|
Name |
Accession |
Description |
Interval |
E-value |
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
1-539 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 989.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 1 MAKDIKFSSDARAAMVRGVDTLADTVKVTLGPKGRNVVLEKAFGSPLITNDGVTIAKEIELEDHFENMGAKLVSEVASKT 80
Cdd:PRK00013 1 MAKDIKFGEDARRKLLRGVNKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDPFENMGAQLVKEVASKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 81 NDIAGDGTTTATVLTQAIVREGLKNVTAGANPIGIRRGIEAAVSTAVEELKAIAQPVANKEAIAQVAAVSSRS-EKVGEY 159
Cdd:PRK00013 81 NDVAGDGTTTATVLAQAIVREGLKNVAAGANPMDLKRGIDKAVEAAVEELKKISKPVEDKEEIAQVATISANGdEEIGKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 160 ISEAMERVGNDGVITIEESRGMETELEVVEGMQFDRGYLSQYMVTDNEKMVADLDNPFILVTDKKISNIQDVLPLLEEVL 239
Cdd:PRK00013 161 IAEAMEKVGKEGVITVEESKGFETELEVVEGMQFDRGYLSPYFVTDPEKMEAELENPYILITDKKISNIQDLLPVLEQVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 240 KTSRPLLIIADDVDGEALPTLVLNKIRGTFNVVAVKAPGFGDRRKAMLEDIAVLTGATVITEDLGLELKDATMAALGQAS 319
Cdd:PRK00013 241 QSGKPLLIIAEDVEGEALATLVVNKLRGTLKVVAVKAPGFGDRRKAMLEDIAILTGGTVISEELGLKLEDATLEDLGQAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 320 KVTVDKDSTVIVEGAGSAEAIANRVNLIKSQLETTTSEFDREKLQERLAKLSGGVAVVKVGAATETALKEMKLRIEDALN 399
Cdd:PRK00013 321 KVVVTKDNTTIVDGAGDKEAIKARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATEVEMKEKKDRVEDALH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 400 ATRAAVEEGIVAGGGTALVNVIAKVAEL-DLEGDDATGRNIVLRALEEPVRQIAYNAGYEGSVIIDKLKNS-PVGTGFNA 477
Cdd:PRK00013 401 ATRAAVEEGIVPGGGVALLRAAPALEALkGLNGDEATGINIVLRALEAPLRQIAENAGLEGSVVVEKVKNGkGKGYGYNA 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1934310476 478 ANGEWVDMVEAGIIDPVKVTRSALQNAASVASLILTTEAVVANKPEPETPAAPAMDPGMMGY 539
Cdd:PRK00013 481 ATGEYVDMIEAGIIDPTKVTRSALQNAASVAGLLLTTEAVVADKPEKKAAAPPMGGGGMGGM 542
|
|
| groEL |
PRK12849 |
chaperonin GroEL; Reviewed |
1-539 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237230 Cd Length: 542 Bit Score: 868.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 1 MAKDIKFSSDARAAMVRGVDTLADTVKVTLGPKGRNVVLEKAFGSPLITNDGVTIAKEIELEDHFENMGAKLVSEVASKT 80
Cdd:PRK12849 1 MAKIIKFDEEARRALERGVNKLADAVKVTLGPKGRNVVIDKSFGAPTITKDGVSIAKEIELEDPFENLGAQLVKEVASKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 81 NDIAGDGTTTATVLTQAIVREGLKNVTAGANPIGIRRGIEAAVSTAVEELKAIAQPVANKEAIAQVAAVSSRS-EKVGEY 159
Cdd:PRK12849 81 NDVAGDGTTTATVLAQALVQEGLKNVAAGANPMDLKRGIDKAVEAVVEELKALARPVSGSEEIAQVATISANGdEEIGEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 160 ISEAMERVGNDGVITIEESRGMETELEVVEGMQFDRGYLSQYMVTDNEKMVADLDNPFILVTDKKISNIQDVLPLLEEVL 239
Cdd:PRK12849 161 IAEAMEKVGKDGVITVEESKTLETELEVTEGMQFDRGYLSPYFVTDPERMEAVLEDPLILLTDKKISSLQDLLPLLEKVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 240 KTSRPLLIIADDVDGEALPTLVLNKIRGTFNVVAVKAPGFGDRRKAMLEDIAVLTGATVITEDLGLELKDATMAALGQAS 319
Cdd:PRK12849 241 QSGKPLLIIAEDVEGEALATLVVNKLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGLKLEEVTLDDLGRAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 320 KVTVDKDSTVIVEGAGSAEAIANRVNLIKSQLETTTSEFDREKLQERLAKLSGGVAVVKVGAATETALKEMKLRIEDALN 399
Cdd:PRK12849 321 RVTITKDNTTIVDGAGDKEAIEARVAQIRRQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATEVELKERKDRVEDALN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 400 ATRAAVEEGIVAGGGTALVNVIAKVAELD-LEGDDATGRNIVLRALEEPVRQIAYNAGYEGSVIIDKLKNSPVGTGFNAA 478
Cdd:PRK12849 401 ATRAAVEEGIVPGGGVALLRAAKALDELAgLNGDQAAGVEIVRRALEAPLRQIAENAGLDGSVVVAKVLELEDGFGFNAA 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1934310476 479 NGEWVDMVEAGIIDPVKVTRSALQNAASVASLILTTEAVVANKPEPETPAAPAMDPGMMGY 539
Cdd:PRK12849 481 TGEYGDLIAAGIIDPVKVTRSALQNAASVAGLLLTTEALVADKPEEEDPPGGMGGMGGMGH 541
|
|
| GroEL |
cd03344 |
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ... |
3-519 |
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: 862.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 3 KDIKFSSDARAAMVRGVDTLADTVKVTLGPKGRNVVLEKAFGSPLITNDGVTIAKEIELEDHFENMGAKLVSEVASKTND 82
Cdd:cd03344 1 KDIKFGEEARKALLRGVNKLADAVKVTLGPKGRNVVIEKSFGSPKITKDGVTVAKEIELEDPFENMGAQLVKEVASKTND 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 83 IAGDGTTTATVLTQAIVREGLKNVTAGANPIGIRRGIEAAVSTAVEELKAIAQPVANKEAIAQVAAVSSRS-EKVGEYIS 161
Cdd:cd03344 81 VAGDGTTTATVLARAIIKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKPVKTKEEIAQVATISANGdEEIGELIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 162 EAMERVGNDGVITIEESRGMETELEVVEGMQFDRGYLSQYMVTDNEKMVADLDNPFILVTDKKISNIQDVLPLLEEVLKT 241
Cdd:cd03344 161 EAMEKVGKDGVITVEEGKTLETELEVVEGMQFDRGYLSPYFVTDPEKMEVELENPYILLTDKKISSIQELLPILELVAKA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 242 SRPLLIIADDVDGEALPTLVLNKIRGTFNVVAVKAPGFGDRRKAMLEDIAVLTGATVITEDLGLELKDATMAALGQASKV 321
Cdd:cd03344 241 GRPLLIIAEDVEGEALATLVVNKLRGGLKVCAVKAPGFGDRRKAMLEDIAILTGGTVISEELGLKLEDVTLEDLGRAKKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 322 TVDKDSTVIVEGAGSAEAIANRVNLIKSQLETTTSEFDREKLQERLAKLSGGVAVVKVGAATETALKEMKLRIEDALNAT 401
Cdd:cd03344 321 VVTKDDTTIIGGAGDKAAIKARIAQIRKQIEETTSDYDKEKLQERLAKLSGGVAVIKVGGATEVELKEKKDRVEDALNAT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 402 RAAVEEGIVAGGGTALVNVIAKVAELD-LEGDDATGRNIVLRALEEPVRQIAYNAGYEGSVIIDKLKNSPVGTGFNAANG 480
Cdd:cd03344 401 RAAVEEGIVPGGGVALLRASPALDKLKaLNGDEKLGIEIVRRALEAPLRQIAENAGVDGSVVVEKVLESPDGFGYDAATG 480
|
490 500 510
....*....|....*....|....*....|....*....
