKS-----------------------------------PKAA 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 378 VIKVGAATEVEMKEKKARVEDALHATRAAVEE-GIVAGGGVALIRARSAIGSVKGDNPDQDA-GIKIVLRAMEEPLRQIV 455
Cdd:pfam00118 337 TILLRGATDHVLDEIERSIHDALCVVKNAIEDpRVVPGGGAVEMELARALREYAKSVSGKEQlAIEAFAEALEVIPKTLA 416
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 456 TNGG----EEASVVVAAVAAGTGNYGYNAATGEYGDLVEAGVVDPTKVTRTALQNAASVAGLLLTTDAAV 521
Cdd:pfam00118 417 ENAGldpiEVLAELRAAHASGEKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKSATEAASTILRIDDII 486
|
|
| chaperonin_like |
cd03333 |
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ... |
142-409 |
5.10e-40 |
|
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: 144.15 E-value: 5.10e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 142 KEIAQVGAISANS-----DTSIGDRIAEAMDKVGKE------GVITVEDGKS---LQDELdvVEGMQFDRGYLSPYFInn 207
Cdd:cd03333 2 ELLLQVATTSLNSklsswDDFLGKLVVDAVLKVGPDnrmddlGVIKVEKIPGgslEDSEL--VVGVVFDKGYASPYMP-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 208 pdkqvAVLDNPFVLLHDKKVSNirdllpileqvakagrplLIIAED-VEGEALATLVVNNIrgilktVAVKApgfgdRRK 286
Cdd:cd03333 78 -----KRLENAKILLLDCPLEY------------------VVIAEKgIDDLALHYLAKAGI------MAVRR-----VKK 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 287 AMLEDIAILTGGQVIAeetglTLEKATLNELGQAKRIEV----GKENTTIIDGAGeaasiearvkqvrtqieeatsdydr 362
Cdd:cd03333 124 EDLERIARATGATIVS-----SLEDLTPEDLGTAELVEEtkigEEKLTFIEGCKG------------------------- 173
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1878327742 363 eklqervaklaGGVAVIKVGAATEVEMKEKKARVEDALHATRAAVEE 409
Cdd:cd03333 174 -----------GKAATILLRGATEVELDEVKRSLHDALCAVRAAVEE 209
|
|
| cpn60 |
cd03343 |
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ... |
9-518 |
1.78e-22 |
|
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: 100.80 E-value: 1.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 9 GDSARAKMVEGVNILANAVKVTLGPKGRNVVLERSFGGPTVTKDGVSVAKEIELkdklQNMGAQMVKEVASKTSDNAGDG 88
Cdd:cd03343 13 GRDAQRMNIAAAKAVAEAVRTTLGPKGMDKMLVDSLGDVTITNDGATILKEMDI----EHPAAKMLVEVAKTQDEEVGDG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 89 TTTATVLAQSIVREGMKYVASGMNPMDLKRGIDKAVAAAIEELRKISKPCTTN-----KEIAQV---GAISANSDTSIGD 160
Cdd:cd03343 89 TTTAVVLAGELLEKAEDLLDQNIHPTVIIEGYRLAAEKALELLDEIAIKVDPDdkdtlRKIAKTsltGKGAEAAKDKLAD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 161 RIAEAMDKVGKEG-----------VITVEDGKSLqDELDVVEGMQFDRGYLSPyfiNNPDK----QVAVLDNPFVLLHDK 225
Cdd:cd03343 169 LVVDAVLQVAEKRdgkyvvdldniKIEKKTGGSV-DDTELIRGIVIDKEVVHP---GMPKRvenaKIALLDAPLEVKKTE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 226 KVSNIR----------------DLLPILEQVAKAGRPLLIIAEDVEGEALATLVVnniRGILKTVAVKapgfgdrrKAML 289
Cdd:cd03343 245 IDAKIRitspdqlqafleqeeaMLKEMVDKIADTGANVVFCQKGIDDLAQHYLAK---AGILAVRRVK--------KSDM 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 290 EDIAILTGGQVIAeetglTLEKATLNELGQAKRIE---VGKENTTIIDGAGEAASIearvkqvrtqieeatsdydreklq 366
Cdd:cd03343 314 EKLARATGAKIVT-----NIDDLTPEDLGEAELVEerkVGDDKMVFVEGCKNPKAV------------------------ 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 367 ervaklaggvaVIKVGAATEVEMKEKKARVEDALHATRAAVEEG-IVAGGGVALI----RARSAIGSVKGDnpDQDAgIK 441
Cdd:cd03343 365 -----------TILLRGGTEHVVDELERALEDALRVVADALEDGkVVAGGGAVEIelakRLREYARSVGGR--EQLA-VE 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 442 IVLRAMEEPLRQIVTNGGEEA----SVVVAAVAAGTGNYGYNAATGEYGDLVEAGVVDPTKVTRTALQNAASVAGLLLTT 517
Cdd:cd03343 431 AFADALEEIPRTLAENAGLDPidtlVELRAAHEKGNKNAGLDVYTGEVVDMLEKGVIEPLRVKKQAIKSATEAATMILRI 510
|
.
