|
Name |
Accession |
Description |
Interval |
E-value |
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
2-532 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 963.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 2 AAKDVKFGDDARQKMLSGVNILADAVKTTLGPKGRNVVLEKAFGAPTVTKDGVSVAKEIELKDKFENMGAQMVKEVASKA 81
Cdd:PRK00013 1 MAKDIKFGEDARRKLLRGVNKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDPFENMGAQLVKEVASKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 82 SDTAGDGTTTATVLAQAIVTEGLKSVAAGFNPMDLKRGIDKAVAAAVDHIAGLATPCADSKSIAQVGTISANSDEHVGTI 161
Cdd:PRK00013 81 NDVAGDGTTTATVLAQAIVREGLKNVAAGANPMDLKRGIDKAVEAAVEELKKISKPVEDKEEIAQVATISANGDEEIGKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 162 IAEAMDKVGKEGVITVEEGQSLENELDVVEGMQFDRGYLSPYFVTNQENMTAELDSPFILLVDKKISNIRDLLPLLEQVA 241
Cdd:PRK00013 161 IAEAMEKVGKEGVITVEESKGFETELEVVEGMQFDRGYLSPYFVTDPEKMEAELENPYILITDKKISNIQDLLPVLEQVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 242 KASKPLLIIAEDVEGEALATLVVNSMRGIVKVAAVKAPGFGDRRKAMLQDIAILTGGTVISEEVGLELEATTLEHLGTAK 321
Cdd:PRK00013 241 QSGKPLLIIAEDVEGEALATLVVNKLRGTLKVVAVKAPGFGDRRKAMLEDIAILTGGTVISEELGLKLEDATLEDLGQAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 322 RVTLSKENTVIVDGAGDVADIEARVKQIRAQIEESSSDYDKEKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVEDALH 401
Cdd:PRK00013 321 KVVVTKDNTTIVDGAGDKEAIKARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATEVEMKEKKDRVEDALH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 402 ATRAAVEEGVVPGGGTALIRAIQAIS-VKGDNEDQNHGIAAALRAMEMPLRQIVTNAGDEASVVVDKVKQGEG-NFGYNA 479
Cdd:PRK00013 401 ATRAAVEEGIVPGGGVALLRAAPALEaLKGLNGDEATGINIVLRALEAPLRQIAENAGLEGSVVVEKVKNGKGkGYGYNA 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1055296569 480 GTGEYGDMLEMGILDPAKVTRSALQAAASIAGLMITTEAMVADIPEDKPAAPD 532
Cdd:PRK00013 481 ATGEYVDMIEAGIIDPTKVTRSALQNAASVAGLLLTTEAVVADKPEKKAAAPP 533
|
|
| groEL |
PRK12849 |
chaperonin GroEL; Reviewed |
2-531 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237230 Cd Length: 542 Bit Score: 877.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 2 AAKDVKFGDDARQKMLSGVNILADAVKTTLGPKGRNVVLEKAFGAPTVTKDGVSVAKEIELKDKFENMGAQMVKEVASKA 81
Cdd:PRK12849 1 MAKIIKFDEEARRALERGVNKLADAVKVTLGPKGRNVVIDKSFGAPTITKDGVSIAKEIELEDPFENLGAQLVKEVASKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 82 SDTAGDGTTTATVLAQAIVTEGLKSVAAGFNPMDLKRGIDKAVAAAVDHIAGLATPCADSKSIAQVGTISANSDEHVGTI 161
Cdd:PRK12849 81 NDVAGDGTTTATVLAQALVQEGLKNVAAGANPMDLKRGIDKAVEAVVEELKALARPVSGSEEIAQVATISANGDEEIGEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 162 IAEAMDKVGKEGVITVEEGQSLENELDVVEGMQFDRGYLSPYFVTNQENMTAELDSPFILLVDKKISNIRDLLPLLEQVA 241
Cdd:PRK12849 161 IAEAMEKVGKDGVITVEESKTLETELEVTEGMQFDRGYLSPYFVTDPERMEAVLEDPLILLTDKKISSLQDLLPLLEKVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 242 KASKPLLIIAEDVEGEALATLVVNSMRGIVKVAAVKAPGFGDRRKAMLQDIAILTGGTVISEEVGLELEATTLEHLGTAK 321
Cdd:PRK12849 241 QSGKPLLIIAEDVEGEALATLVVNKLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGLKLEEVTLDDLGRAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 322 RVTLSKENTVIVDGAGDVADIEARVKQIRAQIEESSSDYDKEKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVEDALH 401
Cdd:PRK12849 321 RVTITKDNTTIVDGAGDKEAIEARVAQIRRQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATEVELKERKDRVEDALN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 402 ATRAAVEEGVVPGGGTALIRAIQAI-SVKGDNEDQNHGIAAALRAMEMPLRQIVTNAGDEASVVVDKVKQGEGNFGYNAG 480
Cdd:PRK12849 401 ATRAAVEEGIVPGGGVALLRAAKALdELAGLNGDQAAGVEIVRRALEAPLRQIAENAGLDGSVVVAKVLELEDGFGFNAA 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1055296569 481 TGEYGDMLEMGILDPAKVTRSALQAAASIAGLMITTEAMVADIPEDKPAAP 531
Cdd:PRK12849 481 TGEYGDLIAAGIIDPVKVTRSALQNAASVAGLLLTTEALVADKPEEEDPPG 531
|
|
| GroEL |
cd03344 |
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ... |
4-522 |
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: 857.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 4 KDVKFGDDARQKMLSGVNILADAVKTTLGPKGRNVVLEKAFGAPTVTKDGVSVAKEIELKDKFENMGAQMVKEVASKASD 83
Cdd:cd03344 1 KDIKFGEEARKALLRGVNKLADAVKVTLGPKGRNVVIEKSFGSPKITKDGVTVAKEIELEDPFENMGAQLVKEVASKTND 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 84 TAGDGTTTATVLAQAIVTEGLKSVAAGFNPMDLKRGIDKAVAAAVDHIAGLATPCADSKSIAQVGTISANSDEHVGTIIA 163
Cdd:cd03344 81 VAGDGTTTATVLARAIIKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKPVKTKEEIAQVATISANGDEEIGELIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 164 EAMDKVGKEGVITVEEGQSLENELDVVEGMQFDRGYLSPYFVTNQENMTAELDSPFILLVDKKISNIRDLLPLLEQVAKA 243
Cdd:cd03344 161 EAMEKVGKDGVITVEEGKTLETELEVVEGMQFDRGYLSPYFVTDPEKMEVELENPYILLTDKKISSIQELLPILELVAKA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 244 SKPLLIIAEDVEGEALATLVVNSMRGIVKVAAVKAPGFGDRRKAMLQDIAILTGGTVISEEVGLELEATTLEHLGTAKRV 323
Cdd:cd03344 241 GRPLLIIAEDVEGEALATLVVNKLRGGLKVCAVKAPGFGDRRKAMLEDIAILTGGTVISEELGLKLEDVTLEDLGRAKKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 324 TLSKENTVIVDGAGDVADIEARVKQIRAQIEESSSDYDKEKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVEDALHAT 403
Cdd:cd03344 321 VVTKDDTTIIGGAGDKAAIKARIAQIRKQIEETTSDYDKEKLQERLAKLSGGVAVIKVGGATEVELKEKKDRVEDALNAT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 404 RAAVEEGVVPGGGTALIRAIQAI-SVKGDNEDQNHGIAAALRAMEMPLRQIVTNAGDEASVVVDKVKQGEGNFGYNAGTG 482
Cdd:cd03344 401 RAAVEEGIVPGGGVALLRASPALdKLKALNGDEKLGIEIVRRALEAPLRQIAENAGVDGSVVVEKVLESPDGFGYDAATG 480