gi 1934310476 481 EWVDMVEAGIIDPVKVTRSALQNAASVASLILTTEAVVA 519
Cdd:cd03344 481 EYVDMIEAGIIDPTKVVRSALQNAASVASLLLTTEALVV 519
|
|
| GroEL |
TIGR02348 |
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ... |
2-523 |
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: 849.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 2 AKDIKFSSDARAAMVRGVDTLADTVKVTLGPKGRNVVLEKAFGSPLITNDGVTIAKEIELEDHFENMGAKLVSEVASKTN 81
Cdd:TIGR02348 1 AKQIKFDEEARKALLRGVDKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDKFENMGAQLVKEVASKTN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 82 DIAGDGTTTATVLTQAIVREGLKNVTAGANPIGIRRGIEAAVSTAVEELKAIAQPVANKEAIAQVAAVSSRS-EKVGEYI 160
Cdd:TIGR02348 81 DVAGDGTTTATVLAQAIVKEGLKNVAAGANPIELKRGIEKAVEAVVEELKKLSKPVKGKKEIAQVATISANNdEEIGSLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 161 SEAMERVGNDGVITIEESRGMETELEVVEGMQFDRGYLSQYMVTDNEKMVADLDNPFILVTDKKISNIQDVLPLLEEVLK 240
Cdd:TIGR02348 161 AEAMEKVGKDGVITVEESKSLETELEVVEGMQFDRGYISPYFVTDAEKMEVELENPYILITDKKISNIKDLLPLLEKVAQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 241 TSRPLLIIADDVDGEALPTLVLNKIRGTFNVVAVKAPGFGDRRKAMLEDIAVLTGATVITEDLGLELKDATMAALGQASK 320
Cdd:TIGR02348 241 SGKPLLIIAEDVEGEALATLVVNKLRGTLNVCAVKAPGFGDRRKAMLEDIAILTGGQVISEELGLKLEEVTLDDLGKAKK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 321 VTVDKDSTVIVEGAGSAEAIANRVNLIKSQLETTTSEFDREKLQERLAKLSGGVAVVKVGAATETALKEMKLRIEDALNA 400
Cdd:TIGR02348 321 VTVDKDNTTIVEGAGDKAAIKARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATETEMKEKKLRIEDALNA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 401 TRAAVEEGIVAGGGTALVNVIAKVAELDLEGDD-ATGRNIVLRALEEPVRQIAYNAGYEGSVIIDKLKNSPVGTGFNAAN 479
Cdd:TIGR02348 401 TRAAVEEGIVPGGGVALLRAAAALEGLKGDGEDeAIGIDIVKRALEAPLRQIAENAGLDGAVVAEKVKELKGNFGFNAAT 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1934310476 480 GEWVDMVEAGIIDPVKVTRSALQNAASVASLILTTEAVVANKPE 523
Cdd:TIGR02348 481 GEYEDLVEAGIIDPTKVTRSALQNAASIAGLLLTTEAVVADKPE 524
|
|
| groEL |
PRK12850 |
chaperonin GroEL; Reviewed |
1-539 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237231 Cd Length: 544 Bit Score: 790.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 1 MAKDIKFSSDARAAMVRGVDTLADTVKVTLGPKGRNVVLEKAFGSPLITNDGVTIAKEIELEDHFENMGAKLVSEVASKT 80
Cdd:PRK12850 2 AAKEIRFSTDARDRLLRGVNILANAVKVTLGPKGRNVVLEKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVKEVASKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 81 NDIAGDGTTTATVLTQAIVREGLKNVTAGANPIGIRRGIEAAVSTAVEELKAIAQPVANKEAIAQVAAVS-SRSEKVGEY 159
Cdd:PRK12850 82 NDLAGDGTTTATVLAQAIVREGAKLVAAGMNPMDLKRGIDLAVAAVVDELKKIAKKVTSSKEIAQVATISaNGDESIGEM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 160 ISEAMERVGNDGVITIEESRGMETELEVVEGMQFDRGYLSQYMVTDNEKMVADLDNPFILVTDKKISNIQDVLPLLEEVL 239
Cdd:PRK12850 162 IAEAMDKVGKEGVITVEEAKTLGTELDVVEGMQFDRGYLSPYFVTNPEKMRAELEDPYILLHEKKISNLQDLLPILEAVV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 240 KTSRPLLIIADDVDGEALPTLVLNKIRGTFNVVAVKAPGFGDRRKAMLEDIAVLTGATVITEDLGLELKDATMAALGQAS 319
Cdd:PRK12850 242 QSGRPLLIIAEDVEGEALATLVVNKLRGGLKSVAVKAPGFGDRRKAMLEDIAVLTGGQVISEDLGIKLENVTLDMLGRAK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 320 KVTVDKDSTVIVEGAGSAEAIANRVNLIKSQLETTTSEFDREKLQERLAKLSGGVAVVKVGAATETALKEMKLRIEDALN 399
Cdd:PRK12850 322 RVLITKENTTIIDGAGDKKNIEARVKQIRAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKEKKDRVDDALH 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 400 ATRAAVEEGIVAGGGTALVNVIAKVAELD-LEGDDATGRNIVLRALEEPVRQIAYNAGYEGSVIIDKLKNSPVGTGFNAA 478
Cdd:PRK12850 402 ATRAAVEEGIVPGGGVALLRARSALRGLKgANADETAGIDIVRRALEEPLRQIATNAGFEGSVVVGKVAELPGNFGFNAQ 481
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1934310476 479 NGEWVDMVEAGIIDPVKVTRSALQNAASVASLILTTEAVVANKP--EPETPAAPAMDPGMMGY 539
Cdd:PRK12850 482 TGEYGDMVEAGIIDPAKVTRTALQDAASIAALLITTEAMVAEAPkkAAAAAAGPGPGMGGMGY 544
|
|
| GroEL |
COG0459 |
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ... |
1-528 |
0e+00 |
|
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227 Cd Length: 497 Bit Score: 767.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 1 MAKDIKFSSDARAAMVRGVDTLADTVKVTLGPKGRNVVLEKAFGSPLITNDGVTIAKEIELEDHFENMGAKLVSEVASKT 80
Cdd:COG0459 1 MAKQILFGEDARRANIRGVKALADAVKVTLGPKGRNVMLVKSFGDPTITNDGVTIAKEIELEDPFENMGAQLVKEVASKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 81 NDIAGDGTTTATVLTQAIVREGLKNVTAGANPIGIRRGIEAAVSTAVEELKAIAQPVANKEAIAQVAAVSSRS-EKVGEY 159
Cdd:COG0459 81 NDEAGDGTTTATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPVDDKEELAQVATISANGdEEIGEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 160 ISEAMERVGNDGVITIEESRGMETELEVVEGMQFDRGYLSQYMVTDNEKMVADLDNPFILVTDKKISNIQDVLPLLEEVL 239
Cdd:COG0459 161 IAEAMEKVGKDGVITVEEGKGLETELEVVEGMQFDKGYLSPYFVTDPEKMPAELENAYILLTDKKISSIQDLLPLLEKVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 240 KTSRPLLIIADDVDGEALPTLVLNKIRGTFNVVAVKAPGFGDRRKAMLEDIAVLTGATVITEDLGLELKDATMAALGQAS 319
Cdd:COG0459 241 QSGKPLLIIAEDIDGEALATLVVNGIRGVLRVVAVKAPGFGDRRKAMLEDIAILTGGRVISEDLGLKLEDVTLDDLGRAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 320 KVTVDKDSTVIVEGAGSAEAIanrvnliksqletttsefdreklqerlaklsggvaVVKVGAATETALKEMKLRIEDALN 399
Cdd:COG0459 321 RVEVDKDNTTIVEGAGNPKAI-----------------------------------VILVGAATEVEVKERKRRVEDALH 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 400 ATRAAVEEGIVAGGGTALVNVIAKVAEL--DLEGDDATGRNIVLRALEEPVRQIAYNAGYEGSVIIDKLKNSP-VGTGFN 476
Cdd:COG0459 366 ATRAAVEEGIVPGGGAALLRAARALRELaaKLEGDEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKVRAAKdKGFGFD 445
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1934310476 477 AANGEWVDMVEAGIIDPVKVTRSALQNAASVASLILTTEAVVANKPEPETPA 528
Cdd:COG0459 446 AATGEYVDMLEAGVIDPAKVKRSALQNAASVAGLILTTEAVIADKPEKEEAA 497
|
|
| groEL |
PRK12851 |
chaperonin GroEL; Reviewed |
1-536 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 171770 Cd Length: 541 Bit Score: 745.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 1 MAKDIKFSSDARAAMVRGVDTLADTVKVTLGPKGRNVVLEKAFGSPLITNDGVTIAKEIELEDHFENMGAKLVSEVASKT 80
Cdd:PRK12851 2 AAKEVKFHVEAREKMLRGVNILADAVKVTLGPKGRNVVIDKSFGAPTITNDGVTIAKEIELEDKFENMGAQMVREVASKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 81 NDIAGDGTTTATVLTQAIVREGLKNVTAGANPIGIRRGIEAAVSTAVEELKAIAQPVANKEAIAQVAAVSSRS-EKVGEY 159
Cdd:PRK12851 82 NDVAGDGTTTATVLAQAIVREGAKAVAAGANPMDLKRGIDRAVAAVVEELKANARPVTTNAEIAQVATISANGdAEIGRL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 160 ISEAMERVGNDGVITIEESRGMETELEVVEGMQFDRGYLSQYMVTDNEKMVADLDNPFILVTDKKISNIQDVLPLLEEVL 239
Cdd:PRK12851 162 VAEAMEKVGNEGVITVEESKTAETELEVVEGMQFDRGYLSPYFVTDADKMEAELEDPYILIHEKKISNLQDLLPVLEAVV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 240 KTSRPLLIIADDVDGEALPTLVLNKIRGTFNVVAVKAPGFGDRRKAMLEDIAVLTGATVITEDLGLELKDATMAALGQAS 319
Cdd:PRK12851 242 QSGKPLLIIAEDVEGEALATLVVNKLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGIKLENVTLEQLGRAK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 320 KVTVDKDSTVIVEGAGSAEAIANRVNLIKSQLETTTSEFDREKLQERLAKLSGGVAVVKVGAATETALKEMKLRIEDALN 399
Cdd:PRK12851 322 KVVVEKENTTIIDGAGSKTEIEGRVAQIRAQIEETTSDYDREKLQERLAKLAGGVAVIRVGASTEVEVKEKKDRVDDALH 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 400 ATRAAVEEGIVAGGGTALVN-VIAKVAELDLEGDDATGRNIVLRALEEPVRQIAYNAGYEGSVIIDKLKNSPVGTGFNAA 478
Cdd:PRK12851 402 ATRAAVEEGIVPGGGVALLRaVKALDKLETANGDQRTGVEIVRRALEAPVRQIAENAGAEGSVVVGKLREKPGGYGFNAA 481
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1934310476 479 NGEWVDMVEAGIIDPVKVTRSALQNAASVASLILTTEAVVANKPEPETPAAPAMDPGM 536
Cdd:PRK12851 482 TNEYGDLYAQGVIDPVKVVRTALQNAASVAGLLLTTEAMVAEKPKKEPAPPAPPGGGM 539
|
|
| PTZ00114 |
PTZ00114 |
Heat shock protein 60; Provisional |
2-536 |
0e+00 |
|
Heat shock protein 60; Provisional
Pssm-ID: 185455 Cd Length: 555 Bit Score: 710.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 2 AKDIKFSSDARAAMVRGVDTLADTVKVTLGPKGRNVVLEKAFGSPLITNDGVTIAKEIELEDHFENMGAKLVSEVASKTN 81
Cdd:PTZ00114 14 GKEIRFGDEARQSLLKGIERLADAVAVTLGPKGRNVIIEQEYGSPKITKDGVTVAKAIEFSDRFENVGAQLIRQVASKTN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 82 DIAGDGTTTATVLTQAIVREGLKNVTAGANPIGIRRGIEAAVSTAVEELKAIAQPVANKEAIAQVAAVSSRSEKV-GEYI 160
Cdd:PTZ00114 94 DKAGDGTTTATILARAIFREGCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQSRPVKTKEDILNVATISANGDVEiGSLI 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 161 SEAMERVGNDGVITIEESRGMETELEVVEGMQFDRGYLSQYMVTDNEKMVADLDNPFILVTDKKISNIQDVLPLLEEVLK 240
Cdd:PTZ00114 174 ADAMDKVGKDGTITVEDGKTLEDELEVVEGMSFDRGYISPYFVTNEKTQKVELENPLILVTDKKISSIQSILPILEHAVK 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 241 TSRPLLIIADDVDGEALPTLVLNKIRGTFNVVAVKAPGFGDRRKAMLEDIAVLTGATVITED-LGLELKDATMAALGQAS 319
