|
Name |
Accession |
Description |
Interval |
E-value |
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
1-525 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 993.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 1 MAKEIKFSEEARRAMLRGVDALADAVKVTLGPKGRNVVLEKKFGSPLITNDGVTIAKEIELEDAFENMGAKLVAEVASKT 80
Cdd:PRK00013 1 MAKDIKFGEDARRKLLRGVNKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDPFENMGAQLVKEVASKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 81 NDVAGDGTTTATVLAQAMIREGLKNVTAGANPVGVRKGMEQAVAVAIENLKEISKPIEGKESIAQVAAISA-ADEEVGSL 159
Cdd:PRK00013 81 NDVAGDGTTTATVLAQAIVREGLKNVAAGANPMDLKRGIDKAVEAAVEELKKISKPVEDKEEIAQVATISAnGDEEIGKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 160 IAEAMERVGNDGVITIEESKGFTTELEVVEGMQFDRGYASPYMVTDSDKMEAVLDNPYILITDKKITNIQEILPVLEQVV 239
Cdd:PRK00013 161 IAEAMEKVGKEGVITVEESKGFETELEVVEGMQFDRGYLSPYFVTDPEKMEAELENPYILITDKKISNIQDLLPVLEQVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 240 QQGKPLLLIAEDVEGEALATLVVNKLRGTFNAVAVKAPGFGDRRKAMLEDIAVLTGGEVITEDLGLDLKSTQIAQLGRAS 319
Cdd:PRK00013 241 QSGKPLLIIAEDVEGEALATLVVNKLRGTLKVVAVKAPGFGDRRKAMLEDIAILTGGTVISEELGLKLEDATLEDLGQAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 320 KVVVTKENTTIVEGAGETDKISARVTQIRAQVEETTSEFDREKLQERLAKLAGGVAVIKVGAATETELKERKLRIEDALN 399
Cdd:PRK00013 321 KVVVTKDNTTIVDGAGDKEAIKARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATEVEMKEKKDRVEDALH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 400 STRAAVEEGIVSGGGTALVNVYNKVAAVE-AEGDAQTGINIVLRALEEPIRQIAHNAGLEGSVIVERLKNEE-IGVGFNA 477
Cdd:PRK00013 401 ATRAAVEEGIVPGGGVALLRAAPALEALKgLNGDEATGINIVLRALEAPLRQIAENAGLEGSVVVEKVKNGKgKGYGYNA 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 16077670 478 ATGEWVNMIEKGIVDPTKVTRSALQNAASVAAMFLTTEAVVADKPEEN 525
Cdd:PRK00013 481 ATGEYVDMIEAGIIDPTKVTRSALQNAASVAGLLLTTEAVVADKPEKK 528
|
|
| GroEL |
cd03344 |
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ... |
3-520 |
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: 889.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 3 KEIKFSEEARRAMLRGVDALADAVKVTLGPKGRNVVLEKKFGSPLITNDGVTIAKEIELEDAFENMGAKLVAEVASKTND 82
Cdd:cd03344 1 KDIKFGEEARKALLRGVNKLADAVKVTLGPKGRNVVIEKSFGSPKITKDGVTVAKEIELEDPFENMGAQLVKEVASKTND 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 83 VAGDGTTTATVLAQAMIREGLKNVTAGANPVGVRKGMEQAVAVAIENLKEISKPIEGKESIAQVAAISA-ADEEVGSLIA 161
Cdd:cd03344 81 VAGDGTTTATVLARAIIKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKPVKTKEEIAQVATISAnGDEEIGELIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 162 EAMERVGNDGVITIEESKGFTTELEVVEGMQFDRGYASPYMVTDSDKMEAVLDNPYILITDKKITNIQEILPVLEQVVQQ 241
Cdd:cd03344 161 EAMEKVGKDGVITVEEGKTLETELEVVEGMQFDRGYLSPYFVTDPEKMEVELENPYILLTDKKISSIQELLPILELVAKA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 242 GKPLLLIAEDVEGEALATLVVNKLRGTFNAVAVKAPGFGDRRKAMLEDIAVLTGGEVITEDLGLDLKSTQIAQLGRASKV 321
Cdd:cd03344 241 GRPLLIIAEDVEGEALATLVVNKLRGGLKVCAVKAPGFGDRRKAMLEDIAILTGGTVISEELGLKLEDVTLEDLGRAKKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 322 VVTKENTTIVEGAGETDKISARVTQIRAQVEETTSEFDREKLQERLAKLAGGVAVIKVGAATETELKERKLRIEDALNST 401
Cdd:cd03344 321 VVTKDDTTIIGGAGDKAAIKARIAQIRKQIEETTSDYDKEKLQERLAKLSGGVAVIKVGGATEVELKEKKDRVEDALNAT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 402 RAAVEEGIVSGGGTALVNVYNKVAAVEAE-GDAQTGINIVLRALEEPIRQIAHNAGLEGSVIVERLKNEEIGVGFNAATG 480
Cdd:cd03344 401 RAAVEEGIVPGGGVALLRASPALDKLKALnGDEKLGIEIVRRALEAPLRQIAENAGVDGSVVVEKVLESPDGFGYDAATG 480
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 16077670 481 EWVNMIEKGIVDPTKVTRSALQNAASVAAMFLTTEAVVAD 520
Cdd:cd03344 481 EYVDMIEAGIIDPTKVVRSALQNAASVASLLLTTEALVVD 520
|
|
| groEL |
PRK12849 |
chaperonin GroEL; Reviewed |
1-524 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237230 Cd Length: 542 Bit Score: 877.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 1 MAKEIKFSEEARRAMLRGVDALADAVKVTLGPKGRNVVLEKKFGSPLITNDGVTIAKEIELEDAFENMGAKLVAEVASKT 80
Cdd:PRK12849 1 MAKIIKFDEEARRALERGVNKLADAVKVTLGPKGRNVVIDKSFGAPTITKDGVSIAKEIELEDPFENLGAQLVKEVASKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 81 NDVAGDGTTTATVLAQAMIREGLKNVTAGANPVGVRKGMEQAVAVAIENLKEISKPIEGKESIAQVAAISA-ADEEVGSL 159
Cdd:PRK12849 81 NDVAGDGTTTATVLAQALVQEGLKNVAAGANPMDLKRGIDKAVEAVVEELKALARPVSGSEEIAQVATISAnGDEEIGEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 160 IAEAMERVGNDGVITIEESKGFTTELEVVEGMQFDRGYASPYMVTDSDKMEAVLDNPYILITDKKITNIQEILPVLEQVV 239
Cdd:PRK12849 161 IAEAMEKVGKDGVITVEESKTLETELEVTEGMQFDRGYLSPYFVTDPERMEAVLEDPLILLTDKKISSLQDLLPLLEKVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 240 QQGKPLLLIAEDVEGEALATLVVNKLRGTFNAVAVKAPGFGDRRKAMLEDIAVLTGGEVITEDLGLDLKSTQIAQLGRAS 319
Cdd:PRK12849 241 QSGKPLLIIAEDVEGEALATLVVNKLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGLKLEEVTLDDLGRAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 320 KVVVTKENTTIVEGAGETDKISARVTQIRAQVEETTSEFDREKLQERLAKLAGGVAVIKVGAATETELKERKLRIEDALN 399
Cdd:PRK12849 321 RVTITKDNTTIVDGAGDKEAIEARVAQIRRQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATEVELKERKDRVEDALN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 400 STRAAVEEGIVSGGGTALVNVYNKVAAVE-AEGDAQTGINIVLRALEEPIRQIAHNAGLEGSVIVERLKNEEIGVGFNAA 478
Cdd:PRK12849 401 ATRAAVEEGIVPGGGVALLRAAKALDELAgLNGDQAAGVEIVRRALEAPLRQIAENAGLDGSVVVAKVLELEDGFGFNAA 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 16077670 479 TGEWVNMIEKGIVDPTKVTRSALQNAASVAAMFLTTEAVVADKPEE 524
Cdd:PRK12849 481 TGEYGDLIAAGIIDPVKVTRSALQNAASVAGLLLTTEALVADKPEE 526
|
|
| 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: 867.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 2 AKEIKFSEEARRAMLRGVDALADAVKVTLGPKGRNVVLEKKFGSPLITNDGVTIAKEIELEDAFENMGAKLVAEVASKTN 81
Cdd:TIGR02348 1 AKQIKFDEEARKALLRGVDKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDKFENMGAQLVKEVASKTN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 82 DVAGDGTTTATVLAQAMIREGLKNVTAGANPVGVRKGMEQAVAVAIENLKEISKPIEGKESIAQVAAISA-ADEEVGSLI 160
Cdd:TIGR02348 81 DVAGDGTTTATVLAQAIVKEGLKNVAAGANPIELKRGIEKAVEAVVEELKKLSKPVKGKKEIAQVATISAnNDEEIGSLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 161 AEAMERVGNDGVITIEESKGFTTELEVVEGMQFDRGYASPYMVTDSDKMEAVLDNPYILITDKKITNIQEILPVLEQVVQ 240
Cdd:TIGR02348 161 AEAMEKVGKDGVITVEESKSLETELEVVEGMQFDRGYISPYFVTDAEKMEVELENPYILITDKKISNIKDLLPLLEKVAQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 241 QGKPLLLIAEDVEGEALATLVVNKLRGTFNAVAVKAPGFGDRRKAMLEDIAVLTGGEVITEDLGLDLKSTQIAQLGRASK 320
Cdd:TIGR02348 241 SGKPLLIIAEDVEGEALATLVVNKLRGTLNVCAVKAPGFGDRRKAMLEDIAILTGGQVISEELGLKLEEVTLDDLGKAKK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 321 VVVTKENTTIVEGAGETDKISARVTQIRAQVEETTSEFDREKLQERLAKLAGGVAVIKVGAATETELKERKLRIEDALNS 400
Cdd:TIGR02348 321 VTVDKDNTTIVEGAGDKAAIKARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATETEMKEKKLRIEDALNA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 401 TRAAVEEGIVSGGGTALVNVYNKVAAVEAEG-DAQTGINIVLRALEEPIRQIAHNAGLEGSVIVERLKNEEIGVGFNAAT 479
Cdd:TIGR02348 401 TRAAVEEGIVPGGGVALLRAAAALEGLKGDGeDEAIGIDIVKRALEAPLRQIAENAGLDGAVVAEKVKELKGNFGFNAAT 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 16077670 480 GEWVNMIEKGIVDPTKVTRSALQNAASVAAMFLTTEAVVADKPE 523
Cdd:TIGR02348 481 GEYEDLVEAGIIDPTKVTRSALQNAASIAGLLLTTEAVVADKPE 524
|
|
| groEL |
PRK12850 |
