|
Name |
Accession |
Description |
Interval |
E-value |
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
1-531 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 1005.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 1 MAKDIKFSEEARRAMLRGVDTLANAVKVTLGPKGRNVVLEKKFGSPLITNDGVTIAKEIELEDAFENMGAKLVAEVASKT 80
Cdd:PRK00013 1 MAKDIKFGEDARRKLLRGVNKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDPFENMGAQLVKEVASKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 81 NDVAGDGTTTATVLAQAMIREGLKNVTAGANPMGIRKGMEKAVAVAVEELKAISKPIQGKDSIAQVAAISA-ADEEVGQL 159
Cdd:PRK00013 81 NDVAGDGTTTATVLAQAIVREGLKNVAAGANPMDLKRGIDKAVEAAVEELKKISKPVEDKEEIAQVATISAnGDEEIGKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 160 IAEAMERVGNDGVITLEESKGFTTELEVVEGMQFDRGYASPYMVTDSDKMEAVLDDPYILITDKKIGNIQEILPVLEQVV 239
Cdd:PRK00013 161 IAEAMEKVGKEGVITVEESKGFETELEVVEGMQFDRGYLSPYFVTDPEKMEAELENPYILITDKKISNIQDLLPVLEQVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 240 QQGKPLLIIAEDVEGEALATLVVNKLRGTFTAVAVKAPGFGDRRKAMLQDVAILTGGEVITEELGLDLKTASIDQLGRAS 319
Cdd:PRK00013 241 QSGKPLLIIAEDVEGEALATLVVNKLRGTLKVVAVKAPGFGDRRKAMLEDIAILTGGTVISEELGLKLEDATLEDLGQAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 320 KIVVTKENTTVVNGAGNAEDILARVNQIKAQLEETTSEFDREKLQERLAKLAGGVAVIKVGAATETELKERKLRIEDALN 399
Cdd:PRK00013 321 KVVVTKDNTTIVDGAGDKEAIKARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATEVEMKEKKDRVEDALH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 400 STRAAVEEGIVAGGGTALVNIYNKVASIEAD-GDTATGINIVLRAIEEPVRQIAHNAGLEGSVIVERLK-GEAVGTGFNA 477
Cdd:PRK00013 401 ATRAAVEEGIVPGGGVALLRAAPALEALKGLnGDEATGINIVLRALEAPLRQIAENAGLEGSVVVEKVKnGKGKGYGYNA 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 502820051 478 ATGEWVNMLDTGIVDPTKVTRSALQNASSVAAMFLTTEAVVADKPEENAAPAMP 531
Cdd:PRK00013 481 ATGEYVDMIEAGIIDPTKVTRSALQNAASVAGLLLTTEAVVADKPEKKAAAPPM 534
|
|
| GroEL |
cd03344 |
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ... |
3-520 |
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: 890.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 3 KDIKFSEEARRAMLRGVDTLANAVKVTLGPKGRNVVLEKKFGSPLITNDGVTIAKEIELEDAFENMGAKLVAEVASKTND 82
Cdd:cd03344 1 KDIKFGEEARKALLRGVNKLADAVKVTLGPKGRNVVIEKSFGSPKITKDGVTVAKEIELEDPFENMGAQLVKEVASKTND 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 83 VAGDGTTTATVLAQAMIREGLKNVTAGANPMGIRKGMEKAVAVAVEELKAISKPIQGKDSIAQVAAISA-ADEEVGQLIA 161
Cdd:cd03344 81 VAGDGTTTATVLARAIIKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKPVKTKEEIAQVATISAnGDEEIGELIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 162 EAMERVGNDGVITLEESKGFTTELEVVEGMQFDRGYASPYMVTDSDKMEAVLDDPYILITDKKIGNIQEILPVLEQVVQQ 241
Cdd:cd03344 161 EAMEKVGKDGVITVEEGKTLETELEVVEGMQFDRGYLSPYFVTDPEKMEVELENPYILLTDKKISSIQELLPILELVAKA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 242 GKPLLIIAEDVEGEALATLVVNKLRGTFTAVAVKAPGFGDRRKAMLQDVAILTGGEVITEELGLDLKTASIDQLGRASKI 321
Cdd:cd03344 241 GRPLLIIAEDVEGEALATLVVNKLRGGLKVCAVKAPGFGDRRKAMLEDIAILTGGTVISEELGLKLEDVTLEDLGRAKKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 322 VVTKENTTVVNGAGNAEDILARVNQIKAQLEETTSEFDREKLQERLAKLAGGVAVIKVGAATETELKERKLRIEDALNST 401
Cdd:cd03344 321 VVTKDDTTIIGGAGDKAAIKARIAQIRKQIEETTSDYDKEKLQERLAKLSGGVAVIKVGGATEVELKEKKDRVEDALNAT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 402 RAAVEEGIVAGGGTALVNIYNKVASIEA-DGDTATGINIVLRAIEEPVRQIAHNAGLEGSVIVERLKGEAVGTGFNAATG 480
Cdd:cd03344 401 RAAVEEGIVPGGGVALLRASPALDKLKAlNGDEKLGIEIVRRALEAPLRQIAENAGVDGSVVVEKVLESPDGFGYDAATG 480
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 502820051 481 EWVNMLDTGIVDPTKVTRSALQNASSVAAMFLTTEAVVAD 520
Cdd:cd03344 481 EYVDMIEAGIIDPTKVVRSALQNAASVASLLLTTEALVVD 520
|
|
| groEL |
PRK12849 |
chaperonin GroEL; Reviewed |
1-529 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237230 Cd Length: 542 Bit Score: 886.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 1 MAKDIKFSEEARRAMLRGVDTLANAVKVTLGPKGRNVVLEKKFGSPLITNDGVTIAKEIELEDAFENMGAKLVAEVASKT 80
Cdd:PRK12849 1 MAKIIKFDEEARRALERGVNKLADAVKVTLGPKGRNVVIDKSFGAPTITKDGVSIAKEIELEDPFENLGAQLVKEVASKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 81 NDVAGDGTTTATVLAQAMIREGLKNVTAGANPMGIRKGMEKAVAVAVEELKAISKPIQGKDSIAQVAAISA-ADEEVGQL 159
Cdd:PRK12849 81 NDVAGDGTTTATVLAQALVQEGLKNVAAGANPMDLKRGIDKAVEAVVEELKALARPVSGSEEIAQVATISAnGDEEIGEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 160 IAEAMERVGNDGVITLEESKGFTTELEVVEGMQFDRGYASPYMVTDSDKMEAVLDDPYILITDKKIGNIQEILPVLEQVV 239
Cdd:PRK12849 161 IAEAMEKVGKDGVITVEESKTLETELEVTEGMQFDRGYLSPYFVTDPERMEAVLEDPLILLTDKKISSLQDLLPLLEKVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 240 QQGKPLLIIAEDVEGEALATLVVNKLRGTFTAVAVKAPGFGDRRKAMLQDVAILTGGEVITEELGLDLKTASIDQLGRAS 319
Cdd:PRK12849 241 QSGKPLLIIAEDVEGEALATLVVNKLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGLKLEEVTLDDLGRAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 320 KIVVTKENTTVVNGAGNAEDILARVNQIKAQLEETTSEFDREKLQERLAKLAGGVAVIKVGAATETELKERKLRIEDALN 399
Cdd:PRK12849 321 RVTITKDNTTIVDGAGDKEAIEARVAQIRRQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATEVELKERKDRVEDALN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 400 STRAAVEEGIVAGGGTALVNIYNKVASIE-ADGDTATGINIVLRAIEEPVRQIAHNAGLEGSVIVERLKGEAVGTGFNAA 478
Cdd:PRK12849 401 ATRAAVEEGIVPGGGVALLRAAKALDELAgLNGDQAAGVEIVRRALEAPLRQIAENAGLDGSVVVAKVLELEDGFGFNAA 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 502820051 479 TGEWVNMLDTGIVDPTKVTRSALQNASSVAAMFLTTEAVVADKPEENAAPA 529
Cdd:PRK12849 481 TGEYGDLIAAGIIDPVKVTRSALQNAASVAGLLLTTEALVADKPEEEDPPG 531
|
|
| GroEL |
TIGR02348 |
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ... |
2-523 |
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: 870.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 2 AKDIKFSEEARRAMLRGVDTLANAVKVTLGPKGRNVVLEKKFGSPLITNDGVTIAKEIELEDAFENMGAKLVAEVASKTN 81
Cdd:TIGR02348 1 AKQIKFDEEARKALLRGVDKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDKFENMGAQLVKEVASKTN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 82 DVAGDGTTTATVLAQAMIREGLKNVTAGANPMGIRKGMEKAVAVAVEELKAISKPIQGKDSIAQVAAISA-ADEEVGQLI 160
Cdd:TIGR02348 81 DVAGDGTTTATVLAQAIVKEGLKNVAAGANPIELKRGIEKAVEAVVEELKKLSKPVKGKKEIAQVATISAnNDEEIGSLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 161 AEAMERVGNDGVITLEESKGFTTELEVVEGMQFDRGYASPYMVTDSDKMEAVLDDPYILITDKKIGNIQEILPVLEQVVQ 240
Cdd:TIGR02348 161 AEAMEKVGKDGVITVEESKSLETELEVVEGMQFDRGYISPYFVTDAEKMEVELENPYILITDKKISNIKDLLPLLEKVAQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 241 QGKPLLIIAEDVEGEALATLVVNKLRGTFTAVAVKAPGFGDRRKAMLQDVAILTGGEVITEELGLDLKTASIDQLGRASK 320
