|
Name |
Accession |
Description |
Interval |
E-value |
| PLN03167 |
PLN03167 |
Chaperonin-60 beta subunit; Provisional |
1-600 |
0e+00 |
|
Chaperonin-60 beta subunit; Provisional
Pssm-ID: 215611 [Multi-domain] Cd Length: 600 Bit Score: 1091.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 1 MASTFTATSSIGSMVAPNGHKSDKKLI--SKLSSSSFGRRQSVCPRprRSSSAIVCAAKELHFNKDGTTIRRLQAGVNKL 78
Cdd:PLN03167 1 MASTFTATSSVGSLAAPNGHKSDNRLSsfASISSSSFGRRQSVRLR--RSRSPKVKAAKELHFNKDGSAIKKLQAGVNKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 79 ADLVGVTLGPKGRNVVLESKYGSPRIVNDGVTVAREVELEDPVENIGAKLVRQAAAKTNDLAGDGTTTSVVLAQGFIAEG 158
Cdd:PLN03167 79 ADLVGVTLGPKGRNVVLESKYGSPKIVNDGVTVAKEVELEDPVENIGAKLVRQAAAKTNDLAGDGTTTSVVLAQGLIAEG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 159 VKVVAAGANPVLITRGIEKTAKALVTELKKMSKEVEDSELADVAAVSAGNNDEIGNMIAEAMSKVGRKGVVTLEEGKSAE 238
Cdd:PLN03167 159 VKVVAAGANPVQITRGIEKTAKALVKELKKMSKEVEDSELADVAAVSAGNNYEVGNMIAEAMSKVGRKGVVTLEEGKSAE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 239 NNLYVVEGMQFDRGYISPYFVTDSEKMSVEFDNCKLLLVDKKITNARDLVGVLEDAIRGGYPILIIAEDIEQEALATLVV 318
Cdd:PLN03167 239 NNLYVVEGMQFDRGYISPYFVTDSEKMSVEYDNCKLLLVDKKITNARDLIGILEDAIRGGYPLLIIAEDIEQEALATLVV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 319 NKLRGTLKIAALRAPGFGERKSQYLDDIAILTGATVIREEVGLSLDKAGKEVLGNASKVVLTKETSTIVGDGSTQDAVKK 398
Cdd:PLN03167 319 NKLRGSLKIAALKAPGFGERKSQYLDDIAILTGGTVIREEVGLSLDKVGKEVLGTAAKVVLTKDTTTIVGDGSTQEAVNK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 399 RVTQIKNLIEQAEQDYEKEKLNERIAKLSGGVAVIQVGAQTETELKEKKLRVEDALNATKAAVEEGIVVGGGCTLLRLAS 478
Cdd:PLN03167 399 RVAQIKNLIEAAEQDYEKEKLNERIAKLSGGVAVIQVGAQTETELKEKKLRVEDALNATKAAVEEGIVVGGGCTLLRLAS 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 479 KVDAIKATLDNDEEKVGADIVKRALSYPLKLIAKNAGVNGSVVSEKVLSNDNVKFGYNAATGKYEDLMAAGIIDPTKVVR 558
Cdd:PLN03167 479 KVDAIKDTLENDEQKVGADIVKRALSYPLKLIAKNAGVNGSVVSEKVLSNDNPKFGYNAATGKYEDLMAAGIIDPTKVVR 558
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 257734882 559 CCLEHAASVAKTFLMSDCVVVEIKEPEPVPVGNPMDNSGYGY 600
Cdd:PLN03167 559 CCLEHAASVAKTFLTSDCVVVEIKEPEPVPAGNPMDNSGYGY 600
|
|
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
55-593 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 799.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 55 AAKELHFNKDGTtiRRLQAGVNKLADLVGVTLGPKGRNVVLESKYGSPRIVNDGVTVAREVELEDPVENIGAKLVRQAAA 134
Cdd:PRK00013 1 MAKDIKFGEDAR--RKLLRGVNKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDPFENMGAQLVKEVAS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 135 KTNDLAGDGTTTSVVLAQGFIAEGVKVVAAGANPVLITRGIEKTAKALVTELKKMSKEVEDS-ELADVAAVSAGNNDEIG 213
Cdd:PRK00013 79 KTNDVAGDGTTTATVLAQAIVREGLKNVAAGANPMDLKRGIDKAVEAAVEELKKISKPVEDKeEIAQVATISANGDEEIG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 214 NMIAEAMSKVGRKGVVTLEEGKSAENNLYVVEGMQFDRGYISPYFVTDSEKMSVEFDNCKLLLVDKKITNARDLVGVLED 293
Cdd:PRK00013 159 KLIAEAMEKVGKEGVITVEESKGFETELEVVEGMQFDRGYLSPYFVTDPEKMEAELENPYILITDKKISNIQDLLPVLEQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 294 AIRGGYPILIIAEDIEQEALATLVVNKLRGTLKIAALRAPGFGERKSQYLDDIAILTGATVIREEVGLSLDKAGKEVLGN 373
Cdd:PRK00013 239 VAQSGKPLLIIAEDVEGEALATLVVNKLRGTLKVVAVKAPGFGDRRKAMLEDIAILTGGTVISEELGLKLEDATLEDLGQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 374 ASKVVLTKETSTIVGDGSTQDAVKKRVTQIKNLIEQAEQDYEKEKLNERIAKLSGGVAVIQVGAQTETELKEKKLRVEDA 453
Cdd:PRK00013 319 AKKVVVTKDNTTIVDGAGDKEAIKARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATEVEMKEKKDRVEDA 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 454 LNATKAAVEEGIVVGGGCTLLRLASKVDAIKatLDNDEEKVGADIVKRALSYPLKLIAKNAGVNGSVVSEKVLSNDNVKF 533
Cdd:PRK00013 399 LHATRAAVEEGIVPGGGVALLRAAPALEALK--GLNGDEATGINIVLRALEAPLRQIAENAGLEGSVVVEKVKNGKGKGY 476
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 534 GYNAATGKYEDLMAAGIIDPTKVVRCCLEHAASVAKTFLMSDCVVVEIKEPEPVPVGNPM 593
Cdd:PRK00013 477 GYNAATGEYVDMIEAGIIDPTKVTRSALQNAASVAGLLLTTEAVVADKPEKKAAAPPMGG 536
|
|
| GroEL |
cd03344 |
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ... |
57-580 |
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: 786.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 57 KELHFNKDGttIRRLQAGVNKLADLVGVTLGPKGRNVVLESKYGSPRIVNDGVTVAREVELEDPVENIGAKLVRQAAAKT 136
Cdd:cd03344 1 KDIKFGEEA--RKALLRGVNKLADAVKVTLGPKGRNVVIEKSFGSPKITKDGVTVAKEIELEDPFENMGAQLVKEVASKT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 137 NDLAGDGTTTSVVLAQGFIAEGVKVVAAGANPVLITRGIEKTAKALVTELKKMSKEVEDS-ELADVAAVSAGNNDEIGNM 215
Cdd:cd03344 79 NDVAGDGTTTATVLARAIIKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKPVKTKeEIAQVATISANGDEEIGEL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 216 IAEAMSKVGRKGVVTLEEGKSAENNLYVVEGMQFDRGYISPYFVTDSEKMSVEFDNCKLLLVDKKITNARDLVGVLEDAI 295
Cdd:cd03344 159 IAEAMEKVGKDGVITVEEGKTLETELEVVEGMQFDRGYLSPYFVTDPEKMEVELENPYILLTDKKISSIQELLPILELVA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 296 RGGYPILIIAEDIEQEALATLVVNKLRGTLKIAALRAPGFGERKSQYLDDIAILTGATVIREEVGLSLDKAGKEVLGNAS 375
Cdd:cd03344 239 KAGRPLLIIAEDVEGEALATLVVNKLRGGLKVCAVKAPGFGDRRKAMLEDIAILTGGTVISEELGLKLEDVTLEDLGRAK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 376 KVVLTKETSTIVGDGSTQDAVKKRVTQIKNLIEQAEQDYEKEKLNERIAKLSGGVAVIQVGAQTETELKEKKLRVEDALN 455
Cdd:cd03344 319 KVVVTKDDTTIIGGAGDKAAIKARIAQIRKQIEETTSDYDKEKLQERLAKLSGGVAVIKVGGATEVELKEKKDRVEDALN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 456 ATKAAVEEGIVVGGGCTLLRLASKVDAIKAtlDNDEEKVGADIVKRALSYPLKLIAKNAGVNGSVVSEKVLSNDNvKFGY 535
Cdd:cd03344 399 ATRAAVEEGIVPGGGVALLRASPALDKLKA--LNGDEKLGIEIVRRALEAPLRQIAENAGVDGSVVVEKVLESPD-GFGY 475
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 257734882 536 NAATGKYEDLMAAGIIDPTKVVRCCLEHAASVAKTFLMSDCVVVE 580
Cdd:cd03344 476 DAATGEYVDMIEAGIIDPTKVVRSALQNAASVASLLLTTEALVVD 520
|
|
| groEL |
PRK12849 |
chaperonin GroEL; Reviewed |
55-592 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237230 Cd Length: 542 Bit Score: 746.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 55 AAKELHFNKDGTtiRRLQAGVNKLADLVGVTLGPKGRNVVLESKYGSPRIVNDGVTVAREVELEDPVENIGAKLVRQAAA 134
Cdd:PRK12849 1 MAKIIKFDEEAR--RALERGVNKLADAVKVTLGPKGRNVVIDKSFGAPTITKDGVSIAKEIELEDPFENLGAQLVKEVAS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 135 KTNDLAGDGTTTSVVLAQGFIAEGVKVVAAGANPVLITRGIEKTAKALVTELKKMSKEVEDS-ELADVAAVSAGNNDEIG 213
Cdd:PRK12849 79 KTNDVAGDGTTTATVLAQALVQEGLKNVAAGANPMDLKRGIDKAVEAVVEELKALARPVSGSeEIAQVATISANGDEEIG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 214 NMIAEAMSKVGRKGVVTLEEGKSAENNLYVVEGMQFDRGYISPYFVTDSEKMSVEFDNCKLLLVDKKITNARDLVGVLED 293
