|
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: 872.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 28 KDVKFGADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDKYKNIGAKLVQDVANNTNE 107
Cdd:cd03344 1 KDIKFGEEARKALLRGVNKLADAVKVTLGPKGRNVVIEKSFGSPKITKDGVTVAKEIELEDPFENMGAQLVKEVASKTND 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 108 EAGDGTTTATVLARSIAKEGFEKISKGANPVEIRRGVMLAVDAVIAELKKQSKPVTTPEEIAQVATISANGDKEIGNIIS 187
Cdd:cd03344 81 VAGDGTTTATVLARAIIKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKPVKTKEEIAQVATISANGDEEIGELIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 188 DAMKKVGRKGVITVKDGKTLNDELEIIEGMKFDRGYISPYFINTSKGQKCEFQDAYVLLSEKKISSIQSIVPALEIANAH 267
Cdd:cd03344 161 EAMEKVGKDGVITVEEGKTLETELEVVEGMQFDRGYLSPYFVTDPEKMEVELENPYILLTDKKISSIQELLPILELVAKA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 268 RKPLVIIAEDVDGEALSTLVLNRLKVGLQVVAVKAPGFGDNRKNQLKDMAIATGGAVFGEEgLTLNLEDVQPHDLGKVGE 347
Cdd:cd03344 241 GRPLLIIAEDVEGEALATLVVNKLRGGLKVCAVKAPGFGDRRKAMLEDIAILTGGTVISEE-LGLKLEDVTLEDLGRAKK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 348 VIVTKDDAMLLKGKGDKAQIEKRIQEIIEQLDVTTSEYEKEKLNERLAKLSDGVAVLKVGGTSDVEVNEKKDRVTDALNA 427
Cdd:cd03344 320 VVVTKDDTTIIGGAGDKAAIKARIAQIRKQIEETTSDYDKEKLQERLAKLSGGVAVIKVGGATEVELKEKKDRVEDALNA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 428 TRAAVEEGIVLGGGCALLRCIPALDSLTPANEDQKIGIEIIKRTLKIPAMTIAKNAGVEGSLIVEKIMQSSSEVGYDAMA 507
Cdd:cd03344 400 TRAAVEEGIVPGGGVALLRASPALDKLKALNGDEKLGIEIVRRALEAPLRQIAENAGVDGSVVVEKVLESPDGFGYDAAT 479
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 41399285 508 GDFVNMVEKGIIDPTKVVRTALLDAAGVASLLTTAEVVVTE 548
Cdd:cd03344 480 GEYVDMIEAGIIDPTKVVRSALQNAASVASLLLTTEALVVD 520
|
|
| PTZ00114 |
PTZ00114 |
Heat shock protein 60; Provisional |
24-555 |
0e+00 |
|
Heat shock protein 60; Provisional
Pssm-ID: 185455 Cd Length: 555 Bit Score: 773.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 24 RAYAKDVKFGADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDKYKNIGAKLVQDVAN 103
Cdd:PTZ00114 11 RFKGKEIRFGDEARQSLLKGIERLADAVAVTLGPKGRNVIIEQEYGSPKITKDGVTVAKAIEFSDRFENVGAQLIRQVAS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 104 NTNEEAGDGTTTATVLARSIAKEGFEKISKGANPVEIRRGVMLAVDAVIAELKKQSKPVTTPEEIAQVATISANGDKEIG 183
Cdd:PTZ00114 91 KTNDKAGDGTTTATILARAIFREGCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQSRPVKTKEDILNVATISANGDVEIG 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 184 NIISDAMKKVGRKGVITVKDGKTLNDELEIIEGMKFDRGYISPYFINTSKGQKCEFQDAYVLLSEKKISSIQSIVPALEI 263
Cdd:PTZ00114 171 SLIADAMDKVGKDGTITVEDGKTLEDELEVVEGMSFDRGYISPYFVTNEKTQKVELENPLILVTDKKISSIQSILPILEH 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 264 ANAHRKPLVIIAEDVDGEALSTLVLNRLKVGLQVVAVKAPGFGDNRKNQLKDMAIATGGAVFGEEGLTLNLEDVQPHDLG 343
Cdd:PTZ00114 251 AVKNKRPLLIIAEDVEGEALQTLIINKLRGGLKVCAVKAPGFGDNRKDILQDIAVLTGATVVSEDNVGLKLDDFDPSMLG 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 344 KVGEVIVTKDDAMLLKGKGDKAQIEKRIQEIIEQLDVTTSEYEKEKLNERLAKLSDGVAVLKVGGTSDVEVNEKKDRVTD 423
Cdd:PTZ00114 331 SAKKVTVTKDETVILTGGGDKAEIKERVELLRSQIERTTSEYDKEKLKERLAKLSGGVAVIKVGGASEVEVNEKKDRIED 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 424 ALNATRAAVEEGIVLGGGCALLRCIPALDSLTPANE---DQKIGIEIIKRTLKIPAMTIAKNAGVEGSLIVEKIMQSS-S 499
Cdd:PTZ00114 411 ALNATRAAVEEGIVPGGGVALLRASKLLDKLEEDNEltpDQRTGVKIVRNALRLPTKQIAENAGVEGAVVVEKILEKKdP 490
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 41399285 500 EVGYDAMAGDFVNMVEKGIIDPTKVVRTALLDAAGVASLLTTAEVVVTEIPKEEKD 555
Cdd:PTZ00114 491 SFGYDAQTGEYVNMFEAGIIDPTKVVRSALVDAASVASLMLTTEAAIVDLPKEKKK 546
|
|
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
27-556 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 756.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 27 AKDVKFGADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDKYKNIGAKLVQDVANNTN 106
Cdd:PRK00013 2 AKDIKFGEDARRKLLRGVNKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDPFENMGAQLVKEVASKTN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 107 EEAGDGTTTATVLARSIAKEGFEKISKGANPVEIRRGVMLAVDAVIAELKKQSKPVTTPEEIAQVATISANGDKEIGNII 186
Cdd:PRK00013 82 DVAGDGTTTATVLAQAIVREGLKNVAAGANPMDLKRGIDKAVEAAVEELKKISKPVEDKEEIAQVATISANGDEEIGKLI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 187 SDAMKKVGRKGVITVKDGKTLNDELEIIEGMKFDRGYISPYFINTSKGQKCEFQDAYVLLSEKKISSIQSIVPALEIANA 266
Cdd:PRK00013 162 AEAMEKVGKEGVITVEESKGFETELEVVEGMQFDRGYLSPYFVTDPEKMEAELENPYILITDKKISNIQDLLPVLEQVAQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 267 HRKPLVIIAEDVDGEALSTLVLNRLKVGLQVVAVKAPGFGDNRKNQLKDMAIATGGAVFGEEgLTLNLEDVQPHDLGKVG 346
Cdd:PRK00013 242 SGKPLLIIAEDVEGEALATLVVNKLRGTLKVVAVKAPGFGDRRKAMLEDIAILTGGTVISEE-LGLKLEDATLEDLGQAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 347 EVIVTKDDAMLLKGKGDKAQIEKRIQEIIEQLDVTTSEYEKEKLNERLAKLSDGVAVLKVGGTSDVEVNEKKDRVTDALN 426
Cdd:PRK00013 321 KVVVTKDNTTIVDGAGDKEAIKARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATEVEMKEKKDRVEDALH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 427 ATRAAVEEGIVLGGGCALLRCIPALDSLTPANEDQKIGIEIIKRTLKIPAMTIAKNAGVEGSLIVEKIMQSSSE-VGYDA 505
Cdd:PRK00013 401 ATRAAVEEGIVPGGGVALLRAAPALEALKGLNGDEATGINIVLRALEAPLRQIAENAGLEGSVVVEKVKNGKGKgYGYNA 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 41399285 506 MAGDFVNMVEKGIIDPTKVVRTALLDAAGVASLLTTAEVVVTEIPKEEKDP 556
Cdd:PRK00013 481 ATGEYVDMIEAGIIDPTKVTRSALQNAASVAGLLLTTEAVVADKPEKKAAA 531
|
|
| groEL |
PRK12849 |
chaperonin GroEL; Reviewed |
27-556 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237230 Cd Length: 542 Bit Score: 714.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 27 AKDVKFGADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDKYKNIGAKLVQDVANNTN 106
Cdd:PRK12849 2 AKIIKFDEEARRALERGVNKLADAVKVTLGPKGRNVVIDKSFGAPTITKDGVSIAKEIELEDPFENLGAQLVKEVASKTN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 107 EEAGDGTTTATVLARSIAKEGFEKISKGANPVEIRRGVMLAVDAVIAELKKQSKPVTTPEEIAQVATISANGDKEIGNII 186
Cdd:PRK12849 82 DVAGDGTTTATVLAQALVQEGLKNVAAGANPMDLKRGIDKAVEAVVEELKALARPVSGSEEIAQVATISANGDEEIGELI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 187 SDAMKKVGRKGVITVKDGKTLNDELEIIEGMKFDRGYISPYFINTSKGQKCEFQDAYVLLSEKKISSIQSIVPALEIANA 266
Cdd:PRK12849 162 AEAMEKVGKDGVITVEESKTLETELEVTEGMQFDRGYLSPYFVTDPERMEAVLEDPLILLTDKKISSLQDLLPLLEKVAQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 267 HRKPLVIIAEDVDGEALSTLVLNRLKVGLQVVAVKAPGFGDNRKNQLKDMAIATGGAVFGEEgLTLNLEDVQPHDLGKVG 346
Cdd:PRK12849 242 SGKPLLIIAEDVEGEALATLVVNKLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGTVISED-LGLKLEEVTLDDLGRAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 347 EVIVTKDDAMLLKGKGDKAQIEKRIQEIIEQLDVTTSEYEKEKLNERLAKLSDGVAVLKVGGTSDVEVNEKKDRVTDALN 426
Cdd:PRK12849 321 RVTITKDNTTIVDGAGDKEAIEARVAQIRRQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATEVELKERKDRVEDALN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 427 ATRAAVEEGIVLGGGCALLRCIPALDSLTPANEDQKIGIEIIKRTLKIPAMTIAKNAGVEGSLIVEKIMQSSSEVGYDAM 506