Cdd:PTZ00114 254 NKRPLLIIAEDVEGEALQTLIINKLRGGLKVCAVKAPGFGDNRKDILQDIAVLTGATVVSEDnVGLKLDDFDPSMLGSAK 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 320 KVTVDKDSTVIVEGAGSAEAIANRVNLIKSQLETTTSEFDREKLQERLAKLSGGVAVVKVGAATETALKEMKLRIEDALN 399
Cdd:PTZ00114 334 KVTVTKDETVILTGGGDKAEIKERVELLRSQIERTTSEYDKEKLKERLAKLSGGVAVIKVGGASEVEVNEKKDRIEDALN 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 400 ATRAAVEEGIVAGGGTALVNVIAKVAEL----DLEGDDATGRNIVLRALEEPVRQIAYNAGYEGSVIIDKLKNS-PVGTG 474
Cdd:PTZ00114 414 ATRAAVEEGIVPGGGVALLRASKLLDKLeednELTPDQRTGVKIVRNALRLPTKQIAENAGVEGAVVVEKILEKkDPSFG 493
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1934310476 475 FNAANGEWVDMVEAGIIDPVKVTRSALQNAASVASLILTTEAVVANKPEPETPAAPAMDPGM 536
Cdd:PTZ00114 494 YDAQTGEYVNMFEAGIIDPTKVVRSALVDAASVASLMLTTEAAIVDLPKEKKKNKNSAAPPM 555
|
|
| groEL |
CHL00093 |
chaperonin GroEL |
1-523 |
0e+00 |
|
chaperonin GroEL
Pssm-ID: 177025 Cd Length: 529 Bit Score: 707.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 1 MAKDIKFSSDARAAMVRGVDTLADTVKVTLGPKGRNVVLEKAFGSPLITNDGVTIAKEIELEDHFENMGAKLVSEVASKT 80
Cdd:CHL00093 1 MSKKILYQDNARRALERGMDILAEAVSVTLGPKGRNVVLEKKYGSPQIVNDGVTIAKEIELEDHIENTGVALIRQAASKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 81 NDIAGDGTTTATVLTQAIVREGLKNVTAGANPIGIRRGIEAAVSTAVEELKAIAQPVANKEAIAQVAAVSS-RSEKVGEY 159
Cdd:CHL00093 81 NDVAGDGTTTATVLAYAIVKQGMKNVAAGANPISLKRGIEKATQYVVSQIAEYARPVEDIQAITQVASISAgNDEEVGSM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 160 ISEAMERVGNDGVITIEESRGMETELEVVEGMQFDRGYLSQYMVTDNEKMVADLDNPFILVTDKKISNI-QDVLPLLEEV 238
Cdd:CHL00093 161 IADAIEKVGREGVISLEEGKSTVTELEITEGMRFEKGFISPYFVTDTERMEVVQENPYILLTDKKITLVqQDLLPILEQV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 239 LKTSRPLLIIADDVDGEALPTLVLNKIRGTFNVVAVKAPGFGDRRKAMLEDIAVLTGATVITEDLGLELKDATMAALGQA 318
Cdd:CHL00093 241 TKTKRPLLIIAEDVEKEALATLVLNKLRGIVNVVAVRAPGFGDRRKAMLEDIAILTGGQVITEDAGLSLETIQLDLLGQA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 319 SKVTVDKDSTVIVeGAGSAEAIANRVNLIKSQLETTTSEFDREKLQERLAKLSGGVAVVKVGAATETALKEMKLRIEDAL 398
Cdd:CHL00093 321 RRIIVTKDSTTII-ADGNEEQVKARCEQLRKQIEIADSSYEKEKLQERLAKLSGGVAVIKVGAATETEMKDKKLRLEDAI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 399 NATRAAVEEGIVAGGGTALVNVIAKV---AELDLEGDDATGRNIVLRALEEPVRQIAYNAGYEGSVIIDKLKNSPVGTGF 475
Cdd:CHL00093 400 NATKAAVEEGIVPGGGATLVHLSENLktwAKNNLKEDELIGALIVARAILAPLKRIAENAGKNGSVIIEKVQEQDFEIGY 479
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1934310476 476 NAANGEWVDMVEAGIIDPVKVTRSALQNAASVASLILTTEAVVANKPE 523
Cdd:CHL00093 480 NAANNKFVNMYEAGIIDPAKVTRSALQNAASIASMILTTECIIVDKKE 527
|
|
| groEL |
PRK12852 |
chaperonin GroEL; Reviewed |
1-535 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237232 Cd Length: 545 Bit Score: 694.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 1 MAKDIKFSSDARAAMVRGVDTLADTVKVTLGPKGRNVVLEKAFGSPLITNDGVTIAKEIELEDHFENMGAKLVSEVASKT 80
Cdd:PRK12852 2 AAKDVKFSGDARDRMLRGVDILANAVKVTLGPKGRNVVIEKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVREVASKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 81 NDIAGDGTTTATVLTQAIVREGLKNVTAGANPIGIRRGIEAAVSTAVEELKAIAQPVANKEAIAQVAAVSSRS-EKVGEY 159
Cdd:PRK12852 82 NDLAGDGTTTATVLAQAIVREGAKAVAAGMNPMDLKRGIDIAVAAVVKDIEKRAKPVASSAEIAQVGTISANGdAAIGKM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 160 ISEAMERVGNDGVITIEESRGMETELEVVEGMQFDRGYLSQYMVTDNEKMVADLDNPFILVTDKKISNIQDVLPLLEEVL 239
Cdd:PRK12852 162 IAQAMQKVGNEGVITVEENKSLETEVDIVEGMKFDRGYLSPYFVTNAEKMTVELDDAYILLHEKKLSGLQAMLPVLEAVV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 240 KTSRPLLIIADDVDGEALPTLVLNKIRGTFNVVAVKAPGFGDRRKAMLEDIAVLTGATVITEDLGLELKDATMAALGQAS 319
Cdd:PRK12852 242 QSGKPLLIIAEDVEGEALATLVVNRLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGQLISEDLGIKLENVTLKMLGRAK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 320 KVTVDKDSTVIVEGAGSAEAIANRVNLIKSQLETTTSEFDREKLQERLAKLSGGVAVVKVGAATETALKEMKLRIEDALN 399
Cdd:PRK12852 322 KVVIDKENTTIVNGAGKKADIEARVGQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKEKKDRVEDALN 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 400 ATRAAVEEGIVAGGGTALVNVIAKVAELDLEGDDAT-GRNIVLRALEEPVRQIAYNAGYEGSVIIDKLKNSPVGT-GFNA 477
Cdd:PRK12852 402 ATRAAVQEGIVPGGGVALLRAKKAVGRINNDNADVQaGINIVLKALEAPIRQIAENAGVEGSIVVGKILENKSETfGFDA 481
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1934310476 478 ANGEWVDMVEAGIIDPVKVTRSALQNAASVASLILTTEAVVANKPEPEtpAAPAMDPG 535
Cdd:PRK12852 482 QTEEYVDMVAKGIIDPAKVVRTALQDAASVAGLLVTTEAMVAELPKKD--AAPAMPAG 537
|
|
| PRK14104 |
PRK14104 |
chaperonin GroEL; Provisional |
2-538 |
0e+00 |
|
chaperonin GroEL; Provisional
Pssm-ID: 172594 Cd Length: 546 Bit Score: 593.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 2 AKDIKFSSDARAAMVRGVDTLADTVKVTLGPKGRNVVLEKAFGSPLITNDGVTIAKEIELEDHFENMGAKLVSEVASKTN 81
Cdd:PRK14104 3 AKEVKFGVDARDRMLRGVDILANAVKVTLGPKGRNVVLDKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVREVASKSA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 82 DIAGDGTTTATVLTQAIVREGLKNVTAGANPIGIRRGIEAAVSTAVEELKAIAQPVANKEAIAQVAAVSSRSE-KVGEYI 160
Cdd:PRK14104 83 DAAGDGTTTATVLAQAIVREGAKSVAAGMNPMDLKRGIDLAVEAVVADLVKNSKKVTSNDEIAQVGTISANGDaEIGKFL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 161 SEAMERVGNDGVITIEESRGMETELEVVEGMQFDRGYLSQYMVTDNEKMVADLDNPFILVTDKKISNIQDVLPLLEEVLK 240
Cdd:PRK14104 163 ADAMKKVGNEGVITVEEAKSLETELDVVEGMQFDRGYISPYFVTNADKMRVEMDDAYILINEKKLSSLNELLPLLEAVVQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 241 TSRPLLIIADDVDGEALPTLVLNKIRGTFNVVAVKAPGFGDRRKAMLEDIAVLTGATVITEDLGLELKDATMAALGQASK 320
Cdd:PRK14104 243 TGKPLVIVAEDVEGEALATLVVNRLRGGLKVAAVKAPGFGDRRKAMLQDIAILTGGQAISEDLGIKLENVTLQMLGRAKK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 321 VTVDKDSTVIVEGAGSAEAIANRVNLIKSQLETTTSEFDREKLQERLAKLSGGVAVVKVGAATETALKEMKLRIEDALNA 400
Cdd:PRK14104 323 VMIDKENTTIVNGAGKKADIEARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKERKDRVDDAMHA 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 401 TRAAVEEGIVAGGGTALVNVIAKVAELDLEGDD-ATGRNIVLRALEEPVRQIAYNAGYEGSVIIDK-LKNSPVGTGFNAA 478
Cdd:PRK14104 403 TRAAVEEGIVPGGGVALLRASEQLKGIKTKNDDqKTGVEIVRKALSAPARQIAINAGEDGSVIVGKiLEKEQYSYGFDSQ 482
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 479 NGEWVDMVEAGIIDPVKVTRSALQNAASVASLILTTEAVVANKPEPETPAAPAMDPGMMG 538
Cdd:PRK14104 483 TGEYGNLVSKGIIDPTKVVRTAIQNAASVAALLITTEAMVAELPKKGGAGPAMPPGGGMG 542
|
|
| PLN03167 |
PLN03167 |
Chaperonin-60 beta subunit; Provisional |
2-539 |
0e+00 |
|
Chaperonin-60 beta subunit; Provisional
Pssm-ID: 215611 [Multi-domain] Cd Length: 600 Bit Score: 543.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 2 AKDIKFSSDARA--AMVRGVDTLADTVKVTLGPKGRNVVLEKAFGSPLITNDGVTIAKEIELEDHFENMGAKLVSEVASK 79
Cdd:PLN03167 56 AKELHFNKDGSAikKLQAGVNKLADLVGVTLGPKGRNVVLESKYGSPKIVNDGVTVAKEVELEDPVENIGAKLVRQAAAK 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 80 TNDIAGDGTTTATVLTQAIVREGLKNVTAGANPIGIRRGIEAAVSTAVEELKAIAQPVANKEaIAQVAAVSS-RSEKVGE 158
Cdd:PLN03167 136 TNDLAGDGTTTSVVLAQGLIAEGVKVVAAGANPVQITRGIEKTAKALVKELKKMSKEVEDSE-LADVAAVSAgNNYEVGN 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 159 YISEAMERVGNDGVITIEESRGMETELEVVEGMQFDRGYLSQYMVTDNEKMVADLDNPFILVTDKKISNIQDVLPLLEEV 238
Cdd:PLN03167 215 MIAEAMSKVGRKGVVTLEEGKSAENNLYVVEGMQFDRGYISPYFVTDSEKMSVEYDNCKLLLVDKKITNARDLIGILEDA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 239 LKTSRPLLIIADDVDGEALPTLVLNKIRGTFNVVAVKAPGFGDRRKAMLEDIAVLTGATVITEDLGLELKDATMAALGQA 318
Cdd:PLN03167 295 IRGGYPLLIIAEDIEQEALATLVVNKLRGSLKIAALKAPGFGERKSQYLDDIAILTGGTVIREEVGLSLDKVGKEVLGTA 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 319 SKVTVDKDSTVIVEGAGSAEAIANRVNLIKSQLETTTSEFDREKLQERLAKLSGGVAVVKVGAATETALKEMKLRIEDAL 398
Cdd:PLN03167 375 AKVVLTKDTTTIVGDGSTQEAVNKRVAQIKNLIEAAEQDYEKEKLNERIAKLSGGVAVIQVGAQTETELKEKKLRVEDAL 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 399 NATRAAVEEGIVAGGGTALVNVIAKVAEL--DLEGDD-ATGRNIVLRALEEPVRQIAYNAGYEGSVIIDK-LKNSPVGTG 474
Cdd:PLN03167 455 NATKAAVEEGIVVGGGCTLLRLASKVDAIkdTLENDEqKVGADIVKRALSYPLKLIAKNAGVNGSVVSEKvLSNDNPKFG 534
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1934310476 475 FNAANGEWVDMVEAGIIDPVKVTRSALQNAASVASLILTTEAVVANKPEPE-TPAAPAMDPGMMGY 539
Cdd:PLN03167 535 YNAATGKYEDLMAAGIIDPTKVVRCCLEHAASVAKTFLTSDCVVVEIKEPEpVPAGNPMDNSGYGY 600
|
|
| chaperonin_type_I_II |
cd00309 |
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ... |
3-519 |
2.00e-153 |
|
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: 446.87 E-value: 2.00e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 3 KDIKFSSDARAAMVRGVDTLADTVKVTLGPKGRNVVLEKAFGSPLITNDGVTIAKEIELEdhfeNMGAKLVSEVASKTND 82
