|
Name |
Accession |
Description |
Interval |
E-value |
| GroEL |
cd03344 |
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ... |
28-548 |
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: 881.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 28 KDVKFGADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDRYKNIGAKLVQDVANNTNE 107
Cdd:cd03344 1 KDIKFGEEARKALLRGVNKLADAVKVTLGPKGRNVVIEKSFGSPKITKDGVTVAKEIELEDPFENMGAQLVKEVASKTND 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 108 EAGDGTTTATVLARAVAKEGFDTISKGANPVEIRRGVMMAVEEVISELKKNSKPVTTPEEIAQVATISANGDTEVGNIIS 187
Cdd:cd03344 81 VAGDGTTTATVLARAIIKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKPVKTKEEIAQVATISANGDEEIGELIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 188 NAMKKVGRKGVITVKDGKTLHDELEIIEGMKFDRGYISPYFINTAKGQKCEFQDAYVLLSEKKISSVQSIVPALEIANQH 267
Cdd:cd03344 161 EAMEKVGKDGVITVEEGKTLETELEVVEGMQFDRGYLSPYFVTDPEKMEVELENPYILLTDKKISSIQELLPILELVAKA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 268 RKPLVIVAEDVDGEALSTLVLNRLKVGLQVVAVKAPGFGDNRKNQLQDMAVSTGGTVFGDEAmGLALEDIQAHDFGKVGE 347
Cdd:cd03344 241 GRPLLIIAEDVEGEALATLVVNKLRGGLKVCAVKAPGFGDRRKAMLEDIAILTGGTVISEEL-GLKLEDVTLEDLGRAKK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 348 VIVTKDDTMLLKGRGDASAIEKRVNEIAEQLESTNSDYEKEKLNERLAKLSDGVAVIKVGGTSDVEVNEKKDRVTDALNA 427
Cdd:cd03344 320 VVVTKDDTTIIGGAGDKAAIKARIAQIRKQIEETTSDYDKEKLQERLAKLSGGVAVIKVGGATEVELKEKKDRVEDALNA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 428 TRAAVEEGIVPGGGCALLRCIPALDNIKPANADQKIGIDIIRRSLRIPAMTIAKNAGVEGSLVVEKILQSSTEIGYDAMN 507
Cdd:cd03344 400 TRAAVEEGIVPGGGVALLRASPALDKLKALNGDEKLGIEIVRRALEAPLRQIAENAGVDGSVVVEKVLESPDGFGYDAAT 479
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 31044489 508 GEYVNMVERGIIDPTKVVRTALLDAAGVASLLSTAEAVVTE 548
Cdd:cd03344 480 GEYVDMIEAGIIDPTKVVRSALQNAASVASLLLTTEALVVD 520
|
|
| PTZ00114 |
PTZ00114 |
Heat shock protein 60; Provisional |
24-558 |
0e+00 |
|
Heat shock protein 60; Provisional
Pssm-ID: 185455 Cd Length: 555 Bit Score: 787.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 24 RAYAKDVKFGADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDRYKNIGAKLVQDVAN 103
Cdd:PTZ00114 11 RFKGKEIRFGDEARQSLLKGIERLADAVAVTLGPKGRNVIIEQEYGSPKITKDGVTVAKAIEFSDRFENVGAQLIRQVAS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 104 NTNEEAGDGTTTATVLARAVAKEGFDTISKGANPVEIRRGVMMAVEEVISELKKNSKPVTTPEEIAQVATISANGDTEVG 183
Cdd:PTZ00114 91 KTNDKAGDGTTTATILARAIFREGCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQSRPVKTKEDILNVATISANGDVEIG 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 184 NIISNAMKKVGRKGVITVKDGKTLHDELEIIEGMKFDRGYISPYFINTAKGQKCEFQDAYVLLSEKKISSVQSIVPALEI 263
Cdd:PTZ00114 171 SLIADAMDKVGKDGTITVEDGKTLEDELEVVEGMSFDRGYISPYFVTNEKTQKVELENPLILVTDKKISSIQSILPILEH 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 264 ANQHRKPLVIVAEDVDGEALSTLVLNRLKVGLQVVAVKAPGFGDNRKNQLQDMAVSTGGTVFGDEAMGLALEDIQAHDFG 343
Cdd:PTZ00114 251 AVKNKRPLLIIAEDVEGEALQTLIINKLRGGLKVCAVKAPGFGDNRKDILQDIAVLTGATVVSEDNVGLKLDDFDPSMLG 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 344 KVGEVIVTKDDTMLLKGRGDASAIEKRVNEIAEQLESTNSDYEKEKLNERLAKLSDGVAVIKVGGTSDVEVNEKKDRVTD 423
Cdd:PTZ00114 331 SAKKVTVTKDETVILTGGGDKAEIKERVELLRSQIERTTSEYDKEKLKERLAKLSGGVAVIKVGGASEVEVNEKKDRIED 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 424 ALNATRAAVEEGIVPGGGCALLRCIPALDNIKPAN---ADQKIGIDIIRRSLRIPAMTIAKNAGVEGSLVVEKILQSS-T 499
Cdd:PTZ00114 411 ALNATRAAVEEGIVPGGGVALLRASKLLDKLEEDNeltPDQRTGVKIVRNALRLPTKQIAENAGVEGAVVVEKILEKKdP 490
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 31044489 500 EIGYDAMNGEYVNMVERGIIDPTKVVRTALLDAAGVASLLSTAEAVVTEIPKEEKEMPA 558
Cdd:PTZ00114 491 SFGYDAQTGEYVNMFEAGIIDPTKVVRSALVDAASVASLMLTTEAAIVDLPKEKKKNKN 549
|
|
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
27-558 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 774.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 27 AKDVKFGADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDRYKNIGAKLVQDVANNTN 106
Cdd:PRK00013 2 AKDIKFGEDARRKLLRGVNKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDPFENMGAQLVKEVASKTN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 107 EEAGDGTTTATVLARAVAKEGFDTISKGANPVEIRRGVMMAVEEVISELKKNSKPVTTPEEIAQVATISANGDTEVGNII 186
Cdd:PRK00013 82 DVAGDGTTTATVLAQAIVREGLKNVAAGANPMDLKRGIDKAVEAAVEELKKISKPVEDKEEIAQVATISANGDEEIGKLI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 187 SNAMKKVGRKGVITVKDGKTLHDELEIIEGMKFDRGYISPYFINTAKGQKCEFQDAYVLLSEKKISSVQSIVPALEIANQ 266
Cdd:PRK00013 162 AEAMEKVGKEGVITVEESKGFETELEVVEGMQFDRGYLSPYFVTDPEKMEAELENPYILITDKKISNIQDLLPVLEQVAQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 267 HRKPLVIVAEDVDGEALSTLVLNRLKVGLQVVAVKAPGFGDNRKNQLQDMAVSTGGTVFGDEaMGLALEDIQAHDFGKVG 346
Cdd:PRK00013 242 SGKPLLIIAEDVEGEALATLVVNKLRGTLKVVAVKAPGFGDRRKAMLEDIAILTGGTVISEE-LGLKLEDATLEDLGQAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 347 EVIVTKDDTMLLKGRGDASAIEKRVNEIAEQLESTNSDYEKEKLNERLAKLSDGVAVIKVGGTSDVEVNEKKDRVTDALN 426
Cdd:PRK00013 321 KVVVTKDNTTIVDGAGDKEAIKARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATEVEMKEKKDRVEDALH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 427 ATRAAVEEGIVPGGGCALLRCIPALDNIKPANADQKIGIDIIRRSLRIPAMTIAKNAGVEGSLVVEKILQSS-TEIGYDA 505
Cdd:PRK00013 401 ATRAAVEEGIVPGGGVALLRAAPALEALKGLNGDEATGINIVLRALEAPLRQIAENAGLEGSVVVEKVKNGKgKGYGYNA 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 31044489 506 MNGEYVNMVERGIIDPTKVVRTALLDAAGVASLLSTAEAVVTEIPKEEKEMPA 558
Cdd:PRK00013 481 ATGEYVDMIEAGIIDPTKVTRSALQNAASVAGLLLTTEAVVADKPEKKAAAPP 533
|
|
| groEL |
PRK12849 |
chaperonin GroEL; Reviewed |
27-558 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237230 Cd Length: 542 Bit Score: 729.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 27 AKDVKFGADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDRYKNIGAKLVQDVANNTN 106
Cdd:PRK12849 2 AKIIKFDEEARRALERGVNKLADAVKVTLGPKGRNVVIDKSFGAPTITKDGVSIAKEIELEDPFENLGAQLVKEVASKTN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 107 EEAGDGTTTATVLARAVAKEGFDTISKGANPVEIRRGVMMAVEEVISELKKNSKPVTTPEEIAQVATISANGDTEVGNII 186
Cdd:PRK12849 82 DVAGDGTTTATVLAQALVQEGLKNVAAGANPMDLKRGIDKAVEAVVEELKALARPVSGSEEIAQVATISANGDEEIGELI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 187 SNAMKKVGRKGVITVKDGKTLHDELEIIEGMKFDRGYISPYFINTAKGQKCEFQDAYVLLSEKKISSVQSIVPALEIANQ 266