Cdd:PRK12849 159 ELIAEAMEKVGKDGVITVEESKTLETELEVTEGMQFDRGYLSPYFVTDPERMEAVLEDPLILLTDKKISSLQDLLPLLEK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 294 AIRGGYPILIIAEDIEQEALATLVVNKLRGTLKIAALRAPGFGERKSQYLDDIAILTGATVIREEVGLSLDKAGKEVLGN 373
Cdd:PRK12849 239 VAQSGKPLLIIAEDVEGEALATLVVNKLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGLKLEEVTLDDLGR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 374 ASKVVLTKETSTIVGDGSTQDAVKKRVTQIKNLIEQAEQDYEKEKLNERIAKLSGGVAVIQVGAQTETELKEKKLRVEDA 453
Cdd:PRK12849 319 AKRVTITKDNTTIVDGAGDKEAIEARVAQIRRQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATEVELKERKDRVEDA 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 454 LNATKAAVEEGIVVGGGCTLLRLASKVDAIKATldNDEEKVGADIVKRALSYPLKLIAKNAGVNGSVVSEKVLSNDNvKF 533
Cdd:PRK12849 399 LNATRAAVEEGIVPGGGVALLRAAKALDELAGL--NGDQAAGVEIVRRALEAPLRQIAENAGLDGSVVVAKVLELED-GF 475
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 257734882 534 GYNAATGKYEDLMAAGIIDPTKVVRCCLEHAASVAKTFLMSDCVVVEIKEPEPVPVGNP 592
Cdd:PRK12849 476 GFNAATGEYGDLIAAGIIDPVKVTRSALQNAASVAGLLLTTEALVADKPEEEDPPGGMG 534
|
|
| GroEL |
TIGR02348 |
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ... |
56-583 |
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: 730.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 56 AKELHFNKDGTtiRRLQAGVNKLADLVGVTLGPKGRNVVLESKYGSPRIVNDGVTVAREVELEDPVENIGAKLVRQAAAK 135
Cdd:TIGR02348 1 AKQIKFDEEAR--KALLRGVDKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDKFENMGAQLVKEVASK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 136 TNDLAGDGTTTSVVLAQGFIAEGVKVVAAGANPVLITRGIEKTAKALVTELKKMSKEVEDS-ELADVAAVSAGNNDEIGN 214
Cdd:TIGR02348 79 TNDVAGDGTTTATVLAQAIVKEGLKNVAAGANPIELKRGIEKAVEAVVEELKKLSKPVKGKkEIAQVATISANNDEEIGS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 215 MIAEAMSKVGRKGVVTLEEGKSAENNLYVVEGMQFDRGYISPYFVTDSEKMSVEFDNCKLLLVDKKITNARDLVGVLEDA 294
Cdd:TIGR02348 159 LIAEAMEKVGKDGVITVEESKSLETELEVVEGMQFDRGYISPYFVTDAEKMEVELENPYILITDKKISNIKDLLPLLEKV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 295 IRGGYPILIIAEDIEQEALATLVVNKLRGTLKIAALRAPGFGERKSQYLDDIAILTGATVIREEVGLSLDKAGKEVLGNA 374
Cdd:TIGR02348 239 AQSGKPLLIIAEDVEGEALATLVVNKLRGTLNVCAVKAPGFGDRRKAMLEDIAILTGGQVISEELGLKLEEVTLDDLGKA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 375 SKVVLTKETSTIVGDGSTQDAVKKRVTQIKNLIEQAEQDYEKEKLNERIAKLSGGVAVIQVGAQTETELKEKKLRVEDAL 454
Cdd:TIGR02348 319 KKVTVDKDNTTIVEGAGDKAAIKARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATETEMKEKKLRIEDAL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 455 NATKAAVEEGIVVGGGCTLLRLASKVDAIKatLDNDEEKVGADIVKRALSYPLKLIAKNAGVNGSVVSEKVLSNDNvKFG 534
Cdd:TIGR02348 399 NATRAAVEEGIVPGGGVALLRAAAALEGLK--GDGEDEAIGIDIVKRALEAPLRQIAENAGLDGAVVAEKVKELKG-NFG 475
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 257734882 535 YNAATGKYEDLMAAGIIDPTKVVRCCLEHAASVAKTFLMSDCVVVEIKE 583
Cdd:TIGR02348 476 FNAATGEYEDLVEAGIIDPTKVTRSALQNAASIAGLLLTTEAVVADKPE 524
|
|
| groEL |
PRK12850 |
chaperonin GroEL; Reviewed |
55-600 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237231 Cd Length: 544 Bit Score: 676.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 55 AAKELHFNKDGTtiRRLQAGVNKLADLVGVTLGPKGRNVVLESKYGSPRIVNDGVTVAREVELEDPVENIGAKLVRQAAA 134
Cdd:PRK12850 2 AAKEIRFSTDAR--DRLLRGVNILANAVKVTLGPKGRNVVLEKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVKEVAS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 135 KTNDLAGDGTTTSVVLAQGFIAEGVKVVAAGANPVLITRGIEKTAKALVTELKKMSKEVEDS-ELADVAAVSAGNNDEIG 213
Cdd:PRK12850 80 KTNDLAGDGTTTATVLAQAIVREGAKLVAAGMNPMDLKRGIDLAVAAVVDELKKIAKKVTSSkEIAQVATISANGDESIG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 214 NMIAEAMSKVGRKGVVTLEEGKSAENNLYVVEGMQFDRGYISPYFVTDSEKMSVEFDNCKLLLVDKKITNARDLVGVLED 293
Cdd:PRK12850 160 EMIAEAMDKVGKEGVITVEEAKTLGTELDVVEGMQFDRGYLSPYFVTNPEKMRAELEDPYILLHEKKISNLQDLLPILEA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 294 AIRGGYPILIIAEDIEQEALATLVVNKLRGTLKIAALRAPGFGERKSQYLDDIAILTGATVIREEVGLSLDKAGKEVLGN 373
Cdd:PRK12850 240 VVQSGRPLLIIAEDVEGEALATLVVNKLRGGLKSVAVKAPGFGDRRKAMLEDIAVLTGGQVISEDLGIKLENVTLDMLGR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 374 ASKVVLTKETSTIVGDGSTQDAVKKRVTQIKNLIEQAEQDYEKEKLNERIAKLSGGVAVIQVGAQTETELKEKKLRVEDA 453
Cdd:PRK12850 320 AKRVLITKENTTIIDGAGDKKNIEARVKQIRAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKEKKDRVDDA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 454 LNATKAAVEEGIVVGGGCTLLRLASKVDAIKAtlDNDEEKVGADIVKRALSYPLKLIAKNAGVNGSVVSEKVLSNdNVKF 533
Cdd:PRK12850 400 LHATRAAVEEGIVPGGGVALLRARSALRGLKG--ANADETAGIDIVRRALEEPLRQIATNAGFEGSVVVGKVAEL-PGNF 476
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 257734882 534 GYNAATGKYEDLMAAGIIDPTKVVRCCLEHAASVAKTFLMSDCVVVEI-KEPEPVPVGNPMDNSGYGY 600
Cdd:PRK12850 477 GFNAQTGEYGDMVEAGIIDPAKVTRTALQDAASIAALLITTEAMVAEApKKAAAAAAGPGPGMGGMGY 544
|
|
| groEL |
CHL00093 |
chaperonin GroEL |
69-583 |
0e+00 |
|
chaperonin GroEL
Pssm-ID: 177025 Cd Length: 529 Bit Score: 668.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 69 RRLQAGVNKLADLVGVTLGPKGRNVVLESKYGSPRIVNDGVTVAREVELEDPVENIGAKLVRQAAAKTNDLAGDGTTTSV 148
Cdd:CHL00093 13 RALERGMDILAEAVSVTLGPKGRNVVLEKKYGSPQIVNDGVTIAKEIELEDHIENTGVALIRQAASKTNDVAGDGTTTAT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 149 VLAQGFIAEGVKVVAAGANPVLITRGIEKTAKALVTELKKMSKEVEDSE-LADVAAVSAGNNDEIGNMIAEAMSKVGRKG 227
Cdd:CHL00093 93 VLAYAIVKQGMKNVAAGANPISLKRGIEKATQYVVSQIAEYARPVEDIQaITQVASISAGNDEEVGSMIADAIEKVGREG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 228 VVTLEEGKSAENNLYVVEGMQFDRGYISPYFVTDSEKMSVEFDNCKLLLVDKKITNAR-DLVGVLEDAIRGGYPILIIAE 306
Cdd:CHL00093 173 VISLEEGKSTVTELEITEGMRFEKGFISPYFVTDTERMEVVQENPYILLTDKKITLVQqDLLPILEQVTKTKRPLLIIAE 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 307 DIEQEALATLVVNKLRGTLKIAALRAPGFGERKSQYLDDIAILTGATVIREEVGLSLDKAGKEVLGNASKVVLTKETSTI 386
Cdd:CHL00093 253 DVEKEALATLVLNKLRGIVNVVAVRAPGFGDRRKAMLEDIAILTGGQVITEDAGLSLETIQLDLLGQARRIIVTKDSTTI 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 387 VGDGsTQDAVKKRVTQIKNLIEQAEQDYEKEKLNERIAKLSGGVAVIQVGAQTETELKEKKLRVEDALNATKAAVEEGIV 466
Cdd:CHL00093 333 IADG-NEEQVKARCEQLRKQIEIADSSYEKEKLQERLAKLSGGVAVIKVGAATETEMKDKKLRLEDAINATKAAVEEGIV 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 467 VGGGCTLLRLASK-VDAIKATLdNDEEKVGADIVKRALSYPLKLIAKNAGVNGSVVSEKVlSNDNVKFGYNAATGKYEDL 545
Cdd:CHL00093 412 PGGGATLVHLSENlKTWAKNNL-KEDELIGALIVARAILAPLKRIAENAGKNGSVIIEKV-QEQDFEIGYNAANNKFVNM 489
|
490 500 510
....*....|....*....|....*....|....*...
