|
Name |
Accession |
Description |
Interval |
E-value |
| GroEL |
cd03344 |
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ... |
4-524 |
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: 863.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 4 KDVKFGADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDKYKNIGAKLVQDVANNTNE 83
Cdd:cd03344 1 KDIKFGEEARKALLRGVNKLADAVKVTLGPKGRNVVIEKSFGSPKITKDGVTVAKEIELEDPFENMGAQLVKEVASKTND 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 84 EAGDGTTTATVLARSIAKEGFEKISKGANPVEIRRGVMLAVDAVIAELKKQSKPVTTPEEIAQVATISANGDKEIGNIIS 163
Cdd:cd03344 81 VAGDGTTTATVLARAIIKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKPVKTKEEIAQVATISANGDEEIGELIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 164 DAMKKVGRKGVITVKDGKTLNDELEIIEGMKFDRGYISPYFINTSKGQKCEFQDAYVLLSEKKISSIQSIVPALEIANAH 243
Cdd:cd03344 161 EAMEKVGKDGVITVEEGKTLETELEVVEGMQFDRGYLSPYFVTDPEKMEVELENPYILLTDKKISSIQELLPILELVAKA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 244 RKPLVIIAEDVDGEALSTLVLNRLKVGLQVVAVKAPGFGDNRKNQLKDMAIATGGAVFGEEgLTLNLEDVQPHDLGKVGE 323
Cdd:cd03344 241 GRPLLIIAEDVEGEALATLVVNKLRGGLKVCAVKAPGFGDRRKAMLEDIAILTGGTVISEE-LGLKLEDVTLEDLGRAKK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 324 VIVTKDDAMLLKGKGDKAQIEKRIQEIIEQLDVTTSEYEKEKLNERLAKLSDGVAVLKVGGTSDVEVNEKKDRVTDALNA 403
Cdd:cd03344 320 VVVTKDDTTIIGGAGDKAAIKARIAQIRKQIEETTSDYDKEKLQERLAKLSGGVAVIKVGGATEVELKEKKDRVEDALNA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 404 TRAAVEEGIVLGGGCALLRCIPALDSLTPANEDQKIGIEIIKRTLKIPAMTIAKNAGVEGSLIVEKIMQSSSEVGYDAMA 483
Cdd:cd03344 400 TRAAVEEGIVPGGGVALLRASPALDKLKALNGDEKLGIEIVRRALEAPLRQIAENAGVDGSVVVEKVLESPDGFGYDAAT 479
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1831502894 484 GDFVNMVEKGIIDPTKVVRTALLDAAGVASLLTTAEVVVTE 524
Cdd:cd03344 480 GEYVDMIEAGIIDPTKVVRSALQNAASVASLLLTTEALVVD 520
|
|
| PTZ00114 |
PTZ00114 |
Heat shock protein 60; Provisional |
2-528 |
0e+00 |
|
Heat shock protein 60; Provisional
Pssm-ID: 185455 Cd Length: 555 Bit Score: 762.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 2 SAKDVKFGADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDKYKNIGAKLVQDVANNT 81
Cdd:PTZ00114 13 KGKEIRFGDEARQSLLKGIERLADAVAVTLGPKGRNVIIEQEYGSPKITKDGVTVAKAIEFSDRFENVGAQLIRQVASKT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 82 NEEAGDGTTTATVLARSIAKEGFEKISKGANPVEIRRGVMLAVDAVIAELKKQSKPVTTPEEIAQVATISANGDKEIGNI 161
Cdd:PTZ00114 93 NDKAGDGTTTATILARAIFREGCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQSRPVKTKEDILNVATISANGDVEIGSL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 162 ISDAMKKVGRKGVITVKDGKTLNDELEIIEGMKFDRGYISPYFINTSKGQKCEFQDAYVLLSEKKISSIQSIVPALEIAN 241
Cdd:PTZ00114 173 IADAMDKVGKDGTITVEDGKTLEDELEVVEGMSFDRGYISPYFVTNEKTQKVELENPLILVTDKKISSIQSILPILEHAV 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 242 AHRKPLVIIAEDVDGEALSTLVLNRLKVGLQVVAVKAPGFGDNRKNQLKDMAIATGGAVFGEEGLTLNLEDVQPHDLGKV 321
Cdd:PTZ00114 253 KNKRPLLIIAEDVEGEALQTLIINKLRGGLKVCAVKAPGFGDNRKDILQDIAVLTGATVVSEDNVGLKLDDFDPSMLGSA 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 322 GEVIVTKDDAMLLKGKGDKAQIEKRIQEIIEQLDVTTSEYEKEKLNERLAKLSDGVAVLKVGGTSDVEVNEKKDRVTDAL 401
Cdd:PTZ00114 333 KKVTVTKDETVILTGGGDKAEIKERVELLRSQIERTTSEYDKEKLKERLAKLSGGVAVIKVGGASEVEVNEKKDRIEDAL 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 402 NATRAAVEEGIVLGGGCALLRCIPALDSLTPANE---DQKIGIEIIKRTLKIPAMTIAKNAGVEGSLIVEKIMQSS-SEV 477
Cdd:PTZ00114 413 NATRAAVEEGIVPGGGVALLRASKLLDKLEEDNEltpDQRTGVKIVRNALRLPTKQIAENAGVEGAVVVEKILEKKdPSF 492
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1831502894 478 GYDAMAGDFVNMVEKGIIDPTKVVRTALLDAAGVASLLTTAEVVVTEIPKE 528
Cdd:PTZ00114 493 GYDAQTGEYVNMFEAGIIDPTKVVRSALVDAASVASLMLTTEAAIVDLPKE 543
|
|
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
3-528 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 745.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 3 AKDVKFGADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDKYKNIGAKLVQDVANNTN 82
Cdd:PRK00013 2 AKDIKFGEDARRKLLRGVNKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDPFENMGAQLVKEVASKTN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 83 EEAGDGTTTATVLARSIAKEGFEKISKGANPVEIRRGVMLAVDAVIAELKKQSKPVTTPEEIAQVATISANGDKEIGNII 162
Cdd:PRK00013 82 DVAGDGTTTATVLAQAIVREGLKNVAAGANPMDLKRGIDKAVEAAVEELKKISKPVEDKEEIAQVATISANGDEEIGKLI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 163 SDAMKKVGRKGVITVKDGKTLNDELEIIEGMKFDRGYISPYFINTSKGQKCEFQDAYVLLSEKKISSIQSIVPALEIANA 242
Cdd:PRK00013 162 AEAMEKVGKEGVITVEESKGFETELEVVEGMQFDRGYLSPYFVTDPEKMEAELENPYILITDKKISNIQDLLPVLEQVAQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 243 HRKPLVIIAEDVDGEALSTLVLNRLKVGLQVVAVKAPGFGDNRKNQLKDMAIATGGAVFGEEgLTLNLEDVQPHDLGKVG 322
Cdd:PRK00013 242 SGKPLLIIAEDVEGEALATLVVNKLRGTLKVVAVKAPGFGDRRKAMLEDIAILTGGTVISEE-LGLKLEDATLEDLGQAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 323 EVIVTKDDAMLLKGKGDKAQIEKRIQEIIEQLDVTTSEYEKEKLNERLAKLSDGVAVLKVGGTSDVEVNEKKDRVTDALN 402
Cdd:PRK00013 321 KVVVTKDNTTIVDGAGDKEAIKARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATEVEMKEKKDRVEDALH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 403 ATRAAVEEGIVLGGGCALLRCIPALDSLTPANEDQKIGIEIIKRTLKIPAMTIAKNAGVEGSLIVEKIMQSSSE-VGYDA 481
Cdd:PRK00013 401 ATRAAVEEGIVPGGGVALLRAAPALEALKGLNGDEATGINIVLRALEAPLRQIAENAGLEGSVVVEKVKNGKGKgYGYNA 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1831502894 482 MAGDFVNMVEKGIIDPTKVVRTALLDAAGVASLLTTAEVVVTEIPKE 528
Cdd:PRK00013 481 ATGEYVDMIEAGIIDPTKVTRSALQNAASVAGLLLTTEAVVADKPEK 527
|
|
| groEL |
PRK12849 |
chaperonin GroEL; Reviewed |
3-528 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237230 Cd Length: 542 Bit Score: 704.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 3 AKDVKFGADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDKYKNIGAKLVQDVANNTN 82
Cdd:PRK12849 2 AKIIKFDEEARRALERGVNKLADAVKVTLGPKGRNVVIDKSFGAPTITKDGVSIAKEIELEDPFENLGAQLVKEVASKTN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 83 EEAGDGTTTATVLARSIAKEGFEKISKGANPVEIRRGVMLAVDAVIAELKKQSKPVTTPEEIAQVATISANGDKEIGNII 162
Cdd:PRK12849 82 DVAGDGTTTATVLAQALVQEGLKNVAAGANPMDLKRGIDKAVEAVVEELKALARPVSGSEEIAQVATISANGDEEIGELI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 163 SDAMKKVGRKGVITVKDGKTLNDELEIIEGMKFDRGYISPYFINTSKGQKCEFQDAYVLLSEKKISSIQSIVPALEIANA 242
