|
Name |
Accession |
Description |
Interval |
E-value |
| groEL |
PRK12849 |
chaperonin GroEL; Reviewed |
1-528 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237230 Cd Length: 542 Bit Score: 835.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 1 MAKLIAFNEEAREGLKRGVDTLADAVKVTLGPKGRNVVLDKAFGGPLVTNDGVTIARDIDVEDPFENLGAQLVKSVAVKT 80
Cdd:PRK12849 1 MAKIIKFDEEARRALERGVNKLADAVKVTLGPKGRNVVIDKSFGAPTITKDGVSIAKEIELEDPFENLGAQLVKEVASKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 81 NDVAGDGTTTATLLAQALVHEGLRNVAAGANPISLNRGIHAASDKAVELLKQRATSVSSSAAIAQVATVSSR-DTEIGDL 159
Cdd:PRK12849 81 NDVAGDGTTTATVLAQALVQEGLKNVAAGANPMDLKRGIDKAVEAVVEELKALARPVSGSEEIAQVATISANgDEEIGEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 160 VAGAMDKVGKDGVVSVEESQSIATELSVTEGVSFNKGFLSPYFITDVEAQQAILDGAQVLLVREKISSLPEFLPILEKIA 239
Cdd:PRK12849 161 IAEAMEKVGKDGVITVEESKTLETELEVTEGMQFDRGYLSPYFVTDPERMEAVLEDPLILLTDKKISSLQDLLPLLEKVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 240 ESGKPTLIMAEDIEGEALSALVINAMRKTLKVAAVKAPYFGDRRKAFMDDLAVVTGATVVTADTGMQLKDVGLEVLGNAR 319
Cdd:PRK12849 241 QSGKPLLIIAEDVEGEALATLVVNKLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGLKLEEVTLDDLGRAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 320 RITITKDETVLVDGAGTAEAVEERRNQIRAEIERTDSDWDREKLEERLAKLSGGVAVIKVGAATETEVNERKLRVEDAIN 399
Cdd:PRK12849 321 RVTITKDNTTIVDGAGDKEAIEARVAQIRRQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATEVELKERKDRVEDALN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 400 AARAAAQEGVIAGGGSVLVQISRELEAFAdEFEGDEAVGVRAVAKALTRPAFWIAENAGKDGAVVVYHIGELENGNGYNA 479
Cdd:PRK12849 401 ATRAAVEEGIVPGGGVALLRAAKALDELA-GLNGDQAAGVEIVRRALEAPLRQIAENAGLDGSVVVAKVLELEDGFGFNA 479
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 512463547 480 ATDTYENLIESGVIDPVKVTHSAVVNATSVARMLLTTEASVVDKPEEEP 528
Cdd:PRK12849 480 ATGEYGDLIAAGIIDPVKVTRSALQNAASVAGLLLTTEALVADKPEEED 528
|
|
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
1-528 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 767.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 1 MAKLIAFNEEAREGLKRGVDTLADAVKVTLGPKGRNVVLDKAFGGPLVTNDGVTIARDIDVEDPFENLGAQLVKSVAVKT 80
Cdd:PRK00013 1 MAKDIKFGEDARRKLLRGVNKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDPFENMGAQLVKEVASKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 81 NDVAGDGTTTATLLAQALVHEGLRNVAAGANPISLNRGIHAASDKAVELLKQRATSVSSSAAIAQVATVSS-RDTEIGDL 159
Cdd:PRK00013 81 NDVAGDGTTTATVLAQAIVREGLKNVAAGANPMDLKRGIDKAVEAAVEELKKISKPVEDKEEIAQVATISAnGDEEIGKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 160 VAGAMDKVGKDGVVSVEESQSIATELSVTEGVSFNKGFLSPYFITDVEAQQAILDGAQVLLVREKISSLPEFLPILEKIA 239
Cdd:PRK00013 161 IAEAMEKVGKEGVITVEESKGFETELEVVEGMQFDRGYLSPYFVTDPEKMEAELENPYILITDKKISNIQDLLPVLEQVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 240 ESGKPTLIMAEDIEGEALSALVINAMRKTLKVAAVKAPYFGDRRKAFMDDLAVVTGATVVTADTGMQLKDVGLEVLGNAR 319
Cdd:PRK00013 241 QSGKPLLIIAEDVEGEALATLVVNKLRGTLKVVAVKAPGFGDRRKAMLEDIAILTGGTVISEELGLKLEDATLEDLGQAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 320 RITITKDETVLVDGAGTAEAVEERRNQIRAEIERTDSDWDREKLEERLAKLSGGVAVIKVGAATETEVNERKLRVEDAIN 399
Cdd:PRK00013 321 KVVVTKDNTTIVDGAGDKEAIKARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATEVEMKEKKDRVEDALH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 400 AARAAAQEGVIAGGGSVLVQISRELEAFADEfEGDEAVGVRAVAKALTRPAFWIAENAGKDGAVVVYHIGELENGN-GYN 478
Cdd:PRK00013 401 ATRAAVEEGIVPGGGVALLRAAPALEALKGL-NGDEATGINIVLRALEAPLRQIAENAGLEGSVVVEKVKNGKGKGyGYN 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 512463547 479 AATDTYENLIESGVIDPVKVTHSAVVNATSVARMLLTTEASVVDKPEEEP 528
Cdd:PRK00013 480 AATGEYVDMIEAGIIDPTKVTRSALQNAASVAGLLLTTEAVVADKPEKKA 529
|
|
| 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: 744.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 3 KLIAFNEEAREGLKRGVDTLADAVKVTLGPKGRNVVLDKAFGGPLVTNDGVTIARDIDVEDPFENLGAQLVKSVAVKTND 82
Cdd:cd03344 1 KDIKFGEEARKALLRGVNKLADAVKVTLGPKGRNVVIEKSFGSPKITKDGVTVAKEIELEDPFENMGAQLVKEVASKTND 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 83 VAGDGTTTATLLAQALVHEGLRNVAAGANPISLNRGIHAASDKAVELLKQRATSVSSSAAIAQVATVSSR-DTEIGDLVA 161
Cdd:cd03344 81 VAGDGTTTATVLARAIIKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKPVKTKEEIAQVATISANgDEEIGELIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 162 GAMDKVGKDGVVSVEESQSIATELSVTEGVSFNKGFLSPYFITDVEAQQAILDGAQVLLVREKISSLPEFLPILEKIAES 241
Cdd:cd03344 161 EAMEKVGKDGVITVEEGKTLETELEVVEGMQFDRGYLSPYFVTDPEKMEVELENPYILLTDKKISSIQELLPILELVAKA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 242 GKPTLIMAEDIEGEALSALVINAMRKTLKVAAVKAPYFGDRRKAFMDDLAVVTGATVVTADTGMQLKDVGLEVLGNARRI 321
Cdd:cd03344 241 GRPLLIIAEDVEGEALATLVVNKLRGGLKVCAVKAPGFGDRRKAMLEDIAILTGGTVISEELGLKLEDVTLEDLGRAKKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 322 TITKDETVLVDGAGTAEAVEERRNQIRAEIERTDSDWDREKLEERLAKLSGGVAVIKVGAATETEVNERKLRVEDAINAA 401
Cdd:cd03344 321 VVTKDDTTIIGGAGDKAAIKARIAQIRKQIEETTSDYDKEKLQERLAKLSGGVAVIKVGGATEVELKEKKDRVEDALNAT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 402 RAAAQEGVIAGGGSVLVQISRELEAFADEfEGDEAVGVRAVAKALTRPAFWIAENAGKDGAVVVYHIGELENGNGYNAAT 481
Cdd:cd03344 401 RAAVEEGIVPGGGVALLRASPALDKLKAL-NGDEKLGIEIVRRALEAPLRQIAENAGVDGSVVVEKVLESPDGFGYDAAT 479
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 512463547 482 DTYENLIESGVIDPVKVTHSAVVNATSVARMLLTTEASVVD 522
Cdd:cd03344 480 GEYVDMIEAGIIDPTKVVRSALQNAASVASLLLTTEALVVD 520
|
|
| 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: 711.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 2 AKLIAFNEEAREGLKRGVDTLADAVKVTLGPKGRNVVLDKAFGGPLVTNDGVTIARDIDVEDPFENLGAQLVKSVAVKTN 81
Cdd:TIGR02348 1 AKQIKFDEEARKALLRGVDKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDKFENMGAQLVKEVASKTN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 82 DVAGDGTTTATLLAQALVHEGLRNVAAGANPISLNRGIHAASDKAVELLKQRATSVSSSAAIAQVATVSS-RDTEIGDLV 160
Cdd:TIGR02348 81 DVAGDGTTTATVLAQAIVKEGLKNVAAGANPIELKRGIEKAVEAVVEELKKLSKPVKGKKEIAQVATISAnNDEEIGSLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 161 AGAMDKVGKDGVVSVEESQSIATELSVTEGVSFNKGFLSPYFITDVEAQQAILDGAQVLLVREKISSLPEFLPILEKIAE 240
Cdd:TIGR02348 161 AEAMEKVGKDGVITVEESKSLETELEVVEGMQFDRGYISPYFVTDAEKMEVELENPYILITDKKISNIKDLLPLLEKVAQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 241 SGKPTLIMAEDIEGEALSALVINAMRKTLKVAAVKAPYFGDRRKAFMDDLAVVTGATVVTADTGMQLKDVGLEVLGNARR 320
Cdd:TIGR02348 241 SGKPLLIIAEDVEGEALATLVVNKLRGTLNVCAVKAPGFGDRRKAMLEDIAILTGGQVISEELGLKLEEVTLDDLGKAKK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 321 ITITKDETVLVDGAGTAEAVEERRNQIRAEIERTDSDWDREKLEERLAKLSGGVAVIKVGAATETEVNERKLRVEDAINA 400
Cdd:TIGR02348 321 VTVDKDNTTIVEGAGDKAAIKARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATETEMKEKKLRIEDALNA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 401 ARAAAQEGVIAGGGSVLVQISRELEAfADEFEGDEAVGVRAVAKALTRPAFWIAENAGKDGAVVVYHIGELENGNGYNAA 480