gi 257734882 546 MAAGIIDPTKVVRCCLEHAASVAKTFLMSDCVVVEIKE 583
Cdd:CHL00093 490 YEAGIIDPAKVTRSALQNAASIASMILTTECIIVDKKE 527
|
|
| PTZ00114 |
PTZ00114 |
Heat shock protein 60; Provisional |
55-586 |
0e+00 |
|
Heat shock protein 60; Provisional
Pssm-ID: 185455 Cd Length: 555 Bit Score: 660.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 55 AAKELHFNKDGTtiRRLQAGVNKLADLVGVTLGPKGRNVVLESKYGSPRIVNDGVTVAREVELEDPVENIGAKLVRQAAA 134
Cdd:PTZ00114 13 KGKEIRFGDEAR--QSLLKGIERLADAVAVTLGPKGRNVIIEQEYGSPKITKDGVTVAKAIEFSDRFENVGAQLIRQVAS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 135 KTNDLAGDGTTTSVVLAQGFIAEGVKVVAAGANPVLITRGIEKTAKALVTELKKMSKEVEDSE-LADVAAVSAGNNDEIG 213
Cdd:PTZ00114 91 KTNDKAGDGTTTATILARAIFREGCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQSRPVKTKEdILNVATISANGDVEIG 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 214 NMIAEAMSKVGRKGVVTLEEGKSAENNLYVVEGMQFDRGYISPYFVTDSEKMSVEFDNCKLLLVDKKITNARDLVGVLED 293
Cdd:PTZ00114 171 SLIADAMDKVGKDGTITVEDGKTLEDELEVVEGMSFDRGYISPYFVTNEKTQKVELENPLILVTDKKISSIQSILPILEH 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 294 AIRGGYPILIIAEDIEQEALATLVVNKLRGTLKIAALRAPGFGERKSQYLDDIAILTGATVIREE-VGLSLDKAGKEVLG 372
Cdd:PTZ00114 251 AVKNKRPLLIIAEDVEGEALQTLIINKLRGGLKVCAVKAPGFGDNRKDILQDIAVLTGATVVSEDnVGLKLDDFDPSMLG 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 373 NASKVVLTKETSTIVGDGSTQDAVKKRVTQIKNLIEQAEQDYEKEKLNERIAKLSGGVAVIQVGAQTETELKEKKLRVED 452
Cdd:PTZ00114 331 SAKKVTVTKDETVILTGGGDKAEIKERVELLRSQIERTTSEYDKEKLKERLAKLSGGVAVIKVGGASEVEVNEKKDRIED 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 453 ALNATKAAVEEGIVVGGGCTLLRLASKVDAIKATLDND-EEKVGADIVKRALSYPLKLIAKNAGVNGSVVSEKVLSNDNV 531
Cdd:PTZ00114 411 ALNATRAAVEEGIVPGGGVALLRASKLLDKLEEDNELTpDQRTGVKIVRNALRLPTKQIAENAGVEGAVVVEKILEKKDP 490
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 257734882 532 KFGYNAATGKYEDLMAAGIIDPTKVVRCCLEHAASVAKTFLMSDCVVVEIKEPEP 586
Cdd:PTZ00114 491 SFGYDAQTGEYVNMFEAGIIDPTKVVRSALVDAASVASLMLTTEAAIVDLPKEKK 545
|
|
| GroEL |
COG0459 |
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ... |
55-586 |
0e+00 |
|
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227 Cd Length: 497 Bit Score: 660.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 55 AAKELHFNKDGTtiRRLQAGVNKLADLVGVTLGPKGRNVVLESKYGSPRIVNDGVTVAREVELEDPVENIGAKLVRQAAA 134
Cdd:COG0459 1 MAKQILFGEDAR--RANIRGVKALADAVKVTLGPKGRNVMLVKSFGDPTITNDGVTIAKEIELEDPFENMGAQLVKEVAS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 135 KTNDLAGDGTTTSVVLAQGFIAEGVKVVAAGANPVLITRGIEKTAKALVTELKKMSKEVEDSE-LADVAAVSAGNNDEIG 213
Cdd:COG0459 79 KTNDEAGDGTTTATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPVDDKEeLAQVATISANGDEEIG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 214 NMIAEAMSKVGRKGVVTLEEGKSAENNLYVVEGMQFDRGYISPYFVTDSEKMSVEFDNCKLLLVDKKITNARDLVGVLED 293
Cdd:COG0459 159 ELIAEAMEKVGKDGVITVEEGKGLETELEVVEGMQFDKGYLSPYFVTDPEKMPAELENAYILLTDKKISSIQDLLPLLEK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 294 AIRGGYPILIIAEDIEQEALATLVVNKLRGTLKIAALRAPGFGERKSQYLDDIAILTGATVIREEVGLSLDKAGKEVLGN 373
Cdd:COG0459 239 VAQSGKPLLIIAEDIDGEALATLVVNGIRGVLRVVAVKAPGFGDRRKAMLEDIAILTGGRVISEDLGLKLEDVTLDDLGR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 374 ASKVVLTKETSTIVGDGSTQDAVkkrvtqiknlieqaeqdyekeklneriaklsggvaVIQVGAQTETELKEKKLRVEDA 453
Cdd:COG0459 319 AKRVEVDKDNTTIVEGAGNPKAI-----------------------------------VILVGAATEVEVKERKRRVEDA 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 454 LNATKAAVEEGIVVGGGCTLLRLASKVDAIKATLDNDeEKVGADIVKRALSYPLKLIAKNAGVNGSVVSEKVLSNDNVKF 533
Cdd:COG0459 364 LHATRAAVEEGIVPGGGAALLRAARALRELAAKLEGD-EQLGIEIVARALEAPLRQIAENAGLDGSVVVEKVRAAKDKGF 442
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 257734882 534 GYNAATGKYEDLMAAGIIDPTKVVRCCLEHAASVAKTFLMSDCVVVEIKEPEP 586
Cdd:COG0459 443 GFDAATGEYVDMLEAGVIDPAKVKRSALQNAASVAGLILTTEAVIADKPEKEE 495
|
|
| groEL |
PRK12851 |
chaperonin GroEL; Reviewed |
55-592 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 171770 Cd Length: 541 Bit Score: 645.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 55 AAKELHFNKDGTtiRRLQAGVNKLADLVGVTLGPKGRNVVLESKYGSPRIVNDGVTVAREVELEDPVENIGAKLVRQAAA 134
Cdd:PRK12851 2 AAKEVKFHVEAR--EKMLRGVNILADAVKVTLGPKGRNVVIDKSFGAPTITNDGVTIAKEIELEDKFENMGAQMVREVAS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 135 KTNDLAGDGTTTSVVLAQGFIAEGVKVVAAGANPVLITRGIEKTAKALVTELKKMSKEVE-DSELADVAAVSAGNNDEIG 213
Cdd:PRK12851 80 KTNDVAGDGTTTATVLAQAIVREGAKAVAAGANPMDLKRGIDRAVAAVVEELKANARPVTtNAEIAQVATISANGDAEIG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 214 NMIAEAMSKVGRKGVVTLEEGKSAENNLYVVEGMQFDRGYISPYFVTDSEKMSVEFDNCKLLLVDKKITNARDLVGVLED 293
Cdd:PRK12851 160 RLVAEAMEKVGNEGVITVEESKTAETELEVVEGMQFDRGYLSPYFVTDADKMEAELEDPYILIHEKKISNLQDLLPVLEA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 294 AIRGGYPILIIAEDIEQEALATLVVNKLRGTLKIAALRAPGFGERKSQYLDDIAILTGATVIREEVGLSLDKAGKEVLGN 373
Cdd:PRK12851 240 VVQSGKPLLIIAEDVEGEALATLVVNKLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGIKLENVTLEQLGR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 374 ASKVVLTKETSTIVGDGSTQDAVKKRVTQIKNLIEQAEQDYEKEKLNERIAKLSGGVAVIQVGAQTETELKEKKLRVEDA 453
Cdd:PRK12851 320 AKKVVVEKENTTIIDGAGSKTEIEGRVAQIRAQIEETTSDYDREKLQERLAKLAGGVAVIRVGASTEVEVKEKKDRVDDA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 454 LNATKAAVEEGIVVGGGCTLLRLASKVDAIKATldNDEEKVGADIVKRALSYPLKLIAKNAGVNGSVVSEKVLSNDNvKF 533
Cdd:PRK12851 400 LHATRAAVEEGIVPGGGVALLRAVKALDKLETA--NGDQRTGVEIVRRALEAPVRQIAENAGAEGSVVVGKLREKPG-GY 476
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 257734882 534 GYNAATGKYEDLMAAGIIDPTKVVRCCLEHAASVAKTFLMSDCVVVEIKEPEPVPVGNP 592
Cdd:PRK12851 477 GFNAATNEYGDLYAQGVIDPVKVVRTALQNAASVAGLLLTTEAMVAEKPKKEPAPPAPP 535
|
|
| groEL |
PRK12852 |
chaperonin GroEL; Reviewed |
55-598 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237232 Cd Length: 545 Bit Score: 610.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 55 AAKELHFNKDGTTirRLQAGVNKLADLVGVTLGPKGRNVVLESKYGSPRIVNDGVTVAREVELEDPVENIGAKLVRQAAA 134
Cdd:PRK12852 2 AAKDVKFSGDARD--RMLRGVDILANAVKVTLGPKGRNVVIEKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVREVAS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 135 KTNDLAGDGTTTSVVLAQGFIAEGVKVVAAGANPVLITRGIEKTAKALVTELKKMSKEVEDS-ELADVAAVSAGNNDEIG 213
Cdd:PRK12852 80 KTNDLAGDGTTTATVLAQAIVREGAKAVAAGMNPMDLKRGIDIAVAAVVKDIEKRAKPVASSaEIAQVGTISANGDAAIG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 214 NMIAEAMSKVGRKGVVTLEEGKSAENNLYVVEGMQFDRGYISPYFVTDSEKMSVEFDNCKLLLVDKKITNARDLVGVLED 293
Cdd:PRK12852 160 KMIAQAMQKVGNEGVITVEENKSLETEVDIVEGMKFDRGYLSPYFVTNAEKMTVELDDAYILLHEKKLSGLQAMLPVLEA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 294 AIRGGYPILIIAEDIEQEALATLVVNKLRGTLKIAALRAPGFGERKSQYLDDIAILTGATVIREEVGLSLDKAGKEVLGN 373
Cdd:PRK12852 240 VVQSGKPLLIIAEDVEGEALATLVVNRLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGQLISEDLGIKLENVTLKMLGR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 374 ASKVVLTKETSTIVGDGSTQDAVKKRVTQIKNLIEQAEQDYEKEKLNERIAKLSGGVAVIQVGAQTETELKEKKLRVEDA 453