Cdd:PRK12849 162 AEAMEKVGKDGVITVEESKTLETELEVTEGMQFDRGYLSPYFVTDPERMEAVLEDPLILLTDKKISSLQDLLPLLEKVAQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 267 HRKPLVIVAEDVDGEALSTLVLNRLKVGLQVVAVKAPGFGDNRKNQLQDMAVSTGGTVFGDEaMGLALEDIQAHDFGKVG 346
Cdd:PRK12849 242 SGKPLLIIAEDVEGEALATLVVNKLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGTVISED-LGLKLEEVTLDDLGRAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 347 EVIVTKDDTMLLKGRGDASAIEKRVNEIAEQLESTNSDYEKEKLNERLAKLSDGVAVIKVGGTSDVEVNEKKDRVTDALN 426
Cdd:PRK12849 321 RVTITKDNTTIVDGAGDKEAIEARVAQIRRQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATEVELKERKDRVEDALN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 427 ATRAAVEEGIVPGGGCALLRCIPALDNIKPANADQKIGIDIIRRSLRIPAMTIAKNAGVEGSLVVEKILQSSTEIGYDAM 506
Cdd:PRK12849 401 ATRAAVEEGIVPGGGVALLRAAKALDELAGLNGDQAAGVEIVRRALEAPLRQIAENAGLDGSVVVAKVLELEDGFGFNAA 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 31044489 507 NGEYVNMVERGIIDPTKVVRTALLDAAGVASLLSTAEAVVTEIPKEEKEMPA 558
Cdd:PRK12849 481 TGEYGDLIAAGIIDPVKVTRSALQNAASVAGLLLTTEALVADKPEEEDPPGG 532
|
|
| GroEL |
TIGR02348 |
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ... |
27-551 |
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: 701.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 27 AKDVKFGADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDRYKNIGAKLVQDVANNTN 106
Cdd:TIGR02348 1 AKQIKFDEEARKALLRGVDKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDKFENMGAQLVKEVASKTN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 107 EEAGDGTTTATVLARAVAKEGFDTISKGANPVEIRRGVMMAVEEVISELKKNSKPVTTPEEIAQVATISANGDTEVGNII 186
Cdd:TIGR02348 81 DVAGDGTTTATVLAQAIVKEGLKNVAAGANPIELKRGIEKAVEAVVEELKKLSKPVKGKKEIAQVATISANNDEEIGSLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 187 SNAMKKVGRKGVITVKDGKTLHDELEIIEGMKFDRGYISPYFINTAKGQKCEFQDAYVLLSEKKISSVQSIVPALEIANQ 266
Cdd:TIGR02348 161 AEAMEKVGKDGVITVEESKSLETELEVVEGMQFDRGYISPYFVTDAEKMEVELENPYILITDKKISNIKDLLPLLEKVAQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 267 HRKPLVIVAEDVDGEALSTLVLNRLKVGLQVVAVKAPGFGDNRKNQLQDMAVSTGGTVFgDEAMGLALEDIQAHDFGKVG 346
Cdd:TIGR02348 241 SGKPLLIIAEDVEGEALATLVVNKLRGTLNVCAVKAPGFGDRRKAMLEDIAILTGGQVI-SEELGLKLEEVTLDDLGKAK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 347 EVIVTKDDTMLLKGRGDASAIEKRVNEIAEQLESTNSDYEKEKLNERLAKLSDGVAVIKVGGTSDVEVNEKKDRVTDALN 426
Cdd:TIGR02348 320 KVTVDKDNTTIVEGAGDKAAIKARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATETEMKEKKLRIEDALN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 427 ATRAAVEEGIVPGGGCALLRCIPALDNIKPANADQKIGIDIIRRSLRIPAMTIAKNAGVEGSLVVEKILQSSTEIGYDAM 506
Cdd:TIGR02348 400 ATRAAVEEGIVPGGGVALLRAAAALEGLKGDGEDEAIGIDIVKRALEAPLRQIAENAGLDGAVVAEKVKELKGNFGFNAA 479
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 31044489 507 NGEYVNMVERGIIDPTKVVRTALLDAAGVASLLSTAEAVVTEIPK 551
Cdd:TIGR02348 480 TGEYEDLVEAGIIDPTKVTRSALQNAASIAGLLLTTEAVVADKPE 524
|
|
| groEL |
PRK12850 |
chaperonin GroEL; Reviewed |
27-553 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237231 Cd Length: 544 Bit Score: 696.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 27 AKDVKFGADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDRYKNIGAKLVQDVANNTN 106
Cdd:PRK12850 3 AKEIRFSTDARDRLLRGVNILANAVKVTLGPKGRNVVLEKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVKEVASKTN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 107 EEAGDGTTTATVLARAVAKEGFDTISKGANPVEIRRGVMMAVEEVISELKKNSKPVTTPEEIAQVATISANGDTEVGNII 186
Cdd:PRK12850 83 DLAGDGTTTATVLAQAIVREGAKLVAAGMNPMDLKRGIDLAVAAVVDELKKIAKKVTSSKEIAQVATISANGDESIGEMI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 187 SNAMKKVGRKGVITVKDGKTLHDELEIIEGMKFDRGYISPYFINTAKGQKCEFQDAYVLLSEKKISSVQSIVPALEIANQ 266
Cdd:PRK12850 163 AEAMDKVGKEGVITVEEAKTLGTELDVVEGMQFDRGYLSPYFVTNPEKMRAELEDPYILLHEKKISNLQDLLPILEAVVQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 267 HRKPLVIVAEDVDGEALSTLVLNRLKVGLQVVAVKAPGFGDNRKNQLQDMAVSTGGTVFGDEaMGLALEDIQAHDFGKVG 346
Cdd:PRK12850 243 SGRPLLIIAEDVEGEALATLVVNKLRGGLKSVAVKAPGFGDRRKAMLEDIAVLTGGQVISED-LGIKLENVTLDMLGRAK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 347 EVIVTKDDTMLLKGRGDASAIEKRVNEIAEQLESTNSDYEKEKLNERLAKLSDGVAVIKVGGTSDVEVNEKKDRVTDALN 426
Cdd:PRK12850 322 RVLITKENTTIIDGAGDKKNIEARVKQIRAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKEKKDRVDDALH 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 427 ATRAAVEEGIVPGGGCALLRCIPALDNIKPANADQKIGIDIIRRSLRIPAMTIAKNAGVEGSLVVEKILQSSTEIGYDAM 506
Cdd:PRK12850 402 ATRAAVEEGIVPGGGVALLRARSALRGLKGANADETAGIDIVRRALEEPLRQIATNAGFEGSVVVGKVAELPGNFGFNAQ 481
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 31044489 507 NGEYVNMVERGIIDPTKVVRTALLDAAGVASLLSTAEAVVTEIPKEE 553
Cdd:PRK12850 482 TGEYGDMVEAGIIDPAKVTRTALQDAASIAALLITTEAMVAEAPKKA 528
|
|
| groEL |
PRK12852 |
chaperonin GroEL; Reviewed |
27-558 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237232 Cd Length: 545 Bit Score: 661.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 27 AKDVKFGADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDRYKNIGAKLVQDVANNTN 106
Cdd:PRK12852 3 AKDVKFSGDARDRMLRGVDILANAVKVTLGPKGRNVVIEKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVREVASKTN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 107 EEAGDGTTTATVLARAVAKEGFDTISKGANPVEIRRGVMMAVEEVISELKKNSKPVTTPEEIAQVATISANGDTEVGNII 186
Cdd:PRK12852 83 DLAGDGTTTATVLAQAIVREGAKAVAAGMNPMDLKRGIDIAVAAVVKDIEKRAKPVASSAEIAQVGTISANGDAAIGKMI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 187 SNAMKKVGRKGVITVKDGKTLHDELEIIEGMKFDRGYISPYFINTAKGQKCEFQDAYVLLSEKKISSVQSIVPALEIANQ 266
Cdd:PRK12852 163 AQAMQKVGNEGVITVEENKSLETEVDIVEGMKFDRGYLSPYFVTNAEKMTVELDDAYILLHEKKLSGLQAMLPVLEAVVQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 267 HRKPLVIVAEDVDGEALSTLVLNRLKVGLQVVAVKAPGFGDNRKNQLQDMAVSTGGTVFGDEaMGLALEDIQAHDFGKVG 346
Cdd:PRK12852 243 SGKPLLIIAEDVEGEALATLVVNRLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGQLISED-LGIKLENVTLKMLGRAK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 347 EVIVTKDDTMLLKGRGDASAIEKRVNEIAEQLESTNSDYEKEKLNERLAKLSDGVAVIKVGGTSDVEVNEKKDRVTDALN 426
