|
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: 868.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 28 KDVKFGADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDKYKNIGAKLVQDVANNTNE 107
Cdd:cd03344 1 KDIKFGEEARKALLRGVNKLADAVKVTLGPKGRNVVIEKSFGSPKITKDGVTVAKEIELEDPFENMGAQLVKEVASKTND 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 108 EAGDGTTTATVLARSIAKEGFEKISKGANPVEIRRGVMLAVDAVIAELKKQSKPVTTPEEIAQVATISANGDKDIGNIIS 187
Cdd:cd03344 81 VAGDGTTTATVLARAIIKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKPVKTKEEIAQVATISANGDEEIGELIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 188 DAMKKVGRKGVITVKDGKTLNDELEIIEGMKFDRGYISPYFINTSKGQKCEFQDAYVLLSEKKISSVQSIVPALEIANAH 267
Cdd:cd03344 161 EAMEKVGKDGVITVEEGKTLETELEVVEGMQFDRGYLSPYFVTDPEKMEVELENPYILLTDKKISSIQELLPILELVAKA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 268 RKPLVIIAEDVDGEALSTLVLNRLKVGLQVVAVKAPGFGDNRKNQLKDMAIATGGAVFGEEgLNLNLEDVQAHDLGKVGE 347
Cdd:cd03344 241 GRPLLIIAEDVEGEALATLVVNKLRGGLKVCAVKAPGFGDRRKAMLEDIAILTGGTVISEE-LGLKLEDVTLEDLGRAKK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 348 VIVTKDDAMLLKGKGDKAHIEKRIQEITEQLDITTSEYEKEKLNERLAKLSDGVAVLKVGGTSDVEVNEKKDRVTDALNA 427
Cdd:cd03344 320 VVVTKDDTTIIGGAGDKAAIKARIAQIRKQIEETTSDYDKEKLQERLAKLSGGVAVIKVGGATEVELKEKKDRVEDALNA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 428 TRAAVEEGIVLGGGCALLRCIPALDSLKPANEDQKIGIEIIKRALKIPAMTIAKNAGVEGSLIVEKILQSSSEVGYDAML 507
Cdd:cd03344 400 TRAAVEEGIVPGGGVALLRASPALDKLKALNGDEKLGIEIVRRALEAPLRQIAENAGVDGSVVVEKVLESPDGFGYDAAT 479
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1252004249 508 GDFVNMVEKGIIDPTKVVRTALLDAAGVASLLTTAEAVVTE 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: 774.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 24 RAYAKDVKFGADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDKYKNIGAKLVQDVAN 103
Cdd:PTZ00114 11 RFKGKEIRFGDEARQSLLKGIERLADAVAVTLGPKGRNVIIEQEYGSPKITKDGVTVAKAIEFSDRFENVGAQLIRQVAS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 104 NTNEEAGDGTTTATVLARSIAKEGFEKISKGANPVEIRRGVMLAVDAVIAELKKQSKPVTTPEEIAQVATISANGDKDIG 183
Cdd:PTZ00114 91 KTNDKAGDGTTTATILARAIFREGCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQSRPVKTKEDILNVATISANGDVEIG 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 184 NIISDAMKKVGRKGVITVKDGKTLNDELEIIEGMKFDRGYISPYFINTSKGQKCEFQDAYVLLSEKKISSVQSIVPALEI 263
Cdd:PTZ00114 171 SLIADAMDKVGKDGTITVEDGKTLEDELEVVEGMSFDRGYISPYFVTNEKTQKVELENPLILVTDKKISSIQSILPILEH 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 264 ANAHRKPLVIIAEDVDGEALSTLVLNRLKVGLQVVAVKAPGFGDNRKNQLKDMAIATGGAVFGEEGLNLNLEDVQAHDLG 343
Cdd:PTZ00114 251 AVKNKRPLLIIAEDVEGEALQTLIINKLRGGLKVCAVKAPGFGDNRKDILQDIAVLTGATVVSEDNVGLKLDDFDPSMLG 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 344 KVGEVIVTKDDAMLLKGKGDKAHIEKRIQEITEQLDITTSEYEKEKLNERLAKLSDGVAVLKVGGTSDVEVNEKKDRVTD 423
Cdd:PTZ00114 331 SAKKVTVTKDETVILTGGGDKAEIKERVELLRSQIERTTSEYDKEKLKERLAKLSGGVAVIKVGGASEVEVNEKKDRIED 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 424 ALNATRAAVEEGIVLGGGCALLRCIPALDSLKPANE---DQKIGIEIIKRALKIPAMTIAKNAGVEGSLIVEKILQSS-S 499
Cdd:PTZ00114 411 ALNATRAAVEEGIVPGGGVALLRASKLLDKLEEDNEltpDQRTGVKIVRNALRLPTKQIAENAGVEGAVVVEKILEKKdP 490
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1252004249 500 EVGYDAMLGDFVNMVEKGIIDPTKVVRTALLDAAGVASLLTTAEAVVTEIPKEEKD 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: 760.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 27 AKDVKFGADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDKYKNIGAKLVQDVANNTN 106
Cdd:PRK00013 2 AKDIKFGEDARRKLLRGVNKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDPFENMGAQLVKEVASKTN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 107 EEAGDGTTTATVLARSIAKEGFEKISKGANPVEIRRGVMLAVDAVIAELKKQSKPVTTPEEIAQVATISANGDKDIGNII 186
Cdd:PRK00013 82 DVAGDGTTTATVLAQAIVREGLKNVAAGANPMDLKRGIDKAVEAAVEELKKISKPVEDKEEIAQVATISANGDEEIGKLI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 187 SDAMKKVGRKGVITVKDGKTLNDELEIIEGMKFDRGYISPYFINTSKGQKCEFQDAYVLLSEKKISSVQSIVPALEIANA 266
Cdd:PRK00013 162 AEAMEKVGKEGVITVEESKGFETELEVVEGMQFDRGYLSPYFVTDPEKMEAELENPYILITDKKISNIQDLLPVLEQVAQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 267 HRKPLVIIAEDVDGEALSTLVLNRLKVGLQVVAVKAPGFGDNRKNQLKDMAIATGGAVFGEEgLNLNLEDVQAHDLGKVG 346
Cdd:PRK00013 242 SGKPLLIIAEDVEGEALATLVVNKLRGTLKVVAVKAPGFGDRRKAMLEDIAILTGGTVISEE-LGLKLEDATLEDLGQAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 347 EVIVTKDDAMLLKGKGDKAHIEKRIQEITEQLDITTSEYEKEKLNERLAKLSDGVAVLKVGGTSDVEVNEKKDRVTDALN 426
Cdd:PRK00013 321 KVVVTKDNTTIVDGAGDKEAIKARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATEVEMKEKKDRVEDALH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 427 ATRAAVEEGIVLGGGCALLRCIPALDSLKPANEDQKIGIEIIKRALKIPAMTIAKNAGVEGSLIVEKILQSSSE-VGYDA 505
Cdd:PRK00013 401 ATRAAVEEGIVPGGGVALLRAAPALEALKGLNGDEATGINIVLRALEAPLRQIAENAGLEGSVVVEKVKNGKGKgYGYNA 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1252004249 506 MLGDFVNMVEKGIIDPTKVVRTALLDAAGVASLLTTAEAVVTEIPKEEKDP 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: 716.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 27 AKDVKFGADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDKYKNIGAKLVQDVANNTN 106
Cdd:PRK12849 2 AKIIKFDEEARRALERGVNKLADAVKVTLGPKGRNVVIDKSFGAPTITKDGVSIAKEIELEDPFENLGAQLVKEVASKTN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 107 EEAGDGTTTATVLARSIAKEGFEKISKGANPVEIRRGVMLAVDAVIAELKKQSKPVTTPEEIAQVATISANGDKDIGNII 186
Cdd:PRK12849 82 DVAGDGTTTATVLAQALVQEGLKNVAAGANPMDLKRGIDKAVEAVVEELKALARPVSGSEEIAQVATISANGDEEIGELI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 187 SDAMKKVGRKGVITVKDGKTLNDELEIIEGMKFDRGYISPYFINTSKGQKCEFQDAYVLLSEKKISSVQSIVPALEIANA 266
Cdd:PRK12849 162 AEAMEKVGKDGVITVEESKTLETELEVTEGMQFDRGYLSPYFVTDPERMEAVLEDPLILLTDKKISSLQDLLPLLEKVAQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 267 HRKPLVIIAEDVDGEALSTLVLNRLKVGLQVVAVKAPGFGDNRKNQLKDMAIATGGAVFGEEgLNLNLEDVQAHDLGKVG 346
Cdd:PRK12849 242 SGKPLLIIAEDVEGEALATLVVNKLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGTVISED-LGLKLEEVTLDDLGRAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 347 EVIVTKDDAMLLKGKGDKAHIEKRIQEITEQLDITTSEYEKEKLNERLAKLSDGVAVLKVGGTSDVEVNEKKDRVTDALN 426
Cdd:PRK12849 321 RVTITKDNTTIVDGAGDKEAIEARVAQIRRQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATEVELKERKDRVEDALN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 427 ATRAAVEEGIVLGGGCALLRCIPALDSLKPANEDQKIGIEIIKRALKIPAMTIAKNAGVEGSLIVEKILQSSSEVGYDAM 506