gi 1878327742 518 D 518
Cdd:cd03343 511 D 511
|
|
| chap_CCT_epsi |
TIGR02343 |
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ... |
23-333 |
7.77e-15 |
|
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: 77.15 E-value: 7.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 23 LANAVKVTLGPKGRNVVLERSFGGPTVTKDGVSVAKEIELkdklQNMGAQMVKEVASKTSDNAGDGTTTATVLAQSIVRE 102
Cdd:TIGR02343 39 VASILRTSLGPKGMDKMLISPDGDITVTNDGATILSQMDV----DNQIAKLMVELSKSQDDEIGDGTTGVVVLAGALLEQ 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 103 GMKYVASGMNPMDLKRGIDKAVAAAIEELRKISKPCTTNKEIAQVGAISANsdTSIGDRIA----EAMDKVGKEGVITVE 178
Cdd:TIGR02343 115 AEELLDKGIHPIKIADGFEEAARIAVEHLEEISDEISADNNNREPLIQAAK--TSLGSKIVskchRRFAEIAVDAVLNVA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 179 D-----------------GKSLQDElDVVEGMQFDRGYLSPYFINN-PDKQVAVLDNPF-----VLLHDKKVSNIRD--- 232
Cdd:TIGR02343 193 DmerrdvdfdlikvegkvGGSLEDT-KLIKGIIIDKDFSHPQMPKEvEDAKIAILTCPFeppkpKTKHKLDISSVEEykk 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 233 --------LLPILEQVAKAGRPLLIIAEDVEGEALATLVVNNIRgilktvAVKAPGFGDrrkamLEDIAILTGGQVIAEE 304
Cdd:TIGR02343 272 lqkyeqqkFKEMIDDIKKSGANLVICQWGFDDEANHLLLQNDLP------AVRWVGGQE-----LELIAIATGGRIVPRF 340
|
330 340
....*....|....*....|....*....
