|
Name |
Accession |
Description |
Interval |
E-value |
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
1-525 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 942.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 1 MAKEIIFDTRARQRILNGVNTLANAVRVTLGPKGRNVVIEKSFGAPLITKDGVTVAKEIELEDKFEDMGAKMVKEVASKT 80
Cdd:PRK00013 1 MAKDIKFGEDARRKLLRGVNKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDPFENMGAQLVKEVASKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 81 SDTAGDGTTTATVLAQAILREGTKLVTAGHNPMEIKRGIDKAVTAVVEELHKMATETSERGQIAQVGTISANNDESIGNL 160
Cdd:PRK00013 81 NDVAGDGTTTATVLAQAIVREGLKNVAAGANPMDLKRGIDKAVEAAVEELKKISKPVEDKEEIAQVATISANGDEEIGKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 161 IAEAMEKVGKEGVITVEEAKGLEDELEFVEGMQFDRGYLSPYFVTDAERMEATFDNPFILLFDKKVSSMKDLLPLLEQVh 240
Cdd:PRK00013 161 IAEAMEKVGKEGVITVEESKGFETELEVVEGMQFDRGYLSPYFVTDPEKMEAELENPYILITDKKISNIQDLLPVLEQV- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 241 GQGNRPLLIIAEDIDGEALATLVVNKLRGVLNVAAVKAPGFGDRRKAMLEDIAILTGGNVISEERGMKLEAATLQDLGTA 320
Cdd:PRK00013 240 AQSGKPLLIIAEDVEGEALATLVVNKLRGTLKVVAVKAPGFGDRRKAMLEDIAILTGGTVISEELGLKLEDATLEDLGQA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 321 GTVTITKDSTTIVGGQGTKDAITGRVNQIKAQIESTTSDYDREKLQERLAKLVGGVAVIKVGAQTEIEMKEKKARVEDAL 400
Cdd:PRK00013 320 KKVVVTKDNTTIVDGAGDKEAIKARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATEVEMKEKKDRVEDAL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 401 NATRAAVEEGIVPGGGVAVLRASKVLDGLE-LEREQAFGVDIVRRAAQEPIRQISANAGVEGSIVIQNVL-SKDGNYGYN 478
Cdd:PRK00013 400 HATRAAVEEGIVPGGGVALLRAAPALEALKgLNGDEATGINIVLRALEAPLRQIAENAGLEGSVVVEKVKnGKGKGYGYN 479
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1724166201 479 ARTDVYEDLVKAGVIDPVKVTRTALQNAASIAGLMLTTEAMIAEKPK 525
Cdd:PRK00013 480 AATGEYVDMIEAGIIDPTKVTRSALQNAASVAGLLLTTEAVVADKPE 526
|
|
| groEL |
PRK12849 |
chaperonin GroEL; Reviewed |
1-525 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237230 Cd Length: 542 Bit Score: 874.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 1 MAKEIIFDTRARQRILNGVNTLANAVRVTLGPKGRNVVIEKSFGAPLITKDGVTVAKEIELEDKFEDMGAKMVKEVASKT 80
Cdd:PRK12849 1 MAKIIKFDEEARRALERGVNKLADAVKVTLGPKGRNVVIDKSFGAPTITKDGVSIAKEIELEDPFENLGAQLVKEVASKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 81 SDTAGDGTTTATVLAQAILREGTKLVTAGHNPMEIKRGIDKAVTAVVEELHKMATETSERGQIAQVGTISANNDESIGNL 160
Cdd:PRK12849 81 NDVAGDGTTTATVLAQALVQEGLKNVAAGANPMDLKRGIDKAVEAVVEELKALARPVSGSEEIAQVATISANGDEEIGEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 161 IAEAMEKVGKEGVITVEEAKGLEDELEFVEGMQFDRGYLSPYFVTDAERMEATFDNPFILLFDKKVSSMKDLLPLLEQVh 240
Cdd:PRK12849 161 IAEAMEKVGKDGVITVEESKTLETELEVTEGMQFDRGYLSPYFVTDPERMEAVLEDPLILLTDKKISSLQDLLPLLEKV- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 241 GQGNRPLLIIAEDIDGEALATLVVNKLRGVLNVAAVKAPGFGDRRKAMLEDIAILTGGNVISEERGMKLEAATLQDLGTA 320
Cdd:PRK12849 240 AQSGKPLLIIAEDVEGEALATLVVNKLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGLKLEEVTLDDLGRA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 321 GTVTITKDSTTIVGGQGTKDAITGRVNQIKAQIESTTSDYDREKLQERLAKLVGGVAVIKVGAQTEIEMKEKKARVEDAL 400
Cdd:PRK12849 320 KRVTITKDNTTIVDGAGDKEAIEARVAQIRRQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATEVELKERKDRVEDAL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 401 NATRAAVEEGIVPGGGVAVLRASKVLDGLE-LEREQAFGVDIVRRAAQEPIRQISANAGVEGSIVIQNVLSKDGNYGYNA 479
Cdd:PRK12849 400 NATRAAVEEGIVPGGGVALLRAAKALDELAgLNGDQAAGVEIVRRALEAPLRQIAENAGLDGSVVVAKVLELEDGFGFNA 479
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1724166201 480 RTDVYEDLVKAGVIDPVKVTRTALQNAASIAGLMLTTEAMIAEKPK 525
Cdd:PRK12849 480 ATGEYGDLIAAGIIDPVKVTRSALQNAASVAGLLLTTEALVADKPE 525
|
|
| GroEL |
cd03344 |
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ... |
3-522 |
0e+00 |
|
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings, each composed of 7-9 subunits. The symmetry of type I is seven-fold and they are found in eubacteria (GroEL) and in organelles of eubacterial descent (hsp60 and RBP). With the aid of cochaperonin GroES, GroEL encapsulates non-native substrate proteins inside the cavity of the GroEL-ES complex and promotes folding by using energy derived from ATP hydrolysis.