Cdd:PRK12849 401 ATRAAVEEGIVPGGGVALLRAAKALDELAGLNGDQAAGVEIVRRALEAPLRQIAENAGLDGSVVVAKVLELEDGFGFNAA 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 41399285 507 AGDFVNMVEKGIIDPTKVVRTALLDAAGVASLLTTAEVVVTEIPKEEKDP 556
Cdd:PRK12849 481 TGEYGDLIAAGIIDPVKVTRSALQNAASVAGLLLTTEALVADKPEEEDPP 530
|
|
| GroEL |
TIGR02348 |
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ... |
27-551 |
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: 689.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 27 AKDVKFGADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDKYKNIGAKLVQDVANNTN 106
Cdd:TIGR02348 1 AKQIKFDEEARKALLRGVDKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDKFENMGAQLVKEVASKTN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 107 EEAGDGTTTATVLARSIAKEGFEKISKGANPVEIRRGVMLAVDAVIAELKKQSKPVTTPEEIAQVATISANGDKEIGNII 186
Cdd:TIGR02348 81 DVAGDGTTTATVLAQAIVKEGLKNVAAGANPIELKRGIEKAVEAVVEELKKLSKPVKGKKEIAQVATISANNDEEIGSLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 187 SDAMKKVGRKGVITVKDGKTLNDELEIIEGMKFDRGYISPYFINTSKGQKCEFQDAYVLLSEKKISSIQSIVPALEIANA 266
Cdd:TIGR02348 161 AEAMEKVGKDGVITVEESKSLETELEVVEGMQFDRGYISPYFVTDAEKMEVELENPYILITDKKISNIKDLLPLLEKVAQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 267 HRKPLVIIAEDVDGEALSTLVLNRLKVGLQVVAVKAPGFGDNRKNQLKDMAIATGGAVFGEEgLTLNLEDVQPHDLGKVG 346
Cdd:TIGR02348 241 SGKPLLIIAEDVEGEALATLVVNKLRGTLNVCAVKAPGFGDRRKAMLEDIAILTGGQVISEE-LGLKLEEVTLDDLGKAK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 347 EVIVTKDDAMLLKGKGDKAQIEKRIQEIIEQLDVTTSEYEKEKLNERLAKLSDGVAVLKVGGTSDVEVNEKKDRVTDALN 426
Cdd:TIGR02348 320 KVTVDKDNTTIVEGAGDKAAIKARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATETEMKEKKLRIEDALN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 427 ATRAAVEEGIVLGGGCALLRCIPALDSLTPANEDQKIGIEIIKRTLKIPAMTIAKNAGVEGSLIVEKIMQSSSEVGYDAM 506
Cdd:TIGR02348 400 ATRAAVEEGIVPGGGVALLRAAAALEGLKGDGEDEAIGIDIVKRALEAPLRQIAENAGLDGAVVAEKVKELKGNFGFNAA 479
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 41399285 507 AGDFVNMVEKGIIDPTKVVRTALLDAAGVASLLTTAEVVVTEIPK 551
Cdd:TIGR02348 480 TGEYEDLVEAGIIDPTKVTRSALQNAASIAGLLLTTEAVVADKPE 524
|
|
| groEL |
PRK12850 |
chaperonin GroEL; Reviewed |
27-553 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237231 Cd Length: 544 Bit Score: 682.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 27 AKDVKFGADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDKYKNIGAKLVQDVANNTN 106
Cdd:PRK12850 3 AKEIRFSTDARDRLLRGVNILANAVKVTLGPKGRNVVLEKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVKEVASKTN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 107 EEAGDGTTTATVLARSIAKEGFEKISKGANPVEIRRGVMLAVDAVIAELKKQSKPVTTPEEIAQVATISANGDKEIGNII 186
Cdd:PRK12850 83 DLAGDGTTTATVLAQAIVREGAKLVAAGMNPMDLKRGIDLAVAAVVDELKKIAKKVTSSKEIAQVATISANGDESIGEMI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 187 SDAMKKVGRKGVITVKDGKTLNDELEIIEGMKFDRGYISPYFINTSKGQKCEFQDAYVLLSEKKISSIQSIVPALEIANA 266
Cdd:PRK12850 163 AEAMDKVGKEGVITVEEAKTLGTELDVVEGMQFDRGYLSPYFVTNPEKMRAELEDPYILLHEKKISNLQDLLPILEAVVQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 267 HRKPLVIIAEDVDGEALSTLVLNRLKVGLQVVAVKAPGFGDNRKNQLKDMAIATGGAVFGEEgLTLNLEDVQPHDLGKVG 346
Cdd:PRK12850 243 SGRPLLIIAEDVEGEALATLVVNKLRGGLKSVAVKAPGFGDRRKAMLEDIAVLTGGQVISED-LGIKLENVTLDMLGRAK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 347 EVIVTKDDAMLLKGKGDKAQIEKRIQEIIEQLDVTTSEYEKEKLNERLAKLSDGVAVLKVGGTSDVEVNEKKDRVTDALN 426
Cdd:PRK12850 322 RVLITKENTTIIDGAGDKKNIEARVKQIRAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKEKKDRVDDALH 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 427 ATRAAVEEGIVLGGGCALLRCIPALDSLTPANEDQKIGIEIIKRTLKIPAMTIAKNAGVEGSLIVEKIMQSSSEVGYDAM 506
Cdd:PRK12850 402 ATRAAVEEGIVPGGGVALLRARSALRGLKGANADETAGIDIVRRALEEPLRQIATNAGFEGSVVVGKVAELPGNFGFNAQ 481
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 41399285 507 AGDFVNMVEKGIIDPTKVVRTALLDAAGVASLLTTAEVVVTEIPKEE 553
Cdd:PRK12850 482 TGEYGDMVEAGIIDPAKVTRTALQDAASIAALLITTEAMVAEAPKKA 528
|
|
| groEL |
PRK12852 |
chaperonin GroEL; Reviewed |
27-556 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237232 Cd Length: 545 Bit Score: 647.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 27 AKDVKFGADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDKYKNIGAKLVQDVANNTN 106
Cdd:PRK12852 3 AKDVKFSGDARDRMLRGVDILANAVKVTLGPKGRNVVIEKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVREVASKTN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 107 EEAGDGTTTATVLARSIAKEGFEKISKGANPVEIRRGVMLAVDAVIAELKKQSKPVTTPEEIAQVATISANGDKEIGNII 186
Cdd:PRK12852 83 DLAGDGTTTATVLAQAIVREGAKAVAAGMNPMDLKRGIDIAVAAVVKDIEKRAKPVASSAEIAQVGTISANGDAAIGKMI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 187 SDAMKKVGRKGVITVKDGKTLNDELEIIEGMKFDRGYISPYFINTSKGQKCEFQDAYVLLSEKKISSIQSIVPALEIANA 266
Cdd:PRK12852 163 AQAMQKVGNEGVITVEENKSLETEVDIVEGMKFDRGYLSPYFVTNAEKMTVELDDAYILLHEKKLSGLQAMLPVLEAVVQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 267 HRKPLVIIAEDVDGEALSTLVLNRLKVGLQVVAVKAPGFGDNRKNQLKDMAIATGGAVFGEEgLTLNLEDVQPHDLGKVG 346
Cdd:PRK12852 243 SGKPLLIIAEDVEGEALATLVVNRLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGQLISED-LGIKLENVTLKMLGRAK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 347 EVIVTKDDAMLLKGKGDKAQIEKRIQEIIEQLDVTTSEYEKEKLNERLAKLSDGVAVLKVGGTSDVEVNEKKDRVTDALN 426
Cdd:PRK12852 322 KVVIDKENTTIVNGAGKKADIEARVGQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKEKKDRVEDALN 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 427 ATRAAVEEGIVLGGGCALLRCIPALDSLTPANEDQKIGIEIIKRTLKIPAMTIAKNAGVEGSLIVEKIMQSSSEV-GYDA 505
Cdd:PRK12852 402 ATRAAVQEGIVPGGGVALLRAKKAVGRINNDNADVQAGINIVLKALEAPIRQIAENAGVEGSIVVGKILENKSETfGFDA 481
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 41399285 506 MAGDFVNMVEKGIIDPTKVVRTALLDAAGVASLLTTAEVVVTEIPKEEKDP 556
Cdd:PRK12852 482 QTEEYVDMVAKGIIDPAKVVRTALQDAASVAGLLVTTEAMVAELPKKDAAP 532
|
|
| groEL |
PRK12851 |
chaperonin GroEL; Reviewed |
27-556 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 171770 Cd Length: 541 Bit Score: 634.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 27 AKDVKFGADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDKYKNIGAKLVQDVANNTN 106
Cdd:PRK12851 3 AKEVKFHVEAREKMLRGVNILADAVKVTLGPKGRNVVIDKSFGAPTITNDGVTIAKEIELEDKFENMGAQMVREVASKTN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 107 EEAGDGTTTATVLARSIAKEGFEKISKGANPVEIRRGVMLAVDAVIAELKKQSKPVTTPEEIAQVATISANGDKEIGNII 186
Cdd:PRK12851 83 DVAGDGTTTATVLAQAIVREGAKAVAAGANPMDLKRGIDRAVAAVVEELKANARPVTTNAEIAQVATISANGDAEIGRLV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 187 SDAMKKVGRKGVITVKDGKTLNDELEIIEGMKFDRGYISPYFINTSKGQKCEFQDAYVLLSEKKISSIQSIVPALEIANA 266
Cdd:PRK12851 163 AEAMEKVGNEGVITVEESKTAETELEVVEGMQFDRGYLSPYFVTDADKMEAELEDPYILIHEKKISNLQDLLPVLEAVVQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 267 HRKPLVIIAEDVDGEALSTLVLNRLKVGLQVVAVKAPGFGDNRKNQLKDMAIATGGAVFGEEgLTLNLEDVQPHDLGKVG 346