Cdd:PRK12849 401 ATRAAVEEGIVPGGGVALLRAAKALDELAGLNGDQAAGVEIVRRALEAPLRQIAENAGLDGSVVVAKVLELEDGFGFNAA 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1252004249 507 LGDFVNMVEKGIIDPTKVVRTALLDAAGVASLLTTAEAVVTEIPKEEKDP 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: 692.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 27 AKDVKFGADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDKYKNIGAKLVQDVANNTN 106
Cdd:TIGR02348 1 AKQIKFDEEARKALLRGVDKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDKFENMGAQLVKEVASKTN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 107 EEAGDGTTTATVLARSIAKEGFEKISKGANPVEIRRGVMLAVDAVIAELKKQSKPVTTPEEIAQVATISANGDKDIGNII 186
Cdd:TIGR02348 81 DVAGDGTTTATVLAQAIVKEGLKNVAAGANPIELKRGIEKAVEAVVEELKKLSKPVKGKKEIAQVATISANNDEEIGSLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 187 SDAMKKVGRKGVITVKDGKTLNDELEIIEGMKFDRGYISPYFINTSKGQKCEFQDAYVLLSEKKISSVQSIVPALEIANA 266
Cdd:TIGR02348 161 AEAMEKVGKDGVITVEESKSLETELEVVEGMQFDRGYISPYFVTDAEKMEVELENPYILITDKKISNIKDLLPLLEKVAQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 267 HRKPLVIIAEDVDGEALSTLVLNRLKVGLQVVAVKAPGFGDNRKNQLKDMAIATGGAVFGEEgLNLNLEDVQAHDLGKVG 346
Cdd:TIGR02348 241 SGKPLLIIAEDVEGEALATLVVNKLRGTLNVCAVKAPGFGDRRKAMLEDIAILTGGQVISEE-LGLKLEEVTLDDLGKAK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 347 EVIVTKDDAMLLKGKGDKAHIEKRIQEITEQLDITTSEYEKEKLNERLAKLSDGVAVLKVGGTSDVEVNEKKDRVTDALN 426
Cdd:TIGR02348 320 KVTVDKDNTTIVEGAGDKAAIKARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATETEMKEKKLRIEDALN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 427 ATRAAVEEGIVLGGGCALLRCIPALDSLKPANEDQKIGIEIIKRALKIPAMTIAKNAGVEGSLIVEKILQSSSEVGYDAM 506
Cdd:TIGR02348 400 ATRAAVEEGIVPGGGVALLRAAAALEGLKGDGEDEAIGIDIVKRALEAPLRQIAENAGLDGAVVAEKVKELKGNFGFNAA 479
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1252004249 507 LGDFVNMVEKGIIDPTKVVRTALLDAAGVASLLTTAEAVVTEIPK 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: 685.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 27 AKDVKFGADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDKYKNIGAKLVQDVANNTN 106
Cdd:PRK12850 3 AKEIRFSTDARDRLLRGVNILANAVKVTLGPKGRNVVLEKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVKEVASKTN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 107 EEAGDGTTTATVLARSIAKEGFEKISKGANPVEIRRGVMLAVDAVIAELKKQSKPVTTPEEIAQVATISANGDKDIGNII 186
Cdd:PRK12850 83 DLAGDGTTTATVLAQAIVREGAKLVAAGMNPMDLKRGIDLAVAAVVDELKKIAKKVTSSKEIAQVATISANGDESIGEMI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 187 SDAMKKVGRKGVITVKDGKTLNDELEIIEGMKFDRGYISPYFINTSKGQKCEFQDAYVLLSEKKISSVQSIVPALEIANA 266
Cdd:PRK12850 163 AEAMDKVGKEGVITVEEAKTLGTELDVVEGMQFDRGYLSPYFVTNPEKMRAELEDPYILLHEKKISNLQDLLPILEAVVQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 267 HRKPLVIIAEDVDGEALSTLVLNRLKVGLQVVAVKAPGFGDNRKNQLKDMAIATGGAVFGEEgLNLNLEDVQAHDLGKVG 346
Cdd:PRK12850 243 SGRPLLIIAEDVEGEALATLVVNKLRGGLKSVAVKAPGFGDRRKAMLEDIAVLTGGQVISED-LGIKLENVTLDMLGRAK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 347 EVIVTKDDAMLLKGKGDKAHIEKRIQEITEQLDITTSEYEKEKLNERLAKLSDGVAVLKVGGTSDVEVNEKKDRVTDALN 426
Cdd:PRK12850 322 RVLITKENTTIIDGAGDKKNIEARVKQIRAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKEKKDRVDDALH 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 427 ATRAAVEEGIVLGGGCALLRCIPALDSLKPANEDQKIGIEIIKRALKIPAMTIAKNAGVEGSLIVEKILQSSSEVGYDAM 506
Cdd:PRK12850 402 ATRAAVEEGIVPGGGVALLRARSALRGLKGANADETAGIDIVRRALEEPLRQIATNAGFEGSVVVGKVAELPGNFGFNAQ 481
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1252004249 507 LGDFVNMVEKGIIDPTKVVRTALLDAAGVASLLTTAEAVVTEIPKEE 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: 648.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 27 AKDVKFGADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDKYKNIGAKLVQDVANNTN 106
Cdd:PRK12852 3 AKDVKFSGDARDRMLRGVDILANAVKVTLGPKGRNVVIEKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVREVASKTN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 107 EEAGDGTTTATVLARSIAKEGFEKISKGANPVEIRRGVMLAVDAVIAELKKQSKPVTTPEEIAQVATISANGDKDIGNII 186
Cdd:PRK12852 83 DLAGDGTTTATVLAQAIVREGAKAVAAGMNPMDLKRGIDIAVAAVVKDIEKRAKPVASSAEIAQVGTISANGDAAIGKMI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 187 SDAMKKVGRKGVITVKDGKTLNDELEIIEGMKFDRGYISPYFINTSKGQKCEFQDAYVLLSEKKISSVQSIVPALEIANA 266
Cdd:PRK12852 163 AQAMQKVGNEGVITVEENKSLETEVDIVEGMKFDRGYLSPYFVTNAEKMTVELDDAYILLHEKKLSGLQAMLPVLEAVVQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 267 HRKPLVIIAEDVDGEALSTLVLNRLKVGLQVVAVKAPGFGDNRKNQLKDMAIATGGAVFGEEgLNLNLEDVQAHDLGKVG 346
Cdd:PRK12852 243 SGKPLLIIAEDVEGEALATLVVNRLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGQLISED-LGIKLENVTLKMLGRAK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 347 EVIVTKDDAMLLKGKGDKAHIEKRIQEITEQLDITTSEYEKEKLNERLAKLSDGVAVLKVGGTSDVEVNEKKDRVTDALN 426
Cdd:PRK12852 322 KVVIDKENTTIVNGAGKKADIEARVGQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKEKKDRVEDALN 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 427 ATRAAVEEGIVLGGGCALLRCIPALDSLKPANEDQKIGIEIIKRALKIPAMTIAKNAGVEGSLIVEKILQSSSEV-GYDA 505
Cdd:PRK12852 402 ATRAAVQEGIVPGGGVALLRAKKAVGRINNDNADVQAGINIVLKALEAPIRQIAENAGVEGSIVVGKILENKSETfGFDA 481
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1252004249 506 MLGDFVNMVEKGIIDPTKVVRTALLDAAGVASLLTTAEAVVTEIPKEEKDP 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: 636.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 27 AKDVKFGADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDKYKNIGAKLVQDVANNTN 106
Cdd:PRK12851 3 AKEVKFHVEAREKMLRGVNILADAVKVTLGPKGRNVVIDKSFGAPTITNDGVTIAKEIELEDKFENMGAQMVREVASKTN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 107 EEAGDGTTTATVLARSIAKEGFEKISKGANPVEIRRGVMLAVDAVIAELKKQSKPVTTPEEIAQVATISANGDKDIGNII 186
Cdd:PRK12851 83 DVAGDGTTTATVLAQAIVREGAKAVAAGANPMDLKRGIDRAVAAVVEELKANARPVTTNAEIAQVATISANGDAEIGRLV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 187 SDAMKKVGRKGVITVKDGKTLNDELEIIEGMKFDRGYISPYFINTSKGQKCEFQDAYVLLSEKKISSVQSIVPALEIANA 266
Cdd:PRK12851 163 AEAMEKVGNEGVITVEESKTAETELEVVEGMQFDRGYLSPYFVTDADKMEAELEDPYILIHEKKISNLQDLLPVLEAVVQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 267 HRKPLVIIAEDVDGEALSTLVLNRLKVGLQVVAVKAPGFGDNRKNQLKDMAIATGGAVFGEEgLNLNLEDVQAHDLGKVG 346
