|
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: 996.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 2 AAKDVKFGNDARIKMLRGVNILADAVKVTLGPKGRNVVLDKSFGSPTITKDGVSVAREIELEDKFENMGAQMVKEVASKA 81
Cdd:PRK00013 1 MAKDIKFGEDARRKLLRGVNKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDPFENMGAQLVKEVASKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 82 NDAAGDGTTTATVLAQSIITEGLKAVAAGMNPMDLKRGIDKAVIAAVEELKKLSVPCSDSKAIAQVGTISANSDSTVGEL 161
Cdd:PRK00013 81 NDVAGDGTTTATVLAQAIVREGLKNVAAGANPMDLKRGIDKAVEAAVEELKKISKPVEDKEEIAQVATISANGDEEIGKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 162 IAQAMEKVGKEGVITVEEGSGLQDELDVVEGMQFDRGYLSPYFINKPETGSIELESPFILLADKKISNIREMLPVLEAVA 241
Cdd:PRK00013 161 IAEAMEKVGKEGVITVEESKGFETELEVVEGMQFDRGYLSPYFVTDPEKMEAELENPYILITDKKISNIQDLLPVLEQVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 242 KAGKPLLIIAEDVEGEALATLVVNTMRGIVKVAAVKAPGFGDRRKAMLQDIATLTAGTVISEEIGLELEKTTLEDLGQAK 321
Cdd:PRK00013 241 QSGKPLLIIAEDVEGEALATLVVNKLRGTLKVVAVKAPGFGDRRKAMLEDIAILTGGTVISEELGLKLEDATLEDLGQAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 322 RVVINKDTTIIIDGVGDEAAIQGRVAQIRQQIEDATSDYDKEKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVEDALH 401
Cdd:PRK00013 321 KVVVTKDNTTIVDGAGDKEAIKARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATEVEMKEKKDRVEDALH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 402 ATRAAVEEGVVAGGGVALIRAAHAIAGLKGDNEDQNVGIKVALRAMESPLRQIVVNAGEEASVIANKVKAGEGS-FGYNA 480
Cdd:PRK00013 401 ATRAAVEEGIVPGGGVALLRAAPALEALKGLNGDEATGINIVLRALEAPLRQIAENAGLEGSVVVEKVKNGKGKgYGYNA 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 488137920 481 YTEEYGDMIAMGILDPTKVTRSALQYAASIAGLMITTECMVTDLPRDDK 529
Cdd:PRK00013 481 ATGEYVDMIEAGIIDPTKVTRSALQNAASVAGLLLTTEAVVADKPEKKA 529
|
|
| 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: 900.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 4 KDVKFGNDARIKMLRGVNILADAVKVTLGPKGRNVVLDKSFGSPTITKDGVSVAREIELEDKFENMGAQMVKEVASKAND 83
Cdd:cd03344 1 KDIKFGEEARKALLRGVNKLADAVKVTLGPKGRNVVIEKSFGSPKITKDGVTVAKEIELEDPFENMGAQLVKEVASKTND 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 84 AAGDGTTTATVLAQSIITEGLKAVAAGMNPMDLKRGIDKAVIAAVEELKKLSVPCSDSKAIAQVGTISANSDSTVGELIA 163
Cdd:cd03344 81 VAGDGTTTATVLARAIIKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKPVKTKEEIAQVATISANGDEEIGELIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 164 QAMEKVGKEGVITVEEGSGLQDELDVVEGMQFDRGYLSPYFINKPETGSIELESPFILLADKKISNIREMLPVLEAVAKA 243
Cdd:cd03344 161 EAMEKVGKDGVITVEEGKTLETELEVVEGMQFDRGYLSPYFVTDPEKMEVELENPYILLTDKKISSIQELLPILELVAKA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 244 GKPLLIIAEDVEGEALATLVVNTMRGIVKVAAVKAPGFGDRRKAMLQDIATLTAGTVISEEIGLELEKTTLEDLGQAKRV 323
Cdd:cd03344 241 GRPLLIIAEDVEGEALATLVVNKLRGGLKVCAVKAPGFGDRRKAMLEDIAILTGGTVISEELGLKLEDVTLEDLGRAKKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 324 VINKDTTIIIDGVGDEAAIQGRVAQIRQQIEDATSDYDKEKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVEDALHAT 403
Cdd:cd03344 321 VVTKDDTTIIGGAGDKAAIKARIAQIRKQIEETTSDYDKEKLQERLAKLSGGVAVIKVGGATEVELKEKKDRVEDALNAT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 404 RAAVEEGVVAGGGVALIRAAHAIAGLKGDNEDQNVGIKVALRAMESPLRQIVVNAGEEASVIANKVKAGEGSFGYNAYTE 483
Cdd:cd03344 401 RAAVEEGIVPGGGVALLRASPALDKLKALNGDEKLGIEIVRRALEAPLRQIAENAGVDGSVVVEKVLESPDGFGYDAATG 480
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 488137920 484 EYGDMIAMGILDPTKVTRSALQYAASIAGLMITTECMVTD 523
Cdd:cd03344 481 EYVDMIEAGIIDPTKVVRSALQNAASVASLLLTTEALVVD 520
|
|
| groEL |
PRK12849 |
chaperonin GroEL; Reviewed |
2-529 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237230 Cd Length: 542 Bit Score: 899.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 2 AAKDVKFGNDARIKMLRGVNILADAVKVTLGPKGRNVVLDKSFGSPTITKDGVSVAREIELEDKFENMGAQMVKEVASKA 81
Cdd:PRK12849 1 MAKIIKFDEEARRALERGVNKLADAVKVTLGPKGRNVVIDKSFGAPTITKDGVSIAKEIELEDPFENLGAQLVKEVASKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 82 NDAAGDGTTTATVLAQSIITEGLKAVAAGMNPMDLKRGIDKAVIAAVEELKKLSVPCSDSKAIAQVGTISANSDSTVGEL 161
Cdd:PRK12849 81 NDVAGDGTTTATVLAQALVQEGLKNVAAGANPMDLKRGIDKAVEAVVEELKALARPVSGSEEIAQVATISANGDEEIGEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 162 IAQAMEKVGKEGVITVEEGSGLQDELDVVEGMQFDRGYLSPYFINKPETGSIELESPFILLADKKISNIREMLPVLEAVA 241
Cdd:PRK12849 161 IAEAMEKVGKDGVITVEESKTLETELEVTEGMQFDRGYLSPYFVTDPERMEAVLEDPLILLTDKKISSLQDLLPLLEKVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 242 KAGKPLLIIAEDVEGEALATLVVNTMRGIVKVAAVKAPGFGDRRKAMLQDIATLTAGTVISEEIGLELEKTTLEDLGQAK 321
Cdd:PRK12849 241 QSGKPLLIIAEDVEGEALATLVVNKLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGLKLEEVTLDDLGRAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 322 RVVINKDTTIIIDGVGDEAAIQGRVAQIRQQIEDATSDYDKEKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVEDALH 401
Cdd:PRK12849 321 RVTITKDNTTIVDGAGDKEAIEARVAQIRRQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATEVELKERKDRVEDALN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 402 ATRAAVEEGVVAGGGVALIRAAHAIAGLKGDNEDQNVGIKVALRAMESPLRQIVVNAGEEASVIANKVKAGEGSFGYNAY 481
Cdd:PRK12849 401 ATRAAVEEGIVPGGGVALLRAAKALDELAGLNGDQAAGVEIVRRALEAPLRQIAENAGLDGSVVVAKVLELEDGFGFNAA 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 488137920 482 TEEYGDMIAMGILDPTKVTRSALQYAASIAGLMITTECMVTDLPRDDK 529
Cdd:PRK12849 481 TGEYGDLIAAGIIDPVKVTRSALQNAASVAGLLLTTEALVADKPEEED 528
