|
Name |
Accession |
Description |
Interval |
E-value |
| GroEL |
cd03344 |
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ... |
28-548 |
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: 840.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 28 KDVRFGPEVRAMMLQGVDVLADAVAVTMGPKGRNVIIEQSWGSPKITKDGVTVAKSIALKDKFQNIGAKLVQDVANNTNE 107
Cdd:cd03344 1 KDIKFGEEARKALLRGVNKLADAVKVTLGPKGRNVVIEKSFGSPKITKDGVTVAKEIELEDPFENMGAQLVKEVASKTND 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 108 EAGDGTTTATVLARAIAKEGFEKISRGASPVEIRRGVMLAIETVKDNLRRLSRPVNTPEEICQVATISANGDKSVGNLIS 187
Cdd:cd03344 81 VAGDGTTTATVLARAIIKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKPVKTKEEIAQVATISANGDEEIGELIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 188 EAIKKVGRDGVITVKDGKTLCDELEVIEGMKFDRGYISPYFINTSKGAKVEFQDALLLFCEKKIKSAPSIVPALELANAQ 267
Cdd:cd03344 161 EAMEKVGKDGVITVEEGKTLETELEVVEGMQFDRGYLSPYFVTDPEKMEVELENPYILLTDKKISSIQELLPILELVAKA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 268 RKPLVIIAEDLEAEALSTLVVNRLKVGLQVCAVKAPGFGDNRKENLMDMAVATGGIVFGDEANMvRLEDIKMSDFGRVGE 347
Cdd:cd03344 241 GRPLLIIAEDVEGEALATLVVNKLRGGLKVCAVKAPGFGDRRKAMLEDIAILTGGTVISEELGL-KLEDVTLEDLGRAKK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 348 VVVSKDDTMLLKGKGQKAEVEKRVEGLREAIKESTSSYEKEKMQERLARLSSGVALLRVGGSSDVEVSEKKDRVIDALNA 427
Cdd:cd03344 320 VVVTKDDTTIIGGAGDKAAIKARIAQIRKQIEETTSDYDKEKLQERLAKLSGGVAVIKVGGATEVELKEKKDRVEDALNA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 428 TRAAVEEGIVPGGGTALLRCIQKLNDLKGANEDQNMGIEIIRRALRMPCLTIAKNAGVDGAMVVAKVEILDGDYGYDALK 507
Cdd:cd03344 400 TRAAVEEGIVPGGGVALLRASPALDKLKALNGDEKLGIEIVRRALEAPLRQIAENAGVDGSVVVEKVLESPDGFGYDAAT 479
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 45550132 508 GEYGNMIERGIIDPTKVVRTAISDAAGVASLLTTAEAVVTE 548
Cdd:cd03344 480 GEYVDMIEAGIIDPTKVVRSALQNAASVASLLLTTEALVVD 520
|
|
| PTZ00114 |
PTZ00114 |
Heat shock protein 60; Provisional |
23-553 |
0e+00 |
|
Heat shock protein 60; Provisional
Pssm-ID: 185455 Cd Length: 555 Bit Score: 758.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 23 ARNYAKDVRFGPEVRAMMLQGVDVLADAVAVTMGPKGRNVIIEQSWGSPKITKDGVTVAKSIALKDKFQNIGAKLVQDVA 102
Cdd:PTZ00114 10 YRFKGKEIRFGDEARQSLLKGIERLADAVAVTLGPKGRNVIIEQEYGSPKITKDGVTVAKAIEFSDRFENVGAQLIRQVA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 103 NNTNEEAGDGTTTATVLARAIAKEGFEKISRGASPVEIRRGVMLAIETVKDNLRRLSRPVNTPEEICQVATISANGDKSV 182
Cdd:PTZ00114 90 SKTNDKAGDGTTTATILARAIFREGCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQSRPVKTKEDILNVATISANGDVEI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 183 GNLISEAIKKVGRDGVITVKDGKTLCDELEVIEGMKFDRGYISPYFINTSKGAKVEFQDALLLFCEKKIKSAPSIVPALE 262
Cdd:PTZ00114 170 GSLIADAMDKVGKDGTITVEDGKTLEDELEVVEGMSFDRGYISPYFVTNEKTQKVELENPLILVTDKKISSIQSILPILE 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 263 LANAQRKPLVIIAEDLEAEALSTLVVNRLKVGLQVCAVKAPGFGDNRKENLMDMAVATGGIVFGDEANMVRLEDIKMSDF 342
Cdd:PTZ00114 250 HAVKNKRPLLIIAEDVEGEALQTLIINKLRGGLKVCAVKAPGFGDNRKDILQDIAVLTGATVVSEDNVGLKLDDFDPSML 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 343 GRVGEVVVSKDDTMLLKGKGQKAEVEKRVEGLREAIKESTSSYEKEKMQERLARLSSGVALLRVGGSSDVEVSEKKDRVI 422
Cdd:PTZ00114 330 GSAKKVTVTKDETVILTGGGDKAEIKERVELLRSQIERTTSEYDKEKLKERLAKLSGGVAVIKVGGASEVEVNEKKDRIE 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 423 DALNATRAAVEEGIVPGGGTALLRCIQKLNDLKGANE---DQNMGIEIIRRALRMPCLTIAKNAGVDGAMVVAKV-EILD 498
Cdd:PTZ00114 410 DALNATRAAVEEGIVPGGGVALLRASKLLDKLEEDNEltpDQRTGVKIVRNALRLPTKQIAENAGVEGAVVVEKIlEKKD 489
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 45550132 499 GDYGYDALKGEYGNMIERGIIDPTKVVRTAISDAAGVASLLTTAEAVVTELPLEE 553
Cdd:PTZ00114 490 PSFGYDAQTGEYVNMFEAGIIDPTKVVRSALVDAASVASLMLTTEAAIVDLPKEK 544
|
|
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
27-553 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 719.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 27 AKDVRFGPEVRAMMLQGVDVLADAVAVTMGPKGRNVIIEQSWGSPKITKDGVTVAKSIALKDKFQNIGAKLVQDVANNTN 106
Cdd:PRK00013 2 AKDIKFGEDARRKLLRGVNKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDPFENMGAQLVKEVASKTN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 107 EEAGDGTTTATVLARAIAKEGFEKISRGASPVEIRRGVMLAIETVKDNLRRLSRPVNTPEEICQVATISANGDKSVGNLI 186
Cdd:PRK00013 82 DVAGDGTTTATVLAQAIVREGLKNVAAGANPMDLKRGIDKAVEAAVEELKKISKPVEDKEEIAQVATISANGDEEIGKLI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 187 SEAIKKVGRDGVITVKDGKTLCDELEVIEGMKFDRGYISPYFINTSKGAKVEFQDALLLFCEKKIKSAPSIVPALELANA 266
Cdd:PRK00013 162 AEAMEKVGKEGVITVEESKGFETELEVVEGMQFDRGYLSPYFVTDPEKMEAELENPYILITDKKISNIQDLLPVLEQVAQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 267 QRKPLVIIAEDLEAEALSTLVVNRLKVGLQVCAVKAPGFGDNRKENLMDMAVATGGIVFGDEANMvRLEDIKMSDFGRVG 346
Cdd:PRK00013 242 SGKPLLIIAEDVEGEALATLVVNKLRGTLKVVAVKAPGFGDRRKAMLEDIAILTGGTVISEELGL-KLEDATLEDLGQAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 347 EVVVSKDDTMLLKGKGQKAEVEKRVEGLREAIKESTSSYEKEKMQERLARLSSGVALLRVGGSSDVEVSEKKDRVIDALN 426
Cdd:PRK00013 321 KVVVTKDNTTIVDGAGDKEAIKARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATEVEMKEKKDRVEDALH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 427 ATRAAVEEGIVPGGGTALLRCIQKLNDLKGANEDQNMGIEIIRRALRMPCLTIAKNAGVDGAMVVAKV-EILDGDYGYDA 505
Cdd:PRK00013 401 ATRAAVEEGIVPGGGVALLRAAPALEALKGLNGDEATGINIVLRALEAPLRQIAENAGLEGSVVVEKVkNGKGKGYGYNA 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 45550132 506 LKGEYGNMIERGIIDPTKVVRTAISDAAGVASLLTTAEAVVTELPLEE 553
Cdd:PRK00013 481 ATGEYVDMIEAGIIDPTKVTRSALQNAASVAGLLLTTEAVVADKPEKK 528
|
|
| groEL |
PRK12849 |
chaperonin GroEL; Reviewed |
27-553 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237230 Cd Length: 542 Bit Score: 697.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 27 AKDVRFGPEVRAMMLQGVDVLADAVAVTMGPKGRNVIIEQSWGSPKITKDGVTVAKSIALKDKFQNIGAKLVQDVANNTN 106
Cdd:PRK12849 2 AKIIKFDEEARRALERGVNKLADAVKVTLGPKGRNVVIDKSFGAPTITKDGVSIAKEIELEDPFENLGAQLVKEVASKTN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 107 EEAGDGTTTATVLARAIAKEGFEKISRGASPVEIRRGVMLAIETVKDNLRRLSRPVNTPEEICQVATISANGDKSVGNLI 186
Cdd:PRK12849 82 DVAGDGTTTATVLAQALVQEGLKNVAAGANPMDLKRGIDKAVEAVVEELKALARPVSGSEEIAQVATISANGDEEIGELI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 187 SEAIKKVGRDGVITVKDGKTLCDELEVIEGMKFDRGYISPYFINTSKGAKVEFQDALLLFCEKKIKSAPSIVPALELANA 266
Cdd:PRK12849 162 AEAMEKVGKDGVITVEESKTLETELEVTEGMQFDRGYLSPYFVTDPERMEAVLEDPLILLTDKKISSLQDLLPLLEKVAQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 267 QRKPLVIIAEDLEAEALSTLVVNRLKVGLQVCAVKAPGFGDNRKENLMDMAVATGGIVFGDEANMvRLEDIKMSDFGRVG 346
