|
Name |
Accession |
Description |
Interval |
E-value |
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
1-534 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 972.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 1 MAKELKFAEDARRAMLRGVDKLADTVKTTIGPKGRNVVLEQSYGSPTITNDGVTIAKNIELEDHFENMGAKLVSEVASKT 80
Cdd:PRK00013 1 MAKDIKFGEDARRKLLRGVNKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDPFENMGAQLVKEVASKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 81 NDIAGDGTTTATVLTQAIVNEGMKNVTAGANPVGIRRGIEKATAAAVAELKTMSHDVKTKDDIAQIASISAAN-PEVGQL 159
Cdd:PRK00013 81 NDVAGDGTTTATVLAQAIVREGLKNVAAGANPMDLKRGIDKAVEAAVEELKKISKPVEDKEEIAQVATISANGdEEIGKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 160 IADAMEKVGNDGVITIEDSRGVDTSVDVVEGMSFDRGYMSQYMVTDNDKMEANLDNPYVLITDKKIANIQDILPLLQSVV 239
Cdd:PRK00013 161 IAEAMEKVGKEGVITVEESKGFETELEVVEGMQFDRGYLSPYFVTDPEKMEAELENPYILITDKKISNIQDLLPVLEQVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 240 QEGRALLIIADDITGEALPTLVLNKIRGTFNVVAVKAPGFGDRRKAQLEDIAVLTGGTVISDDLGMQLKDATIDQLGSAN 319
Cdd:PRK00013 241 QSGKPLLIIAEDVEGEALATLVVNKLRGTLKVVAVKAPGFGDRRKAMLEDIAILTGGTVISEELGLKLEDATLEDLGQAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 320 KVTVTKDNTTIVDGAGDKAAIADRVEQIKKAIAETSSDFDKEKLQERLAKLAGGVAVVKVGAATETELKERKYRIEDALN 399
Cdd:PRK00013 321 KVVVTKDNTTIVDGAGDKEAIKARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATEVEMKEKKDRVEDALH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 400 ATRAAVQEGFVPGGGTALVNVIPALEKVEAEtTGDEQTGVKIVKAALEAPVRQIAENAGVEGSVIINQLKNEQP-GIGYN 478
Cdd:PRK00013 401 ATRAAVEEGIVPGGGVALLRAAPALEALKGL-NGDEATGINIVLRALEAPLRQIAENAGLEGSVVVEKVKNGKGkGYGYN 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 518035950 479 AAEDKFEDMVAAGIVDPTKVTRSALQNAASVSALLLTTEAVVADKPEPKDAAPMNP 534
Cdd:PRK00013 480 AATGEYVDMIEAGIIDPTKVTRSALQNAASVAGLLLTTEAVVADKPEKKAAAPPMG 535
|
|
| GroEL |
cd03344 |
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ... |
3-522 |
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: 877.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 3 KELKFAEDARRAMLRGVDKLADTVKTTIGPKGRNVVLEQSYGSPTITNDGVTIAKNIELEDHFENMGAKLVSEVASKTND 82
Cdd:cd03344 1 KDIKFGEEARKALLRGVNKLADAVKVTLGPKGRNVVIEKSFGSPKITKDGVTVAKEIELEDPFENMGAQLVKEVASKTND 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 83 IAGDGTTTATVLTQAIVNEGMKNVTAGANPVGIRRGIEKATAAAVAELKTMSHDVKTKDDIAQIASISAAN-PEVGQLIA 161
Cdd:cd03344 81 VAGDGTTTATVLARAIIKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKPVKTKEEIAQVATISANGdEEIGELIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 162 DAMEKVGNDGVITIEDSRGVDTSVDVVEGMSFDRGYMSQYMVTDNDKMEANLDNPYVLITDKKIANIQDILPLLQSVVQE 241
Cdd:cd03344 161 EAMEKVGKDGVITVEEGKTLETELEVVEGMQFDRGYLSPYFVTDPEKMEVELENPYILLTDKKISSIQELLPILELVAKA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 242 GRALLIIADDITGEALPTLVLNKIRGTFNVVAVKAPGFGDRRKAQLEDIAVLTGGTVISDDLGMQLKDATIDQLGSANKV 321
Cdd:cd03344 241 GRPLLIIAEDVEGEALATLVVNKLRGGLKVCAVKAPGFGDRRKAMLEDIAILTGGTVISEELGLKLEDVTLEDLGRAKKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 322 TVTKDNTTIVDGAGDKAAIADRVEQIKKAIAETSSDFDKEKLQERLAKLAGGVAVVKVGAATETELKERKYRIEDALNAT 401
Cdd:cd03344 321 VVTKDDTTIIGGAGDKAAIKARIAQIRKQIEETTSDYDKEKLQERLAKLSGGVAVIKVGGATEVELKEKKDRVEDALNAT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 402 RAAVQEGFVPGGGTALVNVIPALEKVEAEtTGDEQTGVKIVKAALEAPVRQIAENAGVEGSVIINQLKNEQPGIGYNAAE 481
Cdd:cd03344 401 RAAVEEGIVPGGGVALLRASPALDKLKAL-NGDEKLGIEIVRRALEAPLRQIAENAGVDGSVVVEKVLESPDGFGYDAAT 479
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 518035950 482 DKFEDMVAAGIVDPTKVTRSALQNAASVSALLLTTEAVVAD 522
Cdd:cd03344 480 GEYVDMIEAGIIDPTKVVRSALQNAASVASLLLTTEALVVD 520
|
|
| groEL |
PRK12849 |
chaperonin GroEL; Reviewed |
1-531 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237230 Cd Length: 542 Bit Score: 854.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 1 MAKELKFAEDARRAMLRGVDKLADTVKTTIGPKGRNVVLEQSYGSPTITNDGVTIAKNIELEDHFENMGAKLVSEVASKT 80
Cdd:PRK12849 1 MAKIIKFDEEARRALERGVNKLADAVKVTLGPKGRNVVIDKSFGAPTITKDGVSIAKEIELEDPFENLGAQLVKEVASKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 81 NDIAGDGTTTATVLTQAIVNEGMKNVTAGANPVGIRRGIEKATAAAVAELKTMSHDVKTKDDIAQIASISAAN-PEVGQL 159
Cdd:PRK12849 81 NDVAGDGTTTATVLAQALVQEGLKNVAAGANPMDLKRGIDKAVEAVVEELKALARPVSGSEEIAQVATISANGdEEIGEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 160 IADAMEKVGNDGVITIEDSRGVDTSVDVVEGMSFDRGYMSQYMVTDNDKMEANLDNPYVLITDKKIANIQDILPLLQSVV 239
Cdd:PRK12849 161 IAEAMEKVGKDGVITVEESKTLETELEVTEGMQFDRGYLSPYFVTDPERMEAVLEDPLILLTDKKISSLQDLLPLLEKVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 240 QEGRALLIIADDITGEALPTLVLNKIRGTFNVVAVKAPGFGDRRKAQLEDIAVLTGGTVISDDLGMQLKDATIDQLGSAN 319
Cdd:PRK12849 241 QSGKPLLIIAEDVEGEALATLVVNKLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGLKLEEVTLDDLGRAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 320 KVTVTKDNTTIVDGAGDKAAIADRVEQIKKAIAETSSDFDKEKLQERLAKLAGGVAVVKVGAATETELKERKYRIEDALN 399
Cdd:PRK12849 321 RVTITKDNTTIVDGAGDKEAIEARVAQIRRQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATEVELKERKDRVEDALN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 400 ATRAAVQEGFVPGGGTALVNVIPALEKVeAETTGDEQTGVKIVKAALEAPVRQIAENAGVEGSVIINQLKNEQPGIGYNA 479
Cdd:PRK12849 401 ATRAAVEEGIVPGGGVALLRAAKALDEL-AGLNGDQAAGVEIVRRALEAPLRQIAENAGLDGSVVVAKVLELEDGFGFNA 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 518035950 480 AEDKFEDMVAAGIVDPTKVTRSALQNAASVSALLLTTEAVVADKPEPKDAAP 531
Cdd:PRK12849 480 ATGEYGDLIAAGIIDPVKVTRSALQNAASVAGLLLTTEALVADKPEEEDPPG 531
|
|
| GroEL |
TIGR02348 |
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ... |
2-525 |
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: 845.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 2 AKELKFAEDARRAMLRGVDKLADTVKTTIGPKGRNVVLEQSYGSPTITNDGVTIAKNIELEDHFENMGAKLVSEVASKTN 81
Cdd:TIGR02348 1 AKQIKFDEEARKALLRGVDKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDKFENMGAQLVKEVASKTN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 82 DIAGDGTTTATVLTQAIVNEGMKNVTAGANPVGIRRGIEKATAAAVAELKTMSHDVKTKDDIAQIASISAAN-PEVGQLI 160
Cdd:TIGR02348 81 DVAGDGTTTATVLAQAIVKEGLKNVAAGANPIELKRGIEKAVEAVVEELKKLSKPVKGKKEIAQVATISANNdEEIGSLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 161 ADAMEKVGNDGVITIEDSRGVDTSVDVVEGMSFDRGYMSQYMVTDNDKMEANLDNPYVLITDKKIANIQDILPLLQSVVQ 240
Cdd:TIGR02348 161 AEAMEKVGKDGVITVEESKSLETELEVVEGMQFDRGYISPYFVTDAEKMEVELENPYILITDKKISNIKDLLPLLEKVAQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 241 EGRALLIIADDITGEALPTLVLNKIRGTFNVVAVKAPGFGDRRKAQLEDIAVLTGGTVISDDLGMQLKDATIDQLGSANK 320
Cdd:TIGR02348 241 SGKPLLIIAEDVEGEALATLVVNKLRGTLNVCAVKAPGFGDRRKAMLEDIAILTGGQVISEELGLKLEEVTLDDLGKAKK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 321 VTVTKDNTTIVDGAGDKAAIADRVEQIKKAIAETSSDFDKEKLQERLAKLAGGVAVVKVGAATETELKERKYRIEDALNA 400
Cdd:TIGR02348 321 VTVDKDNTTIVEGAGDKAAIKARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATETEMKEKKLRIEDALNA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 401 TRAAVQEGFVPGGGTALVNVIPALEKVEaETTGDEQTGVKIVKAALEAPVRQIAENAGVEGSVIINQLKNEQPGIGYNAA 480
Cdd:TIGR02348 401 TRAAVEEGIVPGGGVALLRAAAALEGLK-GDGEDEAIGIDIVKRALEAPLRQIAENAGLDGAVVAEKVKELKGNFGFNAA 479
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 518035950 481 EDKFEDMVAAGIVDPTKVTRSALQNAASVSALLLTTEAVVADKPE 525
Cdd:TIGR02348 480 TGEYEDLVEAGIIDPTKVTRSALQNAASIAGLLLTTEAVVADKPE 524
|
|
| groEL |
PRK12850 |
chaperonin GroEL; Reviewed |
1-534 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237231 Cd Length: 544 Bit Score: 775.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 1 MAKELKFAEDARRAMLRGVDKLADTVKTTIGPKGRNVVLEQSYGSPTITNDGVTIAKNIELEDHFENMGAKLVSEVASKT 80