|
|
| GroEL |
TIGR02348 |
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ... |
3-525 |
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: 888.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 3 AKDVKFGNDARIKMLRGVNILADAVKVTLGPKGRNVVLDKSFGSPTITKDGVSVAREIELEDKFENMGAQMVKEVASKAN 82
Cdd:TIGR02348 1 AKQIKFDEEARKALLRGVDKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDKFENMGAQLVKEVASKTN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 83 DAAGDGTTTATVLAQSIITEGLKAVAAGMNPMDLKRGIDKAVIAAVEELKKLSVPCSDSKAIAQVGTISANSDSTVGELI 162
Cdd:TIGR02348 81 DVAGDGTTTATVLAQAIVKEGLKNVAAGANPIELKRGIEKAVEAVVEELKKLSKPVKGKKEIAQVATISANNDEEIGSLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 163 AQAMEKVGKEGVITVEEGSGLQDELDVVEGMQFDRGYLSPYFINKPETGSIELESPFILLADKKISNIREMLPVLEAVAK 242
Cdd:TIGR02348 161 AEAMEKVGKDGVITVEESKSLETELEVVEGMQFDRGYISPYFVTDAEKMEVELENPYILITDKKISNIKDLLPLLEKVAQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 243 AGKPLLIIAEDVEGEALATLVVNTMRGIVKVAAVKAPGFGDRRKAMLQDIATLTAGTVISEEIGLELEKTTLEDLGQAKR 322
Cdd:TIGR02348 241 SGKPLLIIAEDVEGEALATLVVNKLRGTLNVCAVKAPGFGDRRKAMLEDIAILTGGQVISEELGLKLEEVTLDDLGKAKK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 323 VVINKDTTIIIDGVGDEAAIQGRVAQIRQQIEDATSDYDKEKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVEDALHA 402
Cdd:TIGR02348 321 VTVDKDNTTIVEGAGDKAAIKARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATETEMKEKKLRIEDALNA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 403 TRAAVEEGVVAGGGVALIRAAHAIAGLKGDNEDQNVGIKVALRAMESPLRQIVVNAGEEASVIANKVKAGEGSFGYNAYT 482
Cdd:TIGR02348 401 TRAAVEEGIVPGGGVALLRAAAALEGLKGDGEDEAIGIDIVKRALEAPLRQIAENAGLDGAVVAEKVKELKGNFGFNAAT 480
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 488137920 483 EEYGDMIAMGILDPTKVTRSALQYAASIAGLMITTECMVTDLP 525
Cdd:TIGR02348 481 GEYEDLVEAGIIDPTKVTRSALQNAASIAGLLLTTEAVVADKP 523
|
|
| groEL |
PRK12850 |
chaperonin GroEL; Reviewed |
1-528 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237231 Cd Length: 544 Bit Score: 845.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 1 MAAKDVKFGNDARIKMLRGVNILADAVKVTLGPKGRNVVLDKSFGSPTITKDGVSVAREIELEDKFENMGAQMVKEVASK 80
Cdd:PRK12850 1 MAAKEIRFSTDARDRLLRGVNILANAVKVTLGPKGRNVVLEKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVKEVASK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 81 ANDAAGDGTTTATVLAQSIITEGLKAVAAGMNPMDLKRGIDKAVIAAVEELKKLSVPCSDSKAIAQVGTISANSDSTVGE 160
Cdd:PRK12850 81 TNDLAGDGTTTATVLAQAIVREGAKLVAAGMNPMDLKRGIDLAVAAVVDELKKIAKKVTSSKEIAQVATISANGDESIGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 161 LIAQAMEKVGKEGVITVEEGSGLQDELDVVEGMQFDRGYLSPYFINKPETGSIELESPFILLADKKISNIREMLPVLEAV 240
Cdd:PRK12850 161 MIAEAMDKVGKEGVITVEEAKTLGTELDVVEGMQFDRGYLSPYFVTNPEKMRAELEDPYILLHEKKISNLQDLLPILEAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 241 AKAGKPLLIIAEDVEGEALATLVVNTMRGIVKVAAVKAPGFGDRRKAMLQDIATLTAGTVISEEIGLELEKTTLEDLGQA 320
Cdd:PRK12850 241 VQSGRPLLIIAEDVEGEALATLVVNKLRGGLKSVAVKAPGFGDRRKAMLEDIAVLTGGQVISEDLGIKLENVTLDMLGRA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 321 KRVVINKDTTIIIDGVGDEAAIQGRVAQIRQQIEDATSDYDKEKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVEDAL 400
Cdd:PRK12850 321 KRVLITKENTTIIDGAGDKKNIEARVKQIRAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKEKKDRVDDAL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 401 HATRAAVEEGVVAGGGVALIRAAHAIAGLKGDNEDQNVGIKVALRAMESPLRQIVVNAGEEASVIANKVKAGEGSFGYNA 480
Cdd:PRK12850 401 HATRAAVEEGIVPGGGVALLRARSALRGLKGANADETAGIDIVRRALEEPLRQIATNAGFEGSVVVGKVAELPGNFGFNA 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 488137920 481 YTEEYGDMIAMGILDPTKVTRSALQYAASIAGLMITTECMVTDLPRDD 528
Cdd:PRK12850 481 QTGEYGDMVEAGIIDPAKVTRTALQDAASIAALLITTEAMVAEAPKKA 528
|
|
| groEL |
PRK12852 |
chaperonin GroEL; Reviewed |
1-529 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237232 Cd Length: 545 Bit Score: 786.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 1 MAAKDVKFGNDARIKMLRGVNILADAVKVTLGPKGRNVVLDKSFGSPTITKDGVSVAREIELEDKFENMGAQMVKEVASK 80
Cdd:PRK12852 1 MAAKDVKFSGDARDRMLRGVDILANAVKVTLGPKGRNVVIEKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVREVASK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 81 ANDAAGDGTTTATVLAQSIITEGLKAVAAGMNPMDLKRGIDKAVIAAVEELKKLSVPCSDSKAIAQVGTISANSDSTVGE 160
Cdd:PRK12852 81 TNDLAGDGTTTATVLAQAIVREGAKAVAAGMNPMDLKRGIDIAVAAVVKDIEKRAKPVASSAEIAQVGTISANGDAAIGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 161 LIAQAMEKVGKEGVITVEEGSGLQDELDVVEGMQFDRGYLSPYFINKPETGSIELESPFILLADKKISNIREMLPVLEAV 240
Cdd:PRK12852 161 MIAQAMQKVGNEGVITVEENKSLETEVDIVEGMKFDRGYLSPYFVTNAEKMTVELDDAYILLHEKKLSGLQAMLPVLEAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 241 AKAGKPLLIIAEDVEGEALATLVVNTMRGIVKVAAVKAPGFGDRRKAMLQDIATLTAGTVISEEIGLELEKTTLEDLGQA 320
Cdd:PRK12852 241 VQSGKPLLIIAEDVEGEALATLVVNRLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGQLISEDLGIKLENVTLKMLGRA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 321 KRVVINKDTTIIIDGVGDEAAIQGRVAQIRQQIEDATSDYDKEKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVEDAL 400
Cdd:PRK12852 321 KKVVIDKENTTIVNGAGKKADIEARVGQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKEKKDRVEDAL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 401 HATRAAVEEGVVAGGGVALIRAAHAIAGLKGDNEDQNVGIKVALRAMESPLRQIVVNAGEEASVIANKVKAGEG-SFGYN 479