Cdd:PRK12852 322 KVVIDKENTTIVNGAGKKADIEARVGQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKEKKDRVEDALN 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 427 ATRAAVEEGIVPGGGCALLRCIPALDNIKPANADQKIGIDIIRRSLRIPAMTIAKNAGVEGSLVVEKILQSSTE-IGYDA 505
Cdd:PRK12852 402 ATRAAVQEGIVPGGGVALLRAKKAVGRINNDNADVQAGINIVLKALEAPIRQIAENAGVEGSIVVGKILENKSEtFGFDA 481
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 31044489 506 MNGEYVNMVERGIIDPTKVVRTALLDAAGVASLLSTAEAVVTEIPKEEKEMPA 558
Cdd:PRK12852 482 QTEEYVDMVAKGIIDPAKVVRTALQDAASVAGLLVTTEAMVAELPKKDAAPAM 534
|
|
| groEL |
PRK12851 |
chaperonin GroEL; Reviewed |
27-558 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 171770 Cd Length: 541 Bit Score: 650.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 27 AKDVKFGADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDRYKNIGAKLVQDVANNTN 106
Cdd:PRK12851 3 AKEVKFHVEAREKMLRGVNILADAVKVTLGPKGRNVVIDKSFGAPTITNDGVTIAKEIELEDKFENMGAQMVREVASKTN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 107 EEAGDGTTTATVLARAVAKEGFDTISKGANPVEIRRGVMMAVEEVISELKKNSKPVTTPEEIAQVATISANGDTEVGNII 186
Cdd:PRK12851 83 DVAGDGTTTATVLAQAIVREGAKAVAAGANPMDLKRGIDRAVAAVVEELKANARPVTTNAEIAQVATISANGDAEIGRLV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 187 SNAMKKVGRKGVITVKDGKTLHDELEIIEGMKFDRGYISPYFINTAKGQKCEFQDAYVLLSEKKISSVQSIVPALEIANQ 266
Cdd:PRK12851 163 AEAMEKVGNEGVITVEESKTAETELEVVEGMQFDRGYLSPYFVTDADKMEAELEDPYILIHEKKISNLQDLLPVLEAVVQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 267 HRKPLVIVAEDVDGEALSTLVLNRLKVGLQVVAVKAPGFGDNRKNQLQDMAVSTGGTVFGDEAmGLALEDIQAHDFGKVG 346
Cdd:PRK12851 243 SGKPLLIIAEDVEGEALATLVVNKLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGTVISEDL-GIKLENVTLEQLGRAK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 347 EVIVTKDDTMLLKGRGDASAIEKRVNEIAEQLESTNSDYEKEKLNERLAKLSDGVAVIKVGGTSDVEVNEKKDRVTDALN 426
Cdd:PRK12851 322 KVVVEKENTTIIDGAGSKTEIEGRVAQIRAQIEETTSDYDREKLQERLAKLAGGVAVIRVGASTEVEVKEKKDRVDDALH 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 427 ATRAAVEEGIVPGGGCALLRCIPALDNIKPANADQKIGIDIIRRSLRIPAMTIAKNAGVEGSLVVEKILQSSTEIGYDAM 506
Cdd:PRK12851 402 ATRAAVEEGIVPGGGVALLRAVKALDKLETANGDQRTGVEIVRRALEAPVRQIAENAGAEGSVVVGKLREKPGGYGFNAA 481
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 31044489 507 NGEYVNMVERGIIDPTKVVRTALLDAAGVASLLSTAEAVVTEIPKEEKEMPA 558
Cdd:PRK12851 482 TNEYGDLYAQGVIDPVKVVRTALQNAASVAGLLLTTEAMVAEKPKKEPAPPA 533
|
|
| GroEL |
COG0459 |
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ... |
27-556 |
0e+00 |
|
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227 Cd Length: 497 Bit Score: 633.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 27 AKDVKFGADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDRYKNIGAKLVQDVANNTN 106
Cdd:COG0459 2 AKQILFGEDARRANIRGVKALADAVKVTLGPKGRNVMLVKSFGDPTITNDGVTIAKEIELEDPFENMGAQLVKEVASKTN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 107 EEAGDGTTTATVLARAVAKEGFDTISKGANPVEIRRGVMMAVEEVISELKKNSKPVTTPEEIAQVATISANGDTEVGNII 186
Cdd:COG0459 82 DEAGDGTTTATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPVDDKEELAQVATISANGDEEIGELI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 187 SNAMKKVGRKGVITVKDGKTLHDELEIIEGMKFDRGYISPYFINTAKGQKCEFQDAYVLLSEKKISSVQSIVPALEIANQ 266
Cdd:COG0459 162 AEAMEKVGKDGVITVEEGKGLETELEVVEGMQFDKGYLSPYFVTDPEKMPAELENAYILLTDKKISSIQDLLPLLEKVAQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 267 HRKPLVIVAEDVDGEALSTLVLNRLKVGLQVVAVKAPGFGDNRKNQLQDMAVSTGGTVFGDEaMGLALEDIQAHDFGKVG 346
Cdd:COG0459 242 SGKPLLIIAEDIDGEALATLVVNGIRGVLRVVAVKAPGFGDRRKAMLEDIAILTGGRVISED-LGLKLEDVTLDDLGRAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 347 EVIVTKDDTMLLKGRGDASAIekrvneiaeqlestnsdyekeklnerlaklsdgvaVIKVGGTSDVEVNEKKDRVTDALN 426
Cdd:COG0459 321 RVEVDKDNTTIVEGAGNPKAI-----------------------------------VILVGAATEVEVKERKRRVEDALH 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 427 ATRAAVEEGIVPGGGCALLRCIPALDNIKP-ANADQKIGIDIIRRSLRIPAMTIAKNAGVEGSLVVEKIL-QSSTEIGYD 504
Cdd:COG0459 366 ATRAAVEEGIVPGGGAALLRAARALRELAAkLEGDEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKVRaAKDKGFGFD 445
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 31044489 505 AMNGEYVNMVERGIIDPTKVVRTALLDAAGVASLLSTAEAVVTEIPKEEKEM 556
Cdd:COG0459 446 AATGEYVDMLEAGVIDPAKVKRSALQNAASVAGLILTTEAVIADKPEKEEAA 497
|
|
| PRK14104 |
PRK14104 |
chaperonin GroEL; Provisional |
27-558 |
0e+00 |
|
chaperonin GroEL; Provisional
Pssm-ID: 172594 Cd Length: 546 Bit Score: 599.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 27 AKDVKFGADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDRYKNIGAKLVQDVANNTN 106
Cdd:PRK14104 3 AKEVKFGVDARDRMLRGVDILANAVKVTLGPKGRNVVLDKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVREVASKSA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 107 EEAGDGTTTATVLARAVAKEGFDTISKGANPVEIRRGVMMAVEEVISELKKNSKPVTTPEEIAQVATISANGDTEVGNII 186
Cdd:PRK14104 83 DAAGDGTTTATVLAQAIVREGAKSVAAGMNPMDLKRGIDLAVEAVVADLVKNSKKVTSNDEIAQVGTISANGDAEIGKFL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 187 SNAMKKVGRKGVITVKDGKTLHDELEIIEGMKFDRGYISPYFINTAKGQKCEFQDAYVLLSEKKISSVQSIVPALEIANQ 266
Cdd:PRK14104 163 ADAMKKVGNEGVITVEEAKSLETELDVVEGMQFDRGYISPYFVTNADKMRVEMDDAYILINEKKLSSLNELLPLLEAVVQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 267 HRKPLVIVAEDVDGEALSTLVLNRLKVGLQVVAVKAPGFGDNRKNQLQDMAVSTGGTVFgDEAMGLALEDIQAHDFGKVG 346
Cdd:PRK14104 243 TGKPLVIVAEDVEGEALATLVVNRLRGGLKVAAVKAPGFGDRRKAMLQDIAILTGGQAI-SEDLGIKLENVTLQMLGRAK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 347 EVIVTKDDTMLLKGRGDASAIEKRVNEIAEQLESTNSDYEKEKLNERLAKLSDGVAVIKVGGTSDVEVNEKKDRVTDALN 426
Cdd:PRK14104 322 KVMIDKENTTIVNGAGKKADIEARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKERKDRVDDAMH 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 427 ATRAAVEEGIVPGGGCALLRCIPALDNIKPANADQKIGIDIIRRSLRIPAMTIAKNAGVEGSLVVEKILQSST-EIGYDA 505
Cdd:PRK14104 402 ATRAAVEEGIVPGGGVALLRASEQLKGIKTKNDDQKTGVEIVRKALSAPARQIAINAGEDGSVIVGKILEKEQySYGFDS 481
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 31044489 506 MNGEYVNMVERGIIDPTKVVRTALLDAAGVASLLSTAEAVVTEIPKEEKEMPA 558
Cdd:PRK14104 482 QTGEYGNLVSKGIIDPTKVVRTAIQNAASVAALLITTEAMVAELPKKGGAGPA 534
|
|
| groEL |
CHL00093 |
chaperonin GroEL |
27-553 |
0e+00 |
|
chaperonin GroEL
Pssm-ID: 177025 Cd Length: 529 Bit Score: 552.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 27 AKDVKFGADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDRYKNIGAKLVQDVANNTN 106
Cdd:CHL00093 2 SKKILYQDNARRALERGMDILAEAVSVTLGPKGRNVVLEKKYGSPQIVNDGVTIAKEIELEDHIENTGVALIRQAASKTN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 107 EEAGDGTTTATVLARAVAKEGFDTISKGANPVEIRRGVMMAVEEVISELKKNSKPVTTPEEIAQVATISANGDTEVGNII 186
Cdd:CHL00093 82 DVAGDGTTTATVLAYAIVKQGMKNVAAGANPISLKRGIEKATQYVVSQIAEYARPVEDIQAITQVASISAGNDEEVGSMI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 187 SNAMKKVGRKGVITVKDGKTLHDELEIIEGMKFDRGYISPYFINTAKGQKCEFQDAYVLLSEKKISSV-QSIVPALEIAN 265
Cdd:CHL00093 162 ADAIEKVGREGVISLEEGKSTVTELEITEGMRFEKGFISPYFVTDTERMEVVQENPYILLTDKKITLVqQDLLPILEQVT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 266 QHRKPLVIVAEDVDGEALSTLVLNRLKVGLQVVAVKAPGFGDNRKNQLQDMAVSTGGTVFGDEAmGLALEDIQAHDFGKV 345
Cdd:CHL00093 242 KTKRPLLIIAEDVEKEALATLVLNKLRGIVNVVAVRAPGFGDRRKAMLEDIAILTGGQVITEDA-GLSLETIQLDLLGQA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 346 GEVIVTKDDTMLLkGRGDASAIEKRVNEIAEQLESTNSDYEKEKLNERLAKLSDGVAVIKVGGTSDVEVNEKKDRVTDAL 425
Cdd:CHL00093 321 RRIIVTKDSTTII-ADGNEEQVKARCEQLRKQIEIADSSYEKEKLQERLAKLSGGVAVIKVGAATETEMKDKKLRLEDAI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 426 NATRAAVEEGIVPGGGCALLRCIPALDNIKPAN--ADQKIGIDIIRRSLRIPAMTIAKNAGVEGSLVVEKILQSSTEIGY 503
Cdd:CHL00093 400 NATKAAVEEGIVPGGGATLVHLSENLKTWAKNNlkEDELIGALIVARAILAPLKRIAENAGKNGSVIIEKVQEQDFEIGY 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 31044489 504 DAMNGEYVNMVERGIIDPTKVVRTALLDAAGVASLLSTAEAVVTEIPKEE 553
Cdd:CHL00093 480 NAANNKFVNMYEAGIIDPAKVTRSALQNAASIASMILTTECIIVDKKESS 529
|
|
| PLN03167 |
PLN03167 |
Chaperonin-60 beta subunit; Provisional |
12-553 |
5.87e-172 |
|
Chaperonin-60 beta subunit; Provisional
Pssm-ID: 215611 [Multi-domain] Cd Length: 600 Bit Score: 500.61 E-value: 5.87e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 12 RPVCRALAPHLTRAYAKDVKFGADARAL--MLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDR 89
Cdd:PLN03167 41 QSVRLRRSRSPKVKAAKELHFNKDGSAIkkLQAGVNKLADLVGVTLGPKGRNVVLESKYGSPKIVNDGVTVAKEVELEDP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 90 YKNIGAKLVQDVANNTNEEAGDGTTTATVLARAVAKEGFDTISKGANPVEIRRGVMMAVEEVISELKKNSKPVTTpEEIA 169
Cdd:PLN03167 121 VENIGAKLVRQAAAKTNDLAGDGTTTSVVLAQGLIAEGVKVVAAGANPVQITRGIEKTAKALVKELKKMSKEVED-SELA 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 170 QVATISANGDTEVGNIISNAMKKVGRKGVITVKDGKTLHDELEIIEGMKFDRGYISPYFINTAKGQKCEFQDAYVLLSEK 249
Cdd:PLN03167 200 DVAAVSAGNNYEVGNMIAEAMSKVGRKGVVTLEEGKSAENNLYVVEGMQFDRGYISPYFVTDSEKMSVEYDNCKLLLVDK 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 250 KISSVQSIVPALEIANQHRKPLVIVAEDVDGEALSTLVLNRLKVGLQVVAVKAPGFGDNRKNQLQDMAVSTGGTVFGDEa 329
Cdd:PLN03167 280 KITNARDLIGILEDAIRGGYPLLIIAEDIEQEALATLVVNKLRGSLKIAALKAPGFGERKSQYLDDIAILTGGTVIREE- 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 330 MGLALEDIQAHDFGKVGEVIVTKDDTMLLKGRGDASAIEKRVNEIAEQLESTNSDYEKEKLNERLAKLSDGVAVIKVGGT 409
Cdd:PLN03167 359 VGLSLDKVGKEVLGTAAKVVLTKDTTTIVGDGSTQEAVNKRVAQIKNLIEAAEQDYEKEKLNERIAKLSGGVAVIQVGAQ 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 410 SDVEVNEKKDRVTDALNATRAAVEEGIVPGGGCALLRCIPALDNIKPA--NADQKIGIDIIRRSLRIPAMTIAKNAGVEG 487
Cdd:PLN03167 439 TETELKEKKLRVEDALNATKAAVEEGIVVGGGCTLLRLASKVDAIKDTleNDEQKVGADIVKRALSYPLKLIAKNAGVNG 518
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 31044489 488 SLVVEKILQSST-EIGYDAMNGEYVNMVERGIIDPTKVVRTALLDAAGVASLLSTAEAVVTEIPKEE 553
Cdd:PLN03167 519 SVVSEKVLSNDNpKFGYNAATGKYEDLMAAGIIDPTKVVRCCLEHAASVAKTFLTSDCVVVEIKEPE 585
|
|
| chaperonin_type_I_II |
cd00309 |
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ... |
28-547 |
1.44e-147 |
|
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: 433.01 E-value: 1.44e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 28 KDVKFGADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKdrykNIGAKLVQDVANNTNE 107
Cdd:cd00309 1 KEREFGEEARLSNINAAKALADAVKTTLGPKGMDKMLVDSLGDPTITNDGATILKEIEVE----HPAAKLLVEVAKSQDD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 108 EAGDGTTTATVLARAVAKEGFDTISKGANPVEIRRGVMMAVEEVISELKKNSKP--VTTPEEIAQVATISAN------GD 179
Cdd:cd00309 77 EVGDGTTTVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVPidVEDREELLKVATTSLNsklvsgGD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 180 TEVGNIISNAMKKVGR------KGVITVKDGKT-LHDELEIIEGMKFDRGYISPYFintakgqKCEFQDAYVLLSEKKIS 252
Cdd:cd00309 157 DFLGELVVDAVLKVGKengdvdLGVIRVEKKKGgSLEDSELVVGMVFDKGYLSPYM-------PKRLENAKILLLDCKLE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 253 SvqsivpaleianqhrkplVIVAED-VDGEALSTLVLnrlkvgLQVVAVKApgfgdNRKNQLQDMAVSTGGTVFGDeamg 331
Cdd:cd00309 230 Y------------------VVIAEKgIDDEALHYLAK------LGIMAVRR-----VRKEDLERIAKATGATIVSR---- 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 332 laLEDIQAHDFGKVGEVIVTK----DDTMLLKGRGdasaiekrvneiaeqlestnsdyekeklnerlaklsDGVAVIKVG 407
Cdd:cd00309 277 --LEDLTPEDLGTAGLVEETKigdeKYTFIEGCKG------------------------------------GKVATILLR 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 408 GTSDVEVNEKKDRVTDALNATRAAVEE-GIVPGGGCALLRCIPALDNIKP-ANADQKIGIDIIRRSLRIPAMTIAKNAGV 485
Cdd:cd00309 319 GATEVELDEAERSLHDALCAVRAAVEDgGIVPGGGAAEIELSKALEELAKtLPGKEQLGIEAFADALEVIPRTLAENAGL 398
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31044489 486 EGSLVVEKILQSSTEIGYDA----MNGEYVNMVERGIIDPTKVVRTALLDAAGVASLLSTAEAVVT 547
Cdd:cd00309 399 DPIEVVTKLRAKHAEGGGNAggdvETGEIVDMKEAGIIDPLKVKRQALKSATEAASLILTIDDIIV 464
|
|
| Cpn60_TCP1 |
pfam00118 |
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ... |
47-546 |
6.63e-73 |
|
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: 241.34 E-value: 6.63e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 47 LADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDRYknigAKLVQDVANNTNEEAGDGTTTATVLARAVAKE 126
Cdd:pfam00118 1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELEIQHPA----AKLLVEAAKAQDEEVGDGTTTVVVLAGELLEE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 127 GFDTISKGANPVEIRRGVMMAVEEVISELKKN-SKPVTTP--EEIAQVATISANGD------TEVGNIISNAMK------ 191
Cdd:pfam00118 77 AEKLLAAGVHPTTIIEGYEKALEKALEILDSIiSIPVEDVdrEDLLKVARTSLSSKiisresDFLAKLVVDAVLaipknd 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 192 ---KVGRKGVITVKDGKTlhDELEIIEGMKFDRGYISPyfintakGQKCEFQDAYVLLSEKKISSVQSIVPA-------- 260