Cdd:PRK12849 162 AEAMEKVGKDGVITVEESKTLETELEVTEGMQFDRGYLSPYFVTDPERMEAVLEDPLILLTDKKISSLQDLLPLLEKVAQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 243 HRKPLVIIAEDVDGEALSTLVLNRLKVGLQVVAVKAPGFGDNRKNQLKDMAIATGGAVFGEEgLTLNLEDVQPHDLGKVG 322
Cdd:PRK12849 242 SGKPLLIIAEDVEGEALATLVVNKLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGTVISED-LGLKLEEVTLDDLGRAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 323 EVIVTKDDAMLLKGKGDKAQIEKRIQEIIEQLDVTTSEYEKEKLNERLAKLSDGVAVLKVGGTSDVEVNEKKDRVTDALN 402
Cdd:PRK12849 321 RVTITKDNTTIVDGAGDKEAIEARVAQIRRQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATEVELKERKDRVEDALN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 403 ATRAAVEEGIVLGGGCALLRCIPALDSLTPANEDQKIGIEIIKRTLKIPAMTIAKNAGVEGSLIVEKIMQSSSEVGYDAM 482
Cdd:PRK12849 401 ATRAAVEEGIVPGGGVALLRAAKALDELAGLNGDQAAGVEIVRRALEAPLRQIAENAGLDGSVVVAKVLELEDGFGFNAA 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1831502894 483 AGDFVNMVEKGIIDPTKVVRTALLDAAGVASLLTTAEVVVTEIPKE 528
Cdd:PRK12849 481 TGEYGDLIAAGIIDPVKVTRSALQNAASVAGLLLTTEALVADKPEE 526
|
|
| GroEL |
TIGR02348 |
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ... |
3-527 |
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: 681.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 3 AKDVKFGADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDKYKNIGAKLVQDVANNTN 82
Cdd:TIGR02348 1 AKQIKFDEEARKALLRGVDKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDKFENMGAQLVKEVASKTN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 83 EEAGDGTTTATVLARSIAKEGFEKISKGANPVEIRRGVMLAVDAVIAELKKQSKPVTTPEEIAQVATISANGDKEIGNII 162
Cdd:TIGR02348 81 DVAGDGTTTATVLAQAIVKEGLKNVAAGANPIELKRGIEKAVEAVVEELKKLSKPVKGKKEIAQVATISANNDEEIGSLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 163 SDAMKKVGRKGVITVKDGKTLNDELEIIEGMKFDRGYISPYFINTSKGQKCEFQDAYVLLSEKKISSIQSIVPALEIANA 242
Cdd:TIGR02348 161 AEAMEKVGKDGVITVEESKSLETELEVVEGMQFDRGYISPYFVTDAEKMEVELENPYILITDKKISNIKDLLPLLEKVAQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 243 HRKPLVIIAEDVDGEALSTLVLNRLKVGLQVVAVKAPGFGDNRKNQLKDMAIATGGAVFGEEgLTLNLEDVQPHDLGKVG 322
Cdd:TIGR02348 241 SGKPLLIIAEDVEGEALATLVVNKLRGTLNVCAVKAPGFGDRRKAMLEDIAILTGGQVISEE-LGLKLEEVTLDDLGKAK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 323 EVIVTKDDAMLLKGKGDKAQIEKRIQEIIEQLDVTTSEYEKEKLNERLAKLSDGVAVLKVGGTSDVEVNEKKDRVTDALN 402
Cdd:TIGR02348 320 KVTVDKDNTTIVEGAGDKAAIKARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATETEMKEKKLRIEDALN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 403 ATRAAVEEGIVLGGGCALLRCIPALDSLTPANEDQKIGIEIIKRTLKIPAMTIAKNAGVEGSLIVEKIMQSSSEVGYDAM 482
Cdd:TIGR02348 400 ATRAAVEEGIVPGGGVALLRAAAALEGLKGDGEDEAIGIDIVKRALEAPLRQIAENAGLDGAVVAEKVKELKGNFGFNAA 479
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1831502894 483 AGDFVNMVEKGIIDPTKVVRTALLDAAGVASLLTTAEVVVTEIPK 527
Cdd:TIGR02348 480 TGEYEDLVEAGIIDPTKVTRSALQNAASIAGLLLTTEAVVADKPE 524
|
|
| groEL |
PRK12850 |
chaperonin GroEL; Reviewed |
2-528 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237231 Cd Length: 544 Bit Score: 675.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 2 SAKDVKFGADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDKYKNIGAKLVQDVANNT 81
Cdd:PRK12850 2 AAKEIRFSTDARDRLLRGVNILANAVKVTLGPKGRNVVLEKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVKEVASKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 82 NEEAGDGTTTATVLARSIAKEGFEKISKGANPVEIRRGVMLAVDAVIAELKKQSKPVTTPEEIAQVATISANGDKEIGNI 161
Cdd:PRK12850 82 NDLAGDGTTTATVLAQAIVREGAKLVAAGMNPMDLKRGIDLAVAAVVDELKKIAKKVTSSKEIAQVATISANGDESIGEM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 162 ISDAMKKVGRKGVITVKDGKTLNDELEIIEGMKFDRGYISPYFINTSKGQKCEFQDAYVLLSEKKISSIQSIVPALEIAN 241
Cdd:PRK12850 162 IAEAMDKVGKEGVITVEEAKTLGTELDVVEGMQFDRGYLSPYFVTNPEKMRAELEDPYILLHEKKISNLQDLLPILEAVV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 242 AHRKPLVIIAEDVDGEALSTLVLNRLKVGLQVVAVKAPGFGDNRKNQLKDMAIATGGAVFGEEgLTLNLEDVQPHDLGKV 321
Cdd:PRK12850 242 QSGRPLLIIAEDVEGEALATLVVNKLRGGLKSVAVKAPGFGDRRKAMLEDIAVLTGGQVISED-LGIKLENVTLDMLGRA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 322 GEVIVTKDDAMLLKGKGDKAQIEKRIQEIIEQLDVTTSEYEKEKLNERLAKLSDGVAVLKVGGTSDVEVNEKKDRVTDAL 401
Cdd:PRK12850 321 KRVLITKENTTIIDGAGDKKNIEARVKQIRAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKEKKDRVDDAL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 402 NATRAAVEEGIVLGGGCALLRCIPALDSLTPANEDQKIGIEIIKRTLKIPAMTIAKNAGVEGSLIVEKIMQSSSEVGYDA 481
Cdd:PRK12850 401 HATRAAVEEGIVPGGGVALLRARSALRGLKGANADETAGIDIVRRALEEPLRQIATNAGFEGSVVVGKVAELPGNFGFNA 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1831502894 482 MAGDFVNMVEKGIIDPTKVVRTALLDAAGVASLLTTAEVVVTEIPKE 528
Cdd:PRK12850 481 QTGEYGDMVEAGIIDPAKVTRTALQDAASIAALLITTEAMVAEAPKK 527
|
|
| groEL |
PRK12852 |
chaperonin GroEL; Reviewed |
2-528 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237232 Cd Length: 545 Bit Score: 637.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 2 SAKDVKFGADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDKYKNIGAKLVQDVANNT 81
Cdd:PRK12852 2 AAKDVKFSGDARDRMLRGVDILANAVKVTLGPKGRNVVIEKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVREVASKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 82 NEEAGDGTTTATVLARSIAKEGFEKISKGANPVEIRRGVMLAVDAVIAELKKQSKPVTTPEEIAQVATISANGDKEIGNI 161
Cdd:PRK12852 82 NDLAGDGTTTATVLAQAIVREGAKAVAAGMNPMDLKRGIDIAVAAVVKDIEKRAKPVASSAEIAQVGTISANGDAAIGKM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 162 ISDAMKKVGRKGVITVKDGKTLNDELEIIEGMKFDRGYISPYFINTSKGQKCEFQDAYVLLSEKKISSIQSIVPALEIAN 241
Cdd:PRK12852 162 IAQAMQKVGNEGVITVEENKSLETEVDIVEGMKFDRGYLSPYFVTNAEKMTVELDDAYILLHEKKLSGLQAMLPVLEAVV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 242 AHRKPLVIIAEDVDGEALSTLVLNRLKVGLQVVAVKAPGFGDNRKNQLKDMAIATGGAVFGEEgLTLNLEDVQPHDLGKV 321
Cdd:PRK12852 242 QSGKPLLIIAEDVEGEALATLVVNRLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGQLISED-LGIKLENVTLKMLGRA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 322 GEVIVTKDDAMLLKGKGDKAQIEKRIQEIIEQLDVTTSEYEKEKLNERLAKLSDGVAVLKVGGTSDVEVNEKKDRVTDAL 401