chaperonin GroEL; Reviewed |
1-525 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237231 Cd Length: 544 Bit Score: 818.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 1 MAKEIKFSEEARRAMLRGVDALADAVKVTLGPKGRNVVLEKKFGSPLITNDGVTIAKEIELEDAFENMGAKLVAEVASKT 80
Cdd:PRK12850 2 AAKEIRFSTDARDRLLRGVNILANAVKVTLGPKGRNVVLEKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVKEVASKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 81 NDVAGDGTTTATVLAQAMIREGLKNVTAGANPVGVRKGMEQAVAVAIENLKEISKPIEGKESIAQVAAISA-ADEEVGSL 159
Cdd:PRK12850 82 NDLAGDGTTTATVLAQAIVREGAKLVAAGMNPMDLKRGIDLAVAAVVDELKKIAKKVTSSKEIAQVATISAnGDESIGEM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 160 IAEAMERVGNDGVITIEESKGFTTELEVVEGMQFDRGYASPYMVTDSDKMEAVLDNPYILITDKKITNIQEILPVLEQVV 239
Cdd:PRK12850 162 IAEAMDKVGKEGVITVEEAKTLGTELDVVEGMQFDRGYLSPYFVTNPEKMRAELEDPYILLHEKKISNLQDLLPILEAVV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 240 QQGKPLLLIAEDVEGEALATLVVNKLRGTFNAVAVKAPGFGDRRKAMLEDIAVLTGGEVITEDLGLDLKSTQIAQLGRAS 319
Cdd:PRK12850 242 QSGRPLLIIAEDVEGEALATLVVNKLRGGLKSVAVKAPGFGDRRKAMLEDIAVLTGGQVISEDLGIKLENVTLDMLGRAK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 320 KVVVTKENTTIVEGAGETDKISARVTQIRAQVEETTSEFDREKLQERLAKLAGGVAVIKVGAATETELKERKLRIEDALN 399
Cdd:PRK12850 322 RVLITKENTTIIDGAGDKKNIEARVKQIRAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKEKKDRVDDALH 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 400 STRAAVEEGIVSGGGTALVNVYNKVAAVE-AEGDAQTGINIVLRALEEPIRQIAHNAGLEGSVIVERLKNEEIGVGFNAA 478
Cdd:PRK12850 402 ATRAAVEEGIVPGGGVALLRARSALRGLKgANADETAGIDIVRRALEEPLRQIATNAGFEGSVVVGKVAELPGNFGFNAQ 481
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 16077670 479 TGEWVNMIEKGIVDPTKVTRSALQNAASVAAMFLTTEAVVADKPEEN 525
Cdd:PRK12850 482 TGEYGDMVEAGIIDPAKVTRTALQDAASIAALLITTEAMVAEAPKKA 528
|
|
| GroEL |
COG0459 |
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ... |
1-525 |
0e+00 |
|
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227 Cd Length: 497 Bit Score: 787.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 1 MAKEIKFSEEARRAMLRGVDALADAVKVTLGPKGRNVVLEKKFGSPLITNDGVTIAKEIELEDAFENMGAKLVAEVASKT 80
Cdd:COG0459 1 MAKQILFGEDARRANIRGVKALADAVKVTLGPKGRNVMLVKSFGDPTITNDGVTIAKEIELEDPFENMGAQLVKEVASKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 81 NDVAGDGTTTATVLAQAMIREGLKNVTAGANPVGVRKGMEQAVAVAIENLKEISKPIEGKESIAQVAAISAA-DEEVGSL 159
Cdd:COG0459 81 NDEAGDGTTTATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPVDDKEELAQVATISANgDEEIGEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 160 IAEAMERVGNDGVITIEESKGFTTELEVVEGMQFDRGYASPYMVTDSDKMEAVLDNPYILITDKKITNIQEILPVLEQVV 239
Cdd:COG0459 161 IAEAMEKVGKDGVITVEEGKGLETELEVVEGMQFDKGYLSPYFVTDPEKMPAELENAYILLTDKKISSIQDLLPLLEKVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 240 QQGKPLLLIAEDVEGEALATLVVNKLRGTFNAVAVKAPGFGDRRKAMLEDIAVLTGGEVITEDLGLDLKSTQIAQLGRAS 319
Cdd:COG0459 241 QSGKPLLIIAEDIDGEALATLVVNGIRGVLRVVAVKAPGFGDRRKAMLEDIAILTGGRVISEDLGLKLEDVTLDDLGRAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 320 KVVVTKENTTIVEGAGETDKIsarvtqiraqveettsefdreklqerlaklaggvaVIKVGAATETELKERKLRIEDALN 399
Cdd:COG0459 321 RVEVDKDNTTIVEGAGNPKAI-----------------------------------VILVGAATEVEVKERKRRVEDALH 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 400 STRAAVEEGIVSGGGTALVNVYNKVA--AVEAEGDAQTGINIVLRALEEPIRQIAHNAGLEGSVIVERLKN-EEIGVGFN 476
Cdd:COG0459 366 ATRAAVEEGIVPGGGAALLRAARALRelAAKLEGDEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKVRAaKDKGFGFD 445
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 16077670 477 AATGEWVNMIEKGIVDPTKVTRSALQNAASVAAMFLTTEAVVADKPEEN 525
Cdd:COG0459 446 AATGEYVDMLEAGVIDPAKVKRSALQNAASVAGLILTTEAVIADKPEKE 494
|
|
| groEL |
PRK12851 |
chaperonin GroEL; Reviewed |
1-525 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 171770 Cd Length: 541 Bit Score: 759.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 1 MAKEIKFSEEARRAMLRGVDALADAVKVTLGPKGRNVVLEKKFGSPLITNDGVTIAKEIELEDAFENMGAKLVAEVASKT 80
Cdd:PRK12851 2 AAKEVKFHVEAREKMLRGVNILADAVKVTLGPKGRNVVIDKSFGAPTITNDGVTIAKEIELEDKFENMGAQMVREVASKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 81 NDVAGDGTTTATVLAQAMIREGLKNVTAGANPVGVRKGMEQAVAVAIENLKEISKPIEGKESIAQVAAISA-ADEEVGSL 159
Cdd:PRK12851 82 NDVAGDGTTTATVLAQAIVREGAKAVAAGANPMDLKRGIDRAVAAVVEELKANARPVTTNAEIAQVATISAnGDAEIGRL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 160 IAEAMERVGNDGVITIEESKGFTTELEVVEGMQFDRGYASPYMVTDSDKMEAVLDNPYILITDKKITNIQEILPVLEQVV 239
Cdd:PRK12851 162 VAEAMEKVGNEGVITVEESKTAETELEVVEGMQFDRGYLSPYFVTDADKMEAELEDPYILIHEKKISNLQDLLPVLEAVV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 240 QQGKPLLLIAEDVEGEALATLVVNKLRGTFNAVAVKAPGFGDRRKAMLEDIAVLTGGEVITEDLGLDLKSTQIAQLGRAS 319
Cdd:PRK12851 242 QSGKPLLIIAEDVEGEALATLVVNKLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGIKLENVTLEQLGRAK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 320 KVVVTKENTTIVEGAGETDKISARVTQIRAQVEETTSEFDREKLQERLAKLAGGVAVIKVGAATETELKERKLRIEDALN 399
Cdd:PRK12851 322 KVVVEKENTTIIDGAGSKTEIEGRVAQIRAQIEETTSDYDREKLQERLAKLAGGVAVIRVGASTEVEVKEKKDRVDDALH 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 400 STRAAVEEGIVSGGGTALVNVYNKVAAVE-AEGDAQTGINIVLRALEEPIRQIAHNAGLEGSVIVERLKNEEIGVGFNAA 478
Cdd:PRK12851 402 ATRAAVEEGIVPGGGVALLRAVKALDKLEtANGDQRTGVEIVRRALEAPVRQIAENAGAEGSVVVGKLREKPGGYGFNAA 481
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 16077670 479 TGEWVNMIEKGIVDPTKVTRSALQNAASVAAMFLTTEAVVADKPEEN 525
Cdd:PRK12851 482 TNEYGDLYAQGVIDPVKVVRTALQNAASVAGLLLTTEAMVAEKPKKE 528
|
|
| groEL |
CHL00093 |
chaperonin GroEL |
1-525 |
0e+00 |
|
chaperonin GroEL
Pssm-ID: 177025 Cd Length: 529 Bit Score: 736.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 1 MAKEIKFSEEARRAMLRGVDALADAVKVTLGPKGRNVVLEKKFGSPLITNDGVTIAKEIELEDAFENMGAKLVAEVASKT 80
Cdd:CHL00093 1 MSKKILYQDNARRALERGMDILAEAVSVTLGPKGRNVVLEKKYGSPQIVNDGVTIAKEIELEDHIENTGVALIRQAASKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 81 NDVAGDGTTTATVLAQAMIREGLKNVTAGANPVGVRKGMEQAVAVAIENLKEISKPIEGKESIAQVAAISAA-DEEVGSL 159
Cdd:CHL00093 81 NDVAGDGTTTATVLAYAIVKQGMKNVAAGANPISLKRGIEKATQYVVSQIAEYARPVEDIQAITQVASISAGnDEEVGSM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 160 IAEAMERVGNDGVITIEESKGFTTELEVVEGMQFDRGYASPYMVTDSDKMEAVLDNPYILITDKKITNI-QEILPVLEQV 238
Cdd:CHL00093 161 IADAIEKVGREGVISLEEGKSTVTELEITEGMRFEKGFISPYFVTDTERMEVVQENPYILLTDKKITLVqQDLLPILEQV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 239 VQQGKPLLLIAEDVEGEALATLVVNKLRGTFNAVAVKAPGFGDRRKAMLEDIAVLTGGEVITEDLGLDLKSTQIAQLGRA 318
Cdd:CHL00093 241 TKTKRPLLIIAEDVEKEALATLVLNKLRGIVNVVAVRAPGFGDRRKAMLEDIAILTGGQVITEDAGLSLETIQLDLLGQA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 319 SKVVVTKENTTIVeGAGETDKISARVTQIRAQVEETTSEFDREKLQERLAKLAGGVAVIKVGAATETELKERKLRIEDAL 398
Cdd:CHL00093 321 RRIIVTKDSTTII-ADGNEEQVKARCEQLRKQIEIADSSYEKEKLQERLAKLSGGVAVIKVGAATETEMKDKKLRLEDAI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 399 NSTRAAVEEGIVSGGGTALVNVYNKV---AAVEAEGDAQTGINIVLRALEEPIRQIAHNAGLEGSVIVERLKNEEIGVGF 475
Cdd:CHL00093 400 NATKAAVEEGIVPGGGATLVHLSENLktwAKNNLKEDELIGALIVARAILAPLKRIAENAGKNGSVIIEKVQEQDFEIGY 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 16077670 476 NAATGEWVNMIEKGIVDPTKVTRSALQNAASVAAMFLTTEAVVADKPEEN 525
Cdd:CHL00093 480 NAANNKFVNMYEAGIIDPAKVTRSALQNAASIASMILTTECIIVDKKESS 529