Cdd:PRK12851 243 SGKPLLIIAEDVEGEALATLVVNKLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGTVISED-LGIKLENVTLEQLGRAK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 347 EVIVTKDDAMLLKGKGDKAQIEKRIQEIIEQLDVTTSEYEKEKLNERLAKLSDGVAVLKVGGTSDVEVNEKKDRVTDALN 426
Cdd:PRK12851 322 KVVVEKENTTIIDGAGSKTEIEGRVAQIRAQIEETTSDYDREKLQERLAKLAGGVAVIRVGASTEVEVKEKKDRVDDALH 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 427 ATRAAVEEGIVLGGGCALLRCIPALDSLTPANEDQKIGIEIIKRTLKIPAMTIAKNAGVEGSLIVEKIMQSSSEVGYDAM 506
Cdd:PRK12851 402 ATRAAVEEGIVPGGGVALLRAVKALDKLETANGDQRTGVEIVRRALEAPVRQIAENAGAEGSVVVGKLREKPGGYGFNAA 481
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 41399285 507 AGDFVNMVEKGIIDPTKVVRTALLDAAGVASLLTTAEVVVTEIPKEEKDP 556
Cdd:PRK12851 482 TNEYGDLYAQGVIDPVKVVRTALQNAASVAGLLLTTEAMVAEKPKKEPAP 531
|
|
| GroEL |
COG0459 |
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ... |
27-556 |
0e+00 |
|
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227 Cd Length: 497 Bit Score: 627.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 27 AKDVKFGADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDKYKNIGAKLVQDVANNTN 106
Cdd:COG0459 2 AKQILFGEDARRANIRGVKALADAVKVTLGPKGRNVMLVKSFGDPTITNDGVTIAKEIELEDPFENMGAQLVKEVASKTN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 107 EEAGDGTTTATVLARSIAKEGFEKISKGANPVEIRRGVMLAVDAVIAELKKQSKPVTTPEEIAQVATISANGDKEIGNII 186
Cdd:COG0459 82 DEAGDGTTTATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPVDDKEELAQVATISANGDEEIGELI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 187 SDAMKKVGRKGVITVKDGKTLNDELEIIEGMKFDRGYISPYFINTSKGQKCEFQDAYVLLSEKKISSIQSIVPALEIANA 266
Cdd:COG0459 162 AEAMEKVGKDGVITVEEGKGLETELEVVEGMQFDKGYLSPYFVTDPEKMPAELENAYILLTDKKISSIQDLLPLLEKVAQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 267 HRKPLVIIAEDVDGEALSTLVLNRLKVGLQVVAVKAPGFGDNRKNQLKDMAIATGGAVFGEEgLTLNLEDVQPHDLGKVG 346
Cdd:COG0459 242 SGKPLLIIAEDIDGEALATLVVNGIRGVLRVVAVKAPGFGDRRKAMLEDIAILTGGRVISED-LGLKLEDVTLDDLGRAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 347 EVIVTKDDAMLLKGKGDKAQIekriqeiieqldvttseyekeklnerlaklsdgvaVLKVGGTSDVEVNEKKDRVTDALN 426
Cdd:COG0459 321 RVEVDKDNTTIVEGAGNPKAI-----------------------------------VILVGAATEVEVKERKRRVEDALH 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 427 ATRAAVEEGIVLGGGCALLRCIPALDSLTPANE-DQKIGIEIIKRTLKIPAMTIAKNAGVEGSLIVEKIMQSSSE-VGYD 504
Cdd:COG0459 366 ATRAAVEEGIVPGGGAALLRAARALRELAAKLEgDEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKVRAAKDKgFGFD 445
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 41399285 505 AMAGDFVNMVEKGIIDPTKVVRTALLDAAGVASLLTTAEVVVTEIPKEEKDP 556
Cdd:COG0459 446 AATGEYVDMLEAGVIDPAKVKRSALQNAASVAGLILTTEAVIADKPEKEEAA 497
|
|
| PRK14104 |
PRK14104 |
chaperonin GroEL; Provisional |
27-552 |
0e+00 |
|
chaperonin GroEL; Provisional
Pssm-ID: 172594 Cd Length: 546 Bit Score: 583.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 27 AKDVKFGADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDKYKNIGAKLVQDVANNTN 106
Cdd:PRK14104 3 AKEVKFGVDARDRMLRGVDILANAVKVTLGPKGRNVVLDKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVREVASKSA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 107 EEAGDGTTTATVLARSIAKEGFEKISKGANPVEIRRGVMLAVDAVIAELKKQSKPVTTPEEIAQVATISANGDKEIGNII 186
Cdd:PRK14104 83 DAAGDGTTTATVLAQAIVREGAKSVAAGMNPMDLKRGIDLAVEAVVADLVKNSKKVTSNDEIAQVGTISANGDAEIGKFL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 187 SDAMKKVGRKGVITVKDGKTLNDELEIIEGMKFDRGYISPYFINTSKGQKCEFQDAYVLLSEKKISSIQSIVPALEIANA 266
Cdd:PRK14104 163 ADAMKKVGNEGVITVEEAKSLETELDVVEGMQFDRGYISPYFVTNADKMRVEMDDAYILINEKKLSSLNELLPLLEAVVQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 267 HRKPLVIIAEDVDGEALSTLVLNRLKVGLQVVAVKAPGFGDNRKNQLKDMAIATGGAVFGEEgLTLNLEDVQPHDLGKVG 346
Cdd:PRK14104 243 TGKPLVIVAEDVEGEALATLVVNRLRGGLKVAAVKAPGFGDRRKAMLQDIAILTGGQAISED-LGIKLENVTLQMLGRAK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 347 EVIVTKDDAMLLKGKGDKAQIEKRIQEIIEQLDVTTSEYEKEKLNERLAKLSDGVAVLKVGGTSDVEVNEKKDRVTDALN 426
Cdd:PRK14104 322 KVMIDKENTTIVNGAGKKADIEARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKERKDRVDDAMH 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 427 ATRAAVEEGIVLGGGCALLRCIPALDSLTPANEDQKIGIEIIKRTLKIPAMTIAKNAGVEGSLIVEKIMQSSS-EVGYDA 505
Cdd:PRK14104 402 ATRAAVEEGIVPGGGVALLRASEQLKGIKTKNDDQKTGVEIVRKALSAPARQIAINAGEDGSVIVGKILEKEQySYGFDS 481
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 41399285 506 MAGDFVNMVEKGIIDPTKVVRTALLDAAGVASLLTTAEVVVTEIPKE 552
Cdd:PRK14104 482 QTGEYGNLVSKGIIDPTKVVRTAIQNAASVAALLITTEAMVAELPKK 528
|
|
| groEL |
CHL00093 |
chaperonin GroEL |
27-553 |
0e+00 |
|
chaperonin GroEL
Pssm-ID: 177025 Cd Length: 529 Bit Score: 537.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 27 AKDVKFGADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDKYKNIGAKLVQDVANNTN 106
Cdd:CHL00093 2 SKKILYQDNARRALERGMDILAEAVSVTLGPKGRNVVLEKKYGSPQIVNDGVTIAKEIELEDHIENTGVALIRQAASKTN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 107 EEAGDGTTTATVLARSIAKEGFEKISKGANPVEIRRGVMLAVDAVIAELKKQSKPVTTPEEIAQVATISANGDKEIGNII 186
Cdd:CHL00093 82 DVAGDGTTTATVLAYAIVKQGMKNVAAGANPISLKRGIEKATQYVVSQIAEYARPVEDIQAITQVASISAGNDEEVGSMI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 187 SDAMKKVGRKGVITVKDGKTLNDELEIIEGMKFDRGYISPYFINTSKGQKCEFQDAYVLLSEKKISSI-QSIVPALEIAN 265
Cdd:CHL00093 162 ADAIEKVGREGVISLEEGKSTVTELEITEGMRFEKGFISPYFVTDTERMEVVQENPYILLTDKKITLVqQDLLPILEQVT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 266 AHRKPLVIIAEDVDGEALSTLVLNRLKVGLQVVAVKAPGFGDNRKNQLKDMAIATGGAVFGEEgLTLNLEDVQPHDLGKV 345
Cdd:CHL00093 242 KTKRPLLIIAEDVEKEALATLVLNKLRGIVNVVAVRAPGFGDRRKAMLEDIAILTGGQVITED-AGLSLETIQLDLLGQA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 346 GEVIVTKDDAMLLkGKGDKAQIEKRIQEIIEQLDVTTSEYEKEKLNERLAKLSDGVAVLKVGGTSDVEVNEKKDRVTDAL 425
Cdd:CHL00093 321 RRIIVTKDSTTII-ADGNEEQVKARCEQLRKQIEIADSSYEKEKLQERLAKLSGGVAVIKVGAATETEMKDKKLRLEDAI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 426 NATRAAVEEGIVLGGGCALLRCIPALDSLTPAN--EDQKIGIEIIKRTLKIPAMTIAKNAGVEGSLIVEKIMQSSSEVGY 503
Cdd:CHL00093 400 NATKAAVEEGIVPGGGATLVHLSENLKTWAKNNlkEDELIGALIVARAILAPLKRIAENAGKNGSVIIEKVQEQDFEIGY 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 41399285 504 DAMAGDFVNMVEKGIIDPTKVVRTALLDAAGVASLLTTAEVVVTEIPKEE 553
Cdd:CHL00093 480 NAANNKFVNMYEAGIIDPAKVTRSALQNAASIASMILTTECIIVDKKESS 529
|
|
| PLN03167 |
PLN03167 |
Chaperonin-60 beta subunit; Provisional |
27-556 |
1.05e-168 |
|
Chaperonin-60 beta subunit; Provisional
Pssm-ID: 215611 [Multi-domain] Cd Length: 600 Bit Score: 492.13 E-value: 1.05e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 27 AKDVKFGADARAL--MLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDKYKNIGAKLVQDVANN 104
Cdd:PLN03167 56 AKELHFNKDGSAIkkLQAGVNKLADLVGVTLGPKGRNVVLESKYGSPKIVNDGVTVAKEVELEDPVENIGAKLVRQAAAK 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 105 TNEEAGDGTTTATVLARSIAKEGFEKISKGANPVEIRRGVMLAVDAVIAELKKQSKPVTTpEEIAQVATISANGDKEIGN 184
Cdd:PLN03167 136 TNDLAGDGTTTSVVLAQGLIAEGVKVVAAGANPVQITRGIEKTAKALVKELKKMSKEVED-SELADVAAVSAGNNYEVGN 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 185 IISDAMKKVGRKGVITVKDGKTLNDELEIIEGMKFDRGYISPYFINTSKGQKCEFQDAYVLLSEKKISSIQSIVPALEIA 264
Cdd:PLN03167 215 MIAEAMSKVGRKGVVTLEEGKSAENNLYVVEGMQFDRGYISPYFVTDSEKMSVEYDNCKLLLVDKKITNARDLIGILEDA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 265 NAHRKPLVIIAEDVDGEALSTLVLNRLKVGLQVVAVKAPGFGDNRKNQLKDMAIATGGAVFGEEgLTLNLEDVQPHDLGK 344
Cdd:PLN03167 295 IRGGYPLLIIAEDIEQEALATLVVNKLRGSLKIAALKAPGFGERKSQYLDDIAILTGGTVIREE-VGLSLDKVGKEVLGT 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 345 VGEVIVTKDDAMLLKGKGDKAQIEKRIQEIIEQLDVTTSEYEKEKLNERLAKLSDGVAVLKVGGTSDVEVNEKKDRVTDA 424
Cdd:PLN03167 374 AAKVVLTKDTTTIVGDGSTQEAVNKRVAQIKNLIEAAEQDYEKEKLNERIAKLSGGVAVIQVGAQTETELKEKKLRVEDA 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 425 LNATRAAVEEGIVLGGGCALLRCIPALDSL--TPANEDQKIGIEIIKRTLKIPAMTIAKNAGVEGSLIVEKIMQSSS-EV 501
Cdd:PLN03167 454 LNATKAAVEEGIVVGGGCTLLRLASKVDAIkdTLENDEQKVGADIVKRALSYPLKLIAKNAGVNGSVVSEKVLSNDNpKF 533
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 41399285 502 GYDAMAGDFVNMVEKGIIDPTKVVRTALLDAAGVASLLTTAEVVVTEIPKEEKDP 556
Cdd:PLN03167 534 GYNAATGKYEDLMAAGIIDPTKVVRCCLEHAASVAKTFLTSDCVVVEIKEPEPVP 588
|
|
| chaperonin_type_I_II |
cd00309 |
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ... |
28-547 |
1.29e-146 |
|
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: 430.70 E-value: 1.29e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 28 KDVKFGADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKdkykNIGAKLVQDVANNTNE 107
Cdd:cd00309 1 KEREFGEEARLSNINAAKALADAVKTTLGPKGMDKMLVDSLGDPTITNDGATILKEIEVE----HPAAKLLVEVAKSQDD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 108 EAGDGTTTATVLARSIAKEGFEKISKGANPVEIRRGVMLAVDAVIAELKKQSKP--VTTPEEIAQVATISAN------GD 179
Cdd:cd00309 77 EVGDGTTTVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVPidVEDREELLKVATTSLNsklvsgGD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 180 KEIGNIISDAMKKVGR------KGVITVKDGKTLN-DELEIIEGMKFDRGYISPYFintskgqKCEFQDAYVLLSEKKIS 252
Cdd:cd00309 157 DFLGELVVDAVLKVGKengdvdLGVIRVEKKKGGSlEDSELVVGMVFDKGYLSPYM-------PKRLENAKILLLDCKLE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 253 SiqsivpaleianahrkplVIIAED-VDGEALSTLVLnrlkvgLQVVAVKApgfgdNRKNQLKDMAIATGGAVFGEeglt 331
Cdd:cd00309 230 Y------------------VVIAEKgIDDEALHYLAK------LGIMAVRR-----VRKEDLERIAKATGATIVSR---- 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 332 lnLEDVQPHDLGKVGEVIVTKddamllkgkgdkaqiekriqeiIEQLDVTTSEYEKEKlnerlaklsdGVAVLKVGGTSD 411
Cdd:cd00309 277 --LEDLTPEDLGTAGLVEETK----------------------IGDEKYTFIEGCKGG----------KVATILLRGATE 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 412 VEVNEKKDRVTDALNATRAAVEE-GIVLGGGCALLRCIPALDSLTP-ANEDQKIGIEIIKRTLKIPAMTIAKNAGVEGSL 489
Cdd:cd00309 323 VELDEAERSLHDALCAVRAAVEDgGIVPGGGAAEIELSKALEELAKtLPGKEQLGIEAFADALEVIPRTLAENAGLDPIE 402
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41399285 490 IVEKIMQSSSEVGYDA----MAGDFVNMVEKGIIDPTKVVRTALLDAAGVASLLTTAEVVVT 547
Cdd:cd00309 403 VVTKLRAKHAEGGGNAggdvETGEIVDMKEAGIIDPLKVKRQALKSATEAASLILTIDDIIV 464
|
|
| Cpn60_TCP1 |
pfam00118 |
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ... |
47-547 |
1.71e-68 |
|
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: 229.40 E-value: 1.71e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 47 LADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDKYknigAKLVQDVANNTNEEAGDGTTTATVLARSIAKE 126
Cdd:pfam00118 1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELEIQHPA----AKLLVEAAKAQDEEVGDGTTTVVVLAGELLEE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 127 GFEKISKGANPVEIRRGVMLAVDAVIAELK-KQSKPVTTP--EEIAQVATISANGD------KEIGNIISDAMK------ 191
Cdd:pfam00118 77 AEKLLAAGVHPTTIIEGYEKALEKALEILDsIISIPVEDVdrEDLLKVARTSLSSKiisresDFLAKLVVDAVLaipknd 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 192 ---KVGRKGVITVKDGKTlnDELEIIEGMKFDRGYISPyfintskGQKCEFQDAYVLLSEKKISSIQSIVPA-------- 260
Cdd:pfam00118 157 gsfDLGNIGVVKILGGSL--EDSELVDGVVLDKGPLHP-------DMPKRLENAKVLLLNCSLEYEKTETKAtvvlsdae 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 261 --LEIANAHRK--------------PLVIIAEDVDGEALSTLVLNRLkVGLQVVavkapgfgdnRKNQLKDMAIATGGAV 324
Cdd:pfam00118 228 qlERFLKAEEEqileivekiidsgvNVVVCQKGIDDLALHFLAKNGI-MALRRV----------KKRDLERLAKATGARA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 325 FGeegltlNLEDVQPHDLGKVG---EVIVTKDDAMLLKGKGDKaqiekriqeiieqldvttseyekeklnerlaklsdGV 401
Cdd:pfam00118 297 VS------SLDDLTPDDLGTAGkveEEKIGDEKYTFIEGCKSP-----------------------------------KA 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 402 AVLKVGGTSDVEVNEKKDRVTDALNATRAAVEE-GIVLGGGCALLRCIPALDSLTPA-NEDQKIGIEIIKRTLKIPAMTI 479
Cdd:pfam00118 336 ATILLRGATDHVLDEIERSIHDALCVVKNAIEDpRVVPGGGAVEMELARALREYAKSvSGKEQLAIEAFAEALEVIPKTL 415
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41399285 480 AKNAGVEGSLIVEKIM----QSSSEVGYDAMAGDFVNMVEKGIIDPTKVVRTALLDAAGVAS-LLTTAEVVVT 547
Cdd:pfam00118 416 AENAGLDPIEVLAELRaahaSGEKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKSATEAAStILRIDDIIKA 488
|
|
| chaperonin_like |
cd03333 |
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ... |
166-434 |
7.36e-37 |
|
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: 136.06 E-value: 7.36e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 166 EEIAQVATISAN-----GDKEIGNIISDAMKKVGR------KGVITVKDGKTLN-DELEIIEGMKFDRGYISPYFintsk 233
Cdd:cd03333 2 ELLLQVATTSLNsklssWDDFLGKLVVDAVLKVGPdnrmddLGVIKVEKIPGGSlEDSELVVGVVFDKGYASPYM----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 234 gqKCEFQDAYVLLSEKKISSiqsivpaleianahrkplVIIAED-VDGEALSTLVLnrlkvgLQVVAVKApgfgdNRKNQ 312
Cdd:cd03333 77 --PKRLENAKILLLDCPLEY------------------VVIAEKgIDDLALHYLAK------AGIMAVRR-----VKKED 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 313 LKDMAIATGGAVFGEegltlnLEDVQPHDLGKVGEVIVTKDdamllkgkGDKAQIekriqeIIEQLDVTtseyekeklne 392
Cdd:cd03333 126 LERIARATGATIVSS------LEDLTPEDLGTAELVEETKI--------GEEKLT------FIEGCKGG----------- 174
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 41399285 393 rlaklsdGVAVLKVGGTSDVEVNEKKDRVTDALNATRAAVEE 434
Cdd:cd03333 175 -------KAATILLRGATEVELDEVKRSLHDALCAVRAAVEE 209
|
|
| cpn60 |
cd03343 |
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ... |
33-539 |
1.23e-21 |
|
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. Archaeal cpn60 (thermosome), together with TF55 from thermophilic bacteria and the eukaryotic cytosol chaperonin (CTT), belong to the type II group of chaperonins. Cpn60 consists of two stacked octameric rings, which are composed of one or two different subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis.