Cdd:PRK12852 320 AKKVVIDKENTTIVNGAGKKADIEARVGQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKEKKDRVEDA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 454 LNATKAAVEEGIVVGGGCTLLRLASKVDAIkaTLDNDEEKVGADIVKRALSYPLKLIAKNAGVNGSVVSEKVLSNDNVKF 533
Cdd:PRK12852 400 LNATRAAVQEGIVPGGGVALLRAKKAVGRI--NNDNADVQAGINIVLKALEAPIRQIAENAGVEGSIVVGKILENKSETF 477
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 257734882 534 GYNAATGKYEDLMAAGIIDPTKVVRCCLEHAASVAKTFLMSDCVVVEI---KEPEPVPVGNPMDNSGY 598
Cdd:PRK12852 478 GFDAQTEEYVDMVAKGIIDPAKVVRTALQDAASVAGLLVTTEAMVAELpkkDAAPAMPAGGGMGGMGF 545
|
|
| PRK14104 |
PRK14104 |
chaperonin GroEL; Provisional |
55-597 |
0e+00 |
|
chaperonin GroEL; Provisional
Pssm-ID: 172594 Cd Length: 546 Bit Score: 527.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 55 AAKELHFNKDGTTirRLQAGVNKLADLVGVTLGPKGRNVVLESKYGSPRIVNDGVTVAREVELEDPVENIGAKLVRQAAA 134
Cdd:PRK14104 2 SAKEVKFGVDARD--RMLRGVDILANAVKVTLGPKGRNVVLDKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVREVAS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 135 KTNDLAGDGTTTSVVLAQGFIAEGVKVVAAGANPVLITRGIEKTAKALVTELKKMSKEV-EDSELADVAAVSAGNNDEIG 213
Cdd:PRK14104 80 KSADAAGDGTTTATVLAQAIVREGAKSVAAGMNPMDLKRGIDLAVEAVVADLVKNSKKVtSNDEIAQVGTISANGDAEIG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 214 NMIAEAMSKVGRKGVVTLEEGKSAENNLYVVEGMQFDRGYISPYFVTDSEKMSVEFDNCKLLLVDKKITNARDLVGVLED 293
Cdd:PRK14104 160 KFLADAMKKVGNEGVITVEEAKSLETELDVVEGMQFDRGYISPYFVTNADKMRVEMDDAYILINEKKLSSLNELLPLLEA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 294 AIRGGYPILIIAEDIEQEALATLVVNKLRGTLKIAALRAPGFGERKSQYLDDIAILTGATVIREEVGLSLDKAGKEVLGN 373
Cdd:PRK14104 240 VVQTGKPLVIVAEDVEGEALATLVVNRLRGGLKVAAVKAPGFGDRRKAMLQDIAILTGGQAISEDLGIKLENVTLQMLGR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 374 ASKVVLTKETSTIVGDGSTQDAVKKRVTQIKNLIEQAEQDYEKEKLNERIAKLSGGVAVIQVGAQTETELKEKKLRVEDA 453
Cdd:PRK14104 320 AKKVMIDKENTTIVNGAGKKADIEARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKERKDRVDDA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 454 LNATKAAVEEGIVVGGGCTLLRLASKVDAIKAtlDNDEEKVGADIVKRALSYPLKLIAKNAGVNGSVVSEKVLSNDNVKF 533
Cdd:PRK14104 400 MHATRAAVEEGIVPGGGVALLRASEQLKGIKT--KNDDQKTGVEIVRKALSAPARQIAINAGEDGSVIVGKILEKEQYSY 477
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 257734882 534 GYNAATGKYEDLMAAGIIDPTKVVRCCLEHAASVAKTFLMSDCVVVEIkePEPVPVGNPMDNSG 597
Cdd:PRK14104 478 GFDSQTGEYGNLVSKGIIDPTKVVRTAIQNAASVAALLITTEAMVAEL--PKKGGAGPAMPPGG 539
|
|
| chaperonin_type_I_II |
cd00309 |
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ... |
68-579 |
4.04e-130 |
|
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: 389.48 E-value: 4.04e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 68 IRRLQAGVNKLADLVGVTLGPKGRNVVLESKYGSPRIVNDGVTVAREVEledpVENIGAKLVRQAAAKTNDLAGDGTTTS 147
Cdd:cd00309 10 RLSNINAAKALADAVKTTLGPKGMDKMLVDSLGDPTITNDGATILKEIE----VEHPAAKLLVEVAKSQDDEVGDGTTTV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 148 VVLAQGFIAEGVKVVAAGANPVLITRGIEKTAKALVTELKKMSKEVEDS---ELADVAAVSAG------NNDEIGNMIAE 218
Cdd:cd00309 86 VVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVPIDVEdreELLKVATTSLNsklvsgGDDFLGELVVD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 219 AMSKVGR------KGVVTLEEGKS-AENNLYVVEGMQFDRGYISPYfvtdsekMSVEFDNCKLLLVDKKITNardlvgvl 291
Cdd:cd00309 166 AVLKVGKengdvdLGVIRVEKKKGgSLEDSELVVGMVFDKGYLSPY-------MPKRLENAKILLLDCKLEY-------- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 292 edairggypiLIIAED-IEQEALATLVVnklrgtLKIAALRApgfgeRKSQYLDDIAILTGATVIreevgLSLDKAGKEV 370
Cdd:cd00309 231 ----------VVIAEKgIDDEALHYLAK------LGIMAVRR-----VRKEDLERIAKATGATIV-----SRLEDLTPED 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 371 LGNASKVVLTKetstIVGDGSTqdavkkRVTQIKNlieqaeqdyekeklneriaklsGGVAVIQVGAQTETELKEKKLRV 450
Cdd:cd00309 285 LGTAGLVEETK----IGDEKYT------FIEGCKG----------------------GKVATILLRGATEVELDEAERSL 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 451 EDALNATKAAVEE-GIVVGGGCTLLRLASKVDAIKATLdNDEEKVGADIVKRALSYPLKLIAKNAGVNGSVVSEKVLS-- 527
Cdd:cd00309 333 HDALCAVRAAVEDgGIVPGGGAAEIELSKALEELAKTL-PGKEQLGIEAFADALEVIPRTLAENAGLDPIEVVTKLRAkh 411
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 257734882 528 -NDNVKFGYNAATGKYEDLMAAGIIDPTKVVRCCLEHAASVAKTFLMSDCVVV 579
Cdd:cd00309 412 aEGGGNAGGDVETGEIVDMKEAGIIDPLKVKRQALKSATEAASLILTIDDIIV 464
|
|
| Cpn60_TCP1 |
pfam00118 |
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ... |
78-581 |
3.45e-90 |
|
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: 287.18 E-value: 3.45e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 78 LADLVGVTLGPKGRNVVLESKYGSPRIVNDGVTVAREVELEDPVenigAKLVRQAAAKTNDLAGDGTTTSVVLAQGFIAE 157
Cdd:pfam00118 1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELEIQHPA----AKLLVEAAKAQDEEVGDGTTTVVVLAGELLEE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 158 GVKVVAAGANPVLITRGIEKTAKALVTELKKM----SKEVEDSELADVAAVSAGNN------DEIGNMIAEAMS------ 221
Cdd:pfam00118 77 AEKLLAAGVHPTTIIEGYEKALEKALEILDSIisipVEDVDREDLLKVARTSLSSKiisresDFLAKLVVDAVLaipknd 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 222 ---KVGRKGVVTLEEGKSaeNNLYVVEGMQFDRGYISPyfvtdseKMSVEFDNCKLLLVDKKITNARD------------ 286
Cdd:pfam00118 157 gsfDLGNIGVVKILGGSL--EDSELVDGVVLDKGPLHP-------DMPKRLENAKVLLLNCSLEYEKTetkatvvlsdae 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 287 ------------LVGVLEDAIRGGYPILIIAEDIEQEALATLVVNKLRgtlkiaALRAPGFGErksqyLDDIAILTGATV 354
Cdd:pfam00118 228 qlerflkaeeeqILEIVEKIIDSGVNVVVCQKGIDDLALHFLAKNGIM------ALRRVKKRD-----LERLAKATGARA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 355 IREEVGLSLDkagkeVLGNASKVVLTKetstiVGDgstqdavkKRVTQIKNlieqaeqdyekeklneriaKLSGGVAVIQ 434
Cdd:pfam00118 297 VSSLDDLTPD-----DLGTAGKVEEEK-----IGD--------EKYTFIEG-------------------CKSPKAATIL 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 435 VGAQTETELKEKKLRVEDALNATKAAVEE-GIVVGGGCTLLRLASKVDAIKATlDNDEEKVGADIVKRALSYPLKLIAKN 513
Cdd:pfam00118 340 LRGATDHVLDEIERSIHDALCVVKNAIEDpRVVPGGGAVEMELARALREYAKS-VSGKEQLAIEAFAEALEVIPKTLAEN 418
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 257734882 514 AGVNGSVVSEKVLS---NDNVKFGYNAATGKYEDLMAAGIIDPTKVVRCCLEHAASVAKTFLMSDCVVVEI 581
Cdd:pfam00118 419 AGLDPIEVLAELRAahaSGEKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKSATEAASTILRIDDIIKAK 489
|
|
| chaperonin_like |
cd03333 |
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ... |
195-463 |
3.97e-33 |
|
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: 126.04 E-value: 3.97e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 195 DSELADVAAVSAG-----NNDEIGNMIAEAMSKVGR------KGVVTLEE--GKSAENNlYVVEGMQFDRGYISPYfvtd 261
Cdd:cd03333 1 RELLLQVATTSLNsklssWDDFLGKLVVDAVLKVGPdnrmddLGVIKVEKipGGSLEDS-ELVVGVVFDKGYASPY---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 262 sekMSVEFDNCKLLLVDKKITNardlvgvledairggypiLIIAED-IEQEALATLVVnklrgtLKIAALRApgfgeRKS 340