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1055296569 483 EYGDMLEMGILDPAKVTRSALQAAASIAGLMITTEAMVAD 522
Cdd:cd03344 481 EYVDMIEAGIIDPTKVVRSALQNAASVASLLLTTEALVVD 520
|
|
| GroEL |
TIGR02348 |
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ... |
3-525 |
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: 844.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 3 AKDVKFGDDARQKMLSGVNILADAVKTTLGPKGRNVVLEKAFGAPTVTKDGVSVAKEIELKDKFENMGAQMVKEVASKAS 82
Cdd:TIGR02348 1 AKQIKFDEEARKALLRGVDKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDKFENMGAQLVKEVASKTN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 83 DTAGDGTTTATVLAQAIVTEGLKSVAAGFNPMDLKRGIDKAVAAAVDHIAGLATPCADSKSIAQVGTISANSDEHVGTII 162
Cdd:TIGR02348 81 DVAGDGTTTATVLAQAIVKEGLKNVAAGANPIELKRGIEKAVEAVVEELKKLSKPVKGKKEIAQVATISANNDEEIGSLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 163 AEAMDKVGKEGVITVEEGQSLENELDVVEGMQFDRGYLSPYFVTNQENMTAELDSPFILLVDKKISNIRDLLPLLEQVAK 242
Cdd:TIGR02348 161 AEAMEKVGKDGVITVEESKSLETELEVVEGMQFDRGYISPYFVTDAEKMEVELENPYILITDKKISNIKDLLPLLEKVAQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 243 ASKPLLIIAEDVEGEALATLVVNSMRGIVKVAAVKAPGFGDRRKAMLQDIAILTGGTVISEEVGLELEATTLEHLGTAKR 322
Cdd:TIGR02348 241 SGKPLLIIAEDVEGEALATLVVNKLRGTLNVCAVKAPGFGDRRKAMLEDIAILTGGQVISEELGLKLEEVTLDDLGKAKK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 323 VTLSKENTVIVDGAGDVADIEARVKQIRAQIEESSSDYDKEKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVEDALHA 402
Cdd:TIGR02348 321 VTVDKDNTTIVEGAGDKAAIKARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATETEMKEKKLRIEDALNA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 403 TRAAVEEGVVPGGGTALIRAIQAI-SVKGDNEDQNHGIAAALRAMEMPLRQIVTNAGDEASVVVDKVKQGEGNFGYNAGT 481
Cdd:TIGR02348 401 TRAAVEEGIVPGGGVALLRAAAALeGLKGDGEDEAIGIDIVKRALEAPLRQIAENAGLDGAVVAEKVKELKGNFGFNAAT 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1055296569 482 GEYGDMLEMGILDPAKVTRSALQAAASIAGLMITTEAMVADIPE 525
Cdd:TIGR02348 481 GEYEDLVEAGIIDPTKVTRSALQNAASIAGLLLTTEAVVADKPE 524
|
|
| groEL |
PRK12850 |
chaperonin GroEL; Reviewed |
1-531 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237231 Cd Length: 544 Bit Score: 832.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 1 MAAKDVKFGDDARQKMLSGVNILADAVKTTLGPKGRNVVLEKAFGAPTVTKDGVSVAKEIELKDKFENMGAQMVKEVASK 80
Cdd:PRK12850 1 MAAKEIRFSTDARDRLLRGVNILANAVKVTLGPKGRNVVLEKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVKEVASK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 81 ASDTAGDGTTTATVLAQAIVTEGLKSVAAGFNPMDLKRGIDKAVAAAVDHIAGLATPCADSKSIAQVGTISANSDEHVGT 160
Cdd:PRK12850 81 TNDLAGDGTTTATVLAQAIVREGAKLVAAGMNPMDLKRGIDLAVAAVVDELKKIAKKVTSSKEIAQVATISANGDESIGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 161 IIAEAMDKVGKEGVITVEEGQSLENELDVVEGMQFDRGYLSPYFVTNQENMTAELDSPFILLVDKKISNIRDLLPLLEQV 240
Cdd:PRK12850 161 MIAEAMDKVGKEGVITVEEAKTLGTELDVVEGMQFDRGYLSPYFVTNPEKMRAELEDPYILLHEKKISNLQDLLPILEAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 241 AKASKPLLIIAEDVEGEALATLVVNSMRGIVKVAAVKAPGFGDRRKAMLQDIAILTGGTVISEEVGLELEATTLEHLGTA 320
Cdd:PRK12850 241 VQSGRPLLIIAEDVEGEALATLVVNKLRGGLKSVAVKAPGFGDRRKAMLEDIAVLTGGQVISEDLGIKLENVTLDMLGRA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 321 KRVTLSKENTVIVDGAGDVADIEARVKQIRAQIEESSSDYDKEKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVEDAL 400
Cdd:PRK12850 321 KRVLITKENTTIIDGAGDKKNIEARVKQIRAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKEKKDRVDDAL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 401 HATRAAVEEGVVPGGGTALIRAIQAIS-VKGDNEDQNHGIAAALRAMEMPLRQIVTNAGDEASVVVDKVKQGEGNFGYNA 479
Cdd:PRK12850 401 HATRAAVEEGIVPGGGVALLRARSALRgLKGANADETAGIDIVRRALEEPLRQIATNAGFEGSVVVGKVAELPGNFGFNA 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1055296569 480 GTGEYGDMLEMGILDPAKVTRSALQAAASIAGLMITTEAMVADIPEDKPAAP 531
Cdd:PRK12850 481 QTGEYGDMVEAGIIDPAKVTRTALQDAASIAALLITTEAMVAEAPKKAAAAA 532
|
|
| groEL |
PRK12852 |
chaperonin GroEL; Reviewed |
1-531 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237232 Cd Length: 545 Bit Score: 773.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 1 MAAKDVKFGDDARQKMLSGVNILADAVKTTLGPKGRNVVLEKAFGAPTVTKDGVSVAKEIELKDKFENMGAQMVKEVASK 80
Cdd:PRK12852 1 MAAKDVKFSGDARDRMLRGVDILANAVKVTLGPKGRNVVIEKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVREVASK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 81 ASDTAGDGTTTATVLAQAIVTEGLKSVAAGFNPMDLKRGIDKAVAAAVDHIAGLATPCADSKSIAQVGTISANSDEHVGT 160
Cdd:PRK12852 81 TNDLAGDGTTTATVLAQAIVREGAKAVAAGMNPMDLKRGIDIAVAAVVKDIEKRAKPVASSAEIAQVGTISANGDAAIGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 161 IIAEAMDKVGKEGVITVEEGQSLENELDVVEGMQFDRGYLSPYFVTNQENMTAELDSPFILLVDKKISNIRDLLPLLEQV 240
Cdd:PRK12852 161 MIAQAMQKVGNEGVITVEENKSLETEVDIVEGMKFDRGYLSPYFVTNAEKMTVELDDAYILLHEKKLSGLQAMLPVLEAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 241 AKASKPLLIIAEDVEGEALATLVVNSMRGIVKVAAVKAPGFGDRRKAMLQDIAILTGGTVISEEVGLELEATTLEHLGTA 320
Cdd:PRK12852 241 VQSGKPLLIIAEDVEGEALATLVVNRLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGQLISEDLGIKLENVTLKMLGRA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 321 KRVTLSKENTVIVDGAGDVADIEARVKQIRAQIEESSSDYDKEKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVEDAL 400
Cdd:PRK12852 321 KKVVIDKENTTIVNGAGKKADIEARVGQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKEKKDRVEDAL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 401 HATRAAVEEGVVPGGGTALIRAIQAIS-VKGDNEDQNHGIAAALRAMEMPLRQIVTNAGDEASVVVDKVKQGEG-NFGYN 478