Pssm-ID: 239459 [Multi-domain] Cd Length: 517 Bit Score: 98.49 E-value: 1.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 33 GADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKdkykNIGAKLVQDVANNTNEEAGDG 112
Cdd:cd03343 13 GRDAQRMNIAAAKAVAEAVRTTLGPKGMDKMLVDSLGDVTITNDGATILKEMDIE----HPAAKMLVEVAKTQDEEVGDG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 113 TTTATVLARSIAKEGFEKISKGANPVEIRRGVMLAVDAVIAELKKQSKPVTTPEE-----IAQVATISANGDKE---IGN 184
Cdd:cd03343 89 TTTAVVLAGELLEKAEDLLDQNIHPTVIIEGYRLAAEKALELLDEIAIKVDPDDKdtlrkIAKTSLTGKGAEAAkdkLAD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 185 IISDAMKKV--GRKGVITV---------KDGKTLNDElEIIEGMKFDRGYISPyfintskGQKCEFQDAyvllsekKISS 253
Cdd:cd03343 169 LVVDAVLQVaeKRDGKYVVdldnikiekKTGGSVDDT-ELIRGIVIDKEVVHP-------GMPKRVENA-------KIAL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 254 IQSivpALEIanahRKPlviiaeDVDGEalstlvlnrlkvgLQVVAV-KAPGFGDNRKNQLKDM--AIATGGA--VFGEE 328
Cdd:cd03343 234 LDA---PLEV----KKT------EIDAK-------------IRITSPdQLQAFLEQEEAMLKEMvdKIADTGAnvVFCQK 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 329 GltlnLEDVQPHDLGKVGEVIV--TKDDAMLLKGKGDKAQIEKRIQEIIEQLDVTTSEYEKEKLNE------RLAKLSDG 400
Cdd:cd03343 288 G----IDDLAQHYLAKAGILAVrrVKKSDMEKLARATGAKIVTNIDDLTPEDLGEAELVEERKVGDdkmvfvEGCKNPKA 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 401 VAVLKVGGTSDVeVNEKKDRVTDALNATRAAVEEG-IVLGGGCALLRCIPALDSLTPANE-DQKIGIEIIKRTLKIPAMT 478
Cdd:cd03343 364 VTILLRGGTEHV-VDELERALEDALRVVADALEDGkVVAGGGAVEIELAKRLREYARSVGgREQLAVEAFADALEEIPRT 442
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41399285 479 IAKNAGVEGsliVEKIMQSSSE-------VGYDAMAGDFVNMVEKGIIDPTKVVRTALLDAAGVASLL 539
Cdd:cd03343 443 LAENAGLDP---IDTLVELRAAhekgnknAGLDVYTGEVVDMLEKGVIEPLRVKKQAIKSATEAATMI 507
|
|
| TCP1_beta |
cd03336 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ... |
33-539 |
4.61e-14 |
|
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.
Pssm-ID: 239452 [Multi-domain] Cd Length: 517 Bit Score: 74.67 E-value: 4.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 33 GADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSW--GSPKVTKDGVTVAKSIDLKdkykNIGAKLVQDVANNTNEEAG 110
Cdd:cd03336 11 GETARLSSFVGAIAIGDLVKTTLGPKGMDKILQSVGrsGGVTVTNDGATILKSIGVD----NPAAKVLVDISKVQDDEVG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 111 DGTTTATVLARSIAKEGFEKISKGANPVEIRRGVMLAVDAVIAELKK-----QSKPVTTPEEIAQVA--TISA---NGDK 180
Cdd:cd03336 87 DGTTSVTVLAAELLREAEKLVAQKIHPQTIIEGYRMATAAAREALLSsavdhSSDEEAFREDLLNIArtTLSSkilTQDK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 181 E-IGNIISDAMKKVGRKG-----VITVKDGKTLNDELeiiegmkFDRGYISPYFINTskGQKCEFQDAYVLLS-----EK 249
Cdd:cd03336 167 EhFAELAVDAVLRLKGSGnldaiQIIKKLGGSLKDSY-------LDEGFLLDKKIGV--NQPKRIENAKILIAntpmdTD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 250 KIS------SIQSIVPALEIANAHRKPLV-----IIAEDVDGEALSTLVLNrlkVGLQVvavkapgFGDNRKnqlkdMAI 318
Cdd:cd03336 238 KIKifgakvRVDSTAKVAEIEEAEKEKMKnkvekILKHGINCFINRQLIYN---YPEQL-------FADAGI-----MAI 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 319 ATggAVF-GEEGLTLNLEdvqphdlgkvGEVIVTKDDAMLLK-GKGDKaqiekrIQEIIEQldvttseyekeklNERLAK 396
Cdd:cd03336 303 EH--ADFdGVERLALVTG----------GEIASTFDHPELVKlGTCKL------IEEIMIG-------------EDKLIR 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 397 LSdGVA-------VLKvgGTSDVEVNEKKDRVTDALNATRAAVEEG-IVLGGGCALLRCIPALDSLTPANEDQK-IGIEI 467
Cdd:cd03336 352 FS-GVAageactiVLR--GASQQILDEAERSLHDALCVLAQTVKDTrVVLGGGCSEMLMAKAVEELAKKTPGKKsLAIEA 428
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41399285 468 IKRTLKIPAMTIAKNAGVEGSLIVEKI----MQSSSEVGYDAMAGDFVNMVEKGIIDPTKVVRTALLDAAGVASLL 539
Cdd:cd03336 429 FAKALRQLPTIIADNAGYDSAELVAQLraahYNGNTTAGLDMRKGTVGDMKELGITESFKVKRQVLLSASEAAEMI 504
|
|
| chap_CCT_beta |
TIGR02341 |
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ... |
33-551 |
7.52e-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: 71.04 E-value: 7.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 33 GADARALMLQGVDLLADAVAVTMGPKGRTVIIEQ--SWGSPKVTKDGVTVAKSIDLKdkykNIGAKLVQDVANNTNEEAG 110
Cdd:TIGR02341 12 AENARLSSFVGAIAIGDLVKSTLGPKGMDKILQSssSDASIMVTNDGATILKSIGVD----NPAAKVLVDMSKVQDDEVG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 111 DGTTTATVLARSIAKEGFEKISKGANPVEIRRGVMLAVDAVIAELKKQS-----KPVTTPEEIAQVA--TISAngdkEIG 183
Cdd:TIGR02341 88 DGTTSVTVLAAELLREAEKLINQKIHPQTIIAGYREATKAARDALLKSAvdngsDEVKFRQDLMNIArtTLSS----KIL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 184 NIISDAMKKVGRKGVITVKdGKTLNDELEIIE--GMKFDRGYISPYFINTSK---GQKCEFQDAYVLLSEKKISS----- 253
Cdd:TIGR02341 164 SQHKDHFAQLAVDAVLRLK-GSGNLEAIQIIKklGGSLADSYLDEGFLLDKKigvNQPKRIENAKILIANTGMDTdkvki 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 254 ------IQSIVPALEIANAHRKPLVIIAEDVDGEALSTLVLNRLkvglqVVAVKAPGFGDnrknqLKDMAIATGgavfge 327
Cdd:TIGR02341 243 fgsrvrVDSTAKVAELEHAEKEKMKEKVEKILKHGINCFINRQL-----IYNYPEQLFAD-----AGVMAIEHA------ 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 328 egltlNLEDVQPHDLGKVGEVIVTKDDAMLLK-GKGDKaqiekrIQEIIEQldvttseyEKEKLNERLAKLSDGVAVLKV 406
Cdd:TIGR02341 307 -----DFEGVERLALVTGGEIVSTFDHPELVKlGSCDL------IEEIMIG--------EDKLLKFSGVKLGEACTIVLR 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 407 GGTSDVeVNEKKDRVTDALNATRAAVEEG-IVLGGGCALLRCIPALDSLTpANEDQK--IGIEIIKRTLKIPAMTIAKNA 483
Cdd:TIGR02341 368 GATQQI-LDEAERSLHDALCVLSQTVKESrTVLGGGCSEMLMSKAVTQEA-QRTPGKeaLAVEAFARALRQLPTIIADNA 445
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41399285 484 GVEGSLIVEKIMQSSSE----VGYDAMAGDFVNMVEKGIIDPTKVVRTALLDAAGVASLLTTAEVVVTEIPK 551
Cdd:TIGR02341 446 GFDSAELVAQLRAAHYNgnttMGLDMNEGTIADMRQLGITESYKVKRAVVSSAAEAAEVILRVDNIIKAAPR 517
|
|
| chap_CCT_epsi |
TIGR02343 |
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ... |
33-521 |
1.55e-12 |
|
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: 70.22 E-value: 1.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 33 GADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDKYknigAKLVQDVANNTNEEAGDG 112
Cdd:TIGR02343 25 GLEAKKSNIAAAKSVASILRTSLGPKGMDKMLISPDGDITVTNDGATILSQMDVDNQI----AKLMVELSKSQDDEIGDG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 113 TTTATVLARSIAKEGFEKISKGANPVEIRRGVMLAVDAVIAELKKQSKPVTTPEEIAQV---ATISANGDKeIGNIISDA 189