Cdd:cd03333 76 ---MPKRLENAKILLLDCPLEY------------------VVIAEKgIDDLALHYLAK------AGIMAVRR-----VKK 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 341 QYLDDIAILTGATVIreevgLSLDKAGKEVLGNASKVVLTKetstIVGDGSTqdavkkRVTQIKNlieqaeqdyekekln 420
Cdd:cd03333 124 EDLERIARATGATIV-----SSLEDLTPEDLGTAELVEETK----IGEEKLT------FIEGCKG--------------- 173
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 257734882 421 eriaklsGGVAVIQVGAQTETELKEKKLRVEDALNATKAAVEE 463
Cdd:cd03333 174 -------GKAATILLRGATEVELDEVKRSLHDALCAVRAAVEE 209
|
|
| thermosome_beta |
NF041083 |
thermosome subunit beta; |
78-578 |
6.74e-19 |
|
thermosome subunit beta;
Pssm-ID: 469010 Cd Length: 519 Bit Score: 90.01 E-value: 6.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 78 LADLVGVTLGPKGRNVVLESKYGSPRIVNDGVTVAREVELEDPveniGAKLVRQAAAKTNDLAGDGTTTSVVLAQGFIAE 157
Cdd:NF041083 29 VAEAVRTTLGPKGMDKMLVDSLGDIVITNDGATILKEMDVQHP----AAKMLVEVAKTQDDEVGDGTTTAVVLAGELLKK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 158 GVKVVAAGANPVLITRGIEKTAKALVTELKKMSKEV--EDSE-LADVAAVS------AGNNDEIGNMIAEAMSKV----G 224
Cdd:NF041083 105 AEELLDQNIHPTIIANGYRLAAEKAIEILDEIAEKVdpDDREtLKKIAETSltskgvEEARDYLAEIAVKAVKQVaekrD 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 225 RKGVVTLE-------EGKSAENNLyVVEGMQFDRGYISPyfvtdseKMSVEFDNCKLLLVDKKITNARDLVgvleDA-IR 296
Cdd:NF041083 185 GKYYVDLDniqiekkHGGSIEDTQ-LIYGIVIDKEVVHP-------GMPKRVENAKIALLDAPLEVKKTEI----DAeIR 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 297 GGYPILIIAEDIEQEALATLVVNKLRGTLKIAALRAPGFGERKSQYLDDIAIL----------------TGATVIReevg 360
Cdd:NF041083 253 ITDPDQLQKFLDQEEKMLKEMVDKIKATGANVVFCQKGIDDLAQHYLAKAGILavrrvkksdmeklakaTGARIVT---- 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 361 lSLDKAGKEVLGNASKVvltkETSTIVGDGSTqdavkkRVTQIKNlieqaeqdyekeklneriAKlsggvAV-IQVGAQT 439
Cdd:NF041083 329 -NIDDLTPEDLGYAELV----EERKVGDDKMV------FVEGCKN------------------PK-----AVtILIRGGT 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 440 ETELKEKKLRVEDALNATKAAVEEG-IVVGGGCTLLRLASKVDAIKATLDNdEEKVGADIVKRALSYPLKLIAKNAGVNG 518
Cdd:NF041083 375 EHVVDEAERALEDALSVVADAVEDGkIVAGGGAPEVELAKRLREYAATVGG-REQLAVEAFAEALEIIPRTLAENAGLDP 453
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 257734882 519 SVVSEKVLS---NDNVKFGYNAATGKYEDLMAAGIIDPTKVVRCCLEHAASVAKTFLMSDCVV 578
Cdd:NF041083 454 IDILVKLRSaheKGKKWAGINVFTGEVVDMWELGVIEPLRVKTQAIKSATEAATMILRIDDVI 516
|
|
| cpn60 |
cd03343 |
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ... |
78-578 |
8.73e-17 |
|
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: 83.47 E-value: 8.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 78 LADLVGVTLGPKGRNVVLESKYGSPRIVNDGVTVAREVELEDPveniGAKLVRQAAAKTNDLAGDGTTTSVVLAQGFIAE 157
Cdd:cd03343 27 VAEAVRTTLGPKGMDKMLVDSLGDVTITNDGATILKEMDIEHP----AAKMLVEVAKTQDEEVGDGTTTAVVLAGELLEK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 158 GVKVVAAGANPVLITRGIEKTAKALVTELKKMSKEV--EDSE-LADVAAVS------AGNNDEIGNMIAEAMSKV----G 224
Cdd:cd03343 103 AEDLLDQNIHPTVIIEGYRLAAEKALELLDEIAIKVdpDDKDtLRKIAKTSltgkgaEAAKDKLADLVVDAVLQVaekrD 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 225 RKGVVTLEEGKSAENNLYVVEGMQFDRGyispyFVTDSEK----MSVEFDNCKLLLVDKKITnardlvgVLEDAIRGGYP 300
Cdd:cd03343 183 GKYVVDLDNIKIEKKTGGSVDDTELIRG-----IVIDKEVvhpgMPKRVENAKIALLDAPLE-------VKKTEIDAKIR 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 301 IL---IIAEDIEQEAlatlvvNKLRGTL-KIAALRA------PGFGERKSQYLDDIAIL----------------TGATV 354
Cdd:cd03343 251 ITspdQLQAFLEQEE------AMLKEMVdKIADTGAnvvfcqKGIDDLAQHYLAKAGILavrrvkksdmeklaraTGAKI 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 355 IReevglSLDKAGKEVLGNASKVvltkETSTIVGDGSTqdavkkRVTQIKNlieqaeqdyekeklneriAKlsgGVAVIQ 434
Cdd:cd03343 325 VT-----NIDDLTPEDLGEAELV----EERKVGDDKMV------FVEGCKN------------------PK---AVTILL 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 435 VGAqTETELKEKKLRVEDALNATKAAVEEG-IVVGGGCTLLRLASKVDAIKATLDNdEEKVGADIVKRALSYPLKLIAKN 513
Cdd:cd03343 369 RGG-TEHVVDELERALEDALRVVADALEDGkVVAGGGAVEIELAKRLREYARSVGG-REQLAVEAFADALEEIPRTLAEN 446
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 257734882 514 AGVNG--SVVSEKVL-SNDNVKFGYNAATGKYEDLMAAGIIDPTKVVRCCLEHAASVAKTFLMSDCVV 578
Cdd:cd03343 447 AGLDPidTLVELRAAhEKGNKNAGLDVYTGEVVDMLEKGVIEPLRVKKQAIKSATEAATMILRIDDVI 514
|
|
| chap_CCT_epsi |
TIGR02343 |
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ... |
73-228 |
1.83e-14 |
|
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: 76.38 E-value: 1.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 73 AGVNKLADLVGVTLGPKGRNVVLESKYGSPRIVNDGVTVAREVELEDPVenigAKLVRQAAAKTNDLAGDGTTTSVVLAQ 152
Cdd:TIGR02343 34 AAAKSVASILRTSLGPKGMDKMLISPDGDITVTNDGATILSQMDVDNQI----AKLMVELSKSQDDEIGDGTTGVVVLAG 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 257734882 153 GFIAEGVKVVAAGANPVLITRGIEKTAKALVTELKKMSKEVEDSEladvaavsagNNDEigNMIAEAMSKVGRKGV 228
Cdd:TIGR02343 110 ALLEQAEELLDKGIHPIKIADGFEEAARIAVEHLEEISDEISADN----------NNRE--PLIQAAKTSLGSKIV 173
|
|
| thermosome_alpha |
NF041082 |
thermosome subunit alpha; |
78-578 |
4.39e-14 |
|
thermosome subunit alpha;
Pssm-ID: 469009 Cd Length: 518 Bit Score: 74.92 E-value: 4.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 78 LADLVGVTLGPKGRNVVLESKYGSPRIVNDGVTVAREVELEDPveniGAKLVRQAAAKTNDLAGDGTTTSVVLAQGFIAE 157
Cdd:NF041082 29 VAEAVRTTLGPKGMDKMLVDSLGDVVITNDGVTILKEMDIEHP----AAKMIVEVAKTQDDEVGDGTTTAVVLAGELLKK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 158 GVKVVAAGANPVLITRGIEKTAKALVTELKKMSKEVEDSE---LADVAAVS------AGNNDEIGNMIAEAMSKVGRK-- 226
Cdd:NF041082 105 AEELLDQDIHPTIIAEGYRLAAEKALEILDEIAIKVDPDDketLKKIAATAmtgkgaEAAKDKLADLVVDAVKAVAEKdg 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 227 -GVVTLE-------EGKSAENNLyVVEGMQFDRGYISPyfvtdseKMSVEFDNCKLLLVD-----KK--------ITNAR 285
Cdd:NF041082 185 gYNVDLDnikvekkVGGSIEDSE-LVEGVVIDKERVHP-------GMPKRVENAKIALLDaplevKKteidakisITDPD 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 286 DLVGVLE----------DAIRGGYPILIIA----EDIEQEALAtlvvnklrgTLKIAALRapgfgERKSQYLDDIAILTG 351
Cdd:NF041082 257 QLQAFLDqeekmlkemvDKIADSGANVVFCqkgiDDLAQHYLA---------KEGILAVR-----RVKKSDMEKLAKATG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 352 ATVIReevglSLDKAGKEVLGNASKVvltkETSTIVGDGSTqdavkkRVTQIKNlieqaeqdyekeklneriAKlsgGVA 431
Cdd:NF041082 323 ARIVT-----SIDDLSPEDLGYAGLV----EERKVGGDKMI------FVEGCKN------------------PK---AVT 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 432 VIQVGAqTETELKEKKLRVEDALNATKAAVEEG-IVVGGGCTLLRLASKVDAIKATLDNDEE-KVGA-----DIVKRALs 504
Cdd:NF041082 367 ILLRGG-TEHVVDEVERALEDALRVVRVVLEDGkVVAGGGAPEVELALRLREYAASVGGREQlAIEAfaealEIIPRTL- 444
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 257734882 505 yplkliAKNAGVN--GSVVSEKVL-SNDNVKFGYNAATGKYEDLMAAGIIDPTKVVRCCLEHAASVAKTFLMSDCVV 578
Cdd:NF041082 445 ------AENAGLDpiDALVELRSAhEKGNKTAGLDVYTGKVVDMLEIGVVEPLRVKTQAIKSATEAAVMILRIDDVI 515
|
|
| chap_CCT_eta |
TIGR02345 |
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ... |
77-579 |
1.17e-13 |
|
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT eta chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.