gi 1878327742 305 TGLTLEKatLNELGQAKRIEVGKENTTII 333
Cdd:TIGR02343 341 QELSKDK--LGKAGLVREISFGTTKDRML 367
|
|
| TCP1_beta |
cd03336 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ... |
9-143 |
2.91e-14 |
|
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: 75.44 E-value: 2.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 9 GDSARAKMVEGVNILANAVKVTLGPKGRNVVLERSF--GGPTVTKDGVSVAKEIelkdKLQNMGAQMVKEVASKTSDNAG 86
Cdd:cd03336 11 GETARLSSFVGAIAIGDLVKTTLGPKGMDKILQSVGrsGGVTVTNDGATILKSI----GVDNPAAKVLVDISKVQDDEVG 86
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1878327742 87 DGTTTATVLAQSIVREGMKYVASGMNPMDLKRGIDKAVAAAIEELRKISKPCTTNKE 143
Cdd:cd03336 87 DGTTSVTVLAAELLREAEKLVAQKIHPQTIIEGYRMATAAAREALLSSAVDHSSDEE 143
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
9-143 |
1.99e-13 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 72.75 E-value: 1.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 9 GDSARAKMVEGVNILANAVKVTLGPKGRNVVLERSFGGP-----TVTKDGVSVAKEIelkdKLQNMGAQMVKEVaSKTSD 83
Cdd:PTZ00212 20 GETARLQSFVGAIAVADLVKTTLGPKGMDKILQPMSEGPrsgnvTVTNDGATILKSV----WLDNPAAKILVDI-SKTQD 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1878327742 84 N-AGDGTTTATVLAQSIVREGMKYVASGMNPMDLKRGIDKAVAAAIEELRKISKPCTTNKE 143
Cdd:PTZ00212 95 EeVGDGTTSVVVLAGELLREAEKLLDQKIHPQTIIEGWRMALDVARKALEEIAFDHGSDEE 155
|
|
| chap_CCT_eta |
TIGR02345 |
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ... |
23-135 |
3.23e-12 |
|
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: 69.02 E-value: 3.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 23 LANAVKVTLGPKGRNVVLERSFGGPTVTKDGVSVAKEIELKdklqNMGAQMVKEVASKTSDNAGDGTTTATVLAQSIVRE 102
Cdd:TIGR02345 30 IAEALKTTLGPRGMDKLIVGSNGKATISNDGATILKLLDIV----HPAAKTLVDIAKSQDAEVGDGTTSVTILAGELLKE 105
|
90 100 110
....*....|....*....|....*....|...
gi 1878327742 103 GMKYVASGMNPMDLKRGIDKAVAAAIEELRKIS 135
Cdd:TIGR02345 106 AKPFIEEGVHPQLIIRCYREALSLAVEKIKEIA 138
|
|
| TCP1_eta |
cd03340 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ... |
13-135 |
8.61e-12 |
|
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: 67.70 E-value: 8.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 13 RAKMVEGVN---ILANAVKVTLGPKGRNVVLERSFGGPTVTKDGVSVAKEIELKdklqNMGAQMVKEVASKTSDNAGDGT 89
Cdd:cd03340 15 KGQLISNINacqAIADAVRTTLGPRGMDKLIVDGRGKVTISNDGATILKLLDIV----HPAAKTLVDIAKSQDAEVGDGT 90
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1878327742 90 TTATVLAQSIVREGMKYVASGMNPMDLKRGIDKAVAAAIEELRKIS 135
Cdd:cd03340 91 TSVVVLAGEFLKEAKPFIEDGVHPQIIIRGYRKALQLAIEKIKEIA 136
|
|
| chap_CCT_beta |
TIGR02341 |
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ... |
9-526 |
1.87e-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: 66.42 E-value: 1.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 9 GDSARAKMVEGVNILANAVKVTLGPKGRNVVLER--SFGGPTVTKDGVSVAKEIelkdKLQNMGAQMVKEVASKTSDNAG 86