Cdd:TIGR02348 401 TRAAVEEGIVPGGGVALLRAAAALEG-LKGDGEDEAIGIDIVKRALEAPLRQIAENAGLDGAVVAEKVKELKGNFGFNAA 479
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 512463547 481 TDTYENLIESGVIDPVKVTHSAVVNATSVARMLLTTEASVVDKPE 525
Cdd:TIGR02348 480 TGEYEDLVEAGIIDPTKVTRSALQNAASIAGLLLTTEAVVADKPE 524
|
|
| GroEL |
COG0459 |
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ... |
1-528 |
0e+00 |
|
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227 Cd Length: 497 Bit Score: 666.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 1 MAKLIAFNEEAREGLKRGVDTLADAVKVTLGPKGRNVVLDKAFGGPLVTNDGVTIARDIDVEDPFENLGAQLVKSVAVKT 80
Cdd:COG0459 1 MAKQILFGEDARRANIRGVKALADAVKVTLGPKGRNVMLVKSFGDPTITNDGVTIAKEIELEDPFENMGAQLVKEVASKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 81 NDVAGDGTTTATLLAQALVHEGLRNVAAGANPISLNRGIHAASDKAVELLKQRATSVSSSAAIAQVATVSSR-DTEIGDL 159
Cdd:COG0459 81 NDEAGDGTTTATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPVDDKEELAQVATISANgDEEIGEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 160 VAGAMDKVGKDGVVSVEESQSIATELSVTEGVSFNKGFLSPYFITDVEAQQAILDGAQVLLVREKISSLPEFLPILEKIA 239
Cdd:COG0459 161 IAEAMEKVGKDGVITVEEGKGLETELEVVEGMQFDKGYLSPYFVTDPEKMPAELENAYILLTDKKISSIQDLLPLLEKVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 240 ESGKPTLIMAEDIEGEALSALVINAMRKTLKVAAVKAPYFGDRRKAFMDDLAVVTGATVVTADTGMQLKDVGLEVLGNAR 319
Cdd:COG0459 241 QSGKPLLIIAEDIDGEALATLVVNGIRGVLRVVAVKAPGFGDRRKAMLEDIAILTGGRVISEDLGLKLEDVTLDDLGRAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 320 RITITKDETVLVDGAGTAEAVeerrnqiraeiertdsdwdrekleerlaklsggvaVIKVGAATETEVNERKLRVEDAIN 399
Cdd:COG0459 321 RVEVDKDNTTIVEGAGNPKAI-----------------------------------VILVGAATEVEVKERKRRVEDALH 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 400 AARAAAQEGVIAGGGSVLVQISRELEAFADEFEGDEAVGVRAVAKALTRPAFWIAENAGKDGAVVVYHIGELENGN-GYN 478
Cdd:COG0459 366 ATRAAVEEGIVPGGGAALLRAARALRELAAKLEGDEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKVRAAKDKGfGFD 445
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 512463547 479 AATDTYENLIESGVIDPVKVTHSAVVNATSVARMLLTTEASVVDKPEEEP 528
Cdd:COG0459 446 AATGEYVDMLEAGVIDPAKVKRSALQNAASVAGLILTTEAVIADKPEKEE 495
|
|
| groEL |
PRK12850 |
chaperonin GroEL; Reviewed |
1-528 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237231 Cd Length: 544 Bit Score: 662.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 1 MAKLIAFNEEAREGLKRGVDTLADAVKVTLGPKGRNVVLDKAFGGPLVTNDGVTIARDIDVEDPFENLGAQLVKSVAVKT 80
Cdd:PRK12850 2 AAKEIRFSTDARDRLLRGVNILANAVKVTLGPKGRNVVLEKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVKEVASKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 81 NDVAGDGTTTATLLAQALVHEGLRNVAAGANPISLNRGIHAASDKAVELLKQRATSVSSSAAIAQVATVS-SRDTEIGDL 159
Cdd:PRK12850 82 NDLAGDGTTTATVLAQAIVREGAKLVAAGMNPMDLKRGIDLAVAAVVDELKKIAKKVTSSKEIAQVATISaNGDESIGEM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 160 VAGAMDKVGKDGVVSVEESQSIATELSVTEGVSFNKGFLSPYFITDVEAQQAILDGAQVLLVREKISSLPEFLPILEKIA 239
Cdd:PRK12850 162 IAEAMDKVGKEGVITVEEAKTLGTELDVVEGMQFDRGYLSPYFVTNPEKMRAELEDPYILLHEKKISNLQDLLPILEAVV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 240 ESGKPTLIMAEDIEGEALSALVINAMRKTLKVAAVKAPYFGDRRKAFMDDLAVVTGATVVTADTGMQLKDVGLEVLGNAR 319
Cdd:PRK12850 242 QSGRPLLIIAEDVEGEALATLVVNKLRGGLKSVAVKAPGFGDRRKAMLEDIAVLTGGQVISEDLGIKLENVTLDMLGRAK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 320 RITITKDETVLVDGAGTAEAVEERRNQIRAEIERTDSDWDREKLEERLAKLSGGVAVIKVGAATETEVNERKLRVEDAIN 399
Cdd:PRK12850 322 RVLITKENTTIIDGAGDKKNIEARVKQIRAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKEKKDRVDDALH 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 400 AARAAAQEGVIAGGGSVLVQISRELEAFADEfEGDEAVGVRAVAKALTRPAFWIAENAGKDGAVVVYHIGELENGNGYNA 479
Cdd:PRK12850 402 ATRAAVEEGIVPGGGVALLRARSALRGLKGA-NADETAGIDIVRRALEEPLRQIATNAGFEGSVVVGKVAELPGNFGFNA 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 512463547 480 ATDTYENLIESGVIDPVKVTHSAVVNATSVARMLLTTEASVVDKPEEEP 528
Cdd:PRK12850 481 QTGEYGDMVEAGIIDPAKVTRTALQDAASIAALLITTEAMVAEAPKKAA 529
|
|
| groEL |
PRK12851 |
chaperonin GroEL; Reviewed |
1-528 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 171770 Cd Length: 541 Bit Score: 632.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 1 MAKLIAFNEEAREGLKRGVDTLADAVKVTLGPKGRNVVLDKAFGGPLVTNDGVTIARDIDVEDPFENLGAQLVKSVAVKT 80
Cdd:PRK12851 2 AAKEVKFHVEAREKMLRGVNILADAVKVTLGPKGRNVVIDKSFGAPTITNDGVTIAKEIELEDKFENMGAQMVREVASKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 81 NDVAGDGTTTATLLAQALVHEGLRNVAAGANPISLNRGIHAASDKAVELLKQRATSVSSSAAIAQVATVSSR-DTEIGDL 159
Cdd:PRK12851 82 NDVAGDGTTTATVLAQAIVREGAKAVAAGANPMDLKRGIDRAVAAVVEELKANARPVTTNAEIAQVATISANgDAEIGRL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 160 VAGAMDKVGKDGVVSVEESQSIATELSVTEGVSFNKGFLSPYFITDVEAQQAILDGAQVLLVREKISSLPEFLPILEKIA 239
Cdd:PRK12851 162 VAEAMEKVGNEGVITVEESKTAETELEVVEGMQFDRGYLSPYFVTDADKMEAELEDPYILIHEKKISNLQDLLPVLEAVV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 240 ESGKPTLIMAEDIEGEALSALVINAMRKTLKVAAVKAPYFGDRRKAFMDDLAVVTGATVVTADTGMQLKDVGLEVLGNAR 319
Cdd:PRK12851 242 QSGKPLLIIAEDVEGEALATLVVNKLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGIKLENVTLEQLGRAK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 320 RITITKDETVLVDGAGTAEAVEERRNQIRAEIERTDSDWDREKLEERLAKLSGGVAVIKVGAATETEVNERKLRVEDAIN 399
Cdd:PRK12851 322 KVVVEKENTTIIDGAGSKTEIEGRVAQIRAQIEETTSDYDREKLQERLAKLAGGVAVIRVGASTEVEVKEKKDRVDDALH 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 400 AARAAAQEGVIAGGGSVLVQISRELEAFADEfEGDEAVGVRAVAKALTRPAFWIAENAGKDGAVVVYHIGELENGNGYNA 479
Cdd:PRK12851 402 ATRAAVEEGIVPGGGVALLRAVKALDKLETA-NGDQRTGVEIVRRALEAPVRQIAENAGAEGSVVVGKLREKPGGYGFNA 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 512463547 480 ATDTYENLIESGVIDPVKVTHSAVVNATSVARMLLTTEASVVDKPEEEP 528
Cdd:PRK12851 481 ATNEYGDLYAQGVIDPVKVVRTALQNAASVAGLLLTTEAMVAEKPKKEP 529
|
|
| PTZ00114 |
PTZ00114 |
Heat shock protein 60; Provisional |
2-531 |
0e+00 |
|
Heat shock protein 60; Provisional
Pssm-ID: 185455 Cd Length: 555 Bit Score: 630.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 2 AKLIAFNEEAREGLKRGVDTLADAVKVTLGPKGRNVVLDKAFGGPLVTNDGVTIARDIDVEDPFENLGAQLVKSVAVKTN 81
Cdd:PTZ00114 14 GKEIRFGDEARQSLLKGIERLADAVAVTLGPKGRNVIIEQEYGSPKITKDGVTVAKAIEFSDRFENVGAQLIRQVASKTN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 82 DVAGDGTTTATLLAQALVHEGLRNVAAGANPISLNRGIHAASDKAVELLKQRATSVSSSAAIAQVATVSSR-DTEIGDLV 160
Cdd:PTZ00114 94 DKAGDGTTTATILARAIFREGCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQSRPVKTKEDILNVATISANgDVEIGSLI 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 161 AGAMDKVGKDGVVSVEESQSIATELSVTEGVSFNKGFLSPYFITDVEAQQAILDGAQVLLVREKISSLPEFLPILEKIAE 240
Cdd:PTZ00114 174 ADAMDKVGKDGTITVEDGKTLEDELEVVEGMSFDRGYISPYFVTNEKTQKVELENPLILVTDKKISSIQSILPILEHAVK 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 241 SGKPTLIMAEDIEGEALSALVINAMRKTLKVAAVKAPYFGDRRKAFMDDLAVVTGATVVTAD-TGMQLKDVGLEVLGNAR 319
