|
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 445953730 1 MSKEIKFSSDARSAMVRGVDILADTVKVTLGPKGRNVVLEKSFGSPLITNDGVTIAKEIELEDHFENMGAKLVSEVASKT 80
Cdd:PRK00013 1 MAKDIKFGEDARRKLLRGVNKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDPFENMGAQLVKEVASKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 81 NDIAGDGTTTATVLTQAIVREGIKNVTAGANPIGIRRGIETAVAAAVEALKNNAIPVANKEAIAQVAAVSSRS-EKVGEY 159
Cdd:PRK00013 81 NDVAGDGTTTATVLAQAIVREGLKNVAAGANPMDLKRGIDKAVEAAVEELKKISKPVEDKEEIAQVATISANGdEEIGKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 160 ISEAMEKVGKDGVITIEESRGMETELEVVEGMQFDRGYLSQYMVTDSEKMVADLENPYILITDKKISNIQEILPLLESIL 239
Cdd:PRK00013 161 IAEAMEKVGKEGVITVEESKGFETELEVVEGMQFDRGYLSPYFVTDPEKMEAELENPYILITDKKISNIQDLLPVLEQVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 240 QSNRPLLIIADDVDGEALPTLVLNKIRGTFNVVAVKAPGFGDRRKAMLEDIAILTGGTVITEDLGLELKDATIEALGQAA 319
Cdd:PRK00013 241 QSGKPLLIIAEDVEGEALATLVVNKLRGTLKVVAVKAPGFGDRRKAMLEDIAILTGGTVISEELGLKLEDATLEDLGQAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 320 RVTVDKDSTVIVEGAGNPEAISNRVAVIKSQIETTTSEFDREKLQERLAKLSGGVAVIKVGAATETELKEMKLRIEDALN 399
Cdd:PRK00013 321 KVVVTKDNTTIVDGAGDKEAIKARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATEVEMKEKKDRVEDALH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 400 ATRAAVEEGIVAGGGTALANVIPAVATLE-LTGDEATGRNIVLRALEEPVRQIAHNAGFEGSIVIDRLKNAE-LGIGFNA 477
Cdd:PRK00013 401 ATRAAVEEGIVPGGGVALLRAAPALEALKgLNGDEATGINIVLRALEAPLRQIAENAGLEGSVVVEKVKNGKgKGYGYNA 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 445953730 478 ATGEWVNMIDQGIIDPVKVSRSALQNAASVASLILTTEAVVANKPEPVAPAPAMDPSMMGGM 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: 878.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 1 MSKEIKFSSDARSAMVRGVDILADTVKVTLGPKGRNVVLEKSFGSPLITNDGVTIAKEIELEDHFENMGAKLVSEVASKT 80
Cdd:PRK12849 1 MAKIIKFDEEARRALERGVNKLADAVKVTLGPKGRNVVIDKSFGAPTITKDGVSIAKEIELEDPFENLGAQLVKEVASKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 81 NDIAGDGTTTATVLTQAIVREGIKNVTAGANPIGIRRGIETAVAAAVEALKNNAIPVANKEAIAQVAAVSSRS-EKVGEY 159
Cdd:PRK12849 81 NDVAGDGTTTATVLAQALVQEGLKNVAAGANPMDLKRGIDKAVEAVVEELKALARPVSGSEEIAQVATISANGdEEIGEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 160 ISEAMEKVGKDGVITIEESRGMETELEVVEGMQFDRGYLSQYMVTDSEKMVADLENPYILITDKKISNIQEILPLLESIL 239
Cdd:PRK12849 161 IAEAMEKVGKDGVITVEESKTLETELEVTEGMQFDRGYLSPYFVTDPERMEAVLEDPLILLTDKKISSLQDLLPLLEKVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 240 QSNRPLLIIADDVDGEALPTLVLNKIRGTFNVVAVKAPGFGDRRKAMLEDIAILTGGTVITEDLGLELKDATIEALGQAA 319
Cdd:PRK12849 241 QSGKPLLIIAEDVEGEALATLVVNKLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGLKLEEVTLDDLGRAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 320 RVTVDKDSTVIVEGAGNPEAISNRVAVIKSQIETTTSEFDREKLQERLAKLSGGVAVIKVGAATETELKEMKLRIEDALN 399
Cdd:PRK12849 321 RVTITKDNTTIVDGAGDKEAIEARVAQIRRQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATEVELKERKDRVEDALN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 400 ATRAAVEEGIVAGGGTALANVIPAVATLE-LTGDEATGRNIVLRALEEPVRQIAHNAGFEGSIVIDRLKNAELGIGFNAA 478
Cdd:PRK12849 401 ATRAAVEEGIVPGGGVALLRAAKALDELAgLNGDQAAGVEIVRRALEAPLRQIAENAGLDGSVVVAKVLELEDGFGFNAA 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 445953730 479 TGEWVNMIDQGIIDPVKVSRSALQNAASVASLILTTEAVVANKPEPVAPAPAMDPsmMGGM 539
Cdd:PRK12849 481 TGEYGDLIAAGIIDPVKVTRSALQNAASVAGLLLTTEALVADKPEEEDPPGGMGG--MGGM 539
|
|
| 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: 865.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 3 KEIKFSSDARSAMVRGVDILADTVKVTLGPKGRNVVLEKSFGSPLITNDGVTIAKEIELEDHFENMGAKLVSEVASKTND 82
Cdd:cd03344 1 KDIKFGEEARKALLRGVNKLADAVKVTLGPKGRNVVIEKSFGSPKITKDGVTVAKEIELEDPFENMGAQLVKEVASKTND 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 83 IAGDGTTTATVLTQAIVREGIKNVTAGANPIGIRRGIETAVAAAVEALKNNAIPVANKEAIAQVAAVSSRS-EKVGEYIS 161
Cdd:cd03344 81 VAGDGTTTATVLARAIIKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKPVKTKEEIAQVATISANGdEEIGELIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 162 EAMEKVGKDGVITIEESRGMETELEVVEGMQFDRGYLSQYMVTDSEKMVADLENPYILITDKKISNIQEILPLLESILQS 241
Cdd:cd03344 161 EAMEKVGKDGVITVEEGKTLETELEVVEGMQFDRGYLSPYFVTDPEKMEVELENPYILLTDKKISSIQELLPILELVAKA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 242 NRPLLIIADDVDGEALPTLVLNKIRGTFNVVAVKAPGFGDRRKAMLEDIAILTGGTVITEDLGLELKDATIEALGQAARV 321
Cdd:cd03344 241 GRPLLIIAEDVEGEALATLVVNKLRGGLKVCAVKAPGFGDRRKAMLEDIAILTGGTVISEELGLKLEDVTLEDLGRAKKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 322 TVDKDSTVIVEGAGNPEAISNRVAVIKSQIETTTSEFDREKLQERLAKLSGGVAVIKVGAATETELKEMKLRIEDALNAT 401
Cdd:cd03344 321 VVTKDDTTIIGGAGDKAAIKARIAQIRKQIEETTSDYDKEKLQERLAKLSGGVAVIKVGGATEVELKEKKDRVEDALNAT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 402 RAAVEEGIVAGGGTALANVIPAVATLE-LTGDEATGRNIVLRALEEPVRQIAHNAGFEGSIVIDRLKNAELGIGFNAATG 480
Cdd:cd03344 401 RAAVEEGIVPGGGVALLRASPALDKLKaLNGDEKLGIEIVRRALEAPLRQIAENAGVDGSVVVEKVLESPDGFGYDAATG 480
|
490 500 510
....*....|....*....|....*....|....*....
gi 445953730 481 EWVNMIDQGIIDPVKVSRSALQNAASVASLILTTEAVVA 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: 848.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 2 SKEIKFSSDARSAMVRGVDILADTVKVTLGPKGRNVVLEKSFGSPLITNDGVTIAKEIELEDHFENMGAKLVSEVASKTN 81
Cdd:TIGR02348 1 AKQIKFDEEARKALLRGVDKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDKFENMGAQLVKEVASKTN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 82 DIAGDGTTTATVLTQAIVREGIKNVTAGANPIGIRRGIETAVAAAVEALKNNAIPVANKEAIAQVAAVSSRS-EKVGEYI 160
Cdd:TIGR02348 81 DVAGDGTTTATVLAQAIVKEGLKNVAAGANPIELKRGIEKAVEAVVEELKKLSKPVKGKKEIAQVATISANNdEEIGSLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 161 SEAMEKVGKDGVITIEESRGMETELEVVEGMQFDRGYLSQYMVTDSEKMVADLENPYILITDKKISNIQEILPLLESILQ 240
Cdd:TIGR02348 161 AEAMEKVGKDGVITVEESKSLETELEVVEGMQFDRGYISPYFVTDAEKMEVELENPYILITDKKISNIKDLLPLLEKVAQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 241 SNRPLLIIADDVDGEALPTLVLNKIRGTFNVVAVKAPGFGDRRKAMLEDIAILTGGTVITEDLGLELKDATIEALGQAAR 320
Cdd:TIGR02348 241 SGKPLLIIAEDVEGEALATLVVNKLRGTLNVCAVKAPGFGDRRKAMLEDIAILTGGQVISEELGLKLEEVTLDDLGKAKK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 321 VTVDKDSTVIVEGAGNPEAISNRVAVIKSQIETTTSEFDREKLQERLAKLSGGVAVIKVGAATETELKEMKLRIEDALNA 400
Cdd:TIGR02348 321 VTVDKDNTTIVEGAGDKAAIKARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATETEMKEKKLRIEDALNA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 401 TRAAVEEGIVAGGGTALANVIPAVATLELTG-DEATGRNIVLRALEEPVRQIAHNAGFEGSIVIDRLKNAELGIGFNAAT 479
Cdd:TIGR02348 401 TRAAVEEGIVPGGGVALLRAAAALEGLKGDGeDEAIGIDIVKRALEAPLRQIAENAGLDGAVVAEKVKELKGNFGFNAAT 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 445953730 480 GEWVNMIDQGIIDPVKVSRSALQNAASVASLILTTEAVVANKPE 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: 803.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 1 MSKEIKFSSDARSAMVRGVDILADTVKVTLGPKGRNVVLEKSFGSPLITNDGVTIAKEIELEDHFENMGAKLVSEVASKT 80
Cdd:PRK12850 2 AAKEIRFSTDARDRLLRGVNILANAVKVTLGPKGRNVVLEKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVKEVASKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 81 NDIAGDGTTTATVLTQAIVREGIKNVTAGANPIGIRRGIETAVAAAVEALKNNAIPVANKEAIAQVAAVS-SRSEKVGEY 159
Cdd:PRK12850 82 NDLAGDGTTTATVLAQAIVREGAKLVAAGMNPMDLKRGIDLAVAAVVDELKKIAKKVTSSKEIAQVATISaNGDESIGEM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 160 ISEAMEKVGKDGVITIEESRGMETELEVVEGMQFDRGYLSQYMVTDSEKMVADLENPYILITDKKISNIQEILPLLESIL 239
Cdd:PRK12850 162 IAEAMDKVGKEGVITVEEAKTLGTELDVVEGMQFDRGYLSPYFVTNPEKMRAELEDPYILLHEKKISNLQDLLPILEAVV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 240 QSNRPLLIIADDVDGEALPTLVLNKIRGTFNVVAVKAPGFGDRRKAMLEDIAILTGGTVITEDLGLELKDATIEALGQAA 319
Cdd:PRK12850 242 QSGRPLLIIAEDVEGEALATLVVNKLRGGLKSVAVKAPGFGDRRKAMLEDIAVLTGGQVISEDLGIKLENVTLDMLGRAK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 320 RVTVDKDSTVIVEGAGNPEAISNRVAVIKSQIETTTSEFDREKLQERLAKLSGGVAVIKVGAATETELKEMKLRIEDALN 399
