|
Name |
Accession |
Description |
Interval |
E-value |
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
2-530 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 1000.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 2 AAKDVKFGNDARVKMLRGVNVLADAVKVTLGPKGRNVVLDKSFGAPTITKDGVSVAREIELEDKFENMGAQMVKEVASKA 81
Cdd:PRK00013 1 MAKDIKFGEDARRKLLRGVNKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDPFENMGAQLVKEVASKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 82 NDAAGDGTTTATVLAQAIVNEGLKAVAAGMNPMDLKRGIDKAVVAAVEELKALSVPCSDSKAIAQVGTISANSDETVGKL 161
Cdd:PRK00013 81 NDVAGDGTTTATVLAQAIVREGLKNVAAGANPMDLKRGIDKAVEAAVEELKKISKPVEDKEEIAQVATISANGDEEIGKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 162 IAEAMDKVGKEGVITVEDGTGLEDELDVVEGMQFDRGYLSPYFINKPDTGAVELESPFILLADKKISNIREMLPVLEAVA 241
Cdd:PRK00013 161 IAEAMEKVGKEGVITVEESKGFETELEVVEGMQFDRGYLSPYFVTDPEKMEAELENPYILITDKKISNIQDLLPVLEQVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 242 KAGKPLVIIAEDVEGEALATLVVNTMRGIVKVAAVKAPGFGDRRKAMLQDIATLTGGTVISEEIGMELEKATLEDLGQAK 321
Cdd:PRK00013 241 QSGKPLLIIAEDVEGEALATLVVNKLRGTLKVVAVKAPGFGDRRKAMLEDIAILTGGTVISEELGLKLEDATLEDLGQAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 322 RVVINKDTTTIIDGVGEESAIQGRVAQIRKQIEEATSDYDREKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVDDALH 401
Cdd:PRK00013 321 KVVVTKDNTTIVDGAGDKEAIKARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATEVEMKEKKDRVEDALH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 402 ATRAAVEEGVVAGGGVALVRVAAKLAGLTGQNEDQNVGIKVALRAMEAPLRQIVSNAGEEPSVVANNVKAGDG-NYGYNA 480
Cdd:PRK00013 401 ATRAAVEEGIVPGGGVALLRAAPALEALKGLNGDEATGINIVLRALEAPLRQIAENAGLEGSVVVEKVKNGKGkGYGYNA 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1993607497 481 ATEEYGNMIDFGILDPTKVTRSALQYAASVAGLMITTECMVTDLPKGDAP 530
Cdd:PRK00013 481 ATGEYVDMIEAGIIDPTKVTRSALQNAASVAGLLLTTEAVVADKPEKKAA 530
|
|
| groEL |
PRK12849 |
chaperonin GroEL; Reviewed |
2-530 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237230 Cd Length: 542 Bit Score: 910.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 2 AAKDVKFGNDARVKMLRGVNVLADAVKVTLGPKGRNVVLDKSFGAPTITKDGVSVAREIELEDKFENMGAQMVKEVASKA 81
Cdd:PRK12849 1 MAKIIKFDEEARRALERGVNKLADAVKVTLGPKGRNVVIDKSFGAPTITKDGVSIAKEIELEDPFENLGAQLVKEVASKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 82 NDAAGDGTTTATVLAQAIVNEGLKAVAAGMNPMDLKRGIDKAVVAAVEELKALSVPCSDSKAIAQVGTISANSDETVGKL 161
Cdd:PRK12849 81 NDVAGDGTTTATVLAQALVQEGLKNVAAGANPMDLKRGIDKAVEAVVEELKALARPVSGSEEIAQVATISANGDEEIGEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 162 IAEAMDKVGKEGVITVEDGTGLEDELDVVEGMQFDRGYLSPYFINKPDTGAVELESPFILLADKKISNIREMLPVLEAVA 241
Cdd:PRK12849 161 IAEAMEKVGKDGVITVEESKTLETELEVTEGMQFDRGYLSPYFVTDPERMEAVLEDPLILLTDKKISSLQDLLPLLEKVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 242 KAGKPLVIIAEDVEGEALATLVVNTMRGIVKVAAVKAPGFGDRRKAMLQDIATLTGGTVISEEIGMELEKATLEDLGQAK 321