Cdd:PRK12852 401 NATRAAVQEGIVPGGGVALLRAKKAVGrINNDNADVQAGINIVLKALEAPIRQIAENAGVEGSIVVGKILENKSeTFGFD 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1055296569 479 AGTGEYGDMLEMGILDPAKVTRSALQAAASIAGLMITTEAMVADIP--EDKPAAP 531
Cdd:PRK12852 481 AQTEEYVDMVAKGIIDPAKVVRTALQDAASVAGLLVTTEAMVAELPkkDAAPAMP 535
|
|
| groEL |
PRK12851 |
chaperonin GroEL; Reviewed |
1-531 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 171770 Cd Length: 541 Bit Score: 764.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 1 MAAKDVKFGDDARQKMLSGVNILADAVKTTLGPKGRNVVLEKAFGAPTVTKDGVSVAKEIELKDKFENMGAQMVKEVASK 80
Cdd:PRK12851 1 MAAKEVKFHVEAREKMLRGVNILADAVKVTLGPKGRNVVIDKSFGAPTITNDGVTIAKEIELEDKFENMGAQMVREVASK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 81 ASDTAGDGTTTATVLAQAIVTEGLKSVAAGFNPMDLKRGIDKAVAAAVDHIAGLATPCADSKSIAQVGTISANSDEHVGT 160
Cdd:PRK12851 81 TNDVAGDGTTTATVLAQAIVREGAKAVAAGANPMDLKRGIDRAVAAVVEELKANARPVTTNAEIAQVATISANGDAEIGR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 161 IIAEAMDKVGKEGVITVEEGQSLENELDVVEGMQFDRGYLSPYFVTNQENMTAELDSPFILLVDKKISNIRDLLPLLEQV 240
Cdd:PRK12851 161 LVAEAMEKVGNEGVITVEESKTAETELEVVEGMQFDRGYLSPYFVTDADKMEAELEDPYILIHEKKISNLQDLLPVLEAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 241 AKASKPLLIIAEDVEGEALATLVVNSMRGIVKVAAVKAPGFGDRRKAMLQDIAILTGGTVISEEVGLELEATTLEHLGTA 320
Cdd:PRK12851 241 VQSGKPLLIIAEDVEGEALATLVVNKLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGIKLENVTLEQLGRA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 321 KRVTLSKENTVIVDGAGDVADIEARVKQIRAQIEESSSDYDKEKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVEDAL 400
Cdd:PRK12851 321 KKVVVEKENTTIIDGAGSKTEIEGRVAQIRAQIEETTSDYDREKLQERLAKLAGGVAVIRVGASTEVEVKEKKDRVDDAL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 401 HATRAAVEEGVVPGGGTALIRAIQAI-SVKGDNEDQNHGIAAALRAMEMPLRQIVTNAGDEASVVVDKVKQGEGNFGYNA 479
Cdd:PRK12851 401 HATRAAVEEGIVPGGGVALLRAVKALdKLETANGDQRTGVEIVRRALEAPVRQIAENAGAEGSVVVGKLREKPGGYGFNA 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1055296569 480 GTGEYGDMLEMGILDPAKVTRSALQAAASIAGLMITTEAMVADIPEDKPAAP 531
Cdd:PRK12851 481 ATNEYGDLYAQGVIDPVKVVRTALQNAASVAGLLLTTEAMVAEKPKKEPAPP 532
|
|
| GroEL |
COG0459 |
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ... |
2-530 |
0e+00 |
|
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227 Cd Length: 497 Bit Score: 739.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 2 AAKDVKFGDDARQKMLSGVNILADAVKTTLGPKGRNVVLEKAFGAPTVTKDGVSVAKEIELKDKFENMGAQMVKEVASKA 81
Cdd:COG0459 1 MAKQILFGEDARRANIRGVKALADAVKVTLGPKGRNVMLVKSFGDPTITNDGVTIAKEIELEDPFENMGAQLVKEVASKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 82 SDTAGDGTTTATVLAQAIVTEGLKSVAAGFNPMDLKRGIDKAVAAAVDHIAGLATPCADSKSIAQVGTISANSDEHVGTI 161
Cdd:COG0459 81 NDEAGDGTTTATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPVDDKEELAQVATISANGDEEIGEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 162 IAEAMDKVGKEGVITVEEGQSLENELDVVEGMQFDRGYLSPYFVTNQENMTAELDSPFILLVDKKISNIRDLLPLLEQVA 241
Cdd:COG0459 161 IAEAMEKVGKDGVITVEEGKGLETELEVVEGMQFDKGYLSPYFVTDPEKMPAELENAYILLTDKKISSIQDLLPLLEKVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 242 KASKPLLIIAEDVEGEALATLVVNSMRGIVKVAAVKAPGFGDRRKAMLQDIAILTGGTVISEEVGLELEATTLEHLGTAK 321
Cdd:COG0459 241 QSGKPLLIIAEDIDGEALATLVVNGIRGVLRVVAVKAPGFGDRRKAMLEDIAILTGGRVISEDLGLKLEDVTLDDLGRAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 322 RVTLSKENTVIVDGAGDVADIearvkqiraqieesssdydkeklqervaklaggvaVIKVGAATEVEMKEKKARVEDALH 401
Cdd:COG0459 321 RVEVDKDNTTIVEGAGNPKAI-----------------------------------VILVGAATEVEVKERKRRVEDALH 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 402 ATRAAVEEGVVPGGGTALIRAIQAIS---VKGDNeDQNHGIAAALRAMEMPLRQIVTNAGDEASVVVDKVKQGE-GNFGY 477
Cdd:COG0459 366 ATRAAVEEGIVPGGGAALLRAARALRelaAKLEG-DEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKVRAAKdKGFGF 444
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1055296569 478 NAGTGEYGDMLEMGILDPAKVTRSALQAAASIAGLMITTEAMVADIPEDKPAA 530
Cdd:COG0459 445 DAATGEYVDMLEAGVIDPAKVKRSALQNAASVAGLILTTEAVIADKPEKEEAA 497
|
|
| PTZ00114 |
PTZ00114 |
Heat shock protein 60; Provisional |
2-532 |
0e+00 |
|
Heat shock protein 60; Provisional
Pssm-ID: 185455 Cd Length: 555 Bit Score: 718.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 2 AAKDVKFGDDARQKMLSGVNILADAVKTTLGPKGRNVVLEKAFGAPTVTKDGVSVAKEIELKDKFENMGAQMVKEVASKA 81
Cdd:PTZ00114 13 KGKEIRFGDEARQSLLKGIERLADAVAVTLGPKGRNVIIEQEYGSPKITKDGVTVAKAIEFSDRFENVGAQLIRQVASKT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 82 SDTAGDGTTTATVLAQAIVTEGLKSVAAGFNPMDLKRGIDKAVAAAVDHIAGLATPCADSKSIAQVGTISANSDEHVGTI 161
Cdd:PTZ00114 93 NDKAGDGTTTATILARAIFREGCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQSRPVKTKEDILNVATISANGDVEIGSL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 162 IAEAMDKVGKEGVITVEEGQSLENELDVVEGMQFDRGYLSPYFVTNQENMTAELDSPFILLVDKKISNIRDLLPLLEQVA 241
Cdd:PTZ00114 173 IADAMDKVGKDGTITVEDGKTLEDELEVVEGMSFDRGYISPYFVTNEKTQKVELENPLILVTDKKISSIQSILPILEHAV 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 242 KASKPLLIIAEDVEGEALATLVVNSMRGIVKVAAVKAPGFGDRRKAMLQDIAILTGGTVISEE-VGLELEATTLEHLGTA 320
Cdd:PTZ00114 253 KNKRPLLIIAEDVEGEALQTLIINKLRGGLKVCAVKAPGFGDNRKDILQDIAVLTGATVVSEDnVGLKLDDFDPSMLGSA 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 321 KRVTLSKENTVIVDGAGDVADIEARVKQIRAQIEESSSDYDKEKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVEDAL 400