Cdd:PRK12850 2 AAKEIRFSTDARDRLLRGVNILANAVKVTLGPKGRNVVLEKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVKEVASKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 81 NDIAGDGTTTATVLTQAIVNEGMKNVTAGANPVGIRRGIEKATAAAVAELKTMSHDVKTKDDIAQIASISAANPE-VGQL 159
Cdd:PRK12850 82 NDLAGDGTTTATVLAQAIVREGAKLVAAGMNPMDLKRGIDLAVAAVVDELKKIAKKVTSSKEIAQVATISANGDEsIGEM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 160 IADAMEKVGNDGVITIEDSRGVDTSVDVVEGMSFDRGYMSQYMVTDNDKMEANLDNPYVLITDKKIANIQDILPLLQSVV 239
Cdd:PRK12850 162 IAEAMDKVGKEGVITVEEAKTLGTELDVVEGMQFDRGYLSPYFVTNPEKMRAELEDPYILLHEKKISNLQDLLPILEAVV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 240 QEGRALLIIADDITGEALPTLVLNKIRGTFNVVAVKAPGFGDRRKAQLEDIAVLTGGTVISDDLGMQLKDATIDQLGSAN 319
Cdd:PRK12850 242 QSGRPLLIIAEDVEGEALATLVVNKLRGGLKSVAVKAPGFGDRRKAMLEDIAVLTGGQVISEDLGIKLENVTLDMLGRAK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 320 KVTVTKDNTTIVDGAGDKAAIADRVEQIKKAIAETSSDFDKEKLQERLAKLAGGVAVVKVGAATETELKERKYRIEDALN 399
Cdd:PRK12850 322 RVLITKENTTIIDGAGDKKNIEARVKQIRAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKEKKDRVDDALH 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 400 ATRAAVQEGFVPGGGTALVNVIPALEKVEAEtTGDEQTGVKIVKAALEAPVRQIAENAGVEGSVIINQLKNEQPGIGYNA 479
Cdd:PRK12850 402 ATRAAVEEGIVPGGGVALLRARSALRGLKGA-NADETAGIDIVRRALEEPLRQIATNAGFEGSVVVGKVAELPGNFGFNA 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 518035950 480 AEDKFEDMVAAGIVDPTKVTRSALQNAASVSALLLTTEAVVADKPEPKDAAPMNP 534
Cdd:PRK12850 481 QTGEYGDMVEAGIIDPAKVTRTALQDAASIAALLITTEAMVAEAPKKAAAAAAGP 535
|
|
| GroEL |
COG0459 |
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ... |
1-530 |
0e+00 |
|
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227 Cd Length: 497 Bit Score: 775.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 1 MAKELKFAEDARRAMLRGVDKLADTVKTTIGPKGRNVVLEQSYGSPTITNDGVTIAKNIELEDHFENMGAKLVSEVASKT 80
Cdd:COG0459 1 MAKQILFGEDARRANIRGVKALADAVKVTLGPKGRNVMLVKSFGDPTITNDGVTIAKEIELEDPFENMGAQLVKEVASKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 81 NDIAGDGTTTATVLTQAIVNEGMKNVTAGANPVGIRRGIEKATAAAVAELKTMSHDVKTKDDIAQIASISAAN-PEVGQL 159
Cdd:COG0459 81 NDEAGDGTTTATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPVDDKEELAQVATISANGdEEIGEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 160 IADAMEKVGNDGVITIEDSRGVDTSVDVVEGMSFDRGYMSQYMVTDNDKMEANLDNPYVLITDKKIANIQDILPLLQSVV 239
Cdd:COG0459 161 IAEAMEKVGKDGVITVEEGKGLETELEVVEGMQFDKGYLSPYFVTDPEKMPAELENAYILLTDKKISSIQDLLPLLEKVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 240 QEGRALLIIADDITGEALPTLVLNKIRGTFNVVAVKAPGFGDRRKAQLEDIAVLTGGTVISDDLGMQLKDATIDQLGSAN 319
Cdd:COG0459 241 QSGKPLLIIAEDIDGEALATLVVNGIRGVLRVVAVKAPGFGDRRKAMLEDIAILTGGRVISEDLGLKLEDVTLDDLGRAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 320 KVTVTKDNTTIVDGAGDKAAIadrveqikkaiaetssdfdkeklqerlaklaggvaVVKVGAATETELKERKYRIEDALN 399
Cdd:COG0459 321 RVEVDKDNTTIVEGAGNPKAI-----------------------------------VILVGAATEVEVKERKRRVEDALH 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 400 ATRAAVQEGFVPGGGTALVNVIPALEKVEAETTGDEQTGVKIVKAALEAPVRQIAENAGVEGSVIINQLKN-EQPGIGYN 478
Cdd:COG0459 366 ATRAAVEEGIVPGGGAALLRAARALRELAAKLEGDEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKVRAaKDKGFGFD 445
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 518035950 479 AAEDKFEDMVAAGIVDPTKVTRSALQNAASVSALLLTTEAVVADKPEPKDAA 530
Cdd:COG0459 446 AATGEYVDMLEAGVIDPAKVKRSALQNAASVAGLILTTEAVIADKPEKEEAA 497
|
|
| groEL |
PRK12851 |
chaperonin GroEL; Reviewed |
1-534 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 171770 Cd Length: 541 Bit Score: 736.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 1 MAKELKFAEDARRAMLRGVDKLADTVKTTIGPKGRNVVLEQSYGSPTITNDGVTIAKNIELEDHFENMGAKLVSEVASKT 80
Cdd:PRK12851 2 AAKEVKFHVEAREKMLRGVNILADAVKVTLGPKGRNVVIDKSFGAPTITNDGVTIAKEIELEDKFENMGAQMVREVASKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 81 NDIAGDGTTTATVLTQAIVNEGMKNVTAGANPVGIRRGIEKATAAAVAELKTMSHDVKTKDDIAQIASISAAN-PEVGQL 159
Cdd:PRK12851 82 NDVAGDGTTTATVLAQAIVREGAKAVAAGANPMDLKRGIDRAVAAVVEELKANARPVTTNAEIAQVATISANGdAEIGRL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 160 IADAMEKVGNDGVITIEDSRGVDTSVDVVEGMSFDRGYMSQYMVTDNDKMEANLDNPYVLITDKKIANIQDILPLLQSVV 239
Cdd:PRK12851 162 VAEAMEKVGNEGVITVEESKTAETELEVVEGMQFDRGYLSPYFVTDADKMEAELEDPYILIHEKKISNLQDLLPVLEAVV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 240 QEGRALLIIADDITGEALPTLVLNKIRGTFNVVAVKAPGFGDRRKAQLEDIAVLTGGTVISDDLGMQLKDATIDQLGSAN 319
Cdd:PRK12851 242 QSGKPLLIIAEDVEGEALATLVVNKLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGIKLENVTLEQLGRAK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 320 KVTVTKDNTTIVDGAGDKAAIADRVEQIKKAIAETSSDFDKEKLQERLAKLAGGVAVVKVGAATETELKERKYRIEDALN 399
Cdd:PRK12851 322 KVVVEKENTTIIDGAGSKTEIEGRVAQIRAQIEETTSDYDREKLQERLAKLAGGVAVIRVGASTEVEVKEKKDRVDDALH 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 400 ATRAAVQEGFVPGGGTALVNVIPALEKVEAEtTGDEQTGVKIVKAALEAPVRQIAENAGVEGSVIINQLKNEQPGIGYNA 479
Cdd:PRK12851 402 ATRAAVEEGIVPGGGVALLRAVKALDKLETA-NGDQRTGVEIVRRALEAPVRQIAENAGAEGSVVVGKLREKPGGYGFNA 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 518035950 480 AEDKFEDMVAAGIVDPTKVTRSALQNAASVSALLLTTEAVVADKPEPKDAAPMNP 534
Cdd:PRK12851 481 ATNEYGDLYAQGVIDPVKVVRTALQNAASVAGLLLTTEAMVAEKPKKEPAPPAPP 535
|
|
| PTZ00114 |
PTZ00114 |
Heat shock protein 60; Provisional |
2-534 |
0e+00 |
|
Heat shock protein 60; Provisional
Pssm-ID: 185455 Cd Length: 555 Bit Score: 711.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 2 AKELKFAEDARRAMLRGVDKLADTVKTTIGPKGRNVVLEQSYGSPTITNDGVTIAKNIELEDHFENMGAKLVSEVASKTN 81
Cdd:PTZ00114 14 GKEIRFGDEARQSLLKGIERLADAVAVTLGPKGRNVIIEQEYGSPKITKDGVTVAKAIEFSDRFENVGAQLIRQVASKTN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 82 DIAGDGTTTATVLTQAIVNEGMKNVTAGANPVGIRRGIEKATAAAVAELKTMSHDVKTKDDIAQIASISA-ANPEVGQLI 160
Cdd:PTZ00114 94 DKAGDGTTTATILARAIFREGCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQSRPVKTKEDILNVATISAnGDVEIGSLI 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 161 ADAMEKVGNDGVITIEDSRGVDTSVDVVEGMSFDRGYMSQYMVTDNDKMEANLDNPYVLITDKKIANIQDILPLLQSVVQ 240
Cdd:PTZ00114 174 ADAMDKVGKDGTITVEDGKTLEDELEVVEGMSFDRGYISPYFVTNEKTQKVELENPLILVTDKKISSIQSILPILEHAVK 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 241 EGRALLIIADDITGEALPTLVLNKIRGTFNVVAVKAPGFGDRRKAQLEDIAVLTGGTVISDD-LGMQLKDATIDQLGSAN 319
Cdd:PTZ00114 254 NKRPLLIIAEDVEGEALQTLIINKLRGGLKVCAVKAPGFGDNRKDILQDIAVLTGATVVSEDnVGLKLDDFDPSMLGSAK 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 320 KVTVTKDNTTIVDGAGDKAAIADRVEQIKKAIAETSSDFDKEKLQERLAKLAGGVAVVKVGAATETELKERKYRIEDALN 399
Cdd:PTZ00114 334 KVTVTKDETVILTGGGDKAEIKERVELLRSQIERTTSEYDKEKLKERLAKLSGGVAVIKVGGASEVEVNEKKDRIEDALN 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 400 ATRAAVQEGFVPGGGTALVNVIPALEKVEA--ETTGDEQTGVKIVKAALEAPVRQIAENAGVEGSVIINQLKNEQ-PGIG 476
Cdd:PTZ00114 414 ATRAAVEEGIVPGGGVALLRASKLLDKLEEdnELTPDQRTGVKIVRNALRLPTKQIAENAGVEGAVVVEKILEKKdPSFG 493
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 518035950 477 YNAAEDKFEDMVAAGIVDPTKVTRSALQNAASVSALLLTTEAVVADKPEPKDAAPMNP 534
Cdd:PTZ00114 494 YDAQTGEYVNMFEAGIIDPTKVVRSALVDAASVASLMLTTEAAIVDLPKEKKKNKNSA 551
|
|
| groEL |
PRK12852 |
chaperonin GroEL; Reviewed |
1-534 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237232 Cd Length: 545 Bit Score: 689.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 1 MAKELKFAEDARRAMLRGVDKLADTVKTTIGPKGRNVVLEQSYGSPTITNDGVTIAKNIELEDHFENMGAKLVSEVASKT 80
Cdd:PRK12852 2 AAKDVKFSGDARDRMLRGVDILANAVKVTLGPKGRNVVIEKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVREVASKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 81 NDIAGDGTTTATVLTQAIVNEGMKNVTAGANPVGIRRGIEKATAAAVAELKTMSHDVKTKDDIAQIASISA-ANPEVGQL 159