Cdd:PRK12852 321 KKVVIDKENTTIVNGAGKKADIEARVGQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKEKKDRVEDAL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 402 NATRAAVEEGIVLGGGCALLRCIPALDSLTPANEDQKIGIEIIKRTLKIPAMTIAKNAGVEGSLIVEKIMQSSSEV-GYD 480
Cdd:PRK12852 401 NATRAAVQEGIVPGGGVALLRAKKAVGRINNDNADVQAGINIVLKALEAPIRQIAENAGVEGSIVVGKILENKSETfGFD 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1831502894 481 AMAGDFVNMVEKGIIDPTKVVRTALLDAAGVASLLTTAEVVVTEIPKE 528
Cdd:PRK12852 481 AQTEEYVDMVAKGIIDPAKVVRTALQDAASVAGLLVTTEAMVAELPKK 528
|
|
| groEL |
PRK12851 |
chaperonin GroEL; Reviewed |
2-528 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 171770 Cd Length: 541 Bit Score: 627.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 2 SAKDVKFGADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDKYKNIGAKLVQDVANNT 81
Cdd:PRK12851 2 AAKEVKFHVEAREKMLRGVNILADAVKVTLGPKGRNVVIDKSFGAPTITNDGVTIAKEIELEDKFENMGAQMVREVASKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 82 NEEAGDGTTTATVLARSIAKEGFEKISKGANPVEIRRGVMLAVDAVIAELKKQSKPVTTPEEIAQVATISANGDKEIGNI 161
Cdd:PRK12851 82 NDVAGDGTTTATVLAQAIVREGAKAVAAGANPMDLKRGIDRAVAAVVEELKANARPVTTNAEIAQVATISANGDAEIGRL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 162 ISDAMKKVGRKGVITVKDGKTLNDELEIIEGMKFDRGYISPYFINTSKGQKCEFQDAYVLLSEKKISSIQSIVPALEIAN 241
Cdd:PRK12851 162 VAEAMEKVGNEGVITVEESKTAETELEVVEGMQFDRGYLSPYFVTDADKMEAELEDPYILIHEKKISNLQDLLPVLEAVV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 242 AHRKPLVIIAEDVDGEALSTLVLNRLKVGLQVVAVKAPGFGDNRKNQLKDMAIATGGAVFGEEgLTLNLEDVQPHDLGKV 321
Cdd:PRK12851 242 QSGKPLLIIAEDVEGEALATLVVNKLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGTVISED-LGIKLENVTLEQLGRA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 322 GEVIVTKDDAMLLKGKGDKAQIEKRIQEIIEQLDVTTSEYEKEKLNERLAKLSDGVAVLKVGGTSDVEVNEKKDRVTDAL 401
Cdd:PRK12851 321 KKVVVEKENTTIIDGAGSKTEIEGRVAQIRAQIEETTSDYDREKLQERLAKLAGGVAVIRVGASTEVEVKEKKDRVDDAL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 402 NATRAAVEEGIVLGGGCALLRCIPALDSLTPANEDQKIGIEIIKRTLKIPAMTIAKNAGVEGSLIVEKIMQSSSEVGYDA 481
Cdd:PRK12851 401 HATRAAVEEGIVPGGGVALLRAVKALDKLETANGDQRTGVEIVRRALEAPVRQIAENAGAEGSVVVGKLREKPGGYGFNA 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1831502894 482 MAGDFVNMVEKGIIDPTKVVRTALLDAAGVASLLTTAEVVVTEIPKE 528
Cdd:PRK12851 481 ATNEYGDLYAQGVIDPVKVVRTALQNAASVAGLLLTTEAMVAEKPKK 527
|
|
| GroEL |
COG0459 |
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ... |
3-528 |
0e+00 |
|
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227 Cd Length: 497 Bit Score: 619.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 3 AKDVKFGADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDKYKNIGAKLVQDVANNTN 82
Cdd:COG0459 2 AKQILFGEDARRANIRGVKALADAVKVTLGPKGRNVMLVKSFGDPTITNDGVTIAKEIELEDPFENMGAQLVKEVASKTN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 83 EEAGDGTTTATVLARSIAKEGFEKISKGANPVEIRRGVMLAVDAVIAELKKQSKPVTTPEEIAQVATISANGDKEIGNII 162
Cdd:COG0459 82 DEAGDGTTTATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPVDDKEELAQVATISANGDEEIGELI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 163 SDAMKKVGRKGVITVKDGKTLNDELEIIEGMKFDRGYISPYFINTSKGQKCEFQDAYVLLSEKKISSIQSIVPALEIANA 242
Cdd:COG0459 162 AEAMEKVGKDGVITVEEGKGLETELEVVEGMQFDKGYLSPYFVTDPEKMPAELENAYILLTDKKISSIQDLLPLLEKVAQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 243 HRKPLVIIAEDVDGEALSTLVLNRLKVGLQVVAVKAPGFGDNRKNQLKDMAIATGGAVFGEEgLTLNLEDVQPHDLGKVG 322
Cdd:COG0459 242 SGKPLLIIAEDIDGEALATLVVNGIRGVLRVVAVKAPGFGDRRKAMLEDIAILTGGRVISED-LGLKLEDVTLDDLGRAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 323 EVIVTKDDAMLLKGKGDKAQIekriqeiieqldvttseyekeklnerlaklsdgvaVLKVGGTSDVEVNEKKDRVTDALN 402
Cdd:COG0459 321 RVEVDKDNTTIVEGAGNPKAI-----------------------------------VILVGAATEVEVKERKRRVEDALH 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 403 ATRAAVEEGIVLGGGCALLRCIPALDSLTPANE-DQKIGIEIIKRTLKIPAMTIAKNAGVEGSLIVEKIMQSSSE-VGYD 480
Cdd:COG0459 366 ATRAAVEEGIVPGGGAALLRAARALRELAAKLEgDEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKVRAAKDKgFGFD 445
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1831502894 481 AMAGDFVNMVEKGIIDPTKVVRTALLDAAGVASLLTTAEVVVTEIPKE 528
Cdd:COG0459 446 AATGEYVDMLEAGVIDPAKVKRSALQNAASVAGLILTTEAVIADKPEK 493
|
|
| PRK14104 |
PRK14104 |
chaperonin GroEL; Provisional |
2-528 |
0e+00 |
|
chaperonin GroEL; Provisional
Pssm-ID: 172594 Cd Length: 546 Bit Score: 577.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 2 SAKDVKFGADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDKYKNIGAKLVQDVANNT 81
Cdd:PRK14104 2 SAKEVKFGVDARDRMLRGVDILANAVKVTLGPKGRNVVLDKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVREVASKS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 82 NEEAGDGTTTATVLARSIAKEGFEKISKGANPVEIRRGVMLAVDAVIAELKKQSKPVTTPEEIAQVATISANGDKEIGNI 161
Cdd:PRK14104 82 ADAAGDGTTTATVLAQAIVREGAKSVAAGMNPMDLKRGIDLAVEAVVADLVKNSKKVTSNDEIAQVGTISANGDAEIGKF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 162 ISDAMKKVGRKGVITVKDGKTLNDELEIIEGMKFDRGYISPYFINTSKGQKCEFQDAYVLLSEKKISSIQSIVPALEIAN 241
Cdd:PRK14104 162 LADAMKKVGNEGVITVEEAKSLETELDVVEGMQFDRGYISPYFVTNADKMRVEMDDAYILINEKKLSSLNELLPLLEAVV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 242 AHRKPLVIIAEDVDGEALSTLVLNRLKVGLQVVAVKAPGFGDNRKNQLKDMAIATGGAVFGEEgLTLNLEDVQPHDLGKV 321
Cdd:PRK14104 242 QTGKPLVIVAEDVEGEALATLVVNRLRGGLKVAAVKAPGFGDRRKAMLQDIAILTGGQAISED-LGIKLENVTLQMLGRA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 322 GEVIVTKDDAMLLKGKGDKAQIEKRIQEIIEQLDVTTSEYEKEKLNERLAKLSDGVAVLKVGGTSDVEVNEKKDRVTDAL 401
Cdd:PRK14104 321 KKVMIDKENTTIVNGAGKKADIEARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKERKDRVDDAM 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 402 NATRAAVEEGIVLGGGCALLRCIPALDSLTPANEDQKIGIEIIKRTLKIPAMTIAKNAGVEGSLIVEKIMQSSS-EVGYD 480
Cdd:PRK14104 401 HATRAAVEEGIVPGGGVALLRASEQLKGIKTKNDDQKTGVEIVRKALSAPARQIAINAGEDGSVIVGKILEKEQySYGFD 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1831502894 481 AMAGDFVNMVEKGIIDPTKVVRTALLDAAGVASLLTTAEVVVTEIPKE 528
Cdd:PRK14104 481 SQTGEYGNLVSKGIIDPTKVVRTAIQNAASVAALLITTEAMVAELPKK 528
|
|
| groEL |
CHL00093 |
chaperonin GroEL |
3-528 |
0e+00 |
|
chaperonin GroEL