Cdd:TIGR02343 101 TTGVVVLAGALLEQAEELLDKGIHPIKIADGFEEAARIAVEHLEEISDEISADNNNREPliqAAKTSLGSK-IVSKCHRR 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 190 MKKVGRKGVITVKD-----------------GKTLNDElEIIEGMKFDRGYISPYFINTSKGQK-----CEFQ------- 240
Cdd:TIGR02343 180 FAEIAVDAVLNVADmerrdvdfdlikvegkvGGSLEDT-KLIKGIIIDKDFSHPQMPKEVEDAKiailtCPFEppkpktk 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 241 --------DAYVLLSEKKISSIQSIVPALEIANAHrkpLVIIAEDVDGEALSTLVLNRLKvglqvvAVKAPGfgdnrKNQ 312
Cdd:TIGR02343 259 hkldissvEEYKKLQKYEQQKFKEMIDDIKKSGAN---LVICQWGFDDEANHLLLQNDLP------AVRWVG-----GQE 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 313 LKDMAIATGGAVFGEegltlnLEDVQPHDLGKVGEV----IVTKDDAMLlkgkgdkaqiekriqeIIEQldvttseyeke 388
Cdd:TIGR02343 325 LELIAIATGGRIVPR------FQELSKDKLGKAGLVreisFGTTKDRML----------------VIEQ----------- 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 389 klnerlAKLSDGVAVLkVGGTSDVEVNEKKDRVTDALNATRAAVEEG-IVLGGGCALLRCIPALDsltpANEDQKIGIE- 466
Cdd:TIGR02343 372 ------CKNSKAVTIF-IRGGNKMIIEEAKRSIHDALCVVRNLIKDSrIVYGGGAAEISCSLAVS----QEADKYPGVEq 440
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41399285 467 ----IIKRTLKIPAMTIAKNAGVE-----GSLIVEKIMQSSSEVGYDAMAGDFVNMVEKGIIDP 521
Cdd:TIGR02343 441 yairAFADALETIPMALAENSGLDpigtlSTLKSLQLKEKNPNLGVDCLGYGTNDMKEQFVFET 504
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
33-539 |
6.39e-12 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 68.13 E-value: 6.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 33 GADARALMLQGVDLLADAVAVTMGPKGRTVIIE-----QSWGSPKVTKDGVTVAKSIDLKdkykNIGAKLVQDVANNTNE 107
Cdd:PTZ00212 20 GETARLQSFVGAIAVADLVKTTLGPKGMDKILQpmsegPRSGNVTVTNDGATILKSVWLD----NPAAKILVDISKTQDE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 108 EAGDGTTTATVLARSIAKEGFEKISKGANPVEIRRGVMLAVDAVIAELKKQSKPVTTPEE--------IAQvATISA--- 176
Cdd:PTZ00212 96 EVGDGTTSVVVLAGELLREAEKLLDQKIHPQTIIEGWRMALDVARKALEEIAFDHGSDEEkfkedllnIAR-TTLSSkll 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 177 NGDKE-IGNIISDAMKKVGRKG-----VITVKDGKTLNDEleiiegmkfdrgYISPYFINTSK---GQKCEFQDAYVLLS 247
Cdd:PTZ00212 175 TVEKDhFAKLAVDAVLRLKGSGnldyiQIIKKPGGTLRDS------------YLEDGFILEKKigvGQPKRLENCKILVA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 248 EK-----KIS------SIQSIVPALEIANAHRKPLV-----IIAEDVdgealsTLVLNRlkvglQVVAvkapgfgdNRKN 311
Cdd:PTZ00212 243 NTpmdtdKIKiygakvKVDSMEKVAEIEAAEKEKMKnkvdkILAHGC------NVFINR-----QLIY--------NYPE 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 312 QL-KD---MAIATggAVF-GEEGLTLNLEdvqphdlgkvGEVIVTKDDAmllkgkgDKAQIE--KRIQEIIeqldvttse 384
Cdd:PTZ00212 304 QLfAEagiMAIEH--ADFdGMERLAAALG----------AEIVSTFDTP-------EKVKLGhcDLIEEIM--------- 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 385 YEKEKLnERLAKLSDGVA---VLKvgGTSDVEVNEKKDRVTDALNATRAAVEEG-IVLGGGCALLRCIPALDSLTPANED 460
Cdd:PTZ00212 356 IGEDKL-IRFSGCAKGEActiVLR--GASTHILDEAERSLHDALCVLSQTVKDTrVVLGGGCSEMLMANAVEELAKKVEG 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 461 QK-IGIEIIKRTLKIPAMTIAKNAGVEGSLIVEKI----MQSSSEVGYDAMAGDFVNMVEKGIIDPTKVVRTALLDAAGV 535
Cdd:PTZ00212 433 KKsLAIEAFAKALRQIPTIIADNGGYDSAELVSKLraehYKGNKTAGIDMEKGTVGDMKELGITESYKVKLSQLCSATEA 512
|
....
gi 41399285 536 ASLL 539
Cdd:PTZ00212 513 AEMI 516
|
|
| chap_CCT_eta |
TIGR02345 |
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ... |
47-167 |
1.70e-11 |
|
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT eta chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.
Pssm-ID: 274086 [Multi-domain] Cd Length: 523 Bit Score: 66.71 E-value: 1.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 47 LADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDKykniGAKLVQDVANNTNEEAGDGTTTATVLARSIAKE 126
Cdd:TIGR02345 30 IAEALKTTLGPRGMDKLIVGSNGKATISNDGATILKLLDIVHP----AAKTLVDIAKSQDAEVGDGTTSVTILAGELLKE 105
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 41399285 127 GFEKISKGANPVEIRRGVMLAVDAVIAELKKQSkpVTTPEE 167
Cdd:TIGR02345 106 AKPFIEEGVHPQLIIRCYREALSLAVEKIKEIA--VTIDEE 144
|
|
| TCP1_epsilon |
cd03339 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ... |
41-529 |
8.98e-11 |
|
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.
Pssm-ID: 239455 Cd Length: 526 Bit Score: 64.24 E-value: 8.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 41 LQGVD------LLADAVAVTM----GPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKdkykNIGAKLVQDVANNTNEEAG 110
Cdd:cd03339 19 LKGLEahkshiLAAKSVANILrtslGPRGMDKILVSPDGEVTVTNDGATILEKMDVD----HQIAKLLVELSKSQDDEIG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 111 DGTTTATVLARSIAKEGFEKISKGANPVEIRRGVMLAVDAVIAELKKQSKPVTTPEE----IAQVATISAnGDKeIGNII 186
Cdd:cd03339 95 DGTTGVVVLAGALLEQAEKLLDRGIHPIRIADGYEQACKIAVEHLEEIADKIEFSPDnkepLIQTAMTSL-GSK-IVSRC 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 187 SDAMKKVGRKGVITVKD--GKTLNDEL--------------EIIEGMKFDRGYISPYFINTSKGQK-----CEFQ----- 240
Cdd:cd03339 173 HRQFAEIAVDAVLSVADleRKDVNFELikvegkvggrledtKLVKGIVIDKDFSHPQMPKEVKDAKiailtCPFEppkpk 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 241 ----------DAYVLLSEKKISSIQSIVPALEIANAHrkpLVIIAEDVDGEALSTLVLNRLKVglqVVAVKAPgfgdnrk 310
Cdd:cd03339 253 tkhklditsvEDYKKLQEYEQKYFREMVEQVKDAGAN---LVICQWGFDDEANHLLLQNGLPA---VRWVGGV------- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 311 nQLKDMAIATGGAVFGEegltlnLEDVQPHDLGKVGEV----IVTKDDAMLlkgkgdkaqiekriqeIIEQLdvttseye 386
Cdd:cd03339 320 -EIELIAIATGGRIVPR------FEDLSPEKLGKAGLVreisFGTTKDKML----------------VIEGC-------- 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 387 keklnerlaKLSDGVAVLkVGGTSDVEVNEKKDRVTDALNATRAAVEEG-IVLGGGCALLRCipaldSLTPANEDQKIG- 464
Cdd:cd03339 369 ---------PNSKAVTIF-IRGGNKMIIEEAKRSLHDALCVVRNLIRDNrIVYGGGAAEISC-----SLAVEKAADKCSg 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 465 -----IEIIKRTLKIPAMTIAKNAGVE--GSLIVEKIMQ---SSSEVGYDAMAGDFVNMVEKGIIDP-----------TK 523
Cdd:cd03339 434 ieqyaMRAFADALESIPLALAENSGLNpiETLSEVKARQvkeKNPHLGIDCLGRGTNDMKEQKVFETliskkqqillaTQ 513
|
....*.
gi 41399285 524 VVRTAL 529
Cdd:cd03339 514 VVKMIL 519
|
|
| TCP1_eta |
cd03340 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ... |
48-157 |
2.39e-10 |
|
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.