Cdd:cd00309 1 KEREFGEEARLSNINAAKALADAVKTTLGPKGMDKMLVDSLGDPTITNDGATILKEIEVE----HPAAKLLVEVAKSQDD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 83 IAGDGTTTATVLTQAIVREGLKNVTAGANPIGIRRGIEAAVSTAVEELKAIAQP--VANKEAIAQVAAVSSRS------- 153
Cdd:cd00309 77 EVGDGTTTVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVPidVEDREELLKVATTSLNSklvsggd 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 154 EKVGEYISEAMERVG------NDGVITIEESRG-METELEVVEGMQFDRGYLSQYMVTdnekmvaDLDNPFILVTDKKIS 226
Cdd:cd00309 157 DFLGELVVDAVLKVGkengdvDLGVIRVEKKKGgSLEDSELVVGMVFDKGYLSPYMPK-------RLENAKILLLDCKLE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 227 NiqdvlplleevlktsrplLIIADD-VDGEALPTLVLNKIrgtfnvVAVKApgfgdRRKAMLEDIAVLTGATVITedlgl 305
Cdd:cd00309 230 Y------------------VVIAEKgIDDEALHYLAKLGI------MAVRR-----VRKEDLERIAKATGATIVS----- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 306 ELKDATMAALGQASKVTVDK----DSTVIVEGAGsaeaianrvnliksqletttsefdreklqerlaklsGGVAVVKVGA 381
Cdd:cd00309 276 RLEDLTPEDLGTAGLVEETKigdeKYTFIEGCKG------------------------------------GKVATILLRG 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 382 ATETALKEMKLRIEDALNATRAAVEE-GIVAGGGTALVNVIAKVAEL--DLEGDDATGRNIVLRALEEPVRQIAYNAGYE 458
Cdd:cd00309 320 ATEVELDEAERSLHDALCAVRAAVEDgGIVPGGGAAEIELSKALEELakTLPGKEQLGIEAFADALEVIPRTLAENAGLD 399
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1934310476 459 GSVIIDKLKNSPVGTGFNAA----NGEWVDMVEAGIIDPVKVTRSALQNAASVASLILTTEAVVA 519
Cdd:cd00309 400 PIEVVTKLRAKHAEGGGNAGgdveTGEIVDMKEAGIIDPLKVKRQALKSATEAASLILTIDDIIV 464
|
|
| Cpn60_TCP1 |
pfam00118 |
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ... |
22-521 |
1.27e-92 |
|
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: 291.41 E-value: 1.27e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 22 LADTVKVTLGPKGRNVVLEKAFGSPLITNDGVTIAKEIELEdhfeNMGAKLVSEVASKTNDIAGDGTTTATVLTQAIVRE 101
Cdd:pfam00118 1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELEIQ----HPAAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 102 GLKNVTAGANPIGIRRGIEAAVSTAVEELKAI-AQPV--ANKEAIAQVAAVSSRS-------EKVGEYISEAMER----- 166
Cdd:pfam00118 77 AEKLLAAGVHPTTIIEGYEKALEKALEILDSIiSIPVedVDREDLLKVARTSLSSkiisresDFLAKLVVDAVLAipknd 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 167 ----VGNDGVITIEESRGMETELevVEGMQFDRGYLSqymvtdnEKMVADLDNPFILVTDKKISNIQD------------ 230
Cdd:pfam00118 157 gsfdLGNIGVVKILGGSLEDSEL--VDGVVLDKGPLH-------PDMPKRLENAKVLLLNCSLEYEKTetkatvvlsdae 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 231 ------------VLPLLEEVLKTSRPLLIIADDVDGEALPTLVLNKIRGTFNVvavkapgfgdrRKAMLEDIAVLTGATV 298
Cdd:pfam00118 228 qlerflkaeeeqILEIVEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMALRRV-----------KKRDLERLAKATGARA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 299 ITedlglELKDATMAALGQASKVTVDK---DSTVIVEGagsaeaianrvnliksqletttsefdreklqerlaKLSGGVA 375
Cdd:pfam00118 297 VS-----SLDDLTPDDLGTAGKVEEEKigdEKYTFIEG-----------------------------------CKSPKAA 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 376 VVKVGAATETALKEMKLRIEDALNATRAAVEE-GIVAGGG---TALVNVIAKVAElDLEGDDATGRNIVLRALEEPVRQI 451
Cdd:pfam00118 337 TILLRGATDHVLDEIERSIHDALCVVKNAIEDpRVVPGGGaveMELARALREYAK-SVSGKEQLAIEAFAEALEVIPKTL 415
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1934310476 452 AYNAGYEGSVIIDKLK----NSPVGTGFNAANGEWVDMVEAGIIDPVKVTRSALQNAASVASLILTTEAVVANK 521
Cdd:pfam00118 416 AENAGLDPIEVLAELRaahaSGEKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKSATEAASTILRIDDIIKAK 489
|
|
| chaperonin_like |
cd03333 |
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ... |
140-407 |
5.47e-38 |
|
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: 138.75 E-value: 5.47e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 140 KEAIAQVAAVSSRS------EKVGEYISEAMERVG------NDGVITIEESRG-METELEVVEGMQFDRGYLSQYMVTDn 206
Cdd:cd03333 1 RELLLQVATTSLNSklsswdDFLGKLVVDAVLKVGpdnrmdDLGVIKVEKIPGgSLEDSELVVGVVFDKGYASPYMPKR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 207 ekmvadLDNPFILVTDKKISNiqdvlplleevlktsrplLIIADD-VDGEALPTLVLNKIrgtfnvVAVKApgfgdRRKA 285
Cdd:cd03333 80 ------LENAKILLLDCPLEY------------------VVIAEKgIDDLALHYLAKAGI------MAVRR-----VKKE 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 286 MLEDIAVLTGATVITedlglELKDATMAALGQASKVTVDKDS----TVIVEGAGsaeaianrvnliksqletttsefdre 361
Cdd:cd03333 125 DLERIARATGATIVS-----SLEDLTPEDLGTAELVEETKIGeeklTFIEGCKG-------------------------- 173
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1934310476 362 klqerlaklsGGVAVVKVGAATETALKEMKLRIEDALNATRAAVEE 407
Cdd:cd03333 174 ----------GKAATILLRGATEVELDEVKRSLHDALCAVRAAVEE 209
|
|
| cpn60 |
cd03343 |
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ... |
10-521 |
1.99e-36 |
|
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: 142.02 E-value: 1.99e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 10 DARAAMVRGVDTLADTVKVTLGPKGRNVVLEKAFGSPLITNDGVTIAKEIELedhfENMGAKLVSEVASKTNDIAGDGTT 89
Cdd:cd03343 15 DAQRMNIAAAKAVAEAVRTTLGPKGMDKMLVDSLGDVTITNDGATILKEMDI----EHPAAKMLVEVAKTQDEEVGDGTT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 90 TATVLTQAIVREGLKNVTAGANPIGIRRGIEAAVSTAVEELKAIAQPV--ANKE---AIAQVAAVSSRSEKVGEYISEam 164
Cdd:cd03343 91 TAVVLAGELLEKAEDLLDQNIHPTVIIEGYRLAAEKALELLDEIAIKVdpDDKDtlrKIAKTSLTGKGAEAAKDKLAD-- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 165 erVGNDGVITIEESRGMETE-------LEVVEGMQFDRGYLSQYMVTD----NEKMVADLDNPFILVTDKKIsniqdvlp 233
Cdd:cd03343 169 --LVVDAVLQVAEKRDGKYVvdldnikIEKKTGGSVDDTELIRGIVIDkevvHPGMPKRVENAKIALLDAPL-------- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 234 lleEVLKTSRPLLIIADDVD---------GEALPTLVlNKIRGT-FNVVAV-------------KAPGFGDRR--KAMLE 288
Cdd:cd03343 239 ---EVKKTEIDAKIRITSPDqlqafleqeEAMLKEMV-DKIADTgANVVFCqkgiddlaqhylaKAGILAVRRvkKSDME 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 289 DIAVLTGATVITedlglELKDATMAALGQASKVTVDK---DSTVIVEGAGSAEAianrVNLIksqletttsefdreklqe 365
Cdd:cd03343 315 KLARATGAKIVT-----NIDDLTPEDLGEAELVEERKvgdDKMVFVEGCKNPKA----VTIL------------------ 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 366 rlakLSGGvavvkvgaaTETALKEMKLRIEDALNATRAAVEEG-IVAGGGTALVNVIAKVAEL--DLEGDDATGRNIVLR 442
Cdd:cd03343 368 ----LRGG---------TEHVVDELERALEDALRVVADALEDGkVVAGGGAVEIELAKRLREYarSVGGREQLAVEAFAD 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 443 ALEEPVRQIAYNAGYEGSVIIDKLK----NSPVGTGFNAANGEWVDMVEAGIIDPVKVTRSALQNAASVASLILTTEAVV 518
Cdd:cd03343 435 ALEEIPRTLAENAGLDPIDTLVELRaaheKGNKNAGLDVYTGEVVDMLEKGVIEPLRVKKQAIKSATEAATMILRIDDVI 514
|
...
gi 1934310476 519 ANK 521
Cdd:cd03343 515 AAK 517
|
|
| thermosome_beta |
NF041083 |
thermosome subunit beta; |
10-521 |
5.02e-35 |
|
thermosome subunit beta;
Pssm-ID: 469010 Cd Length: 519 Bit Score: 137.77 E-value: 5.02e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 10 DARAAMVRGVDTLADTVKVTLGPKGRNVVLEKAFGSPLITNDGVTIAKEIELedhfENMGAKLVSEVASKTNDIAGDGTT 89
Cdd:NF041083 17 DAQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDIVITNDGATILKEMDV----QHPAAKMLVEVAKTQDDEVGDGTT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 90 TATVLTQAIVREGLKNVTAGANPIGIRRGIEAAVSTAVEELKAIAQPVA--NKEAIAQVA-------AVSSRSEKVGEYI 160
Cdd:NF041083 93 TAVVLAGELLKKAEELLDQNIHPTIIANGYRLAAEKAIEILDEIAEKVDpdDRETLKKIAetsltskGVEEARDYLAEIA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 161 SEAMERVGN----------DGVITIEESRGMETELEVVEGMQFDRGYLSQYM--VTDNEKmVADLDNPFILV---TDKKI 225
Cdd:NF041083 173 VKAVKQVAEkrdgkyyvdlDNIQIEKKHGGSIEDTQLIYGIVIDKEVVHPGMpkRVENAK-IALLDAPLEVKkteIDAEI 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 226 S-----NIQDVLPLLEEVLKtsrplliiaDDVDgealptlvlnKIRGT-FNVVAV-------------KAPGFGDRR--K 284
Cdd:NF041083 252 RitdpdQLQKFLDQEEKMLK---------EMVD----------KIKATgANVVFCqkgiddlaqhylaKAGILAVRRvkK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 285 AMLEDIAVLTGATVITedlglELKDATMAALGQASKVTVDK---DSTVIVEGAGSAEAIAnrvnliksqletttsefdre 361
Cdd:NF041083 313 SDMEKLAKATGARIVT-----NIDDLTPEDLGYAELVEERKvgdDKMVFVEGCKNPKAVT-------------------- 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 362 klqerlaklsggvavVKVGAATETALKEMKLRIEDALNATRAAVEEG-IVAGGGTALVNVIAKVAEL--DLEGDDATGRN 438
Cdd:NF041083 368 ---------------ILIRGGTEHVVDEAERALEDALSVVADAVEDGkIVAGGGAPEVELAKRLREYaaTVGGREQLAVE 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 439 IVLRALEEPVRQIAYNAGYEGSVIIDKL----KNSPVGTGFNAANGEWVDMVEAGIIDPVKVTRSALQNAASVASLILTT 514
Cdd:NF041083 433 AFAEALEIIPRTLAENAGLDPIDILVKLrsahEKGKKWAGINVFTGEVVDMWELGVIEPLRVKTQAIKSATEAATMILRI 512
|
....*..