Cdd:PRK12851 243 SGKPLLIIAEDVEGEALATLVVNKLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGTVISED-LGIKLENVTLEQLGRAK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 347 EVIVTKDDAMLLKGKGDKAHIEKRIQEITEQLDITTSEYEKEKLNERLAKLSDGVAVLKVGGTSDVEVNEKKDRVTDALN 426
Cdd:PRK12851 322 KVVVEKENTTIIDGAGSKTEIEGRVAQIRAQIEETTSDYDREKLQERLAKLAGGVAVIRVGASTEVEVKEKKDRVDDALH 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 427 ATRAAVEEGIVLGGGCALLRCIPALDSLKPANEDQKIGIEIIKRALKIPAMTIAKNAGVEGSLIVEKILQSSSEVGYDAM 506
Cdd:PRK12851 402 ATRAAVEEGIVPGGGVALLRAVKALDKLETANGDQRTGVEIVRRALEAPVRQIAENAGAEGSVVVGKLREKPGGYGFNAA 481
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1252004249 507 LGDFVNMVEKGIIDPTKVVRTALLDAAGVASLLTTAEAVVTEIPKEEKDP 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: 629.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 27 AKDVKFGADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDKYKNIGAKLVQDVANNTN 106
Cdd:COG0459 2 AKQILFGEDARRANIRGVKALADAVKVTLGPKGRNVMLVKSFGDPTITNDGVTIAKEIELEDPFENMGAQLVKEVASKTN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 107 EEAGDGTTTATVLARSIAKEGFEKISKGANPVEIRRGVMLAVDAVIAELKKQSKPVTTPEEIAQVATISANGDKDIGNII 186
Cdd:COG0459 82 DEAGDGTTTATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPVDDKEELAQVATISANGDEEIGELI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 187 SDAMKKVGRKGVITVKDGKTLNDELEIIEGMKFDRGYISPYFINTSKGQKCEFQDAYVLLSEKKISSVQSIVPALEIANA 266
Cdd:COG0459 162 AEAMEKVGKDGVITVEEGKGLETELEVVEGMQFDKGYLSPYFVTDPEKMPAELENAYILLTDKKISSIQDLLPLLEKVAQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 267 HRKPLVIIAEDVDGEALSTLVLNRLKVGLQVVAVKAPGFGDNRKNQLKDMAIATGGAVFGEEgLNLNLEDVQAHDLGKVG 346
Cdd:COG0459 242 SGKPLLIIAEDIDGEALATLVVNGIRGVLRVVAVKAPGFGDRRKAMLEDIAILTGGRVISED-LGLKLEDVTLDDLGRAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 347 EVIVTKDDAMLLKGKGDKAHIekriqeiteqldittseyekeklnerlaklsdgvaVLKVGGTSDVEVNEKKDRVTDALN 426
Cdd:COG0459 321 RVEVDKDNTTIVEGAGNPKAI-----------------------------------VILVGAATEVEVKERKRRVEDALH 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 427 ATRAAVEEGIVLGGGCALLRCIPALDSLKPANE-DQKIGIEIIKRALKIPAMTIAKNAGVEGSLIVEKILQSSSE-VGYD 504
Cdd:COG0459 366 ATRAAVEEGIVPGGGAALLRAARALRELAAKLEgDEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKVRAAKDKgFGFD 445
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1252004249 505 AMLGDFVNMVEKGIIDPTKVVRTALLDAAGVASLLTTAEAVVTEIPKEEKDP 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: 587.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 27 AKDVKFGADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDKYKNIGAKLVQDVANNTN 106
Cdd:PRK14104 3 AKEVKFGVDARDRMLRGVDILANAVKVTLGPKGRNVVLDKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVREVASKSA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 107 EEAGDGTTTATVLARSIAKEGFEKISKGANPVEIRRGVMLAVDAVIAELKKQSKPVTTPEEIAQVATISANGDKDIGNII 186
Cdd:PRK14104 83 DAAGDGTTTATVLAQAIVREGAKSVAAGMNPMDLKRGIDLAVEAVVADLVKNSKKVTSNDEIAQVGTISANGDAEIGKFL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 187 SDAMKKVGRKGVITVKDGKTLNDELEIIEGMKFDRGYISPYFINTSKGQKCEFQDAYVLLSEKKISSVQSIVPALEIANA 266
Cdd:PRK14104 163 ADAMKKVGNEGVITVEEAKSLETELDVVEGMQFDRGYISPYFVTNADKMRVEMDDAYILINEKKLSSLNELLPLLEAVVQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 267 HRKPLVIIAEDVDGEALSTLVLNRLKVGLQVVAVKAPGFGDNRKNQLKDMAIATGGAVFGEEgLNLNLEDVQAHDLGKVG 346
Cdd:PRK14104 243 TGKPLVIVAEDVEGEALATLVVNRLRGGLKVAAVKAPGFGDRRKAMLQDIAILTGGQAISED-LGIKLENVTLQMLGRAK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 347 EVIVTKDDAMLLKGKGDKAHIEKRIQEITEQLDITTSEYEKEKLNERLAKLSDGVAVLKVGGTSDVEVNEKKDRVTDALN 426
Cdd:PRK14104 322 KVMIDKENTTIVNGAGKKADIEARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKERKDRVDDAMH 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 427 ATRAAVEEGIVLGGGCALLRCIPALDSLKPANEDQKIGIEIIKRALKIPAMTIAKNAGVEGSLIVEKILQSSS-EVGYDA 505
Cdd:PRK14104 402 ATRAAVEEGIVPGGGVALLRASEQLKGIKTKNDDQKTGVEIVRKALSAPARQIAINAGEDGSVIVGKILEKEQySYGFDS 481
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1252004249 506 MLGDFVNMVEKGIIDPTKVVRTALLDAAGVASLLTTAEAVVTEIPKE 552
Cdd:PRK14104 482 QTGEYGNLVSKGIIDPTKVVRTAIQNAASVAALLITTEAMVAELPKK 528
|
|
| groEL |
CHL00093 |
chaperonin GroEL |
27-553 |
0e+00 |
|
chaperonin GroEL
Pssm-ID: 177025 Cd Length: 529 Bit Score: 538.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 27 AKDVKFGADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDKYKNIGAKLVQDVANNTN 106
Cdd:CHL00093 2 SKKILYQDNARRALERGMDILAEAVSVTLGPKGRNVVLEKKYGSPQIVNDGVTIAKEIELEDHIENTGVALIRQAASKTN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 107 EEAGDGTTTATVLARSIAKEGFEKISKGANPVEIRRGVMLAVDAVIAELKKQSKPVTTPEEIAQVATISANGDKDIGNII 186
Cdd:CHL00093 82 DVAGDGTTTATVLAYAIVKQGMKNVAAGANPISLKRGIEKATQYVVSQIAEYARPVEDIQAITQVASISAGNDEEVGSMI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 187 SDAMKKVGRKGVITVKDGKTLNDELEIIEGMKFDRGYISPYFINTSKGQKCEFQDAYVLLSEKKISSV-QSIVPALEIAN 265
Cdd:CHL00093 162 ADAIEKVGREGVISLEEGKSTVTELEITEGMRFEKGFISPYFVTDTERMEVVQENPYILLTDKKITLVqQDLLPILEQVT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 266 AHRKPLVIIAEDVDGEALSTLVLNRLKVGLQVVAVKAPGFGDNRKNQLKDMAIATGGAVFGEEgLNLNLEDVQAHDLGKV 345
Cdd:CHL00093 242 KTKRPLLIIAEDVEKEALATLVLNKLRGIVNVVAVRAPGFGDRRKAMLEDIAILTGGQVITED-AGLSLETIQLDLLGQA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 346 GEVIVTKDDAMLLkGKGDKAHIEKRIQEITEQLDITTSEYEKEKLNERLAKLSDGVAVLKVGGTSDVEVNEKKDRVTDAL 425
Cdd:CHL00093 321 RRIIVTKDSTTII-ADGNEEQVKARCEQLRKQIEIADSSYEKEKLQERLAKLSGGVAVIKVGAATETEMKDKKLRLEDAI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 426 NATRAAVEEGIVLGGGCALLRCIPALDSLKPAN--EDQKIGIEIIKRALKIPAMTIAKNAGVEGSLIVEKILQSSSEVGY 503
Cdd:CHL00093 400 NATKAAVEEGIVPGGGATLVHLSENLKTWAKNNlkEDELIGALIVARAILAPLKRIAENAGKNGSVIIEKVQEQDFEIGY 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1252004249 504 DAMLGDFVNMVEKGIIDPTKVVRTALLDAAGVASLLTTAEAVVTEIPKEE 553
Cdd:CHL00093 480 NAANNKFVNMYEAGIIDPAKVTRSALQNAASIASMILTTECIIVDKKESS 529
|
|
| PLN03167 |
PLN03167 |
Chaperonin-60 beta subunit; Provisional |
27-556 |
4.25e-169 |
|
Chaperonin-60 beta subunit; Provisional
Pssm-ID: 215611 [Multi-domain] Cd Length: 600 Bit Score: 493.29 E-value: 4.25e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 27 AKDVKFGADARAL--MLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDKYKNIGAKLVQDVANN 104
Cdd:PLN03167 56 AKELHFNKDGSAIkkLQAGVNKLADLVGVTLGPKGRNVVLESKYGSPKIVNDGVTVAKEVELEDPVENIGAKLVRQAAAK 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 105 TNEEAGDGTTTATVLARSIAKEGFEKISKGANPVEIRRGVMLAVDAVIAELKKQSKPVTTpEEIAQVATISANGDKDIGN 184
Cdd:PLN03167 136 TNDLAGDGTTTSVVLAQGLIAEGVKVVAAGANPVQITRGIEKTAKALVKELKKMSKEVED-SELADVAAVSAGNNYEVGN 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 185 IISDAMKKVGRKGVITVKDGKTLNDELEIIEGMKFDRGYISPYFINTSKGQKCEFQDAYVLLSEKKISSVQSIVPALEIA 264
Cdd:PLN03167 215 MIAEAMSKVGRKGVVTLEEGKSAENNLYVVEGMQFDRGYISPYFVTDSEKMSVEYDNCKLLLVDKKITNARDLIGILEDA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 265 NAHRKPLVIIAEDVDGEALSTLVLNRLKVGLQVVAVKAPGFGDNRKNQLKDMAIATGGAVFGEEgLNLNLEDVQAHDLGK 344
Cdd:PLN03167 295 IRGGYPLLIIAEDIEQEALATLVVNKLRGSLKIAALKAPGFGERKSQYLDDIAILTGGTVIREE-VGLSLDKVGKEVLGT 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 345 VGEVIVTKDDAMLLKGKGDKAHIEKRIQEITEQLDITTSEYEKEKLNERLAKLSDGVAVLKVGGTSDVEVNEKKDRVTDA 424
Cdd:PLN03167 374 AAKVVLTKDTTTIVGDGSTQEAVNKRVAQIKNLIEAAEQDYEKEKLNERIAKLSGGVAVIQVGAQTETELKEKKLRVEDA 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 425 LNATRAAVEEGIVLGGGCALLRCIPALDSLKPA--NEDQKIGIEIIKRALKIPAMTIAKNAGVEGSLIVEKILQSSS-EV 501
Cdd:PLN03167 454 LNATKAAVEEGIVVGGGCTLLRLASKVDAIKDTleNDEQKVGADIVKRALSYPLKLIAKNAGVNGSVVSEKVLSNDNpKF 533
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1252004249 502 GYDAMLGDFVNMVEKGIIDPTKVVRTALLDAAGVASLLTTAEAVVTEIPKEEKDP 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 |
2.19e-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: 429.93 E-value: 2.19e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 28 KDVKFGADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKdkykNIGAKLVQDVANNTNE 107
Cdd:cd00309 1 KEREFGEEARLSNINAAKALADAVKTTLGPKGMDKMLVDSLGDPTITNDGATILKEIEVE----HPAAKLLVEVAKSQDD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 108 EAGDGTTTATVLARSIAKEGFEKISKGANPVEIRRGVMLAVDAVIAELKKQSKP--VTTPEEIAQVATISAN------GD 179
Cdd:cd00309 77 EVGDGTTTVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVPidVEDREELLKVATTSLNsklvsgGD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 180 KDIGNIISDAMKKVGR------KGVITVKDGKTLN-DELEIIEGMKFDRGYISPYFintskgqKCEFQDAYVLLSEKKIS 252
Cdd:cd00309 157 DFLGELVVDAVLKVGKengdvdLGVIRVEKKKGGSlEDSELVVGMVFDKGYLSPYM-------PKRLENAKILLLDCKLE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 253 SvqsivpaleianahrkplVIIAED-VDGEALSTLVLnrlkvgLQVVAVKApgfgdNRKNQLKDMAIATGGAVFGEegln 331
Cdd:cd00309 230 Y------------------VVIAEKgIDDEALHYLAK------LGIMAVRR-----VRKEDLERIAKATGATIVSR---- 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 332 lnLEDVQAHDLGKVGEVIVTKddamllKGKGDKAHIEKriqeiteqldittseyEKEKlnerlaklsdGVAVLKVGGTSD 411
Cdd:cd00309 277 --LEDLTPEDLGTAGLVEETK------IGDEKYTFIEG----------------CKGG----------KVATILLRGATE 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 412 VEVNEKKDRVTDALNATRAAVEE-GIVLGGGCALLRCIPALDSLKP-ANEDQKIGIEIIKRALKIPAMTIAKNAGVEGSL 489
Cdd:cd00309 323 VELDEAERSLHDALCAVRAAVEDgGIVPGGGAAEIELSKALEELAKtLPGKEQLGIEAFADALEVIPRTLAENAGLDPIE 402
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1252004249 490 IVEKILQSSSEVGYDA----MLGDFVNMVEKGIIDPTKVVRTALLDAAGVASLLTTAEAVVT 547
Cdd:cd00309 403 VVTKLRAKHAEGGGNAggdvETGEIVDMKEAGIIDPLKVKRQALKSATEAASLILTIDDIIV 464
|
|
| Cpn60_TCP1 |
pfam00118 |
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ... |
47-546 |
9.83e-69 |
|
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: 230.17 E-value: 9.83e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 47 LADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDKYknigAKLVQDVANNTNEEAGDGTTTATVLARSIAKE 126
Cdd:pfam00118 1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELEIQHPA----AKLLVEAAKAQDEEVGDGTTTVVVLAGELLEE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 127 GFEKISKGANPVEIRRGVMLAVDAVIAELK-KQSKPVTTP--EEIAQVATISANGDKD------IGNIISDAMK------ 191
Cdd:pfam00118 77 AEKLLAAGVHPTTIIEGYEKALEKALEILDsIISIPVEDVdrEDLLKVARTSLSSKIIsresdfLAKLVVDAVLaipknd 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 192 ---KVGRKGVITVKDGKTlnDELEIIEGMKFDRGYISPyfintskGQKCEFQDAYVLLSEKKISSVQSIVPA-------- 260
Cdd:pfam00118 157 gsfDLGNIGVVKILGGSL--EDSELVDGVVLDKGPLHP-------DMPKRLENAKVLLLNCSLEYEKTETKAtvvlsdae 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 261 --LEIANAHRK--------------PLVIIAEDVDGEALSTLVLNRLkVGLQVVavkapgfgdnRKNQLKDMAIATGGAV 324
Cdd:pfam00118 228 qlERFLKAEEEqileivekiidsgvNVVVCQKGIDDLALHFLAKNGI-MALRRV----------KKRDLERLAKATGARA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 325 FGeeglnlNLEDVQAHDLGKVG---EVIVTKDDAMLLKGKGDKahiekriqeiteqldittseyekeklnerlaklsdGV 401
Cdd:pfam00118 297 VS------SLDDLTPDDLGTAGkveEEKIGDEKYTFIEGCKSP-----------------------------------KA 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 402 AVLKVGGTSDVEVNEKKDRVTDALNATRAAVEE-GIVLGGGCALLRCIPALDSL-KPANEDQKIGIEIIKRALKIPAMTI 479
Cdd:pfam00118 336 ATILLRGATDHVLDEIERSIHDALCVVKNAIEDpRVVPGGGAVEMELARALREYaKSVSGKEQLAIEAFAEALEVIPKTL 415
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1252004249 480 AKNAGVEGSLIVEKIL----QSSSEVGYDAMLGDFVNMVEKGIIDPTKVVRTALLDAAGVASLLTTAEAVV 546
Cdd:pfam00118 416 AENAGLDPIEVLAELRaahaSGEKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKSATEAASTILRIDDII 486
|
|
| chaperonin_like |
cd03333 |
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ... |
166-434 |
3.18e-35 |
|
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: 131.43 E-value: 3.18e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 166 EEIAQVATISAN-----GDKDIGNIISDAMKKVGR------KGVITVKDGKTLN-DELEIIEGMKFDRGYISPYFintsk 233
Cdd:cd03333 2 ELLLQVATTSLNsklssWDDFLGKLVVDAVLKVGPdnrmddLGVIKVEKIPGGSlEDSELVVGVVFDKGYASPYM----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 234 gqKCEFQDAYVLLSEKKISSvqsivpaleianahrkplVIIAED-VDGEALSTLVLnrlkvgLQVVAVKApgfgdNRKNQ 312
Cdd:cd03333 77 --PKRLENAKILLLDCPLEY------------------VVIAEKgIDDLALHYLAK------AGIMAVRR-----VKKED 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 313 LKDMAIATGGAVFGEeglnlnLEDVQAHDLGKVGEVIVTKDdamllkgkGDKAHIekRIQEITEQldittseyekeklne 392
Cdd:cd03333 126 LERIARATGATIVSS------LEDLTPEDLGTAELVEETKI--------GEEKLT--FIEGCKGG--------------- 174
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1252004249 393 rlaklsdGVAVLKVGGTSDVEVNEKKDRVTDALNATRAAVEE 434
Cdd:cd03333 175 -------KAATILLRGATEVELDEVKRSLHDALCAVRAAVEE 209
|
|
| cpn60 |