Pssm-ID: 274086 [Multi-domain] Cd Length: 523 Bit Score: 73.64 E-value: 1.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 77 KLADLVGVTLGPKGRNVVLESKYGSPRIVNDGVTVAREVELEDPVenigAKLVRQAAAKTNDLAGDGTTTSVVLAQGFIA 156
Cdd:TIGR02345 29 AIAEALKTTLGPRGMDKLIVGSNGKATISNDGATILKLLDIVHPA----AKTLVDIAKSQDAEVGDGTTSVTILAGELLK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 157 EGVKVVAAGANPVLITRGIEKTAKALVTELKKMSKEVEDS-----ELADVAAVSAGNNDEIGN-------MIAEAMSKVG 224
Cdd:TIGR02345 105 EAKPFIEEGVHPQLIIRCYREALSLAVEKIKEIAVTIDEEkgeqrELLEKCAATALSSKLISHnkeffskMIVDAVLSLD 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 225 RKGV------VTLEEGKSAENNLYvVEGMQFDRGYISPYFvtdsEKMSVEFDNCKLLLVDKKI------TNARDLVGVLE 292
Cdd:TIGR02345 185 RDDLdlkligIKKVQGGALEDSQL-VNGVAFKKTFSYAGF----EQQPKKFANPKILLLNVELelkaekDNAEIRVEDVE 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 293 DAIRggypIL-----IIAEDIEQ--EALATLVVNKLrgtlkiaalrapGFGERKSQYLDDIAILTGATVIREEVGLSLDK 365
Cdd:TIGR02345 260 DYQA----IVdaewaIIFRKLEKivESGANVVLSKL------------PIGDLATQYFADRDIFCAGRVSAEDLKRVIKA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 366 AGKEVLGNASKvvLTKETSTIVGDGSTQDAVKKRVtqikNLIeqaeQDYEKEKLNERIakLSGGVAviQVGAQTETELKE 445
Cdd:TIGR02345 324 CGGSIQSTTSD--LEADVLGTCALFEERQIGSERY----NYF----TGCPHAKTCTII--LRGGAE--QFIEEAERSLHD 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 446 KKLRVEDALNATKaaveegIVVGGGCTLLRLASKVDAIKATLDNDEEKVgADIVKRALSYPLKLIAKNAGVNGSVVSEKV 525
Cdd:TIGR02345 390 AIMIVRRALKNKK------IVAGGGAIEMELSKCLRDYSKTIDGKQQLI-INAFAKALEIIPRQLCENAGFDSIEILNKL 462
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 257734882 526 L---SNDNVKFGYNAATGKYEDLMAAGIIDPTKVVRCCLEHAASVAKTFLMSDCVVV 579
Cdd:TIGR02345 463 RsrhAKGGKWYGVDINTEDIGDNFEAFVWEPALVKINALKAAFEAACTILSVDETIT 519
|
|
| TCP1_epsilon |
cd03339 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ... |
78-228 |
1.30e-12 |
|
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: 70.41 E-value: 1.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 78 LADLVGVTLGPKGRNVVLESKYGSPRIVNDGVTVAREVELEDPVenigAKLVRQAAAKTNDLAGDGTTTSVVLAQGFIAE 157
Cdd:cd03339 35 VANILRTSLGPRGMDKILVSPDGEVTVTNDGATILEKMDVDHQI----AKLLVELSKSQDDEIGDGTTGVVVLAGALLEQ 110
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 257734882 158 GVKVVAAGANPVLITRGIEKTAKALVTELKKMSKEVEDSEladvaavsagnnDEIGNMIAEAMSKVGRKGV 228
Cdd:cd03339 111 AEKLLDRGIHPIRIADGYEQACKIAVEHLEEIADKIEFSP------------DNKEPLIQTAMTSLGSKIV 169
|
|
| TCP1_delta |
cd03338 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ... |
78-205 |
9.69e-11 |
|
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: 64.23 E-value: 9.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 78 LADLVGVTLGPKGRNVVLESKYGSPRIVNDGVTVAREVELEDPVENIGAKLvrqaaAKTNDL-AGDGTTTSVVLAQGFIA 156
Cdd:cd03338 20 VADAIRTSLGPRGMDKMIQTGKGEVIITNDGATILKQMSVLHPAAKMLVEL-----SKAQDIeAGDGTTSVVVLAGALLS 94
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 257734882 157 EGVKVVAAGANPVLITRGIEKTAKALVTELKKMSKEVE---DSELADVAAVS 205
Cdd:cd03338 95 ACESLLKKGIHPTVISESFQIAAKKAVEILDSMSIPVDlndRESLIKSATTS 146
|
|
| chap_CCT_alpha |
TIGR02340 |
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ... |
77-586 |
2.47e-10 |
|
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT alpha chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.
Pssm-ID: 274081 [Multi-domain] Cd Length: 536 Bit Score: 63.20 E-value: 2.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 77 KLADLVGVTLGPKGRNVVLESKYGSPRIVNDGVTVAREVELEDPveniGAKLVRQAAAKTNDLAGDGTTTSVVLAQGFIA 156
Cdd:TIGR02340 23 AIANIVKTSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHP----AAKILVELAQLQDREVGDGTTSVVIIAAELLK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 157 EGVKVVAAGANPVLITRGIEKTAKALVTELKK-MSKEVED---SELADVAAVS------AGNNDEIGNMIAEAMSKV--- 223
Cdd:TIGR02340 99 RADELVKNKIHPTSVISGYRLACKEAVKYIKEnLSVSVDElgrEALINVAKTSmsskiiGLDSDFFSNIVVDAVLAVktt 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 224 GRKGVVTL---------EEGKSAENNLYVvegmqfdRGYISPYFVTdSEKMSVEFDNCKLLLVDKKITNARDLVGV---- 290
Cdd:TIGR02340 179 NENGETKYpikainilkAHGKSARESMLV-------KGYALNCTVA-SQQMPKRIKNAKIACLDFNLQKAKMALGVqivv 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 291 -----LEDA---------------IRGGYPILIIAEDIEQEALATLVVNKLRGTLKIaalrapgfgerKSQYLDDIAILT 350
Cdd:TIGR02340 251 ddpekLEQIrqreaditkerikkiLDAGANVVLTTGGIDDMCLKYFVEAGAMGVRRC-----------KKEDLKRIAKAT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 351 GATVIreevgLSL-DKAGKEV-----LGNASKVVLTKetstiVGDgstqdavkKRVTQIKNLieqaeqdyekeklneria 424
Cdd:TIGR02340 320 GATLV-----STLaDLEGEETfeasyLGFADEVVQER-----IAD--------DECILIKGT------------------ 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 425 KLSGGVAVIQVGAQtETELKEKKLRVEDALNATKAAVEEGIVV-GGGCTLLRLASKVDAIKATLDNDEEKVGADIVKRAL 503
Cdd:TIGR02340 364 KKRKSASIILRGAN-DFMLDEMERSLHDALCVVKRTLESNSVVpGGGAVEAALSIYLENFATTLGSREQLAIAEFARALL 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 504 SYPlKLIAKNAGVNGSVVSEKVLSNDNVK-----------FGYNAATGKYEDLMAAGIIDPTKVVRCCLEHAASVAKTFL 572
Cdd:TIGR02340 443 IIP-KTLAVNAAKDSTELVAKLRAYHAAAqlkpekkhlkwYGLDLVNGKIRDNKEAGVLEPTVSKVKSLKFATEAAITIL 521
|
570
....*....|....