Cdd:pfam00118 157 gsfDLGNIGVVKILGGSL--EDSELVDGVVLDKGPLHP-------DMPKRLENAKVLLLNCSLEYEKTETKAtvvlsdae 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 261 --LEIANQHRK--------------PLVIVAEDVDGEALSTLVLNRLkVGLQVVavkapgfgdnRKNQLQDMAVSTGGTV 324
Cdd:pfam00118 228 qlERFLKAEEEqileivekiidsgvNVVVCQKGIDDLALHFLAKNGI-MALRRV----------KKRDLERLAKATGARA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 325 FGDeamglaLEDIQAHDFGKVG---EVIVTKDDTMLLKGRGDAsaiekrvneiaeqlestnsdyekeklnerlaklsdGV 401
Cdd:pfam00118 297 VSS------LDDLTPDDLGTAGkveEEKIGDEKYTFIEGCKSP-----------------------------------KA 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 402 AVIKVGGTSDVEVNEKKDRVTDALNATRAAVEE-GIVPGGGCALLRCIPALDNI-KPANADQKIGIDIIRRSLRIPAMTI 479
Cdd:pfam00118 336 ATILLRGATDHVLDEIERSIHDALCVVKNAIEDpRVVPGGGAVEMELARALREYaKSVSGKEQLAIEAFAEALEVIPKTL 415
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 31044489 480 AKNAGVEGSLVVEKIL----QSSTEIGYDAMNGEYVNMVERGIIDPTKVVRTALLDAAGVASLLSTAEAVV 546
Cdd:pfam00118 416 AENAGLDPIEVLAELRaahaSGEKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKSATEAASTILRIDDII 486
|
|
| chaperonin_like |
cd03333 |
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ... |
166-434 |
6.22e-35 |
|
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: 130.66 E-value: 6.22e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 166 EEIAQVATISAN-----GDTEVGNIISNAMKKVGR------KGVITVKD--GKTLHDElEIIEGMKFDRGYISPYFinta 232
Cdd:cd03333 2 ELLLQVATTSLNsklssWDDFLGKLVVDAVLKVGPdnrmddLGVIKVEKipGGSLEDS-ELVVGVVFDKGYASPYM---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 233 kgqKCEFQDAYVLLSEKKISSvqsivpaleianqhrkplVIVAED-VDGEALSTLVLnrlkvgLQVVAVKApgfgdNRKN 311
Cdd:cd03333 77 ---PKRLENAKILLLDCPLEY------------------VVIAEKgIDDLALHYLAK------AGIMAVRR-----VKKE 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 312 QLQDMAVSTGGTVFGDeamglaLEDIQAHDFGKVGEVIVTKDdtmllkgrgdasaIEKRVNEIaEQLESTnsdyekekln 391
Cdd:cd03333 125 DLERIARATGATIVSS------LEDLTPEDLGTAELVEETKI-------------GEEKLTFI-EGCKGG---------- 174
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 31044489 392 erlaklsdGVAVIKVGGTSDVEVNEKKDRVTDALNATRAAVEE 434
Cdd:cd03333 175 --------KAATILLRGATEVELDEVKRSLHDALCAVRAAVEE 209
|
|
| cpn60 |
cd03343 |
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ... |
33-539 |
9.42e-20 |
|
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: 92.71 E-value: 9.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 33 GADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKdrykNIGAKLVQDVANNTNEEAGDG 112
Cdd:cd03343 13 GRDAQRMNIAAAKAVAEAVRTTLGPKGMDKMLVDSLGDVTITNDGATILKEMDIE----HPAAKMLVEVAKTQDEEVGDG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 113 TTTATVLARAVAKEGFDTISKGANPVEIRRGVMMAVEEVISELKKNSKPVTTPEE-----IAQVATISANGDTE---VGN 184
Cdd:cd03343 89 TTTAVVLAGELLEKAEDLLDQNIHPTVIIEGYRLAAEKALELLDEIAIKVDPDDKdtlrkIAKTSLTGKGAEAAkdkLAD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 185 IISNAMKKV--GRKGVITV---------KDGKTLHDElEIIEGMKFDRGYISPyfintakGQKCEFQDAYVLLsekkiss 253
Cdd:cd03343 169 LVVDAVLQVaeKRDGKYVVdldnikiekKTGGSVDDT-ELIRGIVIDKEVVHP-------GMPKRVENAKIAL------- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 254 vqsIVPALEIanqhRKPLV---IVAEDVDgealstlvlnrlkvglqvvavKAPGFGDNRKNQLQDMA---VSTGGTVF-- 325
Cdd:cd03343 234 ---LDAPLEV----KKTEIdakIRITSPD---------------------QLQAFLEQEEAMLKEMVdkiADTGANVVfc 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 326 ----GDEAMG-------LALEDIQAHDFGKV----GEVIVTKDDTMLLKGRGDASAIEKRvneiaeqlestnSDYEKEKL 390
Cdd:cd03343 286 qkgiDDLAQHylakagiLAVRRVKKSDMEKLaratGAKIVTNIDDLTPEDLGEAELVEER------------KVGDDKMV 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 391 NERLAKLSDGVAVIKVGGTSDVeVNEKKDRVTDALNATRAAVEEG-IVPGGGCALLRCIPALDNIKPA-NADQKIGIDII 468
Cdd:cd03343 354 FVEGCKNPKAVTILLRGGTEHV-VDELERALEDALRVVADALEDGkVVAGGGAVEIELAKRLREYARSvGGREQLAVEAF 432
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 31044489 469 RRSLRIPAMTIAKNAGVEGslvVEKILQ-------SSTEIGYDAMNGEYVNMVERGIIDPTKVVRTALLDAAGVASLL 539
Cdd:cd03343 433 ADALEEIPRTLAENAGLDP---IDTLVElraahekGNKNAGLDVYTGEVVDMLEKGVIEPLRVKKQAIKSATEAATMI 507
|
|
| chap_CCT_epsi |
TIGR02343 |
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ... |
33-521 |
1.30e-12 |
|
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: 70.22 E-value: 1.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 33 GADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDRYknigAKLVQDVANNTNEEAGDG 112
Cdd:TIGR02343 25 GLEAKKSNIAAAKSVASILRTSLGPKGMDKMLISPDGDITVTNDGATILSQMDVDNQI----AKLMVELSKSQDDEIGDG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 113 TTTATVLARAVAKEGFDTISKGANPVEIRRGVMMAVEEVISELKKNSKPVTTPEEIAQVATISANgdTEVGNIISNA--- 189
Cdd:TIGR02343 101 TTGVVVLAGALLEQAEELLDKGIHPIKIADGFEEAARIAVEHLEEISDEISADNNNREPLIQAAK--TSLGSKIVSKchr 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 190 -MKKVGRKGVITVKD-----------------GKTLHDElEIIEGMKFDRGYISPYFINTAKGQK-----CEFQDAYVLL 246
Cdd:TIGR02343 179 rFAEIAVDAVLNVADmerrdvdfdlikvegkvGGSLEDT-KLIKGIIIDKDFSHPQMPKEVEDAKiailtCPFEPPKPKT 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 247 SEK-KISSVQSIvPALEIANQHR------------KPLVIVAEDVDGEALSTLVLNRLKvglqvvAVKAPGfgdnrKNQL 313
Cdd:TIGR02343 258 KHKlDISSVEEY-KKLQKYEQQKfkemiddikksgANLVICQWGFDDEANHLLLQNDLP------AVRWVG-----GQEL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 314 QDMAVSTGGTVFGdeamglALEDIQAHDFGKVGEV----IVTKDDTMLlkgrgdasaiekrvneIAEQlestnsdyekek 389
Cdd:TIGR02343 326 ELIAIATGGRIVP------RFQELSKDKLGKAGLVreisFGTTKDRML----------------VIEQ------------ 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 390 lnerlAKLSDGVAVIkVGGTSDVEVNEKKDRVTDALNATRAAVEEG-IVPGGGCALLRCIPALDNIkpanADQKIGID-- 466
Cdd:TIGR02343 372 -----CKNSKAVTIF-IRGGNKMIIEEAKRSIHDALCVVRNLIKDSrIVYGGGAAEISCSLAVSQE----ADKYPGVEqy 441
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 31044489 467 IIR---RSLRIPAMTIAKNAGVE--GSLVVEKILQSSTE---IGYDAMNGEYVNMVERGIIDP 521
Cdd:TIGR02343 442 AIRafaDALETIPMALAENSGLDpiGTLSTLKSLQLKEKnpnLGVDCLGYGTNDMKEQFVFET 504
|
|
| TCP1_beta |
cd03336 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ... |
33-552 |
2.95e-12 |
|
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: 69.28 E-value: 2.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 33 GADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSW--GSPKVTKDGVTVAKSIDLKdrykNIGAKLVQDVANNTNEEAG 110