Cdd:PTZ00114 333 KKVTVTKDETVILTGGGDKAEIKERVELLRSQIERTTSEYDKEKLKERLAKLSGGVAVIKVGGASEVEVNEKKDRIEDAL 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 401 HATRAAVEEGVVPGGGTALIRAIQAI-SVKGDNE---DQNHGIAAALRAMEMPLRQIVTNAGDEASVVVDKVKQG-EGNF 475
Cdd:PTZ00114 413 NATRAAVEEGIVPGGGVALLRASKLLdKLEEDNEltpDQRTGVKIVRNALRLPTKQIAENAGVEGAVVVEKILEKkDPSF 492
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1055296569 476 GYNAGTGEYGDMLEMGILDPAKVTRSALQAAASIAGLMITTEAMVADIPEDKPAAPD 532
Cdd:PTZ00114 493 GYDAQTGEYVNMFEAGIIDPTKVVRSALVDAASVASLMLTTEAAIVDLPKEKKKNKN 549
|
|
| groEL |
CHL00093 |
chaperonin GroEL |
3-527 |
0e+00 |
|
chaperonin GroEL
Pssm-ID: 177025 Cd Length: 529 Bit Score: 657.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 3 AKDVKFGDDARQKMLSGVNILADAVKTTLGPKGRNVVLEKAFGAPTVTKDGVSVAKEIELKDKFENMGAQMVKEVASKAS 82
Cdd:CHL00093 2 SKKILYQDNARRALERGMDILAEAVSVTLGPKGRNVVLEKKYGSPQIVNDGVTIAKEIELEDHIENTGVALIRQAASKTN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 83 DTAGDGTTTATVLAQAIVTEGLKSVAAGFNPMDLKRGIDKAVAAAVDHIAGLATPCADSKSIAQVGTISANSDEHVGTII 162
Cdd:CHL00093 82 DVAGDGTTTATVLAYAIVKQGMKNVAAGANPISLKRGIEKATQYVVSQIAEYARPVEDIQAITQVASISAGNDEEVGSMI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 163 AEAMDKVGKEGVITVEEGQSLENELDVVEGMQFDRGYLSPYFVTNQENMTAELDSPFILLVDKKISNIR-DLLPLLEQVA 241
Cdd:CHL00093 162 ADAIEKVGREGVISLEEGKSTVTELEITEGMRFEKGFISPYFVTDTERMEVVQENPYILLTDKKITLVQqDLLPILEQVT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 242 KASKPLLIIAEDVEGEALATLVVNSMRGIVKVAAVKAPGFGDRRKAMLQDIAILTGGTVISEEVGLELEATTLEHLGTAK 321
Cdd:CHL00093 242 KTKRPLLIIAEDVEKEALATLVLNKLRGIVNVVAVRAPGFGDRRKAMLEDIAILTGGQVITEDAGLSLETIQLDLLGQAR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 322 RVTLSKENTVIVdGAGDVADIEARVKQIRAQIEESSSDYDKEKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVEDALH 401
Cdd:CHL00093 322 RIIVTKDSTTII-ADGNEEQVKARCEQLRKQIEIADSSYEKEKLQERLAKLSGGVAVIKVGAATETEMKDKKLRLEDAIN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 402 ATRAAVEEGVVPGGGTALIRAIQAISVKGDN---EDQNHGIAAALRAMEMPLRQIVTNAGDEASVVVDKVKQGEGNFGYN 478
Cdd:CHL00093 401 ATKAAVEEGIVPGGGATLVHLSENLKTWAKNnlkEDELIGALIVARAILAPLKRIAENAGKNGSVIIEKVQEQDFEIGYN 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1055296569 479 AGTGEYGDMLEMGILDPAKVTRSALQAAASIAGLMITTEAMVADIPEDK 527
Cdd:CHL00093 481 AANNKFVNMYEAGIIDPAKVTRSALQNAASIASMILTTECIIVDKKESS 529
|
|
| PRK14104 |
PRK14104 |
chaperonin GroEL; Provisional |
1-531 |
0e+00 |
|
chaperonin GroEL; Provisional
Pssm-ID: 172594 Cd Length: 546 Bit Score: 644.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 1 MAAKDVKFGDDARQKMLSGVNILADAVKTTLGPKGRNVVLEKAFGAPTVTKDGVSVAKEIELKDKFENMGAQMVKEVASK 80
Cdd:PRK14104 1 MSAKEVKFGVDARDRMLRGVDILANAVKVTLGPKGRNVVLDKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVREVASK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 81 ASDTAGDGTTTATVLAQAIVTEGLKSVAAGFNPMDLKRGIDKAVAAAVDHIAGLATPCADSKSIAQVGTISANSDEHVGT 160
Cdd:PRK14104 81 SADAAGDGTTTATVLAQAIVREGAKSVAAGMNPMDLKRGIDLAVEAVVADLVKNSKKVTSNDEIAQVGTISANGDAEIGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 161 IIAEAMDKVGKEGVITVEEGQSLENELDVVEGMQFDRGYLSPYFVTNQENMTAELDSPFILLVDKKISNIRDLLPLLEQV 240
Cdd:PRK14104 161 FLADAMKKVGNEGVITVEEAKSLETELDVVEGMQFDRGYISPYFVTNADKMRVEMDDAYILINEKKLSSLNELLPLLEAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 241 AKASKPLLIIAEDVEGEALATLVVNSMRGIVKVAAVKAPGFGDRRKAMLQDIAILTGGTVISEEVGLELEATTLEHLGTA 320
Cdd:PRK14104 241 VQTGKPLVIVAEDVEGEALATLVVNRLRGGLKVAAVKAPGFGDRRKAMLQDIAILTGGQAISEDLGIKLENVTLQMLGRA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 321 KRVTLSKENTVIVDGAGDVADIEARVKQIRAQIEESSSDYDKEKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVEDAL 400
Cdd:PRK14104 321 KKVMIDKENTTIVNGAGKKADIEARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKERKDRVDDAM 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 401 HATRAAVEEGVVPGGGTALIRAIQAIS-VKGDNEDQNHGIAAALRAMEMPLRQIVTNAGDEASVVVDKVKQGEG-NFGYN 478
Cdd:PRK14104 401 HATRAAVEEGIVPGGGVALLRASEQLKgIKTKNDDQKTGVEIVRKALSAPARQIAINAGEDGSVIVGKILEKEQySYGFD 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1055296569 479 AGTGEYGDMLEMGILDPAKVTRSALQAAASIAGLMITTEAMVADIPEDKPAAP 531
Cdd:PRK14104 481 SQTGEYGNLVSKGIIDPTKVVRTAIQNAASVAALLITTEAMVAELPKKGGAGP 533
|
|
| PLN03167 |
PLN03167 |
Chaperonin-60 beta subunit; Provisional |
2-530 |
0e+00 |
|
Chaperonin-60 beta subunit; Provisional
Pssm-ID: 215611 [Multi-domain] Cd Length: 600 Bit Score: 527.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 2 AAKDVKFGDD--ARQKMLSGVNILADAVKTTLGPKGRNVVLEKAFGAPTVTKDGVSVAKEIELKDKFENMGAQMVKEVAS 79
Cdd:PLN03167 55 AAKELHFNKDgsAIKKLQAGVNKLADLVGVTLGPKGRNVVLESKYGSPKIVNDGVTVAKEVELEDPVENIGAKLVRQAAA 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 80 KASDTAGDGTTTATVLAQAIVTEGLKSVAAGFNPMDLKRGIDKAVAAAVDHIAGLATPCADSKsIAQVGTISANSDEHVG 159
Cdd:PLN03167 135 KTNDLAGDGTTTSVVLAQGLIAEGVKVVAAGANPVQITRGIEKTAKALVKELKKMSKEVEDSE-LADVAAVSAGNNYEVG 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 160 TIIAEAMDKVGKEGVITVEEGQSLENELDVVEGMQFDRGYLSPYFVTNQENMTAELDSPFILLVDKKISNIRDLLPLLEQ 239
Cdd:PLN03167 214 NMIAEAMSKVGRKGVVTLEEGKSAENNLYVVEGMQFDRGYISPYFVTDSEKMSVEYDNCKLLLVDKKITNARDLIGILED 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 240 VAKASKPLLIIAEDVEGEALATLVVNSMRGIVKVAAVKAPGFGDRRKAMLQDIAILTGGTVISEEVGLELEATTLEHLGT 319