Cdd:PRK12849 241 QSGKPLLIIAEDVEGEALATLVVNKLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGLKLEEVTLDDLGRAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 322 RVVINKDTTTIIDGVGEESAIQGRVAQIRKQIEEATSDYDREKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVDDALH 401
Cdd:PRK12849 321 RVTITKDNTTIVDGAGDKEAIEARVAQIRRQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATEVELKERKDRVEDALN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 402 ATRAAVEEGVVAGGGVALVRVAAKLAGLTGQNEDQNVGIKVALRAMEAPLRQIVSNAGEEPSVVANNVKAGDGNYGYNAA 481
Cdd:PRK12849 401 ATRAAVEEGIVPGGGVALLRAAKALDELAGLNGDQAAGVEIVRRALEAPLRQIAENAGLDGSVVVAKVLELEDGFGFNAA 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1993607497 482 TEEYGNMIDFGILDPTKVTRSALQYAASVAGLMITTECMVTDLPKGDAP 530
Cdd:PRK12849 481 TGEYGDLIAAGIIDPVKVTRSALQNAASVAGLLLTTEALVADKPEEEDP 529
|
|
| GroEL |
cd03344 |
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ... |
4-523 |
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: 901.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 4 KDVKFGNDARVKMLRGVNVLADAVKVTLGPKGRNVVLDKSFGAPTITKDGVSVAREIELEDKFENMGAQMVKEVASKAND 83
Cdd:cd03344 1 KDIKFGEEARKALLRGVNKLADAVKVTLGPKGRNVVIEKSFGSPKITKDGVTVAKEIELEDPFENMGAQLVKEVASKTND 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 84 AAGDGTTTATVLAQAIVNEGLKAVAAGMNPMDLKRGIDKAVVAAVEELKALSVPCSDSKAIAQVGTISANSDETVGKLIA 163
Cdd:cd03344 81 VAGDGTTTATVLARAIIKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKPVKTKEEIAQVATISANGDEEIGELIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 164 EAMDKVGKEGVITVEDGTGLEDELDVVEGMQFDRGYLSPYFINKPDTGAVELESPFILLADKKISNIREMLPVLEAVAKA 243
Cdd:cd03344 161 EAMEKVGKDGVITVEEGKTLETELEVVEGMQFDRGYLSPYFVTDPEKMEVELENPYILLTDKKISSIQELLPILELVAKA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 244 GKPLVIIAEDVEGEALATLVVNTMRGIVKVAAVKAPGFGDRRKAMLQDIATLTGGTVISEEIGMELEKATLEDLGQAKRV 323
Cdd:cd03344 241 GRPLLIIAEDVEGEALATLVVNKLRGGLKVCAVKAPGFGDRRKAMLEDIAILTGGTVISEELGLKLEDVTLEDLGRAKKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 324 VINKDTTTIIDGVGEESAIQGRVAQIRKQIEEATSDYDREKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVDDALHAT 403
Cdd:cd03344 321 VVTKDDTTIIGGAGDKAAIKARIAQIRKQIEETTSDYDKEKLQERLAKLSGGVAVIKVGGATEVELKEKKDRVEDALNAT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 404 RAAVEEGVVAGGGVALVRVAAKLAGLTGQNEDQNVGIKVALRAMEAPLRQIVSNAGEEPSVVANNVKAGDGNYGYNAATE 483
Cdd:cd03344 401 RAAVEEGIVPGGGVALLRASPALDKLKALNGDEKLGIEIVRRALEAPLRQIAENAGVDGSVVVEKVLESPDGFGYDAATG 480
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1993607497 484 EYGNMIDFGILDPTKVTRSALQYAASVAGLMITTECMVTD 523
Cdd:cd03344 481 EYVDMIEAGIIDPTKVVRSALQNAASVASLLLTTEALVVD 520
|
|
| GroEL |
TIGR02348 |
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ... |
3-526 |
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: 899.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 3 AKDVKFGNDARVKMLRGVNVLADAVKVTLGPKGRNVVLDKSFGAPTITKDGVSVAREIELEDKFENMGAQMVKEVASKAN 82