Cdd:PRK12852 82 NDLAGDGTTTATVLAQAIVREGAKAVAAGMNPMDLKRGIDIAVAAVVKDIEKRAKPVASSAEIAQVGTISAnGDAAIGKM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 160 IADAMEKVGNDGVITIEDSRGVDTSVDVVEGMSFDRGYMSQYMVTDNDKMEANLDNPYVLITDKKIANIQDILPLLQSVV 239
Cdd:PRK12852 162 IAQAMQKVGNEGVITVEENKSLETEVDIVEGMKFDRGYLSPYFVTNAEKMTVELDDAYILLHEKKLSGLQAMLPVLEAVV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 240 QEGRALLIIADDITGEALPTLVLNKIRGTFNVVAVKAPGFGDRRKAQLEDIAVLTGGTVISDDLGMQLKDATIDQLGSAN 319
Cdd:PRK12852 242 QSGKPLLIIAEDVEGEALATLVVNRLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGQLISEDLGIKLENVTLKMLGRAK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 320 KVTVTKDNTTIVDGAGDKAAIADRVEQIKKAIAETSSDFDKEKLQERLAKLAGGVAVVKVGAATETELKERKYRIEDALN 399
Cdd:PRK12852 322 KVVIDKENTTIVNGAGKKADIEARVGQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKEKKDRVEDALN 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 400 ATRAAVQEGFVPGGGTALVNVIPALEKVeAETTGDEQTGVKIVKAALEAPVRQIAENAGVEGSVIINQ-LKNEQPGIGYN 478
Cdd:PRK12852 402 ATRAAVQEGIVPGGGVALLRAKKAVGRI-NNDNADVQAGINIVLKALEAPIRQIAENAGVEGSIVVGKiLENKSETFGFD 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 518035950 479 AAEDKFEDMVAAGIVDPTKVTRSALQNAASVSALLLTTEAVVADKPEpKDAAPMNP 534
Cdd:PRK12852 481 AQTEEYVDMVAKGIIDPAKVVRTALQDAASVAGLLVTTEAMVAELPK-KDAAPAMP 535
|
|
| groEL |
CHL00093 |
chaperonin GroEL |
1-525 |
0e+00 |
|
chaperonin GroEL
Pssm-ID: 177025 Cd Length: 529 Bit Score: 687.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 1 MAKELKFAEDARRAMLRGVDKLADTVKTTIGPKGRNVVLEQSYGSPTITNDGVTIAKNIELEDHFENMGAKLVSEVASKT 80
Cdd:CHL00093 1 MSKKILYQDNARRALERGMDILAEAVSVTLGPKGRNVVLEKKYGSPQIVNDGVTIAKEIELEDHIENTGVALIRQAASKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 81 NDIAGDGTTTATVLTQAIVNEGMKNVTAGANPVGIRRGIEKATAAAVAELKTMSHDVKTKDDIAQIASISAAN-PEVGQL 159
Cdd:CHL00093 81 NDVAGDGTTTATVLAYAIVKQGMKNVAAGANPISLKRGIEKATQYVVSQIAEYARPVEDIQAITQVASISAGNdEEVGSM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 160 IADAMEKVGNDGVITIEDSRGVDTSVDVVEGMSFDRGYMSQYMVTDNDKMEANLDNPYVLITDKKIANI-QDILPLLQSV 238
Cdd:CHL00093 161 IADAIEKVGREGVISLEEGKSTVTELEITEGMRFEKGFISPYFVTDTERMEVVQENPYILLTDKKITLVqQDLLPILEQV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 239 VQEGRALLIIADDITGEALPTLVLNKIRGTFNVVAVKAPGFGDRRKAQLEDIAVLTGGTVISDDLGMQLKDATIDQLGSA 318
Cdd:CHL00093 241 TKTKRPLLIIAEDVEKEALATLVLNKLRGIVNVVAVRAPGFGDRRKAMLEDIAILTGGQVITEDAGLSLETIQLDLLGQA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 319 NKVTVTKDNTTIVdGAGDKAAIADRVEQIKKAIAETSSDFDKEKLQERLAKLAGGVAVVKVGAATETELKERKYRIEDAL 398
Cdd:CHL00093 321 RRIIVTKDSTTII-ADGNEEQVKARCEQLRKQIEIADSSYEKEKLQERLAKLSGGVAVIKVGAATETEMKDKKLRLEDAI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 399 NATRAAVQEGFVPGGGTALVNVIPALEK-VEAETTGDEQTGVKIVKAALEAPVRQIAENAGVEGSVIINQLKNEQPGIGY 477
Cdd:CHL00093 400 NATKAAVEEGIVPGGGATLVHLSENLKTwAKNNLKEDELIGALIVARAILAPLKRIAENAGKNGSVIIEKVQEQDFEIGY 479
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 518035950 478 NAAEDKFEDMVAAGIVDPTKVTRSALQNAASVSALLLTTEAVVADKPE 525
Cdd:CHL00093 480 NAANNKFVNMYEAGIIDPAKVTRSALQNAASIASMILTTECIIVDKKE 527
|
|
| PRK14104 |
PRK14104 |
chaperonin GroEL; Provisional |
2-534 |
0e+00 |
|
chaperonin GroEL; Provisional
Pssm-ID: 172594 Cd Length: 546 Bit Score: 596.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 2 AKELKFAEDARRAMLRGVDKLADTVKTTIGPKGRNVVLEQSYGSPTITNDGVTIAKNIELEDHFENMGAKLVSEVASKTN 81
Cdd:PRK14104 3 AKEVKFGVDARDRMLRGVDILANAVKVTLGPKGRNVVLDKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVREVASKSA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 82 DIAGDGTTTATVLTQAIVNEGMKNVTAGANPVGIRRGIEKATAAAVAELKTMSHDVKTKDDIAQIASISA-ANPEVGQLI 160
Cdd:PRK14104 83 DAAGDGTTTATVLAQAIVREGAKSVAAGMNPMDLKRGIDLAVEAVVADLVKNSKKVTSNDEIAQVGTISAnGDAEIGKFL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 161 ADAMEKVGNDGVITIEDSRGVDTSVDVVEGMSFDRGYMSQYMVTDNDKMEANLDNPYVLITDKKIANIQDILPLLQSVVQ 240
Cdd:PRK14104 163 ADAMKKVGNEGVITVEEAKSLETELDVVEGMQFDRGYISPYFVTNADKMRVEMDDAYILINEKKLSSLNELLPLLEAVVQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 241 EGRALLIIADDITGEALPTLVLNKIRGTFNVVAVKAPGFGDRRKAQLEDIAVLTGGTVISDDLGMQLKDATIDQLGSANK 320
Cdd:PRK14104 243 TGKPLVIVAEDVEGEALATLVVNRLRGGLKVAAVKAPGFGDRRKAMLQDIAILTGGQAISEDLGIKLENVTLQMLGRAKK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 321 VTVTKDNTTIVDGAGDKAAIADRVEQIKKAIAETSSDFDKEKLQERLAKLAGGVAVVKVGAATETELKERKYRIEDALNA 400
Cdd:PRK14104 323 VMIDKENTTIVNGAGKKADIEARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKERKDRVDDAMHA 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 401 TRAAVQEGFVPGGGTALVNVIPALEKVEAETTgDEQTGVKIVKAALEAPVRQIAENAGVEGSVIINQ-LKNEQPGIGYNA 479
Cdd:PRK14104 403 TRAAVEEGIVPGGGVALLRASEQLKGIKTKND-DQKTGVEIVRKALSAPARQIAINAGEDGSVIVGKiLEKEQYSYGFDS 481
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 518035950 480 AEDKFEDMVAAGIVDPTKVTRSALQNAASVSALLLTTEAVVADKPEPKDAAPMNP 534
Cdd:PRK14104 482 QTGEYGNLVSKGIIDPTKVVRTAIQNAASVAALLITTEAMVAELPKKGGAGPAMP 536
|
|
| PLN03167 |
PLN03167 |
Chaperonin-60 beta subunit; Provisional |
2-534 |
0e+00 |
|
Chaperonin-60 beta subunit; Provisional
Pssm-ID: 215611 [Multi-domain] Cd Length: 600 Bit Score: 556.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 2 AKELKFAED--ARRAMLRGVDKLADTVKTTIGPKGRNVVLEQSYGSPTITNDGVTIAKNIELEDHFENMGAKLVSEVASK 79
Cdd:PLN03167 56 AKELHFNKDgsAIKKLQAGVNKLADLVGVTLGPKGRNVVLESKYGSPKIVNDGVTVAKEVELEDPVENIGAKLVRQAAAK 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 80 TNDIAGDGTTTATVLTQAIVNEGMKNVTAGANPVGIRRGIEKATAAAVAELKTMSHDVKtKDDIAQIASISAAN-PEVGQ 158
Cdd:PLN03167 136 TNDLAGDGTTTSVVLAQGLIAEGVKVVAAGANPVQITRGIEKTAKALVKELKKMSKEVE-DSELADVAAVSAGNnYEVGN 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 159 LIADAMEKVGNDGVITIEDSRGVDTSVDVVEGMSFDRGYMSQYMVTDNDKMEANLDNPYVLITDKKIANIQDILPLLQSV 238
Cdd:PLN03167 215 MIAEAMSKVGRKGVVTLEEGKSAENNLYVVEGMQFDRGYISPYFVTDSEKMSVEYDNCKLLLVDKKITNARDLIGILEDA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 239 VQEGRALLIIADDITGEALPTLVLNKIRGTFNVVAVKAPGFGDRRKAQLEDIAVLTGGTVISDDLGMQLKDATIDQLGSA 318
Cdd:PLN03167 295 IRGGYPLLIIAEDIEQEALATLVVNKLRGSLKIAALKAPGFGERKSQYLDDIAILTGGTVIREEVGLSLDKVGKEVLGTA 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 319 NKVTVTKDNTTIVDGAGDKAAIADRVEQIKKAIAETSSDFDKEKLQERLAKLAGGVAVVKVGAATETELKERKYRIEDAL 398
Cdd:PLN03167 375 AKVVLTKDTTTIVGDGSTQEAVNKRVAQIKNLIEAAEQDYEKEKLNERIAKLSGGVAVIQVGAQTETELKEKKLRVEDAL 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 399 NATRAAVQEGFVPGGGTALVNVIPALEKVEAETTGDEQ-TGVKIVKAALEAPVRQIAENAGVEGSVIINQ-LKNEQPGIG 476
Cdd:PLN03167 455 NATKAAVEEGIVVGGGCTLLRLASKVDAIKDTLENDEQkVGADIVKRALSYPLKLIAKNAGVNGSVVSEKvLSNDNPKFG 534
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 518035950 477 YNAAEDKFEDMVAAGIVDPTKVTRSALQNAASVSALLLTTEAVVADKPEPKDAAPMNP 534
Cdd:PLN03167 535 YNAATGKYEDLMAAGIIDPTKVVRCCLEHAASVAKTFLTSDCVVVEIKEPEPVPAGNP 592
|
|
| chaperonin_type_I_II |
cd00309 |
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ... |
3-521 |
6.92e-157 |
|
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: 455.73 E-value: 6.92e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 3 KELKFAEDARRAMLRGVDKLADTVKTTIGPKGRNVVLEQSYGSPTITNDGVTIAKNIELEdhfeNMGAKLVSEVASKTND 82
Cdd:cd00309 1 KEREFGEEARLSNINAAKALADAVKTTLGPKGMDKMLVDSLGDPTITNDGATILKEIEVE----HPAAKLLVEVAKSQDD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 83 IAGDGTTTATVLTQAIVNEGMKNVTAGANPVGIRRGIEKATAAAVAELKTMS--HDVKTKDDIAQIASISAA-------N 153
Cdd:cd00309 77 EVGDGTTTVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAvpIDVEDREELLKVATTSLNsklvsggD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 154 PEVGQLIADAMEKVG------NDGVITIEDSRG---VDTSvdVVEGMSFDRGYMSQYmvtdndkMEANLDNPYVLITDKK 224
Cdd:cd00309 157 DFLGELVVDAVLKVGkengdvDLGVIRVEKKKGgslEDSE--LVVGMVFDKGYLSPY-------MPKRLENAKILLLDCK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 225 IANiqdilpllqsvvqegralLIIADD-ITGEALPTLVLNKIrgtfnvVAVKApgfgdRRKAQLEDIAVLTGGTVISDdl 303