Cdd:TIGR02341 12 AENARLSSFVGAIAIGDLVKSTLGPKGMDKILQSssSDASIMVTNDGATILKSI----GVDNPAAKVLVDMSKVQDDEVG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 87 DGTTTATVLAQSIVREGMKYVASGMNPMDLKRGIDKAVAAAIEELRKISKPCTTNKEIAQVGAISAnSDTSIGDRI---- 162
Cdd:TIGR02341 88 DGTTSVTVLAAELLREAEKLINQKIHPQTIIAGYREATKAARDALLKSAVDNGSDEVKFRQDLMNI-ARTTLSSKIlsqh 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 163 AEAMDKVGKEGVITVEDGKSLqDELDVVE--GMQFDRGYLSPYFINNP---DKQVAVLDNPFVLLH------DK-KVSNI 230
Cdd:TIGR02341 167 KDHFAQLAVDAVLRLKGSGNL-EAIQIIKklGGSLADSYLDEGFLLDKkigVNQPKRIENAKILIAntgmdtDKvKIFGS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 231 R---DLLPILEQVAKAGRPLL------IIAEDVEGEALATLVVNNIRGILKTVAVKAPGFGDRRKamLEDIAILTGGQVI 301
Cdd:TIGR02341 246 RvrvDSTAKVAELEHAEKEKMkekvekILKHGINCFINRQLIYNYPEQLFADAGVMAIEHADFEG--VERLALVTGGEIV 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 302 AeetglTLEKATLNELGQAKRIE---VGKENTTIIDG--AGEAASIEARvkqvrtqieeatsdydreklqervaklaggv 376
Cdd:TIGR02341 324 S-----TFDHPELVKLGSCDLIEeimIGEDKLLKFSGvkLGEACTIVLR------------------------------- 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 377 avikvgAATEVEMKEKKARVEDALHATRAAVEEG-IVAGGGVALIRARSAIGSVKGDNPDQDAgikIVLRAMEEPLRQIV 455
Cdd:TIGR02341 368 ------GATQQILDEAERSLHDALCVLSQTVKESrTVLGGGCSEMLMSKAVTQEAQRTPGKEA---LAVEAFARALRQLP 438
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1878327742 456 T----NGG----EEASVVVAAVAAGTGNYGYNAATGEYGDLVEAGVVDPTKVTRTALQNAASVAGLLLTTDAAVCELPK 526
Cdd:TIGR02341 439 TiiadNAGfdsaELVAQLRAAHYNGNTTMGLDMNEGTIADMRQLGITESYKVKRAVVSSAAEAAEVILRVDNIIKAAPR 517
|
|
| TCP1_epsilon |
cd03339 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ... |
13-324 |
7.74e-11 |
|
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: 64.63 E-value: 7.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 13 RAKMVEGV--NIL-----ANAVKVTLGPKGRNVVLERSFGGPTVTKDGVSVAKEIELkdklQNMGAQMVKEVASKTSDNA 85
Cdd:cd03339 18 RLKGLEAHksHILaaksvANILRTSLGPRGMDKILVSPDGEVTVTNDGATILEKMDV----DHQIAKLLVELSKSQDDEI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 86 GDGTTTATVLAQSIVREGMKYVASGMNPMDLKRGIDKAVAAAIEELRKISKPCTTNKEiaQVGAISANSDTSIGDRIA-- 163
Cdd:cd03339 94 GDGTTGVVVLAGALLEQAEKLLDRGIHPIRIADGYEQACKIAVEHLEEIADKIEFSPD--NKEPLIQTAMTSLGSKIVsr 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 164 --EAMDKVGKEGVITVED-----------------GKSLQDElDVVEGMQFDRGYLSPYFINN-PDKQVAVLDNPFV--- 220
Cdd:cd03339 172 chRQFAEIAVDAVLSVADlerkdvnfelikvegkvGGRLEDT-KLVKGIVIDKDFSHPQMPKEvKDAKIAILTCPFEppk 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 221 -----LLHDKKVSNIRDL--------LPILEQVAKAGRPLLIIAEDVEGEALATLVVNNIRgilktvAVKAPGFGDrrka 287
Cdd:cd03339 251 pktkhKLDITSVEDYKKLqeyeqkyfREMVEQVKDAGANLVICQWGFDDEANHLLLQNGLP------AVRWVGGVE---- 320
|
330 340 350
....*....|....*....|....*....|....*..