|
|
| groEL |
PRK12852 |
chaperonin GroEL; Reviewed |
1-525 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237232 Cd Length: 545 Bit Score: 708.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 1 MAKEIKFSEEARRAMLRGVDALADAVKVTLGPKGRNVVLEKKFGSPLITNDGVTIAKEIELEDAFENMGAKLVAEVASKT 80
Cdd:PRK12852 2 AAKDVKFSGDARDRMLRGVDILANAVKVTLGPKGRNVVIEKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVREVASKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 81 NDVAGDGTTTATVLAQAMIREGLKNVTAGANPVGVRKGMEQAVAVAIENLKEISKPIEGKESIAQVAAISA-ADEEVGSL 159
Cdd:PRK12852 82 NDLAGDGTTTATVLAQAIVREGAKAVAAGMNPMDLKRGIDIAVAAVVKDIEKRAKPVASSAEIAQVGTISAnGDAAIGKM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 160 IAEAMERVGNDGVITIEESKGFTTELEVVEGMQFDRGYASPYMVTDSDKMEAVLDNPYILITDKKITNIQEILPVLEQVV 239
Cdd:PRK12852 162 IAQAMQKVGNEGVITVEENKSLETEVDIVEGMKFDRGYLSPYFVTNAEKMTVELDDAYILLHEKKLSGLQAMLPVLEAVV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 240 QQGKPLLLIAEDVEGEALATLVVNKLRGTFNAVAVKAPGFGDRRKAMLEDIAVLTGGEVITEDLGLDLKSTQIAQLGRAS 319
Cdd:PRK12852 242 QSGKPLLIIAEDVEGEALATLVVNRLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGQLISEDLGIKLENVTLKMLGRAK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 320 KVVVTKENTTIVEGAGETDKISARVTQIRAQVEETTSEFDREKLQERLAKLAGGVAVIKVGAATETELKERKLRIEDALN 399
Cdd:PRK12852 322 KVVIDKENTTIVNGAGKKADIEARVGQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKEKKDRVEDALN 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 400 STRAAVEEGIVSGGGTALVNVYNKVAAVE-AEGDAQTGINIVLRALEEPIRQIAHNAGLEGSVIVER-LKNEEIGVGFNA 477
Cdd:PRK12852 402 ATRAAVQEGIVPGGGVALLRAKKAVGRINnDNADVQAGINIVLKALEAPIRQIAENAGVEGSIVVGKiLENKSETFGFDA 481
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 16077670 478 ATGEWVNMIEKGIVDPTKVTRSALQNAASVAAMFLTTEAVVADKPEEN 525
Cdd:PRK12852 482 QTEEYVDMVAKGIIDPAKVVRTALQDAASVAGLLVTTEAMVAELPKKD 529
|
|
| PTZ00114 |
PTZ00114 |
Heat shock protein 60; Provisional |
2-524 |
0e+00 |
|
Heat shock protein 60; Provisional
Pssm-ID: 185455 Cd Length: 555 Bit Score: 707.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 2 AKEIKFSEEARRAMLRGVDALADAVKVTLGPKGRNVVLEKKFGSPLITNDGVTIAKEIELEDAFENMGAKLVAEVASKTN 81
Cdd:PTZ00114 14 GKEIRFGDEARQSLLKGIERLADAVAVTLGPKGRNVIIEQEYGSPKITKDGVTVAKAIEFSDRFENVGAQLIRQVASKTN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 82 DVAGDGTTTATVLAQAMIREGLKNVTAGANPVGVRKGMEQAVAVAIENLKEISKPIEGKESIAQVAAISA-ADEEVGSLI 160
Cdd:PTZ00114 94 DKAGDGTTTATILARAIFREGCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQSRPVKTKEDILNVATISAnGDVEIGSLI 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 161 AEAMERVGNDGVITIEESKGFTTELEVVEGMQFDRGYASPYMVTDSDKMEAVLDNPYILITDKKITNIQEILPVLEQVVQ 240
Cdd:PTZ00114 174 ADAMDKVGKDGTITVEDGKTLEDELEVVEGMSFDRGYISPYFVTNEKTQKVELENPLILVTDKKISSIQSILPILEHAVK 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 241 QGKPLLLIAEDVEGEALATLVVNKLRGTFNAVAVKAPGFGDRRKAMLEDIAVLTGGEVITED-LGLDLKSTQIAQLGRAS 319
Cdd:PTZ00114 254 NKRPLLIIAEDVEGEALQTLIINKLRGGLKVCAVKAPGFGDNRKDILQDIAVLTGATVVSEDnVGLKLDDFDPSMLGSAK 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 320 KVVVTKENTTIVEGAGETDKISARVTQIRAQVEETTSEFDREKLQERLAKLAGGVAVIKVGAATETELKERKLRIEDALN 399
Cdd:PTZ00114 334 KVTVTKDETVILTGGGDKAEIKERVELLRSQIERTTSEYDKEKLKERLAKLSGGVAVIKVGGASEVEVNEKKDRIEDALN 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 400 STRAAVEEGIVSGGGTALVNVYNKVAAVE----AEGDAQTGINIVLRALEEPIRQIAHNAGLEGSVIVER-LKNEEIGVG 474
Cdd:PTZ00114 414 ATRAAVEEGIVPGGGVALLRASKLLDKLEedneLTPDQRTGVKIVRNALRLPTKQIAENAGVEGAVVVEKiLEKKDPSFG 493
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 16077670 475 FNAATGEWVNMIEKGIVDPTKVTRSALQNAASVAAMFLTTEAVVADKPEE 524
Cdd:PTZ00114 494 YDAQTGEYVNMFEAGIIDPTKVVRSALVDAASVASLMLTTEAAIVDLPKE 543
|
|
| PRK14104 |
PRK14104 |
chaperonin GroEL; Provisional |
2-525 |
0e+00 |
|
chaperonin GroEL; Provisional
Pssm-ID: 172594 Cd Length: 546 Bit Score: 621.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 2 AKEIKFSEEARRAMLRGVDALADAVKVTLGPKGRNVVLEKKFGSPLITNDGVTIAKEIELEDAFENMGAKLVAEVASKTN 81
Cdd:PRK14104 3 AKEVKFGVDARDRMLRGVDILANAVKVTLGPKGRNVVLDKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVREVASKSA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 82 DVAGDGTTTATVLAQAMIREGLKNVTAGANPVGVRKGMEQAVAVAIENLKEISKPIEGKESIAQVAAISA-ADEEVGSLI 160
Cdd:PRK14104 83 DAAGDGTTTATVLAQAIVREGAKSVAAGMNPMDLKRGIDLAVEAVVADLVKNSKKVTSNDEIAQVGTISAnGDAEIGKFL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 161 AEAMERVGNDGVITIEESKGFTTELEVVEGMQFDRGYASPYMVTDSDKMEAVLDNPYILITDKKITNIQEILPVLEQVVQ 240
Cdd:PRK14104 163 ADAMKKVGNEGVITVEEAKSLETELDVVEGMQFDRGYISPYFVTNADKMRVEMDDAYILINEKKLSSLNELLPLLEAVVQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 241 QGKPLLLIAEDVEGEALATLVVNKLRGTFNAVAVKAPGFGDRRKAMLEDIAVLTGGEVITEDLGLDLKSTQIAQLGRASK 320
Cdd:PRK14104 243 TGKPLVIVAEDVEGEALATLVVNRLRGGLKVAAVKAPGFGDRRKAMLQDIAILTGGQAISEDLGIKLENVTLQMLGRAKK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 321 VVVTKENTTIVEGAGETDKISARVTQIRAQVEETTSEFDREKLQERLAKLAGGVAVIKVGAATETELKERKLRIEDALNS 400
Cdd:PRK14104 323 VMIDKENTTIVNGAGKKADIEARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKERKDRVDDAMHA 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 401 TRAAVEEGIVSGGGTALVNVYNKVAAVEAEGDAQ-TGINIVLRALEEPIRQIAHNAGLEGSVIVER-LKNEEIGVGFNAA 478
Cdd:PRK14104 403 TRAAVEEGIVPGGGVALLRASEQLKGIKTKNDDQkTGVEIVRKALSAPARQIAINAGEDGSVIVGKiLEKEQYSYGFDSQ 482
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 16077670 479 TGEWVNMIEKGIVDPTKVTRSALQNAASVAAMFLTTEAVVADKPEEN 525
Cdd:PRK14104 483 TGEYGNLVSKGIIDPTKVVRTAIQNAASVAALLITTEAMVAELPKKG 529
|
|
| PLN03167 |
PLN03167 |
Chaperonin-60 beta subunit; Provisional |
2-523 |
0e+00 |
|
Chaperonin-60 beta subunit; Provisional
Pssm-ID: 215611 [Multi-domain] Cd Length: 600 Bit Score: 553.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 2 AKEIKFSEE--ARRAMLRGVDALADAVKVTLGPKGRNVVLEKKFGSPLITNDGVTIAKEIELEDAFENMGAKLVAEVASK 79
Cdd:PLN03167 56 AKELHFNKDgsAIKKLQAGVNKLADLVGVTLGPKGRNVVLESKYGSPKIVNDGVTVAKEVELEDPVENIGAKLVRQAAAK 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 80 TNDVAGDGTTTATVLAQAMIREGLKNVTAGANPVGVRKGMEQAVAVAIENLKEISKPIEGKEsIAQVAAISAADE-EVGS 158
Cdd:PLN03167 136 TNDLAGDGTTTSVVLAQGLIAEGVKVVAAGANPVQITRGIEKTAKALVKELKKMSKEVEDSE-LADVAAVSAGNNyEVGN 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 159 LIAEAMERVGNDGVITIEESKGFTTELEVVEGMQFDRGYASPYMVTDSDKMEAVLDNPYILITDKKITNIQEILPVLEQV 238
Cdd:PLN03167 215 MIAEAMSKVGRKGVVTLEEGKSAENNLYVVEGMQFDRGYISPYFVTDSEKMSVEYDNCKLLLVDKKITNARDLIGILEDA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 239 VQQGKPLLLIAEDVEGEALATLVVNKLRGTFNAVAVKAPGFGDRRKAMLEDIAVLTGGEVITEDLGLDLKSTQIAQLGRA 318
Cdd:PLN03167 295 IRGGYPLLIIAEDIEQEALATLVVNKLRGSLKIAALKAPGFGERKSQYLDDIAILTGGTVIREEVGLSLDKVGKEVLGTA 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 319 SKVVVTKENTTIVEGAGETDKISARVTQIRAQVEETTSEFDREKLQERLAKLAGGVAVIKVGAATETELKERKLRIEDAL 398
Cdd:PLN03167 375 AKVVLTKDTTTIVGDGSTQEAVNKRVAQIKNLIEAAEQDYEKEKLNERIAKLSGGVAVIQVGAQTETELKEKKLRVEDAL 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 399 NSTRAAVEEGIVSGGGTALVNVYNKVAAVEA--EGDAQ-TGINIVLRALEEPIRQIAHNAGLEGSVIVER-LKNEEIGVG 474
Cdd:PLN03167 455 NATKAAVEEGIVVGGGCTLLRLASKVDAIKDtlENDEQkVGADIVKRALSYPLKLIAKNAGVNGSVVSEKvLSNDNPKFG 534