Cdd:cd00309 228 LEY------------------VVIAEKgIDDEALHYLAKLGI------MAVRR-----VRKEDLERIAKATGATIVSR-- 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 304 gmqLKDATIDQLGSANKVTVTK----DNTTIVDGAGdkaaiadrveqikkaiaetssdfdkeklqerlaklaGGVAVVKV 379
Cdd:cd00309 277 ---LEDLTPEDLGTAGLVEETKigdeKYTFIEGCKG------------------------------------GKVATILL 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 380 GAATETELKERKYRIEDALNATRAAVQE-GFVPGGGTALVNVIPALEKVEAETTGDEQTGVKIVKAALEAPVRQIAENAG 458
Cdd:cd00309 318 RGATEVELDEAERSLHDALCAVRAAVEDgGIVPGGGAAEIELSKALEELAKTLPGKEQLGIEAFADALEVIPRTLAENAG 397
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518035950 459 VEGSVIINQLKNEQPGIGYNAAED----KFEDMVAAGIVDPTKVTRSALQNAASVSALLLTTEAVVA 521
Cdd:cd00309 398 LDPIEVVTKLRAKHAEGGGNAGGDvetgEIVDMKEAGIIDPLKVKRQALKSATEAASLILTIDDIIV 464
|
|
| Cpn60_TCP1 |
pfam00118 |
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ... |
22-523 |
9.33e-94 |
|
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: 294.88 E-value: 9.33e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 22 LADTVKTTIGPKGRNVVLEQSYGSPTITNDGVTIAKNIELEdhfeNMGAKLVSEVASKTNDIAGDGTTTATVLTQAIVNE 101
Cdd:pfam00118 1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELEIQ----HPAAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 102 GMKNVTAGANPVGIRRGIEKATAAAVAELK---TMSHDVKTKDDIAQIASISAAN-------PEVGQLIADAME------ 165
Cdd:pfam00118 77 AEKLLAAGVHPTTIIEGYEKALEKALEILDsiiSIPVEDVDREDLLKVARTSLSSkiisresDFLAKLVVDAVLaipknd 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 166 ---KVGNDGVITIEDSRGVDTSvdVVEGMSFDRGYMSQYMVTDndkmeanLDNPYVLITDKKIANIQD------------ 230
Cdd:pfam00118 157 gsfDLGNIGVVKILGGSLEDSE--LVDGVVLDKGPLHPDMPKR-------LENAKVLLLNCSLEYEKTetkatvvlsdae 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 231 ------------ILPLLQSVVQEGRALLIIADDITGEALPTLVLNKIRGTFNVvavkapgfgdrRKAQLEDIAVLTGGTV 298
Cdd:pfam00118 228 qlerflkaeeeqILEIVEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMALRRV-----------KKRDLERLAKATGARA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 299 ISddlgmQLKDATIDQLGSANKV---TVTKDNTTIVDGAGDkaaiadrveqikkaiaetssdfdkeklqerlaklaGGVA 375
Cdd:pfam00118 297 VS-----SLDDLTPDDLGTAGKVeeeKIGDEKYTFIEGCKS-----------------------------------PKAA 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 376 VVKVGAATETELKERKYRIEDALNATRAAVQE-GFVPGGGTALVNVIPALEKVEAETTGDEQTGVKIVKAALEAPVRQIA 454
Cdd:pfam00118 337 TILLRGATDHVLDEIERSIHDALCVVKNAIEDpRVVPGGGAVEMELARALREYAKSVSGKEQLAIEAFAEALEVIPKTLA 416
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518035950 455 ENAGVEGSVIINQLKNEQ----PGIGYNAAEDKFEDMVAAGIVDPTKVTRSALQNAASVSALLLTTEAVVADK 523
Cdd:pfam00118 417 ENAGLDPIEVLAELRAAHasgeKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKSATEAASTILRIDDIIKAK 489
|
|
| chaperonin_like |
cd03333 |
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ... |
140-407 |
1.80e-37 |
|
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: 137.21 E-value: 1.80e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 140 KDDIAQIASISAA------NPEVGQLIADAMEKVG------NDGVITIEDSRG---VDTSVdvVEGMSFDRGYMSQYMvt 204
Cdd:cd03333 1 RELLLQVATTSLNsklsswDDFLGKLVVDAVLKVGpdnrmdDLGVIKVEKIPGgslEDSEL--VVGVVFDKGYASPYM-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 205 dndkmEANLDNPYVLITDKKIANiqdilpllqsvvqegralLIIADD-ITGEALPTLVLNKIrgtfnvVAVKApgfgdRR 283
Cdd:cd03333 77 -----PKRLENAKILLLDCPLEY------------------VVIAEKgIDDLALHYLAKAGI------MAVRR-----VK 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 284 KAQLEDIAVLTGGTVISDdlgmqLKDATIDQLGSANKVTVTKD----NTTIVDGAGdkaaiadrveqikkaiaetssdfd 359
Cdd:cd03333 123 KEDLERIARATGATIVSS-----LEDLTPEDLGTAELVEETKIgeekLTFIEGCKG------------------------ 173
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 518035950 360 keklqerlaklaGGVAVVKVGAATETELKERKYRIEDALNATRAAVQE 407
Cdd:cd03333 174 ------------GKAATILLRGATEVELDEVKRSLHDALCAVRAAVEE 209
|
|
| cpn60 |
cd03343 |
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ... |
9-521 |
2.18e-34 |
|
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: 136.24 E-value: 2.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 9 EDARRAMLRGVDKLADTVKTTIGPKGRNVVLEQSYGSPTITNDGVTIAKNIELEdhfeNMGAKLVSEVASKTNDIAGDGT 88
Cdd:cd03343 14 RDAQRMNIAAAKAVAEAVRTTLGPKGMDKMLVDSLGDVTITNDGATILKEMDIE----HPAAKMLVEVAKTQDEEVGDGT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 89 TTATVLTQAIVNEGMKNVTAGANPVGIRRGIEKATAAAVAELKTMSHDVKTKDD--IAQIASISAAnpevGQLIADAMEK 166
Cdd:cd03343 90 TTAVVLAGELLEKAEDLLDQNIHPTVIIEGYRLAAEKALELLDEIAIKVDPDDKdtLRKIAKTSLT----GKGAEAAKDK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 167 VGN---DGVITIEDSRGVDTSVDV-------VEGMSFDRGYMSQYMVTD----NDKMEANLDNPYVLITDKKIA------ 226
Cdd:cd03343 166 LADlvvDAVLQVAEKRDGKYVVDLdnikiekKTGGSVDDTELIRGIVIDkevvHPGMPKRVENAKIALLDAPLEvkktei 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 227 ----NIQDILPLLQSVVQEGRALLIIADDITGEALPTLVLNKirGTFNVVA---VKAPGFGDRR--KAQLEDIAVLTGGT 297
Cdd:cd03343 246 dakiRITSPDQLQAFLEQEEAMLKEMVDKIADTGANVVFCQK--GIDDLAQhylAKAGILAVRRvkKSDMEKLARATGAK 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 298 VISDdlgmqLKDATIDQLGSANKVTVTKDnttivdgAGDKAAIadrVEQIKKAIAETssdfdkeklqerlaklaggvavV 377
Cdd:cd03343 324 IVTN-----IDDLTPEDLGEAELVEERKV-------GDDKMVF---VEGCKNPKAVT----------------------I 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 378 KVGAATETELKERKYRIEDALNATRAAVQEG-FVPGGGTALVNVIPALEKVEAETTGDEQTGVKIVKAALEAPVRQIAEN 456
Cdd:cd03343 367 LLRGGTEHVVDELERALEDALRVVADALEDGkVVAGGGAVEIELAKRLREYARSVGGREQLAVEAFADALEEIPRTLAEN 446
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518035950 457 AGVEGSVIINQLK----NEQPGIGYNAAEDKFEDMVAAGIVDPTKVTRSALQNAASVSALLLTTEAVVA 521
Cdd:cd03343 447 AGLDPIDTLVELRaaheKGNKNAGLDVYTGEVVDMLEKGVIEPLRVKKQAIKSATEAATMILRIDDVIA 515
|
|
| thermosome_alpha |
NF041082 |
thermosome subunit alpha; |
10-521 |
5.23e-31 |
|
thermosome subunit alpha;
Pssm-ID: 469009 Cd Length: 518 Bit Score: 126.54 E-value: 5.23e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 10 DARRAMLRGVDKLADTVKTTIGPKGRNVVLEQSYGSPTITNDGVTIAKNIELedhfENMGAKLVSEVASKTNDIAGDGTT 89
Cdd:NF041082 17 DAQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDVVITNDGVTILKEMDI----EHPAAKMIVEVAKTQDDEVGDGTT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 90 TATVLTQAIVNEGMKNVTAGANPVGIRRGIEKATAAAVAELKTMSHDVKTKDD-----IAQIA----SISAANPEVGQLI 160
Cdd:NF041082 93 TAVVLAGELLKKAEELLDQDIHPTIIAEGYRLAAEKALEILDEIAIKVDPDDKetlkkIAATAmtgkGAEAAKDKLADLV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 161 ADAMEKVGNDgvitiEDSRGVDTS---VDVVEGMSFDRGYMSQYMVTDNDKMEANLdnPYVlITDKKIA----------- 226
Cdd:NF041082 173 VDAVKAVAEK-----DGGYNVDLDnikVEKKVGGSIEDSELVEGVVIDKERVHPGM--PKR-VENAKIAlldaplevkkt 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 227 ------NIQDILPLLQSVVQEGRALLIIADDI--TGEalptlvlnkirgtfNVVAV-------------KAPGFGDRR-- 283
Cdd:NF041082 245 eidakiSITDPDQLQAFLDQEEKMLKEMVDKIadSGA--------------NVVFCqkgiddlaqhylaKEGILAVRRvk 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 284 KAQLEDIAVLTGGTVISDdlgmqLKDATIDQLGSANKVT---VTKDNTTIVDGAGDKAAIAdrveqikkaiaetssdfdk 360
Cdd:NF041082 311 KSDMEKLAKATGARIVTS-----IDDLSPEDLGYAGLVEerkVGGDKMIFVEGCKNPKAVT------------------- 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 361 eklqerlaklaggvavVKVGAATETELKERKYRIEDALNATRAAVQEG-FVPGGGTALVNVIPALEKVEAETTGDEQTGV 439
Cdd:NF041082 367 ----------------ILLRGGTEHVVDEVERALEDALRVVRVVLEDGkVVAGGGAPEVELALRLREYAASVGGREQLAI 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 440 KIVKAALEAPVRQIAENAGVEGSVIINQLKNEQPG----IGYNAAEDKFEDMVAAGIVDPTKVTRSALQNAASVSALLLT 515
Cdd:NF041082 431 EAFAEALEIIPRTLAENAGLDPIDALVELRSAHEKgnktAGLDVYTGKVVDMLEIGVVEPLRVKTQAIKSATEAAVMILR 510
|
....*.