Cdd:TIGR02348 241 SGKPLLIIAEDVEGEALATLVVNKLRGTLNVCAVKAPGFGDRRKAMLEDIAILTGGQVISEELGLKLEEVTLDDLGKAKK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 321 IVVTKENTTVVNGAGNAEDILARVNQIKAQLEETTSEFDREKLQERLAKLAGGVAVIKVGAATETELKERKLRIEDALNS 400
Cdd:TIGR02348 321 VTVDKDNTTIVEGAGDKAAIKARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATETEMKEKKLRIEDALNA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 401 TRAAVEEGIVAGGGTALVNIYNKVASIEADG-DTATGINIVLRAIEEPVRQIAHNAGLEGSVIVERLKGEAVGTGFNAAT 479
Cdd:TIGR02348 401 TRAAVEEGIVPGGGVALLRAAAALEGLKGDGeDEAIGIDIVKRALEAPLRQIAENAGLDGAVVAEKVKELKGNFGFNAAT 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 502820051 480 GEWVNMLDTGIVDPTKVTRSALQNASSVAAMFLTTEAVVADKPE 523
Cdd:TIGR02348 481 GEYEDLVEAGIIDPTKVTRSALQNAASIAGLLLTTEAVVADKPE 524
|
|
| groEL |
PRK12850 |
chaperonin GroEL; Reviewed |
1-531 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237231 Cd Length: 544 Bit Score: 827.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 1 MAKDIKFSEEARRAMLRGVDTLANAVKVTLGPKGRNVVLEKKFGSPLITNDGVTIAKEIELEDAFENMGAKLVAEVASKT 80
Cdd:PRK12850 2 AAKEIRFSTDARDRLLRGVNILANAVKVTLGPKGRNVVLEKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVKEVASKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 81 NDVAGDGTTTATVLAQAMIREGLKNVTAGANPMGIRKGMEKAVAVAVEELKAISKPIQGKDSIAQVAAISA-ADEEVGQL 159
Cdd:PRK12850 82 NDLAGDGTTTATVLAQAIVREGAKLVAAGMNPMDLKRGIDLAVAAVVDELKKIAKKVTSSKEIAQVATISAnGDESIGEM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 160 IAEAMERVGNDGVITLEESKGFTTELEVVEGMQFDRGYASPYMVTDSDKMEAVLDDPYILITDKKIGNIQEILPVLEQVV 239
Cdd:PRK12850 162 IAEAMDKVGKEGVITVEEAKTLGTELDVVEGMQFDRGYLSPYFVTNPEKMRAELEDPYILLHEKKISNLQDLLPILEAVV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 240 QQGKPLLIIAEDVEGEALATLVVNKLRGTFTAVAVKAPGFGDRRKAMLQDVAILTGGEVITEELGLDLKTASIDQLGRAS 319
Cdd:PRK12850 242 QSGRPLLIIAEDVEGEALATLVVNKLRGGLKSVAVKAPGFGDRRKAMLEDIAVLTGGQVISEDLGIKLENVTLDMLGRAK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 320 KIVVTKENTTVVNGAGNAEDILARVNQIKAQLEETTSEFDREKLQERLAKLAGGVAVIKVGAATETELKERKLRIEDALN 399
Cdd:PRK12850 322 RVLITKENTTIIDGAGDKKNIEARVKQIRAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKEKKDRVDDALH 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 400 STRAAVEEGIVAGGGTALVNIYNKVASIE-ADGDTATGINIVLRAIEEPVRQIAHNAGLEGSVIVERLKGEAVGTGFNAA 478
Cdd:PRK12850 402 ATRAAVEEGIVPGGGVALLRARSALRGLKgANADETAGIDIVRRALEEPLRQIATNAGFEGSVVVGKVAELPGNFGFNAQ 481
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 502820051 479 TGEWVNMLDTGIVDPTKVTRSALQNASSVAAMFLTTEAVVADKPEENAAPAMP 531
Cdd:PRK12850 482 TGEYGDMVEAGIIDPAKVTRTALQDAASIAALLITTEAMVAEAPKKAAAAAAG 534
|
|
| GroEL |
COG0459 |
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ... |
1-528 |
0e+00 |
|
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227 Cd Length: 497 Bit Score: 785.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 1 MAKDIKFSEEARRAMLRGVDTLANAVKVTLGPKGRNVVLEKKFGSPLITNDGVTIAKEIELEDAFENMGAKLVAEVASKT 80
Cdd:COG0459 1 MAKQILFGEDARRANIRGVKALADAVKVTLGPKGRNVMLVKSFGDPTITNDGVTIAKEIELEDPFENMGAQLVKEVASKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 81 NDVAGDGTTTATVLAQAMIREGLKNVTAGANPMGIRKGMEKAVAVAVEELKAISKPIQGKDSIAQVAAISAA-DEEVGQL 159
Cdd:COG0459 81 NDEAGDGTTTATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPVDDKEELAQVATISANgDEEIGEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 160 IAEAMERVGNDGVITLEESKGFTTELEVVEGMQFDRGYASPYMVTDSDKMEAVLDDPYILITDKKIGNIQEILPVLEQVV 239
Cdd:COG0459 161 IAEAMEKVGKDGVITVEEGKGLETELEVVEGMQFDKGYLSPYFVTDPEKMPAELENAYILLTDKKISSIQDLLPLLEKVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 240 QQGKPLLIIAEDVEGEALATLVVNKLRGTFTAVAVKAPGFGDRRKAMLQDVAILTGGEVITEELGLDLKTASIDQLGRAS 319
Cdd:COG0459 241 QSGKPLLIIAEDIDGEALATLVVNGIRGVLRVVAVKAPGFGDRRKAMLEDIAILTGGRVISEDLGLKLEDVTLDDLGRAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 320 KIVVTKENTTVVNGAGNAEDIlarvnqikaqleettsefdreklqerlaklaggvaVIKVGAATETELKERKLRIEDALN 399
Cdd:COG0459 321 RVEVDKDNTTIVEGAGNPKAI-----------------------------------VILVGAATEVEVKERKRRVEDALH 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 400 STRAAVEEGIVAGGGTALVNIYNKVASI--EADGDTATGINIVLRAIEEPVRQIAHNAGLEGSVIVERLK-GEAVGTGFN 476
Cdd:COG0459 366 ATRAAVEEGIVPGGGAALLRAARALRELaaKLEGDEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKVRaAKDKGFGFD 445
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 502820051 477 AATGEWVNMLDTGIVDPTKVTRSALQNASSVAAMFLTTEAVVADKPEENAAP 528
Cdd:COG0459 446 AATGEYVDMLEAGVIDPAKVKRSALQNAASVAGLILTTEAVIADKPEKEEAA 497
|
|
| groEL |
PRK12851 |
chaperonin GroEL; Reviewed |
1-531 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 171770 Cd Length: 541 Bit Score: 769.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 1 MAKDIKFSEEARRAMLRGVDTLANAVKVTLGPKGRNVVLEKKFGSPLITNDGVTIAKEIELEDAFENMGAKLVAEVASKT 80
Cdd:PRK12851 2 AAKEVKFHVEAREKMLRGVNILADAVKVTLGPKGRNVVIDKSFGAPTITNDGVTIAKEIELEDKFENMGAQMVREVASKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 81 NDVAGDGTTTATVLAQAMIREGLKNVTAGANPMGIRKGMEKAVAVAVEELKAISKPIQGKDSIAQVAAISA-ADEEVGQL 159
Cdd:PRK12851 82 NDVAGDGTTTATVLAQAIVREGAKAVAAGANPMDLKRGIDRAVAAVVEELKANARPVTTNAEIAQVATISAnGDAEIGRL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 160 IAEAMERVGNDGVITLEESKGFTTELEVVEGMQFDRGYASPYMVTDSDKMEAVLDDPYILITDKKIGNIQEILPVLEQVV 239
Cdd:PRK12851 162 VAEAMEKVGNEGVITVEESKTAETELEVVEGMQFDRGYLSPYFVTDADKMEAELEDPYILIHEKKISNLQDLLPVLEAVV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 240 QQGKPLLIIAEDVEGEALATLVVNKLRGTFTAVAVKAPGFGDRRKAMLQDVAILTGGEVITEELGLDLKTASIDQLGRAS 319
Cdd:PRK12851 242 QSGKPLLIIAEDVEGEALATLVVNKLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGIKLENVTLEQLGRAK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 320 KIVVTKENTTVVNGAGNAEDILARVNQIKAQLEETTSEFDREKLQERLAKLAGGVAVIKVGAATETELKERKLRIEDALN 399
Cdd:PRK12851 322 KVVVEKENTTIIDGAGSKTEIEGRVAQIRAQIEETTSDYDREKLQERLAKLAGGVAVIRVGASTEVEVKEKKDRVDDALH 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 400 STRAAVEEGIVAGGGTALVNIYNKVASIE-ADGDTATGINIVLRAIEEPVRQIAHNAGLEGSVIVERLKGEAVGTGFNAA 478
Cdd:PRK12851 402 ATRAAVEEGIVPGGGVALLRAVKALDKLEtANGDQRTGVEIVRRALEAPVRQIAENAGAEGSVVVGKLREKPGGYGFNAA 481
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 502820051 479 TGEWVNMLDTGIVDPTKVTRSALQNASSVAAMFLTTEAVVADKPEENAAPAMP 531
Cdd:PRK12851 482 TNEYGDLYAQGVIDPVKVVRTALQNAASVAGLLLTTEAMVAEKPKKEPAPPAP 534
|
|
| groEL |
CHL00093 |
chaperonin GroEL |
1-525 |
0e+00 |
|