Cdd:PRK12852 401 NATRAAVQEGIVPGGGVALLRAKKAVGRINNDNADVQAGINIVLKALEAPIRQIAENAGVEGSIVVGKILENKSeTFGFD 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 488137920 480 AYTEEYGDMIAMGILDPTKVTRSALQYAASIAGLMITTECMVTDLPRDDK 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: 774.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 1 MAAKDVKFGNDARIKMLRGVNILADAVKVTLGPKGRNVVLDKSFGSPTITKDGVSVAREIELEDKFENMGAQMVKEVASK 80
Cdd:PRK12851 1 MAAKEVKFHVEAREKMLRGVNILADAVKVTLGPKGRNVVIDKSFGAPTITNDGVTIAKEIELEDKFENMGAQMVREVASK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 81 ANDAAGDGTTTATVLAQSIITEGLKAVAAGMNPMDLKRGIDKAVIAAVEELKKLSVPCSDSKAIAQVGTISANSDSTVGE 160
Cdd:PRK12851 81 TNDVAGDGTTTATVLAQAIVREGAKAVAAGANPMDLKRGIDRAVAAVVEELKANARPVTTNAEIAQVATISANGDAEIGR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 161 LIAQAMEKVGKEGVITVEEGSGLQDELDVVEGMQFDRGYLSPYFINKPETGSIELESPFILLADKKISNIREMLPVLEAV 240
Cdd:PRK12851 161 LVAEAMEKVGNEGVITVEESKTAETELEVVEGMQFDRGYLSPYFVTDADKMEAELEDPYILIHEKKISNLQDLLPVLEAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 241 AKAGKPLLIIAEDVEGEALATLVVNTMRGIVKVAAVKAPGFGDRRKAMLQDIATLTAGTVISEEIGLELEKTTLEDLGQA 320
Cdd:PRK12851 241 VQSGKPLLIIAEDVEGEALATLVVNKLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGIKLENVTLEQLGRA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 321 KRVVINKDTTIIIDGVGDEAAIQGRVAQIRQQIEDATSDYDKEKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVEDAL 400
Cdd:PRK12851 321 KKVVVEKENTTIIDGAGSKTEIEGRVAQIRAQIEETTSDYDREKLQERLAKLAGGVAVIRVGASTEVEVKEKKDRVDDAL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 401 HATRAAVEEGVVAGGGVALIRAAHAIAGLKGDNEDQNVGIKVALRAMESPLRQIVVNAGEEASVIANKVKAGEGSFGYNA 480
Cdd:PRK12851 401 HATRAAVEEGIVPGGGVALLRAVKALDKLETANGDQRTGVEIVRRALEAPVRQIAENAGAEGSVVVGKLREKPGGYGFNA 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 488137920 481 YTEEYGDMIAMGILDPTKVTRSALQYAASIAGLMITTECMVTDLPRDDK 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: 762.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 2 AAKDVKFGNDARIKMLRGVNILADAVKVTLGPKGRNVVLDKSFGSPTITKDGVSVAREIELEDKFENMGAQMVKEVASKA 81
Cdd:COG0459 1 MAKQILFGEDARRANIRGVKALADAVKVTLGPKGRNVMLVKSFGDPTITNDGVTIAKEIELEDPFENMGAQLVKEVASKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 82 NDAAGDGTTTATVLAQSIITEGLKAVAAGMNPMDLKRGIDKAVIAAVEELKKLSVPCSDSKAIAQVGTISANSDSTVGEL 161
Cdd:COG0459 81 NDEAGDGTTTATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPVDDKEELAQVATISANGDEEIGEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 162 IAQAMEKVGKEGVITVEEGSGLQDELDVVEGMQFDRGYLSPYFINKPETGSIELESPFILLADKKISNIREMLPVLEAVA 241
Cdd:COG0459 161 IAEAMEKVGKDGVITVEEGKGLETELEVVEGMQFDKGYLSPYFVTDPEKMPAELENAYILLTDKKISSIQDLLPLLEKVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 242 KAGKPLLIIAEDVEGEALATLVVNTMRGIVKVAAVKAPGFGDRRKAMLQDIATLTAGTVISEEIGLELEKTTLEDLGQAK 321
Cdd:COG0459 241 QSGKPLLIIAEDIDGEALATLVVNGIRGVLRVVAVKAPGFGDRRKAMLEDIAILTGGRVISEDLGLKLEDVTLDDLGRAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 322 RVVINKDTTIIIDGVGDEAAIqgrvaqirqqiedatsdydkeklqervaklaggvaVIKVGAATEVEMKEKKARVEDALH 401
Cdd:COG0459 321 RVEVDKDNTTIVEGAGNPKAI-----------------------------------VILVGAATEVEVKERKRRVEDALH 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 402 ATRAAVEEGVVAGGGVALIRAAHAIAGLKGDNE-DQNVGIKVALRAMESPLRQIVVNAGEEASVIANKVKAGE-GSFGYN 479
Cdd:COG0459 366 ATRAAVEEGIVPGGGAALLRAARALRELAAKLEgDEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKVRAAKdKGFGFD 445
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 488137920 480 AYTEEYGDMIAMGILDPTKVTRSALQYAASIAGLMITTECMVTDLPRDDK 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: 746.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 2 AAKDVKFGNDARIKMLRGVNILADAVKVTLGPKGRNVVLDKSFGSPTITKDGVSVAREIELEDKFENMGAQMVKEVASKA 81
Cdd:PTZ00114 13 KGKEIRFGDEARQSLLKGIERLADAVAVTLGPKGRNVIIEQEYGSPKITKDGVTVAKAIEFSDRFENVGAQLIRQVASKT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 82 NDAAGDGTTTATVLAQSIITEGLKAVAAGMNPMDLKRGIDKAVIAAVEELKKLSVPCSDSKAIAQVGTISANSDSTVGEL 161
Cdd:PTZ00114 93 NDKAGDGTTTATILARAIFREGCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQSRPVKTKEDILNVATISANGDVEIGSL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 162 IAQAMEKVGKEGVITVEEGSGLQDELDVVEGMQFDRGYLSPYFINKPETGSIELESPFILLADKKISNIREMLPVLEAVA 241
Cdd:PTZ00114 173 IADAMDKVGKDGTITVEDGKTLEDELEVVEGMSFDRGYISPYFVTNEKTQKVELENPLILVTDKKISSIQSILPILEHAV 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 242 KAGKPLLIIAEDVEGEALATLVVNTMRGIVKVAAVKAPGFGDRRKAMLQDIATLTAGTVISEE-IGLELEKTTLEDLGQA 320
Cdd:PTZ00114 253 KNKRPLLIIAEDVEGEALQTLIINKLRGGLKVCAVKAPGFGDNRKDILQDIAVLTGATVVSEDnVGLKLDDFDPSMLGSA 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 321 KRVVINKDTTIIIDGVGDEAAIQGRVAQIRQQIEDATSDYDKEKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVEDAL 400
Cdd:PTZ00114 333 KKVTVTKDETVILTGGGDKAEIKERVELLRSQIERTTSEYDKEKLKERLAKLSGGVAVIKVGGASEVEVNEKKDRIEDAL 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 401 HATRAAVEEGVVAGGGVALIRAAHAIAGLKGDNE---DQNVGIKVALRAMESPLRQIVVNAGEEASVIANKVK-AGEGSF 476
Cdd:PTZ00114 413 NATRAAVEEGIVPGGGVALLRASKLLDKLEEDNEltpDQRTGVKIVRNALRLPTKQIAENAGVEGAVVVEKILeKKDPSF 492
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 488137920 477 GYNAYTEEYGDMIAMGILDPTKVTRSALQYAASIAGLMITTECMVTDLPRDDK 529
Cdd:PTZ00114 493 GYDAQTGEYVNMFEAGIIDPTKVVRSALVDAASVASLMLTTEAAIVDLPKEKK 545
|
|
| groEL |
CHL00093 |
chaperonin GroEL |
3-523 |
0e+00 |
|