gi 518035950 516 TEAVVA 521
Cdd:NF041082 511 IDDVIA 516
|
|
| thermosome_beta |
NF041083 |
thermosome subunit beta; |
10-523 |
4.07e-30 |
|
thermosome subunit beta;
Pssm-ID: 469010 Cd Length: 519 Bit Score: 123.91 E-value: 4.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 10 DARRAMLRGVDKLADTVKTTIGPKGRNVVLEQSYGSPTITNDGVTIAKNIELedhfENMGAKLVSEVASKTNDIAGDGTT 89
Cdd:NF041083 17 DAQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDIVITNDGATILKEMDV----QHPAAKMLVEVAKTQDDEVGDGTT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 90 TATVLTQAIVNEGMKNVTAGANPVGIRRGIEKATAAAVAELKTMSHDVKTKDD--IAQIASISAANPEVGqLIADAMEKV 167
Cdd:NF041083 93 TAVVLAGELLKKAEELLDQNIHPTIIANGYRLAAEKAIEILDEIAEKVDPDDRetLKKIAETSLTSKGVE-EARDYLAEI 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 168 GNDGVITIEDSRGVDTSVDV-------VEGMSFDRGYMSQYMVTDNDK----MEANLDNPYVLITDKKI--------ANI 228
Cdd:NF041083 172 AVKAVKQVAEKRDGKYYVDLdniqiekKHGGSIEDTQLIYGIVIDKEVvhpgMPKRVENAKIALLDAPLevkkteidAEI 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 229 QDILP-LLQSVVQEGRALLiiadditgealpTLVLNKIRGT-FNVVAV-------------KAPGFGDRR--KAQLEDIA 291
Cdd:NF041083 252 RITDPdQLQKFLDQEEKML------------KEMVDKIKATgANVVFCqkgiddlaqhylaKAGILAVRRvkKSDMEKLA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 292 VLTGGTVISDdlgmqLKDATIDQLGSANKVT---VTKDNTTIVDGAGDKAAIAdrveqikkaiaetssdfdkeklqerla 368
Cdd:NF041083 320 KATGARIVTN-----IDDLTPEDLGYAELVEerkVGDDKMVFVEGCKNPKAVT--------------------------- 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 369 klaggvavVKVGAATETELKERKYRIEDALNATRAAVQEG-FVPGGGTALVNVIPALEKVEAETTGDEQTGVKIVKAALE 447
Cdd:NF041083 368 --------ILIRGGTEHVVDEAERALEDALSVVADAVEDGkIVAGGGAPEVELAKRLREYAATVGGREQLAVEAFAEALE 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 448 APVRQIAENAGVEGSVIINQL----KNEQPGIGYNAAEDKFEDMVAAGIVDPTKVTRSALQNAASVSALLLTTEAVVADK 523
Cdd:NF041083 440 IIPRTLAENAGLDPIDILVKLrsahEKGKKWAGINVFTGEVVDMWELGVIEPLRVKTQAIKSATEAATMILRIDDVIAAK 519
|
|
| TCP1_delta |
cd03338 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ... |
22-514 |
2.34e-22 |
|
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: 100.44 E-value: 2.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 22 LADTVKTTIGPKGRNVVLEQSYGSPTITNDGVTIAKNIELeDHfenMGAKLVSEVaSKTNDI-AGDGTTTATVLTQAIVN 100
Cdd:cd03338 20 VADAIRTSLGPRGMDKMIQTGKGEVIITNDGATILKQMSV-LH---PAAKMLVEL-SKAQDIeAGDGTTSVVVLAGALLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 101 EGMKNVTAGANPVGIRRGIEKATAAAVAELKTMSH--DVKTKDDIAQIASISAANPEVGQ-------LIADAMEKVGNDG 171
Cdd:cd03338 95 ACESLLKKGIHPTVISESFQIAAKKAVEILDSMSIpvDLNDRESLIKSATTSLNSKVVSQyssllapIAVDAVLKVIDPA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 172 VITIEDSR---------GVDTSVDVVEGMSFDRGYMSQymvtdndkmeanlDNPYVLITDKKIANIQ------------- 229
Cdd:cd03338 175 TATNVDLKdirivkklgGTIEDTELVDGLVFTQKASKK-------------AGGPTRIEKAKIGLIQfclsppktdmdnn 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 230 ----D--------------ILPLLQSVVQEGRALLIIADDITGEALPTL---VLNKIrgtfNVVAVKapgfgDRRKAQLE 288
Cdd:cd03338 242 ivvnDyaqmdrilreerkyILNMCKKIKKSGCNVLLIQKSILRDAVSDLalhFLAKL----KIMVVK-----DIEREEIE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 289 DIAVLTGGTVIsddlgmqlkdATIDQLGSankvtvtkdnttivdgagDKAAIADRVEqikkaiaETSSDFDKEKLQERLA 368
Cdd:cd03338 313 FICKTIGCKPV----------ASIDHFTE------------------DKLGSADLVE-------EVSLGDGKIVKITGVK 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 369 KLAGGVAVVkVGAATETELKERKYRIEDALNATRAAVQEGF-VPGGGTALVNVIPALEKVEAETTGDEQTGVKIVKAALE 447
Cdd:cd03338 358 NPGKTVTIL-VRGSNKLVLDEAERSLHDALCVIRCLVKKRAlIPGGGAPEIEIALQLSEWARTLTGVEQYCVRAFADALE 436
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518035950 448 APVRQIAENAGVEGSVIINQLKNE--QPGI--GYNAAEDKFEDMVAAGIVDPTKVTRSALQNAASVSALLL 514
Cdd:cd03338 437 VIPYTLAENAGLNPISIVTELRNRhaQGEKnaGINVRKGAITNILEENVVQPLLVSTSAITLATETVRMIL 507
|
|
| TCP1_beta |
cd03336 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ... |
8-524 |
6.21e-20 |
|
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: 93.16 E-value: 6.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 8 AEDARRAMLRGVDKLADTVKTTIGPKGRNVVLEQSY--GSPTITNDGVTIAKNIeledHFENMGAKLVSEVASKTNDIAG 85
Cdd:cd03336 11 GETARLSSFVGAIAIGDLVKTTLGPKGMDKILQSVGrsGGVTVTNDGATILKSI----GVDNPAAKVLVDISKVQDDEVG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 86 DGTTTATVLTQAIVNEGMKNVTAGANPVGIRRGIEKATAAAVAELKTMSHD-----VKTKDDIAQIAS-------ISAAN 153
Cdd:cd03336 87 DGTTSVTVLAAELLREAEKLVAQKIHPQTIIEGYRMATAAAREALLSSAVDhssdeEAFREDLLNIARttlsskiLTQDK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 154 PEVGQLIADAMEKVGNDG----VITIEDSRGV--DTSVDvvEGMSFDRGY-MSQYMVTDNDK-MEAN--LDNPYVLITDK 223
Cdd:cd03336 167 EHFAELAVDAVLRLKGSGnldaIQIIKKLGGSlkDSYLD--EGFLLDKKIgVNQPKRIENAKiLIANtpMDTDKIKIFGA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 224 KI-----ANIQDI-----LPLLQSVVQegrallIIADDITGEALPTLVLN---KIRGTFNVVAVKAPGFgdrrkAQLEDI 290
Cdd:cd03336 245 KVrvdstAKVAEIeeaekEKMKNKVEK------ILKHGINCFINRQLIYNypeQLFADAGIMAIEHADF-----DGVERL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 291 AVLTGGTVISddlgmqlkdatidqlgsankvtvTKDNTTIVdgagdKAAIADRVEQIkkAIAEtssdfdkEKLQERLAKL 370
Cdd:cd03336 314 ALVTGGEIAS-----------------------TFDHPELV-----KLGTCKLIEEI--MIGE-------DKLIRFSGVA 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 371 AGGVAVVKVGAATETELKERKYRIEDALNATRAAVQEG-FVPGGGTALVNVIPALEKVEAETTGDEQTGVKIVKAALEAP 449
Cdd:cd03336 357 AGEACTIVLRGASQQILDEAERSLHDALCVLAQTVKDTrVVLGGGCSEMLMAKAVEELAKKTPGKKSLAIEAFAKALRQL 436
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518035950 450 VRQIAENAGVEGSVIINQLK----NEQPGIGYNAAEDKFEDMVAAGIVDPTKVTRSALQNAASVSALLLTTEAVVADKP 524
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 ... |
10-522 |
2.61e-19 |
|
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: 91.02 E-value: 2.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 10 DARRAMLRGVDKLADTVKTTIGPKGRNVVLEQSYGSPTITNDGVTIAKNIELEDHFenmgAKLVSEVASKTNDIAGDGTT 89
Cdd:TIGR02343 27 EAKKSNIAAAKSVASILRTSLGPKGMDKMLISPDGDITVTNDGATILSQMDVDNQI----AKLMVELSKSQDDEIGDGTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 90 TATVLTQAIVNEGMKNVTAGANPVGIRRGIEKATAAAVAELKTMSHDVKTKDDIAQIAsISAANPEVGQLIA----DAME 165
Cdd:TIGR02343 103 GVVVLAGALLEQAEELLDKGIHPIKIADGFEEAARIAVEHLEEISDEISADNNNREPL-IQAAKTSLGSKIVskchRRFA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 166 KVGNDGVITIEDSRGVDTSVDVVE-----GMSFDRGYMSQYMVTDND----KMEANLDNPYVLI-----------TDKK- 224
Cdd:TIGR02343 182 EIAVDAVLNVADMERRDVDFDLIKvegkvGGSLEDTKLIKGIIIDKDfshpQMPKEVEDAKIAIltcpfeppkpkTKHKl 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 225 -IANIQDILPL-----------LQSVVQEGRALLIIADDITGEALPTLVLNkirgtfNVVAVKAPGfgdrrKAQLEDIAV 292
Cdd:TIGR02343 262 dISSVEEYKKLqkyeqqkfkemIDDIKKSGANLVICQWGFDDEANHLLLQN------DLPAVRWVG-----GQELELIAI 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 293 LTGGTVISddlgmQLKDATIDQLGSANKVTVTKDNTTivdgaGDKAAIadrVEQIKKAIAETssdfdkeklqerlaklag 372
Cdd:TIGR02343 331 ATGGRIVP-----RFQELSKDKLGKAGLVREISFGTT-----KDRMLV---IEQCKNSKAVT------------------ 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 373 gvavVKVGAATETELKERKYRIEDALNATRAAVQEG-FVPGGGTALVNVIPALEKVEAETTGDEQTGVKIVKAALEAPVR 451
Cdd:TIGR02343 380 ----IFIRGGNKMIIEEAKRSIHDALCVVRNLIKDSrIVYGGGAAEISCSLAVSQEADKYPGVEQYAIRAFADALETIPM 455
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518035950 452 QIAENAGVE-----GSVIINQLKNEQPGIGYNAAEDKFEDMVAAGIVDPTKVTRSALQNAASVSALLLTTEAVVAD 522
Cdd:TIGR02343 456 ALAENSGLDpigtlSTLKSLQLKEKNPNLGVDCLGYGTNDMKEQFVFETLIGKKQQILLATQLVRMILKIDDVISP 531
|
|
| chap_CCT_eta |
TIGR02345 |
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ... |
16-523 |
1.65e-18 |
|