chaperonin GroEL
Pssm-ID: 177025 Cd Length: 529 Bit Score: 730.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 1 MAKDIKFSEEARRAMLRGVDTLANAVKVTLGPKGRNVVLEKKFGSPLITNDGVTIAKEIELEDAFENMGAKLVAEVASKT 80
Cdd:CHL00093 1 MSKKILYQDNARRALERGMDILAEAVSVTLGPKGRNVVLEKKYGSPQIVNDGVTIAKEIELEDHIENTGVALIRQAASKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 81 NDVAGDGTTTATVLAQAMIREGLKNVTAGANPMGIRKGMEKAVAVAVEELKAISKPIQGKDSIAQVAAISAA-DEEVGQL 159
Cdd:CHL00093 81 NDVAGDGTTTATVLAYAIVKQGMKNVAAGANPISLKRGIEKATQYVVSQIAEYARPVEDIQAITQVASISAGnDEEVGSM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 160 IAEAMERVGNDGVITLEESKGFTTELEVVEGMQFDRGYASPYMVTDSDKMEAVLDDPYILITDKKIGNI-QEILPVLEQV 238
Cdd:CHL00093 161 IADAIEKVGREGVISLEEGKSTVTELEITEGMRFEKGFISPYFVTDTERMEVVQENPYILLTDKKITLVqQDLLPILEQV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 239 VQQGKPLLIIAEDVEGEALATLVVNKLRGTFTAVAVKAPGFGDRRKAMLQDVAILTGGEVITEELGLDLKTASIDQLGRA 318
Cdd:CHL00093 241 TKTKRPLLIIAEDVEKEALATLVLNKLRGIVNVVAVRAPGFGDRRKAMLEDIAILTGGQVITEDAGLSLETIQLDLLGQA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 319 SKIVVTKENTTVVNgAGNAEDILARVNQIKAQLEETTSEFDREKLQERLAKLAGGVAVIKVGAATETELKERKLRIEDAL 398
Cdd:CHL00093 321 RRIIVTKDSTTIIA-DGNEEQVKARCEQLRKQIEIADSSYEKEKLQERLAKLSGGVAVIKVGAATETEMKDKKLRLEDAI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 399 NSTRAAVEEGIVAGGGTALVNIYNKV---ASIEADGDTATGINIVLRAIEEPVRQIAHNAGLEGSVIVERLKGEAVGTGF 475
Cdd:CHL00093 400 NATKAAVEEGIVPGGGATLVHLSENLktwAKNNLKEDELIGALIVARAILAPLKRIAENAGKNGSVIIEKVQEQDFEIGY 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 502820051 476 NAATGEWVNMLDTGIVDPTKVTRSALQNASSVAAMFLTTEAVVADKPEEN 525
Cdd:CHL00093 480 NAANNKFVNMYEAGIIDPAKVTRSALQNAASIASMILTTECIIVDKKESS 529
|
|
| groEL |
PRK12852 |
chaperonin GroEL; Reviewed |
1-531 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237232 Cd Length: 545 Bit Score: 728.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 1 MAKDIKFSEEARRAMLRGVDTLANAVKVTLGPKGRNVVLEKKFGSPLITNDGVTIAKEIELEDAFENMGAKLVAEVASKT 80
Cdd:PRK12852 2 AAKDVKFSGDARDRMLRGVDILANAVKVTLGPKGRNVVIEKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVREVASKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 81 NDVAGDGTTTATVLAQAMIREGLKNVTAGANPMGIRKGMEKAVAVAVEELKAISKPIQGKDSIAQVAAISA-ADEEVGQL 159
Cdd:PRK12852 82 NDLAGDGTTTATVLAQAIVREGAKAVAAGMNPMDLKRGIDIAVAAVVKDIEKRAKPVASSAEIAQVGTISAnGDAAIGKM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 160 IAEAMERVGNDGVITLEESKGFTTELEVVEGMQFDRGYASPYMVTDSDKMEAVLDDPYILITDKKIGNIQEILPVLEQVV 239
Cdd:PRK12852 162 IAQAMQKVGNEGVITVEENKSLETEVDIVEGMKFDRGYLSPYFVTNAEKMTVELDDAYILLHEKKLSGLQAMLPVLEAVV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 240 QQGKPLLIIAEDVEGEALATLVVNKLRGTFTAVAVKAPGFGDRRKAMLQDVAILTGGEVITEELGLDLKTASIDQLGRAS 319
Cdd:PRK12852 242 QSGKPLLIIAEDVEGEALATLVVNRLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGQLISEDLGIKLENVTLKMLGRAK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 320 KIVVTKENTTVVNGAGNAEDILARVNQIKAQLEETTSEFDREKLQERLAKLAGGVAVIKVGAATETELKERKLRIEDALN 399
Cdd:PRK12852 322 KVVIDKENTTIVNGAGKKADIEARVGQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKEKKDRVEDALN 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 400 STRAAVEEGIVAGGGTALVNIYNKVASIEADG-DTATGINIVLRAIEEPVRQIAHNAGLEGSVIVER-LKGEAVGTGFNA 477
Cdd:PRK12852 402 ATRAAVQEGIVPGGGVALLRAKKAVGRINNDNaDVQAGINIVLKALEAPIRQIAENAGVEGSIVVGKiLENKSETFGFDA 481
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 502820051 478 ATGEWVNMLDTGIVDPTKVTRSALQNASSVAAMFLTTEAVVADKPEENAAPAMP 531
Cdd:PRK12852 482 QTEEYVDMVAKGIIDPAKVVRTALQDAASVAGLLVTTEAMVAELPKKDAAPAMP 535
|
|
| PTZ00114 |
PTZ00114 |
Heat shock protein 60; Provisional |
2-532 |
0e+00 |
|
Heat shock protein 60; Provisional
Pssm-ID: 185455 Cd Length: 555 Bit Score: 712.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 2 AKDIKFSEEARRAMLRGVDTLANAVKVTLGPKGRNVVLEKKFGSPLITNDGVTIAKEIELEDAFENMGAKLVAEVASKTN 81
Cdd:PTZ00114 14 GKEIRFGDEARQSLLKGIERLADAVAVTLGPKGRNVIIEQEYGSPKITKDGVTVAKAIEFSDRFENVGAQLIRQVASKTN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 82 DVAGDGTTTATVLAQAMIREGLKNVTAGANPMGIRKGMEKAVAVAVEELKAISKPIQGKDSIAQVAAISA-ADEEVGQLI 160
Cdd:PTZ00114 94 DKAGDGTTTATILARAIFREGCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQSRPVKTKEDILNVATISAnGDVEIGSLI 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 161 AEAMERVGNDGVITLEESKGFTTELEVVEGMQFDRGYASPYMVTDSDKMEAVLDDPYILITDKKIGNIQEILPVLEQVVQ 240
Cdd:PTZ00114 174 ADAMDKVGKDGTITVEDGKTLEDELEVVEGMSFDRGYISPYFVTNEKTQKVELENPLILVTDKKISSIQSILPILEHAVK 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 241 QGKPLLIIAEDVEGEALATLVVNKLRGTFTAVAVKAPGFGDRRKAMLQDVAILTGGEVITEE-LGLDLKTASIDQLGRAS 319
Cdd:PTZ00114 254 NKRPLLIIAEDVEGEALQTLIINKLRGGLKVCAVKAPGFGDNRKDILQDIAVLTGATVVSEDnVGLKLDDFDPSMLGSAK 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 320 KIVVTKENTTVVNGAGNAEDILARVNQIKAQLEETTSEFDREKLQERLAKLAGGVAVIKVGAATETELKERKLRIEDALN 399
Cdd:PTZ00114 334 KVTVTKDETVILTGGGDKAEIKERVELLRSQIERTTSEYDKEKLKERLAKLSGGVAVIKVGGASEVEVNEKKDRIEDALN 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 400 STRAAVEEGIVAGGGTALVNIYNKVASIEAD----GDTATGINIVLRAIEEPVRQIAHNAGLEGSVIVER-LKGEAVGTG 474
Cdd:PTZ00114 414 ATRAAVEEGIVPGGGVALLRASKLLDKLEEDneltPDQRTGVKIVRNALRLPTKQIAENAGVEGAVVVEKiLEKKDPSFG 493
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502820051 475 FNAATGEWVNMLDTGIVDPTKVTRSALQNASSVAAMFLTTEAVVADKPEE---NAAPAMPD 532
Cdd:PTZ00114 494 YDAQTGEYVNMFEAGIIDPTKVVRSALVDAASVASLMLTTEAAIVDLPKEkkkNKNSAAPP 554
|
|
| PRK14104 |
PRK14104 |
chaperonin GroEL; Provisional |
2-531 |
0e+00 |
|
chaperonin GroEL; Provisional
Pssm-ID: 172594 Cd Length: 546 Bit Score: 628.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 2 AKDIKFSEEARRAMLRGVDTLANAVKVTLGPKGRNVVLEKKFGSPLITNDGVTIAKEIELEDAFENMGAKLVAEVASKTN 81
Cdd:PRK14104 3 AKEVKFGVDARDRMLRGVDILANAVKVTLGPKGRNVVLDKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVREVASKSA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 82 DVAGDGTTTATVLAQAMIREGLKNVTAGANPMGIRKGMEKAVAVAVEELKAISKPIQGKDSIAQVAAISA-ADEEVGQLI 160
Cdd:PRK14104 83 DAAGDGTTTATVLAQAIVREGAKSVAAGMNPMDLKRGIDLAVEAVVADLVKNSKKVTSNDEIAQVGTISAnGDAEIGKFL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 161 AEAMERVGNDGVITLEESKGFTTELEVVEGMQFDRGYASPYMVTDSDKMEAVLDDPYILITDKKIGNIQEILPVLEQVVQ 240
Cdd:PRK14104 163 ADAMKKVGNEGVITVEEAKSLETELDVVEGMQFDRGYISPYFVTNADKMRVEMDDAYILINEKKLSSLNELLPLLEAVVQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 241 QGKPLLIIAEDVEGEALATLVVNKLRGTFTAVAVKAPGFGDRRKAMLQDVAILTGGEVITEELGLDLKTASIDQLGRASK 320