Cdd:PRK12850 322 RVLITKENTTIIDGAGDKKNIEARVKQIRAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKEKKDRVDDALH 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 400 ATRAAVEEGIVAGGGTALANVIPAVATLE-LTGDEATGRNIVLRALEEPVRQIAHNAGFEGSIVIDRLKNAELGIGFNAA 478
Cdd:PRK12850 402 ATRAAVEEGIVPGGGVALLRARSALRGLKgANADETAGIDIVRRALEEPLRQIATNAGFEGSVVVGKVAELPGNFGFNAQ 481
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 445953730 479 TGEWVNMIDQGIIDPVKVSRSALQNAASVASLILTTEAVVANKPEPVAPAPAMDPSMMGGM 539
Cdd:PRK12850 482 TGEYGDMVEAGIIDPAKVTRTALQDAASIAALLITTEAMVAEAPKKAAAAAAGPGPGMGGM 542
|
|
| 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: 776.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 1 MSKEIKFSSDARSAMVRGVDILADTVKVTLGPKGRNVVLEKSFGSPLITNDGVTIAKEIELEDHFENMGAKLVSEVASKT 80
Cdd:COG0459 1 MAKQILFGEDARRANIRGVKALADAVKVTLGPKGRNVMLVKSFGDPTITNDGVTIAKEIELEDPFENMGAQLVKEVASKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 81 NDIAGDGTTTATVLTQAIVREGIKNVTAGANPIGIRRGIETAVAAAVEALKNNAIPVANKEAIAQVAAVSSRS-EKVGEY 159
Cdd:COG0459 81 NDEAGDGTTTATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPVDDKEELAQVATISANGdEEIGEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 160 ISEAMEKVGKDGVITIEESRGMETELEVVEGMQFDRGYLSQYMVTDSEKMVADLENPYILITDKKISNIQEILPLLESIL 239
Cdd:COG0459 161 IAEAMEKVGKDGVITVEEGKGLETELEVVEGMQFDKGYLSPYFVTDPEKMPAELENAYILLTDKKISSIQDLLPLLEKVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 240 QSNRPLLIIADDVDGEALPTLVLNKIRGTFNVVAVKAPGFGDRRKAMLEDIAILTGGTVITEDLGLELKDATIEALGQAA 319
Cdd:COG0459 241 QSGKPLLIIAEDIDGEALATLVVNGIRGVLRVVAVKAPGFGDRRKAMLEDIAILTGGRVISEDLGLKLEDVTLDDLGRAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 320 RVTVDKDSTVIVEGAGNPEAIsnrvaviksqietttsefdreklqerlaklsggvaVIKVGAATETELKEMKLRIEDALN 399
Cdd:COG0459 321 RVEVDKDNTTIVEGAGNPKAI-----------------------------------VILVGAATEVEVKERKRRVEDALH 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 400 ATRAAVEEGIVAGGGTALANVIPAVATL--ELTGDEATGRNIVLRALEEPVRQIAHNAGFEGSIVIDRLKNAEL-GIGFN 476
Cdd:COG0459 366 ATRAAVEEGIVPGGGAALLRAARALRELaaKLEGDEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKVRAAKDkGFGFD 445
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 445953730 477 AATGEWVNMIDQGIIDPVKVSRSALQNAASVASLILTTEAVVANKPEPVAPA 528
Cdd:COG0459 446 AATGEYVDMLEAGVIDPAKVKRSALQNAASVAGLILTTEAVIADKPEKEEAA 497
|
|
| groEL |
PRK12851 |
chaperonin GroEL; Reviewed |
1-537 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 171770 Cd Length: 541 Bit Score: 750.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 1 MSKEIKFSSDARSAMVRGVDILADTVKVTLGPKGRNVVLEKSFGSPLITNDGVTIAKEIELEDHFENMGAKLVSEVASKT 80
Cdd:PRK12851 2 AAKEVKFHVEAREKMLRGVNILADAVKVTLGPKGRNVVIDKSFGAPTITNDGVTIAKEIELEDKFENMGAQMVREVASKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 81 NDIAGDGTTTATVLTQAIVREGIKNVTAGANPIGIRRGIETAVAAAVEALKNNAIPVANKEAIAQVAAVSSRS-EKVGEY 159
Cdd:PRK12851 82 NDVAGDGTTTATVLAQAIVREGAKAVAAGANPMDLKRGIDRAVAAVVEELKANARPVTTNAEIAQVATISANGdAEIGRL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 160 ISEAMEKVGKDGVITIEESRGMETELEVVEGMQFDRGYLSQYMVTDSEKMVADLENPYILITDKKISNIQEILPLLESIL 239
Cdd:PRK12851 162 VAEAMEKVGNEGVITVEESKTAETELEVVEGMQFDRGYLSPYFVTDADKMEAELEDPYILIHEKKISNLQDLLPVLEAVV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 240 QSNRPLLIIADDVDGEALPTLVLNKIRGTFNVVAVKAPGFGDRRKAMLEDIAILTGGTVITEDLGLELKDATIEALGQAA 319
Cdd:PRK12851 242 QSGKPLLIIAEDVEGEALATLVVNKLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGIKLENVTLEQLGRAK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 320 RVTVDKDSTVIVEGAGNPEAISNRVAVIKSQIETTTSEFDREKLQERLAKLSGGVAVIKVGAATETELKEMKLRIEDALN 399
Cdd:PRK12851 322 KVVVEKENTTIIDGAGSKTEIEGRVAQIRAQIEETTSDYDREKLQERLAKLAGGVAVIRVGASTEVEVKEKKDRVDDALH 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 400 ATRAAVEEGIVAGGGTALANVIPAVATLE-LTGDEATGRNIVLRALEEPVRQIAHNAGFEGSIVIDRLKNAELGIGFNAA 478
Cdd:PRK12851 402 ATRAAVEEGIVPGGGVALLRAVKALDKLEtANGDQRTGVEIVRRALEAPVRQIAENAGAEGSVVVGKLREKPGGYGFNAA 481
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 445953730 479 TGEWVNMIDQGIIDPVKVSRSALQNAASVASLILTTEAVVANKPEPVAPAPAMDPSMMG 537
Cdd:PRK12851 482 TNEYGDLYAQGVIDPVKVVRTALQNAASVAGLLLTTEAMVAEKPKKEPAPPAPPGGGMD 540
|
|
| groEL |
CHL00093 |
chaperonin GroEL |
1-523 |
0e+00 |
|
chaperonin GroEL
Pssm-ID: 177025 Cd Length: 529 Bit Score: 708.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 1 MSKEIKFSSDARSAMVRGVDILADTVKVTLGPKGRNVVLEKSFGSPLITNDGVTIAKEIELEDHFENMGAKLVSEVASKT 80
Cdd:CHL00093 1 MSKKILYQDNARRALERGMDILAEAVSVTLGPKGRNVVLEKKYGSPQIVNDGVTIAKEIELEDHIENTGVALIRQAASKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 81 NDIAGDGTTTATVLTQAIVREGIKNVTAGANPIGIRRGIETAVAAAVEALKNNAIPVANKEAIAQVAAVSS-RSEKVGEY 159
Cdd:CHL00093 81 NDVAGDGTTTATVLAYAIVKQGMKNVAAGANPISLKRGIEKATQYVVSQIAEYARPVEDIQAITQVASISAgNDEEVGSM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 160 ISEAMEKVGKDGVITIEESRGMETELEVVEGMQFDRGYLSQYMVTDSEKMVADLENPYILITDKKISNI-QEILPLLESI 238
Cdd:CHL00093 161 IADAIEKVGREGVISLEEGKSTVTELEITEGMRFEKGFISPYFVTDTERMEVVQENPYILLTDKKITLVqQDLLPILEQV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 239 LQSNRPLLIIADDVDGEALPTLVLNKIRGTFNVVAVKAPGFGDRRKAMLEDIAILTGGTVITEDLGLELKDATIEALGQA 318
Cdd:CHL00093 241 TKTKRPLLIIAEDVEKEALATLVLNKLRGIVNVVAVRAPGFGDRRKAMLEDIAILTGGQVITEDAGLSLETIQLDLLGQA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 319 ARVTVDKDSTVIVeGAGNPEAISNRVAVIKSQIETTTSEFDREKLQERLAKLSGGVAVIKVGAATETELKEMKLRIEDAL 398
Cdd:CHL00093 321 RRIIVTKDSTTII-ADGNEEQVKARCEQLRKQIEIADSSYEKEKLQERLAKLSGGVAVIKVGAATETEMKDKKLRLEDAI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 399 NATRAAVEEGIVAGGGTALANVIPAV---ATLELTGDEATGRNIVLRALEEPVRQIAHNAGFEGSIVIDRLKNAELGIGF 475
Cdd:CHL00093 400 NATKAAVEEGIVPGGGATLVHLSENLktwAKNNLKEDELIGALIVARAILAPLKRIAENAGKNGSVIIEKVQEQDFEIGY 479
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 445953730 476 NAATGEWVNMIDQGIIDPVKVSRSALQNAASVASLILTTEAVVANKPE 523
Cdd:CHL00093 480 NAANNKFVNMYEAGIIDPAKVTRSALQNAASIASMILTTECIIVDKKE 527
|
|
| groEL |
PRK12852 |
chaperonin GroEL; Reviewed |
1-539 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237232 Cd Length: 545 Bit Score: 706.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 1 MSKEIKFSSDARSAMVRGVDILADTVKVTLGPKGRNVVLEKSFGSPLITNDGVTIAKEIELEDHFENMGAKLVSEVASKT 80
Cdd:PRK12852 2 AAKDVKFSGDARDRMLRGVDILANAVKVTLGPKGRNVVIEKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVREVASKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 81 NDIAGDGTTTATVLTQAIVREGIKNVTAGANPIGIRRGIETAVAAAVEALKNNAIPVANKEAIAQVAAVSSRS-EKVGEY 159
Cdd:PRK12852 82 NDLAGDGTTTATVLAQAIVREGAKAVAAGMNPMDLKRGIDIAVAAVVKDIEKRAKPVASSAEIAQVGTISANGdAAIGKM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 160 ISEAMEKVGKDGVITIEESRGMETELEVVEGMQFDRGYLSQYMVTDSEKMVADLENPYILITDKKISNIQEILPLLESIL 239
Cdd:PRK12852 162 IAQAMQKVGNEGVITVEENKSLETEVDIVEGMKFDRGYLSPYFVTNAEKMTVELDDAYILLHEKKLSGLQAMLPVLEAVV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 240 QSNRPLLIIADDVDGEALPTLVLNKIRGTFNVVAVKAPGFGDRRKAMLEDIAILTGGTVITEDLGLELKDATIEALGQAA 319
Cdd:PRK12852 242 QSGKPLLIIAEDVEGEALATLVVNRLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGQLISEDLGIKLENVTLKMLGRAK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 320 RVTVDKDSTVIVEGAGNPEAISNRVAVIKSQIETTTSEFDREKLQERLAKLSGGVAVIKVGAATETELKEMKLRIEDALN 399
Cdd:PRK12852 322 KVVIDKENTTIVNGAGKKADIEARVGQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKEKKDRVEDALN 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 400 ATRAAVEEGIVAGGGTALANVIPAVATLE-LTGDEATGRNIVLRALEEPVRQIAHNAGFEGSIVIDR-LKNAELGIGFNA 477
Cdd:PRK12852 402 ATRAAVQEGIVPGGGVALLRAKKAVGRINnDNADVQAGINIVLKALEAPIRQIAENAGVEGSIVVGKiLENKSETFGFDA 481
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 445953730 478 ATGEWVNMIDQGIIDPVKVSRSALQNAASVASLILTTEAVVANKPEPVAPAPAMDPSMMGGM 539
Cdd:PRK12852 482 QTEEYVDMVAKGIIDPAKVVRTALQDAASVAGLLVTTEAMVAELPKKDAAPAMPAGGGMGGM 543
|
|
| PTZ00114 |
PTZ00114 |
Heat shock protein 60; Provisional |
2-536 |
0e+00 |
|
Heat shock protein 60; Provisional