Cdd:PTZ00114 254 NKRPLLIIAEDVEGEALQTLIINKLRGGLKVCAVKAPGFGDNRKDILQDIAVLTGATVVSEDnVGLKLDDFDPSMLGSAK 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 320 RITITKDETVLVDGAGTAEAVEERRNQIRAEIERTDSDWDREKLEERLAKLSGGVAVIKVGAATETEVNERKLRVEDAIN 399
Cdd:PTZ00114 334 KVTVTKDETVILTGGGDKAEIKERVELLRSQIERTTSEYDKEKLKERLAKLSGGVAVIKVGGASEVEVNEKKDRIEDALN 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 400 AARAAAQEGVIAGGGSVLVQISRELEAFAD--EFEGDEAVGVRAVAKALTRPAFWIAENAGKDGAVVVYHIGELENGN-G 476
Cdd:PTZ00114 414 ATRAAVEEGIVPGGGVALLRASKLLDKLEEdnELTPDQRTGVKIVRNALRLPTKQIAENAGVEGAVVVEKILEKKDPSfG 493
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 512463547 477 YNAATDTYENLIESGVIDPVKVTHSAVVNATSVARMLLTTEASVVDKPEEEPQHD 531
Cdd:PTZ00114 494 YDAQTGEYVNMFEAGIIDPTKVVRSALVDAASVASLMLTTEAAIVDLPKEKKKNK 548
|
|
| groEL |
CHL00093 |
chaperonin GroEL |
1-527 |
0e+00 |
|
chaperonin GroEL
Pssm-ID: 177025 Cd Length: 529 Bit Score: 615.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 1 MAKLIAFNEEAREGLKRGVDTLADAVKVTLGPKGRNVVLDKAFGGPLVTNDGVTIARDIDVEDPFENLGAQLVKSVAVKT 80
Cdd:CHL00093 1 MSKKILYQDNARRALERGMDILAEAVSVTLGPKGRNVVLEKKYGSPQIVNDGVTIAKEIELEDHIENTGVALIRQAASKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 81 NDVAGDGTTTATLLAQALVHEGLRNVAAGANPISLNRGIHAASDKAVELLKQRATSVSSSAAIAQVATVSS-RDTEIGDL 159
Cdd:CHL00093 81 NDVAGDGTTTATVLAYAIVKQGMKNVAAGANPISLKRGIEKATQYVVSQIAEYARPVEDIQAITQVASISAgNDEEVGSM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 160 VAGAMDKVGKDGVVSVEESQSIATELSVTEGVSFNKGFLSPYFITDVEAQQAILDGAQVLLVREKISSLP-EFLPILEKI 238
Cdd:CHL00093 161 IADAIEKVGREGVISLEEGKSTVTELEITEGMRFEKGFISPYFVTDTERMEVVQENPYILLTDKKITLVQqDLLPILEQV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 239 AESGKPTLIMAEDIEGEALSALVINAMRKTLKVAAVKAPYFGDRRKAFMDDLAVVTGATVVTADTGMQLKDVGLEVLGNA 318
Cdd:CHL00093 241 TKTKRPLLIIAEDVEKEALATLVLNKLRGIVNVVAVRAPGFGDRRKAMLEDIAILTGGQVITEDAGLSLETIQLDLLGQA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 319 RRITITKDETVLVdGAGTAEAVEERRNQIRAEIERTDSDWDREKLEERLAKLSGGVAVIKVGAATETEVNERKLRVEDAI 398
Cdd:CHL00093 321 RRIIVTKDSTTII-ADGNEEQVKARCEQLRKQIEIADSSYEKEKLQERLAKLSGGVAVIKVGAATETEMKDKKLRLEDAI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 399 NAARAAAQEGVIAGGGSVLVQISRELEAFA-DEFEGDEAVGVRAVAKALTRPAFWIAENAGKDGAVVVYHIGELENGNGY 477
Cdd:CHL00093 400 NATKAAVEEGIVPGGGATLVHLSENLKTWAkNNLKEDELIGALIVARAILAPLKRIAENAGKNGSVIIEKVQEQDFEIGY 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 512463547 478 NAATDTYENLIESGVIDPVKVTHSAVVNATSVARMLLTTEASVVDKPEEE 527
Cdd:CHL00093 480 NAANNKFVNMYEAGIIDPAKVTRSALQNAASIASMILTTECIIVDKKESS 529
|
|
| groEL |
PRK12852 |
chaperonin GroEL; Reviewed |
1-529 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237232 Cd Length: 545 Bit Score: 576.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 1 MAKLIAFNEEAREGLKRGVDTLADAVKVTLGPKGRNVVLDKAFGGPLVTNDGVTIARDIDVEDPFENLGAQLVKSVAVKT 80
Cdd:PRK12852 2 AAKDVKFSGDARDRMLRGVDILANAVKVTLGPKGRNVVIEKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVREVASKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 81 NDVAGDGTTTATLLAQALVHEGLRNVAAGANPISLNRGIHAASDKAVELLKQRATSVSSSAAIAQVATVSSR-DTEIGDL 159
Cdd:PRK12852 82 NDLAGDGTTTATVLAQAIVREGAKAVAAGMNPMDLKRGIDIAVAAVVKDIEKRAKPVASSAEIAQVGTISANgDAAIGKM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 160 VAGAMDKVGKDGVVSVEESQSIATELSVTEGVSFNKGFLSPYFITDVEAQQAILDGAQVLLVREKISSLPEFLPILEKIA 239
Cdd:PRK12852 162 IAQAMQKVGNEGVITVEENKSLETEVDIVEGMKFDRGYLSPYFVTNAEKMTVELDDAYILLHEKKLSGLQAMLPVLEAVV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 240 ESGKPTLIMAEDIEGEALSALVINAMRKTLKVAAVKAPYFGDRRKAFMDDLAVVTGATVVTADTGMQLKDVGLEVLGNAR 319
Cdd:PRK12852 242 QSGKPLLIIAEDVEGEALATLVVNRLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGQLISEDLGIKLENVTLKMLGRAK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 320 RITITKDETVLVDGAGTAEAVEERRNQIRAEIERTDSDWDREKLEERLAKLSGGVAVIKVGAATETEVNERKLRVEDAIN 399
Cdd:PRK12852 322 KVVIDKENTTIVNGAGKKADIEARVGQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKEKKDRVEDALN 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 400 AARAAAQEGVIAGGGSVLVQISRELEAFADEfEGDEAVGVRAVAKALTRPAFWIAENAGKDGAVVVYHIGELENGN-GYN 478
Cdd:PRK12852 402 ATRAAVQEGIVPGGGVALLRAKKAVGRINND-NADVQAGINIVLKALEAPIRQIAENAGVEGSIVVGKILENKSETfGFD 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 512463547 479 AATDTYENLIESGVIDPVKVTHSAVVNATSVARMLLTTEASVVDKPEEEPQ 529
Cdd:PRK12852 481 AQTEEYVDMVAKGIIDPAKVVRTALQDAASVAGLLVTTEAMVAELPKKDAA 531
|
|
| PRK14104 |
PRK14104 |
chaperonin GroEL; Provisional |
2-526 |
6.18e-178 |
|
chaperonin GroEL; Provisional
Pssm-ID: 172594 Cd Length: 546 Bit Score: 512.27 E-value: 6.18e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 2 AKLIAFNEEAREGLKRGVDTLADAVKVTLGPKGRNVVLDKAFGGPLVTNDGVTIARDIDVEDPFENLGAQLVKSVAVKTN 81
Cdd:PRK14104 3 AKEVKFGVDARDRMLRGVDILANAVKVTLGPKGRNVVLDKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVREVASKSA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 82 DVAGDGTTTATLLAQALVHEGLRNVAAGANPISLNRGIHAASDKAVELLKQRATSVSSSAAIAQVATVSSR-DTEIGDLV 160
Cdd:PRK14104 83 DAAGDGTTTATVLAQAIVREGAKSVAAGMNPMDLKRGIDLAVEAVVADLVKNSKKVTSNDEIAQVGTISANgDAEIGKFL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 161 AGAMDKVGKDGVVSVEESQSIATELSVTEGVSFNKGFLSPYFITDVEAQQAILDGAQVLLVREKISSLPEFLPILEKIAE 240
Cdd:PRK14104 163 ADAMKKVGNEGVITVEEAKSLETELDVVEGMQFDRGYISPYFVTNADKMRVEMDDAYILINEKKLSSLNELLPLLEAVVQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 241 SGKPTLIMAEDIEGEALSALVINAMRKTLKVAAVKAPYFGDRRKAFMDDLAVVTGATVVTADTGMQLKDVGLEVLGNARR 320
Cdd:PRK14104 243 TGKPLVIVAEDVEGEALATLVVNRLRGGLKVAAVKAPGFGDRRKAMLQDIAILTGGQAISEDLGIKLENVTLQMLGRAKK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 321 ITITKDETVLVDGAGTAEAVEERRNQIRAEIERTDSDWDREKLEERLAKLSGGVAVIKVGAATETEVNERKLRVEDAINA 400
Cdd:PRK14104 323 VMIDKENTTIVNGAGKKADIEARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKERKDRVDDAMHA 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 401 ARAAAQEGVIAGGGSVLVQISRELEAFADEFEgDEAVGVRAVAKALTRPAFWIAENAGKDGAVVVYHIGELEN-GNGYNA 479
Cdd:PRK14104 403 TRAAVEEGIVPGGGVALLRASEQLKGIKTKND-DQKTGVEIVRKALSAPARQIAINAGEDGSVIVGKILEKEQySYGFDS 481
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 512463547 480 ATDTYENLIESGVIDPVKVTHSAVVNATSVARMLLTTEASVVDKPEE 526
Cdd:PRK14104 482 QTGEYGNLVSKGIIDPTKVVRTAIQNAASVAALLITTEAMVAELPKK 528
|
|
| PLN03167 |
PLN03167 |
Chaperonin-60 beta subunit; Provisional |
2-528 |
2.37e-165 |
|
Chaperonin-60 beta subunit; Provisional
Pssm-ID: 215611 [Multi-domain] Cd Length: 600 Bit Score: 482.12 E-value: 2.37e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 2 AKLIAFNEE--AREGLKRGVDTLADAVKVTLGPKGRNVVLDKAFGGPLVTNDGVTIARDIDVEDPFENLGAQLVKSVAVK 79