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 16077670 475 FNAATGEWVNMIEKGIVDPTKVTRSALQNAASVAAMFLTTEAVVADKPE 523
Cdd:PLN03167 535 YNAATGKYEDLMAAGIIDPTKVVRCCLEHAASVAKTFLTSDCVVVEIKE 583
|
|
| chaperonin_type_I_II |
cd00309 |
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ... |
3-519 |
1.47e-158 |
|
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: 459.97 E-value: 1.47e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 3 KEIKFSEEARRAMLRGVDALADAVKVTLGPKGRNVVLEKKFGSPLITNDGVTIAKEIELEdafeNMGAKLVAEVASKTND 82
Cdd:cd00309 1 KEREFGEEARLSNINAAKALADAVKTTLGPKGMDKMLVDSLGDPTITNDGATILKEIEVE----HPAAKLLVEVAKSQDD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 83 VAGDGTTTATVLAQAMIREGLKNVTAGANPVGVRKGMEQAVAVAIENLKEISKPIE--GKESIAQVAAISAA-------D 153
Cdd:cd00309 77 EVGDGTTTVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVPIDveDREELLKVATTSLNsklvsggD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 154 EEVGSLIAEAMERVG------NDGVITIEESKGFT-TELEVVEGMQFDRGYASPYmvtdsdkMEAVLDNPYILITDKKit 226
Cdd:cd00309 157 DFLGELVVDAVLKVGkengdvDLGVIRVEKKKGGSlEDSELVVGMVFDKGYLSPY-------MPKRLENAKILLLDCK-- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 227 niqeilpvLEQVVqqgkplllIAED-VEGEALATLVVNklrgtfNAVAVKApgfgdRRKAMLEDIAVLTGGEVITEdlgl 305
Cdd:cd00309 228 --------LEYVV--------IAEKgIDDEALHYLAKL------GIMAVRR-----VRKEDLERIAKATGATIVSR---- 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 306 dLKSTQIAQLGRASKVVVTK----ENTTIVEGAGetdkisarvtqiraqveettsefdreklqerlaklaGGVAVIKVGA 381
Cdd:cd00309 277 -LEDLTPEDLGTAGLVEETKigdeKYTFIEGCKG------------------------------------GKVATILLRG 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 382 ATETELKERKLRIEDALNSTRAAVEE-GIVSGGGTALVNVYNKVA--AVEAEGDAQTGINIVLRALEEPIRQIAHNAGLE 458
Cdd:cd00309 320 ATEVELDEAERSLHDALCAVRAAVEDgGIVPGGGAAEIELSKALEelAKTLPGKEQLGIEAFADALEVIPRTLAENAGLD 399
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16077670 459 GSVIVERLKNEEIGVGFNAA----TGEWVNMIEKGIVDPTKVTRSALQNAASVAAMFLTTEAVVA 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 |
4.44e-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: 287.56 E-value: 4.44e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 22 LADAVKVTLGPKGRNVVLEKKFGSPLITNDGVTIAKEIELEDAfenmGAKLVAEVASKTNDVAGDGTTTATVLAQAMIRE 101
Cdd:pfam00118 1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELEIQHP----AAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 102 GLKNVTAGANPVGVRKGMEQAVAVAIENLKE---ISKPIEGKESIAQVAAISAA-------DEEVGSLIAEAMER----- 166
Cdd:pfam00118 77 AEKLLAAGVHPTTIIEGYEKALEKALEILDSiisIPVEDVDREDLLKVARTSLSskiisreSDFLAKLVVDAVLAipknd 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 167 ----VGNDGVITIEESKGftTELEVVEGMQFDRGYASPYMVTDsdkmeavLDNPYILITDKKITNIQE------------ 230
Cdd:pfam00118 157 gsfdLGNIGVVKILGGSL--EDSELVDGVVLDKGPLHPDMPKR-------LENAKVLLLNCSLEYEKTetkatvvlsdae 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 231 ------------ILPVLEQVVQQGKPLLLIAEDVEGEALATLVVNKLRGTFNAvavkapgfgdrRKAMLEDIAVLTGGEV 298
Cdd:pfam00118 228 qlerflkaeeeqILEIVEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMALRRV-----------KKRDLERLAKATGARA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 299 ITEDLGLDLKstqiaQLGRASKV---VVTKENTTIVEGAGEtdkisarvtqiraqveettsefdreklqerlaklaGGVA 375
Cdd:pfam00118 297 VSSLDDLTPD-----DLGTAGKVeeeKIGDEKYTFIEGCKS-----------------------------------PKAA 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 376 VIKVGAATETELKERKLRIEDALNSTRAAVEE-GIVSGGGTALVNVYNKVA--AVEAEGDAQTGINIVLRALEEPIRQIA 452
Cdd:pfam00118 337 TILLRGATDHVLDEIERSIHDALCVVKNAIEDpRVVPGGGAVEMELARALReyAKSVSGKEQLAIEAFAEALEVIPKTLA 416
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16077670 453 HNAGLEGSVIVERLKNE----EIGVGFNAATGEWVNMIEKGIVDPTKVTRSALQNAASVAAMFLTTEAVVADK 521
Cdd:pfam00118 417 ENAGLDPIEVLAELRAAhasgEKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKSATEAASTILRIDDIIKAK 489
|
|
| chaperonin_like |
cd03333 |
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ... |
140-407 |
4.37e-41 |
|
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: 147.23 E-value: 4.37e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 140 KESIAQVAAISAA------DEEVGSLIAEAMERVG------NDGVITIEESKGFT-TELEVVEGMQFDRGYASPYmvtds 206
Cdd:cd03333 1 RELLLQVATTSLNsklsswDDFLGKLVVDAVLKVGpdnrmdDLGVIKVEKIPGGSlEDSELVVGVVFDKGYASPY----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 207 dkMEAVLDNPYILITDKKitniqeilpvLEQVVqqgkplllIAED-VEGEALATLVVNklrgtfNAVAVKApgfgdRRKA 285
Cdd:cd03333 76 --MPKRLENAKILLLDCP----------LEYVV--------IAEKgIDDLALHYLAKA------GIMAVRR-----VKKE 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 286 MLEDIAVLTGGEVITEDLGLDLkstqiAQLGRASKVVVTK---ENTTIVEGAGEtdkisarvtqiraqveettsefdrek 362
Cdd:cd03333 125 DLERIARATGATIVSSLEDLTP-----EDLGTAELVEETKigeEKLTFIEGCKG-------------------------- 173
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 16077670 363 lqerlaklaGGVAVIKVGAATETELKERKLRIEDALNSTRAAVEE 407
Cdd:cd03333 174 ---------GKAATILLRGATEVELDEVKRSLHDALCAVRAAVEE 209
|
|
| thermosome_beta |
NF041083 |
thermosome subunit beta; |
10-521 |
3.14e-33 |
|
thermosome subunit beta;
Pssm-ID: 469010 Cd Length: 519 Bit Score: 132.77 E-value: 3.14e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 10 EARRAMLRGVDALADAVKVTLGPKGRNVVLEKKFGSPLITNDGVTIAKEIELedafENMGAKLVAEVASKTNDVAGDGTT 89
Cdd:NF041083 17 DAQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDIVITNDGATILKEMDV----QHPAAKMLVEVAKTQDDEVGDGTT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 90 TATVLAQAMIREGLKNVTAGANPVGVRKGMEQAVAVAIENLKEISKPI--EGKESIAQVA-------AISAADEEVGSLI 160
Cdd:NF041083 93 TAVVLAGELLKKAEELLDQNIHPTIIANGYRLAAEKAIEILDEIAEKVdpDDRETLKKIAetsltskGVEEARDYLAEIA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 161 AEAMERVGN----------DGVITIEESKGFTTELEVVEGMQFDRGYASPymvtdsdKMEAVLDNPYILITDKKItNIQE 230
Cdd:NF041083 173 VKAVKQVAEkrdgkyyvdlDNIQIEKKHGGSIEDTQLIYGIVIDKEVVHP-------GMPKRVENAKIALLDAPL-EVKK 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 231 ilPVLEQVVQQGKPLLLIAEDVEGEALATLVVNKLRGTFNAVAVKAPGFGD--------------RR--KAMLEDIAVLT 294
Cdd:NF041083 245 --TEIDAEIRITDPDQLQKFLDQEEKMLKEMVDKIKATGANVVFCQKGIDDlaqhylakagilavRRvkKSDMEKLAKAT 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 295 GGEVITedlglDLKSTQIAQLGRASKV---VVTKENTTIVEGAGETDKISarvTQIRAQVEETTSEFDREklqerlakla 371
Cdd:NF041083 323 GARIVT-----NIDDLTPEDLGYAELVeerKVGDDKMVFVEGCKNPKAVT---ILIRGGTEHVVDEAERA---------- 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 372 ggvavikvgaatetelkerklrIEDALNSTRAAVEEG-IVSGGGTALVNVYNKVA--AVEAEGDAQTGINIVLRALEEPI 448
Cdd:NF041083 385 ----------------------LEDALSVVADAVEDGkIVAGGGAPEVELAKRLReyAATVGGREQLAVEAFAEALEIIP 442
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16077670 449 RQIAHNAGLEGSVIVERL----KNEEIGVGFNAATGEWVNMIEKGIVDPTKVTRSALQNAASVAAMFLTTEAVVADK 521
Cdd:NF041083 443 RTLAENAGLDPIDILVKLrsahEKGKKWAGINVFTGEVVDMWELGVIEPLRVKTQAIKSATEAATMILRIDDVIAAK 519
|
|
| cpn60 |
cd03343 |
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ... |
9-519 |
3.85e-33 |
|
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: 132.39 E-value: 3.85e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 9 EEARRAMLRGVDALADAVKVTLGPKGRNVVLEKKFGSPLITNDGVTIAKEIELedafENMGAKLVAEVASKTNDVAGDGT 88