Cdd:TIGR02348 1 AKQIKFDEEARKALLRGVDKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDKFENMGAQLVKEVASKTN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 83 DAAGDGTTTATVLAQAIVNEGLKAVAAGMNPMDLKRGIDKAVVAAVEELKALSVPCSDSKAIAQVGTISANSDETVGKLI 162
Cdd:TIGR02348 81 DVAGDGTTTATVLAQAIVKEGLKNVAAGANPIELKRGIEKAVEAVVEELKKLSKPVKGKKEIAQVATISANNDEEIGSLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 163 AEAMDKVGKEGVITVEDGTGLEDELDVVEGMQFDRGYLSPYFINKPDTGAVELESPFILLADKKISNIREMLPVLEAVAK 242
Cdd:TIGR02348 161 AEAMEKVGKDGVITVEESKSLETELEVVEGMQFDRGYISPYFVTDAEKMEVELENPYILITDKKISNIKDLLPLLEKVAQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 243 AGKPLVIIAEDVEGEALATLVVNTMRGIVKVAAVKAPGFGDRRKAMLQDIATLTGGTVISEEIGMELEKATLEDLGQAKR 322
Cdd:TIGR02348 241 SGKPLLIIAEDVEGEALATLVVNKLRGTLNVCAVKAPGFGDRRKAMLEDIAILTGGQVISEELGLKLEEVTLDDLGKAKK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 323 VVINKDTTTIIDGVGEESAIQGRVAQIRKQIEEATSDYDREKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVDDALHA 402
Cdd:TIGR02348 321 VTVDKDNTTIVEGAGDKAAIKARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATETEMKEKKLRIEDALNA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 403 TRAAVEEGVVAGGGVALVRVAAKLAGLTGQNEDQNVGIKVALRAMEAPLRQIVSNAGEEPSVVANNVKAGDGNYGYNAAT 482
Cdd:TIGR02348 401 TRAAVEEGIVPGGGVALLRAAAALEGLKGDGEDEAIGIDIVKRALEAPLRQIAENAGLDGAVVAEKVKELKGNFGFNAAT 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1993607497 483 EEYGNMIDFGILDPTKVTRSALQYAASVAGLMITTECMVTDLPK 526
Cdd:TIGR02348 481 GEYEDLVEAGIIDPTKVTRSALQNAASIAGLLLTTEAVVADKPE 524
|
|
| groEL |
PRK12850 |
chaperonin GroEL; Reviewed |
1-530 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237231 Cd Length: 544 Bit Score: 844.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 1 MAAKDVKFGNDARVKMLRGVNVLADAVKVTLGPKGRNVVLDKSFGAPTITKDGVSVAREIELEDKFENMGAQMVKEVASK 80
Cdd:PRK12850 1 MAAKEIRFSTDARDRLLRGVNILANAVKVTLGPKGRNVVLEKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVKEVASK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 81 ANDAAGDGTTTATVLAQAIVNEGLKAVAAGMNPMDLKRGIDKAVVAAVEELKALSVPCSDSKAIAQVGTISANSDETVGK 160
Cdd:PRK12850 81 TNDLAGDGTTTATVLAQAIVREGAKLVAAGMNPMDLKRGIDLAVAAVVDELKKIAKKVTSSKEIAQVATISANGDESIGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 161 LIAEAMDKVGKEGVITVEDGTGLEDELDVVEGMQFDRGYLSPYFINKPDTGAVELESPFILLADKKISNIREMLPVLEAV 240
Cdd:PRK12850 161 MIAEAMDKVGKEGVITVEEAKTLGTELDVVEGMQFDRGYLSPYFVTNPEKMRAELEDPYILLHEKKISNLQDLLPILEAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 241 AKAGKPLVIIAEDVEGEALATLVVNTMRGIVKVAAVKAPGFGDRRKAMLQDIATLTGGTVISEEIGMELEKATLEDLGQA 320
Cdd:PRK12850 241 VQSGRPLLIIAEDVEGEALATLVVNKLRGGLKSVAVKAPGFGDRRKAMLEDIAVLTGGQVISEDLGIKLENVTLDMLGRA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 321 KRVVINKDTTTIIDGVGEESAIQGRVAQIRKQIEEATSDYDREKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVDDAL 400