Cdd:PRK12849 242 SGKPLLIIAEDVEGEALATLVVNKLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGL-KLEEVTLDDLGRAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 347 EVVVSKDDTMLLKGKGQKAEVEKRVEGLREAIKESTSSYEKEKMQERLARLSSGVALLRVGGSSDVEVSEKKDRVIDALN 426
Cdd:PRK12849 321 RVTITKDNTTIVDGAGDKEAIEARVAQIRRQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATEVELKERKDRVEDALN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 427 ATRAAVEEGIVPGGGTALLRCIQKLNDLKGANEDQNMGIEIIRRALRMPCLTIAKNAGVDGAMVVAKVEILDGDYGYDAL 506
Cdd:PRK12849 401 ATRAAVEEGIVPGGGVALLRAAKALDELAGLNGDQAAGVEIVRRALEAPLRQIAENAGLDGSVVVAKVLELEDGFGFNAA 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 45550132 507 KGEYGNMIERGIIDPTKVVRTAISDAAGVASLLTTAEAVVTELPLEE 553
Cdd:PRK12849 481 TGEYGDLIAAGIIDPVKVTRSALQNAASVAGLLLTTEALVADKPEEE 527
|
|
| GroEL |
TIGR02348 |
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ... |
27-550 |
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: 677.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 27 AKDVRFGPEVRAMMLQGVDVLADAVAVTMGPKGRNVIIEQSWGSPKITKDGVTVAKSIALKDKFQNIGAKLVQDVANNTN 106
Cdd:TIGR02348 1 AKQIKFDEEARKALLRGVDKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDKFENMGAQLVKEVASKTN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 107 EEAGDGTTTATVLARAIAKEGFEKISRGASPVEIRRGVMLAIETVKDNLRRLSRPVNTPEEICQVATISANGDKSVGNLI 186
Cdd:TIGR02348 81 DVAGDGTTTATVLAQAIVKEGLKNVAAGANPIELKRGIEKAVEAVVEELKKLSKPVKGKKEIAQVATISANNDEEIGSLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 187 SEAIKKVGRDGVITVKDGKTLCDELEVIEGMKFDRGYISPYFINTSKGAKVEFQDALLLFCEKKIKSAPSIVPALELANA 266
Cdd:TIGR02348 161 AEAMEKVGKDGVITVEESKSLETELEVVEGMQFDRGYISPYFVTDAEKMEVELENPYILITDKKISNIKDLLPLLEKVAQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 267 QRKPLVIIAEDLEAEALSTLVVNRLKVGLQVCAVKAPGFGDNRKENLMDMAVATGGIVFGDEANMvRLEDIKMSDFGRVG 346
Cdd:TIGR02348 241 SGKPLLIIAEDVEGEALATLVVNKLRGTLNVCAVKAPGFGDRRKAMLEDIAILTGGQVISEELGL-KLEEVTLDDLGKAK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 347 EVVVSKDDTMLLKGKGQKAEVEKRVEGLREAIKESTSSYEKEKMQERLARLSSGVALLRVGGSSDVEVSEKKDRVIDALN 426
Cdd:TIGR02348 320 KVTVDKDNTTIVEGAGDKAAIKARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATETEMKEKKLRIEDALN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 427 ATRAAVEEGIVPGGGTALLRCIQKLNDLKGANEDQNMGIEIIRRALRMPCLTIAKNAGVDGAMVVAKVEILDGDYGYDAL 506
Cdd:TIGR02348 400 ATRAAVEEGIVPGGGVALLRAAAALEGLKGDGEDEAIGIDIVKRALEAPLRQIAENAGLDGAVVAEKVKELKGNFGFNAA 479
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 45550132 507 KGEYGNMIERGIIDPTKVVRTAISDAAGVASLLTTAEAVVTELP 550
Cdd:TIGR02348 480 TGEYEDLVEAGIIDPTKVTRSALQNAASIAGLLLTTEAVVADKP 523
|
|
| groEL |
PRK12850 |
chaperonin GroEL; Reviewed |
27-553 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237231 Cd Length: 544 Bit Score: 652.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 27 AKDVRFGPEVRAMMLQGVDVLADAVAVTMGPKGRNVIIEQSWGSPKITKDGVTVAKSIALKDKFQNIGAKLVQDVANNTN 106
Cdd:PRK12850 3 AKEIRFSTDARDRLLRGVNILANAVKVTLGPKGRNVVLEKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVKEVASKTN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 107 EEAGDGTTTATVLARAIAKEGFEKISRGASPVEIRRGVMLAIETVKDNLRRLSRPVNTPEEICQVATISANGDKSVGNLI 186
Cdd:PRK12850 83 DLAGDGTTTATVLAQAIVREGAKLVAAGMNPMDLKRGIDLAVAAVVDELKKIAKKVTSSKEIAQVATISANGDESIGEMI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 187 SEAIKKVGRDGVITVKDGKTLCDELEVIEGMKFDRGYISPYFINTSKGAKVEFQDALLLFCEKKIKSAPSIVPALELANA 266
Cdd:PRK12850 163 AEAMDKVGKEGVITVEEAKTLGTELDVVEGMQFDRGYLSPYFVTNPEKMRAELEDPYILLHEKKISNLQDLLPILEAVVQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 267 QRKPLVIIAEDLEAEALSTLVVNRLKVGLQVCAVKAPGFGDNRKENLMDMAVATGGIVFGDEANmVRLEDIKMSDFGRVG 346
Cdd:PRK12850 243 SGRPLLIIAEDVEGEALATLVVNKLRGGLKSVAVKAPGFGDRRKAMLEDIAVLTGGQVISEDLG-IKLENVTLDMLGRAK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 347 EVVVSKDDTMLLKGKGQKAEVEKRVEGLREAIKESTSSYEKEKMQERLARLSSGVALLRVGGSSDVEVSEKKDRVIDALN 426
Cdd:PRK12850 322 RVLITKENTTIIDGAGDKKNIEARVKQIRAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKEKKDRVDDALH 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 427 ATRAAVEEGIVPGGGTALLRCIQKLNDLKGANEDQNMGIEIIRRALRMPCLTIAKNAGVDGAMVVAKVEILDGDYGYDAL 506
Cdd:PRK12850 402 ATRAAVEEGIVPGGGVALLRARSALRGLKGANADETAGIDIVRRALEEPLRQIATNAGFEGSVVVGKVAELPGNFGFNAQ 481
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 45550132 507 KGEYGNMIERGIIDPTKVVRTAISDAAGVASLLTTAEAVVTELPLEE 553
Cdd:PRK12850 482 TGEYGDMVEAGIIDPAKVTRTALQDAASIAALLITTEAMVAEAPKKA 528
|
|
| groEL |
PRK12852 |
chaperonin GroEL; Reviewed |
27-553 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237232 Cd Length: 545 Bit Score: 625.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 27 AKDVRFGPEVRAMMLQGVDVLADAVAVTMGPKGRNVIIEQSWGSPKITKDGVTVAKSIALKDKFQNIGAKLVQDVANNTN 106
Cdd:PRK12852 3 AKDVKFSGDARDRMLRGVDILANAVKVTLGPKGRNVVIEKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVREVASKTN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 107 EEAGDGTTTATVLARAIAKEGFEKISRGASPVEIRRGVMLAIETVKDNLRRLSRPVNTPEEICQVATISANGDKSVGNLI 186
Cdd:PRK12852 83 DLAGDGTTTATVLAQAIVREGAKAVAAGMNPMDLKRGIDIAVAAVVKDIEKRAKPVASSAEIAQVGTISANGDAAIGKMI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 187 SEAIKKVGRDGVITVKDGKTLCDELEVIEGMKFDRGYISPYFINTSKGAKVEFQDALLLFCEKKIKSAPSIVPALELANA 266
Cdd:PRK12852 163 AQAMQKVGNEGVITVEENKSLETEVDIVEGMKFDRGYLSPYFVTNAEKMTVELDDAYILLHEKKLSGLQAMLPVLEAVVQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 267 QRKPLVIIAEDLEAEALSTLVVNRLKVGLQVCAVKAPGFGDNRKENLMDMAVATGGIVFGDEANMvRLEDIKMSDFGRVG 346
Cdd:PRK12852 243 SGKPLLIIAEDVEGEALATLVVNRLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGQLISEDLGI-KLENVTLKMLGRAK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 347 EVVVSKDDTMLLKGKGQKAEVEKRVEGLREAIKESTSSYEKEKMQERLARLSSGVALLRVGGSSDVEVSEKKDRVIDALN 426
Cdd:PRK12852 322 KVVIDKENTTIVNGAGKKADIEARVGQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKEKKDRVEDALN 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 427 ATRAAVEEGIVPGGGTALLRCIQKLNDLKGANEDQNMGIEIIRRALRMPCLTIAKNAGVDGAMVVAKV-EILDGDYGYDA 505
Cdd:PRK12852 402 ATRAAVQEGIVPGGGVALLRAKKAVGRINNDNADVQAGINIVLKALEAPIRQIAENAGVEGSIVVGKIlENKSETFGFDA 481
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 45550132 506 LKGEYGNMIERGIIDPTKVVRTAISDAAGVASLLTTAEAVVTELPLEE 553
Cdd:PRK12852 482 QTEEYVDMVAKGIIDPAKVVRTALQDAASVAGLLVTTEAMVAELPKKD 529
|
|
| groEL |
PRK12851 |
chaperonin GroEL; Reviewed |