Pssm-ID: 177025 Cd Length: 529 Bit Score: 531.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 3 AKDVKFGADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDKYKNIGAKLVQDVANNTN 82
Cdd:CHL00093 2 SKKILYQDNARRALERGMDILAEAVSVTLGPKGRNVVLEKKYGSPQIVNDGVTIAKEIELEDHIENTGVALIRQAASKTN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 83 EEAGDGTTTATVLARSIAKEGFEKISKGANPVEIRRGVMLAVDAVIAELKKQSKPVTTPEEIAQVATISANGDKEIGNII 162
Cdd:CHL00093 82 DVAGDGTTTATVLAYAIVKQGMKNVAAGANPISLKRGIEKATQYVVSQIAEYARPVEDIQAITQVASISAGNDEEVGSMI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 163 SDAMKKVGRKGVITVKDGKTLNDELEIIEGMKFDRGYISPYFINTSKGQKCEFQDAYVLLSEKKISSI-QSIVPALEIAN 241
Cdd:CHL00093 162 ADAIEKVGREGVISLEEGKSTVTELEITEGMRFEKGFISPYFVTDTERMEVVQENPYILLTDKKITLVqQDLLPILEQVT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 242 AHRKPLVIIAEDVDGEALSTLVLNRLKVGLQVVAVKAPGFGDNRKNQLKDMAIATGGAVFGEEgLTLNLEDVQPHDLGKV 321
Cdd:CHL00093 242 KTKRPLLIIAEDVEKEALATLVLNKLRGIVNVVAVRAPGFGDRRKAMLEDIAILTGGQVITED-AGLSLETIQLDLLGQA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 322 GEVIVTKDDAMLLkGKGDKAQIEKRIQEIIEQLDVTTSEYEKEKLNERLAKLSDGVAVLKVGGTSDVEVNEKKDRVTDAL 401
Cdd:CHL00093 321 RRIIVTKDSTTII-ADGNEEQVKARCEQLRKQIEIADSSYEKEKLQERLAKLSGGVAVIKVGAATETEMKDKKLRLEDAI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 402 NATRAAVEEGIVLGGGCALLRCIPALDSLTPAN--EDQKIGIEIIKRTLKIPAMTIAKNAGVEGSLIVEKIMQSSSEVGY 479
Cdd:CHL00093 400 NATKAAVEEGIVPGGGATLVHLSENLKTWAKNNlkEDELIGALIVARAILAPLKRIAENAGKNGSVIIEKVQEQDFEIGY 479
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1831502894 480 DAMAGDFVNMVEKGIIDPTKVVRTALLDAAGVASLLTTAEVVVTEIPKE 528
Cdd:CHL00093 480 NAANNKFVNMYEAGIIDPAKVTRSALQNAASIASMILTTECIIVDKKES 528
|
|
| PLN03167 |
PLN03167 |
Chaperonin-60 beta subunit; Provisional |
2-527 |
3.26e-166 |
|
Chaperonin-60 beta subunit; Provisional
Pssm-ID: 215611 [Multi-domain] Cd Length: 600 Bit Score: 484.04 E-value: 3.26e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 2 SAKDVKFGADARAL--MLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDKYKNIGAKLVQDVAN 79
Cdd:PLN03167 55 AAKELHFNKDGSAIkkLQAGVNKLADLVGVTLGPKGRNVVLESKYGSPKIVNDGVTVAKEVELEDPVENIGAKLVRQAAA 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 80 NTNEEAGDGTTTATVLARSIAKEGFEKISKGANPVEIRRGVMLAVDAVIAELKKQSKPVTTpEEIAQVATISANGDKEIG 159
Cdd:PLN03167 135 KTNDLAGDGTTTSVVLAQGLIAEGVKVVAAGANPVQITRGIEKTAKALVKELKKMSKEVED-SELADVAAVSAGNNYEVG 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 160 NIISDAMKKVGRKGVITVKDGKTLNDELEIIEGMKFDRGYISPYFINTSKGQKCEFQDAYVLLSEKKISSIQSIVPALEI 239
Cdd:PLN03167 214 NMIAEAMSKVGRKGVVTLEEGKSAENNLYVVEGMQFDRGYISPYFVTDSEKMSVEYDNCKLLLVDKKITNARDLIGILED 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 240 ANAHRKPLVIIAEDVDGEALSTLVLNRLKVGLQVVAVKAPGFGDNRKNQLKDMAIATGGAVFGEEgLTLNLEDVQPHDLG 319
Cdd:PLN03167 294 AIRGGYPLLIIAEDIEQEALATLVVNKLRGSLKIAALKAPGFGERKSQYLDDIAILTGGTVIREE-VGLSLDKVGKEVLG 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 320 KVGEVIVTKDDAMLLKGKGDKAQIEKRIQEIIEQLDVTTSEYEKEKLNERLAKLSDGVAVLKVGGTSDVEVNEKKDRVTD 399
Cdd:PLN03167 373 TAAKVVLTKDTTTIVGDGSTQEAVNKRVAQIKNLIEAAEQDYEKEKLNERIAKLSGGVAVIQVGAQTETELKEKKLRVED 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 400 ALNATRAAVEEGIVLGGGCALLRCIPALDSL--TPANEDQKIGIEIIKRTLKIPAMTIAKNAGVEGSLIVEKIMQSSS-E 476
Cdd:PLN03167 453 ALNATKAAVEEGIVVGGGCTLLRLASKVDAIkdTLENDEQKVGADIVKRALSYPLKLIAKNAGVNGSVVSEKVLSNDNpK 532
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1831502894 477 VGYDAMAGDFVNMVEKGIIDPTKVVRTALLDAAGVASLLTTAEVVVTEIPK 527
Cdd:PLN03167 533 FGYNAATGKYEDLMAAGIIDPTKVVRCCLEHAASVAKTFLTSDCVVVEIKE 583
|
|
| chaperonin_type_I_II |
cd00309 |
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ... |
4-523 |
4.53e-145 |
|
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: 424.92 E-value: 4.53e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 4 KDVKFGADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKdkykNIGAKLVQDVANNTNE 83
Cdd:cd00309 1 KEREFGEEARLSNINAAKALADAVKTTLGPKGMDKMLVDSLGDPTITNDGATILKEIEVE----HPAAKLLVEVAKSQDD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 84 EAGDGTTTATVLARSIAKEGFEKISKGANPVEIRRGVMLAVDAVIAELKKQSKP--VTTPEEIAQVATISAN------GD 155
Cdd:cd00309 77 EVGDGTTTVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVPidVEDREELLKVATTSLNsklvsgGD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 156 KEIGNIISDAMKKVGR------KGVITVKDGKTLN-DELEIIEGMKFDRGYISPYFintskgqKCEFQDAYVLLSEKKIS 228
Cdd:cd00309 157 DFLGELVVDAVLKVGKengdvdLGVIRVEKKKGGSlEDSELVVGMVFDKGYLSPYM-------PKRLENAKILLLDCKLE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 229 SiqsivpaleianahrkplVIIAED-VDGEALSTLVLnrlkvgLQVVAVKApgfgdNRKNQLKDMAIATGGAVFGEeglt 307
Cdd:cd00309 230 Y------------------VVIAEKgIDDEALHYLAK------LGIMAVRR-----VRKEDLERIAKATGATIVSR---- 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 308 lnLEDVQPHDLGKVGEVIVTKddamllkgkgdkaqiekriqeiIEQLDVTTSEYEKEKlnerlaklsdGVAVLKVGGTSD 387
Cdd:cd00309 277 --LEDLTPEDLGTAGLVEETK----------------------IGDEKYTFIEGCKGG----------KVATILLRGATE 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 388 VEVNEKKDRVTDALNATRAAVEE-GIVLGGGCALLRCIPALDSLTP-ANEDQKIGIEIIKRTLKIPAMTIAKNAGVEGSL 465
Cdd:cd00309 323 VELDEAERSLHDALCAVRAAVEDgGIVPGGGAAEIELSKALEELAKtLPGKEQLGIEAFADALEVIPRTLAENAGLDPIE 402
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1831502894 466 IVEKIMQSSSEVGYDA----MAGDFVNMVEKGIIDPTKVVRTALLDAAGVASLLTTAEVVVT 523
Cdd:cd00309 403 VVTKLRAKHAEGGGNAggdvETGEIVDMKEAGIIDPLKVKRQALKSATEAASLILTIDDIIV 464
|
|
| Cpn60_TCP1 |
pfam00118 |
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ... |
23-523 |
1.03e-67 |
|
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: 226.31 E-value: 1.03e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 23 LADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDKYknigAKLVQDVANNTNEEAGDGTTTATVLARSIAKE 102
Cdd:pfam00118 1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELEIQHPA----AKLLVEAAKAQDEEVGDGTTTVVVLAGELLEE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 103 GFEKISKGANPVEIRRGVMLAVDAVIAELK-KQSKPVTTP--EEIAQVATISANGD------KEIGNIISDAMK------ 167
Cdd:pfam00118 77 AEKLLAAGVHPTTIIEGYEKALEKALEILDsIISIPVEDVdrEDLLKVARTSLSSKiisresDFLAKLVVDAVLaipknd 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 168 ---KVGRKGVITVKDGKTlnDELEIIEGMKFDRGYISPyfintskGQKCEFQDAYVLLSEKKISSIQSIVPA-------- 236