Pssm-ID: 239460 Cd Length: 520 Bit Score: 869.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 3 KEIIFDTRARQRILNGVNTLANAVRVTLGPKGRNVVIEKSFGAPLITKDGVTVAKEIELEDKFEDMGAKMVKEVASKTSD 82
Cdd:cd03344 1 KDIKFGEEARKALLRGVNKLADAVKVTLGPKGRNVVIEKSFGSPKITKDGVTVAKEIELEDPFENMGAQLVKEVASKTND 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 83 TAGDGTTTATVLAQAILREGTKLVTAGHNPMEIKRGIDKAVTAVVEELHKMATETSERGQIAQVGTISANNDESIGNLIA 162
Cdd:cd03344 81 VAGDGTTTATVLARAIIKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKPVKTKEEIAQVATISANGDEEIGELIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 163 EAMEKVGKEGVITVEEAKGLEDELEFVEGMQFDRGYLSPYFVTDAERMEATFDNPFILLFDKKVSSMKDLLPLLEQVHgQ 242
Cdd:cd03344 161 EAMEKVGKDGVITVEEGKTLETELEVVEGMQFDRGYLSPYFVTDPEKMEVELENPYILLTDKKISSIQELLPILELVA-K 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 243 GNRPLLIIAEDIDGEALATLVVNKLRGVLNVAAVKAPGFGDRRKAMLEDIAILTGGNVISEERGMKLEAATLQDLGTAGT 322
Cdd:cd03344 240 AGRPLLIIAEDVEGEALATLVVNKLRGGLKVCAVKAPGFGDRRKAMLEDIAILTGGTVISEELGLKLEDVTLEDLGRAKK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 323 VTITKDSTTIVGGQGTKDAITGRVNQIKAQIESTTSDYDREKLQERLAKLVGGVAVIKVGAQTEIEMKEKKARVEDALNA 402
Cdd:cd03344 320 VVVTKDDTTIIGGAGDKAAIKARIAQIRKQIEETTSDYDKEKLQERLAKLSGGVAVIKVGGATEVELKEKKDRVEDALNA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 403 TRAAVEEGIVPGGGVAVLRASKVLDGLE-LEREQAFGVDIVRRAAQEPIRQISANAGVEGSIVIQNVLSKDGNYGYNART 481
Cdd:cd03344 400 TRAAVEEGIVPGGGVALLRASPALDKLKaLNGDEKLGIEIVRRALEAPLRQIAENAGVDGSVVVEKVLESPDGFGYDAAT 479
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1724166201 482 DVYEDLVKAGVIDPVKVTRTALQNAASIAGLMLTTEAMIAE 522
Cdd:cd03344 480 GEYVDMIEAGIIDPTKVVRSALQNAASVASLLLTTEALVVD 520
|
|
| GroEL |
TIGR02348 |
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ... |
2-525 |
0e+00 |
|
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES cytosolic chaperonin. It is found in bacteria, organelles derived from bacteria, and occasionally in the Archaea. The bacterial GroEL/GroES group I chaperonin is replaced a group II chaperonin, usually called the thermosome in the Archaeota and CCT (chaperone-containing TCP) in the Eukaryota. GroEL, thermosome subunits, and CCT subunits all fall under the scope of pfam00118. [Protein fate, Protein folding and stabilization]
Pssm-ID: 274089 Cd Length: 524 Bit Score: 850.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 2 AKEIIFDTRARQRILNGVNTLANAVRVTLGPKGRNVVIEKSFGAPLITKDGVTVAKEIELEDKFEDMGAKMVKEVASKTS 81
Cdd:TIGR02348 1 AKQIKFDEEARKALLRGVDKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDKFENMGAQLVKEVASKTN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 82 DTAGDGTTTATVLAQAILREGTKLVTAGHNPMEIKRGIDKAVTAVVEELHKMATETSERGQIAQVGTISANNDESIGNLI 161
Cdd:TIGR02348 81 DVAGDGTTTATVLAQAIVKEGLKNVAAGANPIELKRGIEKAVEAVVEELKKLSKPVKGKKEIAQVATISANNDEEIGSLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 162 AEAMEKVGKEGVITVEEAKGLEDELEFVEGMQFDRGYLSPYFVTDAERMEATFDNPFILLFDKKVSSMKDLLPLLEQVHG 241
Cdd:TIGR02348 161 AEAMEKVGKDGVITVEESKSLETELEVVEGMQFDRGYISPYFVTDAEKMEVELENPYILITDKKISNIKDLLPLLEKVAQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 242 QGnRPLLIIAEDIDGEALATLVVNKLRGVLNVAAVKAPGFGDRRKAMLEDIAILTGGNVISEERGMKLEAATLQDLGTAG 321
Cdd:TIGR02348 241 SG-KPLLIIAEDVEGEALATLVVNKLRGTLNVCAVKAPGFGDRRKAMLEDIAILTGGQVISEELGLKLEEVTLDDLGKAK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 322 TVTITKDSTTIVGGQGTKDAITGRVNQIKAQIESTTSDYDREKLQERLAKLVGGVAVIKVGAQTEIEMKEKKARVEDALN 401
Cdd:TIGR02348 320 KVTVDKDNTTIVEGAGDKAAIKARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATETEMKEKKLRIEDALN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 402 ATRAAVEEGIVPGGGVAVLRASKVLDGLELERE-QAFGVDIVRRAAQEPIRQISANAGVEGSIVIQNVLSKDGNYGYNAR 480
Cdd:TIGR02348 400 ATRAAVEEGIVPGGGVALLRAAAALEGLKGDGEdEAIGIDIVKRALEAPLRQIAENAGLDGAVVAEKVKELKGNFGFNAA 479
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1724166201 481 TDVYEDLVKAGVIDPVKVTRTALQNAASIAGLMLTTEAMIAEKPK 525
Cdd:TIGR02348 480 TGEYEDLVEAGIIDPTKVTRSALQNAASIAGLLLTTEAVVADKPE 524
|
|
| groEL |
PRK12850 |
chaperonin GroEL; Reviewed |
1-525 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237231 Cd Length: 544 Bit Score: 817.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 1 MAKEIIFDTRARQRILNGVNTLANAVRVTLGPKGRNVVIEKSFGAPLITKDGVTVAKEIELEDKFEDMGAKMVKEVASKT 80
Cdd:PRK12850 2 AAKEIRFSTDARDRLLRGVNILANAVKVTLGPKGRNVVLEKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVKEVASKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 81 SDTAGDGTTTATVLAQAILREGTKLVTAGHNPMEIKRGIDKAVTAVVEELHKMATETSERGQIAQVGTISANNDESIGNL 160
Cdd:PRK12850 82 NDLAGDGTTTATVLAQAIVREGAKLVAAGMNPMDLKRGIDLAVAAVVDELKKIAKKVTSSKEIAQVATISANGDESIGEM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 161 IAEAMEKVGKEGVITVEEAKGLEDELEFVEGMQFDRGYLSPYFVTDAERMEATFDNPFILLFDKKVSSMKDLLPLLEQVh 240
Cdd:PRK12850 162 IAEAMDKVGKEGVITVEEAKTLGTELDVVEGMQFDRGYLSPYFVTNPEKMRAELEDPYILLHEKKISNLQDLLPILEAV- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 241 GQGNRPLLIIAEDIDGEALATLVVNKLRGVLNVAAVKAPGFGDRRKAMLEDIAILTGGNVISEERGMKLEAATLQDLGTA 320
Cdd:PRK12850 241 VQSGRPLLIIAEDVEGEALATLVVNKLRGGLKSVAVKAPGFGDRRKAMLEDIAVLTGGQVISEDLGIKLENVTLDMLGRA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 321 GTVTITKDSTTIVGGQGTKDAITGRVNQIKAQIESTTSDYDREKLQERLAKLVGGVAVIKVGAQTEIEMKEKKARVEDAL 400
Cdd:PRK12850 321 KRVLITKENTTIIDGAGDKKNIEARVKQIRAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKEKKDRVDDAL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 401 NATRAAVEEGIVPGGGVAVLRASKVLDGLE-LEREQAFGVDIVRRAAQEPIRQISANAGVEGSIVIQNVLSKDGNYGYNA 479