cd03343 |
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ... |
33-539 |
2.99e-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: 103.50 E-value: 2.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 33 GADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKdkykNIGAKLVQDVANNTNEEAGDG 112
Cdd:cd03343 13 GRDAQRMNIAAAKAVAEAVRTTLGPKGMDKMLVDSLGDVTITNDGATILKEMDIE----HPAAKMLVEVAKTQDEEVGDG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 113 TTTATVLARSIAKEGFEKISKGANPVEIRRGVMLAVDAVIAELKKQSKPVTTPEE-----IAQVATISANGDKD---IGN 184
Cdd:cd03343 89 TTTAVVLAGELLEKAEDLLDQNIHPTVIIEGYRLAAEKALELLDEIAIKVDPDDKdtlrkIAKTSLTGKGAEAAkdkLAD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 185 IISDAMKKV--GRKGVITV---------KDGKTLNDElEIIEGMKFDRGYISPyfintskGQKCEFQDAYVLLsekkiss 253
Cdd:cd03343 169 LVVDAVLQVaeKRDGKYVVdldnikiekKTGGSVDDT-ELIRGIVIDKEVVHP-------GMPKRVENAKIAL------- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 254 vqsIVPALEIanahRKPlviiaeDVDGEalstlvlnrlkvgLQVVAV-KAPGFGDNRKNQLKDM--AIATGGA--VFGEE 328
Cdd:cd03343 234 ---LDAPLEV----KKT------EIDAK-------------IRITSPdQLQAFLEQEEAMLKEMvdKIADTGAnvVFCQK 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 329 GlnlnLEDVQAHDLGKVGEVIV--TKDDAMLLKGKGDKAHIEKRIQEITEQLDITTSEYEKEKLNE------RLAKLSDG 400
Cdd:cd03343 288 G----IDDLAQHYLAKAGILAVrrVKKSDMEKLARATGAKIVTNIDDLTPEDLGEAELVEERKVGDdkmvfvEGCKNPKA 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 401 VAVLKVGGTSDVeVNEKKDRVTDALNATRAAVEEGIVLGGGCALLRCIpaldSLKPANEDQKIG------IEIIKRALKI 474
Cdd:cd03343 364 VTILLRGGTEHV-VDELERALEDALRVVADALEDGKVVAGGGAVEIEL----AKRLREYARSVGgreqlaVEAFADALEE 438
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1252004249 475 PAMTIAKNAGVEGsliVEKILQSSSE-------VGYDAMLGDFVNMVEKGIIDPTKVVRTALLDAAGVASLL 539
Cdd:cd03343 439 IPRTLAENAGLDP---IDTLVELRAAhekgnknAGLDVYTGEVVDMLEKGVIEPLRVKKQAIKSATEAATMI 507
|
|
| TCP1_beta |
cd03336 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ... |
33-552 |
2.09e-15 |
|
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: 78.91 E-value: 2.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 33 GADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSW--GSPKVTKDGVTVAKSIDLKdkykNIGAKLVQDVANNTNEEAG 110
Cdd:cd03336 11 GETARLSSFVGAIAIGDLVKTTLGPKGMDKILQSVGrsGGVTVTNDGATILKSIGVD----NPAAKVLVDISKVQDDEVG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 111 DGTTTATVLARSIAKEGFEKISKGANPVEIRRGVMLAVDAVIAELKK-----QSKPVTTPEEIAQVA--TISA---NGDK 180
Cdd:cd03336 87 DGTTSVTVLAAELLREAEKLVAQKIHPQTIIEGYRMATAAAREALLSsavdhSSDEEAFREDLLNIArtTLSSkilTQDK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 181 D-IGNIISDAMKKVGRKG-----VITVKDGKTLNDELeiiegmkFDRGYISPYFINTskGQKCEFQDAYVLLS-----EK 249
Cdd:cd03336 167 EhFAELAVDAVLRLKGSGnldaiQIIKKLGGSLKDSY-------LDEGFLLDKKIGV--NQPKRIENAKILIAntpmdTD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 250 KIS------SVQSIVPALEIANAHRKPLV-----IIAEDVDGEALSTLVLNrlkVGLQVvavkapgFGDNRKnqlkdMAI 318
Cdd:cd03336 238 KIKifgakvRVDSTAKVAEIEEAEKEKMKnkvekILKHGINCFINRQLIYN---YPEQL-------FADAGI-----MAI 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 319 ATggAVF-GEEGLNLNLEdvqahdlgkvGEVIVTKDDAMLLK-GKGDKahiekrIQEITEQldittseyekeklNERLAK 396
Cdd:cd03336 303 EH--ADFdGVERLALVTG----------GEIASTFDHPELVKlGTCKL------IEEIMIG-------------EDKLIR 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 397 LSdGVA-------VLKvgGTSDVEVNEKKDRVTDALNATRAAVEEG-IVLGGGCALLRCIPALDSLKPANEDQK-IGIEI 467
Cdd:cd03336 352 FS-GVAageactiVLR--GASQQILDEAERSLHDALCVLAQTVKDTrVVLGGGCSEMLMAKAVEELAKKTPGKKsLAIEA 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 468 IKRALKIPAMTIAKNAGVEGSLIVEKI----LQSSSEVGYDAMLGDFVNMVEKGIIDPTKVVRTALLDAAGVASLLTTAE 543
Cdd:cd03336 429 FAKALRQLPTIIADNAGYDSAELVAQLraahYNGNTTAGLDMRKGTVGDMKELGITESFKVKRQVLLSASEAAEMILRVD 508
|
....*....
gi 1252004249 544 AVVTEIPKE 552
Cdd:cd03336 509 DIIKCAPRK 517
|
|
| chap_CCT_epsi |
TIGR02343 |
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ... |
33-521 |
1.78e-13 |
|
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: 72.91 E-value: 1.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 33 GADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDKYknigAKLVQDVANNTNEEAGDG 112
Cdd:TIGR02343 25 GLEAKKSNIAAAKSVASILRTSLGPKGMDKMLISPDGDITVTNDGATILSQMDVDNQI----AKLMVELSKSQDDEIGDG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 113 TTTATVLARSIAKEGFEKISKGANPVEIRRGVMLAVDAVIAELKKQSKPVTTPEEIAQV---ATISANGDKdIGNIISDA 189
Cdd:TIGR02343 101 TTGVVVLAGALLEQAEELLDKGIHPIKIADGFEEAARIAVEHLEEISDEISADNNNREPliqAAKTSLGSK-IVSKCHRR 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 190 MKKVGRKGVITVKD-----------------GKTLNDElEIIEGMKFDRGYISPYFINTSKGQK-----CEFQ------- 240
Cdd:TIGR02343 180 FAEIAVDAVLNVADmerrdvdfdlikvegkvGGSLEDT-KLIKGIIIDKDFSHPQMPKEVEDAKiailtCPFEppkpktk 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 241 --------DAYVLLSEKKISSVQSIVPALEIANAHrkpLVIIAEDVDGEALSTLVLNRLKvglqvvAVKAPGfgdnrKNQ 312
Cdd:TIGR02343 259 hkldissvEEYKKLQKYEQQKFKEMIDDIKKSGAN---LVICQWGFDDEANHLLLQNDLP------AVRWVG-----GQE 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 313 LKDMAIATGGAVFGEeglnlnLEDVQAHDLGKVGEVivtkddamllkgkgdkahieKRIQEITEQLDITTSEYEKEklne 392
Cdd:TIGR02343 325 LELIAIATGGRIVPR------FQELSKDKLGKAGLV--------------------REISFGTTKDRMLVIEQCKN---- 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 393 rlaklSDGVAVLkVGGTSDVEVNEKKDRVTDALNATRAAVEEG-IVLGGGCALLRCIPALDSL--KPANEDQKiGIEIIK 469
Cdd:TIGR02343 375 -----SKAVTIF-IRGGNKMIIEEAKRSIHDALCVVRNLIKDSrIVYGGGAAEISCSLAVSQEadKYPGVEQY-AIRAFA 447
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1252004249 470 RALKIPAMTIAKNAGVE--GSLIVEKILQSSSE---VGYDAMLGDFVNMVEKGIIDP 521
Cdd:TIGR02343 448 DALETIPMALAENSGLDpiGTLSTLKSLQLKEKnpnLGVDCLGYGTNDMKEQFVFET 504
|
|
| chap_CCT_beta |
TIGR02341 |
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ... |
33-551 |
6.77e-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: 6.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 33 GADARALMLQGVDLLADAVAVTMGPKGRTVIIEQ--SWGSPKVTKDGVTVAKSIDLKdkykNIGAKLVQDVANNTNEEAG 110
Cdd:TIGR02341 12 AENARLSSFVGAIAIGDLVKSTLGPKGMDKILQSssSDASIMVTNDGATILKSIGVD----NPAAKVLVDMSKVQDDEVG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 111 DGTTTATVLARSIAKEGFEKISKGANPVEIRRGVMLAVDAVIAELKKQS-----KPVTTPEEIAQVA--TISANgdkdIG 183