Cdd:pfam00118 157 gsfDLGNIGVVKILGGSL--EDSELVDGVVLDKGPLHP-------DMPKRLENAKVLLLNCSLEYEKTETKAtvvlsdae 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 237 --LEIANAHRK--------------PLVIIAEDVDGEALSTLVLNRLkVGLQVVavkapgfgdnRKNQLKDMAIATGGAV 300
Cdd:pfam00118 228 qlERFLKAEEEqileivekiidsgvNVVVCQKGIDDLALHFLAKNGI-MALRRV----------KKRDLERLAKATGARA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 301 FGeegltlNLEDVQPHDLGKVG---EVIVTKDDAMLLKGKGDKaqiekriqeiieqldvttseyekeklnerlaklsdGV 377
Cdd:pfam00118 297 VS------SLDDLTPDDLGTAGkveEEKIGDEKYTFIEGCKSP-----------------------------------KA 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 378 AVLKVGGTSDVEVNEKKDRVTDALNATRAAVEE-GIVLGGGCALLRCIPALDSLTPA-NEDQKIGIEIIKRTLKIPAMTI 455
Cdd:pfam00118 336 ATILLRGATDHVLDEIERSIHDALCVVKNAIEDpRVVPGGGAVEMELARALREYAKSvSGKEQLAIEAFAEALEVIPKTL 415
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1831502894 456 AKNAGVEGSLIVEKIM----QSSSEVGYDAMAGDFVNMVEKGIIDPTKVVRTALLDAAGVAS-LLTTAEVVVT 523
Cdd:pfam00118 416 AENAGLDPIEVLAELRaahaSGEKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKSATEAAStILRIDDIIKA 488
|
|
| chaperonin_like |
cd03333 |
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ... |
142-410 |
2.45e-36 |
|
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: 134.13 E-value: 2.45e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 142 EEIAQVATISAN-----GDKEIGNIISDAMKKVGR------KGVITVKDGKTLN-DELEIIEGMKFDRGYISPYFintsk 209
Cdd:cd03333 2 ELLLQVATTSLNsklssWDDFLGKLVVDAVLKVGPdnrmddLGVIKVEKIPGGSlEDSELVVGVVFDKGYASPYM----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 210 gqKCEFQDAYVLLSEKKISSiqsivpaleianahrkplVIIAED-VDGEALSTLVLnrlkvgLQVVAVKApgfgdNRKNQ 288
Cdd:cd03333 77 --PKRLENAKILLLDCPLEY------------------VVIAEKgIDDLALHYLAK------AGIMAVRR-----VKKED 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 289 LKDMAIATGGAVFGEegltlnLEDVQPHDLGKVGEVIVTKDdamllkgkGDKAQIekriqeIIEQLDVTtseyekeklne 368
Cdd:cd03333 126 LERIARATGATIVSS------LEDLTPEDLGTAELVEETKI--------GEEKLT------FIEGCKGG----------- 174
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1831502894 369 rlaklsdGVAVLKVGGTSDVEVNEKKDRVTDALNATRAAVEE 410
Cdd:cd03333 175 -------KAATILLRGATEVELDEVKRSLHDALCAVRAAVEE 209
|
|
| cpn60 |
cd03343 |
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ... |
9-515 |
5.44e-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: 96.18 E-value: 5.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 9 GADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKdkykNIGAKLVQDVANNTNEEAGDG 88
Cdd:cd03343 13 GRDAQRMNIAAAKAVAEAVRTTLGPKGMDKMLVDSLGDVTITNDGATILKEMDIE----HPAAKMLVEVAKTQDEEVGDG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 89 TTTATVLARSIAKEGFEKISKGANPVEIRRGVMLAVDAVIAELKKQSKPVTTPEE-----IAQVATISANGDKE---IGN 160
Cdd:cd03343 89 TTTAVVLAGELLEKAEDLLDQNIHPTVIIEGYRLAAEKALELLDEIAIKVDPDDKdtlrkIAKTSLTGKGAEAAkdkLAD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 161 IISDAMKKV--GRKGVITV---------KDGKTLNDElEIIEGMKFDRGYISPyfintskGQKCEFQDAyvllsekKISS 229
Cdd:cd03343 169 LVVDAVLQVaeKRDGKYVVdldnikiekKTGGSVDDT-ELIRGIVIDKEVVHP-------GMPKRVENA-------KIAL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 230 IQSivpALEIanahRKPlviiaeDVDGEalstlvlnrlkvgLQVVAV-KAPGFGDNRKNQLKDM--AIATGGA--VFGEE 304
Cdd:cd03343 234 LDA---PLEV----KKT------EIDAK-------------IRITSPdQLQAFLEQEEAMLKEMvdKIADTGAnvVFCQK 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 305 GltlnLEDVQPHDLGKVGEVIV--TKDDAMLLKGKGDKAQIEKRIQEIIEQLDVTTSEYEKEKLNE------RLAKLSDG 376
Cdd:cd03343 288 G----IDDLAQHYLAKAGILAVrrVKKSDMEKLARATGAKIVTNIDDLTPEDLGEAELVEERKVGDdkmvfvEGCKNPKA 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 377 VAVLKVGGTSDVeVNEKKDRVTDALNATRAAVEEG-IVLGGGCALLRCIPALDSLTPANE-DQKIGIEIIKRTLKIPAMT 454
Cdd:cd03343 364 VTILLRGGTEHV-VDELERALEDALRVVADALEDGkVVAGGGAVEIELAKRLREYARSVGgREQLAVEAFADALEEIPRT 442
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1831502894 455 IAKNAGVEGsliVEKIMQSSSE-------VGYDAMAGDFVNMVEKGIIDPTKVVRTALLDAAGVASLL 515
Cdd:cd03343 443 LAENAGLDP---IDTLVELRAAhekgnknAGLDVYTGEVVDMLEKGVIEPLRVKKQAIKSATEAATMI 507
|
|
| TCP1_beta |
cd03336 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ... |
9-515 |
1.52e-13 |
|
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.
Pssm-ID: 239452 [Multi-domain] Cd Length: 517 Bit Score: 72.75 E-value: 1.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 9 GADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSW--GSPKVTKDGVTVAKSIDLKdkykNIGAKLVQDVANNTNEEAG 86
Cdd:cd03336 11 GETARLSSFVGAIAIGDLVKTTLGPKGMDKILQSVGrsGGVTVTNDGATILKSIGVD----NPAAKVLVDISKVQDDEVG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 87 DGTTTATVLARSIAKEGFEKISKGANPVEIRRGVMLAVDAVIAELKK-----QSKPVTTPEEIAQVA--TISA---NGDK 156
Cdd:cd03336 87 DGTTSVTVLAAELLREAEKLVAQKIHPQTIIEGYRMATAAAREALLSsavdhSSDEEAFREDLLNIArtTLSSkilTQDK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 157 E-IGNIISDAMKKVGRKG-----VITVKDGKTLNDELeiiegmkFDRGYISPYFINTskGQKCEFQDAYVLLS-----EK 225
Cdd:cd03336 167 EhFAELAVDAVLRLKGSGnldaiQIIKKLGGSLKDSY-------LDEGFLLDKKIGV--NQPKRIENAKILIAntpmdTD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 226 KIS------SIQSIVPALEIANAHRKPLV-----IIAEDVDGEALSTLVLNrlkVGLQVvavkapgFGDNRKnqlkdMAI 294
Cdd:cd03336 238 KIKifgakvRVDSTAKVAEIEEAEKEKMKnkvekILKHGINCFINRQLIYN---YPEQL-------FADAGI-----MAI 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 295 ATggAVF-GEEGLTLNLEdvqphdlgkvGEVIVTKDDAMLLK-GKGDKaqiekrIQEIIEQldvttseyekeklNERLAK 372
Cdd:cd03336 303 EH--ADFdGVERLALVTG----------GEIASTFDHPELVKlGTCKL------IEEIMIG-------------EDKLIR 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 373 LSdGVA-------VLKvgGTSDVEVNEKKDRVTDALNATRAAVEEG-IVLGGGCALLRCIPALDSLTPANEDQK-IGIEI 443
Cdd:cd03336 352 FS-GVAageactiVLR--GASQQILDEAERSLHDALCVLAQTVKDTrVVLGGGCSEMLMAKAVEELAKKTPGKKsLAIEA 428
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1831502894 444 IKRTLKIPAMTIAKNAGVEGSLIVEKI----MQSSSEVGYDAMAGDFVNMVEKGIIDPTKVVRTALLDAAGVASLL 515
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 ... |
9-527 |
2.21e-12 |
|
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT beta chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.