Cdd:PRK14104 243 TGKPLVIVAEDVEGEALATLVVNRLRGGLKVAAVKAPGFGDRRKAMLQDIAILTGGQAISEDLGIKLENVTLQMLGRAKK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 321 IVVTKENTTVVNGAGNAEDILARVNQIKAQLEETTSEFDREKLQERLAKLAGGVAVIKVGAATETELKERKLRIEDALNS 400
Cdd:PRK14104 323 VMIDKENTTIVNGAGKKADIEARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKERKDRVDDAMHA 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 401 TRAAVEEGIVAGGGTALVNIYNKVASIE-ADGDTATGINIVLRAIEEPVRQIAHNAGLEGSVIVER-LKGEAVGTGFNAA 478
Cdd:PRK14104 403 TRAAVEEGIVPGGGVALLRASEQLKGIKtKNDDQKTGVEIVRKALSAPARQIAINAGEDGSVIVGKiLEKEQYSYGFDSQ 482
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 502820051 479 TGEWVNMLDTGIVDPTKVTRSALQNASSVAAMFLTTEAVVADKPEENAA-PAMP 531
Cdd:PRK14104 483 TGEYGNLVSKGIIDPTKVVRTAIQNAASVAALLITTEAMVAELPKKGGAgPAMP 536
|
|
| 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: 552.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 2 AKDIKFSEE--ARRAMLRGVDTLANAVKVTLGPKGRNVVLEKKFGSPLITNDGVTIAKEIELEDAFENMGAKLVAEVASK 79
Cdd:PLN03167 56 AKELHFNKDgsAIKKLQAGVNKLADLVGVTLGPKGRNVVLESKYGSPKIVNDGVTVAKEVELEDPVENIGAKLVRQAAAK 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 80 TNDVAGDGTTTATVLAQAMIREGLKNVTAGANPMGIRKGMEKAVAVAVEELKAISKPIQGKDsIAQVAAISAADE-EVGQ 158
Cdd:PLN03167 136 TNDLAGDGTTTSVVLAQGLIAEGVKVVAAGANPVQITRGIEKTAKALVKELKKMSKEVEDSE-LADVAAVSAGNNyEVGN 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 159 LIAEAMERVGNDGVITLEESKGFTTELEVVEGMQFDRGYASPYMVTDSDKMEAVLDDPYILITDKKIGNIQEILPVLEQV 238
Cdd:PLN03167 215 MIAEAMSKVGRKGVVTLEEGKSAENNLYVVEGMQFDRGYISPYFVTDSEKMSVEYDNCKLLLVDKKITNARDLIGILEDA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 239 VQQGKPLLIIAEDVEGEALATLVVNKLRGTFTAVAVKAPGFGDRRKAMLQDVAILTGGEVITEELGLDLKTASIDQLGRA 318
Cdd:PLN03167 295 IRGGYPLLIIAEDIEQEALATLVVNKLRGSLKIAALKAPGFGERKSQYLDDIAILTGGTVIREEVGLSLDKVGKEVLGTA 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 319 SKIVVTKENTTVVNGAGNAEDILARVNQIKAQLEETTSEFDREKLQERLAKLAGGVAVIKVGAATETELKERKLRIEDAL 398
Cdd:PLN03167 375 AKVVLTKDTTTIVGDGSTQEAVNKRVAQIKNLIEAAEQDYEKEKLNERIAKLSGGVAVIQVGAQTETELKEKKLRVEDAL 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 399 NSTRAAVEEGIVAGGGTALVNIYNKVASIE---ADGDTATGINIVLRAIEEPVRQIAHNAGLEGSVIVER-LKGEAVGTG 474
Cdd:PLN03167 455 NATKAAVEEGIVVGGGCTLLRLASKVDAIKdtlENDEQKVGADIVKRALSYPLKLIAKNAGVNGSVVSEKvLSNDNPKFG 534
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 502820051 475 FNAATGEWVNMLDTGIVDPTKVTRSALQNASSVAAMFLTTEAVVADKPEENAAPA 529
Cdd:PLN03167 535 YNAATGKYEDLMAAGIIDPTKVVRCCLEHAASVAKTFLTSDCVVVEIKEPEPVPA 589
|
|
| chaperonin_type_I_II |
cd00309 |
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ... |
3-519 |
8.99e-156 |
|
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: 453.04 E-value: 8.99e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 3 KDIKFSEEARRAMLRGVDTLANAVKVTLGPKGRNVVLEKKFGSPLITNDGVTIAKEIELEdafeNMGAKLVAEVASKTND 82
Cdd:cd00309 1 KEREFGEEARLSNINAAKALADAVKTTLGPKGMDKMLVDSLGDPTITNDGATILKEIEVE----HPAAKLLVEVAKSQDD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 83 VAGDGTTTATVLAQAMIREGLKNVTAGANPMGIRKGMEKAVAVAVEELKAISKPIQ--GKDSIAQVAAISAA-------D 153
Cdd:cd00309 77 EVGDGTTTVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVPIDveDREELLKVATTSLNsklvsggD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 154 EEVGQLIAEAMERVG------NDGVITLEESKGFT-TELEVVEGMQFDRGYASPYmvtdsdkMEAVLDDPYILITDKKIG 226
Cdd:cd00309 157 DFLGELVVDAVLKVGkengdvDLGVIRVEKKKGGSlEDSELVVGMVFDKGYLSPY-------MPKRLENAKILLLDCKLE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 227 NiqeilpvleqvvqqgkplLIIAED-VEGEALATLVVNKLrgtftaVAVKApgfgdRRKAMLQDVAILTGGEVITEelgl 305
Cdd:cd00309 230 Y------------------VVIAEKgIDDEALHYLAKLGI------MAVRR-----VRKEDLERIAKATGATIVSR---- 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 306 dLKTASIDQLGRASKIVVTK----ENTTVVNGAGnaedilarvnqikaqleettsefdreklqerlaklaGGVAVIKVGA 381
Cdd:cd00309 277 -LEDLTPEDLGTAGLVEETKigdeKYTFIEGCKG------------------------------------GKVATILLRG 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 382 ATETELKERKLRIEDALNSTRAAVEE-GIVAGGGTALVNIYNKVASI--EADGDTATGINIVLRAIEEPVRQIAHNAGLE 458
Cdd:cd00309 320 ATEVELDEAERSLHDALCAVRAAVEDgGIVPGGGAAEIELSKALEELakTLPGKEQLGIEAFADALEVIPRTLAENAGLD 399
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502820051 459 GSVIVERLKGEAVGTGFNAA----TGEWVNMLDTGIVDPTKVTRSALQNASSVAAMFLTTEAVVA 519
Cdd:cd00309 400 PIEVVTKLRAKHAEGGGNAGgdveTGEIVDMKEAGIIDPLKVKRQALKSATEAASLILTIDDIIV 464
|
|
| Cpn60_TCP1 |
pfam00118 |
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ... |
22-521 |
3.77e-86 |
|
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: 274.85 E-value: 3.77e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 22 LANAVKVTLGPKGRNVVLEKKFGSPLITNDGVTIAKEIELEDAfenmGAKLVAEVASKTNDVAGDGTTTATVLAQAMIRE 101
Cdd:pfam00118 1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELEIQHP----AAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 102 GLKNVTAGANPMGIRKGMEKAVAVAVEELK---AISKPIQGKDSIAQVAAISAA-------DEEVGQLIAEAMER----- 166
Cdd:pfam00118 77 AEKLLAAGVHPTTIIEGYEKALEKALEILDsiiSIPVEDVDREDLLKVARTSLSskiisreSDFLAKLVVDAVLAipknd 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 167 ----VGNDGVITLEESKGftTELEVVEGMQFDRGYASPYMVTDsdkmeavLDDPYILITDKKIGNIQE------------ 230
Cdd:pfam00118 157 gsfdLGNIGVVKILGGSL--EDSELVDGVVLDKGPLHPDMPKR-------LENAKVLLLNCSLEYEKTetkatvvlsdae 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 231 ------------ILPVLEQVVQQGKPLLIIAEDVEGEALATLVVNKLRGTFTAvavkapgfgdrRKAMLQDVAILTGGEV 298
Cdd:pfam00118 228 qlerflkaeeeqILEIVEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMALRRV-----------KKRDLERLAKATGARA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 299 ITeelglDLKTASIDQLGRASKI---VVTKENTTVVNGAGNaedilarvnqikaqleettsefdreklqerlaklaGGVA 375
Cdd:pfam00118 297 VS-----SLDDLTPDDLGTAGKVeeeKIGDEKYTFIEGCKS-----------------------------------PKAA 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 376 VIKVGAATETELKERKLRIEDALNSTRAAVEE-GIVAGGGTALVNIYNKVASI--EADGDTATGINIVLRAIEEPVRQIA 452
Cdd:pfam00118 337 TILLRGATDHVLDEIERSIHDALCVVKNAIEDpRVVPGGGAVEMELARALREYakSVSGKEQLAIEAFAEALEVIPKTLA 416
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502820051 453 HNAGLEGSVIVERLKGEAVG----TGFNAATGEWVNMLDTGIVDPTKVTRSALQNASSVAAMFLTTEAVVADK 521
Cdd:pfam00118 417 ENAGLDPIEVLAELRAAHASgekhAGIDVETGEIIDMKEAGVVDPLKVKRQALKSATEAASTILRIDDIIKAK 489
|
|
| chaperonin_like |
cd03333 |
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ... |