gi 1934310476 515 EAVVANK 521
Cdd:NF041083 513 DDVIAAK 519
|
|
| thermosome_alpha |
NF041082 |
thermosome subunit alpha; |
10-521 |
3.01e-33 |
|
thermosome subunit alpha;
Pssm-ID: 469009 Cd Length: 518 Bit Score: 132.70 E-value: 3.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 10 DARAAMVRGVDTLADTVKVTLGPKGRNVVLEKAFGSPLITNDGVTIAKEIELedhfENMGAKLVSEVASKTNDIAGDGTT 89
Cdd:NF041082 17 DAQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDVVITNDGVTILKEMDI----EHPAAKMIVEVAKTQDDEVGDGTT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 90 TATVLTQAIVREGLKNVTAGANPIGIRRGIEAAVSTAVEELKAIAQPV--ANKEAIAQVAA-------VSSRSEKVGEYI 160
Cdd:NF041082 93 TAVVLAGELLKKAEELLDQDIHPTIIAEGYRLAAEKALEILDEIAIKVdpDDKETLKKIAAtamtgkgAEAAKDKLADLV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 161 SEA----MERVGNDGV----ITIEESRG---METELevVEGMQFDRGYLSQYM--VTDNEKmVADLDNPF---------- 217
Cdd:NF041082 173 VDAvkavAEKDGGYNVdldnIKVEKKVGgsiEDSEL--VEGVVIDKERVHPGMpkRVENAK-IALLDAPLevkkteidak 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 218 ILVTDkkISNIQDVLPLLEEVLKtsrplliiaDDVDgealptlvlnKIRGT-FNVVAV-------------KAPGFGDRR 283
Cdd:NF041082 250 ISITD--PDQLQAFLDQEEKMLK---------EMVD----------KIADSgANVVFCqkgiddlaqhylaKEGILAVRR 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 284 --KAMLEDIAVLTGATVITedlglELKDATMAALGQASKVT---VDKDSTVIVEGAGSAEAianrVNLIksqletttsef 358
Cdd:NF041082 309 vkKSDMEKLAKATGARIVT-----SIDDLSPEDLGYAGLVEerkVGGDKMIFVEGCKNPKA----VTIL----------- 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 359 dreklqerlakLSGGvavvkvgaaTETALKEMKLRIEDALNATRAAVEEG-IVAGGGTALVNVIAKVAEldlEGDDATGR 437
Cdd:NF041082 369 -----------LRGG---------TEHVVDEVERALEDALRVVRVVLEDGkVVAGGGAPEVELALRLRE---YAASVGGR 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 438 -----NIVLRALEEPVRQIAYNAGYEGSVIIDKLKN----SPVGTGFNAANGEWVDMVEAGIIDPVKVTRSALQNAASVA 508
Cdd:NF041082 426 eqlaiEAFAEALEIIPRTLAENAGLDPIDALVELRSahekGNKTAGLDVYTGKVVDMLEIGVVEPLRVKTQAIKSATEAA 505
|
570
....*....|...
gi 1934310476 509 SLILTTEAVVANK 521
Cdd:NF041082 506 VMILRIDDVIAAA 518
|
|
| TCP1_beta |
cd03336 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ... |
10-522 |
1.11e-18 |
|
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: 88.93 E-value: 1.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 10 DARAAMVRGVDTLADTVKVTLGPKGRNVVLE--KAFGSPLITNDGVTIAKEIeledHFENMGAKLVSEVASKTNDIAGDG 87
Cdd:cd03336 13 TARLSSFVGAIAIGDLVKTTLGPKGMDKILQsvGRSGGVTVTNDGATILKSI----GVDNPAAKVLVDISKVQDDEVGDG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 88 TTTATVLTQAIVREGLKNVTAGANPIGIRRGIEAAVSTAVEELKAIAQ-----PVANKEAIAQVAAvSSRSEKVGEYISE 162
Cdd:cd03336 89 TTSVTVLAAELLREAEKLVAQKIHPQTIIEGYRMATAAAREALLSSAVdhssdEEAFREDLLNIAR-TTLSSKILTQDKE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 163 AMERVGNDGVITIEESrgmeTELEVVEGMQFDRGYLSQYMVTDN---EKMVA-----DLDNPFILV------TDK-KI-- 225
Cdd:cd03336 168 HFAELAVDAVLRLKGS----GNLDAIQIIKKLGGSLKDSYLDEGfllDKKIGvnqpkRIENAKILIantpmdTDKiKIfg 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 226 SNIQ-DVLPLLEEVLKTSRPLL------IIADDVDGEALPTLVLN---KIRGTFNVVAVKAPGFgdrrkAMLEDIAVLTG 295
Cdd:cd03336 244 AKVRvDSTAKVAEIEEAEKEKMknkvekILKHGINCFINRQLIYNypeQLFADAGIMAIEHADF-----DGVERLALVTG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 296 ATVITedlglelkdatmaalgqaskvTVDKDSTVIVegaGSAEAIAnrvnliksqlETTTSEfdreklqERLAKLSG--- 372
Cdd:cd03336 319 GEIAS---------------------TFDHPELVKL---GTCKLIE----------EIMIGE-------DKLIRFSGvaa 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 373 -GVAVVKVGAATETALKEMKLRIEDALNATRAAVEEG-IVAGGG---TALVNVIAKVAElDLEGDDATGRNIVLRALEEP 447
Cdd:cd03336 358 gEACTIVLRGASQQILDEAERSLHDALCVLAQTVKDTrVVLGGGcseMLMAKAVEELAK-KTPGKKSLAIEAFAKALRQL 436
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1934310476 448 VRQIAYNAGYEGSVIIDKLK----NSPVGTGFNAANGEWVDMVEAGIIDPVKVTRSALQNAASVASLILTTEAVVANKP 522
Cdd:cd03336 437 PTIIADNAGYDSAELVAQLRaahyNGNTTAGLDMRKGTVGDMKELGITESFKVKRQVLLSASEAAEMILRVDDIIKCAP 515
|
|
| chap_CCT_epsi |
TIGR02343 |
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ... |
10-190 |
1.89e-17 |
|
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: 85.24 E-value: 1.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 10 DARAAMVRGVDTLADTVKVTLGPKGRNVVLEKAFGSPLITNDGVTIAKEIELEDHFenmgAKLVSEVASKTNDIAGDGTT 89
Cdd:TIGR02343 27 EAKKSNIAAAKSVASILRTSLGPKGMDKMLISPDGDITVTNDGATILSQMDVDNQI----AKLMVELSKSQDDEIGDGTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 90 TATVLTQAIVREGLKNVTAGANPIGIRRGIEAAVSTAVEELKAIAQPVA----NKEAIAQvAAVSSRSEKVGEYISEAME 165
Cdd:TIGR02343 103 GVVVLAGALLEQAEELLDKGIHPIKIADGFEEAARIAVEHLEEISDEISadnnNREPLIQ-AAKTSLGSKIVSKCHRRFA 181
|
170 180
....*....|....*....|....*..
gi 1934310476 166 RVGNDGVITIE--ESRGMETELEVVEG 190
Cdd:TIGR02343 182 EIAVDAVLNVAdmERRDVDFDLIKVEG 208
|
|
| chap_CCT_eta |
TIGR02345 |
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ... |
3-521 |
1.17e-16 |
|
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: 82.88 E-value: 1.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 3 KDIKFSSDARAAMVRGVD---TLADTVKVTLGPKGRNVVLEKAFGSPLITNDGVTIAKEIELedhfENMGAKLVSEVASK 79
Cdd:TIGR02345 8 KEGTDTSQGKGQLISNINacvAIAEALKTTLGPRGMDKLIVGSNGKATISNDGATILKLLDI----VHPAAKTLVDIAKS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 80 TNDIAGDGTTTATVLTQAIVREGLKNVTAGANPIGIRRGIEAAVSTAVEELKAIAQPVAN-----KEAIAQVAAVSSRSE 154
Cdd:TIGR02345 84 QDAEVGDGTTSVTILAGELLKEAKPFIEEGVHPQLIIRCYREALSLAVEKIKEIAVTIDEekgeqRELLEKCAATALSSK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 155 KVGEYiSEAMERVGNDGVITIEESR-------------GMETELEVVEGMQFDR-----GYLSQYMVTDNEKMV------ 210
Cdd:TIGR02345 164 LISHN-KEFFSKMIVDAVLSLDRDDldlkligikkvqgGALEDSQLVNGVAFKKtfsyaGFEQQPKKFANPKILllnvel 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 211 ---ADLDNPFILVTDKKisNIQDVlplleevlktsrplliiaddVDGE-ALPTLVLNKIRGT-FNVVAVKAPgFGDRRKA 285
Cdd:TIGR02345 243 elkAEKDNAEIRVEDVE--DYQAI--------------------VDAEwAIIFRKLEKIVESgANVVLSKLP-IGDLATQ 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 286 MLEDIAVLTGATVITEDLGlelkdATMAALGqaskvtvdkdstvivegaGSaeaIANRVNLIKSQLETTTSEFDREKL-Q 364
Cdd:TIGR02345 300 YFADRDIFCAGRVSAEDLK-----RVIKACG------------------GS---IQSTTSDLEADVLGTCALFEERQIgS 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 365 ERLAKLSGGvavVKVGAAT-------ETALKEMKLRIEDALNATRAAVEEGIVAGGGTALVNVIAKV---AELDLEGDDA 434
Cdd:TIGR02345 354 ERYNYFTGC---PHAKTCTiilrggaEQFIEEAERSLHDAIMIVRRALKNKKIVAGGGAIEMELSKClrdYSKTIDGKQQ 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 435 TGRNIVLRALEEPVRQIAYNAGYEGSVIIDKLK----NSPVGTGFNAANGEWVDMVEAGIIDPVKVTRSALQNAASVASL 510
Cdd:TIGR02345 431 LIINAFAKALEIIPRQLCENAGFDSIEILNKLRsrhaKGGKWYGVDINTEDIGDNFEAFVWEPALVKINALKAAFEAACT 510
|
570
....*....|.