Cdd:cd03336 11 GETARLSSFVGAIAIGDLVKTTLGPKGMDKILQSVGrsGGVTVTNDGATILKSIGVD----NPAAKVLVDISKVQDDEVG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 111 DGTTTATVLARAVAKEGFDTISKGANPVEIRRGVMMAVEEVISELKKNSKPVTTPEEIAQVATISANGDTEVGNIIS--- 187
Cdd:cd03336 87 DGTTSVTVLAAELLREAEKLVAQKIHPQTIIEGYRMATAAAREALLSSAVDHSSDEEAFREDLLNIARTTLSSKILTqdk 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 188 NAMKKVGRKGVITVKDGKTLhDELEIIE--GMKFDRGYISPYFINTAK---GQKCEFQDAYVLL--------------SE 248
Cdd:cd03336 167 EHFAELAVDAVLRLKGSGNL-DAIQIIKklGGSLKDSYLDEGFLLDKKigvNQPKRIENAKILIantpmdtdkikifgAK 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 249 KKISSVqSIVPALEIANQHR---KPLVIVAEDVDGEALSTLVLN---RLKVGLQVVAVKAPGFGdnrknqlqdmavstgg 322
Cdd:cd03336 246 VRVDST-AKVAEIEEAEKEKmknKVEKILKHGINCFINRQLIYNypeQLFADAGIMAIEHADFD---------------- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 323 tvfGDEAMGLALEdiqahdfgkvGEVIVTKDDTMLLKgRGDASAIEKRVneIAEqlestnsdyekeklnERLAKLSdGVA 402
Cdd:cd03336 309 ---GVERLALVTG----------GEIASTFDHPELVK-LGTCKLIEEIM--IGE---------------DKLIRFS-GVA 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 403 -----VIKVGGTSDVEVNEKKDRVTDALNATRAAVEEG-IVPGGGCALLRCIPALDNI-KPANADQKIGIDIIRRSLRIP 475
Cdd:cd03336 357 ageacTIVLRGASQQILDEAERSLHDALCVLAQTVKDTrVVLGGGCSEMLMAKAVEELaKKTPGKKSLAIEAFAKALRQL 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 476 AMTIAKNAGVEGSLVVEKI----LQSSTEIGYDAMNGEYVNMVERGIIDPTKVVRTALLDAAGVASLLSTAEAVVTEIPK 551
Cdd:cd03336 437 PTIIADNAGYDSAELVAQLraahYNGNTTAGLDMRKGTVGDMKELGITESFKVKRQVLLSASEAAEMILRVDDIIKCAPR 516
|
.
gi 31044489 552 E 552
Cdd:cd03336 517 K 517
|
|
| chap_CCT_beta |
TIGR02341 |
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ... |
33-551 |
9.51e-12 |
|
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: 67.58 E-value: 9.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 33 GADARALMLQGVDLLADAVAVTMGPKGRTVIIEQ--SWGSPKVTKDGVTVAKSIDLKdrykNIGAKLVQDVANNTNEEAG 110
Cdd:TIGR02341 12 AENARLSSFVGAIAIGDLVKSTLGPKGMDKILQSssSDASIMVTNDGATILKSIGVD----NPAAKVLVDMSKVQDDEVG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 111 DGTTTATVLARAVAKEGFDTISKGANPVEIRRGVMMAVEEVISELKKNSKPVTTPEEIAQVATISANGDTEVGNIIS--- 187
Cdd:TIGR02341 88 DGTTSVTVLAAELLREAEKLINQKIHPQTIIAGYREATKAARDALLKSAVDNGSDEVKFRQDLMNIARTTLSSKILSqhk 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 188 NAMKKVGRKGVITVKdGKTLHDELEIIE--GMKFDRGYISPYFINTAK---GQKCEFQDAYVLLSEKKISSVQSIVPALE 262
Cdd:TIGR02341 168 DHFAQLAVDAVLRLK-GSGNLEAIQIIKklGGSLADSYLDEGFLLDKKigvNQPKRIENAKILIANTGMDTDKVKIFGSR 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 263 ianqhrkplviVAEDVDGEALSTLVLNRLKVGLQVVAVKAPGFGDNRKNQLqdmAVSTGGTVFGDeamgLALEDIQAHDF 342
Cdd:TIGR02341 247 -----------VRVDSTAKVAELEHAEKEKMKEKVEKILKHGINCFINRQL---IYNYPEQLFAD----AGVMAIEHADF 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 343 GKV--------GEVIVTKDDTMLLKgRGDASAIEKRVneIAEQlestnsdyekeklneRLAKLSdGVAV-----IKVGGT 409
Cdd:TIGR02341 309 EGVerlalvtgGEIVSTFDHPELVK-LGSCDLIEEIM--IGED---------------KLLKFS-GVKLgeactIVLRGA 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 410 SDVEVNEKKDRVTDALNATRAAVEEG-IVPGGGCALLRCIPALDNIKPANADQK-IGIDIIRRSLRIPAMTIAKNAGVEG 487
Cdd:TIGR02341 370 TQQILDEAERSLHDALCVLSQTVKESrTVLGGGCSEMLMSKAVTQEAQRTPGKEaLAVEAFARALRQLPTIIADNAGFDS 449
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 31044489 488 SLVVEKILQSSTE----IGYDAMNGEYVNMVERGIIDPTKVVRTALLDAAGVASLLSTAEAVVTEIPK 551
Cdd:TIGR02341 450 AELVAQLRAAHYNgnttMGLDMNEGTIADMRQLGITESYKVKRAVVSSAAEAAEVILRVDNIIKAAPR 517
|
|
| chap_CCT_eta |
TIGR02345 |
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ... |
47-167 |
2.38e-11 |
|
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: 66.32 E-value: 2.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 47 LADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLkdryKNIGAKLVQDVANNTNEEAGDGTTTATVLARAVAKE 126
Cdd:TIGR02345 30 IAEALKTTLGPRGMDKLIVGSNGKATISNDGATILKLLDI----VHPAAKTLVDIAKSQDAEVGDGTTSVTILAGELLKE 105
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 31044489 127 GFDTISKGANPVEIRRGVMMAVEEVISELKKNSkpVTTPEE 167
Cdd:TIGR02345 106 AKPFIEEGVHPQLIIRCYREALSLAVEKIKEIA--VTIDEE 144
|
|
| chap_CCT_alpha |
TIGR02340 |
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ... |
33-547 |
4.41e-11 |
|
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT alpha chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.
Pssm-ID: 274081 [Multi-domain] Cd Length: 536 Bit Score: 65.51 E-value: 4.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 33 GADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDRykniGAKLVQDVANNTNEEAGDG 112
Cdd:TIGR02340 10 GQDVRTQNVTAAMAIANIVKTSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHP----AAKILVELAQLQDREVGDG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 113 TTTATVLARAVAKEGFDTISKGANPVEIRRGVMMAVEEVISELKKNSKpvTTPEEIAQVATISA----------NGDTEV 182
Cdd:TIGR02340 86 TTSVVIIAAELLKRADELVKNKIHPTSVISGYRLACKEAVKYIKENLS--VSVDELGREALINVaktsmsskiiGLDSDF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 183 -GNIISNAMKKV---GRKGVIT--VKD-------GKTLHDELeIIEGMKFDRGYISPYFINTAKGQKCEFQDaYVLLSEK 249
Cdd:TIGR02340 164 fSNIVVDAVLAVkttNENGETKypIKAinilkahGKSARESM-LVKGYALNCTVASQQMPKRIKNAKIACLD-FNLQKAK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 250 KISSVQSIV--PAlEIANQHRKPLVIVAEDVDG--EALSTLVLNR-------LKvglQVVAVKAPGFGDNRKNQLQDMAV 318
Cdd:TIGR02340 242 MALGVQIVVddPE-KLEQIRQREADITKERIKKilDAGANVVLTTggiddmcLK---YFVEAGAMGVRRCKKEDLKRIAK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 319 STGGTVFGDEAMGLALEDIQAHDFGKVGEVIVTK---DDTMLLKGRGDASAiekrvneiaeqlestnsdyekeklnerla 395
Cdd:TIGR02340 318 ATGATLVSTLADLEGEETFEASYLGFADEVVQERiadDECILIKGTKKRKS----------------------------- 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 396 klsdgvAVIKVGGTSDVEVNEKKDRVTDALNATRAAVEEG-IVPGGGCALLRCIPALDNI-KPANADQKIGIDIIRRSLR 473
Cdd:TIGR02340 369 ------ASIILRGANDFMLDEMERSLHDALCVVKRTLESNsVVPGGGAVEAALSIYLENFaTTLGSREQLAIAEFARALL 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 474 IPAMTIAKNAGVEGSLVVEKIL------------QSSTEIGYDAMNGEYVNMVERGIIDPTkvvrtalldAAGVASLLST 541
Cdd:TIGR02340 443 IIPKTLAVNAAKDSTELVAKLRayhaaaqlkpekKHLKWYGLDLVNGKIRDNKEAGVLEPT---------VSKVKSLKFA 513
|
....*.