Cdd:TIGR02341 88 DGTTSVTVLAAELLREAEKLINQKIHPQTIIAGYREATKAARDALLKSAvdngsDEVKFRQDLMNIArtTLSSK----IL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 184 NIISDAMKKVGRKGVITVKdGKTLNDELEIIE--GMKFDRGYISPYFINTSK---GQKCEFQDAYVLLSEKKISS----- 253
Cdd:TIGR02341 164 SQHKDHFAQLAVDAVLRLK-GSGNLEAIQIIKklGGSLADSYLDEGFLLDKKigvNQPKRIENAKILIANTGMDTdkvki 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 254 ------VQSIVPALEIANAHRKPLVIIAEDVDGEALSTLVlNRlkvglQVVAvkapgfgdNRKNQLkdmaiatggavFGE 327
Cdd:TIGR02341 243 fgsrvrVDSTAKVAELEHAEKEKMKEKVEKILKHGINCFI-NR-----QLIY--------NYPEQL-----------FAD 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 328 EGLN----LNLEDVQAHDLGKVGEVIVTKDDAMLLK-GKGDKahiekrIQEITEQldittseyEKEKLNERLAKLSDGVA 402
Cdd:TIGR02341 298 AGVMaiehADFEGVERLALVTGGEIVSTFDHPELVKlGSCDL------IEEIMIG--------EDKLLKFSGVKLGEACT 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 403 VLKVGGTSDVeVNEKKDRVTDALNATRAAVEEG-IVLGGGCALLRCIPALDSLKpANEDQK--IGIEIIKRALKIPAMTI 479
Cdd:TIGR02341 364 IVLRGATQQI-LDEAERSLHDALCVLSQTVKESrTVLGGGCSEMLMSKAVTQEA-QRTPGKeaLAVEAFARALRQLPTII 441
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1252004249 480 AKNAGVEGSLIVEKILQSSSE----VGYDAMLGDFVNMVEKGIIDPTKVVRTALLDAAGVASLLTTAEAVVTEIPK 551
Cdd:TIGR02341 442 ADNAGFDSAELVAQLRAAHYNgnttMGLDMNEGTIADMRQLGITESYKVKRAVVSSAAEAAEVILRVDNIIKAAPR 517
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
33-552 |
1.43e-11 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 66.98 E-value: 1.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 33 GADARALMLQGVDLLADAVAVTMGPKGRTVIIE-----QSWGSPKVTKDGVTVAKSIDLKdkykNIGAKLVQDVANNTNE 107
Cdd:PTZ00212 20 GETARLQSFVGAIAVADLVKTTLGPKGMDKILQpmsegPRSGNVTVTNDGATILKSVWLD----NPAAKILVDISKTQDE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 108 EAGDGTTTATVLARSIAKEGFEKISKGANPVEIRRGVMLAVDAVIAELKKQSKPVTTPEE--------IAQvATISA--- 176
Cdd:PTZ00212 96 EVGDGTTSVVVLAGELLREAEKLLDQKIHPQTIIEGWRMALDVARKALEEIAFDHGSDEEkfkedllnIAR-TTLSSkll 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 177 NGDKD-IGNIISDAMKKVGRKG-----VITVKDGKTLNDEleiiegmkfdrgYISPYFINTSK---GQKCEFQDAYVLLS 247
Cdd:PTZ00212 175 TVEKDhFAKLAVDAVLRLKGSGnldyiQIIKKPGGTLRDS------------YLEDGFILEKKigvGQPKRLENCKILVA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 248 EK-----KIS------SVQSIVPALEIANAHRKPLV-----IIAEDVdgealsTLVLNRlkvglQVVAvkapgfgdNRKN 311
Cdd:PTZ00212 243 NTpmdtdKIKiygakvKVDSMEKVAEIEAAEKEKMKnkvdkILAHGC------NVFINR-----QLIY--------NYPE 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 312 QL-KD---MAIATggAVF-GEEGLNLNLEdvqahdlgkvGEVIVTKDDAMLLK-GKGDKahiekrIQEITeqldittseY 385
Cdd:PTZ00212 304 QLfAEagiMAIEH--ADFdGMERLAAALG----------AEIVSTFDTPEKVKlGHCDL------IEEIM---------I 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 386 EKEKLnERLAKLSDGVA---VLKvgGTSDVEVNEKKDRVTDALNATRAAVEEG-IVLGGGCALLRCIPALDSLKPANEDQ 461
Cdd:PTZ00212 357 GEDKL-IRFSGCAKGEActiVLR--GASTHILDEAERSLHDALCVLSQTVKDTrVVLGGGCSEMLMANAVEELAKKVEGK 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 462 K-IGIEIIKRALKIPAMTIAKNAGVEGSLIVEKI----LQSSSEVGYDAMLGDFVNMVEKGIIDPTKVVRTALLDAAGVA 536
Cdd:PTZ00212 434 KsLAIEAFAKALRQIPTIIADNGGYDSAELVSKLraehYKGNKTAGIDMEKGTVGDMKELGITESYKVKLSQLCSATEAA 513
|
570
....*....|....*.
gi 1252004249 537 SLLTTAEAVVTEIPKE 552
Cdd:PTZ00212 514 EMILRVDDIIRCAPRQ 529
|
|
| chap_CCT_eta |
TIGR02345 |
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ... |
47-167 |
1.79e-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: 1.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 47 LADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDKykniGAKLVQDVANNTNEEAGDGTTTATVLARSIAKE 126
Cdd:TIGR02345 30 IAEALKTTLGPRGMDKLIVGSNGKATISNDGATILKLLDIVHP----AAKTLVDIAKSQDAEVGDGTTSVTILAGELLKE 105
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1252004249 127 GFEKISKGANPVEIRRGVMLAVDAVIAELKKQSkpVTTPEE 167
Cdd:TIGR02345 106 AKPFIEEGVHPQLIIRCYREALSLAVEKIKEIA--VTIDEE 144
|
|
| TCP1_eta |
cd03340 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ... |
48-157 |
2.63e-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: 2.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 48 ADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDKykniGAKLVQDVANNTNEEAGDGTTTATVLARSIAKEG 127
Cdd:cd03340 29 ADAVRTTLGPRGMDKLIVDGRGKVTISNDGATILKLLDIVHP----AAKTLVDIAKSQDAEVGDGTTSVVVLAGEFLKEA 104
|
90 100 110
....*....|....*....|....*....|
gi 1252004249 128 FEKISKGANPVEIRRGVMLAVDAVIAELKK 157
Cdd:cd03340 105 KPFIEDGVHPQIIIRGYRKALQLAIEKIKE 134
|
|
| TCP1_epsilon |
cd03339 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ... |
41-529 |
4.20e-10 |
|
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: 62.32 E-value: 4.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 41 LQGVD------LLADAVAVTM----GPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKdkykNIGAKLVQDVANNTNEEAG 110
Cdd:cd03339 19 LKGLEahkshiLAAKSVANILrtslGPRGMDKILVSPDGEVTVTNDGATILEKMDVD----HQIAKLLVELSKSQDDEIG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 111 DGTTTATVLARSIAKEGFEKISKGANPVEIRRGVMLAVDAVIAELKKQSKPVTTPEE----IAQVATISAnGDKdIGNII 186
Cdd:cd03339 95 DGTTGVVVLAGALLEQAEKLLDRGIHPIRIADGYEQACKIAVEHLEEIADKIEFSPDnkepLIQTAMTSL-GSK-IVSRC 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 187 SDAMKKVGRKGVITVKD--GKTLNDEL--------------EIIEGMKFDRGYISPYFINTSKGQK-----CEFQ----- 240
Cdd:cd03339 173 HRQFAEIAVDAVLSVADleRKDVNFELikvegkvggrledtKLVKGIVIDKDFSHPQMPKEVKDAKiailtCPFEppkpk 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 241 ----------DAYVLLSEKKISSVQSIVPALEIANAHrkpLVIIAEDVDGEALSTLVLNRLKVglqVVAVKAPgfgdnrk 310
Cdd:cd03339 253 tkhklditsvEDYKKLQEYEQKYFREMVEQVKDAGAN---LVICQWGFDDEANHLLLQNGLPA---VRWVGGV------- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 311 nQLKDMAIATGGAVFGEeglnlnLEDVQAHDLGKVGEV----IVTKDDAMLLkgkgdkahIEKriqeiteqldittseye 386
Cdd:cd03339 320 -EIELIAIATGGRIVPR------FEDLSPEKLGKAGLVreisFGTTKDKMLV--------IEG----------------- 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 387 keklnerlAKLSDGVAVLkVGGTSDVEVNEKKDRVTDALNATRAAVEEG-IVLGGGCALLRCipaldSLKPANEDQKIG- 464
Cdd:cd03339 368 --------CPNSKAVTIF-IRGGNKMIIEEAKRSLHDALCVVRNLIRDNrIVYGGGAAEISC-----SLAVEKAADKCSg 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 465 -----IEIIKRALKIPAMTIAKNAGVE--GSLIVEKILQ---SSSEVGYDAMLGDFVNMVEKGIIDP-----------TK 523
Cdd:cd03339 434 ieqyaMRAFADALESIPLALAENSGLNpiETLSEVKARQvkeKNPHLGIDCLGRGTNDMKEQKVFETliskkqqillaTQ 513
|
....*.