27-553 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 171770 Cd Length: 541 Bit Score: 619.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 27 AKDVRFGPEVRAMMLQGVDVLADAVAVTMGPKGRNVIIEQSWGSPKITKDGVTVAKSIALKDKFQNIGAKLVQDVANNTN 106
Cdd:PRK12851 3 AKEVKFHVEAREKMLRGVNILADAVKVTLGPKGRNVVIDKSFGAPTITNDGVTIAKEIELEDKFENMGAQMVREVASKTN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 107 EEAGDGTTTATVLARAIAKEGFEKISRGASPVEIRRGVMLAIETVKDNLRRLSRPVNTPEEICQVATISANGDKSVGNLI 186
Cdd:PRK12851 83 DVAGDGTTTATVLAQAIVREGAKAVAAGANPMDLKRGIDRAVAAVVEELKANARPVTTNAEIAQVATISANGDAEIGRLV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 187 SEAIKKVGRDGVITVKDGKTLCDELEVIEGMKFDRGYISPYFINTSKGAKVEFQDALLLFCEKKIKSAPSIVPALELANA 266
Cdd:PRK12851 163 AEAMEKVGNEGVITVEESKTAETELEVVEGMQFDRGYLSPYFVTDADKMEAELEDPYILIHEKKISNLQDLLPVLEAVVQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 267 QRKPLVIIAEDLEAEALSTLVVNRLKVGLQVCAVKAPGFGDNRKENLMDMAVATGGIVFGDEANMvRLEDIKMSDFGRVG 346
Cdd:PRK12851 243 SGKPLLIIAEDVEGEALATLVVNKLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGI-KLENVTLEQLGRAK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 347 EVVVSKDDTMLLKGKGQKAEVEKRVEGLREAIKESTSSYEKEKMQERLARLSSGVALLRVGGSSDVEVSEKKDRVIDALN 426
Cdd:PRK12851 322 KVVVEKENTTIIDGAGSKTEIEGRVAQIRAQIEETTSDYDREKLQERLAKLAGGVAVIRVGASTEVEVKEKKDRVDDALH 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 427 ATRAAVEEGIVPGGGTALLRCIQKLNDLKGANEDQNMGIEIIRRALRMPCLTIAKNAGVDGAMVVAKVEILDGDYGYDAL 506
Cdd:PRK12851 402 ATRAAVEEGIVPGGGVALLRAVKALDKLETANGDQRTGVEIVRRALEAPVRQIAENAGAEGSVVVGKLREKPGGYGFNAA 481
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 45550132 507 KGEYGNMIERGIIDPTKVVRTAISDAAGVASLLTTAEAVVTELPLEE 553
Cdd:PRK12851 482 TNEYGDLYAQGVIDPVKVVRTALQNAASVAGLLLTTEAMVAEKPKKE 528
|
|
| GroEL |
COG0459 |
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ... |
27-553 |
0e+00 |
|
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227 Cd Length: 497 Bit Score: 603.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 27 AKDVRFGPEVRAMMLQGVDVLADAVAVTMGPKGRNVIIEQSWGSPKITKDGVTVAKSIALKDKFQNIGAKLVQDVANNTN 106
Cdd:COG0459 2 AKQILFGEDARRANIRGVKALADAVKVTLGPKGRNVMLVKSFGDPTITNDGVTIAKEIELEDPFENMGAQLVKEVASKTN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 107 EEAGDGTTTATVLARAIAKEGFEKISRGASPVEIRRGVMLAIETVKDNLRRLSRPVNTPEEICQVATISANGDKSVGNLI 186
Cdd:COG0459 82 DEAGDGTTTATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPVDDKEELAQVATISANGDEEIGELI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 187 SEAIKKVGRDGVITVKDGKTLCDELEVIEGMKFDRGYISPYFINTSKGAKVEFQDALLLFCEKKIKSAPSIVPALELANA 266
Cdd:COG0459 162 AEAMEKVGKDGVITVEEGKGLETELEVVEGMQFDKGYLSPYFVTDPEKMPAELENAYILLTDKKISSIQDLLPLLEKVAQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 267 QRKPLVIIAEDLEAEALSTLVVNRLKVGLQVCAVKAPGFGDNRKENLMDMAVATGGIVFGDEANMvRLEDIKMSDFGRVG 346
Cdd:COG0459 242 SGKPLLIIAEDIDGEALATLVVNGIRGVLRVVAVKAPGFGDRRKAMLEDIAILTGGRVISEDLGL-KLEDVTLDDLGRAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 347 EVVVSKDDTMLLKGKGQKAEVekrveglreaikestssyekekmqerlarlssgvaLLRVGGSSDVEVSEKKDRVIDALN 426
Cdd:COG0459 321 RVEVDKDNTTIVEGAGNPKAI-----------------------------------VILVGAATEVEVKERKRRVEDALH 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 427 ATRAAVEEGIVPGGGTALLRCIQKLNDL-KGANEDQNMGIEIIRRALRMPCLTIAKNAGVDGAMVVAKVEIL-DGDYGYD 504
Cdd:COG0459 366 ATRAAVEEGIVPGGGAALLRAARALRELaAKLEGDEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKVRAAkDKGFGFD 445
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 45550132 505 ALKGEYGNMIERGIIDPTKVVRTAISDAAGVASLLTTAEAVVTELPLEE 553
Cdd:COG0459 446 AATGEYVDMLEAGVIDPAKVKRSALQNAASVAGLILTTEAVIADKPEKE 494
|
|
| PRK14104 |
PRK14104 |
chaperonin GroEL; Provisional |
27-550 |
0e+00 |
|
chaperonin GroEL; Provisional
Pssm-ID: 172594 Cd Length: 546 Bit Score: 571.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 27 AKDVRFGPEVRAMMLQGVDVLADAVAVTMGPKGRNVIIEQSWGSPKITKDGVTVAKSIALKDKFQNIGAKLVQDVANNTN 106
Cdd:PRK14104 3 AKEVKFGVDARDRMLRGVDILANAVKVTLGPKGRNVVLDKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVREVASKSA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 107 EEAGDGTTTATVLARAIAKEGFEKISRGASPVEIRRGVMLAIETVKDNLRRLSRPVNTPEEICQVATISANGDKSVGNLI 186
Cdd:PRK14104 83 DAAGDGTTTATVLAQAIVREGAKSVAAGMNPMDLKRGIDLAVEAVVADLVKNSKKVTSNDEIAQVGTISANGDAEIGKFL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 187 SEAIKKVGRDGVITVKDGKTLCDELEVIEGMKFDRGYISPYFINTSKGAKVEFQDALLLFCEKKIKSAPSIVPALELANA 266
Cdd:PRK14104 163 ADAMKKVGNEGVITVEEAKSLETELDVVEGMQFDRGYISPYFVTNADKMRVEMDDAYILINEKKLSSLNELLPLLEAVVQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 267 QRKPLVIIAEDLEAEALSTLVVNRLKVGLQVCAVKAPGFGDNRKENLMDMAVATGGIVFGDEANmVRLEDIKMSDFGRVG 346
Cdd:PRK14104 243 TGKPLVIVAEDVEGEALATLVVNRLRGGLKVAAVKAPGFGDRRKAMLQDIAILTGGQAISEDLG-IKLENVTLQMLGRAK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 347 EVVVSKDDTMLLKGKGQKAEVEKRVEGLREAIKESTSSYEKEKMQERLARLSSGVALLRVGGSSDVEVSEKKDRVIDALN 426
Cdd:PRK14104 322 KVMIDKENTTIVNGAGKKADIEARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKERKDRVDDAMH 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 427 ATRAAVEEGIVPGGGTALLRCIQKLNDLKGANEDQNMGIEIIRRALRMPCLTIAKNAGVDGAMVVAKveILDGD---YGY 503
Cdd:PRK14104 402 ATRAAVEEGIVPGGGVALLRASEQLKGIKTKNDDQKTGVEIVRKALSAPARQIAINAGEDGSVIVGK--ILEKEqysYGF 479
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 45550132 504 DALKGEYGNMIERGIIDPTKVVRTAISDAAGVASLLTTAEAVVTELP 550
Cdd:PRK14104 480 DSQTGEYGNLVSKGIIDPTKVVRTAIQNAASVAALLITTEAMVAELP 526
|
|
| groEL |
CHL00093 |
chaperonin GroEL |
27-548 |
0e+00 |
|
chaperonin GroEL
Pssm-ID: 177025 Cd Length: 529 Bit Score: 531.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 27 AKDVRFGPEVRAMMLQGVDVLADAVAVTMGPKGRNVIIEQSWGSPKITKDGVTVAKSIALKDKFQNIGAKLVQDVANNTN 106
Cdd:CHL00093 2 SKKILYQDNARRALERGMDILAEAVSVTLGPKGRNVVLEKKYGSPQIVNDGVTIAKEIELEDHIENTGVALIRQAASKTN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 107 EEAGDGTTTATVLARAIAKEGFEKISRGASPVEIRRGVMLAIETVKDNLRRLSRPVNTPEEICQVATISANGDKSVGNLI 186
Cdd:CHL00093 82 DVAGDGTTTATVLAYAIVKQGMKNVAAGANPISLKRGIEKATQYVVSQIAEYARPVEDIQAITQVASISAGNDEEVGSMI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 187 SEAIKKVGRDGVITVKDGKTLCDELEVIEGMKFDRGYISPYFINTSKGAKVEFQDALLLFCEKKIKSAPS-IVPALELAN 265
Cdd:CHL00093 162 ADAIEKVGREGVISLEEGKSTVTELEITEGMRFEKGFISPYFVTDTERMEVVQENPYILLTDKKITLVQQdLLPILEQVT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 266 AQRKPLVIIAEDLEAEALSTLVVNRLKVGLQVCAVKAPGFGDNRKENLMDMAVATGGIVFGDEANMvRLEDIKMSDFGRV 345
Cdd:CHL00093 242 KTKRPLLIIAEDVEKEALATLVLNKLRGIVNVVAVRAPGFGDRRKAMLEDIAILTGGQVITEDAGL-SLETIQLDLLGQA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 346 GEVVVSKDDTMLLkGKGQKAEVEKRVEGLREAIKESTSSYEKEKMQERLARLSSGVALLRVGGSSDVEVSEKKDRVIDAL 425