Cdd:PRK12850 401 HATRAAVEEGIVPGGGVALLRARSALRGLKgANADETAGIDIVRRALEEPLRQIATNAGFEGSVVVGKVAELPGNFGFNA 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1724166201 480 RTDVYEDLVKAGVIDPVKVTRTALQNAASIAGLMLTTEAMIAEKPK 525
Cdd:PRK12850 481 QTGEYGDMVEAGIIDPAKVTRTALQDAASIAALLITTEAMVAEAPK 526
|
|
| groEL |
PRK12851 |
chaperonin GroEL; Reviewed |
1-525 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 171770 Cd Length: 541 Bit Score: 758.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 1 MAKEIIFDTRARQRILNGVNTLANAVRVTLGPKGRNVVIEKSFGAPLITKDGVTVAKEIELEDKFEDMGAKMVKEVASKT 80
Cdd:PRK12851 2 AAKEVKFHVEAREKMLRGVNILADAVKVTLGPKGRNVVIDKSFGAPTITNDGVTIAKEIELEDKFENMGAQMVREVASKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 81 SDTAGDGTTTATVLAQAILREGTKLVTAGHNPMEIKRGIDKAVTAVVEELHKMATETSERGQIAQVGTISANNDESIGNL 160
Cdd:PRK12851 82 NDVAGDGTTTATVLAQAIVREGAKAVAAGANPMDLKRGIDRAVAAVVEELKANARPVTTNAEIAQVATISANGDAEIGRL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 161 IAEAMEKVGKEGVITVEEAKGLEDELEFVEGMQFDRGYLSPYFVTDAERMEATFDNPFILLFDKKVSSMKDLLPLLEQVh 240
Cdd:PRK12851 162 VAEAMEKVGNEGVITVEESKTAETELEVVEGMQFDRGYLSPYFVTDADKMEAELEDPYILIHEKKISNLQDLLPVLEAV- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 241 GQGNRPLLIIAEDIDGEALATLVVNKLRGVLNVAAVKAPGFGDRRKAMLEDIAILTGGNVISEERGMKLEAATLQDLGTA 320
Cdd:PRK12851 241 VQSGKPLLIIAEDVEGEALATLVVNKLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGIKLENVTLEQLGRA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 321 GTVTITKDSTTIVGGQGTKDAITGRVNQIKAQIESTTSDYDREKLQERLAKLVGGVAVIKVGAQTEIEMKEKKARVEDAL 400
Cdd:PRK12851 321 KKVVVEKENTTIIDGAGSKTEIEGRVAQIRAQIEETTSDYDREKLQERLAKLAGGVAVIRVGASTEVEVKEKKDRVDDAL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 401 NATRAAVEEGIVPGGGVAVLRASKVLDGLE-LEREQAFGVDIVRRAAQEPIRQISANAGVEGSIVIQNVLSKDGNYGYNA 479
Cdd:PRK12851 401 HATRAAVEEGIVPGGGVALLRAVKALDKLEtANGDQRTGVEIVRRALEAPVRQIAENAGAEGSVVVGKLREKPGGYGFNA 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1724166201 480 RTDVYEDLVKAGVIDPVKVTRTALQNAASIAGLMLTTEAMIAEKPK 525
Cdd:PRK12851 481 ATNEYGDLYAQGVIDPVKVVRTALQNAASVAGLLLTTEAMVAEKPK 526
|
|
| GroEL |
COG0459 |
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ... |
1-525 |
0e+00 |
|
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227 Cd Length: 497 Bit Score: 751.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 1 MAKEIIFDTRARQRILNGVNTLANAVRVTLGPKGRNVVIEKSFGAPLITKDGVTVAKEIELEDKFEDMGAKMVKEVASKT 80
Cdd:COG0459 1 MAKQILFGEDARRANIRGVKALADAVKVTLGPKGRNVMLVKSFGDPTITNDGVTIAKEIELEDPFENMGAQLVKEVASKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 81 SDTAGDGTTTATVLAQAILREGTKLVTAGHNPMEIKRGIDKAVTAVVEELHKMATETSERGQIAQVGTISANNDESIGNL 160
Cdd:COG0459 81 NDEAGDGTTTATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPVDDKEELAQVATISANGDEEIGEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 161 IAEAMEKVGKEGVITVEEAKGLEDELEFVEGMQFDRGYLSPYFVTDAERMEATFDNPFILLFDKKVSSMKDLLPLLEQVH 240
Cdd:COG0459 161 IAEAMEKVGKDGVITVEEGKGLETELEVVEGMQFDKGYLSPYFVTDPEKMPAELENAYILLTDKKISSIQDLLPLLEKVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 241 GQGnRPLLIIAEDIDGEALATLVVNKLRGVLNVAAVKAPGFGDRRKAMLEDIAILTGGNVISEERGMKLEAATLQDLGTA 320
Cdd:COG0459 241 QSG-KPLLIIAEDIDGEALATLVVNGIRGVLRVVAVKAPGFGDRRKAMLEDIAILTGGRVISEDLGLKLEDVTLDDLGRA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 321 GTVTITKDSTTIVGGQGTKDAItgrvnqikaqiesttsdydreklqerlaklvggvaVIKVGAQTEIEMKEKKARVEDAL 400
Cdd:COG0459 320 KRVEVDKDNTTIVEGAGNPKAI-----------------------------------VILVGAATEVEVKERKRRVEDAL 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 401 NATRAAVEEGIVPGGGVAVLRASKVLDGL--ELEREQAFGVDIVRRAAQEPIRQISANAGVEGSIVIQNVLS-KDGNYGY 477
Cdd:COG0459 365 HATRAAVEEGIVPGGGAALLRAARALRELaaKLEGDEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKVRAaKDKGFGF 444
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1724166201 478 NARTDVYEDLVKAGVIDPVKVTRTALQNAASIAGLMLTTEAMIAEKPK 525
Cdd:COG0459 445 DAATGEYVDMLEAGVIDPAKVKRSALQNAASVAGLILTTEAVIADKPE 492
|
|
| groEL |
PRK12852 |
chaperonin GroEL; Reviewed |
1-525 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237232 Cd Length: 545 Bit Score: 739.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 1 MAKEIIFDTRARQRILNGVNTLANAVRVTLGPKGRNVVIEKSFGAPLITKDGVTVAKEIELEDKFEDMGAKMVKEVASKT 80
Cdd:PRK12852 2 AAKDVKFSGDARDRMLRGVDILANAVKVTLGPKGRNVVIEKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVREVASKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 81 SDTAGDGTTTATVLAQAILREGTKLVTAGHNPMEIKRGIDKAVTAVVEELHKMATETSERGQIAQVGTISANNDESIGNL 160
Cdd:PRK12852 82 NDLAGDGTTTATVLAQAIVREGAKAVAAGMNPMDLKRGIDIAVAAVVKDIEKRAKPVASSAEIAQVGTISANGDAAIGKM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 161 IAEAMEKVGKEGVITVEEAKGLEDELEFVEGMQFDRGYLSPYFVTDAERMEATFDNPFILLFDKKVSSMKDLLPLLEQVh 240
Cdd:PRK12852 162 IAQAMQKVGNEGVITVEENKSLETEVDIVEGMKFDRGYLSPYFVTNAEKMTVELDDAYILLHEKKLSGLQAMLPVLEAV- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 241 GQGNRPLLIIAEDIDGEALATLVVNKLRGVLNVAAVKAPGFGDRRKAMLEDIAILTGGNVISEERGMKLEAATLQDLGTA 320
Cdd:PRK12852 241 VQSGKPLLIIAEDVEGEALATLVVNRLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGQLISEDLGIKLENVTLKMLGRA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 321 GTVTITKDSTTIVGGQGTKDAITGRVNQIKAQIESTTSDYDREKLQERLAKLVGGVAVIKVGAQTEIEMKEKKARVEDAL 400
Cdd:PRK12852 321 KKVVIDKENTTIVNGAGKKADIEARVGQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKEKKDRVEDAL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 401 NATRAAVEEGIVPGGGVAVLRASKVLDGLELER-EQAFGVDIVRRAAQEPIRQISANAGVEGSIVIQNVLS-KDGNYGYN 478
