|
Name |
Accession |
Description |
Interval |
E-value |
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
2-521 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 956.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 2 EARAKMLRGVNVLADAVKVSLGPKGRNVVLDKSFGAPIITKDGVSVAREIELQDKFENMGAQMVKEVASKANDASGDGTT 81
Cdd:PRK00013 10 DARRKLLRGVNKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDPFENMGAQLVKEVASKTNDVAGDGTT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 82 TATVLAQSIVNEGLKAVAAGMNPMDLKRGIDKAVIAAVEELRKLSSPCEDSKAIAQVGTISANSDETVGALIAEAMAKVG 161
Cdd:PRK00013 90 TATVLAQAIVREGLKNVAAGANPMDLKRGIDKAVEAAVEELKKISKPVEDKEEIAQVATISANGDEEIGKLIAEAMEKVG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 162 KEGVITVEEGSGLQDELDVVEGMQFDRGYLSPYFVNKAESGSVELDNPFILLIDKKISNIREMLPILEAVAKSSKPLLII 241
Cdd:PRK00013 170 KEGVITVEESKGFETELEVVEGMQFDRGYLSPYFVTDPEKMEAELENPYILITDKKISNIQDLLPVLEQVAQSGKPLLII 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 242 AEDVEGEALATLVVNNMRGIVKVAAVKAPGFGDRRKAMLQDIAVLTAGTVISEEIGLDLEKSTLKDMGQAKRVVITKDTT 321
Cdd:PRK00013 250 AEDVEGEALATLVVNKLRGTLKVVAVKAPGFGDRRKAMLEDIAILTGGTVISEELGLKLEDATLEDLGQAKKVVVTKDNT 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 322 TIIDGIGDKVSINNRVAQINQQRDEATSDYDREKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVEDALHATRAAVEEG 401
Cdd:PRK00013 330 TIVDGAGDKEAIKARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATEVEMKEKKDRVEDALHATRAAVEEG 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 402 VVAGGGVALIRAANSIRNIRGDNEDQNVGIKVACRAMEAPLRQIVDNAGEEPSVIANNVRASEG-NIGYNVVSEKYGNMI 480
Cdd:PRK00013 410 IVPGGGVALLRAAPALEALKGLNGDEATGINIVLRALEAPLRQIAENAGLEGSVVVEKVKNGKGkGYGYNAATGEYVDMI 489
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 383081607 481 EMGILDPTKVTRSALQYAASIAGLMITTECMITELAKEEKP 521
Cdd:PRK00013 490 EAGIIDPTKVTRSALQNAASVAGLLLTTEAVVADKPEKKAA 530
|
|
| groEL |
PRK12849 |
chaperonin GroEL; Reviewed |
2-521 |
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 383081607 2 EARAKMLRGVNVLADAVKVSLGPKGRNVVLDKSFGAPIITKDGVSVAREIELQDKFENMGAQMVKEVASKANDASGDGTT 81
Cdd:PRK12849 10 EARRALERGVNKLADAVKVTLGPKGRNVVIDKSFGAPTITKDGVSIAKEIELEDPFENLGAQLVKEVASKTNDVAGDGTT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 82 TATVLAQSIVNEGLKAVAAGMNPMDLKRGIDKAVIAAVEELRKLSSPCEDSKAIAQVGTISANSDETVGALIAEAMAKVG 161
Cdd:PRK12849 90 TATVLAQALVQEGLKNVAAGANPMDLKRGIDKAVEAVVEELKALARPVSGSEEIAQVATISANGDEEIGELIAEAMEKVG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 162 KEGVITVEEGSGLQDELDVVEGMQFDRGYLSPYFVNKAESGSVELDNPFILLIDKKISNIREMLPILEAVAKSSKPLLII 241
Cdd:PRK12849 170 KDGVITVEESKTLETELEVTEGMQFDRGYLSPYFVTDPERMEAVLEDPLILLTDKKISSLQDLLPLLEKVAQSGKPLLII 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 242 AEDVEGEALATLVVNNMRGIVKVAAVKAPGFGDRRKAMLQDIAVLTAGTVISEEIGLDLEKSTLKDMGQAKRVVITKDTT 321
Cdd:PRK12849 250 AEDVEGEALATLVVNKLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGLKLEEVTLDDLGRAKRVTITKDNT 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 322 TIIDGIGDKVSINNRVAQINQQRDEATSDYDREKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVEDALHATRAAVEEG 401
Cdd:PRK12849 330 TIVDGAGDKEAIEARVAQIRRQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATEVELKERKDRVEDALNATRAAVEEG 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 402 VVAGGGVALIRAANSIRNIRGDNEDQNVGIKVACRAMEAPLRQIVDNAGEEPSVIANNVRASEGNIGYNVVSEKYGNMIE 481
Cdd:PRK12849 410 IVPGGGVALLRAAKALDELAGLNGDQAAGVEIVRRALEAPLRQIAENAGLDGSVVVAKVLELEDGFGFNAATGEYGDLIA 489
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 383081607 482 MGILDPTKVTRSALQYAASIAGLMITTECMITELAKEEKP 521
Cdd:PRK12849 490 AGIIDPVKVTRSALQNAASVAGLLLTTEALVADKPEEEDP 529
|
|
| GroEL |
cd03344 |
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ... |
2-514 |
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: 871.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 2 EARAKMLRGVNVLADAVKVSLGPKGRNVVLDKSFGAPIITKDGVSVAREIELQDKFENMGAQMVKEVASKANDASGDGTT 81
Cdd:cd03344 8 EARKALLRGVNKLADAVKVTLGPKGRNVVIEKSFGSPKITKDGVTVAKEIELEDPFENMGAQLVKEVASKTNDVAGDGTT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 82 TATVLAQSIVNEGLKAVAAGMNPMDLKRGIDKAVIAAVEELRKLSSPCEDSKAIAQVGTISANSDETVGALIAEAMAKVG 161
Cdd:cd03344 88 TATVLARAIIKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKPVKTKEEIAQVATISANGDEEIGELIAEAMEKVG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 162 KEGVITVEEGSGLQDELDVVEGMQFDRGYLSPYFVNKAESGSVELDNPFILLIDKKISNIREMLPILEAVAKSSKPLLII 241
Cdd:cd03344 168 KDGVITVEEGKTLETELEVVEGMQFDRGYLSPYFVTDPEKMEVELENPYILLTDKKISSIQELLPILELVAKAGRPLLII 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 242 AEDVEGEALATLVVNNMRGIVKVAAVKAPGFGDRRKAMLQDIAVLTAGTVISEEIGLDLEKSTLKDMGQAKRVVITKDTT 321
Cdd:cd03344 248 AEDVEGEALATLVVNKLRGGLKVCAVKAPGFGDRRKAMLEDIAILTGGTVISEELGLKLEDVTLEDLGRAKKVVVTKDDT 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 322 TIIDGIGDKVSINNRVAQINQQRDEATSDYDREKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVEDALHATRAAVEEG 401
Cdd:cd03344 328 TIIGGAGDKAAIKARIAQIRKQIEETTSDYDKEKLQERLAKLSGGVAVIKVGGATEVELKEKKDRVEDALNATRAAVEEG 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 402 VVAGGGVALIRAANSIRNIRGDNEDQNVGIKVACRAMEAPLRQIVDNAGEEPSVIANNVRASEGNIGYNVVSEKYGNMIE 481
Cdd:cd03344 408 IVPGGGVALLRASPALDKLKALNGDEKLGIEIVRRALEAPLRQIAENAGVDGSVVVEKVLESPDGFGYDAATGEYVDMIE 487
|
490 500 510
....*....|....*....|....*....|...