Cdd:CHL00093 321 RRIIVTKDSTTII-ADGNEEQVKARCEQLRKQIEIADSSYEKEKLQERLAKLSGGVAVIKVGAATETEMKDKKLRLEDAI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 426 NATRAAVEEGIVPGGGTALLRCIQKLNDLKGAN--EDQNMGIEIIRRALRMPCLTIAKNAGVDGAMVVAKVEILDGDYGY 503
Cdd:CHL00093 400 NATKAAVEEGIVPGGGATLVHLSENLKTWAKNNlkEDELIGALIVARAILAPLKRIAENAGKNGSVIIEKVQEQDFEIGY 479
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 45550132 504 DALKGEYGNMIERGIIDPTKVVRTAISDAAGVASLLTTAEAVVTE 548
Cdd:CHL00093 480 NAANNKFVNMYEAGIIDPAKVTRSALQNAASIASMILTTECIIVD 524
|
|
| PLN03167 |
PLN03167 |
Chaperonin-60 beta subunit; Provisional |
24-553 |
8.70e-157 |
|
Chaperonin-60 beta subunit; Provisional
Pssm-ID: 215611 [Multi-domain] Cd Length: 600 Bit Score: 461.70 E-value: 8.70e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 24 RNYAKDVRFGPEVRAM--MLQGVDVLADAVAVTMGPKGRNVIIEQSWGSPKITKDGVTVAKSIALKDKFQNIGAKLVQDV 101
Cdd:PLN03167 53 VKAAKELHFNKDGSAIkkLQAGVNKLADLVGVTLGPKGRNVVLESKYGSPKIVNDGVTVAKEVELEDPVENIGAKLVRQA 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 102 ANNTNEEAGDGTTTATVLARAIAKEGFEKISRGASPVEIRRGVMLAIETVKDNLRRLSRPVNTpEEICQVATISANGDKS 181
Cdd:PLN03167 133 AAKTNDLAGDGTTTSVVLAQGLIAEGVKVVAAGANPVQITRGIEKTAKALVKELKKMSKEVED-SELADVAAVSAGNNYE 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 182 VGNLISEAIKKVGRDGVITVKDGKTLCDELEVIEGMKFDRGYISPYFINTSKGAKVEFQDALLLFCEKKIKSAPSIVPAL 261
Cdd:PLN03167 212 VGNMIAEAMSKVGRKGVVTLEEGKSAENNLYVVEGMQFDRGYISPYFVTDSEKMSVEYDNCKLLLVDKKITNARDLIGIL 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 262 ELANAQRKPLVIIAEDLEAEALSTLVVNRLKVGLQVCAVKAPGFGDNRKENLMDMAVATGGIVFGDEANMvRLEDIKMSD 341
Cdd:PLN03167 292 EDAIRGGYPLLIIAEDIEQEALATLVVNKLRGSLKIAALKAPGFGERKSQYLDDIAILTGGTVIREEVGL-SLDKVGKEV 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 342 FGRVGEVVVSKDDTMLLKGKGQKAEVEKRVEGLREAIKESTSSYEKEKMQERLARLSSGVALLRVGGSSDVEVSEKKDRV 421
Cdd:PLN03167 371 LGTAAKVVLTKDTTTIVGDGSTQEAVNKRVAQIKNLIEAAEQDYEKEKLNERIAKLSGGVAVIQVGAQTETELKEKKLRV 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 422 IDALNATRAAVEEGIVPGGGTALLRCIQKLNDLKGA--NEDQNMGIEIIRRALRMPCLTIAKNAGVDGAMVVAKVEILDG 499
Cdd:PLN03167 451 EDALNATKAAVEEGIVVGGGCTLLRLASKVDAIKDTleNDEQKVGADIVKRALSYPLKLIAKNAGVNGSVVSEKVLSNDN 530
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 45550132 500 -DYGYDALKGEYGNMIERGIIDPTKVVRTAISDAAGVASLLTTAEAVVTELPLEE 553
Cdd:PLN03167 531 pKFGYNAATGKYEDLMAAGIIDPTKVVRCCLEHAASVAKTFLTSDCVVVEIKEPE 585
|
|
| chaperonin_type_I_II |
cd00309 |
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ... |
28-547 |
3.33e-141 |
|
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: 416.83 E-value: 3.33e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 28 KDVRFGPEVRAMMLQGVDVLADAVAVTMGPKGRNVIIEQSWGSPKITKDGVTVAKSIALkdkfQNIGAKLVQDVANNTNE 107
Cdd:cd00309 1 KEREFGEEARLSNINAAKALADAVKTTLGPKGMDKMLVDSLGDPTITNDGATILKEIEV----EHPAAKLLVEVAKSQDD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 108 EAGDGTTTATVLARAIAKEGFEKISRGASPVEIRRGVMLAIETVKDNLRRLSRP--VNTPEEICQVATISAN------GD 179
Cdd:cd00309 77 EVGDGTTTVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVPidVEDREELLKVATTSLNsklvsgGD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 180 KSVGNLISEAIKKVGR------DGVITVKDGKT-LCDELEVIEGMKFDRGYISPYFintskgaKVEFQDALLLFCEKKIK 252
Cdd:cd00309 157 DFLGELVVDAVLKVGKengdvdLGVIRVEKKKGgSLEDSELVVGMVFDKGYLSPYM-------PKRLENAKILLLDCKLE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 253 SapsivpalelanaqrkplVIIAEDL-EAEALSTLVVnrlkvgLQVCAVKApgfgdNRKENLMDMAVATGGIVfgdeanM 331
Cdd:cd00309 230 Y------------------VVIAEKGiDDEALHYLAK------LGIMAVRR-----VRKEDLERIAKATGATI------V 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 332 VRLEDIKMSDFGRVGEVVVSK----DDTMLLKGKGqkaevekrveglreaikestssyekekmqerlarlsSGVALLRVG 407
Cdd:cd00309 275 SRLEDLTPEDLGTAGLVEETKigdeKYTFIEGCKG------------------------------------GKVATILLR 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 408 GSSDVEVSEKKDRVIDALNATRAAVEE-GIVPGGGTALLRCIQKLNDL-KGANEDQNMGIEIIRRALRMPCLTIAKNAGV 485
Cdd:cd00309 319 GATEVELDEAERSLHDALCAVRAAVEDgGIVPGGGAAEIELSKALEELaKTLPGKEQLGIEAFADALEVIPRTLAENAGL 398
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45550132 486 DGAMVVAKVEIL----DGDYGYDALKGEYGNMIERGIIDPTKVVRTAISDAAGVASLLTTAEAVVT 547
Cdd:cd00309 399 DPIEVVTKLRAKhaegGGNAGGDVETGEIVDMKEAGIIDPLKVKRQALKSATEAASLILTIDDIIV 464
|
|
| Cpn60_TCP1 |
pfam00118 |
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ... |
47-546 |
5.11e-70 |
|
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: 233.63 E-value: 5.11e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 47 LADAVAVTMGPKGRNVIIEQSWGSPKITKDGVTVAKSIalkdKFQNIGAKLVQDVANNTNEEAGDGTTTATVLARAIAKE 126
Cdd:pfam00118 1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKEL----EIQHPAAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 127 GFEKISRGASPVEIRRGVMLAIETVKDNLRR-LSRPVNTP--EEICQVATISANGDKS------VGNLISEAIK------ 191
Cdd:pfam00118 77 AEKLLAAGVHPTTIIEGYEKALEKALEILDSiISIPVEDVdrEDLLKVARTSLSSKIIsresdfLAKLVVDAVLaipknd 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 192 ---KVGRDGVITVKDGKTlcDELEVIEGMKFDRGYISPYFINTSKGAKVefqdaLLLFCE-----KKIKSAPSIVPALEL 263
Cdd:pfam00118 157 gsfDLGNIGVVKILGGSL--EDSELVDGVVLDKGPLHPDMPKRLENAKV-----LLLNCSleyekTETKATVVLSDAEQL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 264 ANAQRKPLVIIAEDLEA--EALSTLVVNRLKVG---LQVCA-VKAPGFGDNRKENLMDMAVATGGIVfgdeanMVRLEDI 337
Cdd:pfam00118 230 ERFLKAEEEQILEIVEKiiDSGVNVVVCQKGIDdlaLHFLAkNGIMALRRVKKRDLERLAKATGARA------VSSLDDL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 338 KMSDFGRVG---EVVVSKDDTMLLKGkgqkaevekrveglreaikestssyekekmqerlaRLSSGVALLRVGGSSDVEV 414
Cdd:pfam00118 304 TPDDLGTAGkveEEKIGDEKYTFIEG-----------------------------------CKSPKAATILLRGATDHVL 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 415 SEKKDRVIDALNATRAAVEE-GIVPGGGTALLRCIQKLNDL-KGANEDQNMGIEIIRRALRMPCLTIAKNAGVDGAMVVA 492
Cdd:pfam00118 349 DEIERSIHDALCVVKNAIEDpRVVPGGGAVEMELARALREYaKSVSGKEQLAIEAFAEALEVIPKTLAENAGLDPIEVLA 428
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 45550132 493 KVEIL----DGDYGYDALKGEYGNMIERGIIDPTKVVRTAISDAAGVASLLTTAEAVV 546
Cdd:pfam00118 429 ELRAAhasgEKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKSATEAASTILRIDDII 486
|
|
| chaperonin_like |
cd03333 |
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ... |
166-434 |
6.47e-31 |
|
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: 119.49 E-value: 6.47e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 166 EEICQVATISAN-----GDKSVGNLISEAIKKVGRD------GVITVKDGKT-LCDELEVIEGMKFDRGYISPYFintsk 233