Pssm-ID: 274082 Cd Length: 519 Bit Score: 69.12 E-value: 2.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 9 GADARALMLQGVDLLADAVAVTMGPKGRTVIIEQ--SWGSPKVTKDGVTVAKSIDLKdkykNIGAKLVQDVANNTNEEAG 86
Cdd:TIGR02341 12 AENARLSSFVGAIAIGDLVKSTLGPKGMDKILQSssSDASIMVTNDGATILKSIGVD----NPAAKVLVDMSKVQDDEVG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 87 DGTTTATVLARSIAKEGFEKISKGANPVEIRRGVMLAVDAVIAELKKQS-----KPVTTPEEIAQVA--TISAngdkEIG 159
Cdd:TIGR02341 88 DGTTSVTVLAAELLREAEKLINQKIHPQTIIAGYREATKAARDALLKSAvdngsDEVKFRQDLMNIArtTLSS----KIL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 160 NIISDAMKKVGRKGVITVKdGKTLNDELEIIE--GMKFDRGYISPYFINTSK---GQKCEFQDAYVLLSEKKISS----- 229
Cdd:TIGR02341 164 SQHKDHFAQLAVDAVLRLK-GSGNLEAIQIIKklGGSLADSYLDEGFLLDKKigvNQPKRIENAKILIANTGMDTdkvki 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 230 ------IQSIVPALEIANAHRKPLVIIAEDVDGEALSTLVLNRLkvglqVVAVKAPGFGDnrknqLKDMAIATGgavfge 303
Cdd:TIGR02341 243 fgsrvrVDSTAKVAELEHAEKEKMKEKVEKILKHGINCFINRQL-----IYNYPEQLFAD-----AGVMAIEHA------ 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 304 egltlNLEDVQPHDLGKVGEVIVTKDDAMLLK-GKGDKaqiekrIQEIIEQldvttseyEKEKLNERLAKLSDGVAVLKV 382
Cdd:TIGR02341 307 -----DFEGVERLALVTGGEIVSTFDHPELVKlGSCDL------IEEIMIG--------EDKLLKFSGVKLGEACTIVLR 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 383 GGTSDVeVNEKKDRVTDALNATRAAVEEG-IVLGGGCALLRCIPALDSLTPANEDQK-IGIEIIKRTLKIPAMTIAKNAG 460
Cdd:TIGR02341 368 GATQQI-LDEAERSLHDALCVLSQTVKESrTVLGGGCSEMLMSKAVTQEAQRTPGKEaLAVEAFARALRQLPTIIADNAG 446
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1831502894 461 VEGSLIVEKIMQSSSE----VGYDAMAGDFVNMVEKGIIDPTKVVRTALLDAAGVASLLTTAEVVVTEIPK 527
Cdd:TIGR02341 447 FDSAELVAQLRAAHYNgnttMGLDMNEGTIADMRQLGITESYKVKRAVVSSAAEAAEVILRVDNIIKAAPR 517
|
|
| chap_CCT_epsi |
TIGR02343 |
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ... |
9-497 |
2.96e-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: 69.06 E-value: 2.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 9 GADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDKYknigAKLVQDVANNTNEEAGDG 88
Cdd:TIGR02343 25 GLEAKKSNIAAAKSVASILRTSLGPKGMDKMLISPDGDITVTNDGATILSQMDVDNQI----AKLMVELSKSQDDEIGDG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 89 TTTATVLARSIAKEGFEKISKGANPVEIRRGVMLAVDAVIAELKKQSKPVTTPEEIAQV---ATISANGDKeIGNIISDA 165
Cdd:TIGR02343 101 TTGVVVLAGALLEQAEELLDKGIHPIKIADGFEEAARIAVEHLEEISDEISADNNNREPliqAAKTSLGSK-IVSKCHRR 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 166 MKKVGRKGVITVKD-----------------GKTLNDElEIIEGMKFDRGYISPYFINTSKGQK-----CEFQ------- 216
Cdd:TIGR02343 180 FAEIAVDAVLNVADmerrdvdfdlikvegkvGGSLEDT-KLIKGIIIDKDFSHPQMPKEVEDAKiailtCPFEppkpktk 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 217 --------DAYVLLSEKKISSIQSIVPALEIANAHrkpLVIIAEDVDGEALSTLVLNRLKvglqvvAVKAPGfgdnrKNQ 288
Cdd:TIGR02343 259 hkldissvEEYKKLQKYEQQKFKEMIDDIKKSGAN---LVICQWGFDDEANHLLLQNDLP------AVRWVG-----GQE 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 289 LKDMAIATGGAVFGEegltlnLEDVQPHDLGKVGEV----IVTKDDAMLlkgkgdkaqiekriqeIIEQldvttseyeke 364
Cdd:TIGR02343 325 LELIAIATGGRIVPR------FQELSKDKLGKAGLVreisFGTTKDRML----------------VIEQ----------- 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 365 klnerlAKLSDGVAVLkVGGTSDVEVNEKKDRVTDALNATRAAVEEG-IVLGGGCALLRCIPALDsltpANEDQKIGIE- 442
Cdd:TIGR02343 372 ------CKNSKAVTIF-IRGGNKMIIEEAKRSIHDALCVVRNLIKDSrIVYGGGAAEISCSLAVS----QEADKYPGVEq 440
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1831502894 443 ----IIKRTLKIPAMTIAKNAGVE-----GSLIVEKIMQSSSEVGYDAMAGDFVNMVEKGIIDP 497
Cdd:TIGR02343 441 yairAFADALETIPMALAENSGLDpigtlSTLKSLQLKEKNPNLGVDCLGYGTNDMKEQFVFET 504
|
|
| chap_CCT_eta |
TIGR02345 |
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ... |
23-143 |
2.25e-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: 65.94 E-value: 2.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 23 LADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDKykniGAKLVQDVANNTNEEAGDGTTTATVLARSIAKE 102
Cdd:TIGR02345 30 IAEALKTTLGPRGMDKLIVGSNGKATISNDGATILKLLDIVHP----AAKTLVDIAKSQDAEVGDGTTSVTILAGELLKE 105
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1831502894 103 GFEKISKGANPVEIRRGVMLAVDAVIAELKKQSkpVTTPEE 143
Cdd:TIGR02345 106 AKPFIEEGVHPQLIIRCYREALSLAVEKIKEIA--VTIDEE 144
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
9-515 |
2.42e-11 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 66.21 E-value: 2.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 9 GADARALMLQGVDLLADAVAVTMGPKGRTVIIE-----QSWGSPKVTKDGVTVAKSIDLKdkykNIGAKLVQDVANNTNE 83
Cdd:PTZ00212 20 GETARLQSFVGAIAVADLVKTTLGPKGMDKILQpmsegPRSGNVTVTNDGATILKSVWLD----NPAAKILVDISKTQDE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 84 EAGDGTTTATVLARSIAKEGFEKISKGANPVEIRRGVMLAVDAVIAELKKQSKPVTTPEE--------IAQvATISA--- 152
Cdd:PTZ00212 96 EVGDGTTSVVVLAGELLREAEKLLDQKIHPQTIIEGWRMALDVARKALEEIAFDHGSDEEkfkedllnIAR-TTLSSkll 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 153 NGDKE-IGNIISDAMKKVGRKG-----VITVKDGKTLNDEleiiegmkfdrgYISPYFINTSK---GQKCEFQDAYVLLS 223
Cdd:PTZ00212 175 TVEKDhFAKLAVDAVLRLKGSGnldyiQIIKKPGGTLRDS------------YLEDGFILEKKigvGQPKRLENCKILVA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 224 EK-----KIS------SIQSIVPALEIANAHRKPLV-----IIAEDVdgealsTLVLNRlkvglQVVAvkapgfgdNRKN 287
Cdd:PTZ00212 243 NTpmdtdKIKiygakvKVDSMEKVAEIEAAEKEKMKnkvdkILAHGC------NVFINR-----QLIY--------NYPE 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 288 QL-KD---MAIATggAVF-GEEGLTLNLEdvqphdlgkvGEVIVTKDDAmllkgkgDKAQIE--KRIQEIIeqldvttse 360
Cdd:PTZ00212 304 QLfAEagiMAIEH--ADFdGMERLAAALG----------AEIVSTFDTP-------EKVKLGhcDLIEEIM--------- 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 361 YEKEKLnERLAKLSDGVA---VLKvgGTSDVEVNEKKDRVTDALNATRAAVEEG-IVLGGGCALLRCIPALDSLTPANED 436
Cdd:PTZ00212 356 IGEDKL-IRFSGCAKGEActiVLR--GASTHILDEAERSLHDALCVLSQTVKDTrVVLGGGCSEMLMANAVEELAKKVEG 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 437 QK-IGIEIIKRTLKIPAMTIAKNAGVEGSLIVEKI----MQSSSEVGYDAMAGDFVNMVEKGIIDPTKVVRTALLDAAGV 511
Cdd:PTZ00212 433 KKsLAIEAFAKALRQIPTIIADNGGYDSAELVSKLraehYKGNKTAGIDMEKGTVGDMKELGITESYKVKLSQLCSATEA 512
|
....