Cdd:cd03343 14 RDAQRMNIAAAKAVAEAVRTTLGPKGMDKMLVDSLGDVTITNDGATILKEMDI----EHPAAKMLVEVAKTQDEEVGDGT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 89 TTATVLAQAMIREGLKNVTAGANPVGVRKGMEQAVAVAIENLKEISKPIEGKE-----SIAQVAAISAADEEVGSLIAE- 162
Cdd:cd03343 90 TTAVVLAGELLEKAEDLLDQNIHPTVIIEGYRLAAEKALELLDEIAIKVDPDDkdtlrKIAKTSLTGKGAEAAKDKLADl 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 163 ------AMERVGNDGV------ITIEESKGFTTE-LEVVEGMQFDRGYASPymvtdsdKMEAVLDNPYILITDK------ 223
Cdd:cd03343 170 vvdavlQVAEKRDGKYvvdldnIKIEKKTGGSVDdTELIRGIVIDKEVVHP-------GMPKRVENAKIALLDAplevkk 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 224 -------KITNIQEILPVLEQVVQQGKPLLliaeDVEGEALATLVVNKlRGTFNAVA---VKAPGFGDRR--KAMLEDIA 291
Cdd:cd03343 243 teidakiRITSPDQLQAFLEQEEAMLKEMV----DKIADTGANVVFCQ-KGIDDLAQhylAKAGILAVRRvkKSDMEKLA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 292 VLTGGEVITEDlgLDLKSTQIAQLGRASKVVVTKENTTIVEGAGETDKISarvTQIRAQVEETTSEFDREklqerlakla 371
Cdd:cd03343 318 RATGAKIVTNI--DDLTPEDLGEAELVEERKVGDDKMVFVEGCKNPKAVT---ILLRGGTEHVVDELERA---------- 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 372 ggvavikvgaatetelkerklrIEDALNSTRAAVEEG-IVSGGGTALVNVYNKVA--AVEAEGDAQTGINIVLRALEEPI 448
Cdd:cd03343 383 ----------------------LEDALRVVADALEDGkVVAGGGAVEIELAKRLReyARSVGGREQLAVEAFADALEEIP 440
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16077670 449 RQIAHNAGLEG-SVIVE---RLKNEEIGVGFNAATGEWVNMIEKGIVDPTKVTRSALQNAASVAAMFLTTEAVVA 519
Cdd:cd03343 441 RTLAENAGLDPiDTLVElraAHEKGNKNAGLDVYTGEVVDMLEKGVIEPLRVKKQAIKSATEAATMILRIDDVIA 515
|
|
| thermosome_alpha |
NF041082 |
thermosome subunit alpha; |
10-519 |
5.38e-31 |
|
thermosome subunit alpha;
Pssm-ID: 469009 Cd Length: 518 Bit Score: 126.15 E-value: 5.38e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 10 EARRAMLRGVDALADAVKVTLGPKGRNVVLEKKFGSPLITNDGVTIAKEIELedafENMGAKLVAEVASKTNDVAGDGTT 89
Cdd:NF041082 17 DAQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDVVITNDGVTILKEMDI----EHPAAKMIVEVAKTQDDEVGDGTT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 90 TATVLAQAMIREGLKNVTAGANPVGVRKGMEQAVAVAIENLKEISKPI--EGKESIAQVAA-------ISAADEEVGSLI 160
Cdd:NF041082 93 TAVVLAGELLKKAEELLDQDIHPTIIAEGYRLAAEKALEILDEIAIKVdpDDKETLKKIAAtamtgkgAEAAKDKLADLV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 161 AEA----MERVGNDGV----ITIEESKGFTTE-LEVVEGMQFDRGYASPYMVTDSDKME-AVLDNPYIL----ITDK-KI 225
Cdd:NF041082 173 VDAvkavAEKDGGYNVdldnIKVEKKVGGSIEdSELVEGVVIDKERVHPGMPKRVENAKiALLDAPLEVkkteIDAKiSI 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 226 TNIQEILPVLEQVVQQGKPLlliaedvegealatlvVNKLRGTFNAVAVKAPGFGD--------------RR--KAMLED 289
Cdd:NF041082 253 TDPDQLQAFLDQEEKMLKEM----------------VDKIADSGANVVFCQKGIDDlaqhylakegilavRRvkKSDMEK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 290 IAVLTGGEVITedlglDLKSTQIAQLGRASKVV---VTKENTTIVEGAGETDKISarvtqiraqveettsefdreklqer 366
Cdd:NF041082 317 LAKATGARIVT-----SIDDLSPEDLGYAGLVEerkVGGDKMIFVEGCKNPKAVT------------------------- 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 367 laklaggvavIKVGAATETELKERKLRIEDALNSTRAAVEEG-IVSGGGTALVNVYNKVA--AVEAEGDAQTGINIVLRA 443
Cdd:NF041082 367 ----------ILLRGGTEHVVDEVERALEDALRVVRVVLEDGkVVAGGGAPEVELALRLReyAASVGGREQLAIEAFAEA 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 444 LEEPIRQIAHNAGLEGSVIVERLKNE----EIGVGFNAATGEWVNMIEKGIVDPTKVTRSALQNAASVAAMFLTTEAVVA 519
Cdd:NF041082 437 LEIIPRTLAENAGLDPIDALVELRSAhekgNKTAGLDVYTGKVVDMLEIGVVEPLRVKTQAIKSATEAAVMILRIDDVIA 516
|
|
| TCP1_delta |
cd03338 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ... |
21-512 |
2.34e-21 |
|
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: 97.36 E-value: 2.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 21 ALADAVKVTLGPKGRNVVLEKKFGSPLITNDGVTIAKEIELEDAfenmGAKLVAEVaSKTNDV-AGDGTTTATVLAQAMI 99
Cdd:cd03338 19 AVADAIRTSLGPRGMDKMIQTGKGEVIITNDGATILKQMSVLHP----AAKMLVEL-SKAQDIeAGDGTTSVVVLAGALL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 100 REGLKNVTAGANPVGVRKGMEQAVAVAIENLKEISKPIE--GKESIAQVAAISAADEEV---GSLIAE----AMERVGND 170
Cdd:cd03338 94 SACESLLKKGIHPTVISESFQIAAKKAVEILDSMSIPVDlnDRESLIKSATTSLNSKVVsqySSLLAPiavdAVLKVIDP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 171 GV--------ITIEESKGFTTE-LEVVEGMQFDRGYAS------------------------PYM-----VTDSDKMEAV 212
Cdd:cd03338 174 ATatnvdlkdIRIVKKLGGTIEdTELVDGLVFTQKASKkaggptriekakigliqfclsppkTDMdnnivVNDYAQMDRI 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 213 L--DNPYILITDKKItniqeilpvleqvVQQGKPLLLIAEDVEGEALATLvvnklrgtfnavavkAPGFGDRRKAML--- 287
Cdd:cd03338 254 LreERKYILNMCKKI-------------KKSGCNVLLIQKSILRDAVSDL---------------ALHFLAKLKIMVvkd 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 288 ---EDIavltggEVITEDLGldlkstqiaqlgraSKVVVTKENTTivegageTDKISARVTqiraqVEETTSEFDREKLQ 364
Cdd:cd03338 306 ierEEI------EFICKTIG--------------CKPVASIDHFT-------EDKLGSADL-----VEEVSLGDGKIVKI 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 365 ERLAKLAGGVAVIkVGAATETELKERKLRIEDALNSTRAAVEE-GIVSGGGTALVNVYNKVAaveAEGDAQTGIN-IVLR 442
Cdd:cd03338 354 TGVKNPGKTVTIL-VRGSNKLVLDEAERSLHDALCVIRCLVKKrALIPGGGAPEIEIALQLS---EWARTLTGVEqYCVR 429
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16077670 443 ALEEPIRQI----AHNAGLEGSVIVERLKNE----EIGVGFNAATGEWVNMIEKGIVDPTKVTRSALQNAASVAAMFL 512
Cdd:cd03338 430 AFADALEVIpytlAENAGLNPISIVTELRNRhaqgEKNAGINVRKGAITNILEENVVQPLLVSTSAITLATETVRMIL 507
|
|
| chap_CCT_epsi |
TIGR02343 |
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ... |
10-520 |
3.02e-21 |
|
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: 97.18 E-value: 3.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 10 EARRAMLRGVDALADAVKVTLGPKGRNVVLEKKFGSPLITNDGVTIAKEIELEdafeNMGAKLVAEVASKTNDVAGDGTT 89
Cdd:TIGR02343 27 EAKKSNIAAAKSVASILRTSLGPKGMDKMLISPDGDITVTNDGATILSQMDVD----NQIAKLMVELSKSQDDEIGDGTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 90 TATVLAQAMIREGLKNVTAGANPVGVRKGMEQAVAVAIENLKEISKPIEGKESIAQvAAISAADEEVGSLIA----EAME 165
Cdd:TIGR02343 103 GVVVLAGALLEQAEELLDKGIHPIKIADGFEEAARIAVEHLEEISDEISADNNNRE-PLIQAAKTSLGSKIVskchRRFA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 166 RVGNDGVITIE--------------ESK--GFTTELEVVEGMQFDRGYASPYMVTD-SDKMEAVLDNPY---ILITDKK- 224
Cdd:TIGR02343 182 EIAVDAVLNVAdmerrdvdfdlikvEGKvgGSLEDTKLIKGIIIDKDFSHPQMPKEvEDAKIAILTCPFeppKPKTKHKl 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 225 -ITNIQEILPVLEQVVQQGKPLLliaEDVEgEALATLVV---------NKLRGTFNAVAVKAPGFGDrrkamLEDIAVLT 294
Cdd:TIGR02343 262 dISSVEEYKKLQKYEQQKFKEMI---DDIK-KSGANLVIcqwgfddeaNHLLLQNDLPAVRWVGGQE-----LELIAIAT 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 295 GGEVIT--EDLGLDlkstqiaQLGRASKVV-----VTKENTTIVEGAGETDKISarvtqiraqveettsefdreklqerl 367
Cdd:TIGR02343 333 GGRIVPrfQELSKD-------KLGKAGLVReisfgTTKDRMLVIEQCKNSKAVT-------------------------- 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 368 aklaggvavIKVGAATETELKERKLRIEDALNSTRAAVEEG-IVSGGGTALVNVynkVAAVEAEGDAQTG-----INIVL 441
Cdd:TIGR02343 380 ---------IFIRGGNKMIIEEAKRSIHDALCVVRNLIKDSrIVYGGGAAEISC---SLAVSQEADKYPGveqyaIRAFA 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 442 RALEEPIRQIAHNAGL---EGSVIVERLKNEE----IGVGFNaatGEWVN-MIEKGIVDPTKVTRSALQNAASVAAMFLT 513
Cdd:TIGR02343 448 DALETIPMALAENSGLdpiGTLSTLKSLQLKEknpnLGVDCL---GYGTNdMKEQFVFETLIGKKQQILLATQLVRMILK 524
|
....*..