Cdd:cd03333 2 ELLLQVATTSLNsklssWDDFLGKLVVDAVLKVGPDnrmddlGVIKVEKIPGgSLEDSELVVGVVFDKGYASPYM----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 234 gaKVEFQDALLLFCEKKIKSapsivpalelanaqrkplVIIAEDL-EAEALSTLVVnrlkvgLQVCAVKApgfgdNRKEN 312
Cdd:cd03333 77 --PKRLENAKILLLDCPLEY------------------VVIAEKGiDDLALHYLAK------AGIMAVRR-----VKKED 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 313 LMDMAVATGGIVfgdeanMVRLEDIKMSDFGRVGEVVVSKD----DTMLLKGKGqkaevekrveglreaikestssyeke 388
Cdd:cd03333 126 LERIARATGATI------VSSLEDLTPEDLGTAELVEETKIgeekLTFIEGCKG-------------------------- 173
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 45550132 389 kmqerlarlsSGVALLRVGGSSDVEVSEKKDRVIDALNATRAAVEE 434
Cdd:cd03333 174 ----------GKAATILLRGATEVELDEVKRSLHDALCAVRAAVEE 209
|
|
| cpn60 |
cd03343 |
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ... |
33-539 |
5.78e-23 |
|
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: 102.34 E-value: 5.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 33 GPEVRAMMLQGVDVLADAVAVTMGPKGRNVIIEQSWGSPKITKDGVTVAKSIALkdkfQNIGAKLVQDVANNTNEEAGDG 112
Cdd:cd03343 13 GRDAQRMNIAAAKAVAEAVRTTLGPKGMDKMLVDSLGDVTITNDGATILKEMDI----EHPAAKMLVEVAKTQDEEVGDG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 113 TTTATVLARAIAKEGFEKISRGASPVEIRRGVMLAIETVKDNLRRLSRPVNTPEE--ICQVATISANGdKSVG------- 183
Cdd:cd03343 89 TTTAVVLAGELLEKAEDLLDQNIHPTVIIEGYRLAAEKALELLDEIAIKVDPDDKdtLRKIAKTSLTG-KGAEaakdkla 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 184 NLISEAIKKV--GRDGVITV---------KDGKTLcDELEVIEGMKFDRGYISPYFINTSKGAKVEFQDALLLFCEKKIK 252
Cdd:cd03343 168 DLVVDAVLQVaeKRDGKYVVdldnikiekKTGGSV-DDTELIRGIVIDKEVVHPGMPKRVENAKIALLDAPLEVKKTEID 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 253 SAPSIVPALELANAQrkplviiaeDLEAEALSTLVVNRLKVGLQVCAV-------------KAPGFGDNR--KENLMDMA 317
Cdd:cd03343 247 AKIRITSPDQLQAFL---------EQEEAMLKEMVDKIADTGANVVFCqkgiddlaqhylaKAGILAVRRvkKSDMEKLA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 318 VATGGIVFGDeanmvrLEDIKMSDFGRVGEVVVSK--DDTMLLkgkgqkaevekrVEGLREAikestssyekekmqerla 395
Cdd:cd03343 318 RATGAKIVTN------IDDLTPEDLGEAELVEERKvgDDKMVF------------VEGCKNP------------------ 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 396 rlsSGVALLrVGGSSDVEVSEKKDRVIDALNATRAAVEEG-IVPGGGTALLRCIQKLNDL-KGANEDQNMGIEIIRRALR 473
Cdd:cd03343 362 ---KAVTIL-LRGGTEHVVDELERALEDALRVVADALEDGkVVAGGGAVEIELAKRLREYaRSVGGREQLAVEAFADALE 437
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 474 MPCLTIAKNAGVDGAMVVAKV----EILDGDYGYDALKGEYGNMIERGIIDPTKVVRTAISDAAGVASLL 539
Cdd:cd03343 438 EIPRTLAENAGLDPIDTLVELraahEKGNKNAGLDVYTGEVVDMLEKGVIEPLRVKKQAIKSATEAATMI 507
|
|
| chap_CCT_beta |
TIGR02341 |
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ... |
43-550 |
1.39e-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: 73.36 E-value: 1.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 43 GVDVLADAVAVTMGPKGRNVIIEQ--SWGSPKITKDGVTVAKSIALkdkfQNIGAKLVQDVANNTNEEAGDGTTTATVLA 120
Cdd:TIGR02341 22 GAIAIGDLVKSTLGPKGMDKILQSssSDASIMVTNDGATILKSIGV----DNPAAKVLVDMSKVQDDEVGDGTTSVTVLA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 121 RAIAKEGFEKISRGASPVEIRRGVMLAIETVKDNLRRLS-----RPVNTPEEICQVATISANGDKSVGNliSEAIKKVGR 195
Cdd:TIGR02341 98 AELLREAEKLINQKIHPQTIIAGYREATKAARDALLKSAvdngsDEVKFRQDLMNIARTTLSSKILSQH--KDHFAQLAV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 196 DGVITVKdGKTLCDELEVIE--GMKFDRGYISPYFINTSKGAkvefqdallLFCEKKIKSAPSIVPALELANAQRKPL-V 272
Cdd:TIGR02341 176 DAVLRLK-GSGNLEAIQIIKklGGSLADSYLDEGFLLDKKIG---------VNQPKRIENAKILIANTGMDTDKVKIFgS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 273 IIAEDLEAEALSTLVVNRLKVGLQVCAVKAPGFGD--NRK--ENLMDMAVATGGIVFGDEANMVRLEDIKMSdfgRVGEV 348
Cdd:TIGR02341 246 RVRVDSTAKVAELEHAEKEKMKEKVEKILKHGINCfiNRQliYNYPEQLFADAGVMAIEHADFEGVERLALV---TGGEI 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 349 VVSKDDTMLLKgKGQKAEVEKRVEGlreaikestssyekekmQERLARLsSGVAL-----LRVGGSSDVEVSEKKDRVID 423
Cdd:TIGR02341 323 VSTFDHPELVK-LGSCDLIEEIMIG-----------------EDKLLKF-SGVKLgeactIVLRGATQQILDEAERSLHD 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 424 ALNATRAAVEEGIVPGGGTALLRCIQKLNDLKGANED--QNMGIEIIRRALRMPCLTIAKNAGVDGAMVVAKV--EILDG 499
Cdd:TIGR02341 384 ALCVLSQTVKESRTVLGGGCSEMLMSKAVTQEAQRTPgkEALAVEAFARALRQLPTIIADNAGFDSAELVAQLraAHYNG 463
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 45550132 500 DY--GYDALKGEYGNMIERGIIDPTKVVRTAISDAAGVASLLTTAEAVVTELP 550
Cdd:TIGR02341 464 NTtmGLDMNEGTIADMRQLGITESYKVKRAVVSSAAEAAEVILRVDNIIKAAP 516
|
|
| TCP1_beta |
cd03336 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ... |
33-550 |
3.48e-13 |
|
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.
Pssm-ID: 239452 [Multi-domain] Cd Length: 517 Bit Score: 71.98 E-value: 3.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 33 GPEVRAMMLQGVDVLADAVAVTMGPKGRNVIIEQSW--GSPKITKDGVTVAKSIALkdkfQNIGAKLVQDVANNTNEEAG 110
Cdd:cd03336 11 GETARLSSFVGAIAIGDLVKTTLGPKGMDKILQSVGrsGGVTVTNDGATILKSIGV----DNPAAKVLVDISKVQDDEVG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 111 DGTTTATVLARAIAKEGFEKISRGASPVEIRRGVMLAIETVKDNLRRL-----SRPVNTPEEICQVA--TISA---NGDK 180
Cdd:cd03336 87 DGTTSVTVLAAELLREAEKLVAQKIHPQTIIEGYRMATAAAREALLSSavdhsSDEEAFREDLLNIArtTLSSkilTQDK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 181 S-VGNLISEAIKKVGRDG-----VITVKDGKTLCDELeviegmkFDRGYISPYFINTSKGAKVEfqDALLLFC-----EK 249
Cdd:cd03336 167 EhFAELAVDAVLRLKGSGnldaiQIIKKLGGSLKDSY-------LDEGFLLDKKIGVNQPKRIE--NAKILIAntpmdTD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 250 KIKSAPSIVPALELANaqrkplviIAEDLEAEalstlvvnRLKVGLQVCAVKAPGFG--DNRK--ENLMDMAVATGGIVf 325
Cdd:cd03336 238 KIKIFGAKVRVDSTAK--------VAEIEEAE--------KEKMKNKVEKILKHGINcfINRQliYNYPEQLFADAGIM- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 326 gdeanmvrleDIKMSDFGRV--------GEVVVSKDDTMLLK-GKGQKAEvekrveglreaikestssyekEKM--QERL 394
Cdd:cd03336 301 ----------AIEHADFDGVerlalvtgGEIASTFDHPELVKlGTCKLIE---------------------EIMigEDKL 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 395 ARLsSGVAL-------LRvgGSSDVEVSEKKDRVIDALNATRAAVEEG-IVPGGGTALLRCIQKLNDLkgANE---DQNM 463
Cdd:cd03336 350 IRF-SGVAAgeactivLR--GASQQILDEAERSLHDALCVLAQTVKDTrVVLGGGCSEMLMAKAVEEL--AKKtpgKKSL 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 464 GIEIIRRALRMPCLTIAKNAGVDGAMVVAKV--EILDG--DYGYDALKGEYGNMIERGIIDPTKVVRTAISDAAGVASLL 539
Cdd:cd03336 425 AIEAFAKALRQLPTIIADNAGYDSAELVAQLraAHYNGntTAGLDMRKGTVGDMKELGITESFKVKRQVLLSASEAAEMI 504
|
570
....*....|.