gi 31044489 542 AEAVVT 547
Cdd:TIGR02340 514 TEAAIT 519
|
|
| TCP1_delta |
cd03338 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ... |
47-240 |
1.07e-10 |
|
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: 64.23 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 47 LADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKdrykNIGAKLVQDVANNTNEEAGDGTTTATVLARAVAKE 126
Cdd:cd03338 20 VADAIRTSLGPRGMDKMIQTGKGEVIITNDGATILKQMSVL----HPAAKMLVELSKAQDIEAGDGTTSVVVLAGALLSA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 127 GFDTISKGANPVEIRRGVMMAVEEVISELKKNSKPV--TTPEEIAQVATISANG---------------DTEVGNIISNA 189
Cdd:cd03338 96 CESLLKKGIHPTVISESFQIAAKKAVEILDSMSIPVdlNDRESLIKSATTSLNSkvvsqyssllapiavDAVLKVIDPAT 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 31044489 190 MKKVGRKGV-ITVKDGKTLHDElEIIEGM----KFDRGYISPYFINTAKGQKCEFQ 240
Cdd:cd03338 176 ATNVDLKDIrIVKKLGGTIEDT-ELVDGLvftqKASKKAGGPTRIEKAKIGLIQFC 230
|
|
| TCP1_eta |
cd03340 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ... |
48-157 |
1.95e-10 |
|
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.
Pssm-ID: 239456 [Multi-domain] Cd Length: 522 Bit Score: 63.46 E-value: 1.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 48 ADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKdrykNIGAKLVQDVANNTNEEAGDGTTTATVLARAVAKEG 127
Cdd:cd03340 29 ADAVRTTLGPRGMDKLIVDGRGKVTISNDGATILKLLDIV----HPAAKTLVDIAKSQDAEVGDGTTSVVVLAGEFLKEA 104
|
90 100 110
....*....|....*....|....*....|
gi 31044489 128 FDTISKGANPVEIRRGVMMAVEEVISELKK 157
Cdd:cd03340 105 KPFIEDGVHPQIIIRGYRKALQLAIEKIKE 134
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
33-159 |
2.23e-10 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 63.12 E-value: 2.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 33 GADARALMLQGVDLLADAVAVTMGPKGRTVIIE-----QSWGSPKVTKDGVTVAKSIDLKdrykNIGAKLVQDVANNTNE 107
Cdd:PTZ00212 20 GETARLQSFVGAIAVADLVKTTLGPKGMDKILQpmsegPRSGNVTVTNDGATILKSVWLD----NPAAKILVDISKTQDE 95
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 31044489 108 EAGDGTTTATVLARAVAKEGFDTISKGANPVEIRRGVMMAVEEVISELKKNS 159
Cdd:PTZ00212 96 EVGDGTTSVVVLAGELLREAEKLLDQKIHPQTIIEGWRMALDVARKALEEIA 147
|
|
| chap_CCT_delta |
TIGR02342 |
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ... |
34-240 |
2.26e-09 |
|
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: 59.80 E-value: 2.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 34 ADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKdrykNIGAKLVQDVANNTNEEAGDGT 113
Cdd:TIGR02342 8 QDVRTSNIVAAKAVADAIRTSLGPKGMDKMIQDGKGEVIITNDGATILKQMAVL----HPAAKMLVELSKAQDIEAGDGT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 114 TTATVLARAVAKEGFDTISKGANPVEIRRGVMMAVEEVISELKKNSKPVTTPEEIAQVATISANGDTEVGNIISNAMKKV 193
Cdd:TIGR02342 84 TSVVILAGALLGACERLLNKGIHPTIISESFQSAADEAIKILDEMSIPVDLSDREQLLKSATTSLSSKVVSQYSSLLAPL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 31044489 194 GRKGVITVKDGKTLH-----------------DELEIIEGMKFDRGYI----SPYFINTAKGQKCEFQ 240
Cdd:TIGR02342 164 AVDAVLKVIDPENAKnvdlndikvvkklggtiDDTELIEGLVFTQKASksagGPTRIEKAKIGLIQFQ 231
|
|
| chap_CCT_gamma |
TIGR02344 |
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ... |
41-213 |
8.17e-09 |
|
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: 58.21 E-value: 8.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 41 LQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKdrykNIGAKLVQDVANNTNEEAGDGTTTATVLA 120
Cdd:TIGR02344 22 IQAAKAVADIIRTCLGPRSMLKMLLDPMGGIVMTNDGNAILREIDVA----HPAAKSMIELSRTQDEEVGDGTTSVIILA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 121 RAVAKEGFDTISKGANPVEIRRGVMMAVEEVISELKKNSKPVTTPEEIAQVATISANGDTEVGNIISNAMKKVGRKGVIT 200
Cdd:TIGR02344 98 GEMLSVAEPFLEQNIHPTVIIRAYRKALDDALSVLEEISIPVDVNDDAAMLKLIQSCIGTKFVSRWSDLMCDLALDAVRT 177
|
170
....*....|...
gi 31044489 201 VKDGKTLHDELEI 213
Cdd:TIGR02344 178 VQRDENGRKEIDI 190
|
|
| TCP1_epsilon |
cd03339 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ... |
41-529 |
1.66e-08 |
|
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: 57.31 E-value: 1.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 41 LQGVD------LLADAVAVTM----GPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKdrykNIGAKLVQDVANNTNEEAG 110
Cdd:cd03339 19 LKGLEahkshiLAAKSVANILrtslGPRGMDKILVSPDGEVTVTNDGATILEKMDVD----HQIAKLLVELSKSQDDEIG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 111 DGTTTATVLARAVAKEGFDTISKGANPVEIRRGVMMAVEEVISELKKNSKPVTTPEE----IAQVATISANgdTEVGNII 186
Cdd:cd03339 95 DGTTGVVVLAGALLEQAEKLLDRGIHPIRIADGYEQACKIAVEHLEEIADKIEFSPDnkepLIQTAMTSLG--SKIVSRC 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 187 SNAMKKVGRKGVITVKD--------------GKT--LHDELEIIEGMKFDRGYISPYFINTAKGQK-----CEFQ----- 240
Cdd:cd03339 173 HRQFAEIAVDAVLSVADlerkdvnfelikveGKVggRLEDTKLVKGIVIDKDFSHPQMPKEVKDAKiailtCPFEppkpk 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 241 ----------DAYVLLSE----KKISSVQSIVPALeiANqhrkpLVIVAEDVDGEALSTLVLNRLKVglqVVAVKAPgfg 306
Cdd:cd03339 253 tkhklditsvEDYKKLQEyeqkYFREMVEQVKDAG--AN-----LVICQWGFDDEANHLLLQNGLPA---VRWVGGV--- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 307 dnrknQLQDMAVSTGGTVFGdeamglALEDIQAHDFGKVGEV----IVTKDDTMLlkgrgdasaiekrvneIAEQLESTN 382
Cdd:cd03339 320 -----EIELIAIATGGRIVP------RFEDLSPEKLGKAGLVreisFGTTKDKML----------------VIEGCPNSK 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 383 sdyekeklnerlaklsdgvAV-IKVGGTSDVEVNEKKDRVTDALNATRAAVEEG-IVPGGGCALLRCIPALDNIkpanAD 460
Cdd:cd03339 373 -------------------AVtIFIRGGNKMIIEEAKRSLHDALCVVRNLIRDNrIVYGGGAAEISCSLAVEKA----AD 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 461 QKIGID--IIR---RSLRIPAMTIAKNAGVE--GSLVVEKILQSSTE---IGYDAMNGEYVNMVERGIIDP--------- 521
Cdd:cd03339 430 KCSGIEqyAMRafaDALESIPLALAENSGLNpiETLSEVKARQVKEKnphLGIDCLGRGTNDMKEQKVFETliskkqqil 509
|
570
....*....|
gi 31044489 522 --TKVVRTAL 529
Cdd:cd03339 510 laTQVVKMIL 519
|
|
| TCP1_alpha |
cd03335 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ... |
33-522 |
1.17e-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: 54.60 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 33 GADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDRykniGAKLVQDVANNTNEEAGDG 112