Pssm-ID: 185455 Cd Length: 555 Bit Score: 702.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 2 SKEIKFSSDARSAMVRGVDILADTVKVTLGPKGRNVVLEKSFGSPLITNDGVTIAKEIELEDHFENMGAKLVSEVASKTN 81
Cdd:PTZ00114 14 GKEIRFGDEARQSLLKGIERLADAVAVTLGPKGRNVIIEQEYGSPKITKDGVTVAKAIEFSDRFENVGAQLIRQVASKTN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 82 DIAGDGTTTATVLTQAIVREGIKNVTAGANPIGIRRGIETAVAAAVEALKNNAIPVANKEAIAQVAAVSSRSEKV-GEYI 160
Cdd:PTZ00114 94 DKAGDGTTTATILARAIFREGCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQSRPVKTKEDILNVATISANGDVEiGSLI 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 161 SEAMEKVGKDGVITIEESRGMETELEVVEGMQFDRGYLSQYMVTDSEKMVADLENPYILITDKKISNIQEILPLLESILQ 240
Cdd:PTZ00114 174 ADAMDKVGKDGTITVEDGKTLEDELEVVEGMSFDRGYISPYFVTNEKTQKVELENPLILVTDKKISSIQSILPILEHAVK 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 241 SNRPLLIIADDVDGEALPTLVLNKIRGTFNVVAVKAPGFGDRRKAMLEDIAILTGGTVITED-LGLELKDATIEALGQAA 319
Cdd:PTZ00114 254 NKRPLLIIAEDVEGEALQTLIINKLRGGLKVCAVKAPGFGDNRKDILQDIAVLTGATVVSEDnVGLKLDDFDPSMLGSAK 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 320 RVTVDKDSTVIVEGAGNPEAISNRVAVIKSQIETTTSEFDREKLQERLAKLSGGVAVIKVGAATETELKEMKLRIEDALN 399
Cdd:PTZ00114 334 KVTVTKDETVILTGGGDKAEIKERVELLRSQIERTTSEYDKEKLKERLAKLSGGVAVIKVGGASEVEVNEKKDRIEDALN 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 400 ATRAAVEEGIVAGGGTALANVIPAVATLE----LTGDEATGRNIVLRALEEPVRQIAHNAGFEGSIVIDR-LKNAELGIG 474
Cdd:PTZ00114 414 ATRAAVEEGIVPGGGVALLRASKLLDKLEedneLTPDQRTGVKIVRNALRLPTKQIAENAGVEGAVVVEKiLEKKDPSFG 493
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 445953730 475 FNAATGEWVNMIDQGIIDPVKVSRSALQNAASVASLILTTEAVVANKPEPVAPAPAMDPSMM 536
Cdd:PTZ00114 494 YDAQTGEYVNMFEAGIIDPTKVVRSALVDAASVASLMLTTEAAIVDLPKEKKKNKNSAAPPM 555
|
|
| PRK14104 |
PRK14104 |
chaperonin GroEL; Provisional |
2-539 |
0e+00 |
|
chaperonin GroEL; Provisional
Pssm-ID: 172594 Cd Length: 546 Bit Score: 606.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 2 SKEIKFSSDARSAMVRGVDILADTVKVTLGPKGRNVVLEKSFGSPLITNDGVTIAKEIELEDHFENMGAKLVSEVASKTN 81
Cdd:PRK14104 3 AKEVKFGVDARDRMLRGVDILANAVKVTLGPKGRNVVLDKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVREVASKSA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 82 DIAGDGTTTATVLTQAIVREGIKNVTAGANPIGIRRGIETAVAAAVEALKNNAIPVANKEAIAQVAAVSSRSE-KVGEYI 160
Cdd:PRK14104 83 DAAGDGTTTATVLAQAIVREGAKSVAAGMNPMDLKRGIDLAVEAVVADLVKNSKKVTSNDEIAQVGTISANGDaEIGKFL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 161 SEAMEKVGKDGVITIEESRGMETELEVVEGMQFDRGYLSQYMVTDSEKMVADLENPYILITDKKISNIQEILPLLESILQ 240
Cdd:PRK14104 163 ADAMKKVGNEGVITVEEAKSLETELDVVEGMQFDRGYISPYFVTNADKMRVEMDDAYILINEKKLSSLNELLPLLEAVVQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 241 SNRPLLIIADDVDGEALPTLVLNKIRGTFNVVAVKAPGFGDRRKAMLEDIAILTGGTVITEDLGLELKDATIEALGQAAR 320
Cdd:PRK14104 243 TGKPLVIVAEDVEGEALATLVVNRLRGGLKVAAVKAPGFGDRRKAMLQDIAILTGGQAISEDLGIKLENVTLQMLGRAKK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 321 VTVDKDSTVIVEGAGNPEAISNRVAVIKSQIETTTSEFDREKLQERLAKLSGGVAVIKVGAATETELKEMKLRIEDALNA 400
Cdd:PRK14104 323 VMIDKENTTIVNGAGKKADIEARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKERKDRVDDAMHA 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 401 TRAAVEEGIVAGGGTALANVIPAVATLELTG-DEATGRNIVLRALEEPVRQIAHNAGFEGSIVIDR-LKNAELGIGFNAA 478
Cdd:PRK14104 403 TRAAVEEGIVPGGGVALLRASEQLKGIKTKNdDQKTGVEIVRKALSAPARQIAINAGEDGSVIVGKiLEKEQYSYGFDSQ 482
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 445953730 479 TGEWVNMIDQGIIDPVKVSRSALQNAASVASLILTTEAVVANKPEPVAPAPAMDPSM-MGGM 539
Cdd:PRK14104 483 TGEYGNLVSKGIIDPTKVVRTAIQNAASVAALLITTEAMVAELPKKGGAGPAMPPGGgMGGM 544
|
|
| PLN03167 |
PLN03167 |
Chaperonin-60 beta subunit; Provisional |
2-537 |
0e+00 |
|
Chaperonin-60 beta subunit; Provisional
Pssm-ID: 215611 [Multi-domain] Cd Length: 600 Bit Score: 536.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 2 SKEIKFSSD--ARSAMVRGVDILADTVKVTLGPKGRNVVLEKSFGSPLITNDGVTIAKEIELEDHFENMGAKLVSEVASK 79
Cdd:PLN03167 56 AKELHFNKDgsAIKKLQAGVNKLADLVGVTLGPKGRNVVLESKYGSPKIVNDGVTVAKEVELEDPVENIGAKLVRQAAAK 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 80 TNDIAGDGTTTATVLTQAIVREGIKNVTAGANPIGIRRGIETAVAAAVEALKNNAIPVANKEaIAQVAAVSS-RSEKVGE 158
Cdd:PLN03167 136 TNDLAGDGTTTSVVLAQGLIAEGVKVVAAGANPVQITRGIEKTAKALVKELKKMSKEVEDSE-LADVAAVSAgNNYEVGN 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 159 YISEAMEKVGKDGVITIEESRGMETELEVVEGMQFDRGYLSQYMVTDSEKMVADLENPYILITDKKISNIQEILPLLESI 238
Cdd:PLN03167 215 MIAEAMSKVGRKGVVTLEEGKSAENNLYVVEGMQFDRGYISPYFVTDSEKMSVEYDNCKLLLVDKKITNARDLIGILEDA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 239 LQSNRPLLIIADDVDGEALPTLVLNKIRGTFNVVAVKAPGFGDRRKAMLEDIAILTGGTVITEDLGLELKDATIEALGQA 318
Cdd:PLN03167 295 IRGGYPLLIIAEDIEQEALATLVVNKLRGSLKIAALKAPGFGERKSQYLDDIAILTGGTVIREEVGLSLDKVGKEVLGTA 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 319 ARVTVDKDSTVIVEGAGNPEAISNRVAVIKSQIETTTSEFDREKLQERLAKLSGGVAVIKVGAATETELKEMKLRIEDAL 398
Cdd:PLN03167 375 AKVVLTKDTTTIVGDGSTQEAVNKRVAQIKNLIEAAEQDYEKEKLNERIAKLSGGVAVIQVGAQTETELKEKKLRVEDAL 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 399 NATRAAVEEGIVAGGGTALANVIPAVATLELTGD---EATGRNIVLRALEEPVRQIAHNAGFEGSIVIDR-LKNAELGIG 474
Cdd:PLN03167 455 NATKAAVEEGIVVGGGCTLLRLASKVDAIKDTLEndeQKVGADIVKRALSYPLKLIAKNAGVNGSVVSEKvLSNDNPKFG 534
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 445953730 475 FNAATGEWVNMIDQGIIDPVKVSRSALQNAASVASLILTTEAVVAN--KPEPVAPAPAMDPSMMG 537
Cdd:PLN03167 535 YNAATGKYEDLMAAGIIDPTKVVRCCLEHAASVAKTFLTSDCVVVEikEPEPVPAGNPMDNSGYG 599
|
|
| chaperonin_type_I_II |
cd00309 |
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ... |
3-519 |
3.15e-149 |
|
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: 436.09 E-value: 3.15e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 3 KEIKFSSDARSAMVRGVDILADTVKVTLGPKGRNVVLEKSFGSPLITNDGVTIAKEIELEdhfeNMGAKLVSEVASKTND 82
Cdd:cd00309 1 KEREFGEEARLSNINAAKALADAVKTTLGPKGMDKMLVDSLGDPTITNDGATILKEIEVE----HPAAKLLVEVAKSQDD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 83 IAGDGTTTATVLTQAIVREGIKNVTAGANPIGIRRGIETAVAAAVEALKNNAIP--VANKEAIAQVAAVSSRS------- 153
Cdd:cd00309 77 EVGDGTTTVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVPidVEDREELLKVATTSLNSklvsggd 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 154 EKVGEYISEAMEKVGK------DGVITIEESRG-METELEVVEGMQFDRGYLSQYMVTdsekmvaDLENPYILITDKKIS 226
Cdd:cd00309 157 DFLGELVVDAVLKVGKengdvdLGVIRVEKKKGgSLEDSELVVGMVFDKGYLSPYMPK-------RLENAKILLLDCKLE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 227 NiqeilpllesilqsnrplLIIADD-VDGEALPTLVLNKIrgtfnvVAVKApgfgdRRKAMLEDIAILTGGTVITedlgl 305
Cdd:cd00309 230 Y------------------VVIAEKgIDDEALHYLAKLGI------MAVRR-----VRKEDLERIAKATGATIVS----- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 306 ELKDATIEALGQAARVTVDK----DSTVIVEGAGnpeaisnrvaviksqietttsefdreklqerlaklsGGVAVIKVGA 381
Cdd:cd00309 276 RLEDLTPEDLGTAGLVEETKigdeKYTFIEGCKG------------------------------------GKVATILLRG 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 382 ATETELKEMKLRIEDALNATRAAVEE-GIVAGGGTALANVIPAVATL--ELTGDEATGRNIVLRALEEPVRQIAHNAGFE 458
Cdd:cd00309 320 ATEVELDEAERSLHDALCAVRAAVEDgGIVPGGGAAEIELSKALEELakTLPGKEQLGIEAFADALEVIPRTLAENAGLD 399
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 445953730 459 GSIVIDRLKNAELGIGFNAA----TGEWVNMIDQGIIDPVKVSRSALQNAASVASLILTTEAVVA 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 |
1.25e-91 |
|
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: 289.10 E-value: 1.25e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 22 LADTVKVTLGPKGRNVVLEKSFGSPLITNDGVTIAKEIELEdhfeNMGAKLVSEVASKTNDIAGDGTTTATVLTQAIVRE 101
Cdd:pfam00118 1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELEIQ----HPAAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 102 GIKNVTAGANPIGIRRGIETAVAAAVEALKNN-AIPV--ANKEAIAQVAAVSSRS-------EKVGEYISEAME------ 165
Cdd:pfam00118 77 AEKLLAAGVHPTTIIEGYEKALEKALEILDSIiSIPVedVDREDLLKVARTSLSSkiisresDFLAKLVVDAVLaipknd 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 166 ---KVGKDGVITIEESRGMETELevVEGMQFDRGYLsqymvtdSEKMVADLENPYILITDKKISNIQE------------ 230