gi 45550132 540 TTAEAVVTELP 550
Cdd:cd03336 505 LRVDDIIKCAP 515
|
|
| TCP1_delta |
cd03338 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ... |
35-533 |
4.45e-13 |
|
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: 71.55 E-value: 4.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 35 EVRAMMLQGVDVLADAVAVTMGPKGRNVIIEQSWGSPKITKDGVTVAKSIALkdkfQNIGAKLVQDVANNTNEEAGDGTT 114
Cdd:cd03338 8 DVRLSNIQAAKAVADAIRTSLGPRGMDKMIQTGKGEVIITNDGATILKQMSV----LHPAAKMLVELSKAQDIEAGDGTT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 115 TATVLARAIAKEGFEKISRGASPVEIRRGVMLAIETVKDNLRRLSRPV--NTPEEICQVATISANG------DKSVGNLI 186
Cdd:cd03338 84 SVVVLAGALLSACESLLKKGIHPTVISESFQIAAKKAVEILDSMSIPVdlNDRESLIKSATTSLNSkvvsqySSLLAPIA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 187 SEAIKKVG----------RDGVITVKDGKTLCDElEVIEGM----KFDRGYISPYFINTSKGAKVEFQ------------ 240
Cdd:cd03338 164 VDAVLKVIdpatatnvdlKDIRIVKKLGGTIEDT-ELVDGLvftqKASKKAGGPTRIEKAKIGLIQFClsppktdmdnni 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 241 ---------------DALLLFCEKKIKSAPsivpalelANaqrkpLVIIAEDLEAEALSTLVVNRLKvGLQVCAVKapgf 305
Cdd:cd03338 243 vvndyaqmdrilreeRKYILNMCKKIKKSG--------CN-----VLLIQKSILRDAVSDLALHFLA-KLKIMVVK---- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 306 gDNRKENLMDMAVATGGIVFGDeanmvrLEDIKMSDFGRVGEV-VVSKDDTMLLKgkgqkaevekrVEGLREAIKESTss 384
Cdd:cd03338 305 -DIEREEIEFICKTIGCKPVAS------IDHFTEDKLGSADLVeEVSLGDGKIVK-----------ITGVKNPGKTVT-- 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 385 yekekmqerlarlssgvALLRvgGSSDVEVSEKKDRVIDALNATRAAVEE-GIVPGGGTALLRCIQKLNDLkgANEDQNM 463
Cdd:cd03338 365 -----------------ILVR--GSNKLVLDEAERSLHDALCVIRCLVKKrALIPGGGAPEIEIALQLSEW--ARTLTGV 423
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45550132 464 GIEIIR---RALRMPCLTIAKNAGVDGAMVVAKV--EILDGD--YGYDALKGEYGNMIERGIIDPTKVVRTAISDAA 533
Cdd:cd03338 424 EQYCVRafaDALEVIPYTLAENAGLNPISIVTELrnRHAQGEknAGINVRKGAITNILEENVVQPLLVSTSAITLAT 500
|
|
| chap_CCT_alpha |
TIGR02340 |
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ... |
33-553 |
3.67e-12 |
|
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: 68.98 E-value: 3.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 33 GPEVRAMMLQGVDVLADAVAVTMGPKGRNVIIEQSWGSPKITKDGVTVAKSIALKDKfqniGAKLVQDVANNTNEEAGDG 112
Cdd:TIGR02340 10 GQDVRTQNVTAAMAIANIVKTSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHP----AAKILVELAQLQDREVGDG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 113 TTTATVLARAIAKEGFEKISRGASPVEIRRGVMLAI-ETVKDNLRRLSRPVNT--PEEICQVA-------TISANGDkSV 182
Cdd:TIGR02340 86 TTSVVIIAAELLKRADELVKNKIHPTSVISGYRLACkEAVKYIKENLSVSVDElgREALINVAktsmsskIIGLDSD-FF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 183 GNLISEA---IKKVGRDGVIT--VKDGKTL------CDELEVIEGMKFDRGYISPYFINTSKGAKVefqdALLLFCEKKI 251
Cdd:TIGR02340 165 SNIVVDAvlaVKTTNENGETKypIKAINILkahgksARESMLVKGYALNCTVASQQMPKRIKNAKI----ACLDFNLQKA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 252 KSA--PSIVP--ALELANAQRKPLVIIAED----LEAEA---LSTLVVNRLKVGLQVCAvKAPGFGDNRKENLMDMAVAT 320
Cdd:TIGR02340 241 KMAlgVQIVVddPEKLEQIRQREADITKERikkiLDAGAnvvLTTGGIDDMCLKYFVEA-GAMGVRRCKKEDLKRIAKAT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 321 GGIVFGDEANMVRLEDIKMSDFGRVGEVV---VSKDDTMLLKGKGQKaevekrveglreaikestssyekekmqerlarl 397
Cdd:TIGR02340 320 GATLVSTLADLEGEETFEASYLGFADEVVqerIADDECILIKGTKKR--------------------------------- 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 398 SSGVALLRvgGSSDVEVSEKKDRVIDALNATRAAVEEG-IVPGGG---TALLRCIQKLNDLKGANEdqNMGIEIIRRALR 473
Cdd:TIGR02340 367 KSASIILR--GANDFMLDEMERSLHDALCVVKRTLESNsVVPGGGaveAALSIYLENFATTLGSRE--QLAIAEFARALL 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 474 MPCLTIAKNAGVDGAMVVAKV------EILDGD------YGYDALKGEYGNMIERGIIDPTkvvrtaisdAAGVASLLTT 541
Cdd:TIGR02340 443 IIPKTLAVNAAKDSTELVAKLrayhaaAQLKPEkkhlkwYGLDLVNGKIRDNKEAGVLEPT---------VSKVKSLKFA 513
|
570
....*....|..
gi 45550132 542 AEAVVTELPLEE 553
Cdd:TIGR02340 514 TEAAITILRIDD 525
|
|
| chap_CCT_epsi |
TIGR02343 |
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ... |
41-521 |
4.94e-11 |
|
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT epsilon chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.
Pssm-ID: 274084 [Multi-domain] Cd Length: 532 Bit Score: 65.21 E-value: 4.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 41 LQGVDVL------ADAVAVTM----GPKGRNVIIEQSWGSPKITKDGVTVAKSIALkdkfQNIGAKLVQDVANNTNEEAG 110
Cdd:TIGR02343 23 LKGLEAKksniaaAKSVASILrtslGPKGMDKMLISPDGDITVTNDGATILSQMDV----DNQIAKLMVELSKSQDDEIG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 111 DGTTTATVLARAIAKEGFEKISRGASPVEIRRG----VMLAIETVKDNLRRLSRPVNTPEEICQVATISAnGDKSVgNLI 186
Cdd:TIGR02343 99 DGTTGVVVLAGALLEQAEELLDKGIHPIKIADGfeeaARIAVEHLEEISDEISADNNNREPLIQAAKTSL-GSKIV-SKC 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 187 SEAIKKVGRDGVITVKD-----------------GKTLCDElEVIEGMKFDRGYISPYFINTSKGAKVefqdALLL--FC 247
Cdd:TIGR02343 177 HRRFAEIAVDAVLNVADmerrdvdfdlikvegkvGGSLEDT-KLIKGIIIDKDFSHPQMPKEVEDAKI----AILTcpFE 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 248 EKKIKSAPSIVpaleLANAQR-KPLviiaEDLEAEALSTLVVNRLKVGLQVcAVKAPGFGDNRKENLMD----------- 315
Cdd:TIGR02343 252 PPKPKTKHKLD----ISSVEEyKKL----QKYEQQKFKEMIDDIKKSGANL-VICQWGFDDEANHLLLQndlpavrwvgg 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 316 -----MAVATGGIVfgdeanMVRLEDIKMSDFGRVGEVvvskddtmllkgkgqkaevekrveglreaiKESTSSYEKEKM 390
Cdd:TIGR02343 323 qelelIAIATGGRI------VPRFQELSKDKLGKAGLV------------------------------REISFGTTKDRM 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 391 Q--ERLARlSSGVALLrVGGSSDVEVSEKKDRVIDALNATRAAVEEG-IVPGGGTALLRCIQKLNDL--KGANEDQnMGI 465
Cdd:TIGR02343 367 LviEQCKN-SKAVTIF-IRGGNKMIIEEAKRSIHDALCVVRNLIKDSrIVYGGGAAEISCSLAVSQEadKYPGVEQ-YAI 443
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45550132 466 EIIRRALRMPCLTIAKNAGVD--GAMVVAK---VEILDGDYGYDALKGEYGNMIERGIIDP 521
Cdd:TIGR02343 444 RAFADALETIPMALAENSGLDpiGTLSTLKslqLKEKNPNLGVDCLGYGTNDMKEQFVFET 504
|
|
| chap_CCT_delta |
TIGR02342 |
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ... |
35-547 |
6.01e-11 |
|
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT delta chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.