gi 383081607 482 MGILDPTKVTRSALQYAASIAGLMITTECMITE 514
Cdd:cd03344 488 AGIIDPTKVVRSALQNAASVASLLLTTEALVVD 520
|
|
| GroEL |
TIGR02348 |
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ... |
2-515 |
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: 854.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 2 EARAKMLRGVNVLADAVKVSLGPKGRNVVLDKSFGAPIITKDGVSVAREIELQDKFENMGAQMVKEVASKANDASGDGTT 81
Cdd:TIGR02348 9 EARKALLRGVDKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDKFENMGAQLVKEVASKTNDVAGDGTT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 82 TATVLAQSIVNEGLKAVAAGMNPMDLKRGIDKAVIAAVEELRKLSSPCEDSKAIAQVGTISANSDETVGALIAEAMAKVG 161
Cdd:TIGR02348 89 TATVLAQAIVKEGLKNVAAGANPIELKRGIEKAVEAVVEELKKLSKPVKGKKEIAQVATISANNDEEIGSLIAEAMEKVG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 162 KEGVITVEEGSGLQDELDVVEGMQFDRGYLSPYFVNKAESGSVELDNPFILLIDKKISNIREMLPILEAVAKSSKPLLII 241
Cdd:TIGR02348 169 KDGVITVEESKSLETELEVVEGMQFDRGYISPYFVTDAEKMEVELENPYILITDKKISNIKDLLPLLEKVAQSGKPLLII 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 242 AEDVEGEALATLVVNNMRGIVKVAAVKAPGFGDRRKAMLQDIAVLTAGTVISEEIGLDLEKSTLKDMGQAKRVVITKDTT 321
Cdd:TIGR02348 249 AEDVEGEALATLVVNKLRGTLNVCAVKAPGFGDRRKAMLEDIAILTGGQVISEELGLKLEEVTLDDLGKAKKVTVDKDNT 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 322 TIIDGIGDKVSINNRVAQINQQRDEATSDYDREKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVEDALHATRAAVEEG 401
Cdd:TIGR02348 329 TIVEGAGDKAAIKARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATETEMKEKKLRIEDALNATRAAVEEG 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 402 VVAGGGVALIRAANSIRNIRGDNEDQNVGIKVACRAMEAPLRQIVDNAGEEPSVIANNVRASEGNIGYNVVSEKYGNMIE 481
Cdd:TIGR02348 409 IVPGGGVALLRAAAALEGLKGDGEDEAIGIDIVKRALEAPLRQIAENAGLDGAVVAEKVKELKGNFGFNAATGEYEDLVE 488
|
490 500 510
....*....|....*....|....*....|....
gi 383081607 482 MGILDPTKVTRSALQYAASIAGLMITTECMITEL 515
Cdd:TIGR02348 489 AGIIDPTKVTRSALQNAASIAGLLLTTEAVVADK 522
|
|
| groEL |
PRK12850 |
chaperonin GroEL; Reviewed |
1-521 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237231 Cd Length: 544 Bit Score: 818.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 1 SEARAKMLRGVNVLADAVKVSLGPKGRNVVLDKSFGAPIITKDGVSVAREIELQDKFENMGAQMVKEVASKANDASGDGT 80
Cdd:PRK12850 10 TDARDRLLRGVNILANAVKVTLGPKGRNVVLEKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVKEVASKTNDLAGDGT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 81 TTATVLAQSIVNEGLKAVAAGMNPMDLKRGIDKAVIAAVEELRKLSSPCEDSKAIAQVGTISANSDETVGALIAEAMAKV 160
Cdd:PRK12850 90 TTATVLAQAIVREGAKLVAAGMNPMDLKRGIDLAVAAVVDELKKIAKKVTSSKEIAQVATISANGDESIGEMIAEAMDKV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 161 GKEGVITVEEGSGLQDELDVVEGMQFDRGYLSPYFVNKAESGSVELDNPFILLIDKKISNIREMLPILEAVAKSSKPLLI 240
Cdd:PRK12850 170 GKEGVITVEEAKTLGTELDVVEGMQFDRGYLSPYFVTNPEKMRAELEDPYILLHEKKISNLQDLLPILEAVVQSGRPLLI 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 241 IAEDVEGEALATLVVNNMRGIVKVAAVKAPGFGDRRKAMLQDIAVLTAGTVISEEIGLDLEKSTLKDMGQAKRVVITKDT 320
Cdd:PRK12850 250 IAEDVEGEALATLVVNKLRGGLKSVAVKAPGFGDRRKAMLEDIAVLTGGQVISEDLGIKLENVTLDMLGRAKRVLITKEN 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 321 TTIIDGIGDKVSINNRVAQINQQRDEATSDYDREKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVEDALHATRAAVEE 400
Cdd:PRK12850 330 TTIIDGAGDKKNIEARVKQIRAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKEKKDRVDDALHATRAAVEE 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 401 GVVAGGGVALIRAANSIRNIRGDNEDQNVGIKVACRAMEAPLRQIVDNAGEEPSVIANNVRASEGNIGYNVVSEKYGNMI 480
Cdd:PRK12850 410 GIVPGGGVALLRARSALRGLKGANADETAGIDIVRRALEEPLRQIATNAGFEGSVVVGKVAELPGNFGFNAQTGEYGDMV 489
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 383081607 481 EMGILDPTKVTRSALQYAASIAGLMITTECMITELAKEEKP 521
Cdd:PRK12850 490 EAGIIDPAKVTRTALQDAASIAALLITTEAMVAEAPKKAAA 530
|
|
| groEL |
PRK12852 |
chaperonin GroEL; Reviewed |
1-521 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237232 Cd Length: 545 Bit Score: 752.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 1 SEARAKMLRGVNVLADAVKVSLGPKGRNVVLDKSFGAPIITKDGVSVAREIELQDKFENMGAQMVKEVASKANDASGDGT 80
Cdd:PRK12852 10 GDARDRMLRGVDILANAVKVTLGPKGRNVVIEKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVREVASKTNDLAGDGT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 81 TTATVLAQSIVNEGLKAVAAGMNPMDLKRGIDKAVIAAVEELRKLSSPCEDSKAIAQVGTISANSDETVGALIAEAMAKV 160
Cdd:PRK12852 90 TTATVLAQAIVREGAKAVAAGMNPMDLKRGIDIAVAAVVKDIEKRAKPVASSAEIAQVGTISANGDAAIGKMIAQAMQKV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 161 GKEGVITVEEGSGLQDELDVVEGMQFDRGYLSPYFVNKAESGSVELDNPFILLIDKKISNIREMLPILEAVAKSSKPLLI 240
Cdd:PRK12852 170 GNEGVITVEENKSLETEVDIVEGMKFDRGYLSPYFVTNAEKMTVELDDAYILLHEKKLSGLQAMLPVLEAVVQSGKPLLI 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 241 IAEDVEGEALATLVVNNMRGIVKVAAVKAPGFGDRRKAMLQDIAVLTAGTVISEEIGLDLEKSTLKDMGQAKRVVITKDT 320