Cdd:PLN03167 294 AIRGGYPLLIIAEDIEQEALATLVVNKLRGSLKIAALKAPGFGERKSQYLDDIAILTGGTVIREEVGLSLDKVGKEVLGT 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 320 AKRVTLSKENTVIVDGAGDVADIEARVKQIRAQIEESSSDYDKEKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVEDA 399
Cdd:PLN03167 374 AAKVVLTKDTTTIVGDGSTQEAVNKRVAQIKNLIEAAEQDYEKEKLNERIAKLSGGVAVIQVGAQTETELKEKKLRVEDA 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 400 LHATRAAVEEGVVPGGGTALIR---AIQAISVKGDNEDQNHGIAAALRAMEMPLRQIVTNAGDEASVVVDKVKQGEG-NF 475
Cdd:PLN03167 454 LNATKAAVEEGIVVGGGCTLLRlasKVDAIKDTLENDEQKVGADIVKRALSYPLKLIAKNAGVNGSVVSEKVLSNDNpKF 533
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1055296569 476 GYNAGTGEYGDMLEMGILDPAKVTRSALQAAASIAGLMITTEAMVADIPEDKPAA 530
Cdd:PLN03167 534 GYNAATGKYEDLMAAGIIDPTKVVRCCLEHAASVAKTFLTSDCVVVEIKEPEPVP 588
|
|
| chaperonin_type_I_II |
cd00309 |
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ... |
4-521 |
4.27e-139 |
|
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: 410.28 E-value: 4.27e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 4 KDVKFGDDARQKMLSGVNILADAVKTTLGPKGRNVVLEKAFGAPTVTKDGVSVAKEIELkdkfENMGAQMVKEVASKASD 83
Cdd:cd00309 1 KEREFGEEARLSNINAAKALADAVKTTLGPKGMDKMLVDSLGDPTITNDGATILKEIEV----EHPAAKLLVEVAKSQDD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 84 TAGDGTTTATVLAQAIVTEGLKSVAAGFNPMDLKRGIDKAVAAAVDHIAGLATP--CADSKSIAQVGTISANS------D 155
Cdd:cd00309 77 EVGDGTTTVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVPidVEDREELLKVATTSLNSklvsggD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 156 EHVGTIIAEAMDKVGKE------GVITVEEGQS---LENELdvVEGMQFDRGYLSPYfvtnqenMTAELDSPFILLVDKK 226
Cdd:cd00309 157 DFLGELVVDAVLKVGKEngdvdlGVIRVEKKKGgslEDSEL--VVGMVFDKGYLSPY-------MPKRLENAKILLLDCK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 227 ISNirdllplleqvakaskplLIIAED-VEGEALATLVVNsmrgivKVAAVKApgfgdRRKAMLQDIAILTGGTVISeev 305
Cdd:cd00309 228 LEY------------------VVIAEKgIDDEALHYLAKL------GIMAVRR-----VRKEDLERIAKATGATIVS--- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 306 glELEATTLEHLGTAKRVTLSK----ENTVIVDGAGdvadiearvkqiraqieesssdydkeklqervaklaGGVAVIKV 381
Cdd:cd00309 276 --RLEDLTPEDLGTAGLVEETKigdeKYTFIEGCKG------------------------------------GKVATILL 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 382 GAATEVEMKEKKARVEDALHATRAAVEE-GVVPGGGTALIRAIQAIS--VKGDNEDQNHGIAAALRAMEMPLRQIVTNAG 458
Cdd:cd00309 318 RGATEVELDEAERSLHDALCAVRAAVEDgGIVPGGGAAEIELSKALEelAKTLPGKEQLGIEAFADALEVIPRTLAENAG 397
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1055296569 459 DEASVVVDKVKQGEGNFGYNAG----TGEYGDMLEMGILDPAKVTRSALQAAASIAGLMITTEAMVA 521
Cdd:cd00309 398 LDPIEVVTKLRAKHAEGGGNAGgdveTGEIVDMKEAGIIDPLKVKRQALKSATEAASLILTIDDIIV 464
|
|
| Cpn60_TCP1 |
pfam00118 |
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ... |
23-523 |
1.95e-71 |
|
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: 236.33 E-value: 1.95e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 23 LADAVKTTLGPKGRNVVLEKAFGAPTVTKDGVSVAKEIELkdkfENMGAQMVKEVASKASDTAGDGTTTATVLAQAIVTE 102
Cdd:pfam00118 1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELEI----QHPAAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 103 GLKSVAAGFNPMDLKRGIDKAVAAAVDHIAG-LATPC--ADSKSIAQVGTISANSD------EHVGTIIAEA-------- 165
Cdd:pfam00118 77 AEKLLAAGVHPTTIIEGYEKALEKALEILDSiISIPVedVDREDLLKVARTSLSSKiisresDFLAKLVVDAvlaipknd 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 166 -MDKVGKEGVITVEEGQSleNELDVVEGMQFDRGYLSPyfvtnqeNMTAELDSPFILLVDKKISNIRD------------ 232
Cdd:pfam00118 157 gSFDLGNIGVVKILGGSL--EDSELVDGVVLDKGPLHP-------DMPKRLENAKVLLLNCSLEYEKTetkatvvlsdae 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 233 ------------LLPLLEQVAKASKPLLIIAEDVEGEALATLVVNSMRGIVKVaavkapgfgdrRKAMLQDIAILTGGTV 300
Cdd:pfam00118 228 qlerflkaeeeqILEIVEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMALRRV-----------KKRDLERLAKATGARA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 301 ISeevglELEATTLEHLGTAKRV---TLSKENTVIVDGAGDvadiearvkqiraqieesssdydkeklqervaklaGGVA 377
Cdd:pfam00118 297 VS-----SLDDLTPDDLGTAGKVeeeKIGDEKYTFIEGCKS-----------------------------------PKAA 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 378 VIKVGAATEVEMKEKKARVEDALHATRAAVEE-GVVPGGG---TALIRAIQAISVKGDNEDQnHGIAAALRAMEMPLRQI 453
Cdd:pfam00118 337 TILLRGATDHVLDEIERSIHDALCVVKNAIEDpRVVPGGGaveMELARALREYAKSVSGKEQ-LAIEAFAEALEVIPKTL 415
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1055296569 454 VTNAGDEASVVVDKVK----QGEGNFGYNAGTGEYGDMLEMGILDPAKVTRSALQAAASIAGLMITTEAMVADI 523
Cdd:pfam00118 416 AENAGLDPIEVLAELRaahaSGEKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKSATEAASTILRIDDIIKAK 489
|
|
| chaperonin_like |
cd03333 |
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ... |
142-409 |
6.91e-41 |
|
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings, each composed of 7-9 subunits. There are 2 main chaperonin groups. The symmetry of type I is seven-fold and they are found in eubacteria (GroEL) and in organelles of eubacterial descent (hsp60 and RBP). The symmetry of type II is eight- or nine-fold and they are found in archea (thermosome), thermophilic bacteria (TF55) and in the eukaryotic cytosol (CTT). Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. This superfamily also contains related domains from Fab1-like phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinases that only contain the intermediate and apical domains.