gi 16077670 514 TEAVVAD 520
Cdd:TIGR02343 525 IDDVISP 531
|
|
| TCP1_beta |
cd03336 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ... |
9-524 |
5.87e-19 |
|
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: 90.08 E-value: 5.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 9 EEARRAMLRGVDALADAVKVTLGPKGRNVVLE--KKFGSPLITNDGVTIAKEIELEdafeNMGAKLVAEVASKTNDVAGD 86
Cdd:cd03336 12 ETARLSSFVGAIAIGDLVKTTLGPKGMDKILQsvGRSGGVTVTNDGATILKSIGVD----NPAAKVLVDISKVQDDEVGD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 87 GTTTATVLAQAMIREGLKNVTAGANPVGVRKGMEQAVAVAIENLKEI-----SKPIEGKESIAQVAA-------ISAADE 154
Cdd:cd03336 88 GTTSVTVLAAELLREAEKLVAQKIHPQTIIEGYRMATAAAREALLSSavdhsSDEEAFREDLLNIARttlsskiLTQDKE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 155 EVGSLIAEAMERVGNDG----VITIEESKGFTTELEVVEGMQFDR--GYASPymvtdsdkmeAVLDNPYILI------TD 222
Cdd:cd03336 168 HFAELAVDAVLRLKGSGnldaIQIIKKLGGSLKDSYLDEGFLLDKkiGVNQP----------KRIENAKILIantpmdTD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 223 K-KI----------TNIQEIlPVLEQVVQQGKPLLLIAEDVEGEALATLVVNKLRGTFNAVAVKAPGFGDRrkAMLEDIA 291
Cdd:cd03336 238 KiKIfgakvrvdstAKVAEI-EEAEKEKMKNKVEKILKHGINCFINRQLIYNYPEQLFADAGIMAIEHADF--DGVERLA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 292 VLTGGEVITEdlgldLKSTQIAQLGRASKVvvtkENTTIVEgagetdkisarvtqiraqveettsefdrEKLQERLAKLA 371
Cdd:cd03336 315 LVTGGEIAST-----FDHPELVKLGTCKLI----EEIMIGE----------------------------DKLIRFSGVAA 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 372 GGVAVIKVGAATETELKERKLRIEDALNSTRAAVEEG-IVSGGGTALVNVYNKV--AAVEAEGDAQTGINIVLRALEEPI 448
Cdd:cd03336 358 GEACTIVLRGASQQILDEAERSLHDALCVLAQTVKDTrVVLGGGCSEMLMAKAVeeLAKKTPGKKSLAIEAFAKALRQLP 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 449 RQIAHNAGLEGSVIVERLK----NEEIGVGFNAATGEWVNMIEKGIVDPTKVTRSALQNAASVAAMFLTTEAVVADKPEE 524
Cdd:cd03336 438 TIIADNAGYDSAELVAQLRaahyNGNTTAGLDMRKGTVGDMKELGITESFKVKRQVLLSASEAAEMILRVDDIIKCAPRK 517
|
|
| chap_CCT_eta |
TIGR02345 |
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ... |
16-521 |
3.75e-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: 87.51 E-value: 3.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 16 LRGVDALADAVKVTLGPKGRNVVLEKKFGSPLITNDGVTIAKEIELedafENMGAKLVAEVASKTNDVAGDGTTTATVLA 95
Cdd:TIGR02345 24 INACVAIAEALKTTLGPRGMDKLIVGSNGKATISNDGATILKLLDI----VHPAAKTLVDIAKSQDAEVGDGTTSVTILA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 96 QAMIREGLKNVTAGANPVGVRKGMEQAVAVAIENLKEISKPI-----EGKESIAQVAA-------ISAADEEVGSLIAEA 163
Cdd:TIGR02345 100 GELLKEAKPFIEEGVHPQLIIRCYREALSLAVEKIKEIAVTIdeekgEQRELLEKCAAtalssklISHNKEFFSKMIVDA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 164 MERVGND----GVITIEESKGFT-TELEVVEGMQFDRG------------YASPYM-------------------VTDSD 207
Cdd:TIGR02345 180 VLSLDRDdldlKLIGIKKVQGGAlEDSQLVNGVAFKKTfsyagfeqqpkkFANPKIlllnvelelkaekdnaeirVEDVE 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 208 KMEAVLDNPYILITDKkitniqeilpvLEQVVQQGkpllliaedvegealATLVVNKLrgtfnavavkapGFGDRRKAML 287
Cdd:TIGR02345 260 DYQAIVDAEWAIIFRK-----------LEKIVESG---------------ANVVLSKL------------PIGDLATQYF 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 288 EDIAVLTGGEVITEDLGLDLKSTqiaqlgraskvvvtkenTTIVEGAgeTDKISARVTQIRAQVEETTSEFDREKLQERL 367
Cdd:TIGR02345 302 ADRDIFCAGRVSAEDLKRVIKAC-----------------GGSIQST--TSDLEADVLGTCALFEERQIGSERYNYFTGC 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 368 AKLAGGVAVIKVGAATETELKERKLriEDALNSTRAAVEEGIVSGGGTALVNVYNKV---AAVEAEGDAQTGINIVLRAL 444
Cdd:TIGR02345 363 PHAKTCTIILRGGAEQFIEEAERSL--HDAIMIVRRALKNKKIVAGGGAIEMELSKClrdYSKTIDGKQQLIINAFAKAL 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 445 EEPIRQIAHNAGLEGSVIVERLK----NEEIGVGFNAATGEWVNMIEKGIVDPTKVTRSALQNAASVAAMFLTTEAVVAD 520
Cdd:TIGR02345 441 EIIPRQLCENAGFDSIEILNKLRsrhaKGGKWYGVDINTEDIGDNFEAFVWEPALVKINALKAAFEAACTILSVDETITN 520
|
.
gi 16077670 521 K 521
Cdd:TIGR02345 521 P 521
|
|
| chap_CCT_delta |
TIGR02342 |
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ... |
9-519 |
2.61e-16 |
|
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: 81.75 E-value: 2.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 9 EEARRAMLRGVDALADAVKVTLGPKGRNVVLEKKFGSPLITNDGVTIAKEIELedafENMGAKLVAEVaSKTNDV-AGDG 87
Cdd:TIGR02342 8 QDVRTSNIVAAKAVADAIRTSLGPKGMDKMIQDGKGEVIITNDGATILKQMAV----LHPAAKMLVEL-SKAQDIeAGDG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 88 TTTATVLAQAMIREGLKNVTAGANPVGVRKGMEQAVAVAIENLKEISKPIEGKESIAQV-AAISAADEEVGSLIAEAMER 166
Cdd:TIGR02342 83 TTSVVILAGALLGACERLLNKGIHPTIISESFQSAADEAIKILDEMSIPVDLSDREQLLkSATTSLSSKVVSQYSSLLAP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 167 VGNDGVITIEESK-----------------GFTTELEVVEGMQFD------RGYAS------------------PYM--- 202
Cdd:TIGR02342 163 LAVDAVLKVIDPEnaknvdlndikvvkklgGTIDDTELIEGLVFTqkasksAGGPTriekakigliqfqisppkTDMenq 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 203 --VTDSDKMEAVLDNPYilitdkkitniQEILPVLEQVVQQGKPLLLIAEDVEGEALATLVVNKLrGTFNAVAVKAPgfg 280
Cdd:TIGR02342 243 iiVNDYAQMDRVLKEER-----------AYILNIVKKIKKTGCNVLLIQKSILRDAVNDLALHFL-AKMKIMVVKDI--- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 281 DRrkamlEDIavltggEVITEDLGL----DLKSTQIAQLGRASkvvvtkenttIVEGAGETDKISARVTQIRAqveetts 356
Cdd:TIGR02342 308 ER-----EEI------EFICKTIGCkpiaSIDHFTADKLGSAE----------LVEEVDSDGGKIIKITGIQN------- 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 357 efdreklqerlaklAGGVAVIKVGAATETELKERKLRIEDALNSTRAAVEE-GIVSGGGTALVNVYNKVA--AVEAEGDA 433
Cdd:TIGR02342 360 --------------AGKTVTVVVRGSNKLVIDEAERSLHDALCVIRCLVKKrGLIAGGGAPEIEIARRLSkyARTMKGVE 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 434 QTGINIVLRALEEPIRQIAHNAGLEGSVIVERLKNE----EIGVGFNAATGEWVNMIEKGIVDPTKVTRSALQNAASVAA 509
Cdd:TIGR02342 426 SYCVRAFADALEVIPYTLAENAGLNPIKVVTELRNRhangEKTAGISVRKGGITNMLEEHVLQPLLVTTSAITLASETVR 505
|
570
....*....|
gi 16077670 510 MFLTTEAVVA 519
Cdd:TIGR02342 506 SILKIDDIVF 515
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
9-134 |
3.50e-16 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 81.23 E-value: 3.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 9 EEARRAMLRGVDALADAVKVTLGPKGRNVVLEK-----KFGSPLITNDGVTIAKEIELEdafeNMGAKLVAEVASKTNDV 83
Cdd:PTZ00212 21 ETARLQSFVGAIAVADLVKTTLGPKGMDKILQPmsegpRSGNVTVTNDGATILKSVWLD----NPAAKILVDISKTQDEE 96
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 16077670 84 AGDGTTTATVLAQAMIREGLKNVTAGANPVGVRKGMEQAVAVAIENLKEIS 134
Cdd:PTZ00212 97 VGDGTTSVVVLAGELLREAEKLLDQKIHPQTIIEGWRMALDVARKALEEIA 147
|
|
| TCP1_epsilon |
cd03339 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ... |
9-147 |
5.20e-16 |
|
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.
Pssm-ID: 239455 Cd Length: 526 Bit Score: 80.81 E-value: 5.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 9 EEARRAMLRGVDA----------LADAVKVTLGPKGRNVVLEKKFGSPLITNDGVTIAKEIELEdafeNMGAKLVAEVAS 78
Cdd:cd03339 12 EQEKKKRLKGLEAhkshilaaksVANILRTSLGPRGMDKILVSPDGEVTVTNDGATILEKMDVD----HQIAKLLVELSK 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16077670 79 KTNDVAGDGTTTATVLAQAMIREGLKNVTAGANPVGVRKGMEQAVAVAIENLKEISKPIE----GKESIAQVA 147
Cdd:cd03339 88 SQDDEIGDGTTGVVVLAGALLEQAEKLLDRGIHPIRIADGYEQACKIAVEHLEEIADKIEfspdNKEPLIQTA 160
|
|
| TCP1_eta |
cd03340 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ... |
21-512 |
2.61e-15 |
|
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.