Cdd:PRK12852 250 IAEDVEGEALATLVVNRLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGQLISEDLGIKLENVTLKMLGRAKKVVIDKEN 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 321 TTIIDGIGDKVSINNRVAQINQQRDEATSDYDREKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVEDALHATRAAVEE 400
Cdd:PRK12852 330 TTIVNGAGKKADIEARVGQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKEKKDRVEDALNATRAAVQE 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 401 GVVAGGGVALIRAANSIRNIRGDNEDQNVGIKVACRAMEAPLRQIVDNAGEEPSVIANNVRASEG-NIGYNVVSEKYGNM 479
Cdd:PRK12852 410 GIVPGGGVALLRAKKAVGRINNDNADVQAGINIVLKALEAPIRQIAENAGVEGSIVVGKILENKSeTFGFDAQTEEYVDM 489
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 383081607 480 IEMGILDPTKVTRSALQYAASIAGLMITTECMITELAKEEKP 521
Cdd:PRK12852 490 VAKGIIDPAKVVRTALQDAASVAGLLVTTEAMVAELPKKDAA 531
|
|
| GroEL |
COG0459 |
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ... |
2-521 |
0e+00 |
|
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227 Cd Length: 497 Bit Score: 751.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 2 EARAKMLRGVNVLADAVKVSLGPKGRNVVLDKSFGAPIITKDGVSVAREIELQDKFENMGAQMVKEVASKANDASGDGTT 81
Cdd:COG0459 10 DARRANIRGVKALADAVKVTLGPKGRNVMLVKSFGDPTITNDGVTIAKEIELEDPFENMGAQLVKEVASKTNDEAGDGTT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 82 TATVLAQSIVNEGLKAVAAGMNPMDLKRGIDKAVIAAVEELRKLSSPCEDSKAIAQVGTISANSDETVGALIAEAMAKVG 161
Cdd:COG0459 90 TATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPVDDKEELAQVATISANGDEEIGELIAEAMEKVG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 162 KEGVITVEEGSGLQDELDVVEGMQFDRGYLSPYFVNKAESGSVELDNPFILLIDKKISNIREMLPILEAVAKSSKPLLII 241
Cdd:COG0459 170 KDGVITVEEGKGLETELEVVEGMQFDKGYLSPYFVTDPEKMPAELENAYILLTDKKISSIQDLLPLLEKVAQSGKPLLII 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 242 AEDVEGEALATLVVNNMRGIVKVAAVKAPGFGDRRKAMLQDIAVLTAGTVISEEIGLDLEKSTLKDMGQAKRVVITKDTT 321
Cdd:COG0459 250 AEDIDGEALATLVVNGIRGVLRVVAVKAPGFGDRRKAMLEDIAILTGGRVISEDLGLKLEDVTLDDLGRAKRVEVDKDNT 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 322 TIIDGIGDKVSInnrvaqinqqrdeatsdydreklqervaklaggvaVIKVGAATEVEMKEKKARVEDALHATRAAVEEG 401
Cdd:COG0459 330 TIVEGAGNPKAI-----------------------------------VILVGAATEVEVKERKRRVEDALHATRAAVEEG 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 402 VVAGGGVALIRAANSIRNIRGDNE-DQNVGIKVACRAMEAPLRQIVDNAGEEPSVIANNVRASE-GNIGYNVVSEKYGNM 479
Cdd:COG0459 375 IVPGGGAALLRAARALRELAAKLEgDEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKVRAAKdKGFGFDAATGEYVDM 454
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 383081607 480 IEMGILDPTKVTRSALQYAASIAGLMITTECMITELAKEEKP 521
Cdd:COG0459 455 LEAGVIDPAKVKRSALQNAASVAGLILTTEAVIADKPEKEEA 496
|
|
| groEL |
PRK12851 |
chaperonin GroEL; Reviewed |
1-522 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 171770 Cd Length: 541 Bit Score: 751.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 1 SEARAKMLRGVNVLADAVKVSLGPKGRNVVLDKSFGAPIITKDGVSVAREIELQDKFENMGAQMVKEVASKANDASGDGT 80
Cdd:PRK12851 10 VEAREKMLRGVNILADAVKVTLGPKGRNVVIDKSFGAPTITNDGVTIAKEIELEDKFENMGAQMVREVASKTNDVAGDGT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 81 TTATVLAQSIVNEGLKAVAAGMNPMDLKRGIDKAVIAAVEELRKLSSPCEDSKAIAQVGTISANSDETVGALIAEAMAKV 160
Cdd:PRK12851 90 TTATVLAQAIVREGAKAVAAGANPMDLKRGIDRAVAAVVEELKANARPVTTNAEIAQVATISANGDAEIGRLVAEAMEKV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 161 GKEGVITVEEGSGLQDELDVVEGMQFDRGYLSPYFVNKAESGSVELDNPFILLIDKKISNIREMLPILEAVAKSSKPLLI 240
Cdd:PRK12851 170 GNEGVITVEESKTAETELEVVEGMQFDRGYLSPYFVTDADKMEAELEDPYILIHEKKISNLQDLLPVLEAVVQSGKPLLI 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 241 IAEDVEGEALATLVVNNMRGIVKVAAVKAPGFGDRRKAMLQDIAVLTAGTVISEEIGLDLEKSTLKDMGQAKRVVITKDT 320
Cdd:PRK12851 250 IAEDVEGEALATLVVNKLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGIKLENVTLEQLGRAKKVVVEKEN 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 321 TTIIDGIGDKVSINNRVAQINQQRDEATSDYDREKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVEDALHATRAAVEE 400
Cdd:PRK12851 330 TTIIDGAGSKTEIEGRVAQIRAQIEETTSDYDREKLQERLAKLAGGVAVIRVGASTEVEVKEKKDRVDDALHATRAAVEE 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 401 GVVAGGGVALIRAANSIRNIRGDNEDQNVGIKVACRAMEAPLRQIVDNAGEEPSVIANNVRASEGNIGYNVVSEKYGNMI 480
Cdd:PRK12851 410 GIVPGGGVALLRAVKALDKLETANGDQRTGVEIVRRALEAPVRQIAENAGAEGSVVVGKLREKPGGYGFNAATNEYGDLY 489
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 383081607 481 EMGILDPTKVTRSALQYAASIAGLMITTECMITELAKEEKPD 522
Cdd:PRK12851 490 AQGVIDPVKVVRTALQNAASVAGLLLTTEAMVAEKPKKEPAP 531
|
|
| PTZ00114 |
PTZ00114 |
Heat shock protein 60; Provisional |
2-521 |
0e+00 |
|
Heat shock protein 60; Provisional
Pssm-ID: 185455 Cd Length: 555 Bit Score: 718.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 2 EARAKMLRGVNVLADAVKVSLGPKGRNVVLDKSFGAPIITKDGVSVAREIELQDKFENMGAQMVKEVASKANDASGDGTT 81
Cdd:PTZ00114 22 EARQSLLKGIERLADAVAVTLGPKGRNVIIEQEYGSPKITKDGVTVAKAIEFSDRFENVGAQLIRQVASKTNDKAGDGTT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 82 TATVLAQSIVNEGLKAVAAGMNPMDLKRGIDKAVIAAVEELRKLSSPCEDSKAIAQVGTISANSDETVGALIAEAMAKVG 161