Pssm-ID: 239449 [Multi-domain] Cd Length: 209 Bit Score: 146.46 E-value: 6.91e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 142 KSIAQVGTISANS-----DEHVGTIIAEAMDKVGKE------GVITVEEGQS---LENELdvVEGMQFDRGYLSPYfvtn 207
Cdd:cd03333 2 ELLLQVATTSLNSklsswDDFLGKLVVDAVLKVGPDnrmddlGVIKVEKIPGgslEDSEL--VVGVVFDKGYASPY---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 208 qenMTAELDSPFILLVDKKISNirdllplleqvakaskplLIIAED-VEGEALATLVVNsmrgivKVAAVKApgfgdRRK 286
Cdd:cd03333 76 ---MPKRLENAKILLLDCPLEY------------------VVIAEKgIDDLALHYLAKA------GIMAVRR-----VKK 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 287 AMLQDIAILTGGTVISeevglELEATTLEHLGTAKRVTLSK----ENTVIVDGAGdvadiearvkqiraqieesssdydk 362
Cdd:cd03333 124 EDLERIARATGATIVS-----SLEDLTPEDLGTAELVEETKigeeKLTFIEGCKG------------------------- 173
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1055296569 363 eklqervaklaGGVAVIKVGAATEVEMKEKKARVEDALHATRAAVEE 409
Cdd:cd03333 174 -----------GKAATILLRGATEVELDEVKRSLHDALCAVRAAVEE 209
|
|
| cpn60 |
cd03343 |
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ... |
9-521 |
7.32e-17 |
|
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: 83.47 E-value: 7.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 9 GDDARQKMLSGVNILADAVKTTLGPKGRNVVLEKAFGAPTVTKDGVSVAKEIELkdkfENMGAQMVKEVASKASDTAGDG 88
Cdd:cd03343 13 GRDAQRMNIAAAKAVAEAVRTTLGPKGMDKMLVDSLGDVTITNDGATILKEMDI----EHPAAKMLVEVAKTQDEEVGDG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 89 TTTATVLAQAIVTEGLKSVAAGFNPMDLKRGIDKAVAAAVDHIAGLATPCADS-----KSIAQV---GTISANSDEHVGT 160
Cdd:cd03343 89 TTTAVVLAGELLEKAEDLLDQNIHPTVIIEGYRLAAEKALELLDEIAIKVDPDdkdtlRKIAKTsltGKGAEAAKDKLAD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 161 IIAEAMDKVGKEG------------VITVEEGQSLENELdvVEGMQFDRGYLSPyfvtnqeNMTAELDSPFILLVDKKIS 228
Cdd:cd03343 169 LVVDAVLQVAEKRdgkyvvdldnikIEKKTGGSVDDTEL--IRGIVIDKEVVHP-------GMPKRVENAKIALLDAPLE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 229 ----------NIRD---LLPLLEQVAKASKPLLiiaedvegEALATL---VVNSMRGIVKVAA---VKAPGFGDRR--KA 287
Cdd:cd03343 240 vkkteidakiRITSpdqLQAFLEQEEAMLKEMV--------DKIADTganVVFCQKGIDDLAQhylAKAGILAVRRvkKS 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 288 MLQDIAILTGGTVISeevglELEATTLEHLGTAKRVT---LSKENTVIVDGagdvadiearvkqiraqieesssdydkek 364
Cdd:cd03343 312 DMEKLARATGAKIVT-----NIDDLTPEDLGEAELVEerkVGDDKMVFVEG----------------------------- 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 365 lqervAKLAGGVAVIKVGaATEVEMKEKKARVEDALHATRAAVEEG-VVPGGGTALIRAIQ-----AISVKGdneDQNHG 438
Cdd:cd03343 358 -----CKNPKAVTILLRG-GTEHVVDELERALEDALRVVADALEDGkVVAGGGAVEIELAKrlreyARSVGG---REQLA 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 439 IAAALRAMEMPLRQIVTNAG-DEASVVVD---KVKQGEGNFGYNAGTGEYGDMLEMGILDPAKVTRSALQAAASIAGLMI 514
Cdd:cd03343 429 VEAFADALEEIPRTLAENAGlDPIDTLVElraAHEKGNKNAGLDVYTGEVVDMLEKGVIEPLRVKKQAIKSATEAATMIL 508
|
....*..
gi 1055296569 515 TTEAMVA 521
Cdd:cd03343 509 RIDDVIA 515
|
|
| chap_CCT_eta |
TIGR02345 |
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ... |
7-520 |
4.82e-10 |
|
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: 62.08 E-value: 4.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 7 KFGDDARQ---KMLSGVNI---LADAVKTTLGPKGRNVVLEKAFGAPTVTKDGVSVAKEIELKdkfeNMGAQMVKEVASK 80
Cdd:TIGR02345 8 KEGTDTSQgkgQLISNINAcvaIAEALKTTLGPRGMDKLIVGSNGKATISNDGATILKLLDIV----HPAAKTLVDIAKS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 81 ASDTAGDGTTTATVLAQAIVTEGLKSVAAGFNPMDLKRGIDKAVAAAVDHIAGLATPCADSKS--------IAQVGTIS- 151
Cdd:TIGR02345 84 QDAEVGDGTTSVTILAGELLKEAKPFIEEGVHPQLIIRCYREALSLAVEKIKEIAVTIDEEKGeqrellekCAATALSSk 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 152 --ANSDEHVGTIIAEAMDKVGKE-------GVITVeEGQSLENELdVVEGMQFDRGYlsPYFVTNQEnmtaeldspfill 222
Cdd:TIGR02345 164 liSHNKEFFSKMIVDAVLSLDRDdldlkliGIKKV-QGGALEDSQ-LVNGVAFKKTF--SYAGFEQQ------------- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 223 vDKKISNIRDLLPLLEQVAKASKP-LLIIAEDVEG-----EALATLVVNSMRGIV----KVAAVKAPgFGDRRKAMLQDI 292
Cdd:TIGR02345 227 -PKKFANPKILLLNVELELKAEKDnAEIRVEDVEDyqaivDAEWAIIFRKLEKIVesgaNVVLSKLP-IGDLATQYFADR 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 293 AILTGGTVISEEVgleleattlehlgtaKRVTLSKENTVIvdgaGDVADIEARVKQIRAQIEEsssdydKEKLQERVAKL 372
Cdd:TIGR02345 305 DIFCAGRVSAEDL---------------KRVIKACGGSIQ----STTSDLEADVLGTCALFEE------RQIGSERYNYF 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 373 AGG-----VAVIKVGAATEVeMKEKKARVEDALHATRAAVE-EGVVPGGGTA---LIRAIQAISVKGDNEDQnHGIAAAL 443
Cdd:TIGR02345 360 TGCphaktCTIILRGGAEQF-IEEAERSLHDAIMIVRRALKnKKIVAGGGAIemeLSKCLRDYSKTIDGKQQ-LIINAFA 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 444 RAMEMPLRQIVTNAGDEASVVVDKVK----QGEGNFGYNAGTGEYGDMLEMGILDPAKVTRSALQAAASIAGLMITTEAM 519
Cdd:TIGR02345 438 KALEIIPRQLCENAGFDSIEILNKLRsrhaKGGKWYGVDINTEDIGDNFEAFVWEPALVKINALKAAFEAACTILSVDET 517
|
.