Pssm-ID: 274083 Cd Length: 517 Bit Score: 64.80 E-value: 6.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 35 EVRAMMLQGVDVLADAVAVTMGPKGRNVIIEQSWGSPKITKDGVTVAKSIALkdkfQNIGAKLVQDVANNTNEEAGDGTT 114
Cdd:TIGR02342 9 DVRTSNIVAAKAVADAIRTSLGPKGMDKMIQDGKGEVIITNDGATILKQMAV----LHPAAKMLVELSKAQDIEAGDGTT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 115 TATVLARAIAKEGFEKISRGASPVEIRRGVMLAIETVKDNLRRLSRPVNTPEEICQVATISANGDKSVGNLISEAIKKVG 194
Cdd:TIGR02342 85 SVVILAGALLGACERLLNKGIHPTIISESFQSAADEAIKILDEMSIPVDLSDREQLLKSATTSLSSKVVSQYSSLLAPLA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 195 RDGVITVKDGKT-----------------LCDELEVIEGMKFDRGYI----SPYFINTSKGAKVEFQdalllFCEKKIKS 253
Cdd:TIGR02342 165 VDAVLKVIDPENaknvdlndikvvkklggTIDDTELIEGLVFTQKASksagGPTRIEKAKIGLIQFQ-----ISPPKTDM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 254 APSIVpalelANAQRKPLVIIAEdlEAEALSTLVVNRLKVGLQVCAVKapgfgdnrKENLMDmAVATGGIVFGDEANMVR 333
Cdd:TIGR02342 240 ENQII-----VNDYAQMDRVLKE--ERAYILNIVKKIKKTGCNVLLIQ--------KSILRD-AVNDLALHFLAKMKIMV 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 334 LEDIKMSDFgrvgevvvskddTMLLKGKGQK--AEVEKRVE---GLREAIKESTSSYEKEKMQERLARLSSGVALLrVGG 408
Cdd:TIGR02342 304 VKDIEREEI------------EFICKTIGCKpiASIDHFTAdklGSAELVEEVDSDGGKIIKITGIQNAGKTVTVV-VRG 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 409 SSDVEVSEKKDRVIDALNATRAAVEE-GIVPGGGTALLRCIQKLNDLkgANEDQNMGIEIIRR---ALRMPCLTIAKNAG 484
Cdd:TIGR02342 371 SNKLVIDEAERSLHDALCVIRCLVKKrGLIAGGGAPEIEIARRLSKY--ARTMKGVESYCVRAfadALEVIPYTLAENAG 448
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45550132 485 VDGAMVVAKV----EILDGDYGYDALKGEYGNMIERGIIDPTKVVRTAISDAA-GVASLLTTAEAVVT 547
Cdd:TIGR02342 449 LNPIKVVTELrnrhANGEKTAGISVRKGGITNMLEEHVLQPLLVTTSAITLASeTVRSILKIDDIVFT 516
|
|
| TCP1_eta |
cd03340 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ... |
46-153 |
8.68e-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: 8.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 46 VLADAVAVTMGPKGRNVIIEQSWGSPKITKDGVTVAKSIalkdkfqNI---GAKLVQDVANNTNEEAGDGTTTATVLARA 122
Cdd:cd03340 27 AIADAVRTTLGPRGMDKLIVDGRGKVTISNDGATILKLL-------DIvhpAAKTLVDIAKSQDAEVGDGTTSVVVLAGE 99
|
90 100 110
....*....|....*....|....*....|....*
gi 45550132 123 IAKEGFEKISRGASPVEI----RRGVMLAIETVKD 153
Cdd:cd03340 100 FLKEAKPFIEDGVHPQIIirgyRKALQLAIEKIKE 134
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
33-159 |
2.98e-10 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 62.74 E-value: 2.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 33 GPEVRAMMLQGVDVLADAVAVTMGPKGRNVIIE-----QSWGSPKITKDGVTVAKSIALkdkfQNIGAKLVQDVANNTNE 107
Cdd:PTZ00212 20 GETARLQSFVGAIAVADLVKTTLGPKGMDKILQpmsegPRSGNVTVTNDGATILKSVWL----DNPAAKILVDISKTQDE 95
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 45550132 108 EAGDGTTTATVLARAIAKEGFEKISRGASPVEIRRGVMLAIETVKDNLRRLS 159
Cdd:PTZ00212 96 EVGDGTTSVVVLAGELLREAEKLLDQKIHPQTIIEGWRMALDVARKALEEIA 147
|
|
| chap_CCT_eta |
TIGR02345 |
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ... |
46-154 |
3.54e-10 |
|
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: 62.47 E-value: 3.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 46 VLADAVAVTMGPKGRNVIIEQSWGSPKITKDGVTVAKSIALKDKfqniGAKLVQDVANNTNEEAGDGTTTATVLARAIAK 125
Cdd:TIGR02345 29 AIAEALKTTLGPRGMDKLIVGSNGKATISNDGATILKLLDIVHP----AAKTLVDIAKSQDAEVGDGTTSVTILAGELLK 104
|
90 100 110
....*....|....*....|....*....|...
gi 45550132 126 EGFEKISRGASPVEIRRG----VMLAIETVKDN 154
Cdd:TIGR02345 105 EAKPFIEEGVHPQLIIRCyreaLSLAVEKIKEI 137
|
|
| TCP1_epsilon |
cd03339 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ... |
47-521 |
3.34e-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: 59.62 E-value: 3.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 47 LADAVAVTMGPKGRNVIIEQSWGSPKITKDGVTVAKSIALkdkfQNIGAKLVQDVANNTNEEAGDGTTTATVLARAIAKE 126
Cdd:cd03339 35 VANILRTSLGPRGMDKILVSPDGEVTVTNDGATILEKMDV----DHQIAKLLVELSKSQDDEIGDGTTGVVVLAGALLEQ 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 127 GFEKISRGASPVEIRRGVMLAIETVKDNLRRLSRPV----NTPEEICQVATISAnGDKSVgNLISEAIKKVGRDGVITVK 202
Cdd:cd03339 111 AEKLLDRGIHPIRIADGYEQACKIAVEHLEEIADKIefspDNKEPLIQTAMTSL-GSKIV-SRCHRQFAEIAVDAVLSVA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 203 D--------------GKT--LCDELEVIEGMKFDRGYISPYFINTSKGAKVefqdALLL--FCEKKIKSAPSI-VPALEL 263
Cdd:cd03339 189 DlerkdvnfelikveGKVggRLEDTKLVKGIVIDKDFSHPQMPKEVKDAKI----AILTcpFEPPKPKTKHKLdITSVED 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 264 ANAQRKplviiaedLEAEALSTLVVNRLKVG--LQVCAVkapGFGDNRKENLMD----------------MAVATGG-IV 324
Cdd:cd03339 265 YKKLQE--------YEQKYFREMVEQVKDAGanLVICQW---GFDDEANHLLLQnglpavrwvggveielIAIATGGrIV 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 325 fgdeanmVRLEDIKMSDFGRVGEVvvskddtmllkgkgqkaevekrveglreaiKESTSSYEKEKMQ--ERLARlSSGVA 402
Cdd:cd03339 334 -------PRFEDLSPEKLGKAGLV------------------------------REISFGTTKDKMLviEGCPN-SKAVT 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 403 LLrVGGSSDVEVSEKKDRVIDALNATRAAVEEG-IVPGGGTALLRC---IQKLNDlKGANEDQnMGIEIIRRALRMPCLT 478
Cdd:cd03339 376 IF-IRGGNKMIIEEAKRSLHDALCVVRNLIRDNrIVYGGGAAEISCslaVEKAAD-KCSGIEQ-YAMRAFADALESIPLA 452
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 45550132 479 IAKNAGVDGAMVVAKVEIL-----DGDYGYDALKGEYGNMIERGIIDP 521
Cdd:cd03339 453 LAENSGLNPIETLSEVKARqvkekNPHLGIDCLGRGTNDMKEQKVFET 500
|
|
| TCP1_alpha |
cd03335 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ... |
33-522 |
1.32e-08 |
|
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.
Pssm-ID: 239451 Cd Length: 527 Bit Score: 57.68 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 33 GPEVRAMMLQGVDVLADAVAVTMGPKGRNVIIEQSWGSPKITKDGVTVAKSIALKDKfqniGAKLVQDVANNTNEEAGDG 112
Cdd:cd03335 6 GQDVRTQNVTAAMAIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHP----AAKILVELAQLQDKEVGDG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 113 TTTATVLARAIAKEGFEKISRGASPVEIRRGVMLAI-ETVKDNLRRLSRPVNT--PEEICQVA-------TISANGDkSV 182
Cdd:cd03335 82 TTSVVIIAAELLKRANELVKQKIHPTTIISGYRLACkEAVKYIKEHLSISVDNlgKESLINVAktsmsskIIGADSD-FF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 183 GNLISEAIKKV-----GRDGVITVKD-------GKTLCDELeVIEGMKFDRGYISPYFINTSKGAKVefqdALLLFCEKK 250
Cdd:cd03335 161 ANMVVDAILAVkttneKGKTKYPIKAvnilkahGKSAKESY-LVNGYALNCTRASQGMPTRVKNAKI----ACLDFNLQK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 251 IKSA--PSIV---PAlELANAQRKPLVIIAED----LEAEA---LSTLVVNRLKVGLQVCAvKAPGFGDNRKENLMDMAV 318
Cdd:cd03335 236 TKMKlgVQVVvtdPE-KLEKIRQRESDITKERikkiLAAGAnvvLTTGGIDDMCLKYFVEA-GAMAVRRVKKEDLRRIAK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 319 ATGGIVFGDEANMVRLEDIKMSDFGRVGEVV---VSKDDTMLLKGkgqkaevekrveglreaikestssyekekmqerLA 395
Cdd:cd03335 314 ATGATLVSTLANLEGEETFDPSYLGEAEEVVqerIGDDELILIKG---------------------------------TK 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 396 RLSSGVALLRvgGSSDVEVSEKKDRVIDALNATRAAVEEG-IVPGGG---TALLRCIQKLNDLKGANEdqNMGIEIIRRA 471
Cdd:cd03335 361 KRSSASIILR--GANDFMLDEMERSLHDALCVVKRTLESNsVVPGGGaveTALSIYLENFATTLGSRE--QLAIAEFAEA 436
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45550132 472 LRMPCLTIAKNAGVDGAMVVAKV------EILDGD------YGYDALKGEYGNMIERGIIDPT 522
Cdd:cd03335 437 LLVIPKTLAVNAAKDATELVAKLrayhaaAQVKPDkkhlkwYGLDLINGKVRDNLEAGVLEPT 499
|
|
| chap_CCT_zeta |
TIGR02347 |
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ... |
38-539 |
2.57e-08 |
|
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: 56.67 E-value: 2.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 38 AMMLQGVDVLADAVAVTMGPKGRNVIIEQSWGSPKITKDGVTVAKSIALkdkfQNIGAKLVQDVANNTNEEAGDGTTTAT 117
Cdd:TIGR02347 19 MMNINAARGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEMQI----QHPTASMIARAATAQDDITGDGTTSTV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 118 VLARAIAKEGFEKISRGASPVEIRRGVMLAIETVKDNLR--RLSRPVNTPEEICQVATISANGDK-------SVGNLISE 188
Cdd:TIGR02347 95 LLIGELLKQAERYILEGVHPRIITEGFEIARKEALQFLDkfKVKKEDEVDREFLLNVARTSLRTKlpadladQLTEIVVD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 189 AIKKVGRDG------VITVKDGKTLCD-ELEVIEGMKFDRGYISPyfintskGAKVEFQDALLLFCEKKIKSAPSIVPA- 260
Cdd:TIGR02347 175 AVLAIKKDGedidlfMVEIMEMKHKSAtDTTLIRGLVLDHGARHP-------DMPRRVKNAYILTCNVSLEYEKTEVNSg 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 261 ---------LELANAQRKPL-----VIIaeDLEAEalstLVVNRLKVGLQVCAVKA---PGFGDNRKENLMDMAVATggi 323
Cdd:TIGR02347 248 ffyssaeqrEKLVKAERKFVddrvkKII--ELKKK----VCGKSPDKGFVVINQKGidpPSLDLLAKEGIMALRRAK--- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 324 vfgdEANMVRLEdikmsdFGRVGEVVVSKDDtmllkgkgqkaeVEKRVEGLREAIKESTSSYEKEKMQERLARLSSGVAL 403
Cdd:TIGR02347 319 ----RRNMERLT------LACGGEALNSVED------------LTPECLGWAGLVYETTIGEEKYTFIEECKNPKSCTIL 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 404 LRvgGSSDVEVSEKKDRVIDALNATRAAVEEG-IVPGGGTALLRCIQKLNDL-KGANEDQNMGIEIIRRALRMPCLTIAK 481
Cdd:TIGR02347 377 IK--GPNDHTIAQIKDAVRDGLRAVKNAIEDKcVVPGAGAFEIAAYRHLKEYkKSVKGKAKLGVEAFANALLVIPKTLAE 454
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45550132 482 NAGVDGAMVVAKV--EILDG--DYGYDALKGEYGNMIERGIIDPTKVVRTAISDAAGVASLL 539
Cdd:TIGR02347 455 NSGFDAQDTLVKLedEHDEGgeVVGVDLNTGEPIDPEIKGIWDNYRVKKQLIQSATVIASQL 516
|
|
| TCP1_zeta |
cd03342 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
47-539 |
6.40e-07 |
|
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.