Cdd:PTZ00114 102 TATILARAIFREGCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQSRPVKTKEDILNVATISANGDVEIGSLIADAMDKVG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 162 KEGVITVEEGSGLQDELDVVEGMQFDRGYLSPYFVNKAESGSVELDNPFILLIDKKISNIREMLPILEAVAKSSKPLLII 241
Cdd:PTZ00114 182 KDGTITVEDGKTLEDELEVVEGMSFDRGYISPYFVTNEKTQKVELENPLILVTDKKISSIQSILPILEHAVKNKRPLLII 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 242 AEDVEGEALATLVVNNMRGIVKVAAVKAPGFGDRRKAMLQDIAVLTAGTVISEE-IGLDLEKSTLKDMGQAKRVVITKDT 320
Cdd:PTZ00114 262 AEDVEGEALQTLIINKLRGGLKVCAVKAPGFGDNRKDILQDIAVLTGATVVSEDnVGLKLDDFDPSMLGSAKKVTVTKDE 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 321 TTIIDGIGDKVSINNRVAQINQQRDEATSDYDREKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVEDALHATRAAVEE 400
Cdd:PTZ00114 342 TVILTGGGDKAEIKERVELLRSQIERTTSEYDKEKLKERLAKLSGGVAVIKVGGASEVEVNEKKDRIEDALNATRAAVEE 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 401 GVVAGGGVALIRAANSIRNIRGDNE---DQNVGIKVACRAMEAPLRQIVDNAGEEPSVIANNV-RASEGNIGYNVVSEKY 476
Cdd:PTZ00114 422 GIVPGGGVALLRASKLLDKLEEDNEltpDQRTGVKIVRNALRLPTKQIAENAGVEGAVVVEKIlEKKDPSFGYDAQTGEY 501
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 383081607 477 GNMIEMGILDPTKVTRSALQYAASIAGLMITTECMITELAKEEKP 521
Cdd:PTZ00114 502 VNMFEAGIIDPTKVVRSALVDAASVASLMLTTEAAIVDLPKEKKK 546
|
|
| groEL |
CHL00093 |
chaperonin GroEL |
3-519 |
0e+00 |
|
chaperonin GroEL
Pssm-ID: 177025 Cd Length: 529 Bit Score: 662.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 3 ARAKMLRGVNVLADAVKVSLGPKGRNVVLDKSFGAPIITKDGVSVAREIELQDKFENMGAQMVKEVASKANDASGDGTTT 82
Cdd:CHL00093 11 ARRALERGMDILAEAVSVTLGPKGRNVVLEKKYGSPQIVNDGVTIAKEIELEDHIENTGVALIRQAASKTNDVAGDGTTT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 83 ATVLAQSIVNEGLKAVAAGMNPMDLKRGIDKAVIAAVEELRKLSSPCEDSKAIAQVGTISANSDETVGALIAEAMAKVGK 162
Cdd:CHL00093 91 ATVLAYAIVKQGMKNVAAGANPISLKRGIEKATQYVVSQIAEYARPVEDIQAITQVASISAGNDEEVGSMIADAIEKVGR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 163 EGVITVEEGSGLQDELDVVEGMQFDRGYLSPYFVNKAESGSVELDNPFILLIDKKISNIR-EMLPILEAVAKSSKPLLII 241
Cdd:CHL00093 171 EGVISLEEGKSTVTELEITEGMRFEKGFISPYFVTDTERMEVVQENPYILLTDKKITLVQqDLLPILEQVTKTKRPLLII 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 242 AEDVEGEALATLVVNNMRGIVKVAAVKAPGFGDRRKAMLQDIAVLTAGTVISEEIGLDLEKSTLKDMGQAKRVVITKDTT 321
Cdd:CHL00093 251 AEDVEKEALATLVLNKLRGIVNVVAVRAPGFGDRRKAMLEDIAILTGGQVITEDAGLSLETIQLDLLGQARRIIVTKDST 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 322 TIIdGIGDKVSINNRVAQINQQRDEATSDYDREKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVEDALHATRAAVEEG 401
Cdd:CHL00093 331 TII-ADGNEEQVKARCEQLRKQIEIADSSYEKEKLQERLAKLSGGVAVIKVGAATETEMKDKKLRLEDAINATKAAVEEG 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 402 VVAGGGVALIRAANSIRNIRGDN--EDQNVGIKVACRAMEAPLRQIVDNAGEEPSVIANNVRASEGNIGYNVVSEKYGNM 479
Cdd:CHL00093 410 IVPGGGATLVHLSENLKTWAKNNlkEDELIGALIVARAILAPLKRIAENAGKNGSVIIEKVQEQDFEIGYNAANNKFVNM 489
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 383081607 480 IEMGILDPTKVTRSALQYAASIAGLMITTECMITELAKEE 519
Cdd:CHL00093 490 YEAGIIDPAKVTRSALQNAASIASMILTTECIIVDKKESS 529
|
|
| PRK14104 |
PRK14104 |
chaperonin GroEL; Provisional |
2-518 |
0e+00 |
|
chaperonin GroEL; Provisional
Pssm-ID: 172594 Cd Length: 546 Bit Score: 635.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 2 EARAKMLRGVNVLADAVKVSLGPKGRNVVLDKSFGAPIITKDGVSVAREIELQDKFENMGAQMVKEVASKANDASGDGTT 81
Cdd:PRK14104 11 DARDRMLRGVDILANAVKVTLGPKGRNVVLDKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVREVASKSADAAGDGTT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 82 TATVLAQSIVNEGLKAVAAGMNPMDLKRGIDKAVIAAVEELRKLSSPCEDSKAIAQVGTISANSDETVGALIAEAMAKVG 161
Cdd:PRK14104 91 TATVLAQAIVREGAKSVAAGMNPMDLKRGIDLAVEAVVADLVKNSKKVTSNDEIAQVGTISANGDAEIGKFLADAMKKVG 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 162 KEGVITVEEGSGLQDELDVVEGMQFDRGYLSPYFVNKAESGSVELDNPFILLIDKKISNIREMLPILEAVAKSSKPLLII 241
Cdd:PRK14104 171 NEGVITVEEAKSLETELDVVEGMQFDRGYISPYFVTNADKMRVEMDDAYILINEKKLSSLNELLPLLEAVVQTGKPLVIV 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 242 AEDVEGEALATLVVNNMRGIVKVAAVKAPGFGDRRKAMLQDIAVLTAGTVISEEIGLDLEKSTLKDMGQAKRVVITKDTT 321
Cdd:PRK14104 251 AEDVEGEALATLVVNRLRGGLKVAAVKAPGFGDRRKAMLQDIAILTGGQAISEDLGIKLENVTLQMLGRAKKVMIDKENT 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 322 TIIDGIGDKVSINNRVAQINQQRDEATSDYDREKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVEDALHATRAAVEEG 401
Cdd:PRK14104 331 TIVNGAGKKADIEARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKERKDRVDDAMHATRAAVEEG 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 402 VVAGGGVALIRAANSIRNIRGDNEDQNVGIKVACRAMEAPLRQIVDNAGEEPSVIANNVRASEG-NIGYNVVSEKYGNMI 480
Cdd:PRK14104 411 IVPGGGVALLRASEQLKGIKTKNDDQKTGVEIVRKALSAPARQIAINAGEDGSVIVGKILEKEQySYGFDSQTGEYGNLV 490
|
490 500 510
....*....|....*....|....*....|....*...