gi 1055296569 520 V 520
Cdd:TIGR02345 518 I 518
|
|
| TCP1_eta |
cd03340 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ... |
7-514 |
5.66e-07 |
|
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: 52.29 E-value: 5.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 7 KFGDDARQ---KMLSGVN---ILADAVKTTLGPKGRNVVLEKAFGAPTVTKDGVSVAKEIELKdkfeNMGAQMVKEVASK 80
Cdd:cd03340 6 KEGTDTSQgkgQLISNINacqAIADAVRTTLGPRGMDKLIVDGRGKVTISNDGATILKLLDIV----HPAAKTLVDIAKS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 81 ASDTAGDGTTTATVLAQAIVTEGLKSVAAGFNPMDLKRGIDKAVAAAVDHIAGLATP---------------CA----DS 141
Cdd:cd03340 82 QDAEVGDGTTSVVVLAGEFLKEAKPFIEDGVHPQIIIRGYRKALQLAIEKIKEIAVNidkedkeeqrellekCAatalNS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 142 KSIaqvgtisANSDEHVGTIIAEAMDKVGKE------GVITVeEGQSLENELdVVEGMQFDRGYlsPYFVTNQEnmtael 215
Cdd:cd03340 162 KLI-------ASEKEFFAKMVVDAVLSLDDDldldmiGIKKV-PGGSLEDSQ-LVNGVAFKKTF--SYAGFEQQ------ 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 216 dsPfillvdKKISNIRDLLPLLEQVAKASKP-LLIIAEDVEG-----EALATLVVNSMRGIVKVAA----VKAPgFGDRR 285
Cdd:cd03340 225 --P------KKFKNPKILLLNVELELKAEKDnAEVRVEDPEEyqaivDAEWKIIYDKLEKIVKSGAnvvlSKLP-IGDLA 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 286 KAMLQDIAILTGGTVISEEVgleleattlehlgtaKRVTLSKENTVIvdgaGDVADIEARVKQIRAQIEESSSDYDKEKL 365
Cdd:cd03340 296 TQYFADRDIFCAGRVPEEDL---------------KRVAQATGGSIQ----TTVSNITDDVLGTCGLFEERQVGGERYNI 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 366 QERVAKlAGGVAVIKVGAATEVeMKEKKARVEDALHATRAAVEEG-VVPGGGT---ALIRAIQAISVKGDNEDQNHgIAA 441
Cdd:cd03340 357 FTGCPK-AKTCTIILRGGAEQF-IEEAERSLHDAIMIVRRAIKNDsVVAGGGAiemELSKYLRDYSRTIAGKQQLV-INA 433
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1055296569 442 ALRAMEMPLRQIVTNAGDEASVVVDKVK----QGEG-NFGYNAGTGEYGDMLEMGILDPAKVTRSALQAAASIAGLMI 514
Cdd:cd03340 434 FAKALEIIPRQLCDNAGFDATDILNKLRqkhaQGGGkWYGVDINNEGIADNFEAFVWEPSLVKINALTAATEAACLIL 511
|
|
| TCP1_delta |
cd03338 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ... |
23-507 |
1.14e-06 |
|
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: 51.13 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 23 LADAVKTTLGPKGRNVVLEKAFGAPTVTKDGVSVAKEIELKdkfeNMGAQMVKEVASKASDTAGDGTTTATVLAQAIVTE 102
Cdd:cd03338 20 VADAIRTSLGPRGMDKMIQTGKGEVIITNDGATILKQMSVL----HPAAKMLVELSKAQDIEAGDGTTSVVVLAGALLSA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 103 GLKSVAAGFNPMDLKRGIDKAVAAAVDHIAGLATPC--ADSKSIAQVGTISANS------DEHVGTIIAEAMDKVGKEG- 173
Cdd:cd03338 96 CESLLKKGIHPTVISESFQIAAKKAVEILDSMSIPVdlNDRESLIKSATTSLNSkvvsqySSLLAPIAVDAVLKVIDPAt 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 174 ----------VITVEEGQSLENELdvVEGMQFD-RGYLSPYFVTNQENMT------------AELDSPFIL----LVDKK 226
Cdd:cd03338 176 atnvdlkdirIVKKLGGTIEDTEL--VDGLVFTqKASKKAGGPTRIEKAKigliqfclsppkTDMDNNIVVndyaQMDRI 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 227 ISNIRD-LLPLLEQVAKASKPLLIIAEDVEGEALATLVVNSMRGIvKVAAVKAPgfgDRrkamlQDIAILTGGTVISEEV 305
Cdd:cd03338 254 LREERKyILNMCKKIKKSGCNVLLIQKSILRDAVSDLALHFLAKL-KIMVVKDI---ER-----EEIEFICKTIGCKPVA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 306 glELEATTLEHLGTAKRVtlskentvivdgagdvadiearvkqiraqiEESSSDYDKEKLQERVAKLAGGVAVIkVGAAT 385
Cdd:cd03338 325 --SIDHFTEDKLGSADLV------------------------------EEVSLGDGKIVKITGVKNPGKTVTIL-VRGSN 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 386 EVEMKEKKARVEDALHATRAAVEE-GVVPGGGT-----ALIRAIQAISVKGDNEdqnHGIAAALRAMEMPLRQIVTNAGD 459
Cdd:cd03338 372 KLVLDEAERSLHDALCVIRCLVKKrALIPGGGApeieiALQLSEWARTLTGVEQ---YCVRAFADALEVIPYTLAENAGL 448
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1055296569 460 EASVVV----DKVKQGEGNFGYNAGTGEYGDMLEMGILDPAKVTRSALQAAA 507
Cdd:cd03338 449 NPISIVtelrNRHAQGEKNAGINVRKGAITNILEENVVQPLLVSTSAITLAT 500
|
|
| chap_CCT_epsi |
TIGR02343 |
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ... |
9-131 |
9.54e-06 |
|
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: 48.26 E-value: 9.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 9 GDDARQKMLSGVNILADAVKTTLGPKGRNVVLEKAFGAPTVTKDGVSVAKEIELkdkfENMGAQMVKEVASKASDTAGDG 88
Cdd:TIGR02343 25 GLEAKKSNIAAAKSVASILRTSLGPKGMDKMLISPDGDITVTNDGATILSQMDV----DNQIAKLMVELSKSQDDEIGDG 100
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1055296569 89 TTTATVLAQAIVTEGLKSVAAGFNPMDLKRGIDKAVAAAVDHI 131
Cdd:TIGR02343 101 TTGVVVLAGALLEQAEELLDKGIHPIKIADGFEEAARIAVEHL 143
|
|
| chap_CCT_alpha |
TIGR02340 |
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ... |
9-509 |
1.04e-05 |
|
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: 48.18 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 9 GDDARQKMLSGVNILADAVKTTLGPKGRNVVLEKAFGAPTVTKDGVSVAKEIELkdkfENMGAQMVKEVASKASDTAGDG 88
Cdd:TIGR02340 10 GQDVRTQNVTAAMAIANIVKTSLGPVGLDKMLVDDIGDVTITNDGATILKLLEV----EHPAAKILVELAQLQDREVGDG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 89 TTTATVLAQAIVTEGLKSVAAGFNPMDLKRGIDKAVAAAVDHIA----------GLATPCADSKSIAQVGTISANSDeHV 158
Cdd:TIGR02340 86 TTSVVIIAAELLKRADELVKNKIHPTSVISGYRLACKEAVKYIKenlsvsvdelGREALINVAKTSMSSKIIGLDSD-FF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 159 GTIIAEAMDKVGkegvITVEEGQSLE--NELDVVE--GMQFDRGYLSPYFVTNQ----ENMTAELDSPFILLVDKKISNI 230
Cdd:TIGR02340 165 SNIVVDAVLAVK----TTNENGETKYpiKAINILKahGKSARESMLVKGYALNCtvasQQMPKRIKNAKIACLDFNLQKA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 231 RDLLPL---------LEQVAKasKPLLIIAEDVEG--EALATLVVNSmRGIVKVAA---VKAPGFGDRR--KAMLQDIAI 294
Cdd:TIGR02340 241 KMALGVqivvddpekLEQIRQ--READITKERIKKilDAGANVVLTT-GGIDDMCLkyfVEAGAMGVRRckKEDLKRIAK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 295 LTGGTVISEEVGLELEAT-TLEHLGTAKRVtlskentvivdgagdvadIEARVKqiraqieesssdyDKEKLQERVAKLA 373
Cdd:TIGR02340 318 ATGATLVSTLADLEGEETfEASYLGFADEV------------------VQERIA-------------DDECILIKGTKKR 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 374 GGVAVIKVGaATEVEMKEKKARVEDALHATRAAVEEG-VVPGGG---TALIRAIQAISVKGDNEDQnHGIAAALRAMEMP 449
Cdd:TIGR02340 367 KSASIILRG-ANDFMLDEMERSLHDALCVVKRTLESNsVVPGGGaveAALSIYLENFATTLGSREQ-LAIAEFARALLII 444
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1055296569 450 LRQIVTNAGDEASVVVDKV------------KQGEGNFGYNAGTGEYGDMLEMGILDPA----KVTRSALQAAASI 509
Cdd:TIGR02340 445 PKTLAVNAAKDSTELVAKLrayhaaaqlkpeKKHLKWYGLDLVNGKIRDNKEAGVLEPTvskvKSLKFATEAAITI 520