gi 1831502894 512 ASLL 515
Cdd:PTZ00212 513 AEMI 516
|
|
| TCP1_epsilon |
cd03339 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ... |
17-505 |
2.04e-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: 63.09 E-value: 2.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 17 LQGVD------LLADAVAVTM----GPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKdkykNIGAKLVQDVANNTNEEAG 86
Cdd:cd03339 19 LKGLEahkshiLAAKSVANILrtslGPRGMDKILVSPDGEVTVTNDGATILEKMDVD----HQIAKLLVELSKSQDDEIG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 87 DGTTTATVLARSIAKEGFEKISKGANPVEIRRGVMLAVDAVIAELKKQSKPVTTPEE----IAQVATISAnGDKeIGNII 162
Cdd:cd03339 95 DGTTGVVVLAGALLEQAEKLLDRGIHPIRIADGYEQACKIAVEHLEEIADKIEFSPDnkepLIQTAMTSL-GSK-IVSRC 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 163 SDAMKKVGRKGVITVKD--GKTLNDEL--------------EIIEGMKFDRGYISPYFINTSKGQK-----CEFQ----- 216
Cdd:cd03339 173 HRQFAEIAVDAVLSVADleRKDVNFELikvegkvggrledtKLVKGIVIDKDFSHPQMPKEVKDAKiailtCPFEppkpk 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 217 ----------DAYVLLSEKKISSIQSIVPALEIANAHrkpLVIIAEDVDGEALSTLVLNRLKVglqVVAVKAPgfgdnrk 286
Cdd:cd03339 253 tkhklditsvEDYKKLQEYEQKYFREMVEQVKDAGAN---LVICQWGFDDEANHLLLQNGLPA---VRWVGGV------- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 287 nQLKDMAIATGGAVFGEegltlnLEDVQPHDLGKVGEV----IVTKDDAMLlkgkgdkaqiekriqeIIEQLdvttseye 362
Cdd:cd03339 320 -EIELIAIATGGRIVPR------FEDLSPEKLGKAGLVreisFGTTKDKML----------------VIEGC-------- 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 363 keklnerlaKLSDGVAVLkVGGTSDVEVNEKKDRVTDALNATRAAVEEG-IVLGGGCALLRCipaldSLTPANEDQKIG- 440
Cdd:cd03339 369 ---------PNSKAVTIF-IRGGNKMIIEEAKRSLHDALCVVRNLIRDNrIVYGGGAAEISC-----SLAVEKAADKCSg 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 441 -----IEIIKRTLKIPAMTIAKNAGVE--GSLIVEKIMQ---SSSEVGYDAMAGDFVNMVEKGIIDP-----------TK 499
Cdd:cd03339 434 ieqyaMRAFADALESIPLALAENSGLNpiETLSEVKARQvkeKNPHLGIDCLGRGTNDMKEQKVFETliskkqqillaTQ 513
|
....*.
gi 1831502894 500 VVRTAL 505
Cdd:cd03339 514 VVKMIL 519
|
|
| TCP1_eta |
cd03340 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ... |
24-133 |
2.95e-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: 62.69 E-value: 2.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 24 ADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDKykniGAKLVQDVANNTNEEAGDGTTTATVLARSIAKEG 103
Cdd:cd03340 29 ADAVRTTLGPRGMDKLIVDGRGKVTISNDGATILKLLDIVHP----AAKTLVDIAKSQDAEVGDGTTSVVVLAGEFLKEA 104
|
90 100 110
....*....|....*....|....*....|
gi 1831502894 104 FEKISKGANPVEIRRGVMLAVDAVIAELKK 133
Cdd:cd03340 105 KPFIEDGVHPQIIIRGYRKALQLAIEKIKE 134
|
|
| TCP1_delta |
cd03338 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ... |
23-216 |
6.03e-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: 61.53 E-value: 6.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 23 LADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDKykniGAKLVQDVANNTNEEAGDGTTTATVLARSIAKE 102
Cdd:cd03338 20 VADAIRTSLGPRGMDKMIQTGKGEVIITNDGATILKQMSVLHP----AAKMLVELSKAQDIEAGDGTTSVVVLAGALLSA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 103 GFEKISKGANPVEIRRGVMLAVDAVIAELKKQSKPV--TTPEEIAQVATISANG------DKEIGNIISDAMKKVGRKGV 174
Cdd:cd03338 96 CESLLKKGIHPTVISESFQIAAKKAVEILDSMSIPVdlNDRESLIKSATTSLNSkvvsqySSLLAPIAVDAVLKVIDPAT 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1831502894 175 ----------ITVKDGKTLNDElEIIEGM----KFDRGYISPYFINTSKGQKCEFQ 216
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 ... |
17-528 |
1.46e-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: 57.06 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 17 LQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDKykniGAKLVQDVANNTNEEAGDGTTTATVLA 96
Cdd:TIGR02344 22 IQAAKAVADIIRTCLGPRSMLKMLLDPMGGIVMTNDGNAILREIDVAHP----AAKSMIELSRTQDEEVGDGTTSVIILA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 97 RSIAKEGFEKISKGANPVEIRRGVMLAVDAVIAELKKQSKPVTTPEEIAQVATISANGDKEIGNIISDAMKKVGRKGVIT 176
Cdd:TIGR02344 98 GEMLSVAEPFLEQNIHPTVIIRAYRKALDDALSVLEEISIPVDVNDDAAMLKLIQSCIGTKFVSRWSDLMCDLALDAVRT 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 177 VKDGKTLNDELEIIEgmkfdrgyispyFINTSKGQKCEFQDAYVLlsekKISSIQSIVPALEIANAHRKPLVII----AE 252
Cdd:TIGR02344 178 VQRDENGRKEIDIKR------------YAKVEKIPGGDIEDSCVL----KGVMINKDVTHPKMRRYIENPRIVLldcpLE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 253 DVDGEALSTLVLNRLKVGLQVVAVKApgfgDNRKNQLKDMAIATGGAVFGEEGLTlnleDVQPHDLGKVGEVIVTK---- 328
Cdd:TIGR02344 242 YKKGESQTNIEITKEEDWNRILQMEE----EYVQLMCEDIIAVKPDLVITEKGVS----DLAQHYLLKANITAIRRvrkt 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 329 DDAMLLKGKGdkAQIEKRIQEIIEQlDVTTSE--YEKEKLNERL------AKLSDGVAVLKVGGTSDVeVNEKKDRVTDA 400
Cdd:TIGR02344 314 DNNRIARACG--ATIVNRPEELRES-DVGTGCglFEVKKIGDEYftfiteCKDPKACTILLRGASKDI-LNEVERNLQDA 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 401 LNATRAAVEEG-IVLGGGCALLRCIPALDSLTPANED-QKIGIEIIKRTLKIPAMTIAKNAGVE-----GSLIVEKIMQS 473
Cdd:TIGR02344 390 MAVARNVLLDPkLVPGGGATEMAVSVALTEKSKKLEGvEQWPYRAVADALEIIPRTLAQNCGANvirtlTELRAKHAQEN 469
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1831502894 474 SSEVGYDAMAGDFVNMVEKGIIDPTKVVRTALLDAAGVASLLTTAEVVVTEIPKE 528
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 ... |
10-197 |
4.71e-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: 55.56 E-value: 4.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 10 ADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDKykniGAKLVQDVANNTNEEAGDGT 89
Cdd:TIGR02342 8 QDVRTSNIVAAKAVADAIRTSLGPKGMDKMIQDGKGEVIITNDGATILKQMAVLHP----AAKMLVELSKAQDIEAGDGT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 90 TTATVLARSIAKEGFEKISKGANPVEIRRGVMLAVDAVIAELKKQSKPVTTPEEIAQVATISANGDKEIGNIISDAMKKV 169
Cdd:TIGR02342 84 TSVVILAGALLGACERLLNKGIHPTIISESFQSAADEAIKILDEMSIPVDLSDREQLLKSATTSLSSKVVSQYSSLLAPL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1831502894 170 GRKGVITVKDGKT-----LND------------ELEIIEGMKFDR 197
Cdd:TIGR02342 164 AVDAVLKVIDPENaknvdLNDikvvkklggtidDTELIEGLVFTQ 208
|
|
| TCP1_gamma |
cd03337 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ... |
23-178 |
4.17e-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: 52.30 E-value: 4.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 23 LADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKdkykNIGAKLVQDVANNTNEEAGDGTTTATVLARSIAKE 102
Cdd:cd03337 28 VADVIRTCLGPRAMLKMLLDPMGGIVLTNDGNAILREIDVA----HPAAKSMIELSRTQDEEVGDGTTSVIILAGEILAV 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1831502894 103 GFEKISKGANPVEIRRGVMLAVDAVIAELKKQSKPVtTPEEIAQVATI--SANGDKEIgNIISDAMKKVGRKGVITVK 178
Cdd:cd03337 104 AEPFLERGIHPTVIIKAYRKALEDALKILEEISIPV-DVNDRAQMLKIikSCIGTKFV-SRWSDLMCNLALDAVKTVA 179