gi 383081607 481 EMGILDPTKVTRSALQYAASIAGLMITTECMITELAKE 518
Cdd:PRK14104 491 SKGIIDPTKVVRTAIQNAASVAALLITTEAMVAELPKK 528
|
|
| PLN03167 |
PLN03167 |
Chaperonin-60 beta subunit; Provisional |
3-519 |
0e+00 |
|
Chaperonin-60 beta subunit; Provisional
Pssm-ID: 215611 [Multi-domain] Cd Length: 600 Bit Score: 530.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 3 ARAKMLRGVNVLADAVKVSLGPKGRNVVLDKSFGAPIITKDGVSVAREIELQDKFENMGAQMVKEVASKANDASGDGTTT 82
Cdd:PLN03167 67 AIKKLQAGVNKLADLVGVTLGPKGRNVVLESKYGSPKIVNDGVTVAKEVELEDPVENIGAKLVRQAAAKTNDLAGDGTTT 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 83 ATVLAQSIVNEGLKAVAAGMNPMDLKRGIDKAVIAAVEELRKLSSPCEDSKaIAQVGTISANSDETVGALIAEAMAKVGK 162
Cdd:PLN03167 147 SVVLAQGLIAEGVKVVAAGANPVQITRGIEKTAKALVKELKKMSKEVEDSE-LADVAAVSAGNNYEVGNMIAEAMSKVGR 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 163 EGVITVEEGSGLQDELDVVEGMQFDRGYLSPYFVNKAESGSVELDNPFILLIDKKISNIREMLPILEAVAKSSKPLLIIA 242
Cdd:PLN03167 226 KGVVTLEEGKSAENNLYVVEGMQFDRGYISPYFVTDSEKMSVEYDNCKLLLVDKKITNARDLIGILEDAIRGGYPLLIIA 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 243 EDVEGEALATLVVNNMRGIVKVAAVKAPGFGDRRKAMLQDIAVLTAGTVISEEIGLDLEKSTLKDMGQAKRVVITKDTTT 322
Cdd:PLN03167 306 EDIEQEALATLVVNKLRGSLKIAALKAPGFGERKSQYLDDIAILTGGTVIREEVGLSLDKVGKEVLGTAAKVVLTKDTTT 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 323 IIDGIGDKVSINNRVAQINQQRDEATSDYDREKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVEDALHATRAAVEEGV 402
Cdd:PLN03167 386 IVGDGSTQEAVNKRVAQIKNLIEAAEQDYEKEKLNERIAKLSGGVAVIQVGAQTETELKEKKLRVEDALNATKAAVEEGI 465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 403 VAGGGVALIRAANSIRNIRG--DNEDQNVGIKVACRAMEAPLRQIVDNAGEEPSVIANNVRASEG-NIGYNVVSEKYGNM 479
Cdd:PLN03167 466 VVGGGCTLLRLASKVDAIKDtlENDEQKVGADIVKRALSYPLKLIAKNAGVNGSVVSEKVLSNDNpKFGYNAATGKYEDL 545
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 383081607 480 IEMGILDPTKVTRSALQYAASIAGLMITTECMITELAKEE 519
Cdd:PLN03167 546 MAAGIIDPTKVVRCCLEHAASVAKTFLTSDCVVVEIKEPE 585
|
|
| chaperonin_type_I_II |
cd00309 |
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ... |
2-513 |
1.65e-146 |
|
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: 429.16 E-value: 1.65e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 2 EARAKMLRGVNVLADAVKVSLGPKGRNVVLDKSFGAPIITKDGVSVAREIELQdkfeNMGAQMVKEVASKANDASGDGTT 81
Cdd:cd00309 8 EARLSNINAAKALADAVKTTLGPKGMDKMLVDSLGDPTITNDGATILKEIEVE----HPAAKLLVEVAKSQDDEVGDGTT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 82 TATVLAQSIVNEGLKAVAAGMNPMDLKRGIDKAVIAAVEELRKLSSP--CEDSKAIAQVGTISANS------DETVGALI 153
Cdd:cd00309 84 TVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVPidVEDREELLKVATTSLNSklvsggDDFLGELV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 154 AEAMAKVGKE------GVITVEEGSG---LQDELdvVEGMQFDRGYLSPYFvnkaesgSVELDNPFILLIDKKISNirem 224
Cdd:cd00309 164 VDAVLKVGKEngdvdlGVIRVEKKKGgslEDSEL--VVGMVFDKGYLSPYM-------PKRLENAKILLLDCKLEY---- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 225 lpileavaksskplLIIAED-VEGEALATLVVNNmrgivkVAAVKApgfgdRRKAMLQDIAVLTAGTVISEeigldLEKS 303
Cdd:cd00309 231 --------------VVIAEKgIDDEALHYLAKLG------IMAVRR-----VRKEDLERIAKATGATIVSR-----LEDL 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 304 TLKDMGQAKRVVITK----DTTTIIDGIGdkvsinnrvaqinqqrdeatsdydreklqervaklaGGVAVIKVGAATEVE 379
Cdd:cd00309 281 TPEDLGTAGLVEETKigdeKYTFIEGCKG------------------------------------GKVATILLRGATEVE 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 380 MKEKKARVEDALHATRAAVEE-GVVAGGGVALIRAANSIRNI-RGDNEDQNVGIKVACRAMEAPLRQIVDNAGEEPSVIA 457
Cdd:cd00309 325 LDEAERSLHDALCAVRAAVEDgGIVPGGGAAEIELSKALEELaKTLPGKEQLGIEAFADALEVIPRTLAENAGLDPIEVV 404
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 458 NNVRASEGNIGYN----VVSEKYGNMIEMGILDPTKVTRSALQYAASIAGLMITTECMIT 513
Cdd:cd00309 405 TKLRAKHAEGGGNaggdVETGEIVDMKEAGIIDPLKVKRQALKSATEAASLILTIDDIIV 464
|
|
| Cpn60_TCP1 |
pfam00118 |
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ... |
14-512 |
1.68e-77 |
|
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: 252.12 E-value: 1.68e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 14 LADAVKVSLGPKGRNVVLDKSFGAPIITKDGVSVAREIELQDKfenmGAQMVKEVASKANDASGDGTTTATVLAQSIVNE 93
Cdd:pfam00118 1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELEIQHP----AAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 94 GLKAVAAGMNPMDLKRGIDKAVIAAVEEL---RKLSSPCEDSKAIAQVGTISANSD------ETVGALIAEA-------- 156
Cdd:pfam00118 77 AEKLLAAGVHPTTIIEGYEKALEKALEILdsiISIPVEDVDREDLLKVARTSLSSKiisresDFLAKLVVDAvlaipknd 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 157 -MAKVGKEGVITVEEGSGlqDELDVVEGMQFDRGYLSPyfvnkaeSGSVELDNPFILLIDKKISNIRE------------ 223
Cdd:pfam00118 157 gSFDLGNIGVVKILGGSL--EDSELVDGVVLDKGPLHP-------DMPKRLENAKVLLLNCSLEYEKTetkatvvlsdae 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 224 ------------MLPILEAVAKSSKPLLIIAEDVEGEALATLVVNNMRGIVKVaavkapgfgdrRKAMLQDIAVLTAGTV 291