gi 1252004249 524 VVRTAL 529
Cdd:cd03339 514 VVKMIL 519
|
|
| TCP1_delta |
cd03338 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ... |
47-240 |
4.74e-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: 61.92 E-value: 4.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 47 LADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDKykniGAKLVQDVANNTNEEAGDGTTTATVLARSIAKE 126
Cdd:cd03338 20 VADAIRTSLGPRGMDKMIQTGKGEVIITNDGATILKQMSVLHP----AAKMLVELSKAQDIEAGDGTTSVVVLAGALLSA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 127 GFEKISKGANPVEIRRGVMLAVDAVIAELKKQSKPV--TTPEEIAQVATISANG------DKDIGNIISDAMKKVGRKGV 198
Cdd:cd03338 96 CESLLKKGIHPTVISESFQIAAKKAVEILDSMSIPVdlNDRESLIKSATTSLNSkvvsqySSLLAPIAVDAVLKVIDPAT 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1252004249 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 |
5.04e-09 |
|
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: 58.98 E-value: 5.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 41 LQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDKykniGAKLVQDVANNTNEEAGDGTTTATVLA 120
Cdd:TIGR02344 22 IQAAKAVADIIRTCLGPRSMLKMLLDPMGGIVMTNDGNAILREIDVAHP----AAKSMIELSRTQDEEVGDGTTSVIILA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 121 RSIAKEGFEKISKGANPVEIRRGVMLAVDAVIAELKKQSKPVTTPEEIAQVATISAN-GDKDIGNiISDAMKKVGRKGVI 199
Cdd:TIGR02344 98 GEMLSVAEPFLEQNIHPTVIIRAYRKALDDALSVLEEISIPVDVNDDAAMLKLIQSCiGTKFVSR-WSDLMCDLALDAVR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 200 TVKDGKTLNDELEIiegmkfdrgyispyfintskgqkcefqdayvllseKKISSVQSIvPALEIANAHRKPLVIIAEDVD 279
Cdd:TIGR02344 177 TVQRDENGRKEIDI-----------------------------------KRYAKVEKI-PGGDIEDSCVLKGVMINKDVT 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 280 GEALSTLVLN----------RLKVGLQVVAVKAPGFGD-NRKNQLKDMAIATGGA---------VFGEEGLNlnleDVQA 339
Cdd:TIGR02344 221 HPKMRRYIENprivlldcplEYKKGESQTNIEITKEEDwNRILQMEEEYVQLMCEdiiavkpdlVITEKGVS----DLAQ 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 340 HDLGKVGEVIVTK----DDAMLLKGKGdkAHIEKRIQEITEQlDITTSE--YEKEKLNERL------AKLSDGVAVLKVG 407
Cdd:TIGR02344 297 HYLLKANITAIRRvrktDNNRIARACG--ATIVNRPEELRES-DVGTGCglFEVKKIGDEYftfiteCKDPKACTILLRG 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 408 GTSDVeVNEKKDRVTDALNATRAAVEEG-IVLGGGCALLRCIPALDSLKPANED-QKIGIEIIKRALKIPAMTIAKNAGV 485
Cdd:TIGR02344 374 ASKDI-LNEVERNLQDAMAVARNVLLDPkLVPGGGATEMAVSVALTEKSKKLEGvEQWPYRAVADALEIIPRTLAQNCGA 452
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1252004249 486 E-----GSLIVEKILQSSSEVGYDAMLGDFVNMVEKGIIDPTKVVRTALLDAAGVASLLTTAEAVVTEIPKE 552
Cdd:TIGR02344 453 NvirtlTELRAKHAQENNCTWGIDGETGKIVDMKEKGIWEPLAVKLQTYKTAIESACLLLRIDDIVSGVKKK 524
|
|
| chap_CCT_delta |
TIGR02342 |
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ... |
34-547 |
1.07e-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: 57.87 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 34 ADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDKykniGAKLVQDVANNTNEEAGDGT 113
Cdd:TIGR02342 8 QDVRTSNIVAAKAVADAIRTSLGPKGMDKMIQDGKGEVIITNDGATILKQMAVLHP----AAKMLVELSKAQDIEAGDGT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 114 TTATVLARSIAKEGFEKISKGANPVEIRRGVMLAVDAVIAELKKQSKPVTTPEEIAQVATISANGDKDIGNIISDAMKKV 193
Cdd:TIGR02342 84 TSVVILAGALLGACERLLNKGIHPTIISESFQSAADEAIKILDEMSIPVDLSDREQLLKSATTSLSSKVVSQYSSLLAPL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 194 GRKGVITVKDGKT-----LND------------ELEIIEGMKFDRGYISpyfintSKGQKCEFQDAYVLLSEKKISSVQS 256
Cdd:TIGR02342 164 AVDAVLKVIDPENaknvdLNDikvvkklggtidDTELIEGLVFTQKASK------SAGGPTRIEKAKIGLIQFQISPPKT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 257 IVPALEIANAHRKPLVIIAEdvDGEALSTLVLNRLKVGLQVVAVKapgfgdnrKNQLKDMaiatggavfgeeglnlnLED 336
Cdd:TIGR02342 238 DMENQIIVNDYAQMDRVLKE--ERAYILNIVKKIKKTGCNVLLIQ--------KSILRDA-----------------VND 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 337 VQAHDLGKVGeVIVTKD-----DAMLLKGKGDK--AHIEKRIQEITEQLDITtseyEKEKLNER-------LAKLSDGVA 402
Cdd:TIGR02342 291 LALHFLAKMK-IMVVKDiereeIEFICKTIGCKpiASIDHFTADKLGSAELV----EEVDSDGGkiikitgIQNAGKTVT 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 403 VLkVGGTSDVEVNEKKDRVTDALNATRAAVEEGIVLGGGCAllrciPALD-SLKPANEDQKIG------IEIIKRALKIP 475
Cdd:TIGR02342 366 VV-VRGSNKLVIDEAERSLHDALCVIRCLVKKRGLIAGGGA-----PEIEiARRLSKYARTMKgvesycVRAFADALEVI 439
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1252004249 476 AMTIAKNAGVEGSLIV----EKILQSSSEVGYDAMLGDFVNMVEKGIIDPTKVVRTAL-LDAAGVASLLTTAEAVVT 547
Cdd:TIGR02342 440 PYTLAENAGLNPIKVVtelrNRHANGEKTAGISVRKGGITNMLEEHVLQPLLVTTSAItLASETVRSILKIDDIVFT 516
|
|
| chap_CCT_alpha |
TIGR02340 |
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ... |
33-522 |
8.21e-08 |
|
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT alpha chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.
Pssm-ID: 274081 [Multi-domain] Cd Length: 536 Bit Score: 55.11 E-value: 8.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 33 GADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDKykniGAKLVQDVANNTNEEAGDG 112
Cdd:TIGR02340 10 GQDVRTQNVTAAMAIANIVKTSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHP----AAKILVELAQLQDREVGDG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 113 TTTATVLARSIAKEGFEKISKGANPVEIRRGVMLAVDAVIAELKKqsKPVTTPEEIAQVATISA----------NGDKDI 182
Cdd:TIGR02340 86 TTSVVIIAAELLKRADELVKNKIHPTSVISGYRLACKEAVKYIKE--NLSVSVDELGREALINVaktsmsskiiGLDSDF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 183 -GNIISDAMKKV---GRKGVIT--VKDGKTLND------ELEIIEGMKFDRGYISPYFINTSKGQKCEFQDaYVLLSEKK 250
Cdd:TIGR02340 164 fSNIVVDAVLAVkttNENGETKypIKAINILKAhgksarESMLVKGYALNCTVASQQMPKRIKNAKIACLD-FNLQKAKM 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 251 ISSVQSIV--PAlEIANAHRKPLVIIAEDVDG--EALSTLVLNR-------LKvglQVVAVKAPGFGDNRKNQLKDMAIA 319
Cdd:TIGR02340 243 ALGVQIVVddPE-KLEQIRQREADITKERIKKilDAGANVVLTTggiddmcLK---YFVEAGAMGVRRCKKEDLKRIAKA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 320 TGGAVFGEEGlNLNLEDV-QAHDLGKVGEVIVTK---DDAMLLKGKGDKAhiekriqeiteqldittseyekeklnerla 395
Cdd:TIGR02340 319 TGATLVSTLA-DLEGEETfEASYLGFADEVVQERiadDECILIKGTKKRK------------------------------ 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 396 klsdgVAVLKVGGTSDVEVNEKKDRVTDALNATRAAVEEG-IVLGGGcallrCIPALDSLKPANEDQKIG------IEII 468
Cdd:TIGR02340 368 -----SASIILRGANDFMLDEMERSLHDALCVVKRTLESNsVVPGGG-----AVEAALSIYLENFATTLGsreqlaIAEF 437
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1252004249 469 KRALKIPAMTIAKNAGVEGSLIVEKIL------QSSSE------VGYDAMLGDFVNMVEKGIIDPT 522
Cdd:TIGR02340 438 ARALLIIPKTLAVNAAKDSTELVAKLRayhaaaQLKPEkkhlkwYGLDLVNGKIRDNKEAGVLEPT 503
|
|
| TCP1_gamma |
cd03337 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ... |
47-539 |
2.47e-07 |
|
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.