Cdd:PRK12852 401 NATRAAVQEGIVPGGGVALLRAKKAVGRINNDNaDVQAGINIVLKALEAPIRQIAENAGVEGSIVVGKILEnKSETFGFD 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1724166201 479 ARTDVYEDLVKAGVIDPVKVTRTALQNAASIAGLMLTTEAMIAEKPK 525
Cdd:PRK12852 481 AQTEEYVDMVAKGIIDPAKVVRTALQDAASVAGLLVTTEAMVAELPK 527
|
|
| PTZ00114 |
PTZ00114 |
Heat shock protein 60; Provisional |
2-525 |
0e+00 |
|
Heat shock protein 60; Provisional
Pssm-ID: 185455 Cd Length: 555 Bit Score: 735.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 2 AKEIIFDTRARQRILNGVNTLANAVRVTLGPKGRNVVIEKSFGAPLITKDGVTVAKEIELEDKFEDMGAKMVKEVASKTS 81
Cdd:PTZ00114 14 GKEIRFGDEARQSLLKGIERLADAVAVTLGPKGRNVIIEQEYGSPKITKDGVTVAKAIEFSDRFENVGAQLIRQVASKTN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 82 DTAGDGTTTATVLAQAILREGTKLVTAGHNPMEIKRGIDKAVTAVVEELHKMATETSERGQIAQVGTISANNDESIGNLI 161
Cdd:PTZ00114 94 DKAGDGTTTATILARAIFREGCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQSRPVKTKEDILNVATISANGDVEIGSLI 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 162 AEAMEKVGKEGVITVEEAKGLEDELEFVEGMQFDRGYLSPYFVTDAERMEATFDNPFILLFDKKVSSMKDLLPLLEQVHg 241
Cdd:PTZ00114 174 ADAMDKVGKDGTITVEDGKTLEDELEVVEGMSFDRGYISPYFVTNEKTQKVELENPLILVTDKKISSIQSILPILEHAV- 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 242 QGNRPLLIIAEDIDGEALATLVVNKLRGVLNVAAVKAPGFGDRRKAMLEDIAILTGGNVISEER-GMKLEAATLQDLGTA 320
Cdd:PTZ00114 253 KNKRPLLIIAEDVEGEALQTLIINKLRGGLKVCAVKAPGFGDNRKDILQDIAVLTGATVVSEDNvGLKLDDFDPSMLGSA 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 321 GTVTITKDSTTIVGGQGTKDAITGRVNQIKAQIESTTSDYDREKLQERLAKLVGGVAVIKVGAQTEIEMKEKKARVEDAL 400
Cdd:PTZ00114 333 KKVTVTKDETVILTGGGDKAEIKERVELLRSQIERTTSEYDKEKLKERLAKLSGGVAVIKVGGASEVEVNEKKDRIEDAL 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 401 NATRAAVEEGIVPGGGVAVLRASKVLDGLE----LEREQAFGVDIVRRAAQEPIRQISANAGVEGSIVIQNVL-SKDGNY 475
Cdd:PTZ00114 413 NATRAAVEEGIVPGGGVALLRASKLLDKLEedneLTPDQRTGVKIVRNALRLPTKQIAENAGVEGAVVVEKILeKKDPSF 492
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1724166201 476 GYNARTDVYEDLVKAGVIDPVKVTRTALQNAASIAGLMLTTEAMIAEKPK 525
Cdd:PTZ00114 493 GYDAQTGEYVNMFEAGIIDPTKVVRSALVDAASVASLMLTTEAAIVDLPK 542
|
|
| groEL |
CHL00093 |
chaperonin GroEL |
1-525 |
0e+00 |
|
chaperonin GroEL
Pssm-ID: 177025 Cd Length: 529 Bit Score: 647.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 1 MAKEIIFDTRARQRILNGVNTLANAVRVTLGPKGRNVVIEKSFGAPLITKDGVTVAKEIELEDKFEDMGAKMVKEVASKT 80
Cdd:CHL00093 1 MSKKILYQDNARRALERGMDILAEAVSVTLGPKGRNVVLEKKYGSPQIVNDGVTIAKEIELEDHIENTGVALIRQAASKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 81 SDTAGDGTTTATVLAQAILREGTKLVTAGHNPMEIKRGIDKAVTAVVEELHKMATETSERGQIAQVGTISANNDESIGNL 160
Cdd:CHL00093 81 NDVAGDGTTTATVLAYAIVKQGMKNVAAGANPISLKRGIEKATQYVVSQIAEYARPVEDIQAITQVASISAGNDEEVGSM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 161 IAEAMEKVGKEGVITVEEAKGLEDELEFVEGMQFDRGYLSPYFVTDAERMEATFDNPFILLFDKKVSSMK-DLLPLLEQV 239
Cdd:CHL00093 161 IADAIEKVGREGVISLEEGKSTVTELEITEGMRFEKGFISPYFVTDTERMEVVQENPYILLTDKKITLVQqDLLPILEQV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 240 hGQGNRPLLIIAEDIDGEALATLVVNKLRGVLNVAAVKAPGFGDRRKAMLEDIAILTGGNVISEERGMKLEAATLQDLGT 319
Cdd:CHL00093 241 -TKTKRPLLIIAEDVEKEALATLVLNKLRGIVNVVAVRAPGFGDRRKAMLEDIAILTGGQVITEDAGLSLETIQLDLLGQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 320 AGTVTITKDSTTIVgGQGTKDAITGRVNQIKAQIESTTSDYDREKLQERLAKLVGGVAVIKVGAQTEIEMKEKKARVEDA 399
Cdd:CHL00093 320 ARRIIVTKDSTTII-ADGNEEQVKARCEQLRKQIEIADSSYEKEKLQERLAKLSGGVAVIKVGAATETEMKDKKLRLEDA 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 400 LNATRAAVEEGIVPGGGVAVLRASKVLDG---LELEREQAFGVDIVRRAAQEPIRQISANAGVEGSIVIQNVLSKDGNYG 476
Cdd:CHL00093 399 INATKAAVEEGIVPGGGATLVHLSENLKTwakNNLKEDELIGALIVARAILAPLKRIAENAGKNGSVIIEKVQEQDFEIG 478
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1724166201 477 YNARTDVYEDLVKAGVIDPVKVTRTALQNAASIAGLMLTTEAMIAEKPK 525
Cdd:CHL00093 479 YNAANNKFVNMYEAGIIDPAKVTRSALQNAASIASMILTTECIIVDKKE 527
|
|
| PRK14104 |
PRK14104 |
chaperonin GroEL; Provisional |
2-525 |
0e+00 |
|
chaperonin GroEL; Provisional
Pssm-ID: 172594 Cd Length: 546 Bit Score: 630.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 2 AKEIIFDTRARQRILNGVNTLANAVRVTLGPKGRNVVIEKSFGAPLITKDGVTVAKEIELEDKFEDMGAKMVKEVASKTS 81
Cdd:PRK14104 3 AKEVKFGVDARDRMLRGVDILANAVKVTLGPKGRNVVLDKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVREVASKSA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 82 DTAGDGTTTATVLAQAILREGTKLVTAGHNPMEIKRGIDKAVTAVVEELHKMATETSERGQIAQVGTISANNDESIGNLI 161
Cdd:PRK14104 83 DAAGDGTTTATVLAQAIVREGAKSVAAGMNPMDLKRGIDLAVEAVVADLVKNSKKVTSNDEIAQVGTISANGDAEIGKFL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 162 AEAMEKVGKEGVITVEEAKGLEDELEFVEGMQFDRGYLSPYFVTDAERMEATFDNPFILLFDKKVSSMKDLLPLLEQVhG 241
Cdd:PRK14104 163 ADAMKKVGNEGVITVEEAKSLETELDVVEGMQFDRGYISPYFVTNADKMRVEMDDAYILINEKKLSSLNELLPLLEAV-V 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 242 QGNRPLLIIAEDIDGEALATLVVNKLRGVLNVAAVKAPGFGDRRKAMLEDIAILTGGNVISEERGMKLEAATLQDLGTAG 321
Cdd:PRK14104 242 QTGKPLVIVAEDVEGEALATLVVNRLRGGLKVAAVKAPGFGDRRKAMLQDIAILTGGQAISEDLGIKLENVTLQMLGRAK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 322 TVTITKDSTTIVGGQGTKDAITGRVNQIKAQIESTTSDYDREKLQERLAKLVGGVAVIKVGAQTEIEMKEKKARVEDALN 401
Cdd:PRK14104 322 KVMIDKENTTIVNGAGKKADIEARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKERKDRVDDAMH 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 402 ATRAAVEEGIVPGGGVAVLRASKVLDGLELERE-QAFGVDIVRRAAQEPIRQISANAGVEGSIVIQNVLSKDG-NYGYNA 479