|
|
| TCP1_beta |
cd03336 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ... |
9-514 |
1.53e-05 |
|
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: 47.71 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 9 GDDARQKMLSGVNILADAVKTTLGPKGRNVVLE--KAFGAPTVTKDGVSVAKEIELkdkfENMGAQMVKEVASKASDTAG 86
Cdd:cd03336 11 GETARLSSFVGAIAIGDLVKTTLGPKGMDKILQsvGRSGGVTVTNDGATILKSIGV----DNPAAKVLVDISKVQDDEVG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 87 DGTTTATVLAQAIVTEGLKSVAAGFNPMDLKRGIDKAVAAA--------VDHIAGLATPCADSKSIAQVgTISAN----S 154
Cdd:cd03336 87 DGTTSVTVLAAELLREAEKLVAQKIHPQTIIEGYRMATAAAreallssaVDHSSDEEAFREDLLNIART-TLSSKiltqD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 155 DEHVGTIIAEAMDKVGKEGvitveegqslenELDVVEGMQFDRGYLSPYFvtnqenmtaeLDSPFILlvDKKISnirdll 234
Cdd:cd03336 166 KEHFAELAVDAVLRLKGSG------------NLDAIQIIKKLGGSLKDSY----------LDEGFLL--DKKIG------ 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 235 plLEQVAKASKPLLIIAE--------DVEGealATLVVNSMrgiVKVAAVKAPgfgdRRKAMLQDIA-ILTGGtvISEEV 305
Cdd:cd03336 216 --VNQPKRIENAKILIANtpmdtdkiKIFG---AKVRVDST---AKVAEIEEA----EKEKMKNKVEkILKHG--INCFI 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 306 GLELEATTLEHLGTAKRVtlskentVIVDGAgDVADIEARVKQIRAQIEESSSDYDKEKL------------QERVAKL- 372
Cdd:cd03336 282 NRQLIYNYPEQLFADAGI-------MAIEHA-DFDGVERLALVTGGEIASTFDHPELVKLgtcklieeimigEDKLIRFs 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 373 ---AGGVAVIKVGAATEVEMKEKKARVEDALHATRAAVEEG-VVPGGGTALIRAIQAISVKGDNED--QNHGIAAALRAm 446
Cdd:cd03336 354 gvaAGEACTIVLRGASQQILDEAERSLHDALCVLAQTVKDTrVVLGGGCSEMLMAKAVEELAKKTPgkKSLAIEAFAKA- 432
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1055296569 447 empLRQIVT----NAGDEASVVVDKVK----QGEGNFGYNAGTGEYGDMLEMGILDPAKVTRSALQAAASIAGLMI 514
Cdd:cd03336 433 ---LRQLPTiiadNAGYDSAELVAQLRaahyNGNTTAGLDMRKGTVGDMKELGITESFKVKRQVLLSASEAAEMIL 505
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
9-127 |
8.52e-05 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 45.40 E-value: 8.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 9 GDDARQKMLSGVNILADAVKTTLGPKGRNVVLEKAFGAP-----TVTKDGVSVAKEIELkdkfENMGAQMVKEVASKASD 83
Cdd:PTZ00212 20 GETARLQSFVGAIAVADLVKTTLGPKGMDKILQPMSEGPrsgnvTVTNDGATILKSVWL----DNPAAKILVDISKTQDE 95
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1055296569 84 TAGDGTTTATVLAQAIVTEGLKSVAAGFNPMDLKRGIDKAVAAA 127
Cdd:PTZ00212 96 EVGDGTTSVVVLAGELLREAEKLLDQKIHPQTIIEGWRMALDVA 139
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
382-514 |
1.17e-04 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 44.63 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 382 GAATEVeMKEKKARVEDALHATRAAVEEG-VVPGGG---TALIRAIQ--AISVKGDNEDQNHGIAAALRAMEMplrQIVT 455
Cdd:PTZ00212 379 GASTHI-LDEAERSLHDALCVLSQTVKDTrVVLGGGcseMLMANAVEelAKKVEGKKSLAIEAFAKALRQIPT---IIAD 454
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1055296569 456 NAGDEASVVVDKVK----QGEGNFGYNAGTGEYGDMLEMGILDPAKVTRSALQAAASIAGLMI 514
Cdd:PTZ00212 455 NGGYDSAELVSKLRaehyKGNKTAGIDMEKGTVGDMKELGITESYKVKLSQLCSATEAAEMIL 517
|
|
| chap_CCT_beta |
TIGR02341 |
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ... |
9-524 |
2.75e-04 |
|
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: 43.69 E-value: 2.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 9 GDDARQKMLSGVNILADAVKTTLGPKGRNVVLEKA--FGAPTVTKDGVSVAKEIELkdkfENMGAQMVKEVASKASDTAG 86
Cdd:TIGR02341 12 AENARLSSFVGAIAIGDLVKSTLGPKGMDKILQSSssDASIMVTNDGATILKSIGV----DNPAAKVLVDMSKVQDDEVG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 87 DGTTTATVLAQAIVTEGLKSVAAGFNPMDLKRGIDKAVAAAVDHIAGLATPCADSKSIAQVGTISANSDEHVGTIIAEAM 166
Cdd:TIGR02341 88 DGTTSVTVLAAELLREAEKLINQKIHPQTIIAGYREATKAARDALLKSAVDNGSDEVKFRQDLMNIARTTLSSKILSQHK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 167 D---KVGKEGVITVEEGQSLEN-ELDVVEGMQFDRGYLSPYFVTNQE---NMTAELDSPFILL------VDK-KISNIR- 231
Cdd:TIGR02341 168 DhfaQLAVDAVLRLKGSGNLEAiQIIKKLGGSLADSYLDEGFLLDKKigvNQPKRIENAKILIantgmdTDKvKIFGSRv 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 232 --DLLPLLEQVAKASKPLL------IIAEDVEGEALATLVVNSMRGIVKVAAVKAPGFGDRRKamLQDIAILTGGTVISe 303
Cdd:TIGR02341 248 rvDSTAKVAELEHAEKEKMkekvekILKHGINCFINRQLIYNYPEQLFADAGVMAIEHADFEG--VERLALVTGGEIVS- 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 304 evgleleatTLEHLGTAKRvtlskentvivdGAGDVadiearvkqiraqIEESSSDYDKEKLQERVAklAGGVAVIKVGA 383
Cdd:TIGR02341 325 ---------TFDHPELVKL------------GSCDL-------------IEEIMIGEDKLLKFSGVK--LGEACTIVLRG 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 384 ATEVEMKEKKARVEDALHATRAAVEEG-VVPGGGTALIRAIQAISVKGDNEDQNHGIA--AALRAMEMPLRQIVTNAGDE 460
Cdd:TIGR02341 369 ATQQILDEAERSLHDALCVLSQTVKESrTVLGGGCSEMLMSKAVTQEAQRTPGKEALAveAFARALRQLPTIIADNAGFD 448
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1055296569 461 ASVVVDKVK----QGEGNFGYNAGTGEYGDMLEMGILDPAKVTRSALQAAASIAGLMITTEAMVADIP 524
Cdd:TIGR02341 449 SAELVAQLRaahyNGNTTMGLDMNEGTIADMRQLGITESYKVKRAVVSSAAEAAEVILRVDNIIKAAP 516
|
|
| TCP1_epsilon |
cd03339 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ... |
10-142 |
9.70e-04 |
|
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: 41.90 E-value: 9.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 10 DDARQKMLSGV-----NIL-----ADAVKTTLGPKGRNVVLEKAFGAPTVTKDGVSVAKEIELkdkfENMGAQMVKEVAS 79
Cdd:cd03339 12 EQEKKKRLKGLeahksHILaaksvANILRTSLGPRGMDKILVSPDGEVTVTNDGATILEKMDV----DHQIAKLLVELSK 87
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1055296569 80 KASDTAGDGTTTATVLAQAIVTEGLKSVAAGFNPMDLKRGIDKAVAAAVDHIAGLATPCADSK 142
Cdd:cd03339 88 SQDDEIGDGTTGVVVLAGALLEQAEKLLDRGIHPIRIADGYEQACKIAVEHLEEIADKIEFSP 150
|
|
| chap_CCT_delta |
TIGR02342 |
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ... |
11-137 |
1.59e-03 |
|
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: 41.31 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055296569 11 DARQKMLSGVNILADAVKTTLGPKGRNVVLEKAFGAPTVTKDGVSVAKEIELKdkfeNMGAQMVKEVASKASDTAGDGTT 90
Cdd:TIGR02342 9 DVRTSNIVAAKAVADAIRTSLGPKGMDKMIQDGKGEVIITNDGATILKQMAVL----HPAAKMLVELSKAQDIEAGDGTT 84
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1055296569 91 TATVLAQAIVTEGLKSVAAGFNPMDLKRGIDKAVAAAVDHIAGLATP 137
Cdd:TIGR02342 85 SVVILAGALLGACERLLNKGIHPTIISESFQSAADEAIKILDEMSIP 131
|
|
| |