Pssm-ID: 239456 [Multi-domain] Cd Length: 522 Bit Score: 78.48 E-value: 2.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 21 ALADAVKVTLGPKGRNVVLEKKFGSPLITNDGVTIAKEIELEdafeNMGAKLVAEVASKTNDVAGDGTTTATVLAQAMIR 100
Cdd:cd03340 27 AIADAVRTTLGPRGMDKLIVDGRGKVTISNDGATILKLLDIV----HPAAKTLVDIAKSQDAEVGDGTTSVVVLAGEFLK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 101 EGLKNVTAGANPVGVRKGMEQAVAVAIENLKEISKPI------EGKESIAQVAA-------ISAADEEVGSLIAEAMERV 167
Cdd:cd03340 103 EAKPFIEDGVHPQIIIRGYRKALQLAIEKIKEIAVNIdkedkeEQRELLEKCAAtalnsklIASEKEFFAKMVVDAVLSL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 168 GND---GVITIEESKGFT-TELEVVEGMQFDRG------------YASPYM-------------------VTDSDKMEAV 212
Cdd:cd03340 183 DDDldlDMIGIKKVPGGSlEDSQLVNGVAFKKTfsyagfeqqpkkFKNPKIlllnvelelkaekdnaevrVEDPEEYQAI 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 213 LDNPYILITDKkitniqeilpvLEQVVQQGkpllliaedvegealATLVVNKLrgTFNAVAVKApgFGDRRkamlediaV 292
Cdd:cd03340 263 VDAEWKIIYDK-----------LEKIVKSG---------------ANVVLSKL--PIGDLATQY--FADRD--------I 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 293 LTGGEVITEDLGLDLKSTqiaqlgraskvvvtkenttiveGAgetdKISARVTQIRAQVEETTSEFDREKL-QERLAKLA 371
Cdd:cd03340 305 FCAGRVPEEDLKRVAQAT----------------------GG----SIQTTVSNITDDVLGTCGLFEERQVgGERYNIFT 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 372 GGVA------VIKVGAATETELKERKLriEDALNSTRAAVEEGIVSGGGTAL---VNVYNKVAAVEAEGDAQTGINIVLR 442
Cdd:cd03340 359 GCPKaktctiILRGGAEQFIEEAERSL--HDAIMIVRRAIKNDSVVAGGGAIemeLSKYLRDYSRTIAGKQQLVINAFAK 436
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16077670 443 ALEEPIRQIAHNAGLEGSVIVERL-----KNEEIGVGFNAATGEWVNMIEKGIVDPTKVTRSALQNAASVAAMFL 512
Cdd:cd03340 437 ALEIIPRQLCDNAGFDATDILNKLrqkhaQGGGKWYGVDINNEGIADNFEAFVWEPSLVKINALTAATEAACLIL 511
|
|
| chap_CCT_beta |
TIGR02341 |
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ... |
8-522 |
3.73e-14 |
|
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: 74.90 E-value: 3.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 8 SEEARRAMLRGVDALADAVKVTLGPKGRNVVLEK--KFGSPLITNDGVTIAKEIeledAFENMGAKLVAEVASKTNDVAG 85
Cdd:TIGR02341 12 AENARLSSFVGAIAIGDLVKSTLGPKGMDKILQSssSDASIMVTNDGATILKSI----GVDNPAAKVLVDMSKVQDDEVG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 86 DGTTTATVLAQAMIREGLKNVTAGANPVGVRKGMEQAVAVAIENLKEIS-----KPIEGKESIAQVAA-------ISAAD 153
Cdd:TIGR02341 88 DGTTSVTVLAAELLREAEKLINQKIHPQTIIAGYREATKAARDALLKSAvdngsDEVKFRQDLMNIARttlsskiLSQHK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 154 EEVGSLIAEAMERV---GN-DGVITIEESKGFTTELEVVEGMQFDR--GYASPYMV-----------TDSDKMEaVLDNP 216
Cdd:TIGR02341 168 DHFAQLAVDAVLRLkgsGNlEAIQIIKKLGGSLADSYLDEGFLLDKkiGVNQPKRIenakiliantgMDTDKVK-IFGSR 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 217 YILITDKKITNIQEIlpvlEQVVQQGKPLLLIAEDVEGEALATLVVNKLRGTFNAVAVKAPGFGDRRKamLEDIAVLTGG 296
Cdd:TIGR02341 247 VRVDSTAKVAELEHA----EKEKMKEKVEKILKHGINCFINRQLIYNYPEQLFADAGVMAIEHADFEG--VERLALVTGG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 297 EVITEdlgldLKSTQIAQLGRASKVvvtkENTTIVEgagetdkisarvtqiraqveettsefdrEKLQERLAKLAGGVAV 376
Cdd:TIGR02341 321 EIVST-----FDHPELVKLGSCDLI----EEIMIGE----------------------------DKLLKFSGVKLGEACT 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 377 IKVGAATETELKERKLRIEDALNSTRAAVEEGIVSGGGTALVNVYNKVAAVEAE---GDAQTGINIVLRALEEPIRQIAH 453
Cdd:TIGR02341 364 IVLRGATQQILDEAERSLHDALCVLSQTVKESRTVLGGGCSEMLMSKAVTQEAQrtpGKEALAVEAFARALRQLPTIIAD 443
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16077670 454 NAGLEGSVIVERLK----NEEIGVGFNAATGEWVNMIEKGIVDPTKVTRSALQNAASVAAMFLTTEAVVADKP 522
Cdd:TIGR02341 444 NAGFDSAELVAQLRaahyNGNTTMGLDMNEGTIADMRQLGITESYKVKRAVVSSAAEAAEVILRVDNIIKAAP 516
|
|
| chap_CCT_gamma |
TIGR02344 |
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ... |
9-519 |
2.05e-12 |
|
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: 69.38 E-value: 2.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 9 EEARRAMLRGVDA---LADAVKVTLGPKGRNVVLEKKFGSPLITNDGVTIAKEIELedafENMGAKLVAEVASKTNDVAG 85
Cdd:TIGR02344 12 ESGRKAQLSNIQAakaVADIIRTCLGPRSMLKMLLDPMGGIVMTNDGNAILREIDV----AHPAAKSMIELSRTQDEEVG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 86 DGTTTATVLAQAMIREGLKNVTAGANPVGVRKGMEQAVAVAIENLKEISKPIEGKESIAQVAAISAA---------DEEV 156
Cdd:TIGR02344 88 DGTTSVIILAGEMLSVAEPFLEQNIHPTVIIRAYRKALDDALSVLEEISIPVDVNDDAAMLKLIQSCigtkfvsrwSDLM 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 157 GSLIAEAMERVGND--GVITIEESK---------GFTTELEVVEGMQFDRGYASPymvtdsdKMEAVLDNPYILITD--- 222
Cdd:TIGR02344 168 CDLALDAVRTVQRDenGRKEIDIKRyakvekipgGDIEDSCVLKGVMINKDVTHP-------KMRRYIENPRIVLLDcpl 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 223 --KK---ITNI--------QEILPVLEQVVQQgkpllliaedvegealatlvvnklrgtfnavavkapgfgdrrkaMLED 289
Cdd:TIGR02344 241 eyKKgesQTNIeitkeedwNRILQMEEEYVQL--------------------------------------------MCED 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 290 IAVLTGGEVITEDLGLDLkstqiAQ--LGRASKVVVTK----ENTTIVEGAGETdkISARVTQIR-AQVEETTSEFDREK 362
Cdd:TIGR02344 277 IIAVKPDLVITEKGVSDL-----AQhyLLKANITAIRRvrktDNNRIARACGAT--IVNRPEELReSDVGTGCGLFEVKK 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 363 LQERL------AKLAGGVAVIKVGAATETeLKERKLRIEDALNSTRAAVEEGIVSGGGTAL---VNVYNKVAAVEAEGDA 433
Cdd:TIGR02344 350 IGDEYftfiteCKDPKACTILLRGASKDI-LNEVERNLQDAMAVARNVLLDPKLVPGGGATemaVSVALTEKSKKLEGVE 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 434 QTGINIVLRALEEPIRQIAHNAGleGSVIVE----RLKNEEIG---VGFNAATGEWVNMIEKGIVDPTKVTRSALQNAAS 506
Cdd:TIGR02344 429 QWPYRAVADALEIIPRTLAQNCG--ANVIRTltelRAKHAQENnctWGIDGETGKIVDMKEKGIWEPLAVKLQTYKTAIE 506
|
570
....*....|...
gi 16077670 507 VAAMFLTTEAVVA 519
Cdd:TIGR02344 507 SACLLLRIDDIVS 519
|
|
| TCP1_zeta |
cd03342 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
22-512 |
9.57e-12 |
|
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: 67.28 E-value: 9.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 22 LADAVKVTLGPKGRNVVLEKKFGSPLITNDGVTIAKEIEledaFENMGAKLVAEVASKTNDVAGDGTTTATVLAQAMIRE 101
Cdd:cd03342 24 LQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLSEMQ----IQHPTASMIARAATAQDDITGDGTTSNVLLIGELLKQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 102 GLKNVTAGANPVGVRKGMEQAVAVAIENLKEISKPIE---GKESIAQVAAISaADEEVGSLIAEAMERVGNDGVITIEES 178
Cdd:cd03342 100 AERYIQEGVHPRIITEGFELAKNKALKFLESFKVPVEidtDRELLLSVARTS-LRTKLHADLADQLTEIVVDAVLAIYKP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 179 KGFtTELEVVEGMQFDRGYASPY-----MVTD----SDKMEAVLDNPYILIT------DKKITNIQEILPVLeqVVQQG- 242
Cdd:cd03342 179 DEP-IDLHMVEIMQMQHKSDSDTklirgLVLDhgarHPDMPKRVENAYILTCnvsleyEKTEVNSGFFYSVV--INQKGi 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 243 KPLLLiaedvegEALATLVVNKLRGTfnavavkapgfgdRRKAMlEDIAVLTGGEVIT--EDLGLDLkstqiaqLGRASK 320
Cdd:cd03342 256 DPPSL-------DMLAKEGILALRRA-------------KRRNM-ERLTLACGGVAMNsvDDLSPEC-------LGYAGL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 321 V---VVTKENTTIVEGAgeTDKISarVTqiraqveettsefdreklqerlaklaggvavIKVGAATETELKERKLRIEDA 397
Cdd:cd03342 308 VyerTLGEEKYTFIEGV--KNPKS--CT-------------------------------ILIKGPNDHTITQIKDAIRDG 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 398 LNSTRAAVEEG-IVSGGGTALVNVYNKV--AAVEAEGDAQTGINIVLRALEEPIRQIAHNAGLEGSVIVERLKNE----E 470
Cdd:cd03342 353 LRAVKNAIEDKcVVPGAGAFEVALYAHLkeFKKSVKGKAKLGVQAFADALLVIPKTLAENSGLDVQETLVKLQDEyaegG 432
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 16077670 471 IGVGFNAATGEWVNMIEKGIVDPTKVTRSALQNAASVAAMFL 512
Cdd:cd03342 433 QVGGVDLDTGEPMDPESEGIWDNYSVKRQILHSATVIASQLL 474
|
|
| TCP1_alpha |
cd03335 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ... |
9-167 |
5.63e-11 |
|
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: 65.00 E-value: 5.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 9 EEARRAMLRGVDALADAVKVTLGPKGRNVVLEKKFGSPLITNDGVTIAKEIELEDAfenmGAKLVAEVASKTNDVAGDGT 88
Cdd:cd03335 7 QDVRTQNVTAAMAIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHP----AAKILVELAQLQDKEVGDGT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 89 TTATVLAQAMIREGLKNVTAGANPVGVRKGMEQAVAVAIENLKE-ISKPIE--GKESIAQVAA-------ISAADEEVGS 158
Cdd:cd03335 83 TSVVIIAAELLKRANELVKQKIHPTTIISGYRLACKEAVKYIKEhLSISVDnlGKESLINVAKtsmsskiIGADSDFFAN 162
|
....*....