gi 1878327742 288 mLEDIAILTGGQVIAEETGLTLEKatlneLGQAKRIE 324
Cdd:cd03339 321 -IELIAIATGGRIVPRFEDLSPEK-----LGKAGLVR 351
|
|
| TCP1_delta |
cd03338 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ... |
23-143 |
2.77e-10 |
|
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: 62.69 E-value: 2.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 23 LANAVKVTLGPKGRNVVLERSFGGPTVTKDGVSVAKEIelkdKLQNMGAQMVKEVaSKTSD-NAGDGTTTATVLAQSIVR 101
Cdd:cd03338 20 VADAIRTSLGPRGMDKMIQTGKGEVIITNDGATILKQM----SVLHPAAKMLVEL-SKAQDiEAGDGTTSVVVLAGALLS 94
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1878327742 102 EGMKYVASGMNPMDLKRGIDKAVAAAIEELRKISKPCT-TNKE 143
Cdd:cd03338 95 ACESLLKKGIHPTVISESFQIAAKKAVEILDSMSIPVDlNDRE 137
|
|
| chap_CCT_gamma |
TIGR02344 |
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ... |
23-189 |
3.11e-10 |
|
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: 62.45 E-value: 3.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 23 LANAVKVTLGPKGRNVVLERSFGGPTVTKDGVSVAKEIELkdklQNMGAQMVKEVASKTSDNAGDGTTTATVLAQSIVRE 102
Cdd:TIGR02344 28 VADIIRTCLGPRSMLKMLLDPMGGIVMTNDGNAILREIDV----AHPAAKSMIELSRTQDEEVGDGTTSVIILAGEMLSV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 103 GMKYVASGMNPMDLKRGIDKAVAAAIEELRKISKPCTTNKEIAQVGAISANSDTSIGDRIAEAMDKVGKEGVITVEDGKS 182
Cdd:TIGR02344 104 AEPFLEQNIHPTVIIRAYRKALDDALSVLEEISIPVDVNDDAAMLKLIQSCIGTKFVSRWSDLMCDLALDAVRTVQRDEN 183
|
....*..
gi 1878327742 183 LQDELDV 189
Cdd:TIGR02344 184 GRKEIDI 190
|
|
| chap_CCT_zeta |
TIGR02347 |
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ... |
10-144 |
3.44e-10 |
|
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: 62.44 E-value: 3.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 10 DSARAKMVEGVNI-----LANAVKVTLGPKGRNVVLERSFGGPTVTKDGVSVAKEIELkdklQNMGAQMVKEVASKTSDN 84
Cdd:TIGR02347 10 ESLRRDAALMMNInaargLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEMQI----QHPTASMIARAATAQDDI 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1878327742 85 AGDGTTTATVLAQSIVREGMKYVASGMNPMDLKRGIDKAVAAAIEELR--KISKPCTTNKEI 144
Cdd:TIGR02347 86 TGDGTTSTVLLIGELLKQAERYILEGVHPRIITEGFEIARKEALQFLDkfKVKKEDEVDREF 147
|
|
| chap_CCT_alpha |
TIGR02340 |
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ... |
9-113 |
2.69e-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: 59.73 E-value: 2.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 9 GDSARAKMVEGVNILANAVKVTLGPKGRNVVLERSFGGPTVTKDGVSVAKEIELKDKlqnmGAQMVKEVASKTSDNAGDG 88
Cdd:TIGR02340 10 GQDVRTQNVTAAMAIANIVKTSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHP----AAKILVELAQLQDREVGDG 85
|
90 100
....*....|....*....|....*
gi 1878327742 89 TTTATVLAQSIVREGMKYVASGMNP 113
Cdd:TIGR02340 86 TTSVVIIAAELLKRADELVKNKIHP 110
|
|
| chap_CCT_delta |
TIGR02342 |
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ... |
8-137 |
7.19e-09 |
|
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: 58.26 E-value: 7.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 8 FGDSARAKMVEGVNILA-----NAVKVTLGPKGRNVVLERSFGGPTVTKDGVSVAKEIELkdklQNMGAQMVKEVASKTS 82
Cdd:TIGR02342 1 FQDKDKPQDVRTSNIVAakavaDAIRTSLGPKGMDKMIQDGKGEVIITNDGATILKQMAV----LHPAAKMLVELSKAQD 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1878327742 83 DNAGDGTTTATVLAQSIVREGMKYVASGMNPMDLKRGIDKAVAAAIEELRKISKP 137