chaperonin GroEL
Pssm-ID: 177025 Cd Length: 529 Bit Score: 664.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 3 AKDVKFGNDARIKMLRGVNILADAVKVTLGPKGRNVVLDKSFGSPTITKDGVSVAREIELEDKFENMGAQMVKEVASKAN 82
Cdd:CHL00093 2 SKKILYQDNARRALERGMDILAEAVSVTLGPKGRNVVLEKKYGSPQIVNDGVTIAKEIELEDHIENTGVALIRQAASKTN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 83 DAAGDGTTTATVLAQSIITEGLKAVAAGMNPMDLKRGIDKAVIAAVEELKKLSVPCSDSKAIAQVGTISANSDSTVGELI 162
Cdd:CHL00093 82 DVAGDGTTTATVLAYAIVKQGMKNVAAGANPISLKRGIEKATQYVVSQIAEYARPVEDIQAITQVASISAGNDEEVGSMI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 163 AQAMEKVGKEGVITVEEGSGLQDELDVVEGMQFDRGYLSPYFINKPETGSIELESPFILLADKKISNIR-EMLPVLEAVA 241
Cdd:CHL00093 162 ADAIEKVGREGVISLEEGKSTVTELEITEGMRFEKGFISPYFVTDTERMEVVQENPYILLTDKKITLVQqDLLPILEQVT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 242 KAGKPLLIIAEDVEGEALATLVVNTMRGIVKVAAVKAPGFGDRRKAMLQDIATLTAGTVISEEIGLELEKTTLEDLGQAK 321
Cdd:CHL00093 242 KTKRPLLIIAEDVEKEALATLVLNKLRGIVNVVAVRAPGFGDRRKAMLEDIAILTGGQVITEDAGLSLETIQLDLLGQAR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 322 RVVINKDTTIIIdGVGDEAAIQGRVAQIRQQIEDATSDYDKEKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVEDALH 401
Cdd:CHL00093 322 RIIVTKDSTTII-ADGNEEQVKARCEQLRKQIEIADSSYEKEKLQERLAKLSGGVAVIKVGAATETEMKDKKLRLEDAIN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 402 ATRAAVEEGVVAGGGVALiraAHAIAGLKG---DN--EDQNVGIKVALRAMESPLRQIVVNAGEEASVIANKVKAGEGSF 476
Cdd:CHL00093 401 ATKAAVEEGIVPGGGATL---VHLSENLKTwakNNlkEDELIGALIVARAILAPLKRIAENAGKNGSVIIEKVQEQDFEI 477
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 488137920 477 GYNAYTEEYGDMIAMGILDPTKVTRSALQYAASIAGLMITTECMVTD 523
Cdd:CHL00093 478 GYNAANNKFVNMYEAGIIDPAKVTRSALQNAASIASMILTTECIIVD 524
|
|
| PRK14104 |
PRK14104 |
chaperonin GroEL; Provisional |
1-526 |
0e+00 |
|
chaperonin GroEL; Provisional
Pssm-ID: 172594 Cd Length: 546 Bit Score: 660.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 1 MAAKDVKFGNDARIKMLRGVNILADAVKVTLGPKGRNVVLDKSFGSPTITKDGVSVAREIELEDKFENMGAQMVKEVASK 80
Cdd:PRK14104 1 MSAKEVKFGVDARDRMLRGVDILANAVKVTLGPKGRNVVLDKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVREVASK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 81 ANDAAGDGTTTATVLAQSIITEGLKAVAAGMNPMDLKRGIDKAVIAAVEELKKLSVPCSDSKAIAQVGTISANSDSTVGE 160
Cdd:PRK14104 81 SADAAGDGTTTATVLAQAIVREGAKSVAAGMNPMDLKRGIDLAVEAVVADLVKNSKKVTSNDEIAQVGTISANGDAEIGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 161 LIAQAMEKVGKEGVITVEEGSGLQDELDVVEGMQFDRGYLSPYFINKPETGSIELESPFILLADKKISNIREMLPVLEAV 240
Cdd:PRK14104 161 FLADAMKKVGNEGVITVEEAKSLETELDVVEGMQFDRGYISPYFVTNADKMRVEMDDAYILINEKKLSSLNELLPLLEAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 241 AKAGKPLLIIAEDVEGEALATLVVNTMRGIVKVAAVKAPGFGDRRKAMLQDIATLTAGTVISEEIGLELEKTTLEDLGQA 320
Cdd:PRK14104 241 VQTGKPLVIVAEDVEGEALATLVVNRLRGGLKVAAVKAPGFGDRRKAMLQDIAILTGGQAISEDLGIKLENVTLQMLGRA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 321 KRVVINKDTTIIIDGVGDEAAIQGRVAQIRQQIEDATSDYDKEKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVEDAL 400
Cdd:PRK14104 321 KKVMIDKENTTIVNGAGKKADIEARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKERKDRVDDAM 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 401 HATRAAVEEGVVAGGGVALIRAAHAIAGLKGDNEDQNVGIKVALRAMESPLRQIVVNAGEEASVIANKVKAGEG-SFGYN 479
Cdd:PRK14104 401 HATRAAVEEGIVPGGGVALLRASEQLKGIKTKNDDQKTGVEIVRKALSAPARQIAINAGEDGSVIVGKILEKEQySYGFD 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 488137920 480 AYTEEYGDMIAMGILDPTKVTRSALQYAASIAGLMITTECMVTDLPR 526
Cdd:PRK14104 481 SQTGEYGNLVSKGIIDPTKVVRTAIQNAASVAALLITTEAMVAELPK 527
|
|
| PLN03167 |
PLN03167 |
Chaperonin-60 beta subunit; Provisional |
2-525 |
0e+00 |
|
Chaperonin-60 beta subunit; Provisional
Pssm-ID: 215611 [Multi-domain] Cd Length: 600 Bit Score: 552.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 2 AAKDVKFGND--ARIKMLRGVNILADAVKVTLGPKGRNVVLDKSFGSPTITKDGVSVAREIELEDKFENMGAQMVKEVAS 79
Cdd:PLN03167 55 AAKELHFNKDgsAIKKLQAGVNKLADLVGVTLGPKGRNVVLESKYGSPKIVNDGVTVAKEVELEDPVENIGAKLVRQAAA 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 80 KANDAAGDGTTTATVLAQSIITEGLKAVAAGMNPMDLKRGIDKAVIAAVEELKKLSVPCSDSKaIAQVGTISANSDSTVG 159
Cdd:PLN03167 135 KTNDLAGDGTTTSVVLAQGLIAEGVKVVAAGANPVQITRGIEKTAKALVKELKKMSKEVEDSE-LADVAAVSAGNNYEVG 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 160 ELIAQAMEKVGKEGVITVEEGSGLQDELDVVEGMQFDRGYLSPYFINKPETGSIELESPFILLADKKISNIREMLPVLEA 239
Cdd:PLN03167 214 NMIAEAMSKVGRKGVVTLEEGKSAENNLYVVEGMQFDRGYISPYFVTDSEKMSVEYDNCKLLLVDKKITNARDLIGILED 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 240 VAKAGKPLLIIAEDVEGEALATLVVNTMRGIVKVAAVKAPGFGDRRKAMLQDIATLTAGTVISEEIGLELEKTTLEDLGQ 319
Cdd:PLN03167 294 AIRGGYPLLIIAEDIEQEALATLVVNKLRGSLKIAALKAPGFGERKSQYLDDIAILTGGTVIREEVGLSLDKVGKEVLGT 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 320 AKRVVINKDTTIIIDGVGDEAAIQGRVAQIRQQIEDATSDYDKEKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVEDA 399
Cdd:PLN03167 374 AAKVVLTKDTTTIVGDGSTQEAVNKRVAQIKNLIEAAEQDYEKEKLNERIAKLSGGVAVIQVGAQTETELKEKKLRVEDA 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 400 LHATRAAVEEGVVAGGGVALIRAAHAIAGLKG--DNEDQNVGIKVALRAMESPLRQIVVNAGEEASVIANKVKAGEG-SF 476
Cdd:PLN03167 454 LNATKAAVEEGIVVGGGCTLLRLASKVDAIKDtlENDEQKVGADIVKRALSYPLKLIAKNAGVNGSVVSEKVLSNDNpKF 533
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 488137920 477 GYNAYTEEYGDMIAMGILDPTKVTRSALQYAASIAGLMITTECMVTDLP 525