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: 88.66 E-value: 1.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 16 LRGVDKLADTVKTTIGPKGRNVVLEQSYGSPTITNDGVTIAKNIELedhfENMGAKLVSEVASKTNDIAGDGTTTATVLT 95
Cdd:TIGR02345 24 INACVAIAEALKTTLGPRGMDKLIVGSNGKATISNDGATILKLLDI----VHPAAKTLVDIAKSQDAEVGDGTTSVTILA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 96 QAIVNEGMKNVTAGANPVGIRRGIEKATAAAVAELKTMSHDVK-TKDDIAQIASISAANPEVGQLIADAME---KVGNDG 171
Cdd:TIGR02345 100 GELLKEAKPFIEEGVHPQLIIRCYREALSLAVEKIKEIAVTIDeEKGEQRELLEKCAATALSSKLISHNKEffsKMIVDA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 172 VITIEDSRGVDTSVDV-------------VEGMSFDR-----GYMSQYMVTDNDK---------MEANLDNPYVLITDKK 224
Cdd:TIGR02345 180 VLSLDRDDLDLKLIGIkkvqggaledsqlVNGVAFKKtfsyaGFEQQPKKFANPKilllnveleLKAEKDNAEIRVEDVE 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 225 IaniqdilplLQSVVQEGRAllIIADDitgealptlvLNKIRGT-FNVVAVKAPgFGDRRKAQLEDIAVLTGGTVISDDL 303
Cdd:TIGR02345 260 D---------YQAIVDAEWA--IIFRK----------LEKIVESgANVVLSKLP-IGDLATQYFADRDIFCAGRVSAEDL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 304 GmqlkdatidqlgsankvtvtkdntTIVDGAGdkAAIADRVEQIKKAIAETSSDFDKEKL-QERLAKLAGGvavVKVGAA 382
Cdd:TIGR02345 318 K------------------------RVIKACG--GSIQSTTSDLEADVLGTCALFEERQIgSERYNYFTGC---PHAKTC 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 383 T-------ETELKERKYRIEDALNATRAAVQ-EGFVPGGGTALVNVIPALEKVEAETTGDEQTGVKIVKAALEAPVRQIA 454
Cdd:TIGR02345 369 TiilrggaEQFIEEAERSLHDAIMIVRRALKnKKIVAGGGAIEMELSKCLRDYSKTIDGKQQLIINAFAKALEIIPRQLC 448
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518035950 455 ENAGVEGSVIINQL--KNEQPGI--GYNAAEDKFEDMVAAGIVDPTKVTRSALQNAASVSALLLTTEAVVADK 523
Cdd:TIGR02345 449 ENAGFDSIEILNKLrsRHAKGGKwyGVDINTEDIGDNFEAFVWEPALVKINALKAAFEAACTILSVDETITNP 521
|
|
| chap_CCT_delta |
TIGR02342 |
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ... |
9-521 |
1.68e-18 |
|
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: 88.69 E-value: 1.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 9 EDARRAMLRGVDKLADTVKTTIGPKGRNVVLEQSYGSPTITNDGVTIAKNIELEdhfeNMGAKLVSEVaSKTNDI-AGDG 87
Cdd:TIGR02342 8 QDVRTSNIVAAKAVADAIRTSLGPKGMDKMIQDGKGEVIITNDGATILKQMAVL----HPAAKMLVEL-SKAQDIeAGDG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 88 TTTATVLTQAIVNEGMKNVTAGANPVGIRRGIEKATAAAVAELKTMSHDVKTKDDIAQIASISAA-NPEVGQLIADAMEK 166
Cdd:TIGR02342 83 TTSVVILAGALLGACERLLNKGIHPTIISESFQSAADEAIKILDEMSIPVDLSDREQLLKSATTSlSSKVVSQYSSLLAP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 167 VGNDGVITIEDSRGvDTSVD------------------VVEGMSFDRgyMSQYMVTDNDKME---------------ANL 213
Cdd:TIGR02342 163 LAVDAVLKVIDPEN-AKNVDlndikvvkklggtiddteLIEGLVFTQ--KASKSAGGPTRIEkakigliqfqisppkTDM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 214 DNPYVLITDKKIANIQD-----ILPLLQSVVQEGRALLIIADDITGEALPTLVLNKIrGTFNVVAVKapgfgDRRKAQLE 288
Cdd:TIGR02342 240 ENQIIVNDYAQMDRVLKeerayILNIVKKIKKTGCNVLLIQKSILRDAVNDLALHFL-AKMKIMVVK-----DIEREEIE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 289 DIAVLTGGTVISDdlgmqLKDATIDQLGSANKVT-VTKDNTTIVDGAGdkaaiadrveqikkaiaetssdfdkeklqerL 367
Cdd:TIGR02342 314 FICKTIGCKPIAS-----IDHFTADKLGSAELVEeVDSDGGKIIKITG-------------------------------I 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 368 AKLAGGVAVVKVGaATETELKERKYRIEDALNATRAAVQE-GFVPGGGTALVNVIPALEKVEAETTGDEQTGVKIVKAAL 446
Cdd:TIGR02342 358 QNAGKTVTVVVRG-SNKLVIDEAERSLHDALCVIRCLVKKrGLIAGGGAPEIEIARRLSKYARTMKGVESYCVRAFADAL 436
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518035950 447 EAPVRQIAENAGVEGSVIINQLKNEQPG----IGYNAAEDKFEDMVAAGIVDPTKVTRSALQNAASVSALLLTTEAVVA 521
Cdd:TIGR02342 437 EVIPYTLAENAGLNPIKVVTELRNRHANgektAGISVRKGGITNMLEEHVLQPLLVTTSAITLASETVRSILKIDDIVF 515
|
|
| TCP1_eta |
cd03340 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ... |
21-514 |
6.70e-18 |
|
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: 86.57 E-value: 6.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 21 KLADTVKTTIGPKGRNVVLEQSYGSPTITNDGVTIAKNIELedhfENMGAKLVSEVASKTNDIAGDGTTTATVLTQAIVN 100
Cdd:cd03340 27 AIADAVRTTLGPRGMDKLIVDGRGKVTISNDGATILKLLDI----VHPAAKTLVDIAKSQDAEVGDGTTSVVVLAGEFLK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 101 EGMKNVTAGANPVGIRRGIEKATAAAVAELKTMSHDVKTKDD------IAQIAS-------ISAANPEVGQLIADAMEKV 167
Cdd:cd03340 103 EAKPFIEDGVHPQIIIRGYRKALQLAIEKIKEIAVNIDKEDKeeqrelLEKCAAtalnsklIASEKEFFAKMVVDAVLSL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 168 GND------GVI-----TIEDSRgvdtsvdVVEGMSFDR-----GYMSQYMVTDNDK---------MEANLDNPYVLITD 222
Cdd:cd03340 183 DDDldldmiGIKkvpggSLEDSQ-------LVNGVAFKKtfsyaGFEQQPKKFKNPKilllnveleLKAEKDNAEVRVED 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 223 KKIaniqdilplLQSVVQEGRAllIIADDitgealptlvLNKIRGT-FNVVAVKAPgFGDRRKAQLEDIAVLTGGTVISD 301
Cdd:cd03340 256 PEE---------YQAIVDAEWK--IIYDK----------LEKIVKSgANVVLSKLP-IGDLATQYFADRDIFCAGRVPEE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 302 DLGmqlkdatidqlgsankvtvtkdntTIVDGAGdkAAIADRVEQIKKAIAETSSDFDKEKL-QERLAKLAGGVA----- 375
Cdd:cd03340 314 DLK------------------------RVAQATG--GSIQTTVSNITDDVLGTCGLFEERQVgGERYNIFTGCPKaktct 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 376 -VVKVGAATETELKERKyrIEDALNATRAAVQEGFVPGGGTALVNVIPALEKVEAET-TGDEQTGVKIVKAALEAPVRQI 453
Cdd:cd03340 368 iILRGGAEQFIEEAERS--LHDAIMIVRRAIKNDSVVAGGGAIEMELSKYLRDYSRTiAGKQQLVINAFAKALEIIPRQL 445
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518035950 454 AENAGVEGSVIINQL-----KNEQPGIGYNAAEDKFEDMVAAGIVDPTKVTRSALQNAASVSALLL 514
Cdd:cd03340 446 CDNAGFDATDILNKLrqkhaQGGGKWYGVDINNEGIADNFEAFVWEPSLVKINALTAATEAACLIL 511
|
|
| TCP1_theta |
cd03341 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ... |
14-523 |
2.74e-17 |
|
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: 84.58 E-value: 2.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 14 AMLRGVD---KLADTVKTTIGPKGRNVVLEQSYGSPTITNDGVTIAKniELEdhFENMGAKLVSEvASKTNDI-AGDGTT 89
Cdd:cd03341 9 AVLRNIEackELSQITRTSYGPNGMNKMVINHLEKLFVTSDAATILR--ELE--VQHPAAKLLVM-ASQMQEEeIGDGTN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 90 TATVLTQAIVNEGMKNVTAGANPVGIRRGIEKATAAAVAELKTMS-HDVKTKDDIAQIASI--SAANPEV-------GQL 159
Cdd:cd03341 84 LVVVLAGELLEKAEELLRMGLHPSEIIEGYEKALKKALEILEELVvYKIEDLRNKEEVSKAlkTAIASKQygnedflSPL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 160 IADAMEKV--GNDGVITIEDSR-------GVDTSvDVVEGMSFDRgymsqymvtdndkmeaNLDNPYVLITDKKIAniqd 230
Cdd:cd03341 164 VAEACISVlpENIGNFNVDNIRvvkilggSLEDS-KVVRGMVFKR----------------EPEGSVKRVKKAKVA---- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 231 ilpLLQSVVQEGRALLIIADDITGEALptLVLNKirgtFNVVAVKAPGfgdrrKAQLEDIAVLTGGTVIsddlgMQLKDA 310
Cdd:cd03341 223 ---VFSCPFDIGVNVIVAGGSVGDLAL--HYCNK----YGIMVIKINS-----KFELRRLCRTVGATPL-----PRLGAP 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 311 TIDQLGSANKVTVTKdnttivdgagdkaaIADRVEQIKKAIAETSSdfdkeklqerlaklaggVAVVKVGAATETELKER 390
Cdd:cd03341 284 TPEEIGYCDSVYVEE--------------IGDTKVVVFRQNKEDSK-----------------IATIVLRGATQNILDDV 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 391 KYRIEDALNATRAAVQEG-FVPGGGTALVNVIPALEKVEAETTGDEQTGVKIVKAALEAPVRQIAENAGVEGSVIINQL- 468
Cdd:cd03341 333 ERAIDDGVNVFKSLTKDGrFVPGAGATEIELAKKLKEYGEKTPGLEQYAIKKFAEAFEVVPRTLAENAGLDATEVLSELy 412
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 469 -----KNEQPGIGYNAAEDKFEDMVAAGIVDPTKVTRSALQNAASVSALLLTTEAVVADK 523
Cdd:cd03341 413 aahqkGNKSAGVDIESGDEGTKDAKEAGIFDHLATKKWAIKLATEAAVTVLRVDQIIMAK 472
|
|
| chap_CCT_beta |
TIGR02341 |
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ... |
8-527 |
7.14e-17 |
|
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: 83.37 E-value: 7.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 8 AEDARRAMLRGVDKLADTVKTTIGPKGRNVVLEQ--SYGSPTITNDGVTIAKNIELEdhfeNMGAKLVSEVASKTNDIAG 85