Cdd:PLN03167 56 AKELHFNKDgsAIKKLQAGVNKLADLVGVTLGPKGRNVVLESKYGSPKIVNDGVTVAKEVELEDPVENIGAKLVRQAAAK 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 80 TNDVAGDGTTTATLLAQALVHEGLRNVAAGANPISLNRGIHAASDKAVELLKQRATSVSSSaAIAQVATVSS-RDTEIGD 158
Cdd:PLN03167 136 TNDLAGDGTTTSVVLAQGLIAEGVKVVAAGANPVQITRGIEKTAKALVKELKKMSKEVEDS-ELADVAAVSAgNNYEVGN 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 159 LVAGAMDKVGKDGVVSVEESQSIATELSVTEGVSFNKGFLSPYFITDVEAQQAILDGAQVLLVREKISSLPEFLPILEKI 238
Cdd:PLN03167 215 MIAEAMSKVGRKGVVTLEEGKSAENNLYVVEGMQFDRGYISPYFVTDSEKMSVEYDNCKLLLVDKKITNARDLIGILEDA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 239 AESGKPTLIMAEDIEGEALSALVINAMRKTLKVAAVKAPYFGDRRKAFMDDLAVVTGATVVTADTGMQLKDVGLEVLGNA 318
Cdd:PLN03167 295 IRGGYPLLIIAEDIEQEALATLVVNKLRGSLKIAALKAPGFGERKSQYLDDIAILTGGTVIREEVGLSLDKVGKEVLGTA 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 319 RRITITKDETVLVDGAGTAEAVEERRNQIRAEIERTDSDWDREKLEERLAKLSGGVAVIKVGAATETEVNERKLRVEDAI 398
Cdd:PLN03167 375 AKVVLTKDTTTIVGDGSTQEAVNKRVAQIKNLIEAAEQDYEKEKLNERIAKLSGGVAVIQVGAQTETELKEKKLRVEDAL 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 399 NAARAAAQEGVIAGGGSVLVQISRELEAFADEFEGDE-AVGVRAVAKALTRPAFWIAENAGKDGAVVVYHIGELENGN-G 476
Cdd:PLN03167 455 NATKAAVEEGIVVGGGCTLLRLASKVDAIKDTLENDEqKVGADIVKRALSYPLKLIAKNAGVNGSVVSEKVLSNDNPKfG 534
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 512463547 477 YNAATDTYENLIESGVIDPVKVTHSAVVNATSVARMLLTTEASVVDKPEEEP 528
Cdd:PLN03167 535 YNAATGKYEDLMAAGIIDPTKVVRCCLEHAASVAKTFLTSDCVVVEIKEPEP 586
|
|
| chaperonin_type_I_II |
cd00309 |
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ... |
3-521 |
5.97e-124 |
|
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: 371.38 E-value: 5.97e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 3 KLIAFNEEAREGLKRGVDTLADAVKVTLGPKGRNVVLDKAFGGPLVTNDGVTIARDIDVEdpfeNLGAQLVKSVAVKTND 82
Cdd:cd00309 1 KEREFGEEARLSNINAAKALADAVKTTLGPKGMDKMLVDSLGDPTITNDGATILKEIEVE----HPAAKLLVEVAKSQDD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 83 VAGDGTTTATLLAQALVHEGLRNVAAGANPISLNRGIHAASDKAVELLKQRAT--SVSSSAAIAQVATVSSR-------D 153
Cdd:cd00309 77 EVGDGTTTVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVpiDVEDREELLKVATTSLNsklvsggD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 154 TEIGDLVAGAMDKVGKD------GVVSVEESQS-IATELSVTEGVSFNKGFLSPYFITDVEaqqaildGAQVLLVREKIS 226
Cdd:cd00309 157 DFLGELVVDAVLKVGKEngdvdlGVIRVEKKKGgSLEDSELVVGMVFDKGYLSPYMPKRLE-------NAKILLLDCKLE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 227 slpeflpilekiaesgkpTLIMAED-IEGEALSALVInamrktLKVAAVKApyfgdRRKAFMDDLAVVTGATVVTadtgm 305
Cdd:cd00309 230 ------------------YVVIAEKgIDDEALHYLAK------LGIMAVRR-----VRKEDLERIAKATGATIVS----- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 306 QLKDVGLEVLGNARRITITK----DETVLVDGAGtaeaveerrnqiraeiertdsdwdrekleerlaklsGGVAVIKVGA 381
Cdd:cd00309 276 RLEDLTPEDLGTAGLVEETKigdeKYTFIEGCKG------------------------------------GKVATILLRG 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 382 ATETEVNERKLRVEDAINAARAAAQE-GVIAGGGSVLVQISRELEAFADEFEGDEAVGVRAVAKALTRPAFWIAENAGKD 460
Cdd:cd00309 320 ATEVELDEAERSLHDALCAVRAAVEDgGIVPGGGAAEIELSKALEELAKTLPGKEQLGIEAFADALEVIPRTLAENAGLD 399
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 512463547 461 GAVVVYHIGELENGNGYNAA----TDTYENLIESGVIDPVKVTHSAVVNATSVARMLLTTEASVV 521
Cdd:cd00309 400 PIEVVTKLRAKHAEGGGNAGgdveTGEIVDMKEAGIIDPLKVKRQALKSATEAASLILTIDDIIV 464
|
|
| Cpn60_TCP1 |
pfam00118 |
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ... |
22-523 |
2.55e-75 |
|
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: 246.35 E-value: 2.55e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 22 LADAVKVTLGPKGRNVVLDKAFGGPLVTNDGVTIARDIDVEDPfenlGAQLVKSVAVKTNDVAGDGTTTATLLAQALVHE 101
Cdd:pfam00118 1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELEIQHP----AAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 102 GLRNVAAGANPISLNRGIHAASDKAVELLKQ-RATSVSS--SAAIAQVATVS------SRDTE-IGDLVAGA-------- 163
Cdd:pfam00118 77 AEKLLAAGVHPTTIIEGYEKALEKALEILDSiISIPVEDvdREDLLKVARTSlsskiiSRESDfLAKLVVDAvlaipknd 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 164 -MDKVGKDGVVSVEESQSIATELsvTEGVSFNKGFLSP-------------------YFITDVEAQQAILDGAQVLLVRE 223
Cdd:pfam00118 157 gSFDLGNIGVVKILGGSLEDSEL--VDGVVLDKGPLHPdmpkrlenakvlllncsleYEKTETKATVVLSDAEQLERFLK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 224 KisSLPEFLPILEKIAESGKPTLIMAEDIEGEALSALVINamrktlKVAAVKAPyfgdrRKAFMDDLAVVTGATVVtadt 303
Cdd:pfam00118 235 A--EEEQILEIVEKIIDSGVNVVVCQKGIDDLALHFLAKN------GIMALRRV-----KKRDLERLAKATGARAV---- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 304 gMQLKDVGLEVLGNARRI---TITKDETVLVDGagtaeaveerrnqiraeiertdsdwdrekleerlaKLSGGVAVIKVG 380
Cdd:pfam00118 298 -SSLDDLTPDDLGTAGKVeeeKIGDEKYTFIEG-----------------------------------CKSPKAATILLR 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 381 AATETEVNERKLRVEDAINAARAAAQE-GVIAGGGSVLVQISRELEAFADEFEGDEAVGVRAVAKALTRPAFWIAENAGK 459
Cdd:pfam00118 342 GATDHVLDEIERSIHDALCVVKNAIEDpRVVPGGGAVEMELARALREYAKSVSGKEQLAIEAFAEALEVIPKTLAENAGL 421
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 512463547 460 DGAVVVYHI-GELENGN---GYNAATDTYENLIESGVIDPVKVTHSAVVNATSVARMLLTTEASVVDK 523
Cdd:pfam00118 422 DPIEVLAELrAAHASGEkhaGIDVETGEIIDMKEAGVVDPLKVKRQALKSATEAASTILRIDDIIKAK 489
|
|
| cpn60 |
cd03343 |
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ... |
21-514 |
1.06e-29 |
|
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: 122.37 E-value: 1.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 21 TLADAVKVTLGPKGRNVVLDKAFGGPLVTNDGVTIARDIDVEDPfenlGAQLVKSVAVKTNDVAGDGTTTATLLAQALVH 100
Cdd:cd03343 26 AVAEAVRTTLGPKGMDKMLVDSLGDVTITNDGATILKEMDIEHP----AAKMLVEVAKTQDEEVGDGTTTAVVLAGELLE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 101 EGLRNVAAGANPISLNRGIHAASDKAVELLKQRATSVSSSA-----AIAQVAtVSSRDTE-----IGDLVAGAMDKV--- 167
Cdd:cd03343 102 KAEDLLDQNIHPTVIIEGYRLAAEKALELLDEIAIKVDPDDkdtlrKIAKTS-LTGKGAEaakdkLADLVVDAVLQVaek 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 168 GKDGVV--------------SVEESQSIatelsvtEGVSFNKGFLSPYFITDVE-AQQAILDGAqvLLVRE-------KI 225
Cdd:cd03343 181 RDGKYVvdldnikiekktggSVDDTELI-------RGIVIDKEVVHPGMPKRVEnAKIALLDAP--LEVKKteidakiRI 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 226 SS---LPEFLP--------ILEKIAESGKPTLIMAEDIEGEALSALvinAMRKTLKVAAVKapyfgdrrKAFMDDLAVVT 294
Cdd:cd03343 252 TSpdqLQAFLEqeeamlkeMVDKIADTGANVVFCQKGIDDLAQHYL---AKAGILAVRRVK--------KSDMEKLARAT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 295 GATVVTadtgmQLKDVGLEVLGnarrititkdetvlvdgagTAEAVEERRnqiraeiertdsDWDREKLEERLAKLSGGV 374
Cdd:cd03343 321 GAKIVT-----NIDDLTPEDLG-------------------EAELVEERK------------VGDDKMVFVEGCKNPKAV 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 375 AVIKVGAaTETEVNERKLRVEDAINAARAAAQEG-VIAGGGSVLVQISRELEAFADEFEGDEAVGVRAVAKALTRPAFWI 453
Cdd:cd03343 365 TILLRGG-TEHVVDELERALEDALRVVADALEDGkVVAGGGAVEIELAKRLREYARSVGGREQLAVEAFADALEEIPRTL 443