Cdd:PLN03167 534 GYNAATGKYEDLMAAGIIDPTKVVRCCLEHAASVAKTFLTSDCVVVEIK 582
|
|
| chaperonin_type_I_II |
cd00309 |
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ... |
4-522 |
5.07e-150 |
|
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: 438.40 E-value: 5.07e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 4 KDVKFGNDARIKMLRGVNILADAVKVTLGPKGRNVVLDKSFGSPTITKDGVSVAREIELEdkfeNMGAQMVKEVASKAND 83
Cdd:cd00309 1 KEREFGEEARLSNINAAKALADAVKTTLGPKGMDKMLVDSLGDPTITNDGATILKEIEVE----HPAAKLLVEVAKSQDD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 84 AAGDGTTTATVLAQSIITEGLKAVAAGMNPMDLKRGIDKAVIAAVEELKKLSVP--CSDSKAIAQVGTISANS------D 155
Cdd:cd00309 77 EVGDGTTTVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVPidVEDREELLKVATTSLNSklvsggD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 156 STVGELIAQAMEKVGKE------GVITVEEGSG---LQDELdvVEGMQFDRGYLSPYFInkpetgsIELESPFILLADKK 226
Cdd:cd00309 157 DFLGELVVDAVLKVGKEngdvdlGVIRVEKKKGgslEDSEL--VVGMVFDKGYLSPYMP-------KRLENAKILLLDCK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 227 ISNiremlpvleavakagkplLIIAED-VEGEALATLVVNtmrgivKVAAVKApgfgdRRKAMLQDIATLTAGTVISeei 305
Cdd:cd00309 228 LEY------------------VVIAEKgIDDEALHYLAKL------GIMAVRR-----VRKEDLERIAKATGATIVS--- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 306 glELEKTTLEDLGQAKRVVINK----DTTIIIDGVGdeaaiqgrvaqirqqiedatsdydkeklqervaklaGGVAVIKV 381
Cdd:cd00309 276 --RLEDLTPEDLGTAGLVEETKigdeKYTFIEGCKG------------------------------------GKVATILL 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 382 GAATEVEMKEKKARVEDALHATRAAVEE-GVVAGGGVALIRAAHAIAGL-KGDNEDQNVGIKVALRAMESPLRQIVVNAG 459
Cdd:cd00309 318 RGATEVELDEAERSLHDALCAVRAAVEDgGIVPGGGAAEIELSKALEELaKTLPGKEQLGIEAFADALEVIPRTLAENAG 397
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488137920 460 EEASVIANKVKAGEGSFGYNAY----TEEYGDMIAMGILDPTKVTRSALQYAASIAGLMITTECMVT 522
Cdd:cd00309 398 LDPIEVVTKLRAKHAEGGGNAGgdveTGEIVDMKEAGIIDPLKVKRQALKSATEAASLILTIDDIIV 464
|
|
| Cpn60_TCP1 |
pfam00118 |
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ... |
23-521 |
7.26e-77 |
|
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: 250.97 E-value: 7.26e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 23 LADAVKVTLGPKGRNVVLDKSFGSPTITKDGVSVAREIELEDKfenmGAQMVKEVASKANDAAGDGTTTATVLAQSIITE 102
Cdd:pfam00118 1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELEIQHP----AAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 103 GLKAVAAGMNPMDLKRGIDKAVIAAVEELK-KLSVPCS--DSKAIAQVGTISANSDST------VGELIAQAMEKVGKE- 172
Cdd:pfam00118 77 AEKLLAAGVHPTTIIEGYEKALEKALEILDsIISIPVEdvDREDLLKVARTSLSSKIIsresdfLAKLVVDAVLAIPKNd 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 173 --------GVITVEEGSGlqDELDVVEGMQFDRGYLSPyfinkpeTGSIELESPFILLADKKISNIRE------------ 232
Cdd:pfam00118 157 gsfdlgniGVVKILGGSL--EDSELVDGVVLDKGPLHP-------DMPKRLENAKVLLLNCSLEYEKTetkatvvlsdae 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 233 ------------MLPVLEAVAKAGKPLLIIAEDVEGEALATLVVNTMRGIVKVaavkapgfgdrRKAMLQDIATLTAGTV 300
Cdd:pfam00118 228 qlerflkaeeeqILEIVEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMALRRV-----------KKRDLERLAKATGARA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 301 ISEEIGLelektTLEDLGQAKRV---VINKDTTIIIDGVGDeaaiqgrvaqirqqiedatsdydkeklqervaklaGGVA 377
Cdd:pfam00118 297 VSSLDDL-----TPDDLGTAGKVeeeKIGDEKYTFIEGCKS-----------------------------------PKAA 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 378 VIKVGAATEVEMKEKKARVEDALHATRAAVEE-GVVAGGGVALIRAAHAIAGL-KGDNEDQNVGIKVALRAMESPLRQIV 455
Cdd:pfam00118 337 TILLRGATDHVLDEIERSIHDALCVVKNAIEDpRVVPGGGAVEMELARALREYaKSVSGKEQLAIEAFAEALEVIPKTLA 416
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 456 VNAGEEASVIANKVKA----GEGSFGYNAYTEEYGDMIAMGILDPTKVTRSALQYAASIAGLMITTECMV 521
Cdd:pfam00118 417 ENAGLDPIEVLAELRAahasGEKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKSATEAASTILRIDDII 486
|
|
| chaperonin_like |
cd03333 |
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ... |
142-409 |
2.67e-38 |
|
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: 139.52 E-value: 2.67e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 142 KAIAQVGTISANS-----DSTVGELIAQAMEKVGKE------GVITVEEGSG---LQDELdvVEGMQFDRGYLSPYFink 207
Cdd:cd03333 2 ELLLQVATTSLNSklsswDDFLGKLVVDAVLKVGPDnrmddlGVIKVEKIPGgslEDSEL--VVGVVFDKGYASPYM--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 208 petgSIELESPFILLADKKISNiremlpvleavakagkplLIIAED-VEGEALATLVVNtmrgivKVAAVKApgfgdRRK 286
Cdd:cd03333 77 ----PKRLENAKILLLDCPLEY------------------VVIAEKgIDDLALHYLAKA------GIMAVRR-----VKK 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 287 AMLQDIATLTAGTVISeeiglELEKTTLEDLGQAKRVVINK---DTTIIIDGVGDeaaiqgrvaqirqqiedatsdydke 363
Cdd:cd03333 124 EDLERIARATGATIVS-----SLEDLTPEDLGTAELVEETKigeEKLTFIEGCKG------------------------- 173
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 488137920 364 klqervaklaGGVAVIKVGAATEVEMKEKKARVEDALHATRAAVEE 409
Cdd:cd03333 174 ----------GKAATILLRGATEVELDEVKRSLHDALCAVRAAVEE 209
|
|
| cpn60 |
cd03343 |
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ... |
9-515 |
1.15e-21 |
|
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: 98.49 E-value: 1.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 9 GNDARIKMLRGVNILADAVKVTLGPKGRNVVLDKSFGSPTITKDGVSVAREIELedkfENMGAQMVKEVASKANDAAGDG 88