Cdd:pfam00118 157 gsfDLGNIGVVKILGGSLEDSEL--VDGVVLDKGPL-------HPDMPKRLENAKVLLLNCSLEYEKTetkatvvlsdae 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 231 ------------ILPLLESILQSNRPLLIIADDVDGEALPTLVLNKIRGTFNVvavkapgfgdrRKAMLEDIAILTGGTV 298
Cdd:pfam00118 228 qlerflkaeeeqILEIVEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMALRRV-----------KKRDLERLAKATGARA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 299 ITedlglELKDATIEALGQAARVTVDK---DSTVIVEGagnpeaisnrvaviksqietttsefdreklqerlaKLSGGVA 375
Cdd:pfam00118 297 VS-----SLDDLTPDDLGTAGKVEEEKigdEKYTFIEG-----------------------------------CKSPKAA 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 376 VIKVGAATETELKEMKLRIEDALNATRAAVEE-GIVAGGG---TALANVIPAVATlELTGDEATGRNIVLRALEEPVRQI 451
Cdd:pfam00118 337 TILLRGATDHVLDEIERSIHDALCVVKNAIEDpRVVPGGGaveMELARALREYAK-SVSGKEQLAIEAFAEALEVIPKTL 415
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 445953730 452 AHNAGFEGSIVIDRLKNA----ELGIGFNAATGEWVNMIDQGIIDPVKVSRSALQNAASVASLILTTEAVVANK 521
Cdd:pfam00118 416 AENAGLDPIEVLAELRAAhasgEKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKSATEAASTILRIDDIIKAK 489
|
|
| chaperonin_like |
cd03333 |
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ... |
140-407 |
9.31e-42 |
|
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: 148.77 E-value: 9.31e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 140 KEAIAQVAAVSSRS------EKVGEYISEAMEKVGKD------GVITIEESRG-METELEVVEGMQFDRGYLSQYMVTDs 206
Cdd:cd03333 1 RELLLQVATTSLNSklsswdDFLGKLVVDAVLKVGPDnrmddlGVIKVEKIPGgSLEDSELVVGVVFDKGYASPYMPKR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 207 ekmvadLENPYILITDKKISNiqeilpllesilqsnrplLIIADD-VDGEALPTLVLNKIrgtfnvVAVKApgfgdRRKA 285
Cdd:cd03333 80 ------LENAKILLLDCPLEY------------------VVIAEKgIDDLALHYLAKAGI------MAVRR-----VKKE 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 286 MLEDIAILTGGTVITedlglELKDATIEALGQAARVTVDKDS----TVIVEGAGnpeaisnrvaviksqietttsefdre 361
Cdd:cd03333 125 DLERIARATGATIVS-----SLEDLTPEDLGTAELVEETKIGeeklTFIEGCKG-------------------------- 173
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 445953730 362 klqerlaklsGGVAVIKVGAATETELKEMKLRIEDALNATRAAVEE 407
Cdd:cd03333 174 ----------GKAATILLRGATEVELDEVKRSLHDALCAVRAAVEE 209
|
|
| cpn60 |
cd03343 |
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ... |
10-521 |
1.04e-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: 142.79 E-value: 1.04e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 10 DARSAMVRGVDILADTVKVTLGPKGRNVVLEKSFGSPLITNDGVTIAKEIELedhfENMGAKLVSEVASKTNDIAGDGTT 89
Cdd:cd03343 15 DAQRMNIAAAKAVAEAVRTTLGPKGMDKMLVDSLGDVTITNDGATILKEMDI----EHPAAKMLVEVAKTQDEEVGDGTT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 90 TATVLTQAIVREGIKNVTAGANPIGIRRGIETAVAAAVEALKNNAIPV--ANKE---AIAQVAAVSSRSEKVGEYISEam 164
Cdd:cd03343 91 TAVVLAGELLEKAEDLLDQNIHPTVIIEGYRLAAEKALELLDEIAIKVdpDDKDtlrKIAKTSLTGKGAEAAKDKLAD-- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 165 ekVGKDGVITIEESRGMETE-------LEVVEGMQFDRGYLSQYMVTDSEK----MVADLENPYILITDKKISnIQEilP 233
Cdd:cd03343 169 --LVVDAVLQVAEKRDGKYVvdldnikIEKKTGGSVDDTELIRGIVIDKEVvhpgMPKRVENAKIALLDAPLE-VKK--T 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 234 LLESILQSNRPLLIIAD-DVDGEALPTLVlNKIRGT-FNVVAV-------------KAPGFGDRR--KAMLEDIAILTGG 296
Cdd:cd03343 244 EIDAKIRITSPDQLQAFlEQEEAMLKEMV-DKIADTgANVVFCqkgiddlaqhylaKAGILAVRRvkKSDMEKLARATGA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 297 TVITedlglELKDATIEALGQAARVTVDK---DSTVIVEGAGNPEAISnrvaviksqietttsefdreklqerlaklsgg 373
Cdd:cd03343 323 KIVT-----NIDDLTPEDLGEAELVEERKvgdDKMVFVEGCKNPKAVT-------------------------------- 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 374 vavIKVGAATETELKEMKLRIEDALNATRAAVEEG-IVAGGG---TALANVIPAVATlELTGDEATGRNIVLRALEEPVR 449
Cdd:cd03343 366 ---ILLRGGTEHVVDELERALEDALRVVADALEDGkVVAGGGaveIELAKRLREYAR-SVGGREQLAVEAFADALEEIPR 441
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 445953730 450 QIAHNAGFEGSIVIDRLKNA----ELGIGFNAATGEWVNMIDQGIIDPVKVSRSALQNAASVASLILTTEAVVANK 521
Cdd:cd03343 442 TLAENAGLDPIDTLVELRAAhekgNKNAGLDVYTGEVVDMLEKGVIEPLRVKKQAIKSATEAATMILRIDDVIAAK 517
|
|
| thermosome_beta |
NF041083 |
thermosome subunit beta; |
10-521 |
3.99e-35 |
|
thermosome subunit beta;
Pssm-ID: 469010 Cd Length: 519 Bit Score: 138.16 E-value: 3.99e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 10 DARSAMVRGVDILADTVKVTLGPKGRNVVLEKSFGSPLITNDGVTIAKEIELedhfENMGAKLVSEVASKTNDIAGDGTT 89
Cdd:NF041083 17 DAQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDIVITNDGATILKEMDV----QHPAAKMLVEVAKTQDDEVGDGTT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 90 TATVLTQAIVREGIKNVTAGANPIGIRRGIETAVAAAVEALKNNAIPVA--NKEAIAQVAAVSSRSeKVGEYISEAMEKV 167
Cdd:NF041083 93 TAVVLAGELLKKAEELLDQNIHPTIIANGYRLAAEKAIEILDEIAEKVDpdDRETLKKIAETSLTS-KGVEEARDYLAEI 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 168 GKDGVITIEESRGME-------TELEVVEGMQFDRGYLSQYMVTDSEK----MVADLENPYILITDKKISnIQEilPLLE 236
Cdd:NF041083 172 AVKAVKQVAEKRDGKyyvdldnIQIEKKHGGSIEDTQLIYGIVIDKEVvhpgMPKRVENAKIALLDAPLE-VKK--TEID 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 237 SILQSNRPLLIIADDVDGEALPTLVLNKIRGT-FNVVAV-------------KAPGFGDRR--KAMLEDIAILTGGTVIT 300
Cdd:NF041083 249 AEIRITDPDQLQKFLDQEEKMLKEMVDKIKATgANVVFCqkgiddlaqhylaKAGILAVRRvkKSDMEKLAKATGARIVT 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 301 edlglELKDATIEALGQAARVTVDK---DSTVIVEGAGNPEAISnrvaviksqietttsefdreklqerlaklsggvavI 377
Cdd:NF041083 329 -----NIDDLTPEDLGYAELVEERKvgdDKMVFVEGCKNPKAVT-----------------------------------I 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 378 KVGAATETELKEMKLRIEDALNATRAAVEEG-IVAGGGTA---LANVIPAVATlELTGDEATGRNIVLRALEEPVRQIAH 453
Cdd:NF041083 369 LIRGGTEHVVDEAERALEDALSVVADAVEDGkIVAGGGAPeveLAKRLREYAA-TVGGREQLAVEAFAEALEIIPRTLAE 447
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 445953730 454 NAGFEGsivIDRL-------KNAELGIGFNAATGEWVNMIDQGIIDPVKVSRSALQNAASVASLILTTEAVVANK 521
Cdd:NF041083 448 NAGLDP---IDILvklrsahEKGKKWAGINVFTGEVVDMWELGVIEPLRVKTQAIKSATEAATMILRIDDVIAAK 519
|
|
| thermosome_alpha |
NF041082 |
thermosome subunit alpha; |
10-521 |
1.88e-33 |
|
thermosome subunit alpha;
Pssm-ID: 469009 Cd Length: 518 Bit Score: 133.47 E-value: 1.88e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 10 DARSAMVRGVDILADTVKVTLGPKGRNVVLEKSFGSPLITNDGVTIAKEIELedhfENMGAKLVSEVASKTNDIAGDGTT 89
Cdd:NF041082 17 DAQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDVVITNDGVTILKEMDI----EHPAAKMIVEVAKTQDDEVGDGTT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 90 TATVLTQAIVREGIKNVTAGANPIGIRRGIETAVAAAVEALKNNAIPV--ANKEAIAQVAA-------VSSRSEKVGEYI 160
Cdd:NF041082 93 TAVVLAGELLKKAEELLDQDIHPTIIAEGYRLAAEKALEILDEIAIKVdpDDKETLKKIAAtamtgkgAEAAKDKLADLV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 161 SEA----MEKVGKDGV----ITIEESRG---METELevVEGmqfdrgylsqyMVTDSEK----MVADLENPYILI----- 220
Cdd:NF041082 173 VDAvkavAEKDGGYNVdldnIKVEKKVGgsiEDSEL--VEG-----------VVIDKERvhpgMPKRVENAKIALldapl 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 221 ------TDKKIS-----NIQEIL--------PLLESILQSNRPLLIIADDVDGEALPTLVLNKIRGTFNVvavkapgfgd 281
Cdd:NF041082 240 evkkteIDAKISitdpdQLQAFLdqeekmlkEMVDKIADSGANVVFCQKGIDDLAQHYLAKEGILAVRRV---------- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 282 rRKAMLEDIAILTGGTVITedlglELKDATIEALGQAARVT---VDKDSTVIVEGAGNPEAISnrvaviksqietttsef 358
Cdd:NF041082 310 -KKSDMEKLAKATGARIVT-----SIDDLSPEDLGYAGLVEerkVGGDKMIFVEGCKNPKAVT----------------- 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 359 dreklqerlaklsggvavIKVGAATETELKEMKLRIEDALNATRAAVEEG-IVAGGG---TALANVIPAVATlELTGDEA 434
Cdd:NF041082 367 ------------------ILLRGGTEHVVDEVERALEDALRVVRVVLEDGkVVAGGGapeVELALRLREYAA-SVGGREQ 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 435 TGRNIVLRALEEPVRQIAHNAGFEGSIVIDRLKNA----ELGIGFNAATGEWVNMIDQGIIDPVKVSRSALQNAASVASL 510
Cdd:NF041082 428 LAIEAFAEALEIIPRTLAENAGLDPIDALVELRSAhekgNKTAGLDVYTGKVVDMLEIGVVEPLRVKTQAIKSATEAAVM 507
|
570
....*....|.