Cdd:PRK12850 321 KRVLITKENTTIIDGAGDKKNIEARVKQIRAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKEKKDRVDDAL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 401 HATRAAVEEGVVAGGGVALVRVAAKLAGLTGQNEDQNVGIKVALRAMEAPLRQIVSNAGEEPSVVANNVKAGDGNYGYNA 480
Cdd:PRK12850 401 HATRAAVEEGIVPGGGVALLRARSALRGLKGANADETAGIDIVRRALEEPLRQIATNAGFEGSVVVGKVAELPGNFGFNA 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1993607497 481 ATEEYGNMIDFGILDPTKVTRSALQYAASVAGLMITTECMVTDLPKGDAP 530
Cdd:PRK12850 481 QTGEYGDMVEAGIIDPAKVTRTALQDAASIAALLITTEAMVAEAPKKAAA 530
|
|
| groEL |
PRK12852 |
chaperonin GroEL; Reviewed |
1-530 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237232 Cd Length: 545 Bit Score: 786.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 1 MAAKDVKFGNDARVKMLRGVNVLADAVKVTLGPKGRNVVLDKSFGAPTITKDGVSVAREIELEDKFENMGAQMVKEVASK 80
Cdd:PRK12852 1 MAAKDVKFSGDARDRMLRGVDILANAVKVTLGPKGRNVVIEKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVREVASK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 81 ANDAAGDGTTTATVLAQAIVNEGLKAVAAGMNPMDLKRGIDKAVVAAVEELKALSVPCSDSKAIAQVGTISANSDETVGK 160
Cdd:PRK12852 81 TNDLAGDGTTTATVLAQAIVREGAKAVAAGMNPMDLKRGIDIAVAAVVKDIEKRAKPVASSAEIAQVGTISANGDAAIGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 161 LIAEAMDKVGKEGVITVEDGTGLEDELDVVEGMQFDRGYLSPYFINKPDTGAVELESPFILLADKKISNIREMLPVLEAV 240
Cdd:PRK12852 161 MIAQAMQKVGNEGVITVEENKSLETEVDIVEGMKFDRGYLSPYFVTNAEKMTVELDDAYILLHEKKLSGLQAMLPVLEAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 241 AKAGKPLVIIAEDVEGEALATLVVNTMRGIVKVAAVKAPGFGDRRKAMLQDIATLTGGTVISEEIGMELEKATLEDLGQA 320
Cdd:PRK12852 241 VQSGKPLLIIAEDVEGEALATLVVNRLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGQLISEDLGIKLENVTLKMLGRA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 321 KRVVINKDTTTIIDGVGEESAIQGRVAQIRKQIEEATSDYDREKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVDDAL 400
Cdd:PRK12852 321 KKVVIDKENTTIVNGAGKKADIEARVGQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKEKKDRVEDAL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 401 HATRAAVEEGVVAGGGVALVRVAAKLAGLTGQNEDQNVGIKVALRAMEAPLRQIVSNAGEEPSVVANNVKAG-DGNYGYN 479
Cdd:PRK12852 401 NATRAAVQEGIVPGGGVALLRAKKAVGRINNDNADVQAGINIVLKALEAPIRQIAENAGVEGSIVVGKILENkSETFGFD 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1993607497 480 AATEEYGNMIDFGILDPTKVTRSALQYAASVAGLMITTECMVTDLPKGDAP 530
Cdd:PRK12852 481 AQTEEYVDMVAKGIIDPAKVVRTALQDAASVAGLLVTTEAMVAELPKKDAA 531
|
|
| groEL |
PRK12851 |
chaperonin GroEL; Reviewed |
1-531 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 171770 Cd Length: 541 Bit Score: 782.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 1 MAAKDVKFGNDARVKMLRGVNVLADAVKVTLGPKGRNVVLDKSFGAPTITKDGVSVAREIELEDKFENMGAQMVKEVASK 80
Cdd:PRK12851 1 MAAKEVKFHVEAREKMLRGVNILADAVKVTLGPKGRNVVIDKSFGAPTITNDGVTIAKEIELEDKFENMGAQMVREVASK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 81 ANDAAGDGTTTATVLAQAIVNEGLKAVAAGMNPMDLKRGIDKAVVAAVEELKALSVPCSDSKAIAQVGTISANSDETVGK 160