Cdd:pfam00118 228 qlerflkaeeeqILEIVEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMALRRV-----------KKRDLERLAKATGARA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 292 ISEEIGLDLEkstlkDMGQAKRV---VITKDTTTIIDGIGDkvsinnrvaqinqqrdeatsdydreklqervaklaGGVA 368
Cdd:pfam00118 297 VSSLDDLTPD-----DLGTAGKVeeeKIGDEKYTFIEGCKS-----------------------------------PKAA 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 369 VIKVGAATEVEMKEKKARVEDALHATRAAVEE-GVVAGGGVALIRAANSIRNI-RGDNEDQNVGIKVACRAMEAPLRQIV 446
Cdd:pfam00118 337 TILLRGATDHVLDEIERSIHDALCVVKNAIEDpRVVPGGGAVEMELARALREYaKSVSGKEQLAIEAFAEALEVIPKTLA 416
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 447 DNAGEEPSVIANNVRA----SEGNIGYNVVSEKYGNMIEMGILDPTKVTRSALQYAASIAGLMITTECMI 512
Cdd:pfam00118 417 ENAGLDPIEVLAELRAahasGEKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKSATEAASTILRIDDII 486
|
|
| chaperonin_like |
cd03333 |
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ... |
133-400 |
2.46e-39 |
|
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: 142.22 E-value: 2.46e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 133 KAIAQVGTISANS-----DETVGALIAEAMAKVGKE------GVITVEEGSG---LQDELdvVEGMQFDRGYLSPYFvnk 198
Cdd:cd03333 2 ELLLQVATTSLNSklsswDDFLGKLVVDAVLKVGPDnrmddlGVIKVEKIPGgslEDSEL--VVGVVFDKGYASPYM--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 199 aesgSVELDNPFILLIDKKISNiremlpileavaksskplLIIAED-VEGEALATLVVNNmrgivkVAAVKApgfgdRRK 277
Cdd:cd03333 77 ----PKRLENAKILLLDCPLEY------------------VVIAEKgIDDLALHYLAKAG------IMAVRR-----VKK 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 278 AMLQDIAVLTAGTVISEeigldLEKSTLKDMGQAKRVVITK---DTTTIIDGIGDkvsinnrvaqinqqrdeatsdydre 354
Cdd:cd03333 124 EDLERIARATGATIVSS-----LEDLTPEDLGTAELVEETKigeEKLTFIEGCKG------------------------- 173
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 383081607 355 klqervaklaGGVAVIKVGAATEVEMKEKKARVEDALHATRAAVEE 400
Cdd:cd03333 174 ----------GKAATILLRGATEVELDEVKRSLHDALCAVRAAVEE 209
|
|
| cpn60 |
cd03343 |
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ... |
13-506 |
4.11e-18 |
|
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: 87.32 E-value: 4.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 13 VLADAVKVSLGPKGRNVVLDKSFGAPIITKDGVSVAREIELQdkfeNMGAQMVKEVASKANDASGDGTTTATVLAQSIVN 92
Cdd:cd03343 26 AVAEAVRTTLGPKGMDKMLVDSLGDVTITNDGATILKEMDIE----HPAAKMLVEVAKTQDEEVGDGTTTAVVLAGELLE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 93 EGLKAVAAGMNPMDLKRGIDKAVIAAVEELRKLSSPCEDS-----KAIAQVGTISANSDETvgaliAEAMAKVGKEGVIT 167
Cdd:cd03343 102 KAEDLLDQNIHPTVIIEGYRLAAEKALELLDEIAIKVDPDdkdtlRKIAKTSLTGKGAEAA-----KDKLADLVVDAVLQ 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 168 VEEGSGLQDELDV------------VEGMQFDRGY-LSPYFVNKAESGSVEldNPFILLIDKKIS----------NIREM 224
Cdd:cd03343 177 VAEKRDGKYVVDLdnikiekktggsVDDTELIRGIvIDKEVVHPGMPKRVE--NAKIALLDAPLEvkkteidakiRITSP 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 225 LPILEAVAKSSKPLLIIAEDVegEALATLVVNNMRGIVKVAA---VKAPGFGDRR--KAMLQDIAVLTAGTVISeeiglD 299
Cdd:cd03343 255 DQLQAFLEQEEAMLKEMVDKI--ADTGANVVFCQKGIDDLAQhylAKAGILAVRRvkKSDMEKLARATGAKIVT-----N 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 300 LEKSTLKDMGQAKRVvitkdtttiidgigdkvsinnrvaqinqqrdEATSDYDREKLQERVAKLAGGVAVIKVGaATEVE 379
Cdd:cd03343 328 IDDLTPEDLGEAELV-------------------------------EERKVGDDKMVFVEGCKNPKAVTILLRG-GTEHV 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 380 MKEKKARVEDALHATRAAVEEG-VVAGGGVALIRAANSIRnirgdNEDQNVG------IKVACRAMEAPLRQIVDNAGEE 452
Cdd:cd03343 376 VDELERALEDALRVVADALEDGkVVAGGGAVEIELAKRLR-----EYARSVGgreqlaVEAFADALEEIPRTLAENAGLD 450
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 383081607 453 PSVIANNVRA----SEGNIGYNVVSEKYGNMIEMGILDPTKVTRSALQyAASIAGLMI 506
Cdd:cd03343 451 PIDTLVELRAahekGNKNAGLDVYTGEVVDMLEKGVIEPLRVKKQAIK-SATEAATMI 507
|
|
| TCP1_delta |
cd03338 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ... |
14-499 |
8.90e-12 |
|
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: 67.31 E-value: 8.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 14 LADAVKVSLGPKGRNVVLDKSFGAPIITKDGVSVAREIELQdkfeNMGAQMVKEVaSKAND-ASGDGTTTATVLAQSIVN 92
Cdd:cd03338 20 VADAIRTSLGPRGMDKMIQTGKGEVIITNDGATILKQMSVL----HPAAKMLVEL-SKAQDiEAGDGTTSVVVLAGALLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 93 EGLKAVAAGMNPMDLKRGIDKAVIAAVEELRKLSSPCE--DSKAIAQVGTISANS------DETVGALIAEAMAKVGKEG 164
Cdd:cd03338 95 ACESLLKKGIHPTVISESFQIAAKKAVEILDSMSIPVDlnDRESLIKSATTSLNSkvvsqySSLLAPIAVDAVLKVIDPA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 165 VIT---------VEEGSGLQDELDVVEGM----QFDRGYLSPYFVNKAESG---------SVELDNPFIL----LIDKKI 218
Cdd:cd03338 175 TATnvdlkdiriVKKLGGTIEDTELVDGLvftqKASKKAGGPTRIEKAKIGliqfclsppKTDMDNNIVVndyaQMDRIL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 219 SNIRE-MLPILEAVAKSSKPLLIIAEDVEGEALATL---VVNNMrgivKVAAVKAPgfgDRrkamlQDIavltagTVISE 294