Cdd:TIGR02341 12 AENARLSSFVGAIAIGDLVKSTLGPKGMDKILQSssSDASIMVTNDGATILKSIGVD----NPAAKVLVDMSKVQDDEVG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 86 DGTTTATVLTQAIVNEGMKNVTAGANPVGIRRGIEKATAAAVAELKTMSHD-----VKTKDDIAQIASISAANPEVGQLi 160
Cdd:TIGR02341 88 DGTTSVTVLAAELLREAEKLINQKIHPQTIIAGYREATKAARDALLKSAVDngsdeVKFRQDLMNIARTTLSSKILSQH- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 161 ADAMEKVGNDGVITIEDSrgvdTSVDVVEGMSFDRGYMSqymvtdndkmEANLDNPYVLitDKKIANIQdilpllQSVVQ 240
Cdd:TIGR02341 167 KDHFAQLAVDAVLRLKGS----GNLEAIQIIKKLGGSLA----------DSYLDEGFLL--DKKIGVNQ------PKRIE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 241 EGRALLIIADDITGEALPTLVLNKIRGTFNVVAVKAPGfGDRRKAQLEDIAVLTGGTVISDDL----GMQL-KDATIDQL 315
Cdd:TIGR02341 225 NAKILIANTGMDTDKVKIFGSRVRVDSTAKVAELEHAE-KEKMKEKVEKILKHGINCFINRQLiynyPEQLfADAGVMAI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 316 GSANKVTVTKdnTTIVDGaGDKAAIADRVEQIK----KAIAETSsdFDKEKLQERLAKLAGGVAVVKVGAATETELKERK 391
Cdd:TIGR02341 304 EHADFEGVER--LALVTG-GEIVSTFDHPELVKlgscDLIEEIM--IGEDKLLKFSGVKLGEACTIVLRGATQQILDEAE 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 392 YRIEDALNATRAAVQEG-FVPGGGTALVNVIPALEKVEAETTGDEQTGVKIVKAALEAPVRQIAENAGVEGSVIINQLK- 469
Cdd:TIGR02341 379 RSLHDALCVLSQTVKESrTVLGGGCSEMLMSKAVTQEAQRTPGKEALAVEAFARALRQLPTIIADNAGFDSAELVAQLRa 458
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518035950 470 ---NEQPGIGYNAAEDKFEDMVAAGIVDPTKVTRSALQNAASVSALLLTTEAVVADKPEPK 527
Cdd:TIGR02341 459 ahyNGNTTMGLDMNEGTIADMRQLGITESYKVKRAVVSSAAEAAEVILRVDNIIKAAPRKR 519
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
8-147 |
1.98e-15 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 78.92 E-value: 1.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 8 AEDARRAMLRGVDKLADTVKTTIGPKGRNVVLE-----QSYGSPTITNDGVTIAKNIELEdhfeNMGAKLVSEVASKTND 82
Cdd:PTZ00212 20 GETARLQSFVGAIAVADLVKTTLGPKGMDKILQpmsegPRSGNVTVTNDGATILKSVWLD----NPAAKILVDISKTQDE 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 83 IAGDGTTTATVLTQAIVNEGMKNVTAGANPVGIRRGIEKATAAAVAELKTMSHDV-----KTKDDIAQIA 147
Cdd:PTZ00212 96 EVGDGTTSVVVLAGELLREAEKLLDQKIHPQTIIEGWRMALDVARKALEEIAFDHgsdeeKFKEDLLNIA 165
|
|
| TCP1_epsilon |
cd03339 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ... |
9-521 |
4.00e-15 |
|
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: 78.11 E-value: 4.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 9 EDARRAMLRGVD----------KLADTVKTTIGPKGRNVVLEQSYGSPTITNDGVTIAKNIELEDHFenmgAKLVSEVAS 78
Cdd:cd03339 12 EQEKKKRLKGLEahkshilaakSVANILRTSLGPRGMDKILVSPDGEVTVTNDGATILEKMDVDHQI----AKLLVELSK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 79 KTNDIAGDGTTTATVLTQAIVNEGMKNVTAGANPVGIRRGIEKATAAAVAELKTMSHDVKTKDDIAQIAsISAANPEVGQ 158
Cdd:cd03339 88 SQDDEIGDGTTGVVVLAGALLEQAEKLLDRGIHPIRIADGYEQACKIAVEHLEEIADKIEFSPDNKEPL-IQTAMTSLGS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 159 LIA----DAMEKVGNDGVITIEDSRGVDTSVDVVEGMSFDRGYMSQYM-----VTDND----KMEANLDNPYVLI----- 220
Cdd:cd03339 167 KIVsrchRQFAEIAVDAVLSVADLERKDVNFELIKVEGKVGGRLEDTKlvkgiVIDKDfshpQMPKEVKDAKIAIltcpf 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 221 ------TDKK--IANIQDILPL-----------LQSVVQEGRALLIIA---DDitgEALPTLVLNkirgtfNVVAVKAPG 278
Cdd:cd03339 247 eppkpkTKHKldITSVEDYKKLqeyeqkyfremVEQVKDAGANLVICQwgfDD---EANHLLLQN------GLPAVRWVG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 279 fgdrrKAQLEDIAVLTGGTVISddlgmQLKDATIDQLGSANKV-----TVTKDNTTIVDGAGDKAAIADRVEQIKKAIAE 353
Cdd:cd03339 318 -----GVEIELIAIATGGRIVP-----RFEDLSPEKLGKAGLVreisfGTTKDKMLVIEGCPNSKAVTIFIRGGNKMIIE 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 354 tssdfdkeklqerlaklaggvavvkvgaatetelkERKYRIEDALNATRAAVQEG-FVPGGGTALVNVIPALEKVEAETT 432
Cdd:cd03339 388 -----------------------------------EAKRSLHDALCVVRNLIRDNrIVYGGGAAEISCSLAVEKAADKCS 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 433 GDEQTGVKIVKAALEAPVRQIAENAGVE-----GSVIINQLKNEQPGIGYNAAEDKFEDMVAAGIVDPTKVTRSALQNAA 507
Cdd:cd03339 433 GIEQYAMRAFADALESIPLALAENSGLNpietlSEVKARQVKEKNPHLGIDCLGRGTNDMKEQKVFETLISKKQQILLAT 512
|
570
....*....|....
gi 518035950 508 SVSALLLTTEAVVA 521
Cdd:cd03339 513 QVVKMILKIDDVIV 526
|
|
| chap_CCT_theta |
TIGR02346 |
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ... |
22-524 |
5.79e-15 |
|
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: 77.45 E-value: 5.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 22 LADTVKTTIGPKGRNVVLEQSYGSPTITNDGVTIAKNIELEdhfeNMGAKLVSEVASKTNDIAGDGTTTATVLTQAIVNE 101
Cdd:TIGR02346 30 LSQITRTSLGPNGMNKMVINHLEKLFVTNDAATILRELEVQ----HPAAKLLVMASEMQENEIGDGTNLVLVLAGELLNK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 102 GMKNVTAGANPVGIRRGIEKATAAAVAELKTMS----HDVKTKDDIAQIASISAANPEVG------QLIADAM-----EK 166
Cdd:TIGR02346 106 AEELIRMGLHPSEIIKGYEMALKKAMEILEELVvwevKDLRDKDELIKALKASISSKQYGnedflaQLVAQACstvlpKN 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 167 VGNDGVITIEDSRGVDTSV---DVVEGMSFDRGYMSQYMVTDNDKM---EANLDNPyvlITDKK----IANIQDIL---- 232
Cdd:TIGR02346 186 PQNFNVDNIRVCKILGGSLsnsEVLKGMVFNREAEGSVKSVKNAKVavfSCPLDTA---TTETKgtvlIHNAEELLnysk 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 233 ---PLLQSVVQEgralliIADD-----ITGEALPTLVLNKIRgTFNVVAVKAPGfgdrrKAQLEDIAVLTGGTVIsddlg 304
Cdd:TIGR02346 263 geeNQIEAMIKA------IADSgvnviVTGGSVGDMALHYLN-KYNIMVLKIPS-----KFELRRLCKTVGATPL----- 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 305 MQLKDATIDQLGSANKVTVTkdnttivDGAGDKAAIADRVEQIKKaiaetssdfdkeklqerlaklaggVAVVKVGAATE 384
Cdd:TIGR02346 326 PRLGAPTPEEIGYVDSVYVS-------EIGGDKVTVFKQENGDSK------------------------ISTIILRGSTD 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 385 TELKERKYRIEDALNATRAAVQEG-FVPGGGTALVNVIPALEKVEAETTGDEQTGVKIVKAALEAPVRQIAENAGVEGSV 463
Cdd:TIGR02346 375 NLLDDIERAIDDGVNTVKALVKDGrLLPGAGATEIELASRLTKYGEKLPGLDQYAIKKFAEAFEIIPRTLAENAGLNANE 454
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518035950 464 IINQL------KNEQPGIGYNAAEDKFEDMVAAGIVDPTKVTRSALQNAASVSALLLTTEAVVADKP 524
Cdd:TIGR02346 455 VIPKLyaahkkGNKSKGIDIEAESDGVKDASEAGIYDMLATKKWAIKLATEAAVTVLRVDQIIMAKP 521
|
|
| chap_CCT_gamma |
TIGR02344 |
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ... |
22-521 |
1.90e-11 |
|
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: 66.30 E-value: 1.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 22 LADTVKTTIGPKGRNVVLEQSYGSPTITNDGVTIAKNIELEdhfeNMGAKLVSEVASKTNDIAGDGTTTATVLTQAIVNE 101
Cdd:TIGR02344 28 VADIIRTCLGPRSMLKMLLDPMGGIVMTNDGNAILREIDVA----HPAAKSMIELSRTQDEEVGDGTTSVIILAGEMLSV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 102 GMKNVTAGANPVGIRRGIEKATAAAVAELKTMSHDVKTKDDIAQIASISAA---------NPEVGQLIADAMEKVGND-- 170
Cdd:TIGR02344 104 AEPFLEQNIHPTVIIRAYRKALDDALSVLEEISIPVDVNDDAAMLKLIQSCigtkfvsrwSDLMCDLALDAVRTVQRDen 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 171 GVITIEDSRGVdtSVDVVEGMSFD-----RGYMSQYMVTdNDKMEANLDNPYVLITD-----KK--------IANIQDIL 232
Cdd:TIGR02344 184 GRKEIDIKRYA--KVEKIPGGDIEdscvlKGVMINKDVT-HPKMRRYIENPRIVLLDcpleyKKgesqtnieITKEEDWN 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 233 PLLQsvvQEGRALLIIADDItgealptlvlnkirgtfnvVAVKApgfgdrrkaqleDIAVLTGGtvISDDLGMQLKDATI 312
Cdd:TIGR02344 261 RILQ---MEEEYVQLMCEDI-------------------IAVKP------------DLVITEKG--VSDLAQHYLLKANI 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 313 dqlgSANKVTVTKDNTTIVDGAGdkAAIADRVEQIK-KAIAETSSDFDKEKLQERL------AKLAGGVAVVKVGAATET 385
Cdd:TIGR02344 305 ----TAIRRVRKTDNNRIARACG--ATIVNRPEELReSDVGTGCGLFEVKKIGDEYftfiteCKDPKACTILLRGASKDI 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 386 eLKERKYRIEDALNATRAAVQEG-FVPGGGTALVNVIPALEKVEAETTGDEQTGVKIVKAALEAPVRQIAENAGVEGSVI 464
Cdd:TIGR02344 379 -LNEVERNLQDAMAVARNVLLDPkLVPGGGATEMAVSVALTEKSKKLEGVEQWPYRAVADALEIIPRTLAQNCGANVIRT 457