Cdd:PRK12851 81 TNDVAGDGTTTATVLAQAIVREGAKAVAAGANPMDLKRGIDRAVAAVVEELKANARPVTTNAEIAQVATISANGDAEIGR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 161 LIAEAMDKVGKEGVITVEDGTGLEDELDVVEGMQFDRGYLSPYFINKPDTGAVELESPFILLADKKISNIREMLPVLEAV 240
Cdd:PRK12851 161 LVAEAMEKVGNEGVITVEESKTAETELEVVEGMQFDRGYLSPYFVTDADKMEAELEDPYILIHEKKISNLQDLLPVLEAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 241 AKAGKPLVIIAEDVEGEALATLVVNTMRGIVKVAAVKAPGFGDRRKAMLQDIATLTGGTVISEEIGMELEKATLEDLGQA 320
Cdd:PRK12851 241 VQSGKPLLIIAEDVEGEALATLVVNKLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGIKLENVTLEQLGRA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 321 KRVVINKDTTTIIDGVGEESAIQGRVAQIRKQIEEATSDYDREKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVDDAL 400
Cdd:PRK12851 321 KKVVVEKENTTIIDGAGSKTEIEGRVAQIRAQIEETTSDYDREKLQERLAKLAGGVAVIRVGASTEVEVKEKKDRVDDAL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 401 HATRAAVEEGVVAGGGVALVRVAAKLAGLTGQNEDQNVGIKVALRAMEAPLRQIVSNAGEEPSVVANNVKAGDGNYGYNA 480
Cdd:PRK12851 401 HATRAAVEEGIVPGGGVALLRAVKALDKLETANGDQRTGVEIVRRALEAPVRQIAENAGAEGSVVVGKLREKPGGYGFNA 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1993607497 481 ATEEYGNMIDFGILDPTKVTRSALQYAASVAGLMITTECMVTDLPKGDAPD 531
Cdd:PRK12851 481 ATNEYGDLYAQGVIDPVKVVRTALQNAASVAGLLLTTEAMVAEKPKKEPAP 531
|
|
| GroEL |
COG0459 |
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ... |
2-530 |
0e+00 |
|
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227 Cd Length: 497 Bit Score: 765.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 2 AAKDVKFGNDARVKMLRGVNVLADAVKVTLGPKGRNVVLDKSFGAPTITKDGVSVAREIELEDKFENMGAQMVKEVASKA 81
Cdd:COG0459 1 MAKQILFGEDARRANIRGVKALADAVKVTLGPKGRNVMLVKSFGDPTITNDGVTIAKEIELEDPFENMGAQLVKEVASKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 82 NDAAGDGTTTATVLAQAIVNEGLKAVAAGMNPMDLKRGIDKAVVAAVEELKALSVPCSDSKAIAQVGTISANSDETVGKL 161
Cdd:COG0459 81 NDEAGDGTTTATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPVDDKEELAQVATISANGDEEIGEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 162 IAEAMDKVGKEGVITVEDGTGLEDELDVVEGMQFDRGYLSPYFINKPDTGAVELESPFILLADKKISNIREMLPVLEAVA 241
Cdd:COG0459 161 IAEAMEKVGKDGVITVEEGKGLETELEVVEGMQFDKGYLSPYFVTDPEKMPAELENAYILLTDKKISSIQDLLPLLEKVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 242 KAGKPLVIIAEDVEGEALATLVVNTMRGIVKVAAVKAPGFGDRRKAMLQDIATLTGGTVISEEIGMELEKATLEDLGQAK 321
Cdd:COG0459 241 QSGKPLLIIAEDIDGEALATLVVNGIRGVLRVVAVKAPGFGDRRKAMLEDIAILTGGRVISEDLGLKLEDVTLDDLGRAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 322 RVVINKDTTTIIDGVGEESAIqgrvaqirkqieeatsdydreklqervaklaggvaVIKVGAATEVEMKEKKARVDDALH 401
Cdd:COG0459 321 RVEVDKDNTTIVEGAGNPKAI-----------------------------------VILVGAATEVEVKERKRRVEDALH 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 402 ATRAAVEEGVVAGGGVALVRVAAKLAGLTGQNE-DQNVGIKVALRAMEAPLRQIVSNAGEEPSVVANNVKAG-DGNYGYN 479