gi 445953730 511 ILTTEAVVANK 521
Cdd:NF041082 508 ILRIDDVIAAA 518
|
|
| TCP1_beta |
cd03336 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ... |
10-522 |
7.73e-16 |
|
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: 80.07 E-value: 7.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 10 DARSAMVRGVDILADTVKVTLGPKGRNVVLE--KSFGSPLITNDGVTIAKEIeledHFENMGAKLVSEVASKTNDIAGDG 87
Cdd:cd03336 13 TARLSSFVGAIAIGDLVKTTLGPKGMDKILQsvGRSGGVTVTNDGATILKSI----GVDNPAAKVLVDISKVQDDEVGDG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 88 TTTATVLTQAIVREGIKNVTAGANPIGIRRGIETAVAAAVEALKNNAI-----PVANKEAIAQVAAvSSRSEKVGEYISE 162
Cdd:cd03336 89 TTSVTVLAAELLREAEKLVAQKIHPQTIIEGYRMATAAAREALLSSAVdhssdEEAFREDLLNIAR-TTLSSKILTQDKE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 163 AMEKVGKDGVITIEESrgmeTELEVVEGMQFDRGYLSQYMVTDS---EKMVA-----DLENPYILI------TDK-KI-- 225
Cdd:cd03336 168 HFAELAVDAVLRLKGS----GNLDAIQIIKKLGGSLKDSYLDEGfllDKKIGvnqpkRIENAKILIantpmdTDKiKIfg 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 226 --------SNIQEIlPLLESILQSNRPLLIIADDVDGEALPTLVLN---KIRGTFNVVAVKAPGFgdrrkAMLEDIAILT 294
Cdd:cd03336 244 akvrvdstAKVAEI-EEAEKEKMKNKVEKILKHGINCFINRQLIYNypeQLFADAGIMAIEHADF-----DGVERLALVT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 295 GGTVITedlglelkdatiealgqaarvTVDKDSTVIVegaGNPEAISnrvaviksqiETTTSEfdreklqERLAKLSG-- 372
Cdd:cd03336 318 GGEIAS---------------------TFDHPELVKL---GTCKLIE----------EIMIGE-------DKLIRFSGva 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 373 --GVAVIKVGAATETELKEMKLRIEDALNATRAAVEEG-IVAGGG---TALANVIPAVATlELTGDEATGRNIVLRALEE 446
Cdd:cd03336 357 agEACTIVLRGASQQILDEAERSLHDALCVLAQTVKDTrVVLGGGcseMLMAKAVEELAK-KTPGKKSLAIEAFAKALRQ 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 447 PVRQIAHNAGFEGSIVIDRLK----NAELGIGFNAATGEWVNMIDQGIIDPVKVSRSALQNAASVASLILTTEAVVANKP 522
Cdd:cd03336 436 LPTIIADNAGYDSAELVAQLRaahyNGNTTAGLDMRKGTVGDMKELGITESFKVKRQVLLSASEAAEMILRVDDIIKCAP 515
|
|
| chap_CCT_beta |
TIGR02341 |
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ... |
10-524 |
3.67e-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: 77.98 E-value: 3.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 10 DARSAMVRGVDILADTVKVTLGPKGRNVVLEK--SFGSPLITNDGVTIAKEIELEdhfeNMGAKLVSEVASKTNDIAGDG 87
Cdd:TIGR02341 14 NARLSSFVGAIAIGDLVKSTLGPKGMDKILQSssSDASIMVTNDGATILKSIGVD----NPAAKVLVDMSKVQDDEVGDG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 88 TTTATVLTQAIVREGIKNVTAGANPIGIRRGIETAVAAAVEALKNNAI-----PVANKEAIAQVAAvSSRSEKVGEYISE 162
Cdd:TIGR02341 90 TTSVTVLAAELLREAEKLINQKIHPQTIIAGYREATKAARDALLKSAVdngsdEVKFRQDLMNIAR-TTLSSKILSQHKD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 163 AMEKVGKDGVITIEESrgmeTELEVVEGMQFDRGYLSQymvtdsekmvADLENPYILitDKKISNIQEILPLLESILQSN 242
Cdd:TIGR02341 169 HFAQLAVDAVLRLKGS----GNLEAIQIIKKLGGSLAD----------SYLDEGFLL--DKKIGVNQPKRIENAKILIAN 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 243 RPLLIIADDVDGEALptlvlnKIRGTFNVVAVKAPGfGDRRKAMLEDIAILTGGTVITEDLGLE-----LKDATIEALGQ 317
Cdd:TIGR02341 233 TGMDTDKVKIFGSRV------RVDSTAKVAELEHAE-KEKMKEKVEKILKHGINCFINRQLIYNypeqlFADAGVMAIEH 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 318 AARVTVDKDSTV----IVEGAGNPEAIsnRVAVIKSQIETTTSEfdreklqERLAKLSGGVA----VIKVGAATETELKE 389
Cdd:TIGR02341 306 ADFEGVERLALVtggeIVSTFDHPELV--KLGSCDLIEEIMIGE-------DKLLKFSGVKLgeacTIVLRGATQQILDE 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 390 MKLRIEDALNATRAAVEEG-IVAGGGTALANVIPAVATL--ELTGDEATGRNIVLRALEEPVRQIAHNAGFEGSIVIDRL 466
Cdd:TIGR02341 377 AERSLHDALCVLSQTVKESrTVLGGGCSEMLMSKAVTQEaqRTPGKEALAVEAFARALRQLPTIIADNAGFDSAELVAQL 456
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 445953730 467 K----NAELGIGFNAATGEWVNMIDQGIIDPVKVSRSALQNAASVASLILTTEAVVANKPEP 524
Cdd:TIGR02341 457 RaahyNGNTTMGLDMNEGTIADMRQLGITESYKVKRAVVSSAAEAAEVILRVDNIIKAAPRK 518
|
|
| chap_CCT_epsi |
TIGR02343 |
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ... |
10-520 |
1.24e-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: 1.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 10 DARSAMVRGVDILADTVKVTLGPKGRNVVLEKSFGSPLITNDGVTIAKEIELEDHFenmgAKLVSEVASKTNDIAGDGTT 89
Cdd:TIGR02343 27 EAKKSNIAAAKSVASILRTSLGPKGMDKMLISPDGDITVTNDGATILSQMDVDNQI----AKLMVELSKSQDDEIGDGTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 90 TATVLTQAIVREGIKNVTAGANPIGIRRGIETAVAAAVEALKNNA----IPVANKEAIAQvAAVSSRSEKVGEYISEAME 165
Cdd:TIGR02343 103 GVVVLAGALLEQAEELLDKGIHPIKIADGFEEAARIAVEHLEEISdeisADNNNREPLIQ-AAKTSLGSKIVSKCHRRFA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 166 KVGKDGVITIE--ESRGMETELEVVE---GMQFDRGYLSQYMVTDSE----KMVADLENPYILI-----------TDKK- 224
Cdd:TIGR02343 182 EIAVDAVLNVAdmERRDVDFDLIKVEgkvGGSLEDTKLIKGIIIDKDfshpQMPKEVEDAKIAIltcpfeppkpkTKHKl 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 225 -ISNIQEILPL-----------LESILQSNRPLLIIADDVDGEALPTLVLNkirgtfNVVAVKAPGFGDrrkamLEDIAI 292
Cdd:TIGR02343 262 dISSVEEYKKLqkyeqqkfkemIDDIKKSGANLVICQWGFDDEANHLLLQN------DLPAVRWVGGQE-----LELIAI 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 293 LTGGTVITedlglELKDATIEALGQAARVT-----VDKDSTVIVEGAGNPEAISnrvaviksqietttsefdreklqerl 367
Cdd:TIGR02343 331 ATGGRIVP-----RFQELSKDKLGKAGLVReisfgTTKDRMLVIEQCKNSKAVT-------------------------- 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 368 aklsggvavIKVGAATETELKEMKLRIEDALNATRAAVEEG-IVAGGGTALANVIPAV--ATLELTGDEATGRNIVLRAL 444
Cdd:TIGR02343 380 ---------IFIRGGNKMIIEEAKRSIHDALCVVRNLIKDSrIVYGGGAAEISCSLAVsqEADKYPGVEQYAIRAFADAL 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 445 EEPVRQIAHNAGFEGSIVIDRLK-------NAELGIGFNaatGEWVN-MIDQGIIDPVKVSRSALQNAASVASLILTTEA 516
Cdd:TIGR02343 451 ETIPMALAENSGLDPIGTLSTLKslqlkekNPNLGVDCL---GYGTNdMKEQFVFETLIGKKQQILLATQLVRMILKIDD 527
|
....