Cdd:PRK14104 402 ATRAAVEEGIVPGGGVALLRASEQLKGIKTKNDdQKTGVEIVRKALSAPARQIAINAGEDGSVIVGKILEKEQySYGFDS 481
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1724166201 480 RTDVYEDLVKAGVIDPVKVTRTALQNAASIAGLMLTTEAMIAEKPK 525
Cdd:PRK14104 482 QTGEYGNLVSKGIIDPTKVVRTAIQNAASVAALLITTEAMVAELPK 527
|
|
| PLN03167 |
PLN03167 |
Chaperonin-60 beta subunit; Provisional |
2-522 |
0e+00 |
|
Chaperonin-60 beta subunit; Provisional
Pssm-ID: 215611 [Multi-domain] Cd Length: 600 Bit Score: 560.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 2 AKEIIF--DTRARQRILNGVNTLANAVRVTLGPKGRNVVIEKSFGAPLITKDGVTVAKEIELEDKFEDMGAKMVKEVASK 79
Cdd:PLN03167 56 AKELHFnkDGSAIKKLQAGVNKLADLVGVTLGPKGRNVVLESKYGSPKIVNDGVTVAKEVELEDPVENIGAKLVRQAAAK 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 80 TSDTAGDGTTTATVLAQAILREGTKLVTAGHNPMEIKRGIDKAVTAVVEELHKMATETsERGQIAQVGTISANNDESIGN 159
Cdd:PLN03167 136 TNDLAGDGTTTSVVLAQGLIAEGVKVVAAGANPVQITRGIEKTAKALVKELKKMSKEV-EDSELADVAAVSAGNNYEVGN 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 160 LIAEAMEKVGKEGVITVEEAKGLEDELEFVEGMQFDRGYLSPYFVTDAERMEATFDNPFILLFDKKVSSMKDLLPLLEQV 239
Cdd:PLN03167 215 MIAEAMSKVGRKGVVTLEEGKSAENNLYVVEGMQFDRGYISPYFVTDSEKMSVEYDNCKLLLVDKKITNARDLIGILEDA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 240 HgQGNRPLLIIAEDIDGEALATLVVNKLRGVLNVAAVKAPGFGDRRKAMLEDIAILTGGNVISEERGMKLEAATLQDLGT 319
Cdd:PLN03167 295 I-RGGYPLLIIAEDIEQEALATLVVNKLRGSLKIAALKAPGFGERKSQYLDDIAILTGGTVIREEVGLSLDKVGKEVLGT 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 320 AGTVTITKDSTTIVGGQGTKDAITGRVNQIKAQIESTTSDYDREKLQERLAKLVGGVAVIKVGAQTEIEMKEKKARVEDA 399
Cdd:PLN03167 374 AAKVVLTKDTTTIVGDGSTQEAVNKRVAQIKNLIEAAEQDYEKEKLNERIAKLSGGVAVIQVGAQTETELKEKKLRVEDA 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 400 LNATRAAVEEGIVPGGGVAVLRASKVLDGLE--LER-EQAFGVDIVRRAAQEPIRQISANAGVEGSIVIQNVLSKDG-NY 475
Cdd:PLN03167 454 LNATKAAVEEGIVVGGGCTLLRLASKVDAIKdtLENdEQKVGADIVKRALSYPLKLIAKNAGVNGSVVSEKVLSNDNpKF 533
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1724166201 476 GYNARTDVYEDLVKAGVIDPVKVTRTALQNAASIAGLMLTTEAMIAE 522
Cdd:PLN03167 534 GYNAATGKYEDLMAAGIIDPTKVVRCCLEHAASVAKTFLTSDCVVVE 580
|
|
| chaperonin_type_I_II |
cd00309 |
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ... |
3-521 |
1.04e-141 |
|
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: 417.21 E-value: 1.04e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 3 KEIIFDTRARQRILNGVNTLANAVRVTLGPKGRNVVIEKSFGAPLITKDGVTVAKEIELEDkfedMGAKMVKEVASK--- 79
Cdd:cd00309 1 KEREFGEEARLSNINAAKALADAVKTTLGPKGMDKMLVDSLGDPTITNDGATILKEIEVEH----PAAKLLVEVAKSqdd 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 80 ------TSdtagdgtttATVLAQAILREGTKLVTAGHNPMEIKRGIDKAVTAVVEELHKMATETSE--RGQIAQVGTISA 151
Cdd:cd00309 77 evgdgtTT---------VVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVPIDVedREELLKVATTSL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 152 N------NDESIGNLIAEAMEKVGKE------GVITVEEAKG-LEDELEFVEGMQFDRGYLSPYfvtdaerMEATFDNPF 218
Cdd:cd00309 148 NsklvsgGDDFLGELVVDAVLKVGKEngdvdlGVIRVEKKKGgSLEDSELVVGMVFDKGYLSPY-------MPKRLENAK 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 219 ILLFDKKVSSmkdllplleqvhgqgnrplLIIAED-IDGEALATLVvnklrgVLNVAAVKApgfgdRRKAMLEDIAILTG 297
Cdd:cd00309 221 ILLLDCKLEY-------------------VVIAEKgIDDEALHYLA------KLGIMAVRR-----VRKEDLERIAKATG 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 298 GNVISEergmkLEAATLQDLGTAGTVTITK----DSTTIVGGQGtkdaitgrvnqikaqiesttsdydreklqerlaklv 373
Cdd:cd00309 271 ATIVSR-----LEDLTPEDLGTAGLVEETKigdeKYTFIEGCKG------------------------------------ 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 374 GGVAVIKVGAQTEIEMKEKKARVEDALNATRAAVEE-GIVPGGGVAVLRASKVLD--GLELEREQAFGVDIVRRAAQEPI 450
Cdd:cd00309 310 GKVATILLRGATEVELDEAERSLHDALCAVRAAVEDgGIVPGGGAAEIELSKALEelAKTLPGKEQLGIEAFADALEVIP 389
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1724166201 451 RQISANAGVEGSIVIQNVLSKDGNYGYNA----RTDVYEDLVKAGVIDPVKVTRTALQNAASIAGLMLTTEAMIA 521
Cdd:cd00309 390 RTLAENAGLDPIEVVTKLRAKHAEGGGNAggdvETGEIVDMKEAGIIDPLKVKRQALKSATEAASLILTIDDIIV 464
|
|
| Cpn60_TCP1 |
pfam00118 |
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ... |
22-523 |
1.50e-72 |
|
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: 239.41 E-value: 1.50e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 22 LANAVRVTLGPKGRNVVIEKSFGAPLITKDGVTVAKEIELEDKfedmGAKMVKEVASKTSDTAGDGTTTATVLAQAILRE 101
Cdd:pfam00118 1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELEIQHP----AAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 102 GTKLVTAGHNPMEIKRGIDKAVTAVVEELHKMATETSE---RGQIAQVGTISANND------ESIGNLIAEAMEKVGKE- 171
Cdd:pfam00118 77 AEKLLAAGVHPTTIIEGYEKALEKALEILDSIISIPVEdvdREDLLKVARTSLSSKiisresDFLAKLVVDAVLAIPKNd 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 172 --------GVITVEEakGLEDELEFVEGMQFDRGYLSPyfvtdaeRMEATFDNPFILLFDKKVSSMKD------------ 231
Cdd:pfam00118 157 gsfdlgniGVVKILG--GSLEDSELVDGVVLDKGPLHP-------DMPKRLENAKVLLLNCSLEYEKTetkatvvlsdae 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 232 ------------LLPLLEQVHGQGnRPLLIIAEDIDGEALATLVVNKLRGVLNVaavkapgfgdrRKAMLEDIAILTGGN 299
Cdd:pfam00118 228 qlerflkaeeeqILEIVEKIIDSG-VNVVVCQKGIDDLALHFLAKNGIMALRRV-----------KKRDLERLAKATGAR 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 300 VISeergmKLEAATLQDLGTAGTV---TITKDSTTIVggQGTKDaitgrvnqikaqiesttsdydreklqerlaklvGGV 376
Cdd:pfam00118 296 AVS-----SLDDLTPDDLGTAGKVeeeKIGDEKYTFI--EGCKS---------------------------------PKA 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 377 AVIKVGAQTEIEMKEKKARVEDALNATRAAVEE-GIVPGGGVAVLRASKVLD--GLELEREQAFGVDIVRRAAQEPIRQI 453