140-407 |
3.57e-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: 144.53 E-value: 3.57e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 140 KDSIAQVAAISAA------DEEVGQLIAEAMERVG------NDGVITLEESKGFT-TELEVVEGMQFDRGYASPYmvtds 206
Cdd:cd03333 1 RELLLQVATTSLNsklsswDDFLGKLVVDAVLKVGpdnrmdDLGVIKVEKIPGGSlEDSELVVGVVFDKGYASPY----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 207 dkMEAVLDDPYILITDKKIGNiqeilpvleqvvqqgkplLIIAED-VEGEALATLVVNKLrgtftaVAVKApgfgdRRKA 285
Cdd:cd03333 76 --MPKRLENAKILLLDCPLEY------------------VVIAEKgIDDLALHYLAKAGI------MAVRR-----VKKE 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 286 MLQDVAILTGGEVITEelgldLKTASIDQLGRASKIVVTK----ENTTVVNGAGnaedilarvnqikaqleettsefdre 361
Cdd:cd03333 125 DLERIARATGATIVSS-----LEDLTPEDLGTAELVEETKigeeKLTFIEGCKG-------------------------- 173
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 502820051 362 klqerlaklaGGVAVIKVGAATETELKERKLRIEDALNSTRAAVEE 407
Cdd:cd03333 174 ----------GKAATILLRGATEVELDEVKRSLHDALCAVRAAVEE 209
|
|
| cpn60 |
cd03343 |
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ... |
9-519 |
4.75e-30 |
|
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: 123.53 E-value: 4.75e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 9 EEARRAMLRGVDTLANAVKVTLGPKGRNVVLEKKFGSPLITNDGVTIAKEIELedafENMGAKLVAEVASKTNDVAGDGT 88
Cdd:cd03343 14 RDAQRMNIAAAKAVAEAVRTTLGPKGMDKMLVDSLGDVTITNDGATILKEMDI----EHPAAKMLVEVAKTQDEEVGDGT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 89 TTATVLAQAMIREGLKNVTAGANPMGIRKGMEKAVAVAVEELKAISKPIQGKD-----SIAQVAAISAADEEVGQLIAE- 162
Cdd:cd03343 90 TTAVVLAGELLEKAEDLLDQNIHPTVIIEGYRLAAEKALELLDEIAIKVDPDDkdtlrKIAKTSLTGKGAEAAKDKLADl 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 163 ------AMERVGNDGV------ITLEESKGFTTE-LEVVEGMQFDRGYASPymvtdsdKMEAVLDDPYILITDKKIgNIQ 229
Cdd:cd03343 170 vvdavlQVAEKRDGKYvvdldnIKIEKKTGGSVDdTELIRGIVIDKEVVHP-------GMPKRVENAKIALLDAPL-EVK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 230 EilPVLEQVVQQGKPLLIIAEDVEGEALATLVVNKLRGTFTAVAVKAPGFGDRRKAMLQDVAILTGGEViteelgldlKT 309
Cdd:cd03343 242 K--TEIDAKIRITSPDQLQAFLEQEEAMLKEMVDKIADTGANVVFCQKGIDDLAQHYLAKAGILAVRRV---------KK 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 310 ASIDQLGRAS--KIVVTKENTTvvngagnAEDILArvnqikAQLEETTSEFDREKLQERLAKLAGGVAVIKVGaATETEL 387
Cdd:cd03343 311 SDMEKLARATgaKIVTNIDDLT-------PEDLGE------AELVEERKVGDDKMVFVEGCKNPKAVTILLRG-GTEHVV 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 388 KERKLRIEDALNSTRAAVEEG-IVAGGGTALVNIYNKVASiEAD---GDTATGINIVLRAIEEPVRQIAHNAGLEG-SVI 462
Cdd:cd03343 377 DELERALEDALRVVADALEDGkVVAGGGAVEIELAKRLRE-YARsvgGREQLAVEAFADALEEIPRTLAENAGLDPiDTL 455
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 463 VERLKGEAVG---TGFNAATGEWVNMLDTGIVDPTKVTRSALQNASSVAAMFLTTEAVVA 519
Cdd:cd03343 456 VELRAAHEKGnknAGLDVYTGEVVDMLEKGVIEPLRVKKQAIKSATEAATMILRIDDVIA 515
|
|
| thermosome_beta |
NF041083 |
thermosome subunit beta; |
10-521 |
2.29e-29 |
|
thermosome subunit beta;
Pssm-ID: 469010 Cd Length: 519 Bit Score: 121.60 E-value: 2.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 10 EARRAMLRGVDTLANAVKVTLGPKGRNVVLEKKFGSPLITNDGVTIAKEIELedafENMGAKLVAEVASKTNDVAGDGTT 89
Cdd:NF041083 17 DAQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDIVITNDGATILKEMDV----QHPAAKMLVEVAKTQDDEVGDGTT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 90 TATVLAQAMIREGLKNVTAGANPMGIRKGMEKAVAVAVEELKAISKPIQGKD-----SIAQVA----AISAADEEVGQLI 160
Cdd:NF041083 93 TAVVLAGELLKKAEELLDQNIHPTIIANGYRLAAEKAIEILDEIAEKVDPDDretlkKIAETSltskGVEEARDYLAEIA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 161 AEAMERVGN----------DGVITLEESKGFTTELEVVEGMQFDRGYASPymvtdsdKMEAVLDDPYILITDKKIgNIQE 230
Cdd:NF041083 173 VKAVKQVAEkrdgkyyvdlDNIQIEKKHGGSIEDTQLIYGIVIDKEVVHP-------GMPKRVENAKIALLDAPL-EVKK 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 231 ilPVLEQVVQQGKPLLIIAEDVEGEALATLVVNKLRGTFTAVAVKAPGFGD--------------RR--KAMLQDVAILT 294
Cdd:NF041083 245 --TEIDAEIRITDPDQLQKFLDQEEKMLKEMVDKIKATGANVVFCQKGIDDlaqhylakagilavRRvkKSDMEKLAKAT 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 295 GGEVITeelglDLKTASIDQLGRASKI---VVTKENTTVVNGAGN--AEDILARvnqikaqleettsefdreklqerlak 369
Cdd:NF041083 323 GARIVT-----NIDDLTPEDLGYAELVeerKVGDDKMVFVEGCKNpkAVTILIR-------------------------- 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 370 laGGvavikvgaaTETELKERKLRIEDALNSTRAAVEEG-IVAGGGTALVNIYNKVASIEAD--GDTATGINIVLRAIEE 446
Cdd:NF041083 372 --GG---------TEHVVDEAERALEDALSVVADAVEDGkIVAGGGAPEVELAKRLREYAATvgGREQLAVEAFAEALEI 440
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502820051 447 PVRQIAHNAGLEGSVIVERLKGE----AVGTGFNAATGEWVNMLDTGIVDPTKVTRSALQNASSVAAMFLTTEAVVADK 521
Cdd:NF041083 441 IPRTLAENAGLDPIDILVKLRSAhekgKKWAGINVFTGEVVDMWELGVIEPLRVKTQAIKSATEAATMILRIDDVIAAK 519
|
|
| thermosome_alpha |
NF041082 |
thermosome subunit alpha; |
10-519 |
3.43e-27 |
|
thermosome subunit alpha;
Pssm-ID: 469009 Cd Length: 518 Bit Score: 114.98 E-value: 3.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 10 EARRAMLRGVDTLANAVKVTLGPKGRNVVLEKKFGSPLITNDGVTIAKEIELedafENMGAKLVAEVASKTNDVAGDGTT 89
Cdd:NF041082 17 DAQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDVVITNDGVTILKEMDI----EHPAAKMIVEVAKTQDDEVGDGTT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 90 TATVLAQAMIREGLKNVTAGANPMGIRKGMEKAVAVAVEELKAISKPIQGKD-----SIAQVA----AISAADEEVGQLI 160
Cdd:NF041082 93 TAVVLAGELLKKAEELLDQDIHPTIIAEGYRLAAEKALEILDEIAIKVDPDDketlkKIAATAmtgkGAEAAKDKLADLV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 161 AEA----MERVGNDGV----ITLEESKGFTTE-LEVVEGMQFDRGYASPYMVTDSDKME-AVLDDPY----------ILI 220
Cdd:NF041082 173 VDAvkavAEKDGGYNVdldnIKVEKKVGGSIEdSELVEGVVIDKERVHPGMPKRVENAKiALLDAPLevkkteidakISI 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 221 TDkkIGNIQEILPvleqvvQQGKPLLIIAEDVEgEALATLV-----VNKLRGTFTAvavKAPGFGDRR--KAMLQDVAIL 293
Cdd:NF041082 253 TD--PDQLQAFLD------QEEKMLKEMVDKIA-DSGANVVfcqkgIDDLAQHYLA---KEGILAVRRvkKSDMEKLAKA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 294 TGGEVITeelglDLKTASIDQLGRASKIV---VTKENTTVVNGAGNAedilarvnqiKAqleettsefdreklqerlakl 370
Cdd:NF041082 321 TGARIVT-----SIDDLSPEDLGYAGLVEerkVGGDKMIFVEGCKNP----------KA--------------------- 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 371 aggVAVIKVGaATETELKERKLRIEDALNSTRAAVEEG-IVAGGGTALVNIYNKVASiEAD---GDTATGINIVLRAIEE 446
Cdd:NF041082 365 ---VTILLRG-GTEHVVDEVERALEDALRVVRVVLEDGkVVAGGGAPEVELALRLRE-YAAsvgGREQLAIEAFAEALEI 439