gi 257734882 573 MSDCVVVEIKEPEP 586
Cdd:TIGR02340 522 RIDDLIKLNPEQSK 535
|
|
| chap_CCT_beta |
TIGR02341 |
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ... |
70-578 |
2.90e-10 |
|
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: 62.95 E-value: 2.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 70 RLQAGVNKLA--DLVGVTLGPKGRNVVLES--KYGSPRIVNDGVTVAREVeledPVENIGAKLVRQAAAKTNDLAGDGTT 145
Cdd:TIGR02341 16 RLSSFVGAIAigDLVKSTLGPKGMDKILQSssSDASIMVTNDGATILKSI----GVDNPAAKVLVDMSKVQDDEVGDGTT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 146 TSVVLAQGFIAEGVKVVAAGANPVLITRGIEKTAKALVTELKKMSKEVED------SELADVAAVSAG------NNDEIG 213
Cdd:TIGR02341 92 SVTVLAAELLREAEKLINQKIHPQTIIAGYREATKAARDALLKSAVDNGSdevkfrQDLMNIARTTLSskilsqHKDHFA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 214 NMIAEAMSKVgrKGVVTLEE--------GKSAENNLyvvegmqfDRGYISPYFVTDSEKMSVEfdNCKLLLVDKKITNar 285
Cdd:TIGR02341 172 QLAVDAVLRL--KGSGNLEAiqiikklgGSLADSYL--------DEGFLLDKKIGVNQPKRIE--NAKILIANTGMDT-- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 286 DLVGVLEDAIR-GGYPILIIAEDIEQEALATLVVnklrgtlKIAALRAPGFGERKSQYLDDIAILTGATVIREEvglSLD 364
Cdd:TIGR02341 238 DKVKIFGSRVRvDSTAKVAELEHAEKEKMKEKVE-------KILKHGINCFINRQLIYNYPEQLFADAGVMAIE---HAD 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 365 KAGKEVLG--NASKVVLTKETSTIVGDGSTqdavkkrvtqikNLIEQAEQDyEKEKLNERIAKLSGGVAVIQVGAqTETE 442
Cdd:TIGR02341 308 FEGVERLAlvTGGEIVSTFDHPELVKLGSC------------DLIEEIMIG-EDKLLKFSGVKLGEACTIVLRGA-TQQI 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 443 LKEKKLRVEDALNATKAAVEEG-IVVGGGCTLLRLASKVDaIKATLDNDEEKVGADIVKRALSYPLKLIAKNAGVNGSVV 521
Cdd:TIGR02341 374 LDEAERSLHDALCVLSQTVKESrTVLGGGCSEMLMSKAVT-QEAQRTPGKEALAVEAFARALRQLPTIIADNAGFDSAEL 452
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 522 SEKV---LSNDNVKFGYNAATGKYEDLMAAGIIDPTKVVRCCLEHAASVAKTFLMSDCVV 578
Cdd:TIGR02341 453 VAQLraaHYNGNTTMGLDMNEGTIADMRQLGITESYKVKRAVVSSAAEAAEVILRVDNII 512
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
70-195 |
3.08e-10 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 62.74 E-value: 3.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 70 RLQA--GVNKLADLVGVTLGPKGRNVVLES-----KYGSPRIVNDGVTVAREVELEDPVenigAKLVRQAAAKTNDLAGD 142
Cdd:PTZ00212 24 RLQSfvGAIAVADLVKTTLGPKGMDKILQPmsegpRSGNVTVTNDGATILKSVWLDNPA----AKILVDISKTQDEEVGD 99
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 257734882 143 GTTTSVVLAQGFIAEGVKVVAAGANPVLITRGIEktaKALVTELKKMSKEVED 195
Cdd:PTZ00212 100 GTTSVVVLAGELLREAEKLLDQKIHPQTIIEGWR---MALDVARKALEEIAFD 149
|
|
| chap_CCT_delta |
TIGR02342 |
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ... |
78-197 |
4.06e-10 |
|
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: 62.49 E-value: 4.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 78 LADLVGVTLGPKGRNVVLESKYGSPRIVNDGVTVAREVELEDPVenigAKLVRQAAAKTNDLAGDGTTTSVVLAQGFIAE 157
Cdd:TIGR02342 21 VADAIRTSLGPKGMDKMIQDGKGEVIITNDGATILKQMAVLHPA----AKMLVELSKAQDIEAGDGTTSVVILAGALLGA 96
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 257734882 158 GVKVVAAGANPVLITRGIEKTAKALVTELKKMSKEVEDSE 197
Cdd:TIGR02342 97 CERLLNKGIHPTIISESFQSAADEAIKILDEMSIPVDLSD 136
|
|
| TCP1_theta |
cd03341 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ... |
60-579 |
7.90e-10 |
|
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: 61.47 E-value: 7.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 60 HFN-KDGTTIRRLQAgVNKLADLVGVTLGPKGRNVVLESKYGSPRIVNDGVTVAREVELEDPVenigAKLVRQAAAKTND 138
Cdd:cd03341 2 HYSgLEEAVLRNIEA-CKELSQITRTSYGPNGMNKMVINHLEKLFVTSDAATILRELEVQHPA----AKLLVMASQMQEE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 139 LAGDGTTTSVVLAQGFIAEGVKVVAAGANPVLITRGIEKTAKALVTELKKMS-KEVEDseLADVAAVSA----------- 206
Cdd:cd03341 77 EIGDGTNLVVVLAGELLEKAEELLRMGLHPSEIIEGYEKALKKALEILEELVvYKIED--LRNKEEVSKalktaiaskqy 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 207 GNNDEIGNMIAEAMSKVGRK----------GVVTLeEGKSAENNlYVVEGMQFDRgyispyfvtDSEKmSVefdncklll 276
Cdd:cd03341 155 GNEDFLSPLVAEACISVLPEnignfnvdniRVVKI-LGGSLEDS-KVVRGMVFKR---------EPEG-SV--------- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 277 vdKKITNARdlVGVLEDAIRGGYPILIIAEDIEQEALATLvvNKlrgtLKIAALRAPgfgerkSQY-LDDIAILTGATVI 355
Cdd:cd03341 214 --KRVKKAK--VAVFSCPFDIGVNVIVAGGSVGDLALHYC--NK----YGIMVIKIN------SKFeLRRLCRTVGATPL 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 356 -------REEVGlSLDKAGKEVLGNASKVVL-----TKETSTIVGDGSTQdavkkrvtQIKNLIEQAeqdyekeklneri 423
Cdd:cd03341 278 prlgaptPEEIG-YCDSVYVEEIGDTKVVVFrqnkeDSKIATIVLRGATQ--------NILDDVERA------------- 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 424 aklsggvaviqvgaqtetelkekklrVEDALNATKAAVEEG-IVVGGGCTLLRLASKVDAIKATLDNDEEKVgadIVKRA 502
Cdd:cd03341 336 --------------------------IDDGVNVFKSLTKDGrFVPGAGATEIELAKKLKEYGEKTPGLEQYA---IKKFA 386
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 503 LSYPL--KLIAKNAGVNGSVV-----SEKVLSNDNVKFGYNAATGKYEDLMAAGIIDPTKVVRCCLEHAASVAKTFLMSD 575
Cdd:cd03341 387 EAFEVvpRTLAENAGLDATEVlselyAAHQKGNKSAGVDIESGDEGTKDAKEAGIFDHLATKKWAIKLATEAAVTVLRVD 466
|
....
gi 257734882 576 CVVV 579
Cdd:cd03341 467 QIIM 470
|
|
| TCP1_beta |
cd03336 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ... |
60-199 |
1.05e-09 |
|
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: 61.19 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 60 HFNKDGTTIR----RLQA--GVNKLADLVGVTLGPKGRNVVLES--KYGSPRIVNDGVTVAREVELEDPVenigAKLVRQ 131
Cdd:cd03336 1 ILKDGAQEEKgetaRLSSfvGAIAIGDLVKTTLGPKGMDKILQSvgRSGGVTVTNDGATILKSIGVDNPA----AKVLVD 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 257734882 132 AAAKTNDLAGDGTTTSVVLAQGFIAEGVKVVAAGANPVLITRGIEKTAKALVTELKKMSKEVEDSELA 199
Cdd:cd03336 77 ISKVQDDEVGDGTTSVTVLAAELLREAEKLVAQKIHPQTIIEGYRMATAAAREALLSSAVDHSSDEEA 144
|
|
| TCP1_eta |
cd03340 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ... |
77-222 |
1.50e-09 |
|
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: 60.76 E-value: 1.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 77 KLADLVGVTLGPKGRNVVLESKYGSPRIVNDGVTVAREVELEDPVenigAKLVRQAAAKTNDLAGDGTTTSVVLAQGFIA 156
Cdd:cd03340 27 AIADAVRTTLGPRGMDKLIVDGRGKVTISNDGATILKLLDIVHPA----AKTLVDIAKSQDAEVGDGTTSVVVLAGEFLK 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 257734882 157 EGVKVVAAGANPVLITRGIEKTAKALVTELKKM-------SKEVEDSELADVAAVS------AGNNDEIGNMIAEAMSK 222
Cdd:cd03340 103 EAKPFIEDGVHPQIIIRGYRKALQLAIEKIKEIavnidkeDKEEQRELLEKCAATAlnskliASEKEFFAKMVVDAVLS 181
|
|
| chap_CCT_theta |
TIGR02346 |
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ... |
62-579 |
5.10e-09 |
|
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: 58.96 E-value: 5.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 62 NKDGTTIRRLQAgVNKLADLVGVTLGPKGRNVVLESKYGSPRIVNDGVTVAREVELEDPVenigAKLVRQAAAKTNDLAG 141
Cdd:TIGR02346 15 GLEEAVIKNIEA-CKELSQITRTSLGPNGMNKMVINHLEKLFVTNDAATILRELEVQHPA----AKLLVMASEMQENEIG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 142 DGTTTSVVLAQGFIAEGVKVVAAGANPVLITRGIEKTAKALVTELKKMS----------KEVEDSELADVAAVSAGNNDE 211
Cdd:TIGR02346 90 DGTNLVLVLAGELLNKAEELIRMGLHPSEIIKGYEMALKKAMEILEELVvwevkdlrdkDELIKALKASISSKQYGNEDF 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 212 IGNMIAEAMSKVGRKGVVTLE---------EGKSAENNlYVVEGMQFDRGYISPyfVTDSEKMSVEFDNCKLllvDKKIT 282
Cdd:TIGR02346 170 LAQLVAQACSTVLPKNPQNFNvdnirvckiLGGSLSNS-EVLKGMVFNREAEGS--VKSVKNAKVAVFSCPL---DTATT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 283 ---------NARDLVG-------VLEDAIR----GGYPILIIAEDIEQEALATLvvnklrGTLKIAALRAPGFGErksqy 342
Cdd:TIGR02346 244 etkgtvlihNAEELLNyskgeenQIEAMIKaiadSGVNVIVTGGSVGDMALHYL------NKYNIMVLKIPSKFE----- 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 343 LDDIAILTGATVIreevgLSLDKAGKEVLGNASKVvltkETSTIVGDgstqdavkkRVTqiknLIEQAEQDyekeklner 422
Cdd:TIGR02346 313 LRRLCKTVGATPL-----PRLGAPTPEEIGYVDSV----YVSEIGGD---------KVT----VFKQENGD--------- 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 423 iaklsGGVAVIQVGAQTETELKEKKLRVEDALNATKAAVEEG-IVVGGGCTLLRLASKVdaikATLDNDEEKVGADIVKR 501
Cdd:TIGR02346 362 -----SKISTIILRGSTDNLLDDIERAIDDGVNTVKALVKDGrLLPGAGATEIELASRL----TKYGEKLPGLDQYAIKK 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 502 -ALSYPL--KLIAKNAGVNGSVVSEKVLS-----NDNVKFGYNAATGKYEDLMAAGIIDPTKVVRCCLEHAASVAKTFLM 573
Cdd:TIGR02346 433 fAEAFEIipRTLAENAGLNANEVIPKLYAahkkgNKSKGIDIEAESDGVKDASEAGIYDMLATKKWAIKLATEAAVTVLR 512
|
....*.