gi 445953730 517 VVAN 520
Cdd:TIGR02343 528 VISP 531
|
|
| TCP1_delta |
cd03338 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ... |
22-512 |
5.95e-14 |
|
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: 74.25 E-value: 5.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 22 LADTVKVTLGPKGRNVVLEKSFGSPLITNDGVTIAKEIELeDHfenMGAKLVSEVaSKTNDI-AGDGTTTATVLTQAIVR 100
Cdd:cd03338 20 VADAIRTSLGPRGMDKMIQTGKGEVIITNDGATILKQMSV-LH---PAAKMLVEL-SKAQDIeAGDGTTSVVVLAGALLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 101 EGIKNVTAGANPIGIRRGIETAVAAAVEALKNNAIPV--ANKEAIAQVAAVSSRSEKVGEYiSEAMEKVGKDGVITIEES 178
Cdd:cd03338 95 ACESLLKKGIHPTVISESFQIAAKKAVEILDSMSIPVdlNDRESLIKSATTSLNSKVVSQY-SSLLAPIAVDAVLKVIDP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 179 R-----------------GMETELEVVEGMQFD-RGYLSQYMVTDSEKMV------------ADLENPyILITD----KK 224
Cdd:cd03338 174 AtatnvdlkdirivkklgGTIEDTELVDGLVFTqKASKKAGGPTRIEKAKigliqfclsppkTDMDNN-IVVNDyaqmDR 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 225 IsnIQE----ILPLLESILQSNRPLLIIADDVDGEALPTL---VLNKIrgtfNVVAVKAPgfgDRrkamlEDIAILTGGT 297
Cdd:cd03338 253 I--LREerkyILNMCKKIKKSGCNVLLIQKSILRDAVSDLalhFLAKL----KIMVVKDI---ER-----EEIEFICKTI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 298 VITEDLGLELKDAtiEALGQAARV-TVDKDSTVIVegagnpeaisnRVAVIKSQIETTTsefdreklqerlaklsggvav 376
Cdd:cd03338 319 GCKPVASIDHFTE--DKLGSADLVeEVSLGDGKIV-----------KITGVKNPGKTVT--------------------- 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 377 IKVGAATETELKEMKLRIEDALNATRAAVEE-GIVAGGGTA---LANVIPAVATlELTGDEAtgrnIVLRALEEPVRQI- 451
Cdd:cd03338 365 ILVRGSNKLVLDEAERSLHDALCVIRCLVKKrALIPGGGAPeieIALQLSEWAR-TLTGVEQ----YCVRAFADALEVIp 439
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 445953730 452 ---AHNAGFEG-SIVID---RLKNAELGIGFNAATGEWVNMIDQGIIDPVKVSRSALQNAASVASLIL 512
Cdd:cd03338 440 ytlAENAGLNPiSIVTElrnRHAQGEKNAGINVRKGAITNILEENVVQPLLVSTSAITLATETVRMIL 507
|
|
| chap_CCT_eta |
TIGR02345 |
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ... |
16-521 |
8.94e-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: 70.56 E-value: 8.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 16 VRGVDILADTVKVTLGPKGRNVVLEKSFGSPLITNDGVTIAKEIELedhfENMGAKLVSEVASKTNDIAGDGTTTATVLT 95
Cdd:TIGR02345 24 INACVAIAEALKTTLGPRGMDKLIVGSNGKATISNDGATILKLLDI----VHPAAKTLVDIAKSQDAEVGDGTTSVTILA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 96 QAIVREGIKNVTAGANPIGIRRGIETAVAAAVEALKNNAIPVAN-----KEAIAQVAAVSSRSEKVGEYiSEAMEKVGKD 170
Cdd:TIGR02345 100 GELLKEAKPFIEEGVHPQLIIRCYREALSLAVEKIKEIAVTIDEekgeqRELLEKCAATALSSKLISHN-KEFFSKMIVD 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 171 GVITIEESR-------------GMETELEVVEGMQFDRgylsQYMVTDSEKMVADLENPYILITdkkisNIQeilplLEs 237
Cdd:TIGR02345 179 AVLSLDRDDldlkligikkvqgGALEDSQLVNGVAFKK----TFSYAGFEQQPKKFANPKILLL-----NVE-----LE- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 238 iLQSNRPLLII----ADD----VDGE-ALPTLVLNKIRGT-FNVVAVKAPgFGDRRKAMLEDIAILTGGTVITEDLGlel 307
Cdd:TIGR02345 244 -LKAEKDNAEIrvedVEDyqaiVDAEwAIIFRKLEKIVESgANVVLSKLP-IGDLATQYFADRDIFCAGRVSAEDLK--- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 308 kdATIEALGQAARVTVDKdstvivegagnpeaisnrvavIKSQIETTTSEFDREKL-QERLAKLSGG----VAVIKVGAA 382
Cdd:TIGR02345 319 --RVIKACGGSIQSTTSD---------------------LEADVLGTCALFEERQIgSERYNYFTGCphakTCTIILRGG 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 383 TETELKEMKLRIEDALNATRAAVEEGIVAGGGTALANVIPAV---ATLELTGDEATGRNIVLRALEEPVRQIAHNAGFEG 459
Cdd:TIGR02345 376 AEQFIEEAERSLHDAIMIVRRALKNKKIVAGGGAIEMELSKClrdYSKTIDGKQQLIINAFAKALEIIPRQLCENAGFDS 455
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 445953730 460 SIVIDRLKNAE------LGIGFNaaTGEWVNMIDQGIIDPVKVSRSALQNAASVASLILTTEAVVANK 521
Cdd:TIGR02345 456 IEILNKLRSRHakggkwYGVDIN--TEDIGDNFEAFVWEPALVKINALKAAFEAACTILSVDETITNP 521
|
|
| TCP1_zeta |
cd03342 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
22-512 |
1.22e-11 |
|
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: 66.90 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 22 LADTVKVTLGPKGRNVVLEKSFGSPLITNDGVTIAKEIeledHFENMGAKLVSEVASKTNDIAGDGTTTATVLTQAIVRE 101
Cdd:cd03342 24 LQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLSEM----QIQHPTASMIARAATAQDDITGDGTTSNVLLIGELLKQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 102 GIKNVTAGANPIGIRRGIETAVAAAVEALKNNAIPV---ANKEAIAQVAAVSSRSeKVGEYISEAMEKVGKDGVITIEES 178
Cdd:cd03342 100 AERYIQEGVHPRIITEGFELAKNKALKFLESFKVPVeidTDRELLLSVARTSLRT-KLHADLADQLTEIVVDAVLAIYKP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 179 ---------------RGMETELEVVEGMQFDRGylsqymvTDSEKMVADLENPYILITD----------------KKISN 227
Cdd:cd03342 179 depidlhmveimqmqHKSDSDTKLIRGLVLDHG-------ARHPDMPKRVENAYILTCNvsleyektevnsgffySVVIN 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 228 IQEILPLLESILQSNrplliiaddvdgealptlvlnkirgtfNVVAVkapgfgdrRKAM---LEDIAILTGGTVIT--ED 302
Cdd:cd03342 252 QKGIDPPSLDMLAKE---------------------------GILAL--------RRAKrrnMERLTLACGGVAMNsvDD 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 303 LglelkdaTIEALGQAARV---TVDKDSTVIVEGAGNPeaisnrvaviKSqietttsefdreklqerlaklsggvAVIKV 379
Cdd:cd03342 297 L-------SPECLGYAGLVyerTLGEEKYTFIEGVKNP----------KS-------------------------CTILI 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 380 GAATETELKEMKLRIEDALNATRAAVEEG-IVAGGGtalANVIPAVATLELTGDEATGRN-IVLRALEEPVRQI----AH 453
Cdd:cd03342 335 KGPNDHTITQIKDAIRDGLRAVKNAIEDKcVVPGAG---AFEVALYAHLKEFKKSVKGKAkLGVQAFADALLVIpktlAE 411
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 445953730 454 NAGFEGSIVIDRLKN----AELGIGFNAATGEWVNMIDQGIIDPVKVSRSALQNAASVASLIL 512
Cdd:cd03342 412 NSGLDVQETLVKLQDeyaeGGQVGGVDLDTGEPMDPESEGIWDNYSVKRQILHSATVIASQLL 474
|
|
| chap_CCT_delta |
TIGR02342 |
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ... |
10-521 |
1.84e-11 |
|
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: 66.35 E-value: 1.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 10 DARSAMVRGVDILADTVKVTLGPKGRNVVLEKSFGSPLITNDGVTIAKEIELedhfENMGAKLVSEVaSKTNDI-AGDGT 88
Cdd:TIGR02342 9 DVRTSNIVAAKAVADAIRTSLGPKGMDKMIQDGKGEVIITNDGATILKQMAV----LHPAAKMLVEL-SKAQDIeAGDGT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 89 TTATVLTQAIVREGIKNVTAGANPIGIRRGIETAVAAAVEALKNNAIPV--ANKEAIAQVAAVSSRSEKVGEYiSEAMEK 166
Cdd:TIGR02342 84 TSVVILAGALLGACERLLNKGIHPTIISESFQSAADEAIKILDEMSIPVdlSDREQLLKSATTSLSSKVVSQY-SSLLAP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 167 VGKDGVITIEESR-----------------GMETELEVVEGMQFDRGY----------------LSQYMVTDSEkmvADL 213
Cdd:TIGR02342 163 LAVDAVLKVIDPEnaknvdlndikvvkklgGTIDDTELIEGLVFTQKAsksaggptriekakigLIQFQISPPK---TDM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 214 ENPYILITDKKISNIQE-----ILPLLESILQSNRPLLIIADDVDGEALPTLVLNKIrGTFNVVAVKapgfgDRRKAMLE 288
Cdd:TIGR02342 240 ENQIIVNDYAQMDRVLKeerayILNIVKKIKKTGCNVLLIQKSILRDAVNDLALHFL-AKMKIMVVK-----DIEREEIE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 289 DIAILTGGTVITEDLGLelkdaTIEALGQAARVT-VDKDSTVIVegagnpeaisnRVAVIKSQIETTTsefdreklqerl 367
Cdd:TIGR02342 314 FICKTIGCKPIASIDHF-----TADKLGSAELVEeVDSDGGKII-----------KITGIQNAGKTVT------------ 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 368 aklsggvavIKVGAATETELKEMKLRIEDALNATRAAVEE-GIVAGGGTALANVIPAVATL--ELTGDEATGRNIVLRAL 444
Cdd:TIGR02342 366 ---------VVVRGSNKLVIDEAERSLHDALCVIRCLVKKrGLIAGGGAPEIEIARRLSKYarTMKGVESYCVRAFADAL 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 445 EEPVRQIAHNAGFEGSIVIDRLKNA----ELGIGFNAATGEWVNMIDQGIIDPVKVSRSALQNAASVASLILTTEAVVAN 520
Cdd:TIGR02342 437 EVIPYTLAENAGLNPIKVVTELRNRhangEKTAGISVRKGGITNMLEEHVLQPLLVTTSAITLASETVRSILKIDDIVFT 516
|
.
gi 445953730 521 K 521
Cdd:TIGR02342 517 R 517
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
22-522 |
6.45e-11 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 64.66 E-value: 6.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 22 LADTVKVTLGPKGRNVVLEKS-----FGSPLITNDGVTIAKEIELEdhfeNMGAKLVSEVASKTNDIAGDGTTTATVLTQ 96
Cdd:PTZ00212 34 VADLVKTTLGPKGMDKILQPMsegprSGNVTVTNDGATILKSVWLD----NPAAKILVDISKTQDEEVGDGTTSVVVLAG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 97 AIVREGIKNVTAGANPIGIRRGIETAVAAAVEALKNNAIPV-ANKEAIAQ---VAAVSSRSEKVGEYISEAMEKVGKDGV 172
Cdd:PTZ00212 110 ELLREAEKLLDQKIHPQTIIEGWRMALDVARKALEEIAFDHgSDEEKFKEdllNIARTTLSSKLLTVEKDHFAKLAVDAV 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 173 ITIEESrgmeTELEVVEGMQFDRGYLSqymvtDSEkmvadLENPYILitDKKISNIQEILPLLESILQSNRPLliiadDV 252
Cdd:PTZ00212 190 LRLKGS----GNLDYIQIIKKPGGTLR-----DSY-----LEDGFIL--EKKIGVGQPKRLENCKILVANTPM-----DT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 253 DGEalptlvlnKIRGT------FNVVAVKAPGFGDRRKAMLEDIAILTGGTVITEDLGLELKDATIealgqaarvtvdKD 326
Cdd:PTZ00212 249 DKI--------KIYGAkvkvdsMEKVAEIEAAEKEKMKNKVDKILAHGCNVFINRQLIYNYPEQLF------------AE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 327 STVIVEGAGNPEAISNRVAVIKSQIETTTSEFDREKL------------QERLAKLSG----GVAVIKVGAATETELKEM 390
Cdd:PTZ00212 309 AGIMAIEHADFDGMERLAAALGAEIVSTFDTPEKVKLghcdlieeimigEDKLIRFSGcakgEACTIVLRGASTHILDEA 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 391 KLRIEDALNATRAAVEEG-IVAGGGTalANVIPAVATLELTGDEATGRNIVLRALEEPVRQ----IAHNAGFEGSIVIDR 465
Cdd:PTZ00212 389 ERSLHDALCVLSQTVKDTrVVLGGGC--SEMLMANAVEELAKKVEGKKSLAIEAFAKALRQiptiIADNGGYDSAELVSK 466
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 445953730 466 LK------NAELGIGFNaaTGEWVNMIDQGIIDPVKVSRSALQNAASVASLILTTEAVVANKP 522
Cdd:PTZ00212 467 LRaehykgNKTAGIDME--KGTVGDMKELGITESYKVKLSQLCSATEAAEMILRVDDIIRCAP 527
|
|
| TCP1_eta |
cd03340 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ... |
3-521 |
1.46e-10 |
|
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.