Cdd:cd03338 255 REERKyILNMCKKIKKSGCNVLLIQKSILRDAVSDLalhFLAKL----KIMVVKDI---ER-----EEI------EFICK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 295 EIG----LDLEKSTLKDMGQAKRVvitkdtttiidgigdkvsinnrvaqinqqrDEATSDYDREKLQERVAKLAGGVAVI 370
Cdd:cd03338 317 TIGckpvASIDHFTEDKLGSADLV------------------------------EEVSLGDGKIVKITGVKNPGKTVTIL 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 371 kVGAATEVEMKEKKARVEDALHATRAAVEE-GVVAGGGVALIRAANSIRNIrgdnEDQNVGIKVAC-----RAMEAPLRQ 444
Cdd:cd03338 367 -VRGSNKLVLDEAERSLHDALCVIRCLVKKrALIPGGGAPEIEIALQLSEW----ARTLTGVEQYCvrafaDALEVIPYT 441
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 383081607 445 IVDNAGEEPSVIANNVRA----SEGNIGYNVVSEKYGNMIEMGILDPTKVTRSALQYAA 499
Cdd:cd03338 442 LAENAGLNPISIVTELRNrhaqGEKNAGINVRKGAITNILEENVVQPLLVSTSAITLAT 500
|
|
| chap_CCT_epsi |
TIGR02343 |
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ... |
14-132 |
8.33e-10 |
|
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: 61.36 E-value: 8.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 14 LADAVKVSLGPKGRNVVLDKSFGAPIITKDGVSVAREIELQDKFenmgAQMVKEVASKANDASGDGTTTATVLAQSIVNE 93
Cdd:TIGR02343 39 VASILRTSLGPKGMDKMLISPDGDITVTNDGATILSQMDVDNQI----AKLMVELSKSQDDEIGDGTTGVVVLAGALLEQ 114
|
90 100 110
....*....|....*....|....*....|....*....
gi 383081607 94 GLKAVAAGMNPMDLKRGIDKAVIAAVEELRKLSSPCEDS 132
Cdd:TIGR02343 115 AEELLDKGIHPIKIADGFEEAARIAVEHLEEISDEISAD 153
|
|
| TCP1_eta |
cd03340 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ... |
1-126 |
2.06e-09 |
|
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: 59.99 E-value: 2.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 1 SEARAKMLRGVN---VLADAVKVSLGPKGRNVVLDKSFGAPIITKDGVSVAREIELQdkfeNMGAQMVKEVAsKANDAS- 76
Cdd:cd03340 12 SQGKGQLISNINacqAIADAVRTTLGPRGMDKLIVDGRGKVTISNDGATILKLLDIV----HPAAKTLVDIA-KSQDAEv 86
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 383081607 77 GDGTTTATVLAQSIVNEGLKAVAAGMNPMDLKRGIDKAVIAAVEELRKLS 126
Cdd:cd03340 87 GDGTTSVVVLAGEFLKEAKPFIEDGVHPQIIIRGYRKALQLAIEKIKEIA 136
|
|
| TCP1_beta |
cd03336 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ... |
3-124 |
5.61e-09 |
|
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: 58.49 E-value: 5.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 3 ARAKMLRGVNVLADAVKVSLGPKGRNVVL--DKSFGAPIITKDGVSVAREIELqdkfENMGAQMVKEVASKANDASGDGT 80
Cdd:cd03336 14 ARLSSFVGAIAIGDLVKTTLGPKGMDKILqsVGRSGGVTVTNDGATILKSIGV----DNPAAKVLVDISKVQDDEVGDGT 89
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 383081607 81 TTATVLAQSIVNEGLKAVAAGMNPMDLKRGIDKAVIAAVEELRK 124
Cdd:cd03336 90 TSVTVLAAELLREAEKLVAQKIHPQTIIEGYRMATAAAREALLS 133
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
1-126 |
1.64e-08 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 56.96 E-value: 1.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 1 SEARAKMLR-----GVNVLADAVKVSLGPKGRNVVLDKSFGAP-----IITKDGVSVAREIELqdkfENMGAQMVKEVAS 70
Cdd:PTZ00212 16 QEEKGETARlqsfvGAIAVADLVKTTLGPKGMDKILQPMSEGPrsgnvTVTNDGATILKSVWL----DNPAAKILVDISK 91
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 383081607 71 KANDASGDGTTTATVLAQSIVNEGLKAVAAGMNPMDLKRGIDKAVIAAVEELRKLS 126
Cdd:PTZ00212 92 TQDEEVGDGTTSVVVLAGELLREAEKLLDQKIHPQTIIEGWRMALDVARKALEEIA 147
|
|
| TCP1_epsilon |
cd03339 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ... |
14-133 |
4.08e-08 |
|
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.
Pssm-ID: 239455 Cd Length: 526 Bit Score: 55.77 E-value: 4.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 14 LADAVKVSLGPKGRNVVLDKSFGAPIITKDGVSVAREIELQdkfeNMGAQMVKEVASKANDASGDGTTTATVLAQSIVNE 93
Cdd:cd03339 35 VANILRTSLGPRGMDKILVSPDGEVTVTNDGATILEKMDVD----HQIAKLLVELSKSQDDEIGDGTTGVVVLAGALLEQ 110
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 383081607 94 GLKAVAAGMNPMDLKRGIDKAVIAAVEELRKLSSPCEDSK 133
Cdd:cd03339 111 AEKLLDRGIHPIRIADGYEQACKIAVEHLEEIADKIEFSP 150
|
|
| chap_CCT_beta |
TIGR02341 |
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ... |
3-126 |
5.15e-08 |
|
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: 55.64 E-value: 5.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 3 ARAKMLRGVNVLADAVKVSLGPKGRNVVL--DKSFGAPIITKDGVSVAREIELqdkfENMGAQMVKEVASKANDASGDGT 80
Cdd:TIGR02341 15 ARLSSFVGAIAIGDLVKSTLGPKGMDKILqsSSSDASIMVTNDGATILKSIGV----DNPAAKVLVDMSKVQDDEVGDGT 90
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 383081607 81 TTATVLAQSIVNEGLKAVAAGMNPMDLKRGIDKAVIAAVEELRKLS 126
Cdd:TIGR02341 91 TSVTVLAAELLREAEKLINQKIHPQTIIAGYREATKAARDALLKSA 136
|
|
| chap_CCT_zeta |
TIGR02347 |
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ... |
14-132 |
1.29e-07 |
|
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT zeta chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.