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 512463547 454 AENAGKDGA-VVVYHIGELENGN---GYNAATDTYENLIESGVIDPVKVTHSAVVNATSVARMLL 514
Cdd:cd03343 444 AENAGLDPIdTLVELRAAHEKGNknaGLDVYTGEVVDMLEKGVIEPLRVKKQAIKSATEAATMIL 508
|
|
| thermosome_alpha |
NF041082 |
thermosome subunit alpha; |
21-514 |
3.73e-29 |
|
thermosome subunit alpha;
Pssm-ID: 469009 Cd Length: 518 Bit Score: 120.76 E-value: 3.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 21 TLADAVKVTLGPKGRNVVLDKAFGGPLVTNDGVTIARDIDVEDPfenlGAQLVKSVAVKTNDVAGDGTTTATLLAQALVH 100
Cdd:NF041082 28 AVAEAVRTTLGPKGMDKMLVDSLGDVVITNDGVTILKEMDIEHP----AAKMIVEVAKTQDDEVGDGTTTAVVLAGELLK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 101 EGLRNVAAGANPISLNRGIHAASDKAVELLKQRATSVSSS-----AAIAQVAT----VSSRDTEIGDLVAGA----MDKV 167
Cdd:NF041082 104 KAEELLDQDIHPTIIAEGYRLAAEKALEILDEIAIKVDPDdketlKKIAATAMtgkgAEAAKDKLADLVVDAvkavAEKD 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 168 GKDGV----VSVE--ESQSIA-TELsvTEGVSFNKGFLSPYFITDVE-AQQAILDGAqvLLVRE-----KIS-----SLP 229
Cdd:NF041082 184 GGYNVdldnIKVEkkVGGSIEdSEL--VEGVVIDKERVHPGMPKRVEnAKIALLDAP--LEVKKteidaKISitdpdQLQ 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 230 EFL--------PILEKIAESGKPTLIMAEDIEGEALSALvinAMRKTLKVAAVKapyfgdrrKAFMDDLAVVTGATVVTa 301
Cdd:NF041082 260 AFLdqeekmlkEMVDKIADSGANVVFCQKGIDDLAQHYL---AKEGILAVRRVK--------KSDMEKLAKATGARIVT- 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 302 dtgmQLKDVGLEVLGNARRIT---ITKDETVLVDGAGTAEAVEerrnqiraeiertdsdwdrekleerlaklsggvavIK 378
Cdd:NF041082 328 ----SIDDLSPEDLGYAGLVEerkVGGDKMIFVEGCKNPKAVT-----------------------------------IL 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 379 VGAATETEVNERKLRVEDAINAARAAAQEG-VIAGGGSVLVQISRELEAFADEFEGDEAVGVRAVAKALTRPAFWIAENA 457
Cdd:NF041082 369 LRGGTEHVVDEVERALEDALRVVRVVLEDGkVVAGGGAPEVELALRLREYAASVGGREQLAIEAFAEALEIIPRTLAENA 448
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 512463547 458 GKDGA-VVVYHIGELENGN---GYNAATDTYENLIESGVIDPVKVTHSAVVNATSVARMLL 514
Cdd:NF041082 449 GLDPIdALVELRSAHEKGNktaGLDVYTGKVVDMLEIGVVEPLRVKTQAIKSATEAAVMIL 509
|
|
| thermosome_beta |
NF041083 |
thermosome subunit beta; |
22-514 |
1.10e-28 |
|
thermosome subunit beta;
Pssm-ID: 469010 Cd Length: 519 Bit Score: 119.28 E-value: 1.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 22 LADAVKVTLGPKGRNVVLDKAFGGPLVTNDGVTIARDIDVEDPfenlGAQLVKSVAVKTNDVAGDGTTTATLLAQALVHE 101
Cdd:NF041083 29 VAEAVRTTLGPKGMDKMLVDSLGDIVITNDGATILKEMDVQHP----AAKMLVEVAKTQDDEVGDGTTTAVVLAGELLKK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 102 GLRNVAAGANPISLNRGIHAASDKAVELLKQRATSVS----------SSAAIAQVATVSSRDtEIGDLVAGAMDKV---- 167
Cdd:NF041083 105 AEELLDQNIHPTIIANGYRLAAEKAIEILDEIAEKVDpddretlkkiAETSLTSKGVEEARD-YLAEIAVKAVKQVaekr 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 168 -GKDGV----VSVEESQSIATELS-VTEGVSFNKGFLSPYFITDVE-AQQAILDGAqvLLVRE-------KISS---LPE 230
Cdd:NF041083 184 dGKYYVdldnIQIEKKHGGSIEDTqLIYGIVIDKEVVHPGMPKRVEnAKIALLDAP--LEVKKteidaeiRITDpdqLQK 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 231 FL--------PILEKIAESGKPTLIMAEDIEGEALSALvinAMRKTLKVAAVKapyfgdrrKAFMDDLAVVTGATVVTad 302
Cdd:NF041083 262 FLdqeekmlkEMVDKIKATGANVVFCQKGIDDLAQHYL---AKAGILAVRRVK--------KSDMEKLAKATGARIVT-- 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 303 tgmQLKDVGLEVLGNARRIT---ITKDETVLVDGAGTAEAVEerrnqiraeiertdsdwdrekleerlaklsggvavIKV 379
Cdd:NF041083 329 ---NIDDLTPEDLGYAELVEerkVGDDKMVFVEGCKNPKAVT-----------------------------------ILI 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 380 GAATETEVNERKLRVEDAINAARAAAQEG-VIAGGGSVLVQISRELEAFADEFEGDEAVGVRAVAKALTRPAFWIAENAG 458
Cdd:NF041083 371 RGGTEHVVDEAERALEDALSVVADAVEDGkIVAGGGAPEVELAKRLREYAATVGGREQLAVEAFAEALEIIPRTLAENAG 450
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 459 KDGA-VVVYHIGELENGN---GYNAATDTYENLIESGVIDPVKVTHSAVVNATSVARMLL 514
Cdd:NF041083 451 LDPIdILVKLRSAHEKGKkwaGINVFTGEVVDMWELGVIEPLRVKTQAIKSATEAATMIL 510
|
|
| TCP1_delta |
cd03338 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ... |
22-514 |
1.42e-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: 100.82 E-value: 1.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 22 LADAVKVTLGPKGRNVVLDKAFGGPLVTNDGVTIARDIDVEDPFENLGAQLvksvaVKTNDV-AGDGTTTATLLAQALVH 100
Cdd:cd03338 20 VADAIRTSLGPRGMDKMIQTGKGEVIITNDGATILKQMSVLHPAAKMLVEL-----SKAQDIeAGDGTTSVVVLAGALLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 101 EGLRNVAAGANPISLNRGIHAASDKAVELLKQRATSVSSS--AAIAQVAT-------VSSRDTEIGDLVAGAMDKVGKDG 171
Cdd:cd03338 95 ACESLLKKGIHPTVISESFQIAAKKAVEILDSMSIPVDLNdrESLIKSATtslnskvVSQYSSLLAPIAVDAVLKVIDPA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 172 VVSVEESQSIA-----------TELsvTEGVSFN----KGFLSPYFI----------------TDVEAQQAILDGAQV-L 219
Cdd:cd03338 175 TATNVDLKDIRivkklggtiedTEL--VDGLVFTqkasKKAGGPTRIekakigliqfclsppkTDMDNNIVVNDYAQMdR 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 220 LVREKISSLpefLPILEKIAESGKPTLIMAEDIEGEALSALVINAMRKtLKVAAVKapyfgDRRKAFMDDLAVVTGATVV 299
Cdd:cd03338 253 ILREERKYI---LNMCKKIKKSGCNVLLIQKSILRDAVSDLALHFLAK-LKIMVVK-----DIEREEIEFICKTIGCKPV 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 300 ------TADTGMQLKDVGLEVLGNAR--RITITKDE----TVLVDGAGtaeaveerrNQIRAEIERTDSDwdrekleerl 367
Cdd:cd03338 324 asidhfTEDKLGSADLVEEVSLGDGKivKITGVKNPgktvTILVRGSN---------KLVLDEAERSLHD---------- 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 368 aklsgGVAVIKvgaateTEVNERKLrvedainaaraaaqegvIAGGGSVLVQISRELEAFADEFEGDEAVGVRAVAKALT 447
Cdd:cd03338 385 -----ALCVIR------CLVKKRAL-----------------IPGGGAPEIEIALQLSEWARTLTGVEQYCVRAFADALE 436
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 512463547 448 RPAFWIAENAGKDGAVVVYHI-GELENGN---GYNAATDTYENLIESGVIDPVKVTHSAVVNATSVARMLL 514
Cdd:cd03338 437 VIPYTLAENAGLNPISIVTELrNRHAQGEknaGINVRKGAITNILEENVVQPLLVSTSAITLATETVRMIL 507
|
|
| chaperonin_like |
cd03333 |
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ... |
143-396 |
2.30e-22 |
|
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: 95.23 E-value: 2.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 143 IAQVATVSSR------DTEIGDLVAGAMDKVGKD------GVVSVEESQS-IATELSVTEGVSFNKGFLSPYFITDVEaq 209
Cdd:cd03333 4 LLQVATTSLNsklsswDDFLGKLVVDAVLKVGPDnrmddlGVIKVEKIPGgSLEDSELVVGVVFDKGYASPYMPKRLE-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 210 qaildGAQVLLVREKISslpeflpilekiaesgkpTLIMAED-IEGEALSALVInamrktLKVAAVKApyfgdRRKAFMD 288
Cdd:cd03333 82 -----NAKILLLDCPLE------------------YVVIAEKgIDDLALHYLAK------AGIMAVRR-----VKKEDLE 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 289 DLAVVTGATVVTadtgmQLKDVGLEVLGNARRITITKD----ETVLVDGAGtaeaveerrnqiraeiertdsdwdrekle 364
Cdd:cd03333 128 RIARATGATIVS-----SLEDLTPEDLGTAELVEETKIgeekLTFIEGCKG----------------------------- 173
|
250 260 270
....*....|....*....|....*....|..