Pssm-ID: 239453 [Multi-domain] Cd Length: 480 Bit Score: 53.45 E-value: 2.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 47 LADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKdkykNIGAKLVQDVANNTNEEAGDGTTTATVLARSIAKE 126
Cdd:cd03337 28 VADVIRTCLGPRAMLKMLLDPMGGIVLTNDGNAILREIDVA----HPAAKSMIELSRTQDEEVGDGTTSVIILAGEILAV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 127 GFEKISKGANPVEIRRGVMLAVDAVIAELKKQSKPVtTPEEIAQVATI--SANGDKDIgNIISDAMKKVGRKGVITV-KD 203
Cdd:cd03337 104 AEPFLERGIHPTVIIKAYRKALEDALKILEEISIPV-DVNDRAQMLKIikSCIGTKFV-SRWSDLMCNLALDAVKTVaVE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 204 GKTLNDELEIIEGMKFDR---GYISpyfintskgqkcefqDAYVLlsekkissvqsivpaleianahrkplviiaedvDG 280
Cdd:cd03337 182 ENGRKKEIDIKRYAKVEKipgGEIE---------------DSRVL---------------------------------DG 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 281 ealstLVLNRlkvglQVVAVKAPGFGDNRKNQLKDMAIATggAVFGEEGLNlnleDVQAHDLGKVG-EVI--VTK-DDAM 356
Cdd:cd03337 214 -----VMLNK-----DVTHPKMRRRIENPRIVLLDCPLEY--LVITEKGVS----DLAQHYLVKAGiTALrrVRKtDNNR 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 357 LLKGKGdkAHIEKRIQEITEQlDITTSE--YEKEKL-NERLAKLSD-----GVAVLKVGGTSDVeVNEKKDRVTDALNAT 428
Cdd:cd03337 278 IARACG--ATIVNRPEELTES-DVGTGAglFEVKKIgDEYFTFITEckdpkACTILLRGASKDV-LNEVERNLQDAMAVA 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 429 RAAVEEG-IVLGGGCALLRCIPAL-DSLKPANEDQKIGIEIIKRALKIPAMTIAKNAGVEgslIVEKILQ--------SS 498
Cdd:cd03337 354 RNIILNPkLVPGGGATEMAVSHALsEKAKSIEGVEQWPYKAVASALEVIPRTLAQNCGAN---VIRTLTElrakhaqgEN 430
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1252004249 499 SEVGYDAMLGDFVNMVEKGIIDPTKVVRTALLDAAGVASLL 539
Cdd:cd03337 431 STWGIDGETGDIVDMKELGIWDPLAVKAQTYKTAIEAACML 471
|
|
| TCP1_alpha |
cd03335 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ... |
33-193 |
1.06e-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: 51.52 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 33 GADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDKykniGAKLVQDVANNTNEEAGDG 112
Cdd:cd03335 6 GQDVRTQNVTAAMAIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHP----AAKILVELAQLQDKEVGDG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 113 TTTATVLARSIAKEGFEKISKGANPVEIRRGVMLAVDAVIAELKKQ-SKPVTT--PEEIAQVATIS-----ANGDKDI-G 183
Cdd:cd03335 82 TTSVVIIAAELLKRANELVKQKIHPTTIISGYRLACKEAVKYIKEHlSISVDNlgKESLINVAKTSmsskiIGADSDFfA 161
|
170
....*....|
gi 1252004249 184 NIISDAMKKV 193
Cdd:cd03335 162 NMVVDAILAV 171
|
|
| TCP1_zeta |
cd03342 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
408-539 |
2.00e-06 |
|
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.
Pssm-ID: 239458 [Multi-domain] Cd Length: 484 Bit Score: 50.33 E-value: 2.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 408 GTSDVEVNEKKDRVTDALNATRAAVEEGIVLGGGCAL-LRCIPALDSLKP-ANEDQKIGIEIIKRALKIPAMTIAKNAGV 485
Cdd:cd03342 336 GPNDHTITQIKDAIRDGLRAVKNAIEDKCVVPGAGAFeVALYAHLKEFKKsVKGKAKLGVQAFADALLVIPKTLAENSGL 415
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1252004249 486 EGS----LIVEKILQSSSEVGYDAMLGDFVNMVEKGIIDPTKVVRTALLDAAGVASLL 539
Cdd:cd03342 416 DVQetlvKLQDEYAEGGQVGGVDLDTGEPMDPESEGIWDNYSVKRQILHSATVIASQL 473
|
|
| chap_CCT_zeta |
TIGR02347 |
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ... |
47-539 |
5.65e-06 |
|
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT zeta chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.
Pssm-ID: 274088 [Multi-domain] Cd Length: 531 Bit Score: 48.96 E-value: 5.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 47 LADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKdkykNIGAKLVQDVANNTNEEAGDGTTTATVLARSIAKE 126
Cdd:TIGR02347 28 LQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEMQIQ----HPTASMIARAATAQDDITGDGTTSTVLLIGELLKQ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 127 GFEKISKGANPVEIRRGVMLAVDAVIAELK--KQSKPVTTPEEIAQVATISANGDK-------DIGNIISDAMKKVGRKG 197
Cdd:TIGR02347 104 AERYILEGVHPRIITEGFEIARKEALQFLDkfKVKKEDEVDREFLLNVARTSLRTKlpadladQLTEIVVDAVLAIKKDG 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 198 ------VITVKDGKTLND-ELEIIEGMKFDRGYISPyfintskGQKCEFQDAYVLLS----EKKISSVQSivpALEIANA 266
Cdd:TIGR02347 184 edidlfMVEIMEMKHKSAtDTTLIRGLVLDHGARHP-------DMPRRVKNAYILTCnvslEYEKTEVNS---GFFYSSA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 267 HRKPLVIIAED--VDG------EALSTLVLNRLKVGLQVVAVK-----------APGFGDNRKNQLKDM---AIATGGav 324
Cdd:TIGR02347 254 EQREKLVKAERkfVDDrvkkiiELKKKVCGKSPDKGFVVINQKgidppsldllaKEGIMALRRAKRRNMerlTLACGG-- 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 325 fgeEGLNlNLEDVQAHDLGKVGEV--IVTKDDAMLLkgkgdkahiekrIQEITEQLDITtseyekeklnerlaklsdgva 402
Cdd:TIGR02347 332 ---EALN-SVEDLTPECLGWAGLVyeTTIGEEKYTF------------IEECKNPKSCT--------------------- 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 403 vLKVGGTSDVEVNEKKDRVTDALNATRAAVEEG-IVLGGGCALLRCIPALDSLKP-ANEDQKIGIEIIKRALKIPAMTIA 480
Cdd:TIGR02347 375 -ILIKGPNDHTIAQIKDAVRDGLRAVKNAIEDKcVVPGAGAFEIAAYRHLKEYKKsVKGKAKLGVEAFANALLVIPKTLA 453
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1252004249 481 KNAGVEGS----LIVEKILQSSSEVGYDAMLGDFVNMVEKGIIDPTKVVRTALLDAAGVASLL 539
Cdd:TIGR02347 454 ENSGFDAQdtlvKLEDEHDEGGEVVGVDLNTGEPIDPEIKGIWDNYRVKKQLIQSATVIASQL 516
|
|
| chap_CCT_theta |
TIGR02346 |
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ... |
47-221 |
2.37e-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: 47.02 E-value: 2.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 47 LADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDKykniGAKLVQDVANNTNEEAGDGTTTATVLARSIAKE 126
Cdd:TIGR02346 30 LSQITRTSLGPNGMNKMVINHLEKLFVTNDAATILRELEVQHP----AAKLLVMASEMQENEIGDGTNLVLVLAGELLNK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 127 GFEKISKGANPVEIRRGVMLAVDAVIAELKKQSK-PVTTPEEIAQV--ATISANGDKDIGN------IISDAM-----KK 192
Cdd:TIGR02346 106 AEELIRMGLHPSEIIKGYEMALKKAMEILEELVVwEVKDLRDKDELikALKASISSKQYGNedflaqLVAQACstvlpKN 185
|
170 180 190
....*....|....*....|....*....|..
gi 1252004249 193 VGRKGVITVKDGKTLNDEL---EIIEGMKFDR 221
Cdd:TIGR02346 186 PQNFNVDNIRVCKILGGSLsnsEVLKGMVFNR 217
|
|
| TCP1_theta |
cd03341 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ... |
47-171 |
7.31e-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: 42.21 E-value: 7.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252004249 47 LADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDKykniGAKLVQDVANNTNEEAGDGTTTATVLARSIAKE 126
Cdd:cd03341 20 LSQITRTSYGPNGMNKMVINHLEKLFVTSDAATILRELEVQHP----AAKLLVMASQMQEEEIGDGTNLVVVLAGELLEK 95
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1252004249 127 GFEKISKGANPVEIRRGVMLAVDAVIAELK----KQSKPVTTPEEIAQV 171
Cdd:cd03341 96 AEELLRMGLHPSEIIEGYEKALKKALEILEelvvYKIEDLRNKEEVSKA 144
|
|
| |