Pssm-ID: 274088 [Multi-domain] Cd Length: 531 Bit Score: 54.36 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 14 LADAVKVSLGPKGRNVVLDKSFGAPIITKDGVSVAREIELQdkfeNMGAQMVKEVASKANDASGDGTTTATVLAQSIVNE 93
Cdd:TIGR02347 28 LQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEMQIQ----HPTASMIARAATAQDDITGDGTTSTVLLIGELLKQ 103
|
90 100 110
....*....|....*....|....*....|....*....
gi 383081607 94 GLKAVAAGMNPMDLKRGIDKAVIAAVEELRKLSSPCEDS 132
Cdd:TIGR02347 104 AERYILEGVHPRIITEGFEIARKEALQFLDKFKVKKEDE 142
|
|
| TCP1_zeta |
cd03342 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
14-189 |
1.44e-07 |
|
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.
Pssm-ID: 239458 [Multi-domain] Cd Length: 484 Bit Score: 53.80 E-value: 1.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 14 LADAVKVSLGPKGRNVVLDKSFGAPIITKDGVSVAREIELQDKFenmgAQMVKEVASKANDASGDGTTTATVLAQSIVNE 93
Cdd:cd03342 24 LQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLSEMQIQHPT----ASMIARAATAQDDITGDGTTSNVLLIGELLKQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 94 GLKAVAAGMNPMDLKRGIDKAVIAAVEELRKLSSPCE---DSKAIAQVGTISANSDetVGALIAEAMAKVGKEGVITVEE 170
Cdd:cd03342 100 AERYIQEGVHPRIITEGFELAKNKALKFLESFKVPVEidtDRELLLSVARTSLRTK--LHADLADQLTEIVVDAVLAIYK 177
|
170
....*....|....*....
gi 383081607 171 GSGLQDeLDVVEGMQFDRG 189
Cdd:cd03342 178 PDEPID-LHMVEIMQMQHK 195
|
|
| chap_CCT_gamma |
TIGR02344 |
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ... |
14-180 |
1.38e-06 |
|
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT gamma chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.
Pssm-ID: 274085 [Multi-domain] Cd Length: 524 Bit Score: 50.89 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 14 LADAVKVSLGPKGRNVVLDKSFGAPIITKDGVSVAREIELQdkfeNMGAQMVKEVASKANDASGDGTTTATVLAQSIVNE 93
Cdd:TIGR02344 28 VADIIRTCLGPRSMLKMLLDPMGGIVMTNDGNAILREIDVA----HPAAKSMIELSRTQDEEVGDGTTSVIILAGEMLSV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 94 GLKAVAAGMNPMDLKRGIDKAVIAAVEELRKLSSPCEDSKAIAQVGTISANSDETVGALIAEAMAKVGKEGVITVEEGSG 173
Cdd:TIGR02344 104 AEPFLEQNIHPTVIIRAYRKALDDALSVLEEISIPVDVNDDAAMLKLIQSCIGTKFVSRWSDLMCDLALDAVRTVQRDEN 183
|
....*..
gi 383081607 174 LQDELDV 180
Cdd:TIGR02344 184 GRKEIDI 190
|
|
| chap_CCT_theta |
TIGR02346 |
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ... |
14-126 |
2.36e-06 |
|
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT alpha chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.
Pssm-ID: 274087 [Multi-domain] Cd Length: 531 Bit Score: 50.10 E-value: 2.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 14 LADAVKVSLGPKGRNVVLDKSFGAPIITKDGVSVAREIELQdkfeNMGAQMVKEVASKANDASGDGTTTATVLAQSIVNE 93
Cdd:TIGR02346 30 LSQITRTSLGPNGMNKMVINHLEKLFVTNDAATILRELEVQ----HPAAKLLVMASEMQENEIGDGTNLVLVLAGELLNK 105
|
90 100 110
....*....|....*....|....*....|...
gi 383081607 94 GLKAVAAGMNPMDLKRGIDKAVIAAVEELRKLS 126
Cdd:TIGR02346 106 AEELIRMGLHPSEIIKGYEMALKKAMEILEELV 138
|
|
| chap_CCT_alpha |
TIGR02340 |
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ... |
3-104 |
4.27e-06 |
|
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: 49.33 E-value: 4.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 3 ARAKMLRGVNVLADAVKVSLGPKGRNVVLDKSFGAPIITKDGVSVAREIELQDKfenmGAQMVKEVASKANDASGDGTTT 82
Cdd:TIGR02340 13 VRTQNVTAAMAIANIVKTSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHP----AAKILVELAQLQDREVGDGTTS 88
|
90 100
....*....|....*....|..
gi 383081607 83 ATVLAQSIVNEGLKAVAAGMNP 104
Cdd:TIGR02340 89 VVIIAAELLKRADELVKNKIHP 110
|
|
| TCP1_gamma |
cd03337 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ... |
14-180 |
2.26e-05 |
|
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.
Pssm-ID: 239453 [Multi-domain] Cd Length: 480 Bit Score: 46.91 E-value: 2.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 14 LADAVKVSLGPKGR-NVVLDKSfGAPIITKDGVSVAREIELQdkfeNMGAQMVKEVASKANDASGDGTTTATVLAQSIVN 92
Cdd:cd03337 28 VADVIRTCLGPRAMlKMLLDPM-GGIVLTNDGNAILREIDVA----HPAAKSMIELSRTQDEEVGDGTTSVIILAGEILA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 93 EGLKAVAAGMNPMDLKRGIDKAVIAAVEELRKLSSP--CEDSKAIAQVgtISANSDETVGALIAEAMAKVGKEGVITVE- 169
Cdd:cd03337 103 VAEPFLERGIHPTVIIKAYRKALEDALKILEEISIPvdVNDRAQMLKI--IKSCIGTKFVSRWSDLMCNLALDAVKTVAv 180
|
170
....*....|.
gi 383081607 170 EGSGLQDELDV 180
Cdd:cd03337 181 EENGRKKEIDI 191
|
|
| TCP1_theta |
cd03341 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ... |
14-127 |
8.04e-05 |
|
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.
Pssm-ID: 239457 [Multi-domain] Cd Length: 472 Bit Score: 45.29 E-value: 8.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 14 LADAVKVSLGPKGRN--VV--LDKSFgapiITKDGVSVAREIELQdkfeNMGAQMVKEVASKANDASGDGTTTATVLAQS 89
Cdd:cd03341 20 LSQITRTSYGPNGMNkmVInhLEKLF----VTSDAATILRELEVQ----HPAAKLLVMASQMQEEEIGDGTNLVVVLAGE 91
|
90 100 110
....*....|....*....|....*....|....*...
gi 383081607 90 IVNEGLKAVAAGMNPMDLKRGIDKAVIAAVEELRKLSS 127
Cdd:cd03341 92 LLEKAEELLRMGLHPSEIIEGYEKALKKALEILEELVV 129
|
|
| TCP1_alpha |
cd03335 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ... |
2-104 |
1.28e-04 |
|
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.
Pssm-ID: 239451 Cd Length: 527 Bit Score: 44.58 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383081607 2 EARAKMLRGVNVLADAVKVSLGPKGRNVVLDKSFGAPIITKDGVSVAREIELQDKfenmGAQMVKEVASKANDASGDGTT 81
Cdd:cd03335 8 DVRTQNVTAAMAIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHP----AAKILVELAQLQDKEVGDGTT 83
|
90 100
....*....|....*....|...
gi 383081607 82 TATVLAQSIVNEGLKAVAAGMNP 104
Cdd:cd03335 84 SVVIIAAELLKRANELVKQKIHP 106
|
|
| |