gi 512463547 365 erlaklsGGVAVIKVGAATETEVNERKLRVED 396
Cdd:cd03333 174 -------GKAATILLRGATEVELDEVKRSLHD 198
|
|
| chap_CCT_delta |
TIGR02342 |
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ... |
22-514 |
7.08e-19 |
|
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: 89.46 E-value: 7.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 22 LADAVKVTLGPKGRNVVLDKAFGGPLVTNDGVTIARDIDVEDPfenlGAQLVKSVAVKTNDVAGDGTTTATLLAQALVHE 101
Cdd:TIGR02342 21 VADAIRTSLGPKGMDKMIQDGKGEVIITNDGATILKQMAVLHP----AAKMLVELSKAQDIEAGDGTTSVVILAGALLGA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 102 GLRNVAAGANPISLNRGIHAASDKAVELLKQRATSVSSS-------------------------AAIAQVATVSSRDTEI 156
Cdd:TIGR02342 97 CERLLNKGIHPTIISESFQSAADEAIKILDEMSIPVDLSdreqllksattslsskvvsqyssllAPLAVDAVLKVIDPEN 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 157 GDLVAGAMDKVGKDGVVSVEESQSIatelsvtEGVSFNKGF---------------------LSPYfITDVEAQQAILDG 215
Cdd:TIGR02342 177 AKNVDLNDIKVVKKLGGTIDDTELI-------EGLVFTQKAsksaggptriekakigliqfqISPP-KTDMENQIIVNDY 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 216 AQV-LLVREKISSLpefLPILEKIAESGKPTLIMAEDIEGEALSALVINAMRKtLKVAAVKapyfgDRRKAFMDDLAVVT 294
Cdd:TIGR02342 249 AQMdRVLKEERAYI---LNIVKKIKKTGCNVLLIQKSILRDAVNDLALHFLAK-MKIMVVK-----DIEREEIEFICKTI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 295 GAtvvtadtgmqlkdvglevlgnarrITITKDETVLVDGAGTAEAVEErrnqiraeierTDSDwdreklEERLAKLSG-- 372
Cdd:TIGR02342 320 GC------------------------KPIASIDHFTADKLGSAELVEE-----------VDSD------GGKIIKITGiq 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 373 --GVAV-IKVGAATETEVNERKLRVEDAINAARAAAQE-GVIAGGGSVLVQISRELEAFADEFEGDEAVGVRAVAKALTR 448
Cdd:TIGR02342 359 naGKTVtVVVRGSNKLVIDEAERSLHDALCVIRCLVKKrGLIAGGGAPEIEIARRLSKYARTMKGVESYCVRAFADALEV 438
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 449 PAFWIAENAGKDGAVVVYHIGEL-ENGN---GYNAATDTYENLIESGVIDPVKVTHSAVVNATSVARMLL 514
Cdd:TIGR02342 439 IPYTLAENAGLNPIKVVTELRNRhANGEktaGISVRKGGITNMLEEHVLQPLLVTTSAITLASETVRSIL 508
|
|
| TCP1_beta |
cd03336 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ... |
9-514 |
4.06e-17 |
|
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: 84.30 E-value: 4.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 9 EEAREGLKRGVDTLADAVKVTLGPKGRNVVL--DKAFGGPLVTNDGVTIARDIDVEDPfenlGAQLVKSVAVKTNDVAGD 86
Cdd:cd03336 12 ETARLSSFVGAIAIGDLVKTTLGPKGMDKILqsVGRSGGVTVTNDGATILKSIGVDNP----AAKVLVDISKVQDDEVGD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 87 GTTTATLLAQALVHEGLRNVAAGANPISLNRGIHAASDKAVELLKQRATSVSSSAA--------IAQvATVSSRD-TEIG 157
Cdd:cd03336 88 GTTSVTVLAAELLREAEKLVAQKIHPQTIIEGYRMATAAAREALLSSAVDHSSDEEafredllnIAR-TTLSSKIlTQDK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 158 DLVAgamdKVGKDGVVSVEESQSI-ATELSVTEGVSFNKGFLSPYFITDVE---AQQAILDGAQVLLV------------ 221
Cdd:cd03336 167 EHFA----ELAVDAVLRLKGSGNLdAIQIIKKLGGSLKDSYLDEGFLLDKKigvNQPKRIENAKILIAntpmdtdkikif 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 222 --REKISSLPEFLPI--LEKIAESGKPTLIMAEDIEGEALSALVINAMRKTLKVAAVKAPYFGDrrkaF--MDDLAVVTG 295
Cdd:cd03336 243 gaKVRVDSTAKVAEIeeAEKEKMKNKVEKILKHGINCFINRQLIYNYPEQLFADAGIMAIEHAD----FdgVERLALVTG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 296 ATVV-TADTGMQLKdvglevLGNARRItitkdETVLVDgagtaeaveerrnqiraeiertdsdwdreklEERLAKLSG-- 372
Cdd:cd03336 319 GEIAsTFDHPELVK------LGTCKLI-----EEIMIG-------------------------------EDKLIRFSGva 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 373 --GVAVIKVGAATETEVNERKLRVEDAINAARAAAQEG-VIAGGGSVLVQISRELEAFADEFEGDEAVGVRAVAKALTRP 449
Cdd:cd03336 357 agEACTIVLRGASQQILDEAERSLHDALCVLAQTVKDTrVVLGGGCSEMLMAKAVEELAKKTPGKKSLAIEAFAKALRQL 436
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 512463547 450 AFWIAENAGKDGAVVVYHI-GELENGN---GYNAATDTYENLIESGVIDPVKVTHSAVVNATSVARMLL 514
Cdd:cd03336 437 PTIIADNAGYDSAELVAQLrAAHYNGNttaGLDMRKGTVGDMKELGITESFKVKRQVLLSASEAAEMIL 505
|
|
| chap_CCT_epsi |
TIGR02343 |
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ... |
19-514 |
4.15e-16 |
|
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: 81.00 E-value: 4.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 19 VDTLADAVKVTLGPKGRNVVLDKAFGGPLVTNDGVTIARDIDVEDPFENLGAQLVKSvavkTNDVAGDGTTTATLLAQAL 98
Cdd:TIGR02343 36 AKSVASILRTSLGPKGMDKMLISPDGDITVTNDGATILSQMDVDNQIAKLMVELSKS----QDDEIGDGTTGVVVLAGAL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 99 VHEGLRNVAAGANPISLNRGIHAASDKAVELLKQRATSVSSSAAI------AQVATVSS--------RDTEIG-DLVAGA 163
Cdd:TIGR02343 112 LEQAEELLDKGIHPIKIADGFEEAARIAVEHLEEISDEISADNNNrepliqAAKTSLGSkivskchrRFAEIAvDAVLNV 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 164 MDKVGKD---GVVSVEEsqSIATELSVTE---GVSFNKGFLSPYFITDVE-AQQAIL-----------DGAQVLLVREKI 225
Cdd:TIGR02343 192 ADMERRDvdfDLIKVEG--KVGGSLEDTKlikGIIIDKDFSHPQMPKEVEdAKIAILtcpfeppkpktKHKLDISSVEEY 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 226 SSLPE-----FLPILEKIAESGKPTLIMAEDIEGEALSALVINAMRKTLKVAAVKapyfgdrrkafMDDLAVVTGATVVT 300
Cdd:TIGR02343 270 KKLQKyeqqkFKEMIDDIKKSGANLVICQWGFDDEANHLLLQNDLPAVRWVGGQE-----------LELIAIATGGRIVP 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 301 adtgmQLKDVGLEVLGNARRIT-----ITKDETVLVDGAGTAEAVeerrnqiraeiertdsdwdrekleerlaklsggva 375
Cdd:TIGR02343 339 -----RFQELSKDKLGKAGLVReisfgTTKDRMLVIEQCKNSKAV----------------------------------- 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 376 VIKVGAATETEVNERKLRVEDAINAARAAAQEG-VIAGGGSVLVQISRELEAFADEFEGDEAVGVRAVAKALTRPAFWIA 454
Cdd:TIGR02343 379 TIFIRGGNKMIIEEAKRSIHDALCVVRNLIKDSrIVYGGGAAEISCSLAVSQEADKYPGVEQYAIRAFADALETIPMALA 458
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 512463547 455 ENAGKD--GAVVVYHIGELENGN---GYNAATDTYENLIESGVIDPVKVTHSAVVNATSVARMLL 514
Cdd:TIGR02343 459 ENSGLDpiGTLSTLKSLQLKEKNpnlGVDCLGYGTNDMKEQFVFETLIGKKQQILLATQLVRMIL 523
|
|
| chap_CCT_eta |
TIGR02345 |
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ... |
15-523 |
3.05e-15 |
|
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: 78.26 E-value: 3.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 15 LKRGVDT----------------LADAVKVTLGPKGRNVVLDKAFGGPLVTNDGVTIARDIDVEDPfenlGAQLVKSVAV 78
Cdd:TIGR02345 7 LKEGTDTsqgkgqlisninacvaIAEALKTTLGPRGMDKLIVGSNGKATISNDGATILKLLDIVHP----AAKTLVDIAK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 79 KTNDVAGDGTTTATLLAQALVHEGLRNVAAGANPISLNRGIHAASDKAVELLKQRATSVS------------------SS 140
Cdd:TIGR02345 83 SQDAEVGDGTTSVTILAGELLKEAKPFIEEGVHPQLIIRCYREALSLAVEKIKEIAVTIDeekgeqrellekcaatalSS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 141 AAIAQ---------VATVSSRDTEIGDLVAGAMDKVgKDGvvSVEESQSIAtelsvteGVSFNKGFLSPYF--------- 202
Cdd:TIGR02345 163 KLISHnkeffskmiVDAVLSLDRDDLDLKLIGIKKV-QGG--ALEDSQLVN-------GVAFKKTFSYAGFeqqpkkfan 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 203 ----------------------ITDVEAQQAILDgAQVLLVREKisslpeflpiLEKIAESGKptlimaediegealsal 260
Cdd:TIGR02345 233 pkilllnvelelkaekdnaeirVEDVEDYQAIVD-AEWAIIFRK----------LEKIVESGA----------------- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 261 viNAMRKTLKVAAVKAPYFGDRRkafmddlaVVTGATVVTADTGMQLKDVGLEVLGNARRITitkdETVLvdgaGTAEAV 340
Cdd:TIGR02345 285 --NVVLSKLPIGDLATQYFADRD--------IFCAGRVSAEDLKRVIKACGGSIQSTTSDLE----ADVL----GTCALF 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 341 EERrnQIRAEiertdsdwdREKLEERLAKLSGGVAVIKVGAATETEVNERKLrvEDAINAARAAAQ-EGVIAGGGSVLVQ 419
Cdd:TIGR02345 347 EER--QIGSE---------RYNYFTGCPHAKTCTIILRGGAEQFIEEAERSL--HDAIMIVRRALKnKKIVAGGGAIEME 413
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 420 ISRELEAFADEFEGDEAVGVRAVAKALTRPAFWIAENAGKDGAVVVYHIGELENGNGYNAA----TDTYENLIESGVIDP 495
Cdd:TIGR02345 414 LSKCLRDYSKTIDGKQQLIINAFAKALEIIPRQLCENAGFDSIEILNKLRSRHAKGGKWYGvdinTEDIGDNFEAFVWEP 493
|
570 580
....*....|....*....|....*...