Pssm-ID: 239458 [Multi-domain] Cd Length: 484 Bit Score: 52.26 E-value: 6.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 47 LADAVAVTMGPKGRNVIIEQSWGSPKITKDGVTVAKSIalkdKFQNIGAKLVQDVANNTNEEAGDGTTTATVLARAIAKE 126
Cdd:cd03342 24 LQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLSEM----QIQHPTASMIARAATAQDDITGDGTTSNVLLIGELLKQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 127 GFEKISRGASPVEIRRGVMLAIETVKDNLRRLSRPVNTP---EEICQVATISANgdKSVGNLISEAIKKVGRDGVITV-K 202
Cdd:cd03342 100 AERYIQEGVHPRIITEGFELAKNKALKFLESFKVPVEIDtdrELLLSVARTSLR--TKLHADLADQLTEIVVDAVLAIyK 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 203 DGKTLcdELEVIEGMKFDRGYISpyfiNTS--KG-------------AKVEfqDALLLFCEKKIKSAPSIVpalelaNAQ 267
Cdd:cd03342 178 PDEPI--DLHMVEIMQMQHKSDS----DTKliRGlvldhgarhpdmpKRVE--NAYILTCNVSLEYEKTEV------NSG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 268 RKPLVIIAE--------DLEAEAlSTLVVNRLKvglqvcavkapgfgdnrKENLMDMAVATGGivfgdEAnMVRLEDIKM 339
Cdd:cd03342 244 FFYSVVINQkgidppslDMLAKE-GILALRRAK-----------------RRNMERLTLACGG-----VA-MNSVDDLSP 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 340 SDFGRVGEVvvskddtmllkgkgqkaevekrveglreaiKESTSSYEKEKMQERLARLSSGVALLRvgGSSDVEVSEKKD 419
Cdd:cd03342 300 ECLGYAGLV------------------------------YERTLGEEKYTFIEGVKNPKSCTILIK--GPNDHTITQIKD 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 420 RVIDALNATRAAVEEG-IVPGGGTALLRCIQKL-NDLKGANEDQNMGIEIIRRALRMPCLTIAKNAGVDGAMVVAKV--E 495
Cdd:cd03342 348 AIRDGLRAVKNAIEDKcVVPGAGAFEVALYAHLkEFKKSVKGKAKLGVQAFADALLVIPKTLAENSGLDVQETLVKLqdE 427
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 45550132 496 ILDG--DYGYDALKGEYGNMIERGIIDPTKVVRTAISDAAGVASLL 539
Cdd:cd03342 428 YAEGgqVGGVDLDTGEPMDPESEGIWDNYSVKRQILHSATVIASQL 473
|
|
| chap_CCT_theta |
TIGR02346 |
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ... |
47-221 |
3.91e-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: 46.63 E-value: 3.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 47 LADAVAVTMGPKGRNVIIEQSWGSPKITKDGVTVAKSIALkdkfQNIGAKLVQDVANNTNEEAGDGTTTATVLARAIAKE 126
Cdd:TIGR02346 30 LSQITRTSLGPNGMNKMVINHLEKLFVTNDAATILRELEV----QHPAAKLLVMASEMQENEIGDGTNLVLVLAGELLNK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 127 GFEKISRGASPVEIRRGVMLA---------------IETV--KDNLRRLSRPVNTPEEICQVATISANGDKSVGNLISEA 189
Cdd:TIGR02346 106 AEELIRMGLHPSEIIKGYEMAlkkameileelvvweVKDLrdKDELIKALKASISSKQYGNEDFLAQLVAQACSTVLPKN 185
|
170 180 190
....*....|....*....|....*....|...
gi 45550132 190 IKKVGRDGVITVK-DGKTLCDElEVIEGMKFDR 221
Cdd:TIGR02346 186 PQNFNVDNIRVCKiLGGSLSNS-EVLKGMVFNR 217
|
|
| chap_CCT_gamma |
TIGR02344 |
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ... |
41-213 |
5.40e-05 |
|
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: 45.88 E-value: 5.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 41 LQGVDVLADAVAVTMGPKGRNVIIEQSWGSPKITKDGVTVAKSIALkdkfQNIGAKLVQDVANNTNEEAGDGTTTATVLA 120
Cdd:TIGR02344 22 IQAAKAVADIIRTCLGPRSMLKMLLDPMGGIVMTNDGNAILREIDV----AHPAAKSMIELSRTQDEEVGDGTTSVIILA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 121 RAIAKEGFEKISRGASPVEIRRGVMLAIETVKDNLRRLSRPVNTPEEICQVATISAN-GDKSVGNLiSEAIKKVGRDGVI 199
Cdd:TIGR02344 98 GEMLSVAEPFLEQNIHPTVIIRAYRKALDDALSVLEEISIPVDVNDDAAMLKLIQSCiGTKFVSRW-SDLMCDLALDAVR 176
|
170
....*....|....
gi 45550132 200 TVKDGKTLCDELEV 213
Cdd:TIGR02344 177 TVQRDENGRKEIDI 190
|
|
| TCP1_gamma |
cd03337 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ... |
42-196 |
1.83e-04 |
|
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: 44.21 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 42 QGVDVLADAVAVTMGPKGRNVIIEQSWGSPKITKDGVTVAKSIALkdkfQNIGAKLVQDVANNTNEEAGDGTTTATVLAR 121
Cdd:cd03337 23 QAAKTVADVIRTCLGPRAMLKMLLDPMGGIVLTNDGNAILREIDV----AHPAAKSMIELSRTQDEEVGDGTTSVIILAG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 122 AIAKEGFEKISRGASPVEIRRGVMLAIETVKDNLRRLSRPVNtPEEICQVATI--SANGDKSVG-------NLISEAIKK 192
Cdd:cd03337 99 EILAVAEPFLERGIHPTVIIKAYRKALEDALKILEEISIPVD-VNDRAQMLKIikSCIGTKFVSrwsdlmcNLALDAVKT 177
|
....
gi 45550132 193 VGRD 196
Cdd:cd03337 178 VAVE 181
|
|
| TCP1_theta |
cd03341 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ... |
47-221 |
4.16e-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: 42.98 E-value: 4.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 47 LADAVAVTMGPKGRNVIIEQSWGSPKITKDGVTVAKSIalkdKFQNIGAKLVQDVANNTNEEAGDGTTTATVLARAIAKE 126
Cdd:cd03341 20 LSQITRTSYGPNGMNKMVINHLEKLFVTSDAATILREL----EVQHPAAKLLVMASQMQEEEIGDGTNLVVVLAGELLEK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550132 127 GFEKISRGASPVEIRRGVMLAIETVKDNLRRLS----RPVNTPEEICQvATISANGDKSVGN------LISEAI-----K 191
Cdd:cd03341 96 AEELLRMGLHPSEIIEGYEKALKKALEILEELVvykiEDLRNKEEVSK-ALKTAIASKQYGNedflspLVAEACisvlpE 174
|
170 180 190
....*....|....*....|....*....|....
gi 45550132 192 KVGR---DGVITVK-DGKTLCDElEVIEGMKFDR 221
Cdd:cd03341 175 NIGNfnvDNIRVVKiLGGSLEDS-KVVRGMVFKR 207
|
|
| |