Cdd:cd03343 13 GRDAQRMNIAAAKAVAEAVRTTLGPKGMDKMLVDSLGDVTITNDGATILKEMDI----EHPAAKMLVEVAKTQDEEVGDG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 89 TTTATVLAQSIITEGLKAVAAGMNPMDLKRGIDKAVIAAVEELKKLSVPCSDS-----KAIAQVGTISANSDST---VGE 160
Cdd:cd03343 89 TTTAVVLAGELLEKAEDLLDQNIHPTVIIEGYRLAAEKALELLDEIAIKVDPDdkdtlRKIAKTSLTGKGAEAAkdkLAD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 161 LIAQAMEKVGKEG-----------VITVEEGSGLqDELDVVEGMQFDRGYL-----------------SPYFINKPET-G 211
Cdd:cd03343 169 LVVDAVLQVAEKRdgkyvvdldniKIEKKTGGSV-DDTELIRGIVIDKEVVhpgmpkrvenakialldAPLEVKKTEIdA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 212 SIELESPFILLA--DKKISNIREMlpvLEAVAKAGKPLLIIAEDVEGEALATLvvnTMRGIVKVAAVKapgfgdrrKAML 289
Cdd:cd03343 248 KIRITSPDQLQAflEQEEAMLKEM---VDKIADTGANVVFCQKGIDDLAQHYL---AKAGILAVRRVK--------KSDM 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 290 QDIATLTAGTVISeeiglELEKTTLEDLGQAKRVVINKdttiiidgVGDEAAIqgrvaqirqQIEDatsdydkeklqerv 369
Cdd:cd03343 314 EKLARATGAKIVT-----NIDDLTPEDLGEAELVEERK--------VGDDKMV---------FVEG-------------- 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 370 AKLAGGVAVIKVGaATEVEMKEKKARVEDALHATRAAVEEG-VVAGGGVALIRAAhaiagLKGDNEDQNVGIKVAL---- 444
Cdd:cd03343 358 CKNPKAVTILLRG-GTEHVVDELERALEDALRVVADALEDGkVVAGGGAVEIELA-----KRLREYARSVGGREQLavea 431
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488137920 445 --RAMESPLRQIVVNAGEEASVIANKVKA----GEGSFGYNAYTEEYGDMIAMGILDPTKVTRSALQyAASIAGLMI 515
Cdd:cd03343 432 faDALEEIPRTLAENAGLDPIDTLVELRAahekGNKNAGLDVYTGEVVDMLEKGVIEPLRVKKQAIK-SATEAATMI 507
|
|
| chap_CCT_eta |
TIGR02345 |
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ... |
14-515 |
1.94e-14 |
|
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: 75.95 E-value: 1.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 14 IKMLRGVNILADAVKVTLGPKGRNVVLDKSFGSPTITKDGVSVAREIELedkfENMGAQMVKEVASKANDAAGDGTTTAT 93
Cdd:TIGR02345 21 ISNINACVAIAEALKTTLGPRGMDKLIVGSNGKATISNDGATILKLLDI----VHPAAKTLVDIAKSQDAEVGDGTTSVT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 94 VLAQSIITEGLKAVAAGMNPMDLKRGIDKAVIAAVEELKKLSVPCSDSK-----------AIAQVGTISANSDSTVGELI 162
Cdd:TIGR02345 97 ILAGELLKEAKPFIEEGVHPQLIIRCYREALSLAVEKIKEIAVTIDEEKgeqrellekcaATALSSKLISHNKEFFSKMI 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 163 AQAMEKVGKE-------GVITVEEGSgLQDELdVVEGMQFDRGYLSPYFINKPetgsielespfilladKKISNIREMLP 235
Cdd:TIGR02345 177 VDAVLSLDRDdldlkliGIKKVQGGA-LEDSQ-LVNGVAFKKTFSYAGFEQQP----------------KKFANPKILLL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 236 VLEAVAKAGKP-LLIIAEDVEG-----EALATLVVNTMRGIV----KVAAVKAPgFGDRRKAMLQDIATLTAGTVISEEI 305
Cdd:TIGR02345 239 NVELELKAEKDnAEIRVEDVEDyqaivDAEWAIIFRKLEKIVesgaNVVLSKLP-IGDLATQYFADRDIFCAGRVSAEDL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 306 glelekttledlgqaKRVVinkdttiiiDGVGdeAAIQGRVAQIRQQIEDATSDYDKEKL-QERVAKLAGG-----VAVI 379
Cdd:TIGR02345 318 ---------------KRVI---------KACG--GSIQSTTSDLEADVLGTCALFEERQIgSERYNYFTGCphaktCTII 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 380 KVGAATEVeMKEKKARVEDALHATRAAVE-EGVVAGGG---VALIRAAHAIAgLKGDNEDQNVgIKVALRAMESPLRQIV 455
Cdd:TIGR02345 372 LRGGAEQF-IEEAERSLHDAIMIVRRALKnKKIVAGGGaieMELSKCLRDYS-KTIDGKQQLI-INAFAKALEIIPRQLC 448
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488137920 456 VNAGEEASVIANKVKA----GEGSFGYNAYTEEYGDMIAMGILDPTKVTRSALQYAASIAGLMI 515
Cdd:TIGR02345 449 ENAGFDSIEILNKLRSrhakGGKWYGVDINTEDIGDNFEAFVWEPALVKINALKAAFEAACTIL 512
|
|
| TCP1_beta |
cd03336 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ... |
9-526 |
2.81e-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: 2.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 9 GNDARIKMLRGVNILADAVKVTLGPKGRNVVL--DKSFGSPTITKDGVSVAREIELEdkfeNMGAQMVKEVASKANDAAG 86
Cdd:cd03336 11 GETARLSSFVGAIAIGDLVKTTLGPKGMDKILqsVGRSGGVTVTNDGATILKSIGVD----NPAAKVLVDISKVQDDEVG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 87 DGTTTATVLAQSIITEGLKAVAAGMNPMDLKRGIDKAVIAAVEELKKLSVPCSDSKA--------IAQVgTISAnsdstv 158
Cdd:cd03336 87 DGTTSVTVLAAELLREAEKLVAQKIHPQTIIEGYRMATAAAREALLSSAVDHSSDEEafredllnIART-TLSS------ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 159 gELIAQAMEKVGKEGVITVE--EGSGLQDELDVVE--GMQFDRGYLSPYFINKPETG---SIELESPFILLA------DK 225
Cdd:cd03336 160 -KILTQDKEHFAELAVDAVLrlKGSGNLDAIQIIKklGGSLKDSYLDEGFLLDKKIGvnqPKRIENAKILIAntpmdtDK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 226 -KI--SNIR----EMLPVLEAVAKA---GKPLLIIAEDVEGEALATLVVN------TMRGIVkvaAVKAPGFgdrrkAML 289
Cdd:cd03336 239 iKIfgAKVRvdstAKVAEIEEAEKEkmkNKVEKILKHGINCFINRQLIYNypeqlfADAGIM---AIEHADF-----DGV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 290 QDIATLTAGTVISeeiglELEKTTLEDLGQAKR---VVINKDTTIIIDGVgdeaaiqgrvaqirqqiedatsdydkeklq 366
Cdd:cd03336 311 ERLALVTGGEIAS-----TFDHPELVKLGTCKLieeIMIGEDKLIRFSGV------------------------------ 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 367 ervakLAGGVAVIKVGAATEVEMKEKKARVEDALHATRAAVEEG-VVAGGGVALIRAAHAIaglkgDNEDQNVGIKVALr 445
Cdd:cd03336 356 -----AAGEACTIVLRGASQQILDEAERSLHDALCVLAQTVKDTrVVLGGGCSEMLMAKAV-----EELAKKTPGKKSL- 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 446 AMES---PLRQIVV----NAGEEASVIANKVKA----GEGSFGYNAYTEEYGDMIAMGILDPTKVTRSALQYAASIAGLM 514
Cdd:cd03336 425 AIEAfakALRQLPTiiadNAGYDSAELVAQLRAahynGNTTAGLDMRKGTVGDMKELGITESFKVKRQVLLSASEAAEMI 504
|
570
....*....|..