gi 1934310476 511 ILTTEAVVANK 521
Cdd:TIGR02345 511 ILSVDETITNP 521
|
|
| TCP1_delta |
cd03338 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ... |
22-512 |
1.28e-16 |
|
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: 82.72 E-value: 1.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 22 LADTVKVTLGPKGRNVVLEKAFGSPLITNDGVTIAKEIELeDHfenMGAKLVSEVaSKTNDI-AGDGTTTATVLTQAIVR 100
Cdd:cd03338 20 VADAIRTSLGPRGMDKMIQTGKGEVIITNDGATILKQMSV-LH---PAAKMLVEL-SKAQDIeAGDGTTSVVVLAGALLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 101 EGLKNVTAGANPIGIRRGIEAAVSTAVEELKAIAQPV--ANKEAIAQVAA-------VSSRSEKVGEYISEAMERVGNDG 171
Cdd:cd03338 95 ACESLLKKGIHPTVISESFQIAAKKAVEILDSMSIPVdlNDRESLIKSATtslnskvVSQYSSLLAPIAVDAVLKVIDPA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 172 VITIEESR---------GMETELEVVEGMQFD-RGYLSQYMVTDNEKMV------------ADLDNPfILVTD----KKI 225
Cdd:cd03338 175 TATNVDLKdirivkklgGTIEDTELVDGLVFTqKASKKAGGPTRIEKAKigliqfclsppkTDMDNN-IVVNDyaqmDRI 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 226 snIQD----VLPLLEEVLKTSRPLLIIADDVDGEALPTL---VLNKIrgtfNVVAVKAPgfgDRrkamlEDIAVLTGATV 298
Cdd:cd03338 254 --LREerkyILNMCKKIKKSGCNVLLIQKSILRDAVSDLalhFLAKL----KIMVVKDI---ER-----EEIEFICKTIG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 299 ITEDLGLELKDATMaaLGQASKV-TVDKDSTVIVegagsaeaianRVNLIKSQLETTTsefdreklqerlaklsggvavV 377
Cdd:cd03338 320 CKPVASIDHFTEDK--LGSADLVeEVSLGDGKIV-----------KITGVKNPGKTVT---------------------I 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 378 KVGAATETALKEMKLRIEDALNATRAAVEE-GIVAGGGTALVNVIAKVAEL--DLEGDDAtgrnIVLRALEEPVRQIAY- 453
Cdd:cd03338 366 LVRGSNKLVLDEAERSLHDALCVIRCLVKKrALIPGGGAPEIEIALQLSEWarTLTGVEQ----YCVRAFADALEVIPYt 441
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1934310476 454 ---NAGYEGSVIIDKLKNSPVG----TGFNAANGEWVDMVEAGIIDPVKVTRSALQNAASVASLIL 512
Cdd:cd03338 442 laeNAGLNPISIVTELRNRHAQgeknAGINVRKGAITNILEENVVQPLLVSTSAITLATETVRMIL 507
|
|
| TCP1_epsilon |
cd03339 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ... |
10-190 |
3.77e-16 |
|
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: 81.19 E-value: 3.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 10 DARAAMVRGVDTLADTVKVTLGPKGRNVVLEKAFGSPLITNDGVTIAKEIELEDHFenmgAKLVSEVASKTNDIAGDGTT 89
Cdd:cd03339 23 EAHKSHILAAKSVANILRTSLGPRGMDKILVSPDGEVTVTNDGATILEKMDVDHQI----AKLLVELSKSQDDEIGDGTT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 90 TATVLTQAIVREGLKNVTAGANPIGIRRGIEAAVSTAVEELKAIAQPVA----NKEAIAQVAAVSSRSEKVGEYiSEAME 165
Cdd:cd03339 99 GVVVLAGALLEQAEKLLDRGIHPIRIADGYEQACKIAVEHLEEIADKIEfspdNKEPLIQTAMTSLGSKIVSRC-HRQFA 177
|
170 180
....*....|....*....|....*..
gi 1934310476 166 RVGNDGVITIE--ESRGMETELEVVEG 190
Cdd:cd03339 178 EIAVDAVLSVAdlERKDVNFELIKVEG 204
|
|
| chap_CCT_beta |
TIGR02341 |
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ... |
10-524 |
1.92e-15 |
|
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: 79.13 E-value: 1.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 10 DARAAMVRGVDTLADTVKVTLGPKGRNVVLEKA--FGSPLITNDGVTIAKEIELEdhfeNMGAKLVSEVASKTNDIAGDG 87
Cdd:TIGR02341 14 NARLSSFVGAIAIGDLVKSTLGPKGMDKILQSSssDASIMVTNDGATILKSIGVD----NPAAKVLVDMSKVQDDEVGDG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 88 TTTATVLTQAIVREGLKNVTAGANPIGIRRGIEAAVSTAVEELKAIA-----QPVANKEAIAQVAAvSSRSEKVGEYISE 162
Cdd:TIGR02341 90 TTSVTVLAAELLREAEKLINQKIHPQTIIAGYREATKAARDALLKSAvdngsDEVKFRQDLMNIAR-TTLSSKILSQHKD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 163 AMERVGNDGVITIEESrgmeTELEVVEGMQFDRGYLSQymvtdnekmvADLDNPFILvtDKKISNIQdvlPLLEEVLKts 242
Cdd:TIGR02341 169 HFAQLAVDAVLRLKGS----GNLEAIQIIKKLGGSLAD----------SYLDEGFLL--DKKIGVNQ---PKRIENAK-- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 243 rpLLIIADDVDGEALPTLVLN-KIRGTFNVVAVKAPGfGDRRKAMLEDIAVLTGATVITEDLGLELKDATMAALGQASKV 321
Cdd:TIGR02341 228 --ILIANTGMDTDKVKIFGSRvRVDSTAKVAELEHAE-KEKMKEKVEKILKHGINCFINRQLIYNYPEQLFADAGVMAIE 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 322 TVDKDSTVIVEGAGSAEAIANRVNLIKSQLETTTSEFDREKLQERLAKLSGGVA----VVKVGAATETALKEMKLRIEDA 397
Cdd:TIGR02341 305 HADFEGVERLALVTGGEIVSTFDHPELVKLGSCDLIEEIMIGEDKLLKFSGVKLgeacTIVLRGATQQILDEAERSLHDA 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 398 LNATRAAVEEG-IVAGGGTALVNVIAKVAEL--DLEGDDATGRNIVLRALEEPVRQIAYNAGYEGSVIIDKLK----NSP 470
Cdd:TIGR02341 385 LCVLSQTVKESrTVLGGGCSEMLMSKAVTQEaqRTPGKEALAVEAFARALRQLPTIIADNAGFDSAELVAQLRaahyNGN 464
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1934310476 471 VGTGFNAANGEWVDMVEAGIIDPVKVTRSALQNAASVASLILTTEAVVANKPEP 524
Cdd:TIGR02341 465 TTMGLDMNEGTIADMRQLGITESYKVKRAVVSSAAEAAEVILRVDNIIKAAPRK 518
|
|
| TCP1_eta |
cd03340 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ... |
23-521 |
1.93e-15 |
|
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: 78.87 E-value: 1.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 23 ADTVKVTLGPKGRNVVLEKAFGSPLITNDGVTIAKEIELEdhfeNMGAKLVSEVASKTNDIAGDGTTTATVLTQAIVREG 102
Cdd:cd03340 29 ADAVRTTLGPRGMDKLIVDGRGKVTISNDGATILKLLDIV----HPAAKTLVDIAKSQDAEVGDGTTSVVVLAGEFLKEA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 103 LKNVTAGANPIGIRRGIEAAVSTAVEELKAIAQPVANK------EAIAQVAA-------VSSRSEKVGEYISEAMERVGN 169
Cdd:cd03340 105 KPFIEDGVHPQIIIRGYRKALQLAIEKIKEIAVNIDKEdkeeqrELLEKCAAtalnsklIASEKEFFAKMVVDAVLSLDD 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 170 D---GVITIEESRG---METELevVEGMQFDR-----GYLSQYMVTDNEKMV---------ADLDNPFILVTDkkISNIQ 229
Cdd:cd03340 185 DldlDMIGIKKVPGgslEDSQL--VNGVAFKKtfsyaGFEQQPKKFKNPKILllnvelelkAEKDNAEVRVED--PEEYQ 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 230 DVlplleevlktsrplliiaddVDGE-ALPTLVLNKIRGT-FNVVAVKAPgFGDRRKAMLEDIAVLTGATVITEDLGlel 307
Cdd:cd03340 261 AI--------------------VDAEwKIIYDKLEKIVKSgANVVLSKLP-IGDLATQYFADRDIFCAGRVPEEDLK--- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 308 kdATMAALGQASKVTVDkdstvivegagsaeaianrvNLIKSQLETTTSEFDREKLQERLAKLSGG-----VAVVKVGAA 382
Cdd:cd03340 317 --RVAQATGGSIQTTVS--------------------NITDDVLGTCGLFEERQVGGERYNIFTGCpkaktCTIILRGGA 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 383 tETALKEMKLRIEDALNATRAAVEEGIVAGGGTALVNVIAKVAE---LDLEGDDATGRNIVLRALEEPVRQIAYNAGYEG 459
Cdd:cd03340 375 -EQFIEEAERSLHDAIMIVRRAIKNDSVVAGGGAIEMELSKYLRdysRTIAGKQQLVINAFAKALEIIPRQLCDNAGFDA 453
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1934310476 460 SVIIDKL-----KNSPVGTGFNAANGEWVDMVEAGIIDPVKVTRSALQNAASVASLILTTEAVVANK 521
Cdd:cd03340 454 TDILNKLrqkhaQGGGKWYGVDINNEGIADNFEAFVWEPSLVKINALTAATEAACLILSVDETIKNP 520
|
|
| chap_CCT_delta |
TIGR02342 |
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ... |
10-521 |
5.36e-15 |
|
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: 77.52 E-value: 5.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 10 DARAAMVRGVDTLADTVKVTLGPKGRNVVLEKAFGSPLITNDGVTIAKEIELedhfENMGAKLVSEVaSKTNDI-AGDGT 88
Cdd:TIGR02342 9 DVRTSNIVAAKAVADAIRTSLGPKGMDKMIQDGKGEVIITNDGATILKQMAV----LHPAAKMLVEL-SKAQDIeAGDGT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 89 TTATVLTQAIVREGLKNVTAGANPIGIRRGIEAAVSTAVEELKAIAQPV--ANKEAIAQVAAVSSRSEKVGEYiSEAMER 166
Cdd:TIGR02342 84 TSVVILAGALLGACERLLNKGIHPTIISESFQSAADEAIKILDEMSIPVdlSDREQLLKSATTSLSSKVVSQY-SSLLAP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 167 VGNDGVITIEESR-----------------GMETELEVVEGMQFDRGY----------------LSQYMVTDNEkmvADL 213
Cdd:TIGR02342 163 LAVDAVLKVIDPEnaknvdlndikvvkklgGTIDDTELIEGLVFTQKAsksaggptriekakigLIQFQISPPK---TDM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 214 DNPFILVTDKKISNIQD-----VLPLLEEVLKTSRPLLIIADDVDGEALPTLVLNKIrGTFNVVAVKapgfgDRRKAMLE 288
Cdd:TIGR02342 240 ENQIIVNDYAQMDRVLKeerayILNIVKKIKKTGCNVLLIQKSILRDAVNDLALHFL-AKMKIMVVK-----DIEREEIE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 289 DIAVLTGATVITEDLGLelkdaTMAALGQASkvtvdkdstvIVEGAGSAEAIANRVNLIKSQLETTTsefdreklqerla 368
Cdd:TIGR02342 314 FICKTIGCKPIASIDHF-----TADKLGSAE----------LVEEVDSDGGKIIKITGIQNAGKTVT------------- 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 369 klsggvavVKVGAATETALKEMKLRIEDALNATRAAVEE-GIVAGGGTALVNVIAKVAELDLEGDDATGrnIVLRALEEP 447
Cdd:TIGR02342 366 --------VVVRGSNKLVIDEAERSLHDALCVIRCLVKKrGLIAGGGAPEIEIARRLSKYARTMKGVES--YCVRAFADA 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 448 VRQIAY----NAGYEGSVIIDKLKNS----PVGTGFNAANGEWVDMVEAGIIDPVKVTRSALQNAASVASLILTTEAVVA 519
Cdd:TIGR02342 436 LEVIPYtlaeNAGLNPIKVVTELRNRhangEKTAGISVRKGGITNMLEEHVLQPLLVTTSAITLASETVRSILKIDDIVF 515
|
..