Pssm-ID: 239456 [Multi-domain] Cd Length: 522 Bit Score: 63.08 E-value: 2.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 48 ADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDKykniGAKLVQDVANNTNEEAGDGTTTATVLARSIAKEG 127
Cdd:cd03340 29 ADAVRTTLGPRGMDKLIVDGRGKVTISNDGATILKLLDIVHP----AAKTLVDIAKSQDAEVGDGTTSVVVLAGEFLKEA 104
|
90 100 110
....*....|....*....|....*....|
gi 41399285 128 FEKISKGANPVEIRRGVMLAVDAVIAELKK 157
Cdd:cd03340 105 KPFIEDGVHPQIIIRGYRKALQLAIEKIKE 134
|
|
| TCP1_delta |
cd03338 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ... |
47-240 |
3.85e-10 |
|
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.
Pssm-ID: 239454 [Multi-domain] Cd Length: 515 Bit Score: 62.30 E-value: 3.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 47 LADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDKykniGAKLVQDVANNTNEEAGDGTTTATVLARSIAKE 126
Cdd:cd03338 20 VADAIRTSLGPRGMDKMIQTGKGEVIITNDGATILKQMSVLHP----AAKMLVELSKAQDIEAGDGTTSVVVLAGALLSA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 127 GFEKISKGANPVEIRRGVMLAVDAVIAELKKQSKPV--TTPEEIAQVATISANG------DKEIGNIISDAMKKVGRKGV 198
Cdd:cd03338 96 CESLLKKGIHPTVISESFQIAAKKAVEILDSMSIPVdlNDRESLIKSATTSLNSkvvsqySSLLAPIAVDAVLKVIDPAT 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 41399285 199 ----------ITVKDGKTLNDElEIIEGM----KFDRGYISPYFINTSKGQKCEFQ 240
Cdd:cd03338 176 atnvdlkdirIVKKLGGTIEDT-ELVDGLvftqKASKKAGGPTRIEKAKIGLIQFC 230
|
|
| chap_CCT_gamma |
TIGR02344 |
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ... |
41-552 |
1.12e-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: 57.83 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 41 LQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDKykniGAKLVQDVANNTNEEAGDGTTTATVLA 120
Cdd:TIGR02344 22 IQAAKAVADIIRTCLGPRSMLKMLLDPMGGIVMTNDGNAILREIDVAHP----AAKSMIELSRTQDEEVGDGTTSVIILA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 121 RSIAKEGFEKISKGANPVEIRRGVMLAVDAVIAELKKQSKPVTTPEEIAQVATISANGDKEIGNIISDAMKKVGRKGVIT 200
Cdd:TIGR02344 98 GEMLSVAEPFLEQNIHPTVIIRAYRKALDDALSVLEEISIPVDVNDDAAMLKLIQSCIGTKFVSRWSDLMCDLALDAVRT 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 201 VKDGKTLNDELEIIEgmkfdrgyispyFINTSKGQKCEFQDAYVLlsekKISSIQSIVPALEIANAHRKPLVII----AE 276
Cdd:TIGR02344 178 VQRDENGRKEIDIKR------------YAKVEKIPGGDIEDSCVL----KGVMINKDVTHPKMRRYIENPRIVLldcpLE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 277 DVDGEALSTLVLNRLKVGLQVVAVKApgfgDNRKNQLKDMAIATGGAVFGEEGLTlnleDVQPHDLGKVGEVIVTK---- 352
Cdd:TIGR02344 242 YKKGESQTNIEITKEEDWNRILQMEE----EYVQLMCEDIIAVKPDLVITEKGVS----DLAQHYLLKANITAIRRvrkt 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 353 DDAMLLKGKGdkAQIEKRIQEIIEQlDVTTSE--YEKEKLNERL------AKLSDGVAVLKVGGTSDVeVNEKKDRVTDA 424
Cdd:TIGR02344 314 DNNRIARACG--ATIVNRPEELRES-DVGTGCglFEVKKIGDEYftfiteCKDPKACTILLRGASKDI-LNEVERNLQDA 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 425 LNATRAAVEEG-IVLGGGCALLRCIPALDSLTPANED-QKIGIEIIKRTLKIPAMTIAKNAGVE-----GSLIVEKIMQS 497
Cdd:TIGR02344 390 MAVARNVLLDPkLVPGGGATEMAVSVALTEKSKKLEGvEQWPYRAVADALEIIPRTLAQNCGANvirtlTELRAKHAQEN 469
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 41399285 498 SSEVGYDAMAGDFVNMVEKGIIDPTKVVRTALLDAAGVASLLTTAEVVVTEIPKE 552
Cdd:TIGR02344 470 NCTWGIDGETGKIVDMKEKGIWEPLAVKLQTYKTAIESACLLLRIDDIVSGVKKK 524
|
|
| chap_CCT_delta |
TIGR02342 |
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ... |
34-547 |
3.16e-08 |
|
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: 56.33 E-value: 3.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 34 ADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDKykniGAKLVQDVANNTNEEAGDGT 113
Cdd:TIGR02342 8 QDVRTSNIVAAKAVADAIRTSLGPKGMDKMIQDGKGEVIITNDGATILKQMAVLHP----AAKMLVELSKAQDIEAGDGT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 114 TTATVLARSIAKEGFEKISKGANPVEIRRGVMLAVDAVIAELKKQSKPVTTPEEIAQVATISANGDKEIGNIISDAMKKV 193
Cdd:TIGR02342 84 TSVVILAGALLGACERLLNKGIHPTIISESFQSAADEAIKILDEMSIPVDLSDREQLLKSATTSLSSKVVSQYSSLLAPL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 194 GRKGVITVKDGKT-----LND------------ELEIIEGMKFDRGYISpyfintSKGQKCEFQDAYVLLSEKKISSIQS 256
Cdd:TIGR02342 164 AVDAVLKVIDPENaknvdLNDikvvkklggtidDTELIEGLVFTQKASK------SAGGPTRIEKAKIGLIQFQISPPKT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 257 IVPALEIANAHRKPLVIIAEdvDGEALSTLVLNRLKVGLQVVAVKapgfgdnrKNQLKDMaiatggavfgeegltlnLED 336
Cdd:TIGR02342 238 DMENQIIVNDYAQMDRVLKE--ERAYILNIVKKIKKTGCNVLLIQ--------KSILRDA-----------------VND 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 337 VQPHDLGKVGeVIVTKD-----DAMLLKGKGDK--AQIEKRIQEIIEQLD----VTTSEYEKEKLNErLAKLSDGVAVLk 405
Cdd:TIGR02342 291 LALHFLAKMK-IMVVKDiereeIEFICKTIGCKpiASIDHFTADKLGSAElveeVDSDGGKIIKITG-IQNAGKTVTVV- 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 406 VGGTSDVEVNEKKDRVTDALNATRAAVEEGIVLGGGCAllrciPALD-SLTPANEDQKIG------IEIIKRTLKIPAMT 478
Cdd:TIGR02342 368 VRGSNKLVIDEAERSLHDALCVIRCLVKKRGLIAGGGA-----PEIEiARRLSKYARTMKgvesycVRAFADALEVIPYT 442
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41399285 479 IAKNAGVEGSLIV----EKIMQSSSEVGYDAMAGDFVNMVEKGIIDPTKVVRTAL-LDAAGVASLLTTAEVVVT 547
Cdd:TIGR02342 443 LAENAGLNPIKVVtelrNRHANGEKTAGISVRKGGITNMLEEHVLQPLLVTTSAItLASETVRSILKIDDIVFT 516
|
|
| chap_CCT_alpha |
TIGR02340 |
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ... |
33-522 |
3.02e-07 |
|
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: 53.19 E-value: 3.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 33 GADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDKykniGAKLVQDVANNTNEEAGDG 112
Cdd:TIGR02340 10 GQDVRTQNVTAAMAIANIVKTSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHP----AAKILVELAQLQDREVGDG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 113 TTTATVLARSIAKEGFEKISKGANPVEIRRGVMLAVDAVIAELKKqsKPVTTPEEIAQVATISA----------NGDKEI 182
Cdd:TIGR02340 86 TTSVVIIAAELLKRADELVKNKIHPTSVISGYRLACKEAVKYIKE--NLSVSVDELGREALINVaktsmsskiiGLDSDF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 183 -GNIISDAMKKV---GRKGVIT--VKDGKTLND------ELEIIEGMKFDRGYISPYFINTSKGQKCEFQDaYVLLSEKK 250
Cdd:TIGR02340 164 fSNIVVDAVLAVkttNENGETKypIKAINILKAhgksarESMLVKGYALNCTVASQQMPKRIKNAKIACLD-FNLQKAKM 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 251 ISSIQSIV--PAlEIANAHRKPLVIIAEDVDG--EALSTLVLNR-------LKvglQVVAVKAPGFGDNRKNQLKDMAIA 319
Cdd:TIGR02340 243 ALGVQIVVddPE-KLEQIRQREADITKERIKKilDAGANVVLTTggiddmcLK---YFVEAGAMGVRRCKKEDLKRIAKA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 320 TGGAVFGEEGLTLNLEDVQPHDLGKVGEVIVTK---DDAMLLKGKGDKAqiekriqeiieqldvttseyekeklnerlak 396
Cdd:TIGR02340 319 TGATLVSTLADLEGEETFEASYLGFADEVVQERiadDECILIKGTKKRK------------------------------- 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 397 lsdgVAVLKVGGTSDVEVNEKKDRVTDALNATRAAVEEG-IVLGGGCALLRCIPALDSL-TPANEDQKIGIEIIKRTLKI 474
Cdd:TIGR02340 368 ----SASIILRGANDFMLDEMERSLHDALCVVKRTLESNsVVPGGGAVEAALSIYLENFaTTLGSREQLAIAEFARALLI 443
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 475 PAMTIAKNAGVEGSLIVEKIM------QSSSE------VGYDAMAGDFVNMVEKGIIDPT 522
Cdd:TIGR02340 444 IPKTLAVNAAKDSTELVAKLRayhaaaQLKPEkkhlkwYGLDLVNGKIRDNKEAGVLEPT 503
|
|
| TCP1_gamma |
cd03337 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ... |
47-202 |
3.55e-07 |
|
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.