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502820051 447 PVRQIAHNAGLEG-SVIVE-RLKGEA--VGTGFNAATGEWVNMLDTGIVDPTKVTRSALQNASSVAAMFLTTEAVVA 519
Cdd:NF041082 440 IPRTLAENAGLDPiDALVElRSAHEKgnKTAGLDVYTGKVVDMLEIGVVEPLRVKTQAIKSATEAAVMILRIDDVIA 516
|
|
| TCP1_delta |
cd03338 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ... |
22-512 |
3.58e-20 |
|
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: 93.51 E-value: 3.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 22 LANAVKVTLGPKGRNVVLEKKFGSPLITNDGVTIAKEIELEDAfenmGAKLVAEVaSKTNDV-AGDGTTTATVLAQAMIR 100
Cdd:cd03338 20 VADAIRTSLGPRGMDKMIQTGKGEVIITNDGATILKQMSVLHP----AAKMLVEL-SKAQDIeAGDGTTSVVVLAGALLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 101 EGLKNVTAGANPMGIRKGMEKAVAVAVEELKAISKPIQGKD-----SIAQVAAISAADEEVGQLIAE----AMERVGNDG 171
Cdd:cd03338 95 ACESLLKKGIHPTVISESFQIAAKKAVEILDSMSIPVDLNDresliKSATTSLNSKVVSQYSSLLAPiavdAVLKVIDPA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 172 VITLEESK---------GFTTELEVVEGMQFDRGYAS------------------------PYM-----VTDSDKMEAVL 213
Cdd:cd03338 175 TATNVDLKdirivkklgGTIEDTELVDGLVFTQKASKkaggptriekakigliqfclsppkTDMdnnivVNDYAQMDRIL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 214 DDpyilitDKKIgniqeILPVLEQVVQQGKPLLIIAEDVEGEALATLvvnklrgtftavavkAPGFGDRRKAML------ 287
Cdd:cd03338 255 RE------ERKY-----ILNMCKKIKKSGCNVLLIQKSILRDAVSDL---------------ALHFLAKLKIMVvkdier 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 288 QDVailtggEVITEELGLdLKTASIDQLgRASKIvvtkenttvvngaGNAEDIlarvnqikaqlEETTSEFDREKLQERL 367
Cdd:cd03338 309 EEI------EFICKTIGC-KPVASIDHF-TEDKL-------------GSADLV-----------EEVSLGDGKIVKITGV 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 368 AKLAGGVAVIkVGAATETELKERKLRIEDALNSTRAAVEE-GIVAGGGTALVNIYNKVAsieADGDTATGIN-IVLRAIE 445
Cdd:cd03338 357 KNPGKTVTIL-VRGSNKLVLDEAERSLHDALCVIRCLVKKrALIPGGGAPEIEIALQLS---EWARTLTGVEqYCVRAFA 432
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502820051 446 EPVRQI----AHNAGLEGSVIVERLKGE-AVG---TGFNAATGEWVNMLDTGIVDPTKVTRSALQNASSVAAMFL 512
Cdd:cd03338 433 DALEVIpytlAENAGLNPISIVTELRNRhAQGeknAGINVRKGAITNILEENVVQPLLVSTSAITLATETVRMIL 507
|
|
| chap_CCT_epsi |
TIGR02343 |
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ... |
10-137 |
9.43e-17 |
|
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: 83.31 E-value: 9.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 10 EARRAMLRGVDTLANAVKVTLGPKGRNVVLEKKFGSPLITNDGVTIAKEIELEdafeNMGAKLVAEVASKTNDVAGDGTT 89
Cdd:TIGR02343 27 EAKKSNIAAAKSVASILRTSLGPKGMDKMLISPDGDITVTNDGATILSQMDVD----NQIAKLMVELSKSQDDEIGDGTT 102
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 502820051 90 TATVLAQAMIREGLKNVTAGANPMGIRKGMEKAVAVAVEELKAISKPI 137
Cdd:TIGR02343 103 GVVVLAGALLEQAEELLDKGIHPIKIADGFEEAARIAVEHLEEISDEI 150
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
9-134 |
2.79e-16 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 81.61 E-value: 2.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 9 EEARRAMLRGVDTLANAVKVTLGPKGRNVVLEK-----KFGSPLITNDGVTIAKEIELEdafeNMGAKLVAEVASKTNDV 83
Cdd:PTZ00212 21 ETARLQSFVGAIAVADLVKTTLGPKGMDKILQPmsegpRSGNVTVTNDGATILKSVWLD----NPAAKILVDISKTQDEE 96
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 502820051 84 AGDGTTTATVLAQAMIREGLKNVTAGANPMGIRKGMEKAVAVAVEELKAIS 134
Cdd:PTZ00212 97 VGDGTTSVVVLAGELLREAEKLLDQKIHPQTIIEGWRMALDVARKALEEIA 147
|
|
| TCP1_beta |
cd03336 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ... |
9-134 |
7.55e-16 |
|
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: 80.07 E-value: 7.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 9 EEARRAMLRGVDTLANAVKVTLGPKGRNVVLE--KKFGSPLITNDGVTIAKEIELEdafeNMGAKLVAEVASKTNDVAGD 86
Cdd:cd03336 12 ETARLSSFVGAIAIGDLVKTTLGPKGMDKILQsvGRSGGVTVTNDGATILKSIGVD----NPAAKVLVDISKVQDDEVGD 87
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 502820051 87 GTTTATVLAQAMIREGLKNVTAGANPMGIRKGMEKAVAVAVEELKAIS 134
Cdd:cd03336 88 GTTSVTVLAAELLREAEKLVAQKIHPQTIIEGYRMATAAAREALLSSA 135
|
|
| TCP1_epsilon |
cd03339 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ... |
9-137 |
8.65e-16 |
|
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: 80.04 E-value: 8.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 9 EEARRAMLRGVD----------TLANAVKVTLGPKGRNVVLEKKFGSPLITNDGVTIAKEIELEdafeNMGAKLVAEVAS 78
Cdd:cd03339 12 EQEKKKRLKGLEahkshilaakSVANILRTSLGPRGMDKILVSPDGEVTVTNDGATILEKMDVD----HQIAKLLVELSK 87
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 502820051 79 KTNDVAGDGTTTATVLAQAMIREGLKNVTAGANPMGIRKGMEKAVAVAVEELKAISKPI 137
Cdd:cd03339 88 SQDDEIGDGTTGVVVLAGALLEQAEKLLDRGIHPIRIADGYEQACKIAVEHLEEIADKI 146
|
|
| chap_CCT_eta |
TIGR02345 |
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ... |
16-521 |
9.20e-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: 73.64 E-value: 9.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 16 LRGVDTLANAVKVTLGPKGRNVVLEKKFGSPLITNDGVTIAKEIELedafENMGAKLVAEVASKTNDVAGDGTTTATVLA 95
Cdd:TIGR02345 24 INACVAIAEALKTTLGPRGMDKLIVGSNGKATISNDGATILKLLDI----VHPAAKTLVDIAKSQDAEVGDGTTSVTILA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 96 QAMIREGLKNVTAGANPMGIRKGMEKAVAVAVEELKAISKPI-QGKDSIAQVAAISAADEEVGQLIAEAME---RVGNDG 171
Cdd:TIGR02345 100 GELLKEAKPFIEEGVHPQLIIRCYREALSLAVEKIKEIAVTIdEEKGEQRELLEKCAATALSSKLISHNKEffsKMIVDA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 172 VITLEESK-------------GFTTELEVVEGMQFDRG------------YASPYM-------------------VTDSD 207
Cdd:TIGR02345 180 VLSLDRDDldlkligikkvqgGALEDSQLVNGVAFKKTfsyagfeqqpkkFANPKIlllnvelelkaekdnaeirVEDVE 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 208 KMEAVLDDPYILITDKkigniqeilpvLEQVVQQGkplliiaedvegealATLVVNKLrgtftavavkapGFGDRRKAML 287
Cdd:TIGR02345 260 DYQAIVDAEWAIIFRK-----------LEKIVESG---------------ANVVLSKL------------PIGDLATQYF 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 288 QDVAILTGGEVITEElgldlktasidqLGRASKIVvtkenttvvnGAgnaeDILARVNQIKAQLEETTSEFDREKL-QER 366
Cdd:TIGR02345 302 ADRDIFCAGRVSAED------------LKRVIKAC----------GG----SIQSTTSDLEADVLGTCALFEERQIgSER 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 367 LAKLAGG----VAVIKVGAATETELKERKLRIEDALNSTRAAVE-EGIVAGGGTALVNI--YNKVASIEADGDTATGINI 439
Cdd:TIGR02345 356 YNYFTGCphakTCTIILRGGAEQFIEEAERSLHDAIMIVRRALKnKKIVAGGGAIEMELskCLRDYSKTIDGKQQLIINA 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 440 VLRAIEEPVRQIAHNAGLEGSVIVERLK------GEAVGTGFNaaTGEWVNMLDTGIVDPTKVTRSALQNASSVAAMFLT 513
Cdd:TIGR02345 436 FAKALEIIPRQLCENAGFDSIEILNKLRsrhakgGKWYGVDIN--TEDIGDNFEAFVWEPALVKINALKAAFEAACTILS 513
|
....*...