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518035950 465 INQL--KNEQPG---IGYNAAEDKFEDMVAAGIVDPTKVTRSALQNAASVSALLLTTEAVVA 521
Cdd:TIGR02344 458 LTELraKHAQENnctWGIDGETGKIVDMKEKGIWEPLAVKLQTYKTAIESACLLLRIDDIVS 519
|
|
| chap_CCT_alpha |
TIGR02340 |
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ... |
9-528 |
6.45e-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: 64.74 E-value: 6.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 9 EDARRAMLRGVDKLADTVKTTIGPKGRNVVLEQSYGSPTITNDGVTIAKNIELEDHfenmGAKLVSEVASKTNDIAGDGT 88
Cdd:TIGR02340 11 QDVRTQNVTAAMAIANIVKTSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHP----AAKILVELAQLQDREVGDGT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 89 TTATVLTQAIVNEGMKNVTAGANPVGIRRGIEKATAAAVAEL-KTMSHDVKT--KDDIAQIASISAANPEVG-------Q 158
Cdd:TIGR02340 87 TSVVIIAAELLKRADELVKNKIHPTSVISGYRLACKEAVKYIkENLSVSVDElgREALINVAKTSMSSKIIGldsdffsN 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 159 LIADAMEKVgndgviTIEDSRGVDT----SVDVVE--GMS-----FDRGYMSQYMVTDNdKMEANLDNPYVLITDkkiAN 227
Cdd:TIGR02340 167 IVVDAVLAV------KTTNENGETKypikAINILKahGKSaresmLVKGYALNCTVASQ-QMPKRIKNAKIACLD---FN 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 228 IQDI-LPL-LQSVVQEGRALLIIAD---DITGEALPTLvlnkIRGTFNVVA-------------VKAPGFGDRR--KAQL 287
Cdd:TIGR02340 237 LQKAkMALgVQIVVDDPEKLEQIRQreaDITKERIKKI----LDAGANVVLttggiddmclkyfVEAGAMGVRRckKEDL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 288 EDIAVLTGGTVISDDLGMQlKDATID--QLGSANKVTVTK---DNTTIVDGAGDKAAiadrveqikkaiaetssdfdkek 362
Cdd:TIGR02340 313 KRIAKATGATLVSTLADLE-GEETFEasYLGFADEVVQERiadDECILIKGTKKRKS----------------------- 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 363 lqerlaklaggvAVVKVGAATETELKERKYRIEDALNATRAAVQEG-FVPGGGTALVNVIPALEKVEAETTGDEQTGVKI 441
Cdd:TIGR02340 369 ------------ASIILRGANDFMLDEMERSLHDALCVVKRTLESNsVVPGGGAVEAALSIYLENFATTLGSREQLAIAE 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 442 VKAALEAPVRQIAENAGVEGSVII---------NQLKNEQPG---IGYNAAEDKFEDMVAAGIVDPTKVTRSALQNAASV 509
Cdd:TIGR02340 437 FARALLIIPKTLAVNAAKDSTELVaklrayhaaAQLKPEKKHlkwYGLDLVNGKIRDNKEAGVLEPTVSKVKSLKFATEA 516
|
570
....*....|....*....
gi 518035950 510 SALLLTTEAVVADKPEPKD 528
Cdd:TIGR02340 517 AITILRIDDLIKLNPEQSK 535
|
|
| TCP1_zeta |
cd03342 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
22-517 |
2.88e-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: 62.66 E-value: 2.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 22 LADTVKTTIGPKGRNVVLEQSYGSPTITNDGVTIAKNIeledHFENMGAKLVSEVASKTNDIAGDGTTTATVLTQAIVNE 101
Cdd:cd03342 24 LQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLSEM----QIQHPTASMIARAATAQDDITGDGTTSNVLLIGELLKQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 102 GMKNVTAGANPVGIRRGIEKATAAAVAELKTMSHDVKTKDDIAQIASI--SAANPEVGQLIADAMEKVGNDGVITIEDSr 179
Cdd:cd03342 100 AERYIQEGVHPRIITEGFELAKNKALKFLESFKVPVEIDTDRELLLSVarTSLRTKLHADLADQLTEIVVDAVLAIYKP- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 180 gvDTSVDV--VEGMSFDRGYMSQY-----MVTD----NDKMEANLDNPYVLIT------DKKIANIQdilpLLQSVV--Q 240
Cdd:cd03342 179 --DEPIDLhmVEIMQMQHKSDSDTklirgLVLDhgarHPDMPKRVENAYILTCnvsleyEKTEVNSG----FFYSVVinQ 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 241 EGralliiaddITGEALPTLVLNKIrgtfnvVAVkapgfgdRR--KAQLEDIAVLTGGTVISddlgmQLKDATIDQLGSA 318
Cdd:cd03342 253 KG---------IDPPSLDMLAKEGI------LAL-------RRakRRNMERLTLACGGVAMN-----SVDDLSPECLGYA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 319 NKVTVTK---DNTTIVDGAGD--------KAAIADRVEQIKKAIaetssdfdkeklqerlaklAGGVAVVKVGaatetel 387
Cdd:cd03342 306 GLVYERTlgeEKYTFIEGVKNpksctiliKGPNDHTITQIKDAI-------------------RDGLRAVKNA------- 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 388 kerkyrIEDalnatraavqEGFVPGGGTALVNVIPALEKVEAETTGDEQTGVKIVKAALEAPVRQIAENAGVEGSVIINQ 467
Cdd:cd03342 360 ------IED----------KCVVPGAGAFEVALYAHLKEFKKSVKGKAKLGVQAFADALLVIPKTLAENSGLDVQETLVK 423
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 518035950 468 LKNE----QPGIGYNAAEDKFEDMVAAGIVDPTKVTRSALQNAASV-SALLLTTE 517
Cdd:cd03342 424 LQDEyaegGQVGGVDLDTGEPMDPESEGIWDNYSVKRQILHSATVIaSQLLLVDE 478
|
|
| TCP1_alpha |
cd03335 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ... |
9-167 |
1.88e-09 |
|
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: 59.99 E-value: 1.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 9 EDARRAMLRGVDKLADTVKTTIGPKGRNVVLEQSYGSPTITNDGVTIAKNIELEDHfenmGAKLVSEVASKTNDIAGDGT 88
Cdd:cd03335 7 QDVRTQNVTAAMAIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHP----AAKILVELAQLQDKEVGDGT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 89 TTATVLTQAIVNEGMKNVTAGANPVGIRRGIEKATAAAVAELK-TMSHDVKT--KDDIAQIA--SISA----ANPEV-GQ 158
Cdd:cd03335 83 TSVVIIAAELLKRANELVKQKIHPTTIISGYRLACKEAVKYIKeHLSISVDNlgKESLINVAktSMSSkiigADSDFfAN 162
|
....*....
gi 518035950 159 LIADAMEKV 167
Cdd:cd03335 163 MVVDAILAV 171
|
|
| TCP1_gamma |
cd03337 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ... |
22-520 |
2.86e-09 |
|
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: 59.23 E-value: 2.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 22 LADTVKTTIGPKGRNVVLEQSYGSPTITNDGVTIAKNIELEdhfeNMGAKLVSEVASKTNDIAGDGTTTATVLTQAIVNE 101
Cdd:cd03337 28 VADVIRTCLGPRAMLKMLLDPMGGIVLTNDGNAILREIDVA----HPAAKSMIELSRTQDEEVGDGTTSVIILAGEILAV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 102 GMKNVTAGANPVGIRRGIEKATAAAVAELKTMSHDVKTKDD--IAQIASISAANPEVGQLiADAMEKVGNDGVITIE-DS 178
Cdd:cd03337 104 AEPFLERGIHPTVIIKAYRKALEDALKILEEISIPVDVNDRaqMLKIIKSCIGTKFVSRW-SDLMCNLALDAVKTVAvEE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 179 RGVDTSVDVVEGMSFDR---GYMSQYMVTD---------NDKMEANLDNP----------YVLITDKKIANiqdilpLLQ 236
Cdd:cd03337 183 NGRKKEIDIKRYAKVEKipgGEIEDSRVLDgvmlnkdvtHPKMRRRIENPrivlldcpleYLVITEKGVSD------LAQ 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 237 SVVQEGralliiadDITgealptlVLNKIRGTFNvvavkapgfgdRRkaqledIAVLTGGTVISDDLGMQLKDatidqlg 316
Cdd:cd03337 257 HYLVKA--------GIT-------ALRRVRKTDN-----------NR------IARACGATIVNRPEELTESD------- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 317 sankvtvtkdnttIVDGAGdkaaiadrVEQIKKAIAETSSDFDKEklqerlaKLAGGVAVVKVGAATETeLKERKYRIED 396
Cdd:cd03337 298 -------------VGTGAG--------LFEVKKIGDEYFTFITEC-------KDPKACTILLRGASKDV-LNEVERNLQD 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 397 ALNATRAAVQEG-FVPGGGTALVNVIPALEKVEAETTGDEQTGVKIVKAALEAPVRQIAENAGVEGSVIINQLK-----N 470
Cdd:cd03337 349 AMAVARNIILNPkLVPGGGATEMAVSHALSEKAKSIEGVEQWPYKAVASALEVIPRTLAQNCGANVIRTLTELRakhaqG 428
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 518035950 471 EQPGIGYNAAEDKFEDMVAAGIVDPTKVTRSALQNAASVSALLLTTEAVV 520
Cdd:cd03337 429 ENSTWGIDGETGDIVDMKELGIWDPLAVKAQTYKTAIEAACMLLRIDDIV 478
|
|
| chap_CCT_zeta |
TIGR02347 |
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ... |
8-220 |
1.36e-06 |
|
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT zeta chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.
Pssm-ID: 274088 [Multi-domain] Cd Length: 531 Bit Score: 50.89 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 8 AEDARRAM-----LRGVDKLADTVKTTIGPKGRNVVLEQSYGSPTITNDGVTIAKNIeledHFENMGAKLVSEVASKTND 82
Cdd:TIGR02347 9 AESLRRDAalmmnINAARGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEM----QIQHPTASMIARAATAQDD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518035950 83 IAGDGTTTATVLTQAIVNEGMKNVTAGANPVGIRRGIEKATAAA---VAELKTMSHDVKTKDDIAQIASiSAANPEVGQL 159
Cdd:TIGR02347 85 ITGDGTTSTVLLIGELLKQAERYILEGVHPRIITEGFEIARKEAlqfLDKFKVKKEDEVDREFLLNVAR-TSLRTKLPAD 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518035950 160 IADAMEKVGNDGVITIEDS---------------RGVDTSVDVVEGMSFDRGymsqymvTDNDKMEANLDNPYVLI 220
Cdd:TIGR02347 164 LADQLTEIVVDAVLAIKKDgedidlfmveimemkHKSATDTTLIRGLVLDHG-------ARHPDMPRRVKNAYILT 232
|
|
| |