Cdd:pfam00118 336 ATILLRGATDHVLDEIERSIHDALCVVKNAIEDpRVVPGGGAVEMELARALReyAKSVSGKEQLAIEAFAEALEVIPKTL 415
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1724166201 454 SANAGVEGSIVIQNVLSK----DGNYGYNARTDVYEDLVKAGVIDPVKVTRTALQNAASIAGLMLTTEAMIAEK 523
Cdd:pfam00118 416 AENAGLDPIEVLAELRAAhasgEKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKSATEAASTILRIDDIIKAK 489
|
|
| chaperonin_like |
cd03333 |
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ... |
140-409 |
8.03e-44 |
|
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: 154.55 E-value: 8.03e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 140 RGQIAQVGTISAN-----NDESIGNLIAEAMEKVGKE------GVITVEEAKG---LEDELefVEGMQFDRGYLSPYfvt 205
Cdd:cd03333 1 RELLLQVATTSLNsklssWDDFLGKLVVDAVLKVGPDnrmddlGVIKVEKIPGgslEDSEL--VVGVVFDKGYASPY--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 206 daerMEATFDNPFILLFDKKVSSmkdllplleqvhgqgnrplLIIAED-IDGEALATLVVnklrgvLNVAAVKApgfgdR 284
Cdd:cd03333 76 ----MPKRLENAKILLLDCPLEY-------------------VVIAEKgIDDLALHYLAK------AGIMAVRR-----V 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 285 RKAMLEDIAILTGGNVISEergmkLEAATLQDLGTAGTVTITKDS----TTIVGGQGtkdaitgrvnqikaqiesttsdy 360
Cdd:cd03333 122 KKEDLERIARATGATIVSS-----LEDLTPEDLGTAELVEETKIGeeklTFIEGCKG----------------------- 173
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1724166201 361 dreklqerlaklvGGVAVIKVGAQTEIEMKEKKARVEDALNATRAAVEE 409
Cdd:cd03333 174 -------------GKAATILLRGATEVELDEVKRSLHDALCAVRAAVEE 209
|
|
| cpn60 |
cd03343 |
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ... |
21-523 |
8.88e-19 |
|
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: 89.63 E-value: 8.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 21 TLANAVRVTLGPKGRNVVIEKSFGAPLITKDGVTVAKEIELEDKfedmGAKMVKEVASKTSDTAGDGTTTATVLAQAILR 100
Cdd:cd03343 26 AVAEAVRTTLGPKGMDKMLVDSLGDVTITNDGATILKEMDIEHP----AAKMLVEVAKTQDEEVGDGTTTAVVLAGELLE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 101 EGTKLVTAGHNPMEIKRGIDKAVTAVVEELHKMATETSER--------GQIAQVGTISANNDESIGNLIAEAMEKVGKEG 172
Cdd:cd03343 102 KAEDLLDQNIHPTVIIEGYRLAAEKALELLDEIAIKVDPDdkdtlrkiAKTSLTGKGAEAAKDKLADLVVDAVLQVAEKR 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 173 ---------VITVEEAKGLE-DELEFVEGMQFDRGYLSPyfvtdaeRMEATFDNPFILLFDK-------------KVSSM 229
Cdd:cd03343 182 dgkyvvdldNIKIEKKTGGSvDDTELIRGIVIDKEVVHP-------GMPKRVENAKIALLDAplevkkteidakiRITSP 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 230 KDLLPLLEqvhgQGNRPLLIIAEDIdGEALATLVVNKlRGVLNVAA---VKAPGFGDRR--KAMLEDIAILTGGNVISee 304
Cdd:cd03343 255 DQLQAFLE----QEEAMLKEMVDKI-ADTGANVVFCQ-KGIDDLAQhylAKAGILAVRRvkKSDMEKLARATGAKIVT-- 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 305 rgmKLEAATLQDLGTAGTVTITK---DSTTIVGGQGTKDAITgrvnqikaqiesttsdydreklqerlaklvggvavIKV 381
Cdd:cd03343 327 ---NIDDLTPEDLGEAELVEERKvgdDKMVFVEGCKNPKAVT-----------------------------------ILL 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 382 GAQTEIEMKEKKARVEDALNATRAAVEEG-IVPGGGVAVLRASKVLDGLELE---REQaFGVDIVRRAAQEPIRQISANA 457
Cdd:cd03343 369 RGGTEHVVDELERALEDALRVVADALEDGkVVAGGGAVEIELAKRLREYARSvggREQ-LAVEAFADALEEIPRTLAENA 447
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 458 GVEGSIVIQNVLSK----DGNYGYNARTDVYEDLVKAGVIDPVKVTRTALQNAASIAGLMLTTEAMIAEK 523
Cdd:cd03343 448 GLDPIDTLVELRAAhekgNKNAGLDVYTGEVVDMLEKGVIEPLRVKKQAIKSATEAATMILRIDDVIAAK 517
|
|
| thermosome_alpha |
NF041082 |
thermosome subunit alpha; |
21-523 |
1.64e-16 |
|
thermosome subunit alpha;
Pssm-ID: 469009 Cd Length: 518 Bit Score: 82.24 E-value: 1.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 21 TLANAVRVTLGPKGRNVVIEKSFGAPLITKDGVTVAKEIELEDKfedmGAKMVKEVASKTSDTAGDGTTTATVLAQAILR 100
Cdd:NF041082 28 AVAEAVRTTLGPKGMDKMLVDSLGDVVITNDGVTILKEMDIEHP----AAKMIVEVAKTQDDEVGDGTTTAVVLAGELLK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 101 EGTKLVTAGHNPMEIKRGIDKAVTAVVEELHKMAT--ETSERGQIAQVG--TISANNDESIGNLIAE--------AMEKV 168
Cdd:NF041082 104 KAEELLDQDIHPTIIAEGYRLAAEKALEILDEIAIkvDPDDKETLKKIAatAMTGKGAEAAKDKLADlvvdavkaVAEKD 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 169 GKEGV----ITVEEAKGLE-DELEFVEGMQFDRGYLSPyfvtdaeRMEATFDNPFILLFD-----KK--------VSSMK 230
Cdd:NF041082 184 GGYNVdldnIKVEKKVGGSiEDSELVEGVVIDKERVHP-------GMPKRVENAKIALLDaplevKKteidakisITDPD 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 231 DLLPLLEQVHGQgnrpLLIIAEDIdGEALATLVVNKlRGVLNVAA---VKAPGFGDRR--KAMLEDIAILTGGNVISeer 305
Cdd:NF041082 257 QLQAFLDQEEKM----LKEMVDKI-ADSGANVVFCQ-KGIDDLAQhylAKEGILAVRRvkKSDMEKLAKATGARIVT--- 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 306 gmKLEAATLQDLGTAGTVT---ITKDSTTIVggQGTKDAitgrvnqiKAqiesttsdydreklqerlaklvggVAVIKVG 382
Cdd:NF041082 328 --SIDDLSPEDLGYAGLVEerkVGGDKMIFV--EGCKNP--------KA------------------------VTILLRG 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 383 AqTEIEMKEKKARVEDALNATRAAVEEG-IVPGGGVA----VLRASKVLDGLElEREQ----AFGvdivrrAAQEPI-RQ 452
Cdd:NF041082 372 G-TEHVVDEVERALEDALRVVRVVLEDGkVVAGGGAPevelALRLREYAASVG-GREQlaieAFA------EALEIIpRT 443
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1724166201 453 ISANAGVEGSIVIQNVLSK----DGNYGYNARTDVYEDLVKAGVIDPVKVTRTALQNAASIAGLMLTTEAMIAEK 523
Cdd:NF041082 444 LAENAGLDPIDALVELRSAhekgNKTAGLDVYTGKVVDMLEIGVVEPLRVKTQAIKSATEAAVMILRIDDVIAAA 518
|
|
| thermosome_beta |
NF041083 |
thermosome subunit beta; |
22-523 |
1.28e-14 |
|
thermosome subunit beta;