gi 512463547 496 VKVTHSAVVNATSVARMLLTTEASVVDK 523
Cdd:TIGR02345 494 ALVKINALKAAFEAACTILSVDETITNP 521
|
|
| TCP1_eta |
cd03340 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ... |
15-523 |
7.04e-14 |
|
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: 73.86 E-value: 7.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 15 LKRGVDT----------------LADAVKVTLGPKGRNVVLDKAFGGPLVTNDGVTIARDIDVEDPfenlGAQLVKSVAV 78
Cdd:cd03340 5 LKEGTDTsqgkgqlisninacqaIADAVRTTLGPRGMDKLIVDGRGKVTISNDGATILKLLDIVHP----AAKTLVDIAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 79 KTNDVAGDGTTTATLLAQALVHEGLRNVAAGANPISLNRGIHAASDKAVELLKQRATSVS-------------------S 139
Cdd:cd03340 81 SQDAEVGDGTTSVVVLAGEFLKEAKPFIEDGVHPQIIIRGYRKALQLAIEKIKEIAVNIDkedkeeqrellekcaatalN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 140 SAAIAQ---------VATVSSRDTEIGDLVAGaMDKVgKDGvvSVEESQSIAtelsvteGVSFNKGF------------L 198
Cdd:cd03340 161 SKLIASekeffakmvVDAVLSLDDDLDLDMIG-IKKV-PGG--SLEDSQLVN-------GVAFKKTFsyagfeqqpkkfK 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 199 SPYF-------------------ITDVEAQQAILDgAQVLLVREKisslpeflpiLEKIAESGKPTLimaediegeaLSA 259
Cdd:cd03340 230 NPKIlllnvelelkaekdnaevrVEDPEEYQAIVD-AEWKIIYDK----------LEKIVKSGANVV----------LSK 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 260 LVInamrktlkvAAVKAPYFGDRR--------KAFMDDLAVVTGATVVTadTGMQLKDvglEVLgnarrititkdetvlv 331
Cdd:cd03340 289 LPI---------GDLATQYFADRDifcagrvpEEDLKRVAQATGGSIQT--TVSNITD---DVL---------------- 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 332 dgaGTAEAVEERrnQIRAEiertdsdwdREKLEERLAKLSGGVAVIKVGAATETEVNERKLrvEDAINAARAAAQEG-VI 410
Cdd:cd03340 339 ---GTCGLFEER--QVGGE---------RYNIFTGCPKAKTCTIILRGGAEQFIEEAERSL--HDAIMIVRRAIKNDsVV 402
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 411 AGGGSVLVQISRELEAFADEFEGDEAVGVRAVAKALTRPAFWIAENAGKDGAVVVYHIGEL-ENGNGYNAATDTYE---- 485
Cdd:cd03340 403 AGGGAIEMELSKYLRDYSRTIAGKQQLVINAFAKALEIIPRQLCDNAGFDATDILNKLRQKhAQGGGKWYGVDINNegia 482
|
570 580 590
....*....|....*....|....*....|....*...
gi 512463547 486 NLIESGVIDPVKVTHSAVVNATSVARMLLTTEASVVDK 523
Cdd:cd03340 483 DNFEAFVWEPSLVKINALTAATEAACLILSVDETIKNP 520
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
22-514 |
3.31e-13 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 71.98 E-value: 3.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 22 LADAVKVTLGPKGRNVVLDKAFGGP-----LVTNDGVTIARDIDVEDPfenlGAQLVKSVAVKTNDVAGDGTTTATLLAQ 96
Cdd:PTZ00212 34 VADLVKTTLGPKGMDKILQPMSEGPrsgnvTVTNDGATILKSVWLDNP----AAKILVDISKTQDEEVGDGTTSVVVLAG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 97 ALVHEGLRNVAAGANPISLNRGIHAASDKAVELLKQRATSVSSSAA--------IAQvATVSSR----DTE-IGDLVAGA 163
Cdd:PTZ00212 110 ELLREAEKLLDQKIHPQTIIEGWRMALDVARKALEEIAFDHGSDEEkfkedllnIAR-TTLSSKlltvEKDhFAKLAVDA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 164 MDKVGKDGvvSVEESQSIAtelsvTEGVSFNKGFLSPYFITDVE---AQQAILDGAQVLL--------------VREKIS 226
Cdd:PTZ00212 189 VLRLKGSG--NLDYIQIIK-----KPGGTLRDSYLEDGFILEKKigvGQPKRLENCKILVantpmdtdkikiygAKVKVD 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 227 SLPEFLPI--LEKIAESGKPTLIMAEDIEGEALSALVINAMRKTLKVAAVKAPYFGDrrkaF--MDDLAVVTGATVV-TA 301
Cdd:PTZ00212 262 SMEKVAEIeaAEKEKMKNKVDKILAHGCNVFINRQLIYNYPEQLFAEAGIMAIEHAD----FdgMERLAAALGAEIVsTF 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 302 DTGMQLKdvglevLGNARR---ITITKDETVLVDGAGTAEA----VEERRNQIRAEIERTdsdwdrekLEERLAKLSggv 374
Cdd:PTZ00212 338 DTPEKVK------LGHCDLieeIMIGEDKLIRFSGCAKGEActivLRGASTHILDEAERS--------LHDALCVLS--- 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 375 avikvgaateTEVNERKlrvedainaaraaaqegVIAGGGSVLVQISRELEAFADEFEGDEAVGVRAVAKALTRPAFWIA 454
Cdd:PTZ00212 401 ----------QTVKDTR-----------------VVLGGGCSEMLMANAVEELAKKVEGKKSLAIEAFAKALRQIPTIIA 453
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 512463547 455 ENAGKDGAVVVYHI-GELENGN---GYNAATDTYENLIESGVIDPVKVTHSAVVNATSVARMLL 514
Cdd:PTZ00212 454 DNGGYDSAELVSKLrAEHYKGNktaGIDMEKGTVGDMKELGITESYKVKLSQLCSATEAAEMIL 517
|
|
| TCP1_epsilon |
cd03339 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ... |
21-514 |
9.74e-11 |
|
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: 64.24 E-value: 9.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 21 TLADAVKVTLGPKGrnvvLDKAFGGP----LVTNDGVTIARDIDVEDPFENLGAQLVKSvavkTNDVAGDGTTTATLLAQ 96
Cdd:cd03339 34 SVANILRTSLGPRG----MDKILVSPdgevTVTNDGATILEKMDVDHQIAKLLVELSKS----QDDEIGDGTTGVVVLAG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 97 ALVHEGLRNVAAGANPISLNRGIHAASDKAVELLKQRATSVSSSA----AIAQVATVS------SRD----TEIG-DLVA 161
Cdd:cd03339 106 ALLEQAEKLLDRGIHPIRIADGYEQACKIAVEHLEEIADKIEFSPdnkePLIQTAMTSlgskivSRChrqfAEIAvDAVL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 162 GAMDKVGKD---------GVV--SVEESQSIatelsvtEGVSFNKGFLSPYFITDVE-AQQAIL---------------- 213
Cdd:cd03339 186 SVADLERKDvnfelikveGKVggRLEDTKLV-------KGIVIDKDFSHPQMPKEVKdAKIAILtcpfeppkpktkhkld 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 214 ----DGAQVLLVREKisslPEFLPILEKIAESGKPTLIMAEDIEGEALSALV---INAMRktlkvaAVKAPYfgdrrkaf 286
Cdd:cd03339 259 itsvEDYKKLQEYEQ----KYFREMVEQVKDAGANLVICQWGFDDEANHLLLqngLPAVR------WVGGVE-------- 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 287 MDDLAVVTGATVVTadtgmQLKDVGLEVLGNARRI-----TITKDETVLVDGAGTAEAV----EERRNQIRAEIERTDSD 357
Cdd:cd03339 321 IELIAIATGGRIVP-----RFEDLSPEKLGKAGLVreisfGTTKDKMLVIEGCPNSKAVtifiRGGNKMIIEEAKRSLHD 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 358 wdrekleerlaklsgGVAVIkvgaatetevneRKLrVEDAInaaraaaqegVIAGGGSVLVQISRELEAFADEFEGDEAV 437
Cdd:cd03339 396 ---------------ALCVV------------RNL-IRDNR----------IVYGGGAAEISCSLAVEKAADKCSGIEQY 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 438 GVRAVAKALTRPAFWIAENAGKD--GAVVVYHIGELENGN---GYNAATDTYENLIESGVIDPVKVTHSAVVNATSVARM 512
Cdd:cd03339 438 AMRAFADALESIPLALAENSGLNpiETLSEVKARQVKEKNphlGIDCLGRGTNDMKEQKVFETLISKKQQILLATQVVKM 517
|
..
gi 512463547 513 LL 514
Cdd:cd03339 518 IL 519
|
|
| chap_CCT_beta |
TIGR02341 |
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ... |
9-514 |
1.15e-10 |
|
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT beta chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.