gi 488137920 515 ITTECMVTDLPR 526
Cdd:cd03336 505 LRVDDIIKCAPR 516
|
|
| chap_CCT_beta |
TIGR02341 |
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ... |
9-526 |
2.96e-12 |
|
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: 69.12 E-value: 2.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 9 GNDARIKMLRGVNILADAVKVTLGPKGRNVVL--DKSFGSPTITKDGVSVAREIELEdkfeNMGAQMVKEVASKANDAAG 86
Cdd:TIGR02341 12 AENARLSSFVGAIAIGDLVKSTLGPKGMDKILqsSSSDASIMVTNDGATILKSIGVD----NPAAKVLVDMSKVQDDEVG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 87 DGTTTATVLAQSIITEGLKAVAAGMNPMDLKRGIDKAVIAAVEELKKLSVPCSDSKAIAQVGTISANSDSTVGELIAQAM 166
Cdd:TIGR02341 88 DGTTSVTVLAAELLREAEKLINQKIHPQTIIAGYREATKAARDALLKSAVDNGSDEVKFRQDLMNIARTTLSSKILSQHK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 167 EKVGKEGVITV--EEGSGLQDELDVVE--GMQFDRGYLSPYFINKPETGSIE---LESPFILLA------DK-KISNIR- 231
Cdd:TIGR02341 168 DHFAQLAVDAVlrLKGSGNLEAIQIIKklGGSLADSYLDEGFLLDKKIGVNQpkrIENAKILIAntgmdtDKvKIFGSRv 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 232 -----EMLPVLEAVAK---AGKPLLIIAEDVEGEALATLVVNTMRGIVKVAAVKAPGFGDRRKamLQDIATLTAGTVISe 303
Cdd:TIGR02341 248 rvdstAKVAELEHAEKekmKEKVEKILKHGINCFINRQLIYNYPEQLFADAGVMAIEHADFEG--VERLALVTGGEIVS- 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 304 eiglELEKTTLEDLGQAK---RVVINKDTTIIIDGVGdeaaiqgrvaqirqqiedatsdydkeklqervaklAGGVAVIK 380
Cdd:TIGR02341 325 ----TFDHPELVKLGSCDlieEIMIGEDKLLKFSGVK-----------------------------------LGEACTIV 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 381 VGAATEVEMKEKKARVEDALHATRAAVEEG-VVAGGGVALIRAAHAIaglkgDNEDQNVGIK--VALRAMESPLRQ---- 453
Cdd:TIGR02341 366 LRGATQQILDEAERSLHDALCVLSQTVKESrTVLGGGCSEMLMSKAV-----TQEAQRTPGKeaLAVEAFARALRQlpti 440
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488137920 454 IVVNAGEEASVIANKVKA----GEGSFGYNAYTEEYGDMIAMGILDPTKVTRSALQYAASIAGLMITTECMVTDLPR 526
Cdd:TIGR02341 441 IADNAGFDSAELVAQLRAahynGNTTMGLDMNEGTIADMRQLGITESYKVKRAVVSSAAEAAEVILRVDNIIKAAPR 517
|
|
| TCP1_delta |
cd03338 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ... |
18-163 |
2.49e-11 |
|
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: 66.16 E-value: 2.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 18 RGVNI-----LADAVKVTLGPKGRNVVLDKSFGSPTITKDGVSVAREIELEdkfeNMGAQMVKEVaSKAND-AAGDGTTT 91
Cdd:cd03338 10 RLSNIqaakaVADAIRTSLGPRGMDKMIQTGKGEVIITNDGATILKQMSVL----HPAAKMLVEL-SKAQDiEAGDGTTS 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488137920 92 ATVLAQSIITEGLKAVAAGMNPMDLKRGIDKAVIAAVEELKKLSVPCS--DSKAIAQVGTISANSD--STVGELIA 163
Cdd:cd03338 85 VVVLAGALLSACESLLKKGIHPTVISESFQIAAKKAVEILDSMSIPVDlnDRESLIKSATTSLNSKvvSQYSSLLA 160
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
9-526 |
2.84e-11 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 65.82 E-value: 2.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 9 GNDARIKMLRGVNILADAVKVTLGPKGRNVVLDKS-----FGSPTITKDGVSVAREIELEdkfeNMGAQMVKEVASKAND 83
Cdd:PTZ00212 20 GETARLQSFVGAIAVADLVKTTLGPKGMDKILQPMsegprSGNVTVTNDGATILKSVWLD----NPAAKILVDISKTQDE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 84 AAGDGTTTATVLAQSIITEGLKAVAAGMNPMDLKRGIDKAVIAAVEELKKLSVPCSDSKA--------IAQVgTISANSD 155
Cdd:PTZ00212 96 EVGDGTTSVVVLAGELLREAEKLLDQKIHPQTIIEGWRMALDVARKALEEIAFDHGSDEEkfkedllnIART-TLSSKLL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 156 STVGELIAQ----AMEKVGKEG-----VITVEEGSGLQDEldvvegmqfdrgYLSPYFINKPETG---SIELESPFILLA 223
Cdd:PTZ00212 175 TVEKDHFAKlavdAVLRLKGSGnldyiQIIKKPGGTLRDS------------YLEDGFILEKKIGvgqPKRLENCKILVA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 224 ------DK-KISNIR------EMLPVLEAVAKA---GKPLLIIAEDVEGEALATLVVNTMRGIVKVAAVKAPGFGDrrka 287
Cdd:PTZ00212 243 ntpmdtDKiKIYGAKvkvdsmEKVAEIEAAEKEkmkNKVDKILAHGCNVFINRQLIYNYPEQLFAEAGIMAIEHAD---- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 288 mLQDIATLTAgtVISEEIGLELEKTTLEDLGQAKRVvinkdTTIIIdgvGDEAAIqgrvaqirqqiedatsdydkeklqe 367
Cdd:PTZ00212 319 -FDGMERLAA--ALGAEIVSTFDTPEKVKLGHCDLI-----EEIMI---GEDKLI------------------------- 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 368 RVAKLAGGVA--VIKVGAATEVeMKEKKARVEDALHATRAAVEEG-VVAGGGVALIRAAHAIaglkgDNEDQNVGIKVAL 444
Cdd:PTZ00212 363 RFSGCAKGEActIVLRGASTHI-LDEAERSLHDALCVLSQTVKDTrVVLGGGCSEMLMANAV-----EELAKKVEGKKSL 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 445 rAME---SPLRQIVV----NAGEEASVIANKVKA----GEGSFGYNAYTEEYGDMIAMGILDPTKVTRSALQYAASIAGL 513
Cdd:PTZ00212 437 -AIEafaKALRQIPTiiadNGGYDSAELVSKLRAehykGNKTAGIDMEKGTVGDMKELGITESYKVKLSQLCSATEAAEM 515
|
570
....*....|...
gi 488137920 514 MITTECMVTDLPR 526
Cdd:PTZ00212 516 ILRVDDIIRCAPR 528
|
|
| TCP1_eta |
cd03340 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ... |
22-137 |
6.96e-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: 64.62 E-value: 6.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 22 ILADAVKVTLGPKGRNVVLDKSFGSPTITKDGVSVAREIELEdkfeNMGAQMVKEVASKANDAAGDGTTTATVLAQSIIT 101
Cdd:cd03340 27 AIADAVRTTLGPRGMDKLIVDGRGKVTISNDGATILKLLDIV----HPAAKTLVDIAKSQDAEVGDGTTSVVVLAGEFLK 102
|
90 100 110
....*....|....*....|....*....|....*.