Pssm-ID: 469010 Cd Length: 519 Bit Score: 76.53 E-value: 1.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 22 LANAVRVTLGPKGRNVVIEKSFGAPLITKDGVTVAKEIELEDKfedmGAKMVKEVASKTSDTAGDGTTTATVLAQAILRE 101
Cdd:NF041083 29 VAEAVRTTLGPKGMDKMLVDSLGDIVITNDGATILKEMDVQHP----AAKMLVEVAKTQDDEVGDGTTTAVVLAGELLKK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 102 GTKLVTAGHNPMEIKRGIDKAVTAVVEELHKMATETS--ERGQIAQV------GTISANNDESIGNLIAEAMEKV----- 168
Cdd:NF041083 105 AEELLDQNIHPTIIANGYRLAAEKAIEILDEIAEKVDpdDRETLKKIaetsltSKGVEEARDYLAEIAVKAVKQVaekrd 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 169 GKEGV----ITVEEAKGLE-DELEFVEGMQFDRGYLSPyfvtdaeRMEATFDNPFILLFD-----KKV-----------S 227
Cdd:NF041083 185 GKYYVdldnIQIEKKHGGSiEDTQLIYGIVIDKEVVHP-------GMPKRVENAKIALLDaplevKKTeidaeiritdpD 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 228 SMKDLLPLLEQvhgqgnrpllIIAEDIDG-EALATLVVNKLRGVLNVAA---VKAPGFGDRR--KAMLEDIAILTGGNVI 301
Cdd:NF041083 258 QLQKFLDQEEK----------MLKEMVDKiKATGANVVFCQKGIDDLAQhylAKAGILAVRRvkKSDMEKLAKATGARIV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 302 SeergmKLEAATLQDLGTAGTVT---ITKDSTTIVGGQGTKDAITgrvnqikaqiesttsdydreklqerlaklvggvav 378
Cdd:NF041083 328 T-----NIDDLTPEDLGYAELVEerkVGDDKMVFVEGCKNPKAVT----------------------------------- 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 379 IKVGAQTEIEMKEKKARVEDALNATRAAVEEG-IVPGGGVAVLRASKVLDGLELE---REQaFGVDIVRRAAQEPIRQIS 454
Cdd:NF041083 368 ILIRGGTEHVVDEAERALEDALSVVADAVEDGkIVAGGGAPEVELAKRLREYAATvggREQ-LAVEAFAEALEIIPRTLA 446
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1724166201 455 ANAGVEGSIVIQNVLS--KDGN--YGYNARTDVYEDLVKAGVIDPVKVTRTALQNAASIAGLMLTTEAMIAEK 523
Cdd:NF041083 447 ENAGLDPIDILVKLRSahEKGKkwAGINVFTGEVVDMWELGVIEPLRVKTQAIKSATEAATMILRIDDVIAAK 519
|
|
| chap_CCT_eta |
TIGR02345 |
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ... |
16-520 |
1.61e-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: 66.71 E-value: 1.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 16 LNGVNTLANAVRVTLGPKGRNVVIEKSFGAPLITKDGVTVAKEIELEDKfedmGAKMVKEVASKTSDTAGDGTTTATVLA 95
Cdd:TIGR02345 24 INACVAIAEALKTTLGPRGMDKLIVGSNGKATISNDGATILKLLDIVHP----AAKTLVDIAKSQDAEVGDGTTSVTILA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 96 QAILREGTKLVTAGHNPMEIKRGIDKAVTAVVEELHKMATETSERG--------QIAQVGTIS---ANNDESIGNLIAEA 164
Cdd:TIGR02345 100 GELLKEAKPFIEEGVHPQLIIRCYREALSLAVEKIKEIAVTIDEEKgeqrelleKCAATALSSkliSHNKEFFSKMIVDA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 165 MEKVGKE----GVITVEEAKG--LEDELeFVEGMQFDRGYLSPYFvtdaERMEATFDNPFILL--FDKKVSSMKDLLPLl 236
Cdd:TIGR02345 180 VLSLDRDdldlKLIGIKKVQGgaLEDSQ-LVNGVAFKKTFSYAGF----EQQPKKFANPKILLlnVELELKAEKDNAEI- 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 237 eQVHGQGNRPLLIIAEdidgealATLVVNKLRGVL----NVAAVKAPgFGDRRKAMLEDIAILTGGNVISEERGMKLEAa 312
Cdd:TIGR02345 254 -RVEDVEDYQAIVDAE-------WAIIFRKLEKIVesgaNVVLSKLP-IGDLATQYFADRDIFCAGRVSAEDLKRVIKA- 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 313 tlqdlgTAGTVtitkdsttivggQGTKDAITGRVNQIKAQIESTTSDYDREKLQERLAKLVGGVAVIKVGAQTEIEMKEK 392
Cdd:TIGR02345 324 ------CGGSI------------QSTTSDLEADVLGTCALFEERQIGSERYNYFTGCPHAKTCTIILRGGAEQFIEEAER 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 393 KarVEDALNATRAAVE-EGIVPGGGVAVLRASKVLD--GLELEREQAFGVDIVRRAAQEPIRQISANAGVEGSIVIQNVL 469
Cdd:TIGR02345 386 S--LHDAIMIVRRALKnKKIVAGGGAIEMELSKCLRdySKTIDGKQQLIINAFAKALEIIPRQLCENAGFDSIEILNKLR 463
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1724166201 470 SK----DGNYGYNARTDVYEDLVKAGVIDPVKVTRTALQNAASIAGLMLTTEAMI 520
Cdd:TIGR02345 464 SRhakgGKWYGVDINTEDIGDNFEAFVWEPALVKINALKAAFEAACTILSVDETI 518
|
|
| chap_CCT_epsi |
TIGR02343 |
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ... |
19-138 |
2.31e-07 |
|
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: 53.65 E-value: 2.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 19 VNTLANAVRVTLGPKGRNVVIEKSFGAPLITKDGVTVAKEIELEDKFedmgAKMVKEVASKTSDTAGDGTTTATVLAQAI 98
Cdd:TIGR02343 36 AKSVASILRTSLGPKGMDKMLISPDGDITVTNDGATILSQMDVDNQI----AKLMVELSKSQDDEIGDGTTGVVVLAGAL 111
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1724166201 99 LREGTKLVTAGHNPMEIKRGIDKAVTAVVEELHKMATETS 138
Cdd:TIGR02343 112 LEQAEELLDKGIHPIKIADGFEEAARIAVEHLEEISDEIS 151
|
|
| chap_CCT_delta |
TIGR02342 |
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ... |
22-152 |
7.23e-07 |
|
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: 51.71 E-value: 7.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 22 LANAVRVTLGPKGRNVVIEKSFGAPLITKDGVTVAKEIELEDKfedmGAKMVKEVASKTSDTAGDGTTTATVLAQAILRE 101
Cdd:TIGR02342 21 VADAIRTSLGPKGMDKMIQDGKGEVIITNDGATILKQMAVLHP----AAKMLVELSKAQDIEAGDGTTSVVILAGALLGA 96
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1724166201 102 GTKLVTAGHNPMEIKRGIDKAVTAVVEELHKMAT--ETSERGQIAQVGTISAN 152
Cdd:TIGR02342 97 CERLLNKGIHPTIISESFQSAADEAIKILDEMSIpvDLSDREQLLKSATTSLS 149
|
|
| TCP1_delta |
cd03338 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ... |
22-196 |
1.39e-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: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 22 LANAVRVTLGPKGRNVVIEKSFGAPLITKDGVTVAKEIELEDKfedmGAKMVKEVASKTSDTAGDGTTTATVLAQAILRE 101
Cdd:cd03338 20 VADAIRTSLGPRGMDKMIQTGKGEVIITNDGATILKQMSVLHP----AAKMLVELSKAQDIEAGDGTTSVVVLAGALLSA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 102 GTKLVTAGHNPMEIKRGIDKAVTAVVEELHKMAT--ETSERGQIAQVGTISAN------NDESIGNLIAEAMEKVGKEGV 173
Cdd:cd03338 96 CESLLKKGIHPTVISESFQIAAKKAVEILDSMSIpvDLNDRESLIKSATTSLNskvvsqYSSLLAPIAVDAVLKVIDPAT 175
|
170 180 190
....*....|....*....|....*....|..