Pssm-ID: 239456 [Multi-domain] Cd Length: 522 Bit Score: 63.46 E-value: 1.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 3 KEIKFSSDARSAMVRGVD---ILADTVKVTLGPKGRNVVLEKSFGSPLITNDGVTIAKEIELEdhfeNMGAKLVSEVASK 79
Cdd:cd03340 6 KEGTDTSQGKGQLISNINacqAIADAVRTTLGPRGMDKLIVDGRGKVTISNDGATILKLLDIV----HPAAKTLVDIAKS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 80 TNDIAGDGTTTATVLTQAIVREGIKNVTAGANPIGIRRGIETAVAAAVEALKNNAIPVANK------EAIAQVAA----- 148
Cdd:cd03340 82 QDAEVGDGTTSVVVLAGEFLKEAKPFIEDGVHPQIIIRGYRKALQLAIEKIKEIAVNIDKEdkeeqrELLEKCAAtalns 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 149 --VSSRSEKVGEYISEAMEKVGKD---GVITIEESRG---METELevVEGMQFDR-----GYLSQYMVTDSEKMV----- 210
Cdd:cd03340 162 klIASEKEFFAKMVVDAVLSLDDDldlDMIGIKKVPGgslEDSQL--VNGVAFKKtfsyaGFEQQPKKFKNPKILllnve 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 211 ----ADLENPYILITDkkISNIQEIlpllesilqsnrplliiaddVDGE-ALPTLVLNKIRGT-FNVVAVKAPgFGDRRK 284
Cdd:cd03340 240 lelkAEKDNAEVRVED--PEEYQAI--------------------VDAEwKIIYDKLEKIVKSgANVVLSKLP-IGDLAT 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 285 AMLEDIAILTGGTVITEDLGlelkdATIEALGQAARVTVDKdstvivegagnpeaisnrvavIKSQIETTTSEFDREKL- 363
Cdd:cd03340 297 QYFADRDIFCAGRVPEEDLK-----RVAQATGGSIQTTVSN---------------------ITDDVLGTCGLFEERQVg 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 364 QERLAKLSGG-----VAVIKVGAAtETELKEMKLRIEDALNATRAAVEEG-IVAGGGT---ALANVIPAVAtLELTGDEA 434
Cdd:cd03340 351 GERYNIFTGCpkaktCTIILRGGA-EQFIEEAERSLHDAIMIVRRAIKNDsVVAGGGAiemELSKYLRDYS-RTIAGKQQ 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 435 TGRNIVLRALEEPVRQIAHNAGFEGSIVIDRL-----KNAELGIGFNAATGEWVNMIDQGIIDPVKVSRSALQNAASVAS 509
Cdd:cd03340 429 LVINAFAKALEIIPRQLCDNAGFDATDILNKLrqkhaQGGGKWYGVDINNEGIADNFEAFVWEPSLVKINALTAATEAAC 508
|
570
....*....|..
gi 445953730 510 LILTTEAVVANK 521
Cdd:cd03340 509 LILSVDETIKNP 520
|
|
| TCP1_epsilon |
cd03339 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ... |
22-519 |
2.26e-10 |
|
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.
Pssm-ID: 239455 Cd Length: 526 Bit Score: 63.09 E-value: 2.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 22 LADTVKVTLGPKGRNVVLEKSFGSPLITNDGVTIAKEIELEDHFenmgAKLVSEVASKTNDIAGDGTTTATVLTQAIVRE 101
Cdd:cd03339 35 VANILRTSLGPRGMDKILVSPDGEVTVTNDGATILEKMDVDHQI----AKLLVELSKSQDDEIGDGTTGVVVLAGALLEQ 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 102 GIKNVTAGANPIGIRRGIETAVAAAVEALKNNAIPVA----NKEAIAQVAAVSSRSEKVGEYiSEAMEKVGKDGVITIE- 176
Cdd:cd03339 111 AEKLLDRGIHPIRIADGYEQACKIAVEHLEEIADKIEfspdNKEPLIQTAMTSLGSKIVSRC-HRQFAEIAVDAVLSVAd 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 177 -ESRGMETELEVVE---GMQFDRGYLSQYMVTDSE----KMVADLENPYILI-----------TDKK--ISNIQEILPL- 234
Cdd:cd03339 190 lERKDVNFELIKVEgkvGGRLEDTKLVKGIVIDKDfshpQMPKEVKDAKIAIltcpfeppkpkTKHKldITSVEDYKKLq 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 235 ----------LESILQSNRPLLIIADDVDGEALPTLVLNkirgtfNVVAVKAPGFGDrrkamLEDIAILTGGTVIT--ED 302
Cdd:cd03339 270 eyeqkyfremVEQVKDAGANLVICQWGFDDEANHLLLQN------GLPAVRWVGGVE-----IELIAIATGGRIVPrfED 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 303 LglelkdaTIEALGQAARV-----TVDKDSTVIVEGAGNpeaiSNRVAViksqietttseFDReklqerlaklsGGVAVI 377
Cdd:cd03339 339 L-------SPEKLGKAGLVreisfGTTKDKMLVIEGCPN----SKAVTI-----------FIR-----------GGNKMI 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 378 kvgaateteLKEMKLRIEDALNATRAAVEEG-IVAGGGT-------ALANVIPAVATLELTGDEATGrnivlRALEEPVR 449
Cdd:cd03339 386 ---------IEEAKRSLHDALCVVRNLIRDNrIVYGGGAaeiscslAVEKAADKCSGIEQYAMRAFA-----DALESIPL 451
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 445953730 450 QIAHNAGFEGSIVIDRLK-------NAELGIG-FNAATGewvNMIDQGIIDPVKVSRSALQNAASVASLILTTEAVVA 519
Cdd:cd03339 452 ALAENSGLNPIETLSEVKarqvkekNPHLGIDcLGRGTN---DMKEQKVFETLISKKQQILLATQVVKMILKIDDVIV 526
|
|
| chap_CCT_zeta |
TIGR02347 |
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ... |
22-518 |
1.91e-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: 60.13 E-value: 1.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 22 LADTVKVTLGPKGRNVVLEKSFGSPLITNDGVTIAKEIeledHFENMGAKLVSEVASKTNDIAGDGTTTATVLTQAIVRE 101
Cdd:TIGR02347 28 LQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEM----QIQHPTASMIARAATAQDDITGDGTTSTVLLIGELLKQ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 102 GIKNVTAGANPIGIRRGIETAVAAAVEAL---KNNAIPVANKEAIAQVAAVSSRS-------EKVGEYISEAMEKVGKDG 171
Cdd:TIGR02347 104 AERYILEGVHPRIITEGFEIARKEALQFLdkfKVKKEDEVDREFLLNVARTSLRTklpadlaDQLTEIVVDAVLAIKKDG 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 172 -------VITIEESRGMETELEVVEGMQFDRGylsqymvTDSEKMVADLENPYILI------------------------ 220
Cdd:TIGR02347 184 edidlfmVEIMEMKHKSATDTTLIRGLVLDHG-------ARHPDMPRRVKNAYILTcnvsleyektevnsgffyssaeqr 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 221 ----------TDKKISNIQEilplLESILQSNRP---LLIIadDVDGEALPTL-VLNKIrgtfNVVAVKAPgfgdRRKAM 286
Cdd:TIGR02347 257 eklvkaerkfVDDRVKKIIE----LKKKVCGKSPdkgFVVI--NQKGIDPPSLdLLAKE----GIMALRRA----KRRNM 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 287 lEDIAILTGGTVITedlglELKDATIEALGQAARV---TVDKDSTVIVEGAGNPEAISnrvaviksqietttsefdrekl 363
Cdd:TIGR02347 323 -ERLTLACGGEALN-----SVEDLTPECLGWAGLVyetTIGEEKYTFIEECKNPKSCT---------------------- 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 364 qerlaklsggvavIKVGAATETELKEMKLRIEDALNATRAAVEEG-IVAGGGtalANVIPAVATLE-----LTGDEATGR 437
Cdd:TIGR02347 375 -------------ILIKGPNDHTIAQIKDAVRDGLRAVKNAIEDKcVVPGAG---AFEIAAYRHLKeykksVKGKAKLGV 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 438 NIVLRALEEPVRQIAHNAGFEGS----IVIDRLKNAELGIGFNAATGEWVNMIDQGIIDPVKVSRSALQNAASVASLILT 513
Cdd:TIGR02347 439 EAFANALLVIPKTLAENSGFDAQdtlvKLEDEHDEGGEVVGVDLNTGEPIDPEIKGIWDNYRVKKQLIQSATVIASQLLL 518
|
....*
gi 445953730 514 TEAVV 518
Cdd:TIGR02347 519 VDEVM 523
|
|
| chap_CCT_alpha |
TIGR02340 |
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ... |
10-524 |
2.77e-08 |
|
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT alpha chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.
Pssm-ID: 274081 [Multi-domain] Cd Length: 536 Bit Score: 56.27 E-value: 2.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 10 DARSAMVRGVDILADTVKVTLGPKGRNVVLEKSFGSPLITNDGVTIAKEIELEDHfenmGAKLVSEVASKTNDIAGDGTT 89
Cdd:TIGR02340 12 DVRTQNVTAAMAIANIVKTSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHP----AAKILVELAQLQDREVGDGTT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 90 TATVLTQAIVREGIKNVTAGANPIGIRRGIETAVAAAVEALKNN-AIPVAN--KEAIAQVAAVSSRSEKVG---EYIS-- 161
Cdd:TIGR02340 88 SVVIIAAELLKRADELVKNKIHPTSVISGYRLACKEAVKYIKENlSVSVDElgREALINVAKTSMSSKIIGldsDFFSni 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 162 -----EAMEKVGKDGV-------ITIEESRGMET-ELEVVEGMQFDRGYLSQYMVTDSEKM-VADLE---NPY------- 217
Cdd:TIGR02340 168 vvdavLAVKTTNENGEtkypikaINILKAHGKSArESMLVKGYALNCTVASQQMPKRIKNAkIACLDfnlQKAkmalgvq 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 218 ILITD-KKISNIQE-----ILPLLESILQSNRPLLIIADDVDGEALPTLVLNKIRGTFNVvavkapgfgdrRKAMLEDIA 291
Cdd:TIGR02340 248 IVVDDpEKLEQIRQreadiTKERIKKILDAGANVVLTTGGIDDMCLKYFVEAGAMGVRRC-----------KKEDLKRIA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 292 ILTGGTVITEDLGLElKDATIEA--LGQAARvtvdkdstVIVEGAGNPEAIsnrvaVIKSqietttsefdreklqerlAK 369
Cdd:TIGR02340 317 KATGATLVSTLADLE-GEETFEAsyLGFADE--------VVQERIADDECI-----LIKG------------------TK 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 370 LSGGVAVIKVGaATETELKEMKLRIEDALNATRAAVEEG-IVAGGG---TALANVIPAVATlELTGDEATGRNIVLRALE 445
Cdd:TIGR02340 365 KRKSASIILRG-ANDFMLDEMERSLHDALCVVKRTLESNsVVPGGGaveAALSIYLENFAT-TLGSREQLAIAEFARALL 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 446 EPVRQIAHNAGFEGSIVIDRLK--------NAELG----IGFNAATGEWVNMIDQGIIDPVKVSRSALQNAASVASLILT 513
Cdd:TIGR02340 443 IIPKTLAVNAAKDSTELVAKLRayhaaaqlKPEKKhlkwYGLDLVNGKIRDNKEAGVLEPTVSKVKSLKFATEAAITILR 522
|
570
....*....|.