gi 488137920 102 EGLKAVAAGMNPMDLKRGIDKAVIAAVEELKKLSVP 137
Cdd:cd03340 103 EAKPFIEDGVHPQIIIRGYRKALQLAIEKIKEIAVN 138
|
|
| chap_CCT_epsi |
TIGR02343 |
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ... |
9-141 |
5.12e-10 |
|
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: 61.74 E-value: 5.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 9 GNDARIKMLRGVNILADAVKVTLGPKGRNVVLDKSFGSPTITKDGVSVAREIELEDKFenmgAQMVKEVASKANDAAGDG 88
Cdd:TIGR02343 25 GLEAKKSNIAAAKSVASILRTSLGPKGMDKMLISPDGDITVTNDGATILSQMDVDNQI----AKLMVELSKSQDDEIGDG 100
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 488137920 89 TTTATVLAQSIITEGLKAVAAGMNPMDLKRGIDKAVIAAVEELKKLSVPCSDS 141
Cdd:TIGR02343 101 TTGVVVLAGALLEQAEELLDKGIHPIKIADGFEEAARIAVEHLEEISDEISAD 153
|
|
| chap_CCT_delta |
TIGR02342 |
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ... |
8-154 |
8.47e-10 |
|
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: 61.34 E-value: 8.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 8 FGNDARIKMLRGVNILA-----DAVKVTLGPKGRNVVLDKSFGSPTITKDGVSVAREIELEdkfeNMGAQMVKEVaSKAN 82
Cdd:TIGR02342 1 FQDKDKPQDVRTSNIVAakavaDAIRTSLGPKGMDKMIQDGKGEVIITNDGATILKQMAVL----HPAAKMLVEL-SKAQ 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488137920 83 D-AAGDGTTTATVLAQSIITEGLKAVAAGMNPMDLKRGIDKAVIAAVEELKKLSVPC--SDSKAIAQVGTISANS 154
Cdd:TIGR02342 76 DiEAGDGTTSVVILAGALLGACERLLNKGIHPTIISESFQSAADEAIKILDEMSIPVdlSDREQLLKSATTSLSS 150
|
|
| TCP1_epsilon |
cd03339 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ... |
11-142 |
6.11e-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: 58.46 E-value: 6.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 11 DARIKMLRGV-----NILA-----DAVKVTLGPKGrnvvLDKSFGSP----TITKDGVSVAREIELEdkfeNMGAQMVKE 76
Cdd:cd03339 13 QEKKKRLKGLeahksHILAaksvaNILRTSLGPRG----MDKILVSPdgevTVTNDGATILEKMDVD----HQIAKLLVE 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488137920 77 VASKANDAAGDGTTTATVLAQSIITEGLKAVAAGMNPMDLKRGIDKAVIAAVEELKKLSVPCSDSK 142
Cdd:cd03339 85 LSKSQDDEIGDGTTGVVVLAGALLEQAEKLLDRGIHPIRIADGYEQACKIAVEHLEEIADKIEFSP 150
|
|
| chap_CCT_alpha |
TIGR02340 |
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ... |
9-133 |
2.81e-08 |
|
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: 56.27 E-value: 2.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 9 GNDARIKMLRGVNILADAVKVTLGPKGRNVVLDKSFGSPTITKDGVSVAREIELEDKfenmGAQMVKEVASKANDAAGDG 88
Cdd:TIGR02340 10 GQDVRTQNVTAAMAIANIVKTSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHP----AAKILVELAQLQDREVGDG 85
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 488137920 89 TTTATVLAQSIITEGLKAVAAGMNPMDLKRGIDKAVIAAVEELKK 133
Cdd:TIGR02340 86 TTSVVIIAAELLKRADELVKNKIHPTSVISGYRLACKEAVKYIKE 130
|
|
| TCP1_gamma |
cd03337 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ... |
23-189 |
2.89e-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: 53.07 E-value: 2.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 23 LADAVKVTLGPKGR-NVVLDKSfGSPTITKDGVSVAREIELEdkfeNMGAQMVKEVASKANDAAGDGTTTATVLAQSIIT 101
Cdd:cd03337 28 VADVIRTCLGPRAMlKMLLDPM-GGIVLTNDGNAILREIDVA----HPAAKSMIELSRTQDEEVGDGTTSVIILAGEILA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 102 EGLKAVAAGMNPMDLKRGIDKAVIAAVEELKKLSVPCsDSKAIAQVGTISANSDSTvgELIAQAMEKVGK---EGVITVE 178
Cdd:cd03337 103 VAEPFLERGIHPTVIIKAYRKALEDALKILEEISIPV-DVNDRAQMLKIIKSCIGT--KFVSRWSDLMCNlalDAVKTVA 179
|
170
....*....|..
gi 488137920 179 -EGSGLQDELDV 189
Cdd:cd03337 180 vEENGRKKEIDI 191
|
|
| chap_CCT_gamma |
TIGR02344 |
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ... |
23-224 |
6.20e-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: 52.05 E-value: 6.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 23 LADAVKVTLGPKGRNVVLDKSFGSPTITKDGVSVAREIELEdkfeNMGAQMVKEVASKANDAAGDGTTTATVLAQSIITE 102
Cdd:TIGR02344 28 VADIIRTCLGPRSMLKMLLDPMGGIVMTNDGNAILREIDVA----HPAAKSMIELSRTQDEEVGDGTTSVIILAGEMLSV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 103 GLKAVAAGMNPMDLKRGIDKAVIAAVEELKKLSVPCSDSKAIAQVGTISANSDSTVGELIAQAMEKVGKEGVITVEEGSG 182
Cdd:TIGR02344 104 AEPFLEQNIHPTVIIRAYRKALDDALSVLEEISIPVDVNDDAAMLKLIQSCIGTKFVSRWSDLMCDLALDAVRTVQRDEN 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488137920 183 LQDELDV-----VE----GMQFDRGYLSPYFINKPETGSI---ELESPFILLAD 224
Cdd:TIGR02344 184 GRKEIDIkryakVEkipgGDIEDSCVLKGVMINKDVTHPKmrrYIENPRIVLLD 237
|
|
| chap_CCT_zeta |
TIGR02347 |
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ... |
23-136 |
6.66e-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: 52.04 E-value: 6.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 23 LADAVKVTLGPKGRNVVLDKSFGSPTITKDGVSVAREIELEdkfeNMGAQMVKEVASKANDAAGDGTTTATVLAQSIITE 102
Cdd:TIGR02347 28 LQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEMQIQ----HPTASMIARAATAQDDITGDGTTSTVLLIGELLKQ 103
|
90 100 110
....*....|....*....|....*....|....
gi 488137920 103 GLKAVAAGMNPMDLKRGIDKAVIAAVEELKKLSV 136
Cdd:TIGR02347 104 AERYILEGVHPRIITEGFEIARKEALQFLDKFKV 137
|
|
| TCP1_zeta |
cd03342 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
23-137 |
1.33e-06 |
|
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: 51.10 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 23 LADAVKVTLGPKGRNVVLDKSFGSPTITKDGVSVAREIEledkFENMGAQMVKEVASKANDAAGDGTTTATVLAQSIITE 102
Cdd:cd03342 24 LQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLSEMQ----IQHPTASMIARAATAQDDITGDGTTSNVLLIGELLKQ 99
|
90 100 110
....*....|....*....|....*....|....*
gi 488137920 103 GLKAVAAGMNPMDLKRGIDKAVIAAVEELKKLSVP 137
Cdd:cd03342 100 AERYIQEGVHPRIITEGFELAKNKALKFLESFKVP 134
|
|
| TCP1_alpha |
cd03335 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ... |
9-113 |
2.62e-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: 49.98 E-value: 2.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 9 GNDARIKMLRGVNILADAVKVTLGPKGRNVVLDKSFGSPTITKDGVSVAREIELEDKfenmGAQMVKEVASKANDAAGDG 88
Cdd:cd03335 6 GQDVRTQNVTAAMAIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHP----AAKILVELAQLQDKEVGDG 81
|
90 100
....*....|....*....|....*
gi 488137920 89 TTTATVLAQSIITEGLKAVAAGMNP 113
Cdd:cd03335 82 TTSVVIIAAELLKRANELVKQKIHP 106
|
|
| chap_CCT_theta |
TIGR02346 |
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ... |
11-197 |
1.40e-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: 47.79 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 11 DARIKMLRGVNILADAVKVTLGPKGRNVV----LDKSFgsptITKDGVSVAREIELEdkfeNMGAQMVKEVASKANDAAG 86
Cdd:TIGR02346 18 EAVIKNIEACKELSQITRTSLGPNGMNKMvinhLEKLF----VTNDAATILRELEVQ----HPAAKLLVMASEMQENEIG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 87 DGTTTATVLAQSIITEGLKAVAAGMNPMDLKRGIDKAVIAAVEELKKLSV-----------------PCSDSKAIAQVGT 149
Cdd:TIGR02346 90 DGTNLVLVLAGELLNKAEELIRMGLHPSEIIKGYEMALKKAMEILEELVVwevkdlrdkdelikalkASISSKQYGNEDF 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488137920 150 ISansdstvgELIAQAM-----EKVGKEGVITVE----EGSGLQDElDVVEGMQFDR 197
Cdd:TIGR02346 170 LA--------QLVAQACstvlpKNPQNFNVDNIRvckiLGGSLSNS-EVLKGMVFNR 217
|
|
| TCP1_theta |
cd03341 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ... |
23-136 |
2.84e-04 |
|
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: 43.36 E-value: 2.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488137920 23 LADAVKVTLGPKGRN--VV--LDKSFgsptITKDGVSVAREIEledkFENMGAQMVKEVASKANDAAGDGTTTATVLAQS 98
Cdd:cd03341 20 LSQITRTSYGPNGMNkmVInhLEKLF----VTSDAATILRELE----VQHPAAKLLVMASQMQEEEIGDGTNLVVVLAGE 91
|
90 100 110
....*....|....*....|....*....|....*...
gi 488137920 99 IITEGLKAVAAGMNPMDLKRGIDKAVIAAVEELKKLSV 136
Cdd:cd03341 92 LLEKAEELLRMGLHPSEIIEGYEKALKKALEILEELVV 129
|
|
| |