gi 502820051 514 TEAVVADK 521
Cdd:TIGR02345 514 VDETITNP 521
|
|
| chap_CCT_delta |
TIGR02342 |
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ... |
9-519 |
1.21e-13 |
|
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: 73.28 E-value: 1.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 9 EEARRAMLRGVDTLANAVKVTLGPKGRNVVLEKKFGSPLITNDGVTIAKEIELEdafeNMGAKLVAEVaSKTNDV-AGDG 87
Cdd:TIGR02342 8 QDVRTSNIVAAKAVADAIRTSLGPKGMDKMIQDGKGEVIITNDGATILKQMAVL----HPAAKMLVEL-SKAQDIeAGDG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 88 TTTATVLAQAMIREGLKNVTAGANPMGIRKGMEKAVAVAVEELKAISKPIQGKD--SIAQVAAISAADEEVGQ------- 158
Cdd:TIGR02342 83 TTSVVILAGALLGACERLLNKGIHPTIISESFQSAADEAIKILDEMSIPVDLSDreQLLKSATTSLSSKVVSQyssllap 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 159 LIAEAMERV---GNDGVITLEESK------GFTTELEVVEGMQFD------RGYAS------------------PYM--- 202
Cdd:TIGR02342 163 LAVDAVLKVidpENAKNVDLNDIKvvkklgGTIDDTELIEGLVFTqkasksAGGPTriekakigliqfqisppkTDMenq 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 203 --VTDSDKMEAVLDDPYilitdkkigniQEILPVLEQVVQQGKPLLIIAEDVEGEALATLVVNklrgtftavavkapgFG 280
Cdd:TIGR02342 243 iiVNDYAQMDRVLKEER-----------AYILNIVKKIKKTGCNVLLIQKSILRDAVNDLALH---------------FL 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 281 DRRKAML------QDVailtggEVITEELGLdLKTASIDQLgraskivvtkenttvvngagnAEDILArvnqiKAQLEET 354
Cdd:TIGR02342 297 AKMKIMVvkdierEEI------EFICKTIGC-KPIASIDHF---------------------TADKLG-----SAELVEE 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 355 TSEFDREKLQERLAKLAGGVAVIKVGAATETELKERKLRIEDALNSTRAAVEE-GIVAGGGTALVNIYNKVA--SIEADG 431
Cdd:TIGR02342 344 VDSDGGKIIKITGIQNAGKTVTVVVRGSNKLVIDEAERSLHDALCVIRCLVKKrGLIAGGGAPEIEIARRLSkyARTMKG 423
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 432 DTATGINIVLRAIEEPVRQIAHNAGLEGSVIVERLKGE-AVG---TGFNAATGEWVNMLDTGIVDPTKVTRSALQNASSV 507
Cdd:TIGR02342 424 VESYCVRAFADALEVIPYTLAENAGLNPIKVVTELRNRhANGektAGISVRKGGITNMLEEHVLQPLLVTTSAITLASET 503
|
570
....*....|..
gi 502820051 508 AAMFLTTEAVVA 519
Cdd:TIGR02342 504 VRSILKIDDIVF 515
|
|
| chap_CCT_beta |
TIGR02341 |
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ... |
8-522 |
1.52e-13 |
|
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: 72.97 E-value: 1.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 8 SEEARRAMLRGVDTLANAVKVTLGPKGRNVVLEK--KFGSPLITNDGVTIAKEIeledAFENMGAKLVAEVASKTNDVAG 85
Cdd:TIGR02341 12 AENARLSSFVGAIAIGDLVKSTLGPKGMDKILQSssSDASIMVTNDGATILKSI----GVDNPAAKVLVDMSKVQDDEVG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 86 DGTTTATVLAQAMIREGLKNVTAGANPMGIRKGMEKAVAVAVEELKAIS-----KPIQGKDSIAQVAA-------ISAAD 153
Cdd:TIGR02341 88 DGTTSVTVLAAELLREAEKLINQKIHPQTIIAGYREATKAARDALLKSAvdngsDEVKFRQDLMNIARttlsskiLSQHK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 154 EEVGQLIAEAMERV---GN-DGVITLEESKGFTTELEVVEGMQFDR--GYASPYMVTDSDKMEA--VLDDPYILITDKKI 225
Cdd:TIGR02341 168 DHFAQLAVDAVLRLkgsGNlEAIQIIKKLGGSLADSYLDEGFLLDKkiGVNQPKRIENAKILIAntGMDTDKVKIFGSRV 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 226 -----GNIQEiLPVLEQVVQQGKPLLIIAEDVEGEALATLVVNKLRGTFTAVAVKAPGFGDRRKamLQDVAILTGGEVIT 300
Cdd:TIGR02341 248 rvdstAKVAE-LEHAEKEKMKEKVEKILKHGINCFINRQLIYNYPEQLFADAGVMAIEHADFEG--VERLALVTGGEIVS 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 301 EelgldLKTASIDQLGRASKIvvtkENTTVvngagnAEDILARVNQIKaqleettsefdreklqerlaklAGGVAVIKVG 380
Cdd:TIGR02341 325 T-----FDHPELVKLGSCDLI----EEIMI------GEDKLLKFSGVK----------------------LGEACTIVLR 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 381 AATETELKERKLRIEDALNSTRAAVEEGIVAGGGTALVNIYNKVASIEA---DGDTATGINIVLRAIEEPVRQIAHNAGL 457
Cdd:TIGR02341 368 GATQQILDEAERSLHDALCVLSQTVKESRTVLGGGCSEMLMSKAVTQEAqrtPGKEALAVEAFARALRQLPTIIADNAGF 447
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502820051 458 EGSVIVERLKGEAVG----TGFNAATGEWVNMLDTGIVDPTKVTRSALQNASSVAAMFLTTEAVVADKP 522
Cdd:TIGR02341 448 DSAELVAQLRAAHYNgnttMGLDMNEGTIADMRQLGITESYKVKRAVVSSAAEAAEVILRVDNIIKAAP 516
|
|
| TCP1_eta |
cd03340 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ... |
23-512 |
7.37e-13 |
|
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: 70.78 E-value: 7.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 23 ANAVKVTLGPKGRNVVLEKKFGSPLITNDGVTIAKEIELEdafeNMGAKLVAEVASKTNDVAGDGTTTATVLAQAMIREG 102
Cdd:cd03340 29 ADAVRTTLGPRGMDKLIVDGRGKVTISNDGATILKLLDIV----HPAAKTLVDIAKSQDAEVGDGTTSVVVLAGEFLKEA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 103 LKNVTAGANPMGIRKGMEKAVAVAVEELKAISKPIQGKDS------IAQVAA-------ISAADEEVGQLIAEAMERVGN 169
Cdd:cd03340 105 KPFIEDGVHPQIIIRGYRKALQLAIEKIKEIAVNIDKEDKeeqrelLEKCAAtalnsklIASEKEFFAKMVVDAVLSLDD 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 170 DGVITL----EESKGFTTELEVVEGMQFDRG------------YASPYM-------------------VTDSDKMEAVLD 214
Cdd:cd03340 185 DLDLDMigikKVPGGSLEDSQLVNGVAFKKTfsyagfeqqpkkFKNPKIlllnvelelkaekdnaevrVEDPEEYQAIVD 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 215 DPYILITDKkigniqeilpvLEQVVQQGkplliiaedvegealATLVVNKLrgtftavavkapGFGDRRKAMLQDVAILT 294
Cdd:cd03340 265 AEWKIIYDK-----------LEKIVKSG---------------ANVVLSKL------------PIGDLATQYFADRDIFC 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 295 GGEVITEelglDLKtasidqlgraskivvtkentTVVNGAGNAedILARVNQIKAQLEETTSEFDREKL-QERLAKLAGG 373
Cdd:cd03340 307 AGRVPEE----DLK--------------------RVAQATGGS--IQTTVSNITDDVLGTCGLFEERQVgGERYNIFTGC 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 374 VA------VIKVGAATETELKERKLriEDALNSTRAAVEEG-IVAGGGTALVNI--YNKVASIEADGDTATGINIVLRAI 444
Cdd:cd03340 361 PKaktctiILRGGAEQFIEEAERSL--HDAIMIVRRAIKNDsVVAGGGAIEMELskYLRDYSRTIAGKQQLVINAFAKAL 438
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502820051 445 EEPVRQIAHNAGLEGSVIVERL-----KGEAVGTGFNAATGEWVNMLDTGIVDPTKVTRSALQNASSVAAMFL 512
Cdd:cd03340 439 EIIPRQLCDNAGFDATDILNKLrqkhaQGGGKWYGVDINNEGIADNFEAFVWEPSLVKINALTAATEAACLIL 511
|
|
| TCP1_alpha |
cd03335 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ... |
9-167 |
4.88e-11 |
|
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: 65.00 E-value: 4.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 9 EEARRAMLRGVDTLANAVKVTLGPKGRNVVLEKKFGSPLITNDGVTIAKEIELEDAfenmGAKLVAEVASKTNDVAGDGT 88
Cdd:cd03335 7 QDVRTQNVTAAMAIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHP----AAKILVELAQLQDKEVGDGT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 89 TTATVLAQAMIREGLKNVTAGANPMGIRKGMEKAVAVAV---EELKAISKPIQGKDSIAQVAA-------ISAADEEVGQ 158
Cdd:cd03335 83 TSVVIIAAELLKRANELVKQKIHPTTIISGYRLACKEAVkyiKEHLSISVDNLGKESLINVAKtsmsskiIGADSDFFAN 162
|
....*....