gi 1724166201 174 IT---------VEEAKGLEDELEFVEGMQFDR 196
Cdd:cd03338 176 ATnvdlkdiriVKKLGGTIEDTELVDGLVFTQ 207
|
|
| TCP1_eta |
cd03340 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ... |
16-139 |
2.58e-06 |
|
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: 49.98 E-value: 2.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 16 LNGVNTLANAVRVTLGPKGRNVVIEKSFGAPLITKDGVTVAKEIELEDKfedmGAKMVKEVASKTSDTAGDGTTTATVLA 95
Cdd:cd03340 22 INACQAIADAVRTTLGPRGMDKLIVDGRGKVTISNDGATILKLLDIVHP----AAKTLVDIAKSQDAEVGDGTTSVVVLA 97
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1724166201 96 QAILREGTKLVTAGHNPMEIKRGIDKAVTAVVEELHKMATETSE 139
Cdd:cd03340 98 GEFLKEAKPFIEDGVHPQIIIRGYRKALQLAIEKIKEIAVNIDK 141
|
|
| chap_CCT_theta |
TIGR02346 |
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ... |
22-196 |
1.16e-05 |
|
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: 48.17 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 22 LANAVRVTLGPKGRNVVIEKSFGAPLITKDGVTVAKEIELEDKfedmGAKMVKEVASKTSDTAGDGTTTATVLAQAILRE 101
Cdd:TIGR02346 30 LSQITRTSLGPNGMNKMVINHLEKLFVTNDAATILRELEVQHP----AAKLLVMASEMQENEIGDGTNLVLVLAGELLNK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 102 GTKLVTAGHNPMEIKRGIDKAVTAVVEELHKM----ATETSERGQI-----AQVGTISANNDESIGNLIAEAM-----EK 167
Cdd:TIGR02346 106 AEELIRMGLHPSEIIKGYEMALKKAMEILEELvvweVKDLRDKDELikalkASISSKQYGNEDFLAQLVAQACstvlpKN 185
|
170 180 190
....*....|....*....|....*....|...
gi 1724166201 168 VGKEGVITVEEAK----GLEDElEFVEGMQFDR 196
Cdd:TIGR02346 186 PQNFNVDNIRVCKilggSLSNS-EVLKGMVFNR 217
|
|
| TCP1_epsilon |
cd03339 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ... |
21-169 |
3.43e-05 |
|
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: 46.52 E-value: 3.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 21 TLANAVRVTLGPKGRNVVIEKSFGAPLITKDGVTVAKEIELEDKFedmgAKMVKEVASKTSDTAGDGTTTATVLAQAILR 100
Cdd:cd03339 34 SVANILRTSLGPRGMDKILVSPDGEVTVTNDGATILEKMDVDHQI----AKLLVELSKSQDDEIGDGTTGVVVLAGALLE 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1724166201 101 EGTKLVTAGHNPMEIKRGIDKAVTAVVEELHKMATETSergqiaqvgtISANNDEsigNLIAEAMEKVG 169
Cdd:cd03339 110 QAEKLLDRGIHPIRIADGYEQACKIAVEHLEEIADKIE----------FSPDNKE---PLIQTAMTSLG 165
|
|
| TCP1_beta |
cd03336 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ... |
10-139 |
1.82e-04 |
|
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: 44.24 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 10 RARQRILNGVNTLANAVRVTLGPKGRNVVIE--KSFGAPLITKDGVTVAKEIELEDKfedmGAKMVKEVASKTSDTAGDG 87
Cdd:cd03336 13 TARLSSFVGAIAIGDLVKTTLGPKGMDKILQsvGRSGGVTVTNDGATILKSIGVDNP----AAKVLVDISKVQDDEVGDG 88
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1724166201 88 TTTATVLAQAILREGTKLVTAGHNPMEIKRGIDKAVTAVVEELHKMATETSE 139
Cdd:cd03336 89 TTSVTVLAAELLREAEKLVAQKIHPQTIIEGYRMATAAAREALLSSAVDHSS 140
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
10-138 |
1.85e-04 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 44.25 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 10 RARQRILNGVNTLANAVRVTLGPKGRNVVIEKSFGAP-----LITKDGVTVAKEIELEDKfedmGAKMVKEVASKTSDTA 84
Cdd:PTZ00212 22 TARLQSFVGAIAVADLVKTTLGPKGMDKILQPMSEGPrsgnvTVTNDGATILKSVWLDNP----AAKILVDISKTQDEEV 97
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1724166201 85 GDGTTTATVLAQAILREGTKLVTAGHNPMEIKRGIDKAVTAVVEELHKMATETS 138
Cdd:PTZ00212 98 GDGTTSVVVLAGELLREAEKLLDQKIHPQTIIEGWRMALDVARKALEEIAFDHG 151
|
|
| TCP1_theta |
cd03341 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ... |
11-139 |
9.09e-04 |
|
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: 41.82 E-value: 9.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 11 ARQRILNGVNTLANAVRVTLGPKGRN--VV--IEKSFgaplITKDGVTVAKEIEledkFEDMGAKMVKEVASKTSDTAGD 86
Cdd:cd03341 9 AVLRNIEACKELSQITRTSYGPNGMNkmVInhLEKLF----VTSDAATILRELE----VQHPAAKLLVMASQMQEEEIGD 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1724166201 87 GTTTATVLAQAILREGTKLVTAGHNPMEIKRGIDKAVTAVVEELHKMATETSE 139
Cdd:cd03341 81 GTNLVVVLAGELLEKAEELLRMGLHPSEIIEGYEKALKKALEILEELVVYKIE 133
|
|
| chap_CCT_beta |
TIGR02341 |
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ... |
11-138 |
1.02e-03 |
|
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: 41.77 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 11 ARQRILNGVNTLANAVRVTLGPKGRNVVIEK--SFGAPLITKDGVTVAKEIELEDKfedmGAKMVKEVASKTSDTAGDGT 88
Cdd:TIGR02341 15 ARLSSFVGAIAIGDLVKSTLGPKGMDKILQSssSDASIMVTNDGATILKSIGVDNP----AAKVLVDMSKVQDDEVGDGT 90
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1724166201 89 TTATVLAQAILREGTKLVTAGHNPMEIKRGIDKAVTAVVEELHKMATETS 138
Cdd:TIGR02341 91 TSVTVLAAELLREAEKLINQKIHPQTIIAGYREATKAARDALLKSAVDNG 140
|
|
| chap_CCT_alpha |
TIGR02340 |
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ... |
22-142 |
4.01e-03 |
|
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: 40.09 E-value: 4.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724166201 22 LANAVRVTLGPKGRNVVIEKSFGAPLITKDGVTVAKEIELEDKfedmGAKMVKEVASKTSDTAGDGTTTATVLAQAILRE 101
Cdd:TIGR02340 24 IANIVKTSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHP----AAKILVELAQLQDREVGDGTTSVVIIAAELLKR 99
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1724166201 102 GTKLVTAGHNPMEIKRGIDKAVTAVVEELHK-MATETSERGQ 142
Cdd:TIGR02340 100 ADELVKNKIHPTSVISGYRLACKEAVKYIKEnLSVSVDELGR 141
|
|
| |