Cdd:TIGR02342 77 IEAGDGTTSVVILAGALLGACERLLNKGIHPTIISESFQSAADEAIKILDEMSIP 131
|
|
| TCP1_zeta |
cd03342 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
10-145 |
1.21e-08 |
|
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: 57.27 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 10 DSARAKMVEGVNI-----LANAVKVTLGPKGRNVVLERSFGGPTVTKDGVSVAKEIELkdklQNMGAQMVKEVASKTSDN 84
Cdd:cd03342 6 EVLRRGQALAVNIsaakgLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLSEMQI----QHPTASMIARAATAQDDI 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1878327742 85 AGDGTTTATVLAQSIVREGMKYVASGMNPMDLKRGIDKAVAAAIEELR--KISKPCTTNKEIA 145
Cdd:cd03342 82 TGDGTTSNVLLIGELLKQAERYIQEGVHPRIITEGFELAKNKALKFLEsfKVPVEIDTDRELL 144
|
|
| TCP1_alpha |
cd03335 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ... |
9-113 |
3.36e-08 |
|
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: 56.14 E-value: 3.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 9 GDSARAKMVEGVNILANAVKVTLGPKGRNVVLERSFGGPTVTKDGVSVAKEIELKDKlqnmGAQMVKEVASKTSDNAGDG 88
Cdd:cd03335 6 GQDVRTQNVTAAMAIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHP----AAKILVELAQLQDKEVGDG 81
|
90 100
....*....|....*....|....*
gi 1878327742 89 TTTATVLAQSIVREGMKYVASGMNP 113
Cdd:cd03335 82 TTSVVIIAAELLKRANELVKQKIHP 106
|
|
| TCP1_gamma |
cd03337 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ... |
23-178 |
5.24e-08 |
|
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: 55.38 E-value: 5.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 23 LANAVKVTLGPKGRNVVLERSFGGPTVTKDGVSVAKEIELkdklQNMGAQMVKEVASKTSDNAGDGTTTATVLAQSIVRE 102
Cdd:cd03337 28 VADVIRTCLGPRAMLKMLLDPMGGIVLTNDGNAILREIDV----AHPAAKSMIELSRTQDEEVGDGTTSVIILAGEILAV 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1878327742 103 GMKYVASGMNPMDLKRGIDKAVAAAIEELRKISKPCTTNKEIAQVGAISANSDTSIGDRIAEAMDKVGKEGVITVE 178
Cdd:cd03337 104 AEPFLERGIHPTVIIKAYRKALEDALKILEEISIPVDVNDRAQMLKIIKSCIGTKFVSRWSDLMCNLALDAVKTVA 179
|
|
| chap_CCT_theta |
TIGR02346 |
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ... |
10-143 |
1.92e-05 |
|
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: 47.40 E-value: 1.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 10 DSARAKMVEGVNILANAVKVTLGPKGRNVVLERSFGGPTVTKDGVSVAKEIELkdklQNMGAQMVKEVASKTSDNAGDGT 89
Cdd:TIGR02346 17 EEAVIKNIEACKELSQITRTSLGPNGMNKMVINHLEKLFVTNDAATILRELEV----QHPAAKLLVMASEMQENEIGDGT 92
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1878327742 90 TTATVLAQSIVREGMKYVASGMNPMDLKRGIDKAVAAAIEELRKISKPCTTNKE 143
Cdd:TIGR02346 93 NLVLVLAGELLNKAEELIRMGLHPSEIIKGYEMALKKAMEILEELVVWEVKDLR 146
|
|
| TCP1_theta |
cd03341 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ... |
23-131 |
4.49e-03 |
|
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: 39.51 E-value: 4.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878327742 23 LANAVKVTLGPKGRN--VV--LERSFggptVTKDGVSVAKEIELKD---KLQNMGAQMVKEvasktsdNAGDGTTTATVL 95
Cdd:cd03341 20 LSQITRTSYGPNGMNkmVInhLEKLF----VTSDAATILRELEVQHpaaKLLVMASQMQEE-------EIGDGTNLVVVL 88
|
90 100 110
....*....|....*....|....*....|....*.
gi 1878327742 96 AQSIVREGMKYVASGMNPMDLKRGIDKAVAAAIEEL 131
Cdd:cd03341 89 AGELLEKAEELLRMGLHPSEIIEGYEKALKKALEIL 124
|
|
| |