gi 1934310476 520 NK 521
Cdd:TIGR02342 516 TR 517
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
10-528 |
1.70e-13 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 72.75 E-value: 1.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 10 DARAAMVRGVDTLADTVKVTLGPKGRNVVLEKA-----FGSPLITNDGVTIAKEIELEdhfeNMGAKLVSEVASKTNDIA 84
Cdd:PTZ00212 22 TARLQSFVGAIAVADLVKTTLGPKGMDKILQPMsegprSGNVTVTNDGATILKSVWLD----NPAAKILVDISKTQDEEV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 85 GDGTTTATVLTQAIVREGLKNVTAGANPIGIRRGIEAAVSTAVEELKAIAQPVANKEA--------IAQvAAVSSR---- 152
Cdd:PTZ00212 98 GDGTTSVVVLAGELLREAEKLLDQKIHPQTIIEGWRMALDVARKALEEIAFDHGSDEEkfkedllnIAR-TTLSSKlltv 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 153 -SEKVGEYISEAMERVGNDG----VITIEESRGMETELEVVEGMQFDRGY-LSQYMVTDNEK-MVA----DLDNPFILVT 221
Cdd:PTZ00212 177 eKDHFAKLAVDAVLRLKGSGnldyIQIIKKPGGTLRDSYLEDGFILEKKIgVGQPKRLENCKiLVAntpmDTDKIKIYGA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 222 DKKISNIQDVLPL-LEEVLKTSRPLL-IIADDVDGEALPTLVLNKIRGTF---NVVAVKAPGFGDrrkamLEDIAVLTGA 296
Cdd:PTZ00212 257 KVKVDSMEKVAEIeAAEKEKMKNKVDkILAHGCNVFINRQLIYNYPEQLFaeaGIMAIEHADFDG-----MERLAAALGA 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 297 TVITedlglelkdatmaalgqaskvTVDKDSTVIVegaGSAEAIAnrvnliksqlETTTSEfdreklqERLAKLSG---- 372
Cdd:PTZ00212 332 EIVS---------------------TFDTPEKVKL---GHCDLIE----------EIMIGE-------DKLIRFSGcakg 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 373 GVAVVKVGAATETALKEMKLRIEDALNATRAAVEEG-IVAGGGTALVNVIAKVAEL--DLEGDDATGRNIVLRALEEPVR 449
Cdd:PTZ00212 371 EACTIVLRGASTHILDEAERSLHDALCVLSQTVKDTrVVLGGGCSEMLMANAVEELakKVEGKKSLAIEAFAKALRQIPT 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 450 QIAYNAGYEGSVIIDKLK----NSPVGTGFNAANGEWVDMVEAGIIDPVKVTRSALQNAASVASLILTTEAVVANKPEPE 525
Cdd:PTZ00212 451 IIADNGGYDSAELVSKLRaehyKGNKTAGIDMEKGTVGDMKELGITESYKVKLSQLCSATEAAEMILRVDDIIRCAPRQR 530
|
...
gi 1934310476 526 TPA 528
Cdd:PTZ00212 531 EQV 533
|
|
| chap_CCT_alpha |
TIGR02340 |
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ... |
10-525 |
2.51e-11 |
|
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: 65.90 E-value: 2.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 10 DARAAMVRGVDTLADTVKVTLGPKGRNVVLEKAFGSPLITNDGVTIAKEIELEDHfenmGAKLVSEVASKTNDIAGDGTT 89
Cdd:TIGR02340 12 DVRTQNVTAAMAIANIVKTSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHP----AAKILVELAQLQDREVGDGTT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 90 TATVLTQAIVREGLKNVTAGANPIGIRRGIEAAVSTAV---EELKAIAQPVANKEAIAQVAAVSSRSEKVG---EYIS-- 161
Cdd:TIGR02340 88 SVVIIAAELLKRADELVKNKIHPTSVISGYRLACKEAVkyiKENLSVSVDELGREALINVAKTSMSSKIIGldsDFFSni 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 162 -----EAMERVGNDGV-------ITIEESRGMET-ELEVVEGMQFDRGYLSQYMVTDNEKM-VADLD-------NPF--- 217
Cdd:TIGR02340 168 vvdavLAVKTTNENGEtkypikaINILKAHGKSArESMLVKGYALNCTVASQQMPKRIKNAkIACLDfnlqkakMALgvq 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 218 ILVTD-KKISNIQD-----VLPLLEEVLKTSRPLLIIADDVDGEALPTLVLNKIRGTFNVvavkapgfgdrRKAMLEDIA 291
Cdd:TIGR02340 248 IVVDDpEKLEQIRQreadiTKERIKKILDAGANVVLTTGGIDDMCLKYFVEAGAMGVRRC-----------KKEDLKRIA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 292 VLTGATVITE--DL-GLELKDATMaaLGQASKvtvdkdstVIVEGAGSAEAIanrvnLIKSQLETTTSEfdreklqerla 368
Cdd:TIGR02340 317 KATGATLVSTlaDLeGEETFEASY--LGFADE--------VVQERIADDECI-----LIKGTKKRKSAS----------- 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 369 klsggvavVKVGAATETALKEMKLRIEDALNATRAAVEEG-IVAGGG---TALVNVIAKVAeLDLEGDDATGRNIVLRAL 444
Cdd:TIGR02340 371 --------IILRGANDFMLDEMERSLHDALCVVKRTLESNsVVPGGGaveAALSIYLENFA-TTLGSREQLAIAEFARAL 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 445 EEPVRQIAYNAGYEGSVIIDKL------------KNSPVGTGFNAANGEWVDMVEAGIIDPVKVTRSALQNAASVASLIL 512
Cdd:TIGR02340 442 LIIPKTLAVNAAKDSTELVAKLrayhaaaqlkpeKKHLKWYGLDLVNGKIRDNKEAGVLEPTVSKVKSLKFATEAAITIL 521
|
570
....*....|...
gi 1934310476 513 TTEAVVANKPEPE 525
Cdd:TIGR02340 522 RIDDLIKLNPEQS 534
|
|
| chap_CCT_theta |
TIGR02346 |
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ... |
22-530 |
2.87e-11 |
|
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: 65.89 E-value: 2.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 22 LADTVKVTLGPKGRNVVLEKAFGSPLITNDGVTIAKEIELedhfENMGAKLVSEVASKTNDIAGDGTTTATVLTQAIVRE 101
Cdd:TIGR02346 30 LSQITRTSLGPNGMNKMVINHLEKLFVTNDAATILRELEV----QHPAAKLLVMASEMQENEIGDGTNLVLVLAGELLNK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 102 GLKNVTAGANPIGIRRGIEAAVSTAVEELKAI----AQPVANKEAIAQV--AAVSSR--------SEKVGEYISEAM-ER 166
Cdd:TIGR02346 106 AEELIRMGLHPSEIIKGYEMALKKAMEILEELvvweVKDLRDKDELIKAlkASISSKqygnedflAQLVAQACSTVLpKN 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 167 VGNDGVITIEESRGMETEL---EVVEGMQFDRGylSQYMVTDNEKM-VADLDNPF-ILVTDKK----ISNIQDVL----- 232
Cdd:TIGR02346 186 PQNFNVDNIRVCKILGGSLsnsEVLKGMVFNRE--AEGSVKSVKNAkVAVFSCPLdTATTETKgtvlIHNAEELLnyskg 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 233 --PLLEEVLKTsrplliIADD-----VDGEALPTLVLNKIRgTFNVVAVKAPGfgdrrKAMLEDIAVLTGATVItedlgL 305
Cdd:TIGR02346 264 eeNQIEAMIKA------IADSgvnviVTGGSVGDMALHYLN-KYNIMVLKIPS-----KFELRRLCKTVGATPL-----P 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 306 ELKDATMAALGQASKVTVdkdstvivegagsAEAIANRVNLIKSQletttsefdreklqerlaKLSGGVAVVKVGAATET 385
Cdd:TIGR02346 327 RLGAPTPEEIGYVDSVYV-------------SEIGGDKVTVFKQE------------------NGDSKISTIILRGSTDN 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 386 ALKEMKLRIEDALNATRAAVEEG-IVAGGGTALVNVIAKVAEL--DLEGDDATGRNIVLRALEEPVRQIAYNAGYEGSVI 462
Cdd:TIGR02346 376 LLDDIERAIDDGVNTVKALVKDGrLLPGAGATEIELASRLTKYgeKLPGLDQYAIKKFAEAFEIIPRTLAENAGLNANEV 455
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1934310476 463 IDKL------KNSPVGTGFNAANGEWVDMVEAGIIDPVKVTRSALQNAASVASLILTTEAVVANKPE--PETPAAP 530
Cdd:TIGR02346 456 IPKLyaahkkGNKSKGIDIEAESDGVKDASEAGIYDMLATKKWAIKLATEAAVTVLRVDQIIMAKPAggPKPPQGK 531
|
|
| TCP1_zeta |
cd03342 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
21-512 |
1.59e-10 |
|
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: 63.43 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 21 TLADTVKVTLGPKGRNVVLEKAFGSPLITNDGVTIAKEIeledHFENMGAKLVSEVASKTNDIAGDGTTTATVLTQAIVR 100
Cdd:cd03342 23 GLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLSEM----QIQHPTASMIARAATAQDDITGDGTTSNVLLIGELLK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 101 EGLKNVTAGANPIGIRRGIEAAVSTAVEELKAIAQPV---ANKEAIAQVAAVSSRSeKVGEYISEAMERVGNDGVITIEE 177
Cdd:cd03342 99 QAERYIQEGVHPRIITEGFELAKNKALKFLESFKVPVeidTDRELLLSVARTSLRT-KLHADLADQLTEIVVDAVLAIYK 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 178 SrGMETELEVVEGMQFDRGYLSQY-----MVTD----NEKMVADLDNPFILVTDKKIsniqdvlplleEVLKTS------ 242
Cdd:cd03342 178 P-DEPIDLHMVEIMQMQHKSDSDTklirgLVLDhgarHPDMPKRVENAYILTCNVSL-----------EYEKTEvnsgff 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 243 RPLLIIADDVDGEALPTLVLNKIrgtfnvVAVkapgfgdrRKAM---LEDIAVLTGATVIT--EDLGLElkdatmaALGQ 317
Cdd:cd03342 246 YSVVINQKGIDPPSLDMLAKEGI------LAL--------RRAKrrnMERLTLACGGVAMNsvDDLSPE-------CLGY 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 318 ASKVTvdkdstvivegagsaeaianrvnliksqlETTTSEfDREKLQERLAKLSGGVAVVKvgAATETALKEMKLRIEDA 397
Cdd:cd03342 305 AGLVY-----------------------------ERTLGE-EKYTFIEGVKNPKSCTILIK--GPNDHTITQIKDAIRDG 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 398 LNATRAAVEEGIVAGGGTALvnVIAKVAELDLEGDDATGRN-IVLRALEEPVRQI----AYNAGYEGS----VIIDKLKN 468
Cdd:cd03342 353 LRAVKNAIEDKCVVPGAGAF--EVALYAHLKEFKKSVKGKAkLGVQAFADALLVIpktlAENSGLDVQetlvKLQDEYAE 430