Cdd:cd03335 6 GQDVRTQNVTAAMAIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHP----AAKILVELAQLQDKEVGDG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 113 TTTATVLARAVAKEGFDTISKGANPVEIRRGVMMAVEEVISELKKN-SKPVTT--PEEIAQVATIS-----ANGDTEV-G 183
Cdd:cd03335 82 TTSVVIIAAELLKRANELVKQKIHPTTIISGYRLACKEAVKYIKEHlSISVDNlgKESLINVAKTSmsskiIGADSDFfA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 184 NIISNAMKKV---GRKGVIT--VKD-------GKTLHDELeIIEGMKFDRGYISPYFINTAKGQKCEFQDaYVLLSEKKI 251
Cdd:cd03335 162 NMVVDAILAVkttNEKGKTKypIKAvnilkahGKSAKESY-LVNGYALNCTRASQGMPTRVKNAKIACLD-FNLQKTKMK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 252 SSVQSIV--PAlEIANQHRKPLVIVAEDVDG--EALSTLVLN---------RLKVGLQVVAVKAPgfgdnRKNQLQDMAV 318
Cdd:cd03335 240 LGVQVVVtdPE-KLEKIRQRESDITKERIKKilAAGANVVLTtggiddmclKYFVEAGAMAVRRV-----KKEDLRRIAK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 319 STGGTVFGDEAMGLALEDIQAHDFGKVGEVIVTK---DDTMLLKGRGDASAiekrvneiaeqlestnsdyekeklnerla 395
Cdd:cd03335 314 ATGATLVSTLANLEGEETFDPSYLGEAEEVVQERigdDELILIKGTKKRSS----------------------------- 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 396 klsdgvAVIKVGGTSDVEVNEKKDRVTDALNATRAAVEEG-IVPGGGCALLRCIPALDNI-KPANADQKIGIDIIRRSLR 473
Cdd:cd03335 365 ------ASIILRGANDFMLDEMERSLHDALCVVKRTLESNsVVPGGGAVETALSIYLENFaTTLGSREQLAIAEFAEALL 438
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 31044489 474 IPAMTIAKNAGVEGSLVVEKIL------------QSSTEIGYDAMNGEYVNMVERGIIDPT 522
Cdd:cd03335 439 VIPKTLAVNAAKDATELVAKLRayhaaaqvkpdkKHLKWYGLDLINGKVRDNLEAGVLEPT 499
|
|
| TCP1_gamma |
cd03337 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ... |
47-202 |
1.22e-07 |
|
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.
Pssm-ID: 239453 [Multi-domain] Cd Length: 480 Bit Score: 54.22 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 47 LADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKdrykNIGAKLVQDVANNTNEEAGDGTTTATVLARAVAKE 126
Cdd:cd03337 28 VADVIRTCLGPRAMLKMLLDPMGGIVLTNDGNAILREIDVA----HPAAKSMIELSRTQDEEVGDGTTSVIILAGEILAV 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31044489 127 GFDTISKGANPVEIRRGVMMAVEEVISELKKNSKPVTTPEEIAQVATISANGDTEVGNIISNAMKKVGRKGVITVK 202
Cdd:cd03337 104 AEPFLERGIHPTVIIKAYRKALEDALKILEEISIPVDVNDRAQMLKIIKSCIGTKFVSRWSDLMCNLALDAVKTVA 179
|
|
| TCP1_zeta |
cd03342 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
404-543 |
5.00e-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: 5.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 404 IKVGGTSDVEVNEKKDRVTDALNATRAAVEEG-IVPGGGCALLRCIPAL-DNIKPANADQKIGIDIIRRSLRIPAMTIAK 481
Cdd:cd03342 332 ILIKGPNDHTITQIKDAIRDGLRAVKNAIEDKcVVPGAGAFEVALYAHLkEFKKSVKGKAKLGVQAFADALLVIPKTLAE 411
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 31044489 482 NAGVEGS----LVVEKILQSSTEIGYDAMNGEYVNMVERGIIDPTKVVRTALLDAAGVAS-LLSTAE 543
Cdd:cd03342 412 NSGLDVQetlvKLQDEYAEGGQVGGVDLDTGEPMDPESEGIWDNYSVKRQILHSATVIASqLLLVDE 478
|
|
| TCP1_theta |
cd03341 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ... |
47-171 |
9.42e-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: 45.29 E-value: 9.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 47 LADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKdrykNIGAKLVQDVANNTNEEAGDGTTTATVLARAVAKE 126
Cdd:cd03341 20 LSQITRTSYGPNGMNKMVINHLEKLFVTSDAATILRELEVQ----HPAAKLLVMASQMQEEEIGDGTNLVVVLAGELLEK 95
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 31044489 127 GFDTISKGANPVEIRRGVMMAVEEVISELK----KNSKPVTTPEEIAQV 171
Cdd:cd03341 96 AEELLRMGLHPSEIIEGYEKALKKALEILEelvvYKIEDLRNKEEVSKA 144
|
|
| chap_CCT_theta |
TIGR02346 |
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ... |
47-155 |
1.13e-04 |
|
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: 45.09 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 47 LADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKdrykNIGAKLVQDVANNTNEEAGDGTTTATVLARAVAKE 126
Cdd:TIGR02346 30 LSQITRTSLGPNGMNKMVINHLEKLFVTNDAATILRELEVQ----HPAAKLLVMASEMQENEIGDGTNLVLVLAGELLNK 105
|
90 100
....*....|....*....|....*....
gi 31044489 127 GFDTISKGANPVEIRRGVMMAVEEVISEL 155
Cdd:TIGR02346 106 AEELIRMGLHPSEIIKGYEMALKKAMEIL 134
|
|
| chap_CCT_zeta |
TIGR02347 |
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ... |
47-539 |
2.42e-04 |
|
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: 43.95 E-value: 2.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 47 LADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKdrykNIGAKLVQDVANNTNEEAGDGTTTATVLARAVAKE 126
Cdd:TIGR02347 28 LQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEMQIQ----HPTASMIARAATAQDDITGDGTTSTVLLIGELLKQ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 127 GFDTISKGANPVEIRRGVMMAVEEV---ISELKKNSKPVTTPEEIAQVA------TISANGDTEVGNIISNAMKKVGRKG 197
Cdd:TIGR02347 104 AERYILEGVHPRIITEGFEIARKEAlqfLDKFKVKKEDEVDREFLLNVArtslrtKLPADLADQLTEIVVDAVLAIKKDG 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 198 ------VITVKDGKTLHD-ELEIIEGMKFDRGYISPyfintakGQKCEFQDAYVLLS----EKKISSVQSIVpALEIANQ 266
Cdd:TIGR02347 184 edidlfMVEIMEMKHKSAtDTTLIRGLVLDHGARHP-------DMPRRVKNAYILTCnvslEYEKTEVNSGF-FYSSAEQ 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 267 HRKPLVIVAEDVDG------EALSTLVLNRLKVGLQVVAVK-----------APGFGDNRKNQLQDM---AVSTGGtvfg 326
Cdd:TIGR02347 256 REKLVKAERKFVDDrvkkiiELKKKVCGKSPDKGFVVINQKgidppsldllaKEGIMALRRAKRRNMerlTLACGG---- 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 327 dEAMGlALEDIQAHDFGKVGEVivtkddtmllkgrgdasaIEKRVNE----IAEQLESTNSdyekeklnerlaklsdgvA 402
Cdd:TIGR02347 332 -EALN-SVEDLTPECLGWAGLV------------------YETTIGEekytFIEECKNPKS------------------C 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31044489 403 VIKVGGTSDVEVNEKKDRVTDALNATRAAVEEG-IVPGGGCALLRCIPAL-DNIKPANADQKIGIDIIRRSLRIPAMTIA 480
Cdd:TIGR02347 374 TILIKGPNDHTIAQIKDAVRDGLRAVKNAIEDKcVVPGAGAFEIAAYRHLkEYKKSVKGKAKLGVEAFANALLVIPKTLA 453
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 31044489 481 KNAGVEGS----LVVEKILQSSTEIGYDAMNGEYVNMVERGIIDPTKVVRTALLDAAGVASLL 539
Cdd:TIGR02347 454 ENSGFDAQdtlvKLEDEHDEGGEVVGVDLNTGEPIDPEIKGIWDNYRVKKQLIQSATVIASQL 516
|
|
| |