Pssm-ID: 274082 Cd Length: 519 Bit Score: 63.73 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 9 EEAREGLKRGVDTLADAVKVTLGPKGRNVVLDKA--FGGPLVTNDGVTIARDIDVEDPfenlGAQLVKSVAVKTNDVAGD 86
Cdd:TIGR02341 13 ENARLSSFVGAIAIGDLVKSTLGPKGMDKILQSSssDASIMVTNDGATILKSIGVDNP----AAKVLVDMSKVQDDEVGD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 87 GTTTATLLAQALVHEGLRNVAAGANPISLNRGIHAASDKAVELLKQRATSVSSSAA--------IAQVATVSSRDTEIGD 158
Cdd:TIGR02341 89 GTTSVTVLAAELLREAEKLINQKIHPQTIIAGYREATKAARDALLKSAVDNGSDEVkfrqdlmnIARTTLSSKILSQHKD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 159 LVAgamdKVGKDGVVSVEESQSI-ATELSVTEGVSFNKGFLSPYFITDVEA---QQAILDGAQVLLV------------- 221
Cdd:TIGR02341 169 HFA----QLAVDAVLRLKGSGNLeAIQIIKKLGGSLADSYLDEGFLLDKKIgvnQPKRIENAKILIAntgmdtdkvkifg 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 222 -REKISSLPEF--LPILEKIAESGKPTLIMAEDIEGEALSALVINAMRKTLKVAAVKAPYFGDRRKafMDDLAVVTGATV 298
Cdd:TIGR02341 245 sRVRVDSTAKVaeLEHAEKEKMKEKVEKILKHGINCFINRQLIYNYPEQLFADAGVMAIEHADFEG--VERLALVTGGEI 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 299 VTadtgmqlkdvglevlgnarritiTKDETVLVDgAGTAEAVEERRNQiraeiertdsdwdreklEERLAKLSGGVA--- 375
Cdd:TIGR02341 323 VS-----------------------TFDHPELVK-LGSCDLIEEIMIG-----------------EDKLLKFSGVKLgea 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 376 -VIKVGAATETEVNERKLRVEDAINAARAAAQEG-VIAGGGSVLVQISRELEAFADEFEGDEAVGVRAVAKALTRPAFWI 453
Cdd:TIGR02341 362 cTIVLRGATQQILDEAERSLHDALCVLSQTVKESrTVLGGGCSEMLMSKAVTQEAQRTPGKEALAVEAFARALRQLPTII 441
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 512463547 454 AENAGKDGAVVVYHI-GELENGN---GYNAATDTYENLIESGVIDPVKVTHSAVVNATSVARMLL 514
Cdd:TIGR02341 442 ADNAGFDSAELVAQLrAAHYNGNttmGLDMNEGTIADMRQLGITESYKVKRAVVSSAAEAAEVIL 506
|
|
| chap_CCT_alpha |
TIGR02340 |
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ... |
22-528 |
6.82e-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: 61.66 E-value: 6.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 22 LADAVKVTLGPKGRNVVLDKAFGGPLVTNDGVTIARDIDVEDPfenlGAQLVKSVAVKTNDVAGDGTTTATLLAQALVHE 101
Cdd:TIGR02340 24 IANIVKTSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHP----AAKILVELAQLQDREVGDGTTSVVIIAAELLKR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 102 GLRNVAAGANPISLNRGIHAASDKAVELLKQR-ATSVSS--SAAIAQVATVSSRDTEIGdLVAGAMDKVGKDGVVSVEES 178
Cdd:TIGR02340 100 ADELVKNKIHPTSVISGYRLACKEAVKYIKENlSVSVDElgREALINVAKTSMSSKIIG-LDSDFFSNIVVDAVLAVKTT 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 179 QSI-------------------ATELSVTEGVSFNKGFLSPYFITDVE-AQQAILD----------GAQVL--------- 219
Cdd:TIGR02340 179 NENgetkypikainilkahgksARESMLVKGYALNCTVASQQMPKRIKnAKIACLDfnlqkakmalGVQIVvddpekleq 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 220 -------LVREKIsslpeflpilEKIAESGKPTLIMAEDIEGEALSALV-INAMrktlkvaavkapyfGDRR--KAFMDD 289
Cdd:TIGR02340 259 irqreadITKERI----------KKILDAGANVVLTTGGIDDMCLKYFVeAGAM--------------GVRRckKEDLKR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 290 LAVVTGATVVTADTgmqlkdvglevlgnarriTITKDETVLVDGAGTAEAVEERRNQiraeiertdsdwDREKLEERLAK 369
Cdd:TIGR02340 315 IAKATGATLVSTLA------------------DLEGEETFEASYLGFADEVVQERIA------------DDECILIKGTK 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 370 LSGGVAVIKVGaATETEVNERKLRVEDAINAARAAAQEG-VIAGGGSVLVQISRELEAFADEFEGDEAVGVRAVAKALTR 448
Cdd:TIGR02340 365 KRKSASIILRG-ANDFMLDEMERSLHDALCVVKRTLESNsVVPGGGAVEAALSIYLENFATTLGSREQLAIAEFARALLI 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 449 PAFWIAENAGKDGAVVVYHIGELENGNGYNAATDTYENL------------IESGVIDPVKVTHSAVVNATSVARMLLTT 516
Cdd:TIGR02340 444 IPKTLAVNAAKDSTELVAKLRAYHAAAQLKPEKKHLKWYgldlvngkirdnKEAGVLEPTVSKVKSLKFATEAAITILRI 523
|
570
....*....|..
gi 512463547 517 EASVVDKPEEEP 528
Cdd:TIGR02340 524 DDLIKLNPEQSK 535
|
|
| TCP1_gamma |
cd03337 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ... |
21-140 |
6.45e-08 |
|
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.
Pssm-ID: 239453 [Multi-domain] Cd Length: 480 Bit Score: 54.99 E-value: 6.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 21 TLADAVKVTLGPKGR-NVVLDKaFGGPLVTNDGVTIARDIDVEDPfenlGAQLVKSVAVKTNDVAGDGTTTATLLAQALV 99
Cdd:cd03337 27 TVADVIRTCLGPRAMlKMLLDP-MGGIVLTNDGNAILREIDVAHP----AAKSMIELSRTQDEEVGDGTTSVIILAGEIL 101
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 512463547 100 HEGLRNVAAGANPISLNRGIHAASDKAVELLKQRATSVSSS 140
Cdd:cd03337 102 AVAEPFLERGIHPTVIIKAYRKALEDALKILEEISIPVDVN 142
|
|
| chap_CCT_zeta |
TIGR02347 |
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ... |
22-132 |
1.47e-07 |
|
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: 53.97 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 22 LADAVKVTLGPKGRNVVLDKAFGGPLVTNDGVTIARDIDVEDPfenlGAQLVKSVAVKTNDVAGDGTTTATLLAQALVHE 101
Cdd:TIGR02347 28 LQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEMQIQHP----TASMIARAATAQDDITGDGTTSTVLLIGELLKQ 103
|
90 100 110
....*....|....*....|....*....|.
gi 512463547 102 GLRNVAAGANPISLNRGIHAASDKAVELLKQ 132
Cdd:TIGR02347 104 AERYILEGVHPRIITEGFEIARKEALQFLDK 134
|
|
| TCP1_alpha |
cd03335 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ... |
22-139 |
4.03e-07 |
|
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.
Pssm-ID: 239451 Cd Length: 527 Bit Score: 52.67 E-value: 4.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 22 LADAVKVTLGPKGRNVVLDKAFGGPLVTNDGVTIARDIDVEDPfenlGAQLVKSVAVKTNDVAGDGTTTATLLAQALVHE 101
Cdd:cd03335 20 IANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHP----AAKILVELAQLQDKEVGDGTTSVVIIAAELLKR 95
|
90 100 110
....*....|....*....|....*....|....*....
gi 512463547 102 GLRNVAAGANPISLNRGIHAASDKAVELLKQR-ATSVSS 139
Cdd:cd03335 96 ANELVKQKIHPTTIISGYRLACKEAVKYIKEHlSISVDN 134
|
|
| chap_CCT_gamma |
TIGR02344 |
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ... |
21-137 |
6.16e-07 |
|
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT gamma chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.
Pssm-ID: 274085 [Multi-domain] Cd Length: 524 Bit Score: 52.05 E-value: 6.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 21 TLADAVKVTLGPKGRNVVLDKAFGGPLVTNDGVTIARDIDVEDPfenlGAQLVKSVAVKTNDVAGDGTTTATLLAQALVH 100
Cdd:TIGR02344 27 AVADIIRTCLGPRSMLKMLLDPMGGIVMTNDGNAILREIDVAHP----AAKSMIELSRTQDEEVGDGTTSVIILAGEMLS 102
|
90 100 110
....*....|....*....|....*....|....*..
gi 512463547 101 EGLRNVAAGANPISLNRGIHAASDKAVELLKQRATSV 137
Cdd:TIGR02344 103 VAEPFLEQNIHPTVIIRAYRKALDDALSVLEEISIPV 139
|
|
| TCP1_zeta |
cd03342 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
21-137 |
4.29e-06 |
|
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: 49.18 E-value: 4.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 21 TLADAVKVTLGPKGRNVVLDKAFGGPLVTNDGVTIARDIDVEDPFenlgAQLVKSVAVKTNDVAGDGTTTATLLAQALVH 100
Cdd:cd03342 23 GLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLSEMQIQHPT----ASMIARAATAQDDITGDGTTSNVLLIGELLK 98
|
90 100 110
....*....|....*....|....*....|....*..
gi 512463547 101 EGLRNVAAGANPISLNRGIHAASDKAVELLKQRATSV 137
Cdd:cd03342 99 QAERYIQEGVHPRIITEGFELAKNKALKFLESFKVPV 135
|
|
| chap_CCT_theta |
TIGR02346 |
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ... |
22-132 |
5.02e-06 |
|
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT alpha chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.
Pssm-ID: 274087 [Multi-domain] Cd Length: 531 Bit Score: 49.33 E-value: 5.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 22 LADAVKVTLGPKGRN--VV--LDKAFggplVTNDGVTIARDIDVEDPFENLgaqLVKSVAVKTNDVaGDGTTTATLLAQA 97
Cdd:TIGR02346 30 LSQITRTSLGPNGMNkmVInhLEKLF----VTNDAATILRELEVQHPAAKL---LVMASEMQENEI-GDGTNLVLVLAGE 101
|
90 100 110
....*....|....*....|....*....|....*
gi 512463547 98 LVHEGLRNVAAGANPISLNRGIHAASDKAVELLKQ 132
Cdd:TIGR02346 102 LLNKAEELIRMGLHPSEIIKGYEMALKKAMEILEE 136
|
|
| TCP1_theta |
cd03341 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ... |
21-151 |
1.39e-05 |
|
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: 47.60 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463547 21 TLADAVKVTLGPKGRN--VV--LDKAFggplVTNDGVTIARDIDVEDPFENLgaqLVKSVAVKTNDVaGDGTTTATLLAQ 96
Cdd:cd03341 19 ELSQITRTSYGPNGMNkmVInhLEKLF----VTSDAATILRELEVQHPAAKL---LVMASQMQEEEI-GDGTNLVVVLAG 90
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 512463547 97 ALVHEGLRNVAAGANPISLNRGIHAASDKAVELLKQraTSVSSSAAIAQVATVSS 151
Cdd:cd03341 91 ELLEKAEELLRMGLHPSEIIEGYEKALKKALEILEE--LVVYKIEDLRNKEEVSK 143
|
|
| |