gi 445953730 514 TEAVVANKPEP 524
Cdd:TIGR02340 523 IDDLIKLNPEQ 533
|
|
| chap_CCT_gamma |
TIGR02344 |
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ... |
22-519 |
1.75e-07 |
|
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: 53.97 E-value: 1.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 22 LADTVKVTLGPKGRNVVLEKSFGSPLITNDGVTIAKEIELedhfENMGAKLVSEVASKTNDIAGDGTTTATVLTQAIVRE 101
Cdd:TIGR02344 28 VADIIRTCLGPRSMLKMLLDPMGGIVMTNDGNAILREIDV----AHPAAKSMIELSRTQDEEVGDGTTSVIILAGEMLSV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 102 GIKNVTAGANPIGIRRGIETAVAAAVEALKNNAIP--VANKEAIAQVAAVSSRSEKVGEYiSEAMEKVGKDGVITIEESR 179
Cdd:TIGR02344 104 AEPFLEQNIHPTVIIRAYRKALDDALSVLEEISIPvdVNDDAAMLKLIQSCIGTKFVSRW-SDLMCDLALDAVRTVQRDE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 180 GMETELEV-----VE----GMQFDRGYLSQYM----VTDSeKMVADLENPYILITD-----KKISNIQEILPLLESilQS 241
Cdd:TIGR02344 183 NGRKEIDIkryakVEkipgGDIEDSCVLKGVMinkdVTHP-KMRRYIENPRIVLLDcpleyKKGESQTNIEITKEE--DW 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 242 NRPLLIIADDVdgealptlvlnkirgtfnvvavkapgfgdrrKAMLEDIAILTGGTVITE----DLGLE-LKDATIEALg 316
Cdd:TIGR02344 260 NRILQMEEEYV-------------------------------QLMCEDIIAVKPDLVITEkgvsDLAQHyLLKANITAI- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 317 qaaRVTVDKDSTVIVEGAGnpEAISNRVAVIK-SQIETTTSEFDREKLQERL------AKLSGGVAVIKVGAATETeLKE 389
Cdd:TIGR02344 308 ---RRVRKTDNNRIARACG--ATIVNRPEELReSDVGTGCGLFEVKKIGDEYftfiteCKDPKACTILLRGASKDI-LNE 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 390 MKLRIEDALNATRAAVEEG-IVAGGG-TALA-NVIPAVATLELTGDEATGRNIVLRALEEPVRQIAHNAGFEgsiVID-- 464
Cdd:TIGR02344 382 VERNLQDAMAVARNVLLDPkLVPGGGaTEMAvSVALTEKSKKLEGVEQWPYRAVADALEIIPRTLAQNCGAN---VIRtl 458
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 445953730 465 ---RLKNAELG---IGFNAATGEWVNMIDQGIIDPVKVSRSALQNAASVASLILTTEAVVA 519
Cdd:TIGR02344 459 telRAKHAQENnctWGIDGETGKIVDMKEKGIWEPLAVKLQTYKTAIESACLLLRIDDIVS 519
|
|
| TCP1_alpha |
cd03335 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ... |
10-118 |
6.28e-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: 6.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 10 DARSAMVRGVDILADTVKVTLGPKGRNVVLEKSFGSPLITNDGVTIAKEIELEDHfenmGAKLVSEVASKTNDIAGDGTT 89
Cdd:cd03335 8 DVRTQNVTAAMAIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHP----AAKILVELAQLQDKEVGDGTT 83
|
90 100
....*....|....*....|....*....
gi 445953730 90 TATVLTQAIVREGIKNVTAGANPIGIRRG 118
Cdd:cd03335 84 SVVIIAAELLKRANELVKQKIHPTTIISG 112
|
|
| chap_CCT_theta |
TIGR02346 |
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ... |
22-533 |
1.97e-06 |
|
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: 50.48 E-value: 1.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 22 LADTVKVTLGPKGRNVVLEKSFGSPLITNDGVTIAKEIELedhfENMGAKLVSEVASKTNDIAGDGTTTATVLTQAIVRE 101
Cdd:TIGR02346 30 LSQITRTSLGPNGMNKMVINHLEKLFVTNDAATILRELEV----QHPAAKLLVMASEMQENEIGDGTNLVLVLAGELLNK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 102 GIKNVTAGANPIGIRRGIETAVAAAVEALKN----NAIPVANKEAIAQV--AAVSSR--------SEKVGEYISEAM-EK 166
Cdd:TIGR02346 106 AEELIRMGLHPSEIIKGYEMALKKAMEILEElvvwEVKDLRDKDELIKAlkASISSKqygnedflAQLVAQACSTVLpKN 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 167 VGKDGVITIEESRGMETEL---EVVEGMQFDRGylSQYMVTDSEKM-VADLENPY-ILITDKK----ISNIQEIL----- 232
Cdd:TIGR02346 186 PQNFNVDNIRVCKILGGSLsnsEVLKGMVFNRE--AEGSVKSVKNAkVAVFSCPLdTATTETKgtvlIHNAEELLnyskg 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 233 --PLLESILQSnrplliIADD-----VDGEALPTLVLNKIRgTFNVVAVKAPGfgdrrKAMLEDIAILTGGTVItedlgL 305
Cdd:TIGR02346 264 eeNQIEAMIKA------IADSgvnviVTGGSVGDMALHYLN-KYNIMVLKIPS-----KFELRRLCKTVGATPL-----P 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 306 ELKDATIEALGQAARVTVDkdstvivegagnpEAISNRVAVIKSQietttsefdreklqerlaKLSGGVAVIKVGAATET 385
Cdd:TIGR02346 327 RLGAPTPEEIGYVDSVYVS-------------EIGGDKVTVFKQE------------------NGDSKISTIILRGSTDN 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 386 ELKEMKLRIEDALNATRAAVEEG-IVAGGGTALANVIPAVATL--ELTGDEATGRNIVLRALEEPVRQIAHNAGFEGSIV 462
Cdd:TIGR02346 376 LLDDIERAIDDGVNTVKALVKDGrLLPGAGATEIELASRLTKYgeKLPGLDQYAIKKFAEAFEIIPRTLAENAGLNANEV 455
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 445953730 463 IDRLKNAE------LGIGFNAATGEWVNMIDQGIIDPVKVSRSALQNAASVASLILTTEAVVANKPepvAPAPAMDP 533
Cdd:TIGR02346 456 IPKLYAAHkkgnksKGIDIEAESDGVKDASEAGIYDMLATKKWAIKLATEAAVTVLRVDQIIMAKP---AGGPKPPQ 529
|
|
| TCP1_gamma |
cd03337 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ... |
22-232 |
1.40e-05 |
|
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: 47.68 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 22 LADTVKVTLGPKGRNVVLEKSFGSPLITNDGVTIAKEIELEdhfeNMGAKLVSEVASKTNDIAGDGTTTATVLTQAIVRE 101
Cdd:cd03337 28 VADVIRTCLGPRAMLKMLLDPMGGIVLTNDGNAILREIDVA----HPAAKSMIELSRTQDEEVGDGTTSVIILAGEILAV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 102 GIKNVTAGANPIGIRRGIETAVAAAVEALKNNAIPVaNKEAIAQVAAV--SSRSEKVGEYISEAMEKVGKDGVITIEESR 179
Cdd:cd03337 104 AEPFLERGIHPTVIIKAYRKALEDALKILEEISIPV-DVNDRAQMLKIikSCIGTKFVSRWSDLMCNLALDAVKTVAVEE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 180 GMETE---------LEVVEGmqfdrGYLSQYMVTDS---------EKMVADLENP----------YILITDKKISNI-QE 230
Cdd:cd03337 183 NGRKKeidikryakVEKIPG-----GEIEDSRVLDGvmlnkdvthPKMRRRIENPrivlldcpleYLVITEKGVSDLaQH 257
|
..
gi 445953730 231 IL 232
Cdd:cd03337 258 YL 259
|
|
| TCP1_theta |
cd03341 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ... |
22-521 |
1.21e-04 |
|
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.
Pssm-ID: 239457 [Multi-domain] Cd Length: 472 Bit Score: 44.52 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 22 LADTVKVTLGPKGRN--VV--LEKSFgsplITNDGVTIAKEIEledhFENMGAKLVSEvASKTNDI-AGDGTTTATVLTQ 96
Cdd:cd03341 20 LSQITRTSYGPNGMNkmVInhLEKLF----VTSDAATILRELE----VQHPAAKLLVM-ASQMQEEeIGDGTNLVVVLAG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 97 AIVREGIKNVTAGANPIGIRRGIETAVAAAVEALKNNAI----PVANKEAIAQV--AAVSSR--------SEKVGEYISE 162
Cdd:cd03341 91 ELLEKAEELLRMGLHPSEIIEGYEKALKKALEILEELVVykieDLRNKEEVSKAlkTAIASKqygnedflSPLVAEACIS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 163 AMEKvgKDGVITIEESR------GMETELEVVEGMQFDRgylsqymvtDSEKMVADLENPYILI----TDKKISNIqeil 232
Cdd:cd03341 171 VLPE--NIGNFNVDNIRvvkilgGSLEDSKVVRGMVFKR---------EPEGSVKRVKKAKVAVfscpFDIGVNVI---- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 233 pllesILQSNrplliiaddVDGEALPtlVLNKirgtFNVVAVKAPG-FGDRRkamledIAILTGGTVITedlglELKDAT 311
Cdd:cd03341 236 -----VAGGS---------VGDLALH--YCNK----YGIMVIKINSkFELRR------LCRTVGATPLP-----RLGAPT 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 312 IEALGQAARVTVdkdstvivegagnpEAISNRVAVIKSQIETTTSefdreklqerlaklsggVAVIKVGAATETELKEMK 391
Cdd:cd03341 285 PEEIGYCDSVYV--------------EEIGDTKVVVFRQNKEDSK-----------------IATIVLRGATQNILDDVE 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445953730 392 LRIEDALNATRAAVEEG-IVAGGGtalANVIPAVATLELTGDEATGRN--IVLR---ALEEPVRQIAHNAGFEGSIVIDR 465
Cdd:cd03341 334 RAIDDGVNVFKSLTKDGrFVPGAG---ATEIELAKKLKEYGEKTPGLEqyAIKKfaeAFEVVPRTLAENAGLDATEVLSE 410
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 445953730 466 L------KNAELGIGFNAATGEWVNMIDQGIIDPVKVSRSALQNAASVASLILTTEAVVANK 521
Cdd:cd03341 411 LyaahqkGNKSAGVDIESGDEGTKDAKEAGIFDHLATKKWAIKLATEAAVTVLRVDQIIMAK 472
|
|
| |