gi 502820051 159 LIAEAMERV 167
Cdd:cd03335 163 MVVDAILAV 171
|
|
| chap_CCT_alpha |
TIGR02340 |
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ... |
22-167 |
1.62e-10 |
|
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: 63.59 E-value: 1.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 22 LANAVKVTLGPKGRNVVLEKKFGSPLITNDGVTIAKEIELEDAfenmGAKLVAEVASKTNDVAGDGTTTATVLAQAMIRE 101
Cdd:TIGR02340 24 IANIVKTSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHP----AAKILVELAQLQDREVGDGTTSVVIIAAELLKR 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502820051 102 GLKNVTAGANPMGIRKGMEKAVAVAV---EELKAISKPIQGKDSIAQVAA-------ISAADEEVGQLIAEAMERV 167
Cdd:TIGR02340 100 ADELVKNKIHPTSVISGYRLACKEAVkyiKENLSVSVDELGREALINVAKtsmsskiIGLDSDFFSNIVVDAVLAV 175
|
|
| TCP1_gamma |
cd03337 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ... |
21-152 |
6.55e-09 |
|
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: 58.08 E-value: 6.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 21 TLANAVKVTLGPKGRNVVLEKKFGSPLITNDGVTIAKEIELEdafeNMGAKLVAEVASKTNDVAGDGTTTATVLAQAMIR 100
Cdd:cd03337 27 TVADVIRTCLGPRAMLKMLLDPMGGIVLTNDGNAILREIDVA----HPAAKSMIELSRTQDEEVGDGTTSVIILAGEILA 102
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 502820051 101 EGLKNVTAGANPMGIRKGMEKAVAVAVEELKAISKPIQGKDSIAQVAAISAA 152
Cdd:cd03337 103 VAEPFLERGIHPTVIIKAYRKALEDALKILEEISIPVDVNDRAQMLKIIKSC 154
|
|
| TCP1_theta |
cd03341 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ... |
6-130 |
3.87e-08 |
|
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: 55.69 E-value: 3.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 6 KFSEEARRAMLRGVD---TLANAVKVTLGPKGRN--VV--LEKKFgsplITNDGVTIAKEIEledaFENMGAKLVAEVAS 78
Cdd:cd03341 1 RHYSGLEEAVLRNIEackELSQITRTSYGPNGMNkmVInhLEKLF----VTSDAATILRELE----VQHPAAKLLVMASQ 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 502820051 79 KTNDVAGDGTTTATVLAQAMIREGLKNVTAGANPMGIRKGMEKAVAVAVEEL 130
Cdd:cd03341 73 MQEEEIGDGTNLVVVLAGELLEKAEELLRMGLHPSEIIEGYEKALKKALEIL 124
|
|
| chap_CCT_gamma |
TIGR02344 |
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ... |
9-151 |
7.79e-08 |
|
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: 55.13 E-value: 7.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 9 EEARRAMLRGVD---TLANAVKVTLGPKGRNVVLEKKFGSPLITNDGVTIAKEIELedafENMGAKLVAEVASKTNDVAG 85
Cdd:TIGR02344 12 ESGRKAQLSNIQaakAVADIIRTCLGPRSMLKMLLDPMGGIVMTNDGNAILREIDV----AHPAAKSMIELSRTQDEEVG 87
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502820051 86 DGTTTATVLAQAMIREGLKNVTAGANPMGIRKGMEKAVAVAVEELKAISKPIQGKDSIAQVAAISA 151
Cdd:TIGR02344 88 DGTTSVIILAGEMLSVAEPFLEQNIHPTVIIRAYRKALDDALSVLEEISIPVDVNDDAAMLKLIQS 153
|
|
| chap_CCT_theta |
TIGR02346 |
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ... |
22-532 |
1.03e-07 |
|
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: 54.72 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 22 LANAVKVTLGPKGRNVV----LEKKFgsplITNDGVTIAKEIELedafENMGAKLVAEVASKTNDVAGDGTTTATVLAQA 97
Cdd:TIGR02346 30 LSQITRTSLGPNGMNKMvinhLEKLF----VTNDAATILRELEV----QHPAAKLLVMASEMQENEIGDGTNLVLVLAGE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 98 MIREGLKNVTAGANPMGIRKGMEKAVAVAVEELKAIS----KPIQGKDSIAQVAAISAADEEVG------QLIAEAM--- 164
Cdd:TIGR02346 102 LLNKAEELIRMGLHPSEIIKGYEMALKKAMEILEELVvwevKDLRDKDELIKALKASISSKQYGnedflaQLVAQACstv 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 165 --ERVGNDGVITLEESK---GFTTELEVVEGMQFDRGyASPYMVTDSDKMEAVLDDPY-ILITDKKigniqeilpvleqv 238
Cdd:TIGR02346 182 lpKNPQNFNVDNIRVCKilgGSLSNSEVLKGMVFNRE-AEGSVKSVKNAKVAVFSCPLdTATTETK-------------- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 239 vqqGKPLLIIAEDVEG-----EALATLVVNKLRGTFTAVAVKAPGFGDRRKAMLQDVAILTggeviteelgldLKTASID 313
Cdd:TIGR02346 247 ---GTVLIHNAEELLNyskgeENQIEAMIKAIADSGVNVIVTGGSVGDMALHYLNKYNIMV------------LKIPSKF 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 314 QLGRASKIVvtKENTTVVNGAGNAEDI----LARVNQIKAQleeTTSEFDREKLQERlaklaggVAVIKVGAATETELKE 389
Cdd:TIGR02346 312 ELRRLCKTV--GATPLPRLGAPTPEEIgyvdSVYVSEIGGD---KVTVFKQENGDSK-------ISTIILRGSTDNLLDD 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 390 RKLRIEDALNSTRAAVEEG-IVAGGGTALVNIYNKVASIeadGDTATG-----INIVLRAIEEPVRQIAHNAGLEGSVIV 463
Cdd:TIGR02346 380 IERAIDDGVNTVKALVKDGrLLPGAGATEIELASRLTKY---GEKLPGldqyaIKKFAEAFEIIPRTLAENAGLNANEVI 456
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502820051 464 ERL------KGEAVGTGFNAATGEWVNMLDTGIVDPTKVTRSALQNASSVAAMFLTTEAVVADKPEenAAPAMPD 532
Cdd:TIGR02346 457 PKLyaahkkGNKSKGIDIEAESDGVKDASEAGIYDMLATKKWAIKLATEAAVTVLRVDQIIMAKPA--GGPKPPQ 529
|
|
| TCP1_zeta |
cd03342 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
21-221 |
1.41e-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: 50.72 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 21 TLANAVKVTLGPKGRNVVLEKKFGSPLITNDGVTIAKEIEledaFENMGAKLVAEVASKTNDVAGDGTTTATVLAQAMIR 100
Cdd:cd03342 23 GLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLSEMQ----IQHPTASMIARAATAQDDITGDGTTSNVLLIGELLK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 101 EGLKNVTAGANPMGIRKGMEKAVAVAVEELKAISKPIQ---GKDSIAQVAAISaADEEVGQLIAEAMERVGNDGVITLEE 177
Cdd:cd03342 99 QAERYIQEGVHPRIITEGFELAKNKALKFLESFKVPVEidtDRELLLSVARTS-LRTKLHADLADQLTEIVVDAVLAIYK 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 502820051 178 SKGFtTELEVVEGMQFDRGYASPY-----MVTD----SDKMEAVLDDPYILIT 221
Cdd:cd03342 178 PDEP-IDLHMVEIMQMQHKSDSDTklirgLVLDhgarHPDMPKRVENAYILTC 229
|
|
| chap_CCT_zeta |
TIGR02347 |
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ... |
22-220 |
5.04e-06 |
|
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: 49.35 E-value: 5.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 22 LANAVKVTLGPKGRNVVLEKKFGSPLITNDGVTIAKEIELEdafeNMGAKLVAEVASKTNDVAGDGTTTATVLAQAMIRE 101
Cdd:TIGR02347 28 LQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEMQIQ----HPTASMIARAATAQDDITGDGTTSTVLLIGELLKQ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820051 102 GLKNVTAGANPMGIRKGMEKAVAVA---VEELKAISKPIQGKDSIAQVAAISAAD-------EEVGQLIAEAMERVGNDG 171
Cdd:TIGR02347 104 AERYILEGVHPRIITEGFEIARKEAlqfLDKFKVKKEDEVDREFLLNVARTSLRTklpadlaDQLTEIVVDAVLAIKKDG 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 502820051 172 -------VITLEESKGFTTELEVVEGMQFDRGYASPYMVTDsdkmeavLDDPYILI 220
Cdd:TIGR02347 184 edidlfmVEIMEMKHKSATDTTLIRGLVLDHGARHPDMPRR-------VKNAYILT 232
|
|
| |