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1934310476 469 SPVGTGFNAANGEWVDMVEAGIIDPVKVTRSALQNAASVASLIL 512
Cdd:cd03342 431 GGQVGGVDLDTGEPMDPESEGIWDNYSVKRQILHSATVIASQLL 474
|
|
| TCP1_alpha |
cd03335 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ... |
10-507 |
4.83e-10 |
|
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: 61.92 E-value: 4.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 10 DARAAMVRGVDTLADTVKVTLGPKGRNVVLEKAFGSPLITNDGVTIAKEIELEDHfenmGAKLVSEVASKTNDIAGDGTT 89
Cdd:cd03335 8 DVRTQNVTAAMAIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHP----AAKILVELAQLQDKEVGDGTT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 90 TATVLTQAIVREGLKNVTAGANPIGIRRGIEAAVSTAVEELK-AIAQPVAN--KEAIAQVAAVSSRSEKVG---EYIS-- 161
Cdd:cd03335 84 SVVIIAAELLKRANELVKQKIHPTTIISGYRLACKEAVKYIKeHLSISVDNlgKESLINVAKTSMSSKIIGadsDFFAnm 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 162 -----EAMERVGNDGV-------ITIEESRGME-TELEVVEGMQFDRGYLSQYMVT--DNEKmVADLDNPF--------- 217
Cdd:cd03335 164 vvdaiLAVKTTNEKGKtkypikaVNILKAHGKSaKESYLVNGYALNCTRASQGMPTrvKNAK-IACLDFNLqktkmklgv 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 218 -ILVTD-KKISNIQD-----VLPLLEEVLKTSRPLLIIADDVDGEALPTLVlnkirgTFNVVAVkapgfgdRR--KAMLE 288
Cdd:cd03335 243 qVVVTDpEKLEKIRQresdiTKERIKKILAAGANVVLTTGGIDDMCLKYFV------EAGAMAV-------RRvkKEDLR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 289 DIAVLTGATVITE--DL-GLELKDATMaaLGQASKVTVDK---DSTVIVEG--AGSAEAIANRvnliksqletttsefdr 360
Cdd:cd03335 310 RIAKATGATLVSTlaNLeGEETFDPSY--LGEAEEVVQERigdDELILIKGtkKRSSASIILR----------------- 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 361 eklqerlaklsggvavvkvgAATETALKEMKLRIEDALNATRAAVEEG-IVAGGG---TALVNVIAKVAeLDLEGDDATG 436
Cdd:cd03335 371 --------------------GANDFMLDEMERSLHDALCVVKRTLESNsVVPGGGaveTALSIYLENFA-TTLGSREQLA 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 437 RNIVLRALEEPVRQIAYNAGYEGSVIIDKL------------KNSPVGTGFNAANGEWVDMVEAGIIDP----VKVTRSA 500
Cdd:cd03335 430 IAEFAEALLVIPKTLAVNAAKDATELVAKLrayhaaaqvkpdKKHLKWYGLDLINGKVRDNLEAGVLEPtvskIKSLKFA 509
|
....*..
gi 1934310476 501 LQNAASV 507
Cdd:cd03335 510 TEAAITI 516
|
|
| chap_CCT_gamma |
TIGR02344 |
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ... |
21-519 |
5.00e-10 |
|
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: 62.06 E-value: 5.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 21 TLADTVKVTLGPKGRNVVLEKAFGSPLITNDGVTIAKEIELedhfENMGAKLVSEVASKTNDIAGDGTTTATVLTQAIVR 100
Cdd:TIGR02344 27 AVADIIRTCLGPRSMLKMLLDPMGGIVMTNDGNAILREIDV----AHPAAKSMIELSRTQDEEVGDGTTSVIILAGEMLS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 101 EGLKNVTAGANPIGIRRGIEAAVSTAVEELKAIAQP--VANKEAIAQVAAVSSRSEKVGEYiSEAMERVGNDGVITIEES 178
Cdd:TIGR02344 103 VAEPFLEQNIHPTVIIRAYRKALDDALSVLEEISIPvdVNDDAAMLKLIQSCIGTKFVSRW-SDLMCDLALDAVRTVQRD 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 179 RGMETELEV-----VE----GMQFDRGYLSQYMVTDN---EKMVADLDNPFILVTD-----KKISNIQDVLPLLEEvlKT 241
Cdd:TIGR02344 182 ENGRKEIDIkryakVEkipgGDIEDSCVLKGVMINKDvthPKMRRYIENPRIVLLDcpleyKKGESQTNIEITKEE--DW 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 242 SRPLLIIADDVdgealptlvlnkirgtfnvvavkapgfgdrrKAMLEDIAVLTGATVITE----DLGLE-LKDATMAALG 316
Cdd:TIGR02344 260 NRILQMEEEYV-------------------------------QLMCEDIIAVKPDLVITEkgvsDLAQHyLLKANITAIR 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 317 QASKVtvdkDSTVIVEGAGSaeAIANRV-NLIKSQLETTTSEFDREKL-QERLAKLSG----GVAVVKVGAATETALKEM 390
Cdd:TIGR02344 309 RVRKT----DNNRIARACGA--TIVNRPeELRESDVGTGCGLFEVKKIgDEYFTFITEckdpKACTILLRGASKDILNEV 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 391 KLRIEDALNATRAAVEEG-IVAGGGTALVNVIAKVAE--LDLEGDDATGRNIVLRALEEPVRQIAYNAGyeGSVI--IDK 465
Cdd:TIGR02344 383 ERNLQDAMAVARNVLLDPkLVPGGGATEMAVSVALTEksKKLEGVEQWPYRAVADALEIIPRTLAQNCG--ANVIrtLTE 460
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1934310476 466 LKNSPVG-----TGFNAANGEWVDMVEAGIIDPVKVTRSALQNAASVASLILTTEAVVA 519
Cdd:TIGR02344 461 LRAKHAQennctWGIDGETGKIVDMKEKGIWEPLAVKLQTYKTAIESACLLLRIDDIVS 519
|
|
| chap_CCT_zeta |
TIGR02347 |
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ... |
22-220 |
7.30e-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: 58.21 E-value: 7.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 22 LADTVKVTLGPKGRNVVLEKAFGSPLITNDGVTIAKEIeledHFENMGAKLVSEVASKTNDIAGDGTTTATVLTQAIVRE 101
Cdd:TIGR02347 28 LQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEM----QIQHPTASMIARAATAQDDITGDGTTSTVLLIGELLKQ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 102 GLKNVTAGANPIGIRRGIEAAVSTA---VEELKAIAQPVANKEAIAQVAAVSSRS-------EKVGEYISEAMERVGNDG 171
Cdd:TIGR02347 104 AERYILEGVHPRIITEGFEIARKEAlqfLDKFKVKKEDEVDREFLLNVARTSLRTklpadlaDQLTEIVVDAVLAIKKDG 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1934310476 172 -------VITIEESRGMETELEVVEGMQFDRGylsqymvTDNEKMVADLDNPFILV 220
Cdd:TIGR02347 184 edidlfmVEIMEMKHKSATDTTLIRGLVLDHG-------ARHPDMPRRVKNAYILT 232
|
|
| TCP1_theta |
cd03341 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ... |
21-521 |
2.43e-08 |
|
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: 56.46 E-value: 2.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 21 TLADTVKVTLGPKGRN--VV--LEKAFgsplITNDGVTIAKEIEledhFENMGAKLVSEvASKTNDI-AGDGTTTATVLT 95
Cdd:cd03341 19 ELSQITRTSYGPNGMNkmVInhLEKLF----VTSDAATILRELE----VQHPAAKLLVM-ASQMQEEeIGDGTNLVVVLA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 96 QAIVREGLKNVTAGANPIGIRRGIEAAVSTAVEELKAIA----QPVANKEAIAQV--AAVSSR--------SEKVGEYIS 161
Cdd:cd03341 90 GELLEKAEELLRMGLHPSEIIEGYEKALKKALEILEELVvykiEDLRNKEEVSKAlkTAIASKqygnedflSPLVAEACI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 162 EAMER------VGNDGVITIEESRGMETelEVVEGMQFDRGYLSQYMVTDNEKmVADLDNPFilvtDKKISNIqdvlpll 235
Cdd:cd03341 170 SVLPEnignfnVDNIRVVKILGGSLEDS--KVVRGMVFKREPEGSVKRVKKAK-VAVFSCPF----DIGVNVI------- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 236 eevlktsrpllIIADDVDGEALptLVLNKirgtFNVVAVKAPG-FGDRRkamledIAVLTGATVITEdLGLELKDatmaA 314
Cdd:cd03341 236 -----------VAGGSVGDLAL--HYCNK----YGIMVIKINSkFELRR------LCRTVGATPLPR-LGAPTPE----E 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 315 LGQASKVTVdkdstvivegagsaEAIANRVNLIKSQLETTTSefdreklqerlaklsggVAVVKVGAATETALKEMKLRI 394
Cdd:cd03341 288 IGYCDSVYV--------------EEIGDTKVVVFRQNKEDSK-----------------IATIVLRGATQNILDDVERAI 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 395 EDALNATRAAVEEG-IVAGGGTALVNVIAKVAELD--LEGDDATGRNIVLRALEEPVRQIAYNAGYEGSVIIDKL----K 467
Cdd:cd03341 337 DDGVNVFKSLTKDGrFVPGAGATEIELAKKLKEYGekTPGLEQYAIKKFAEAFEVVPRTLAENAGLDATEVLSELyaahQ 416
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1934310476 468 NSPVGTGFNA-ANGEWV-DMVEAGIIDPVKVTRSALQNAASVASLILTTEAVVANK 521
Cdd:cd03341 417 KGNKSAGVDIeSGDEGTkDAKEAGIFDHLATKKWAIKLATEAAVTVLRVDQIIMAK 472
|
|
| TCP1_gamma |
cd03337 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ... |
21-146 |
1.90e-07 |
|
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.
Pssm-ID: 239453 [Multi-domain] Cd Length: 480 Bit Score: 53.45 E-value: 1.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310476 21 TLADTVKVTLGPKGRNVVLEKAFGSPLITNDGVTIAKEIELEdhfeNMGAKLVSEVASKTNDIAGDGTTTATVLTQAIVR 100
Cdd:cd03337 27 TVADVIRTCLGPRAMLKMLLDPMGGIVLTNDGNAILREIDVA----HPAAKSMIELSRTQDEEVGDGTTSVIILAGEILA 102
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1934310476 101 EGLKNVTAGANPIGIRRGIEAAVSTAVEELKAIAQPV--ANKEAIAQV 146
Cdd:cd03337 103 VAEPFLERGIHPTVIIKAYRKALEDALKILEEISIPVdvNDRAQMLKI 150
|
|
| |