Cdd:COG0459 366 ATRAAVEEGIVPGGGAALLRAARALRELAAKLEgDEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKVRAAkDKGFGFD 445
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1993607497 480 AATEEYGNMIDFGILDPTKVTRSALQYAASVAGLMITTECMVTDLPKGDAP 530
Cdd:COG0459 446 AATGEYVDMLEAGVIDPAKVKRSALQNAASVAGLILTTEAVIADKPEKEEA 496
|
|
| PTZ00114 |
PTZ00114 |
Heat shock protein 60; Provisional |
2-530 |
0e+00 |
|
Heat shock protein 60; Provisional
Pssm-ID: 185455 Cd Length: 555 Bit Score: 745.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 2 AAKDVKFGNDARVKMLRGVNVLADAVKVTLGPKGRNVVLDKSFGAPTITKDGVSVAREIELEDKFENMGAQMVKEVASKA 81
Cdd:PTZ00114 13 KGKEIRFGDEARQSLLKGIERLADAVAVTLGPKGRNVIIEQEYGSPKITKDGVTVAKAIEFSDRFENVGAQLIRQVASKT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 82 NDAAGDGTTTATVLAQAIVNEGLKAVAAGMNPMDLKRGIDKAVVAAVEELKALSVPCSDSKAIAQVGTISANSDETVGKL 161
Cdd:PTZ00114 93 NDKAGDGTTTATILARAIFREGCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQSRPVKTKEDILNVATISANGDVEIGSL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 162 IAEAMDKVGKEGVITVEDGTGLEDELDVVEGMQFDRGYLSPYFINKPDTGAVELESPFILLADKKISNIREMLPVLEAVA 241
Cdd:PTZ00114 173 IADAMDKVGKDGTITVEDGKTLEDELEVVEGMSFDRGYISPYFVTNEKTQKVELENPLILVTDKKISSIQSILPILEHAV 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 242 KAGKPLVIIAEDVEGEALATLVVNTMRGIVKVAAVKAPGFGDRRKAMLQDIATLTGGTVISEE-IGMELEKATLEDLGQA 320
Cdd:PTZ00114 253 KNKRPLLIIAEDVEGEALQTLIINKLRGGLKVCAVKAPGFGDNRKDILQDIAVLTGATVVSEDnVGLKLDDFDPSMLGSA 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 321 KRVVINKDTTTIIDGVGEESAIQGRVAQIRKQIEEATSDYDREKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVDDAL 400
Cdd:PTZ00114 333 KKVTVTKDETVILTGGGDKAEIKERVELLRSQIERTTSEYDKEKLKERLAKLSGGVAVIKVGGASEVEVNEKKDRIEDAL 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 401 HATRAAVEEGVVAGGGVALVRVAAKLAGLTGQNE---DQNVGIKVALRAMEAPLRQIVSNAGEEPSVVANNVK-AGDGNY 476
Cdd:PTZ00114 413 NATRAAVEEGIVPGGGVALLRASKLLDKLEEDNEltpDQRTGVKIVRNALRLPTKQIAENAGVEGAVVVEKILeKKDPSF 492
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1993607497 477 GYNAATEEYGNMIDFGILDPTKVTRSALQYAASVAGLMITTECMVTDLPKGDAP 530
Cdd:PTZ00114 493 GYDAQTGEYVNMFEAGIIDPTKVVRSALVDAASVASLMLTTEAAIVDLPKEKKK 546
|
|
| groEL |
CHL00093 |
chaperonin GroEL |
3-528 |
0e+00 |
|
chaperonin GroEL
Pssm-ID: 177025 Cd Length: 529 Bit Score: 681.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 3 AKDVKFGNDARVKMLRGVNVLADAVKVTLGPKGRNVVLDKSFGAPTITKDGVSVAREIELEDKFENMGAQMVKEVASKAN 82
Cdd:CHL00093 2 SKKILYQDNARRALERGMDILAEAVSVTLGPKGRNVVLEKKYGSPQIVNDGVTIAKEIELEDHIENTGVALIRQAASKTN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 83 DAAGDGTTTATVLAQAIVNEGLKAVAAGMNPMDLKRGIDKAVVAAVEELKALSVPCSDSKAIAQVGTISANSDETVGKLI 162
Cdd:CHL00093 82 DVAGDGTTTATVLAYAIVKQGMKNVAAGANPISLKRGIEKATQYVVSQIAEYARPVEDIQAITQVASISAGNDEEVGSMI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 163 AEAMDKVGKEGVITVEDGTGLEDELDVVEGMQFDRGYLSPYFINKPDTGAVELESPFILLADKKISNIR-EMLPVLEAVA 241