|
|
| chap_CCT_alpha |
TIGR02340 |
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ... |
9-498 |
7.78e-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: 51.64 E-value: 7.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 9 GADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDKykniGAKLVQDVANNTNEEAGDG 88
Cdd:TIGR02340 10 GQDVRTQNVTAAMAIANIVKTSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHP----AAKILVELAQLQDREVGDG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 89 TTTATVLARSIAKEGFEKISKGANPVEIRRGVMLAVDAVIAELKKqsKPVTTPEEIAQVATISA----------NGDKEI 158
Cdd:TIGR02340 86 TTSVVIIAAELLKRADELVKNKIHPTSVISGYRLACKEAVKYIKE--NLSVSVDELGREALINVaktsmsskiiGLDSDF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 159 -GNIISDAMKKV---GRKGVIT--VKDGKTLND------ELEIIEGMKFDRGYISPYFINTSKGQKCEFQDaYVLLSEKK 226
Cdd:TIGR02340 164 fSNIVVDAVLAVkttNENGETKypIKAINILKAhgksarESMLVKGYALNCTVASQQMPKRIKNAKIACLD-FNLQKAKM 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 227 ISSIQSIV--PAlEIANAHRKPLVIIAEDVDG--EALSTLVLNR-------LKvglQVVAVKAPGFGDNRKNQLKDMAIA 295
Cdd:TIGR02340 243 ALGVQIVVddPE-KLEQIRQREADITKERIKKilDAGANVVLTTggiddmcLK---YFVEAGAMGVRRCKKEDLKRIAKA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 296 TGGAVFGEEGLTLNLEDVQPHDLGKVGEVIVTK---DDAMLLKGKGDKAqiekriqeiieqldvttseyekeklnerlak 372
Cdd:TIGR02340 319 TGATLVSTLADLEGEETFEASYLGFADEVVQERiadDECILIKGTKKRK------------------------------- 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 373 lsdgVAVLKVGGTSDVEVNEKKDRVTDALNATRAAVEEG-IVLGGGCALLRCIPALDSL-TPANEDQKIGIEIIKRTLKI 450
Cdd:TIGR02340 368 ----SASIILRGANDFMLDEMERSLHDALCVVKRTLESNsVVPGGGAVEAALSIYLENFaTTLGSREQLAIAEFARALLI 443
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 451 PAMTIAKNAGVEGSLIVEKIM------QSSSE------VGYDAMAGDFVNMVEKGIIDPT 498
Cdd:TIGR02340 444 IPKTLAVNAAKDSTELVAKLRayhaaaQLKPEkkhlkwYGLDLVNGKIRDNKEAGVLEPT 503
|
|
| TCP1_alpha |
cd03335 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ... |
9-169 |
1.63e-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: 50.75 E-value: 1.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 9 GADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDKykniGAKLVQDVANNTNEEAGDG 88
Cdd:cd03335 6 GQDVRTQNVTAAMAIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHP----AAKILVELAQLQDKEVGDG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 89 TTTATVLARSIAKEGFEKISKGANPVEIRRGVMLAVDAVIAELKKQ-SKPVTT--PEEIAQVATIS-----ANGDKEI-G 159
Cdd:cd03335 82 TTSVVIIAAELLKRANELVKQKIHPTTIISGYRLACKEAVKYIKEHlSISVDNlgKESLINVAKTSmsskiIGADSDFfA 161
|
170
....*....|
gi 1831502894 160 NIISDAMKKV 169
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 ... |
23-197 |
2.43e-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: 2.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 23 LADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDKykniGAKLVQDVANNTNEEAGDGTTTATVLARSIAKE 102
Cdd:TIGR02346 30 LSQITRTSLGPNGMNKMVINHLEKLFVTNDAATILRELEVQHP----AAKLLVMASEMQENEIGDGTNLVLVLAGELLNK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 103 GFEKISKGANPVEIRRGVMLAVDAVIAELKKQSK-PVTTPEEIAQV--ATISANGDKEIGN------IISDAM-----KK 168
Cdd:TIGR02346 106 AEELIRMGLHPSEIIKGYEMALKKAMEILEELVVwEVKDLRDKDELikALKASISSKQYGNedflaqLVAQACstvlpKN 185
|
170 180 190
....*....|....*....|....*....|..
gi 1831502894 169 VGRKGVITVKDGKTLNDEL---EIIEGMKFDR 197
Cdd:TIGR02346 186 PQNFNVDNIRVCKILGGSLsnsEVLKGMVFNR 217
|
|
| TCP1_zeta |
cd03342 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
384-521 |
5.34e-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: 45.71 E-value: 5.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 384 GTSDVEVNEKKDRVTDALNATRAAVEEGIVLGGGCAL-LRCIPALDSLTP-ANEDQKIGIEIIKRTLKIPAMTIAKNAGV 461
Cdd:cd03342 336 GPNDHTITQIKDAIRDGLRAVKNAIEDKCVVPGAGAFeVALYAHLKEFKKsVKGKAKLGVQAFADALLVIPKTLAENSGL 415
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1831502894 462 EGS----LIVEKIMQSSSEVGYDAMAGDFVNMVEKGIIDPTKVVRTALLDAAGVAS-LLTTAEVV 521
Cdd:cd03342 416 DVQetlvKLQDEYAEGGQVGGVDLDTGEPMDPESEGIWDNYSVKRQILHSATVIASqLLLVDEII 480
|
|
| chap_CCT_zeta |
TIGR02347 |
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ... |
23-522 |
2.51e-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: 43.57 E-value: 2.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 23 LADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKdkykNIGAKLVQDVANNTNEEAGDGTTTATVLARSIAKE 102
Cdd:TIGR02347 28 LQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEMQIQ----HPTASMIARAATAQDDITGDGTTSTVLLIGELLKQ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 103 GFEKISKGANPVEIRRGVMLAVDAVIAELK--KQSKPVTTPEEIAQVATISANGDK-------EIGNIISDAMKKVGRKG 173
Cdd:TIGR02347 104 AERYILEGVHPRIITEGFEIARKEALQFLDkfKVKKEDEVDREFLLNVARTSLRTKlpadladQLTEIVVDAVLAIKKDG 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 174 ------VITVKDGKTLND-ELEIIEGMKFDRGYISPyfintskGQKCEFQDAYVLLS----EKKISSIQSivpALEIANA 242
Cdd:TIGR02347 184 edidlfMVEIMEMKHKSAtDTTLIRGLVLDHGARHP-------DMPRRVKNAYILTCnvslEYEKTEVNS---GFFYSSA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 243 HRKPLVIIAED--VDG------EALSTLVLNRLKVGLQVVAVK-----------APGFGDNRKNQLKDM---AIATGGAV 300
Cdd:TIGR02347 254 EQREKLVKAERkfVDDrvkkiiELKKKVCGKSPDKGFVVINQKgidppsldllaKEGIMALRRAKRRNMerlTLACGGEA 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 301 FGeegltlNLEDVQPHDLGKVGEVIvtkddamllkgkgdkaqiekriQEIIEQLDVTtseYEKEKLNERlaklsdGVAVL 380
Cdd:TIGR02347 334 LN------SVEDLTPECLGWAGLVY----------------------ETTIGEEKYT---FIEECKNPK------SCTIL 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 381 kVGGTSDVEVNEKKDRVTDALNATRAAVEEG-IVLGGGCALLRCIPALDSLTP-ANEDQKIGIEIIKRTLKIPAMTIAKN 458
Cdd:TIGR02347 377 -IKGPNDHTIAQIKDAVRDGLRAVKNAIEDKcVVPGAGAFEIAAYRHLKEYKKsVKGKAKLGVEAFANALLVIPKTLAEN 455
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1831502894 459 AGVEGS----LIVEKIMQSSSEVGYDAMAGDFVNMVEKGIIDPTKVVRTALLDAAGVASLLTTAEVVV 522
Cdd:TIGR02347 456 SGFDAQdtlvKLEDEHDEGGEVVGVDLNTGEPIDPEIKGIWDNYRVKKQLIQSATVIASQLLLVDEVM 523
|
|
| TCP1_theta |
cd03341 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ... |
23-160 |
5.83e-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: 42.59 E-value: 5.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831502894 23 LADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDKykniGAKLVQDVANNTNEEAGDGTTTATVLARSIAKE 102
Cdd:cd03341 20 LSQITRTSYGPNGMNKMVINHLEKLFVTSDAATILRELEVQHP----AAKLLVMASQMQEEEIGDGTNLVVVLAGELLEK 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1831502894 103 GFEKISKGANPVEIRRGVMLAVDAVIAELK----KQSKPVTTPEEIAQvATISANGDKEIGN 160
Cdd:cd03341 96 AEELLRMGLHPSEIIEGYEKALKKALEILEelvvYKIEDLRNKEEVSK-ALKTAIASKQYGN 156
|
|
| |