Pssm-ID: 239453 [Multi-domain] Cd Length: 480 Bit Score: 52.68 E-value: 3.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 47 LADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKdkykNIGAKLVQDVANNTNEEAGDGTTTATVLARSIAKE 126
Cdd:cd03337 28 VADVIRTCLGPRAMLKMLLDPMGGIVLTNDGNAILREIDVA----HPAAKSMIELSRTQDEEVGDGTTSVIILAGEILAV 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41399285 127 GFEKISKGANPVEIRRGVMLAVDAVIAELKKQSKPVtTPEEIAQVATI--SANGDKEIgNIISDAMKKVGRKGVITVK 202
Cdd:cd03337 104 AEPFLERGIHPTVIIKAYRKALEDALKILEEISIPV-DVNDRAQMLKIikSCIGTKFV-SRWSDLMCNLALDAVKTVA 179
|
|
| TCP1_alpha |
cd03335 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ... |
33-193 |
1.19e-06 |
|
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.
Pssm-ID: 239451 Cd Length: 527 Bit Score: 51.13 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 33 GADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDKykniGAKLVQDVANNTNEEAGDG 112
Cdd:cd03335 6 GQDVRTQNVTAAMAIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHP----AAKILVELAQLQDKEVGDG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 113 TTTATVLARSIAKEGFEKISKGANPVEIRRGVMLAVDAVIAELKKQ-SKPVTT--PEEIAQVATIS-----ANGDKEI-G 183
Cdd:cd03335 82 TTSVVIIAAELLKRANELVKQKIHPTTIISGYRLACKEAVKYIKEHlSISVDNlgKESLINVAKTSmsskiIGADSDFfA 161
|
170
....*....|
gi 41399285 184 NIISDAMKKV 193
Cdd:cd03335 162 NMVVDAILAV 171
|
|
| chap_CCT_theta |
TIGR02346 |
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ... |
47-221 |
1.65e-05 |
|
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT alpha chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.
Pssm-ID: 274087 [Multi-domain] Cd Length: 531 Bit Score: 47.79 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 47 LADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDKykniGAKLVQDVANNTNEEAGDGTTTATVLARSIAKE 126
Cdd:TIGR02346 30 LSQITRTSLGPNGMNKMVINHLEKLFVTNDAATILRELEVQHP----AAKLLVMASEMQENEIGDGTNLVLVLAGELLNK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 127 GFEKISKGANPVEIRRGVMLAVDAVIAELKKQSK-PVTTPEEIAQV--ATISANGDKEIGN------IISDAM-----KK 192
Cdd:TIGR02346 106 AEELIRMGLHPSEIIKGYEMALKKAMEILEELVVwEVKDLRDKDELikALKASISSKQYGNedflaqLVAQACstvlpKN 185
|
170 180 190
....*....|....*....|....*....|..
gi 41399285 193 VGRKGVITVKDGKTLNDEL---EIIEGMKFDR 221
Cdd:TIGR02346 186 PQNFNVDNIRVCKILGGSLsnsEVLKGMVFNR 217
|
|
| TCP1_zeta |
cd03342 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
47-545 |
4.28e-05 |
|
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: 46.10 E-value: 4.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 47 LADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKdkykNIGAKLVQDVANNTNEEAGDGTTTATVLARSIAKE 126
Cdd:cd03342 24 LQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLSEMQIQ----HPTASMIARAATAQDDITGDGTTSNVLLIGELLKQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 127 GFEKISKGANPVEIRRGVMLAVDAVIAELK--KQSKPVTTPEEIA-QVATISANGD------KEIGNIISDAMKKVGRKG 197
Cdd:cd03342 100 AERYIQEGVHPRIITEGFELAKNKALKFLEsfKVPVEIDTDRELLlSVARTSLRTKlhadlaDQLTEIVVDAVLAIYKPD 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 198 ---------VITVKDGKTLNDELeiIEGMKFDRGYISPyfintskGQKCEFQDAYVLLS------EKKissiqsivpalE 262
Cdd:cd03342 180 epidlhmveIMQMQHKSDSDTKL--IRGLVLDHGARHP-------DMPKRVENAYILTCnvsleyEKT-----------E 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 263 IANAHRKPLVIIAEDVDGEALSTLV------LNRLKvglqvvavkapgfgdnRKNqLKDMAIATGGAVFGeegltlNLED 336
Cdd:cd03342 240 VNSGFFYSVVINQKGIDPPSLDMLAkegilaLRRAK----------------RRN-MERLTLACGGVAMN------SVDD 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 337 VQPHDLGKVGEVIVTKDdamllkgkGDkaqiEKriQEIIEQLDVTTSeyekeklnerlaklsdgVAVLkVGGTSDVEVNE 416
Cdd:cd03342 297 LSPECLGYAGLVYERTL--------GE----EK--YTFIEGVKNPKS-----------------CTIL-IKGPNDHTITQ 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 417 KKDRVTDALNATRAAVEEGIVLGGGCAL-LRCIPALDSLTP-ANEDQKIGIEIIKRTLKIPAMTIAKNAGVEGS----LI 490
Cdd:cd03342 345 IKDAIRDGLRAVKNAIEDKCVVPGAGAFeVALYAHLKEFKKsVKGKAKLGVQAFADALLVIPKTLAENSGLDVQetlvKL 424
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 41399285 491 VEKIMQSSSEVGYDAMAGDFVNMVEKGIIDPTKVVRTALLDAAGVAS-LLTTAEVV 545
Cdd:cd03342 425 QDEYAEGGQVGGVDLDTGEPMDPESEGIWDNYSVKRQILHSATVIASqLLLVDEII 480
|
|
| chap_CCT_zeta |
TIGR02347 |
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ... |
47-546 |
1.38e-04 |
|
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: 44.73 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 47 LADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKdkykNIGAKLVQDVANNTNEEAGDGTTTATVLARSIAKE 126
Cdd:TIGR02347 28 LQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEMQIQ----HPTASMIARAATAQDDITGDGTTSTVLLIGELLKQ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 127 GFEKISKGANPVEIRRGVMLAVDAVIAELK--KQSKPVTTPEEIAQVATISANGDK-------EIGNIISDAMKKVGRKG 197
Cdd:TIGR02347 104 AERYILEGVHPRIITEGFEIARKEALQFLDkfKVKKEDEVDREFLLNVARTSLRTKlpadladQLTEIVVDAVLAIKKDG 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 198 ---------VITVKDGKTLNDELeiIEGMKFDRGYISPyfintskGQKCEFQDAYVLLS----EKKISSIQSivpALEIA 264
Cdd:TIGR02347 184 edidlfmveIMEMKHKSATDTTL--IRGLVLDHGARHP-------DMPRRVKNAYILTCnvslEYEKTEVNS---GFFYS 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 265 NAHRKPLVIIAED--VDG------EALSTLVLNRLKVGLQVVAVK-----------APGFGDNRKNQLKDM---AIATGG 322
Cdd:TIGR02347 252 SAEQREKLVKAERkfVDDrvkkiiELKKKVCGKSPDKGFVVINQKgidppsldllaKEGIMALRRAKRRNMerlTLACGG 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 323 AVFGeegltlNLEDVQPHDLGKVGEVIvtkddamllkgkgdkaqiekriQEIIEQLDVTtseYEKEKLNERlaklsdGVA 402
Cdd:TIGR02347 332 EALN------SVEDLTPECLGWAGLVY----------------------ETTIGEEKYT---FIEECKNPK------SCT 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 403 VLkVGGTSDVEVNEKKDRVTDALNATRAAVEEG-IVLGGGCALLRCIPALDSLTP-ANEDQKIGIEIIKRTLKIPAMTIA 480
Cdd:TIGR02347 375 IL-IKGPNDHTIAQIKDAVRDGLRAVKNAIEDKcVVPGAGAFEIAAYRHLKEYKKsVKGKAKLGVEAFANALLVIPKTLA 453
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 481 KNAGVEGS----LIVEKIMQSSSEVGYDAMAGDFVNMVEKGIIDPTKVVRTALLDAAGVASLLTTAEVVV 546
Cdd:TIGR02347 454 ENSGFDAQdtlvKLEDEHDEGGEVVGVDLNTGEPIDPEIKGIWDNYRVKKQLIQSATVIASQLLLVDEVM 523
|
|
| TCP1_theta |
cd03341 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ... |
47-184 |
4.91e-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: 4.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41399285 47 LADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDKykniGAKLVQDVANNTNEEAGDGTTTATVLARSIAKE 126
Cdd:cd03341 20 LSQITRTSYGPNGMNKMVINHLEKLFVTSDAATILRELEVQHP----AAKLLVMASQMQEEEIGDGTNLVVVLAGELLEK 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41399285 127 GFEKISKGANPVEIRRGVMLAVDAVIAELK----KQSKPVTTPEEIAQvATISANGDKEIGN 184
Cdd:cd03341 96 AEELLRMGLHPSEIIEGYEKALKKALEILEelvvYKIEDLRNKEEVSK-ALKTAIASKQYGN 156
|
|
| |