gi 257734882 574 SDCVVV 579
Cdd:TIGR02346 513 VDQIIM 518
|
|
| chap_CCT_zeta |
TIGR02347 |
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ... |
62-248 |
6.77e-09 |
|
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: 58.59 E-value: 6.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 62 NKDGTTIRRLQA------GVNKLADLVGVTLGPKGRNVVLESKYGSPRIVNDGVTVAREVELEDPVenigAKLVRQAAAK 135
Cdd:TIGR02347 6 NPKAESLRRDAAlmmninAARGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEMQIQHPT----ASMIARAATA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 136 TNDLAGDGTTTSVVLAQGFIAEGVKVVAAGANPVLITRGIEKTAKALVTELKKMSKEVEDSE----LADVAAVSAGNN-- 209
Cdd:TIGR02347 82 QDDITGDGTTSTVLLIGELLKQAERYILEGVHPRIITEGFEIARKEALQFLDKFKVKKEDEVdrefLLNVARTSLRTKlp 161
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 257734882 210 ----DEIGNMIAEAMSKVGRKGvvtleegksAENNLYVVEGMQ 248
Cdd:TIGR02347 162 adlaDQLTEIVVDAVLAIKKDG---------EDIDLFMVEIME 195
|
|
| TCP1_gamma |
cd03337 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ... |
78-578 |
2.41e-08 |
|
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: 56.54 E-value: 2.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 78 LADLVGVTLGPKGRNVVLESKYGSPRIVNDGVTVAREVELEDPveniGAKLVRQAAAKTNDLAGDGTTTSVVLAQGFIAE 157
Cdd:cd03337 28 VADVIRTCLGPRAMLKMLLDPMGGIVLTNDGNAILREIDVAHP----AAKSMIELSRTQDEEVGDGTTSVIILAGEILAV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 158 GVKVVAAGANPVLITRGIEKTAKALVTELKKMSKEVE---DSELADVAAVSAGN------NDEIGNMIAEAMSKVGRKGV 228
Cdd:cd03337 104 AEPFLERGIHPTVIIKAYRKALEDALKILEEISIPVDvndRAQMLKIIKSCIGTkfvsrwSDLMCNLALDAVKTVAVEEN 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 229 VTLEE-------------GKSAENNlYVVEGMQFDRGYISPyfvtdseKMSVEFDNCKLLLVDKKitnardlvgvLEdai 295
Cdd:cd03337 184 GRKKEidikryakvekipGGEIEDS-RVLDGVMLNKDVTHP-------KMRRRIENPRIVLLDCP----------LE--- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 296 rggYpiLIIAE----DIEQEALatlvvnklrgtLK--IAALRApgfgERKSQyLDDIAILTGATVI-REE------VG-- 360
Cdd:cd03337 243 ---Y--LVITEkgvsDLAQHYL-----------VKagITALRR----VRKTD-NNRIARACGATIVnRPEeltesdVGtg 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 361 ---LSLDKAGKEVLgnaSKVVLTKETS--TIVGDGSTqdavkkrvtqiknlieqaeqdyeKEKLNEriaklsggvaviqv 435
Cdd:cd03337 302 aglFEVKKIGDEYF---TFITECKDPKacTILLRGAS-----------------------KDVLNE-------------- 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 436 gaqTETELkekklrvEDALNATKAAVEEG-IVVGGGCTLLRLASKVdAIKATLDNDEEKVGADIVKRALSYPLKLIAKNA 514
Cdd:cd03337 342 ---VERNL-------QDAMAVARNIILNPkLVPGGGATEMAVSHAL-SEKAKSIEGVEQWPYKAVASALEVIPRTLAQNC 410
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 257734882 515 GVN-GSVVSE---KVLSNDNVKFGYNAATGKYEDLMAAGIIDPTKVVRCCLEHAASVAKTFLMSDCVV 578
Cdd:cd03337 411 GANvIRTLTElraKHAQGENSTWGIDGETGDIVDMKELGIWDPLAVKAQTYKTAIEAACMLLRIDDIV 478
|
|
| TCP1_zeta |
cd03342 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
78-575 |
2.89e-08 |
|
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: 56.50 E-value: 2.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 78 LADLVGVTLGPKGRNVVLESKYGSPRIVNDGVTVAREVELEDPVENIGAKlvrqAAAKTNDLAGDGTTTSVVL------- 150
Cdd:cd03342 24 LQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLSEMQIQHPTASMIAR----AATAQDDITGDGTTSNVLLigellkq 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 151 AQGFIAEGVkvvaagaNPVLITRGIEKTAKALVTELKKMSKEVEDSELADVAAVSAGN--NDEIGNMIAEAMSKVGRKGV 228
Cdd:cd03342 100 AERYIQEGV-------HPRIITEGFELAKNKALKFLESFKVPVEIDTDRELLLSVARTslRTKLHADLADQLTEIVVDAV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 229 VTLEEgKSAENNLYVVEGMQFDRGyispyfvTDSEKMSVefdncKLLLVD---------KKITNARDLV-GV-LE---DA 294
Cdd:cd03342 173 LAIYK-PDEPIDLHMVEIMQMQHK-------SDSDTKLI-----RGLVLDhgarhpdmpKRVENAYILTcNVsLEyekTE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 295 IRGG--YPILIIAEDIEQEALATLVVNklrgtlKIAALRapgfgERKSQYLDDIAILTGATVIReevglSLDKAGKEVLG 372
Cdd:cd03342 240 VNSGffYSVVINQKGIDPPSLDMLAKE------GILALR-----RAKRRNMERLTLACGGVAMN-----SVDDLSPECLG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 373 NASKV---VLTKETSTIVGDgsTQDavKKRVTqiknlieqaeqdyekeklneriaklsggvavIQVGAQTETELKEKKLR 449
Cdd:cd03342 304 YAGLVyerTLGEEKYTFIEG--VKN--PKSCT-------------------------------ILIKGPNDHTITQIKDA 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 450 VEDALNATKAAVEEGIVV-GGGCTLLRLASKVDAIKATLdNDEEKVGADIVKRALSYPLKLIAKNAGVNGSVVSEKVLSN 528
Cdd:cd03342 349 IRDGLRAVKNAIEDKCVVpGAGAFEVALYAHLKEFKKSV-KGKAKLGVQAFADALLVIPKTLAENSGLDVQETLVKLQDE 427
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 257734882 529 ---DNVKFGYNAATGKYEDLMAAGIIDPTKVVRCCLEHAASVAKTFLMSD 575
Cdd:cd03342 428 yaeGGQVGGVDLDTGEPMDPESEGIWDNYSVKRQILHSATVIASQLLLVD 477
|
|
| TCP1_alpha |
cd03335 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ... |
75-575 |
7.44e-07 |
|
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: 51.90 E-value: 7.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 75 VNKLADLVGVTLGPKGRNVVLESKYGSPRIVNDGVTVAREVELEDPveniGAKLVRQAAAKTNDLAGDGTTTSVVLAQGF 154
Cdd:cd03335 17 AMAIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHP----AAKILVELAQLQDKEVGDGTTSVVIIAAEL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 155 IAEGVKVVAAGANPVLITRGIEKTAKALVTELKK-MSKEVED---SELADVAAVS------AGNNDEIGNMIAEAMSKVG 224
Cdd:cd03335 93 LKRANELVKQKIHPTTIISGYRLACKEAVKYIKEhLSISVDNlgkESLINVAKTSmsskiiGADSDFFANMVVDAILAVK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 225 R-----------KGVVTLE-EGKSAENNlYVVEGMQFDRGyispyfvTDSEKMSVEFDNCKLLLVDKKITNARDLVGV-- 290
Cdd:cd03335 173 TtnekgktkypiKAVNILKaHGKSAKES-YLVNGYALNCT-------RASQGMPTRVKNAKIACLDFNLQKTKMKLGVqv 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 291 -------LEdAIRgGYPILIIAEDIEQ--EALATLVVN---------KLRGTLKIAALRapgfgeR-KSQYLDDIAILTG 351
Cdd:cd03335 245 vvtdpekLE-KIR-QRESDITKERIKKilAAGANVVLTtggiddmclKYFVEAGAMAVR------RvKKEDLRRIAKATG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 352 ATVIreevgLSL-DKAGKEV-----LGNASKVVLTKetstiVGDgstqdavkKRVTQIKNLieqaeqdyekeklneriaK 425
Cdd:cd03335 317 ATLV-----STLaNLEGEETfdpsyLGEAEEVVQER-----IGD--------DELILIKGT------------------K 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 426 LSGGVAVIQVGAQtETELKEKKLRVEDALNATKAAVEEG-IVVGGGCTLLRLASKVDAIKATLDNDEEKVGADIVKRALS 504
Cdd:cd03335 361 KRSSASIILRGAN-DFMLDEMERSLHDALCVVKRTLESNsVVPGGGAVETALSIYLENFATTLGSREQLAIAEFAEALLV 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 505 YPlKLIAKNAGVNGSVVSEKVLS----------NDNVKF-GYNAATGKYEDLMAAGIIDPTKVVRCCLEHAASVAKTFLM 573
Cdd:cd03335 440 IP-KTLAVNAAKDATELVAKLRAyhaaaqvkpdKKHLKWyGLDLINGKVRDNLEAGVLEPTVSKIKSLKFATEAAITILR 518
|
..
gi 257734882 574 SD 575
Cdd:cd03335 519 ID 520
|
|
| chap_CCT_gamma |
TIGR02344 |
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ... |
78-232 |
9.47e-06 |
|
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: 48.58 E-value: 9.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 78 LADLVGVTLGPKGRNVVLESKYGSPRIVNDGVTVAREVELEDPveniGAKLVRQAAAKTNDLAGDGTTTSVVLAQGFIAE 157
Cdd:TIGR02344 28 VADIIRTCLGPRSMLKMLLDPMGGIVMTNDGNAILREIDVAHP----AAKSMIELSRTQDEEVGDGTTSVIILAGEMLSV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257734882 158 GVKVVAAGANPVLITRGIEKTAKALVTELKKMSKEVE---DSELADVAAVSAGN------NDEIGNMIAEAMSKVGRKGV 228
Cdd:TIGR02344 104 AEPFLEQNIHPTVIIRAYRKALDDALSVLEEISIPVDvndDAAMLKLIQSCIGTkfvsrwSDLMCDLALDAVRTVQRDEN 183
|
....
gi 257734882 229 VTLE 232
Cdd:TIGR02344 184 GRKE 187
|
|
| |