gi 16077670 159 LIAEAMERV 167
Cdd:cd03335 163 MVVDAILAV 171
|
|
| TCP1_gamma |
cd03337 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ... |
9-222 |
1.29e-10 |
|
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: 63.85 E-value: 1.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 9 EEARRAMLRGVDA---LADAVKVTLGPKGRNVVLEKKFGSPLITNDGVTIAKEIELEdafeNMGAKLVAEVASKTNDVAG 85
Cdd:cd03337 12 ESGRKAQLGNIQAaktVADVIRTCLGPRAMLKMLLDPMGGIVLTNDGNAILREIDVA----HPAAKSMIELSRTQDEEVG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 86 DGTTTATVLAQAMIREGLKNVTAGANPVGVRKGMEQAVAVAIENLKEISKPI--EGKESIAQV-------AAISAADEEV 156
Cdd:cd03337 88 DGTTSVIILAGEILAVAEPFLERGIHPTVIIKAYRKALEDALKILEEISIPVdvNDRAQMLKIikscigtKFVSRWSDLM 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16077670 157 GSLIAEAMERVG---NDGVITIEESK---------GFTTELEVVEGMQFDRGYASPymvtdsdKMEAVLDNPYILITD 222
Cdd:cd03337 168 CNLALDAVKTVAveeNGRKKEIDIKRyakvekipgGEIEDSRVLDGVMLNKDVTHP-------KMRRRIENPRIVLLD 238
|
|
| chap_CCT_theta |
TIGR02346 |
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ... |
14-522 |
1.48e-10 |
|
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: 63.58 E-value: 1.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 14 AMLRGVDA---LADAVKVTLGPKGRNVV----LEKKFgsplITNDGVTIAKEIELEdafeNMGAKLVAEVASKTNDVAGD 86
Cdd:TIGR02346 19 AVIKNIEAckeLSQITRTSLGPNGMNKMvinhLEKLF----VTNDAATILRELEVQ----HPAAKLLVMASEMQENEIGD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 87 GTTTATVLAQAMIREGLKNVTAGANPVGVRKGMEQAVAVAIENLKEIS----KPIEGKESIAQVAAISAADEEVGS---- 158
Cdd:TIGR02346 91 GTNLVLVLAGELLNKAEELIRMGLHPSEIIKGYEMALKKAMEILEELVvwevKDLRDKDELIKALKASISSKQYGNedfl 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 159 --LIAEAM-----ERVGNDGVITIEESK---GFTTELEVVEGMQFDRGyASPYMVTDSDKMEAVLDNPY-ILITDKKITn 227
Cdd:TIGR02346 171 aqLVAQACstvlpKNPQNFNVDNIRVCKilgGSLSNSEVLKGMVFNRE-AEGSVKSVKNAKVAVFSCPLdTATTETKGT- 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 228 iqeilpVLEQVVQQgkpllLIAEDVEGEALATLVVNKLRGTFNAVAVKAPGFGDRRKAMLEDIAVLTggevitedlgldL 307
Cdd:TIGR02346 249 ------VLIHNAEE-----LLNYSKGEENQIEAMIKAIADSGVNVIVTGGSVGDMALHYLNKYNIMV------------L 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 308 KSTQIAQLGRASKVV----VTKENTTIVEGAGETDKISA------RVTQIRaQVEETTSefdreklqerlaklaggVAVI 377
Cdd:TIGR02346 306 KIPSKFELRRLCKTVgatpLPRLGAPTPEEIGYVDSVYVseiggdKVTVFK-QENGDSK-----------------ISTI 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 378 KVGAATETELKERKLRIEDALNSTRAAVEEG-IVSGGGTALVNVYNKVA--AVEAEGDAQTGINIVLRALEEPIRQIAHN 454
Cdd:TIGR02346 368 ILRGSTDNLLDDIERAIDDGVNTVKALVKDGrLLPGAGATEIELASRLTkyGEKLPGLDQYAIKKFAEAFEIIPRTLAEN 447
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16077670 455 AGLEGSVIVERL------KNEEIGVGFNAATGEWVNMIEKGIVDPTKVTRSALQNAASVAAMFLTTEAVVADKP 522
Cdd:TIGR02346 448 AGLNANEVIPKLyaahkkGNKSKGIDIEAESDGVKDASEAGIYDMLATKKWAIKLATEAAVTVLRVDQIIMAKP 521
|
|
| chap_CCT_alpha |
TIGR02340 |
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ... |
9-167 |
4.56e-10 |
|
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT alpha chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.
Pssm-ID: 274081 [Multi-domain] Cd Length: 536 Bit Score: 62.05 E-value: 4.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 9 EEARRAMLRGVDALADAVKVTLGPKGRNVVLEKKFGSPLITNDGVTIAKEIELEDAfenmGAKLVAEVASKTNDVAGDGT 88
Cdd:TIGR02340 11 QDVRTQNVTAAMAIANIVKTSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHP----AAKILVELAQLQDREVGDGT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 89 TTATVLAQAMIREGLKNVTAGANPVGVRKGMEQAVAVAIENLKE-ISKPIE--GKESIAQVAA-------ISAADEEVGS 158
Cdd:TIGR02340 87 TSVVIIAAELLKRADELVKNKIHPTSVISGYRLACKEAVKYIKEnLSVSVDelGREALINVAKtsmsskiIGLDSDFFSN 166
|
....*....
gi 16077670 159 LIAEAMERV 167
Cdd:TIGR02340 167 IVVDAVLAV 175
|
|
| TCP1_theta |
cd03341 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ... |
6-149 |
1.83e-09 |
|
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: 59.93 E-value: 1.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 6 KFSEEARRAMLRGVDA---LADAVKVTLGPKGRN--VV--LEKKFgsplITNDGVTIAKEIEledaFENMGAKLVAEVAS 78
Cdd:cd03341 1 RHYSGLEEAVLRNIEAckeLSQITRTSYGPNGMNkmVInhLEKLF----VTSDAATILRELE----VQHPAAKLLVMASQ 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16077670 79 KTNDVAGDGTTTATVLAQAMIREGLKNVTAGANPVGVRKGMEQAVAVAIENLKEIS-KPIEGKESIAQVAAI 149
Cdd:cd03341 73 MQEEEIGDGTNLVVVLAGELLEKAEELLRMGLHPSEIIEGYEKALKKALEILEELVvYKIEDLRNKEEVSKA 144
|
|
| chap_CCT_zeta |
TIGR02347 |
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ... |
22-518 |
3.40e-08 |
|
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: 56.28 E-value: 3.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 22 LADAVKVTLGPKGRNVVLEKKFGSPLITNDGVTIAKEIELEdafeNMGAKLVAEVASKTNDVAGDGTTTATVLAQAMIRE 101
Cdd:TIGR02347 28 LQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEMQIQ----HPTASMIARAATAQDDITGDGTTSTVLLIGELLKQ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 102 GLKNVTAGANPVGVRKGMEQAVAVAIENLKEISKPIEG---KESIAQVAAISAAD-------EEVGSLIAEAMERVGNDG 171
Cdd:TIGR02347 104 AERYILEGVHPRIITEGFEIARKEALQFLDKFKVKKEDevdREFLLNVARTSLRTklpadlaDQLTEIVVDAVLAIKKDG 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 172 ------VITIEESK-GFTTELEVVEGMQFDRGYASPYMVTDsdkmeavLDNPYILIT----------------------- 221
Cdd:TIGR02347 184 edidlfMVEIMEMKhKSATDTTLIRGLVLDHGARHPDMPRR-------VKNAYILTCnvsleyektevnsgffyssaeqr 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 222 DKKITN--------IQEILPVLEQVVQQGKPLLLIAEDVEG------EALATLVVNKLRGTfnavavkapgfgdRRKAMl 287
Cdd:TIGR02347 257 EKLVKAerkfvddrVKKIIELKKKVCGKSPDKGFVVINQKGidppslDLLAKEGIMALRRA-------------KRRNM- 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 288 EDIAVLTGGEVIT--EDLGLDLkstqiaqLGRASKV---VVTKENTTIVEgagetdkisarvtqiraQVEETTSefdrek 362
Cdd:TIGR02347 323 ERLTLACGGEALNsvEDLTPEC-------LGWAGLVyetTIGEEKYTFIE-----------------ECKNPKS------ 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 363 lqerlaklaggvAVIKVGAATETELKERKLRIEDALNSTRAAVEEG-IVSGGGTALVNVYNKVAAVE--AEGDAQTGINI 439
Cdd:TIGR02347 373 ------------CTILIKGPNDHTIAQIKDAVRDGLRAVKNAIEDKcVVPGAGAFEIAAYRHLKEYKksVKGKAKLGVEA 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077670 440 VLRALEEPIRQIAHNAGLEG-----SVIVERLKNEEIgVGFNAATGEWVNMIEKGIVDPTKVTRSALQNAASVAAMFLTT 514
Cdd:TIGR02347 441 FANALLVIPKTLAENSGFDAqdtlvKLEDEHDEGGEV-VGVDLNTGEPIDPEIKGIWDNYRVKKQLIQSATVIASQLLLV 519
|
....
gi 16077670 515 EAVV 518
Cdd:TIGR02347 520 DEVM 523
|
|
| |