Cdd:CHL00093 162 ADAIEKVGREGVISLEEGKSTVTELEITEGMRFEKGFISPYFVTDTERMEVVQENPYILLTDKKITLVQqDLLPILEQVT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 242 KAGKPLVIIAEDVEGEALATLVVNTMRGIVKVAAVKAPGFGDRRKAMLQDIATLTGGTVISEEIGMELEKATLEDLGQAK 321
Cdd:CHL00093 242 KTKRPLLIIAEDVEKEALATLVLNKLRGIVNVVAVRAPGFGDRRKAMLEDIAILTGGQVITEDAGLSLETIQLDLLGQAR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 322 RVVINKDTTTIIdGVGEESAIQGRVAQIRKQIEEATSDYDREKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVDDALH 401
Cdd:CHL00093 322 RIIVTKDSTTII-ADGNEEQVKARCEQLRKQIEIADSSYEKEKLQERLAKLSGGVAVIKVGAATETEMKDKKLRLEDAIN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 402 ATRAAVEEGVVAGGGVALVRVAAKLAGLTGQN--EDQNVGIKVALRAMEAPLRQIVSNAGEEPSVVANNVKAGDGNYGYN 479
Cdd:CHL00093 401 ATKAAVEEGIVPGGGATLVHLSENLKTWAKNNlkEDELIGALIVARAILAPLKRIAENAGKNGSVIIEKVQEQDFEIGYN 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1993607497 480 AATEEYGNMIDFGILDPTKVTRSALQYAASVAGLMITTECMVTDLPKGD 528
Cdd:CHL00093 481 AANNKFVNMYEAGIIDPAKVTRSALQNAASIASMILTTECIIVDKKESS 529
|
|
| PRK14104 |
PRK14104 |
chaperonin GroEL; Provisional |
1-529 |
0e+00 |
|
chaperonin GroEL; Provisional
Pssm-ID: 172594 Cd Length: 546 Bit Score: 665.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 1 MAAKDVKFGNDARVKMLRGVNVLADAVKVTLGPKGRNVVLDKSFGAPTITKDGVSVAREIELEDKFENMGAQMVKEVASK 80
Cdd:PRK14104 1 MSAKEVKFGVDARDRMLRGVDILANAVKVTLGPKGRNVVLDKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVREVASK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 81 ANDAAGDGTTTATVLAQAIVNEGLKAVAAGMNPMDLKRGIDKAVVAAVEELKALSVPCSDSKAIAQVGTISANSDETVGK 160
Cdd:PRK14104 81 SADAAGDGTTTATVLAQAIVREGAKSVAAGMNPMDLKRGIDLAVEAVVADLVKNSKKVTSNDEIAQVGTISANGDAEIGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 161 LIAEAMDKVGKEGVITVEDGTGLEDELDVVEGMQFDRGYLSPYFINKPDTGAVELESPFILLADKKISNIREMLPVLEAV 240
Cdd:PRK14104 161 FLADAMKKVGNEGVITVEEAKSLETELDVVEGMQFDRGYISPYFVTNADKMRVEMDDAYILINEKKLSSLNELLPLLEAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 241 AKAGKPLVIIAEDVEGEALATLVVNTMRGIVKVAAVKAPGFGDRRKAMLQDIATLTGGTVISEEIGMELEKATLEDLGQA 320
Cdd:PRK14104 241 VQTGKPLVIVAEDVEGEALATLVVNRLRGGLKVAAVKAPGFGDRRKAMLQDIAILTGGQAISEDLGIKLENVTLQMLGRA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 321 KRVVINKDTTTIIDGVGEESAIQGRVAQIRKQIEEATSDYDREKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVDDAL 400
Cdd:PRK14104 321 KKVMIDKENTTIVNGAGKKADIEARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKERKDRVDDAM 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 401 HATRAAVEEGVVAGGGVALVRVAAKLAGLTGQNEDQNVGIKVALRAMEAPLRQIVSNAGEEPSVVANNVKAGDG-NYGYN 479
Cdd:PRK14104 401 HATRAAVEEGIVPGGGVALLRASEQLKGIKTKNDDQKTGVEIVRKALSAPARQIAINAGEDGSVIVGKILEKEQySYGFD 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1993607497 480 AATEEYGNMIDFGILDPTKVTRSALQYAASVAGLMITTECMVTDLPKGDA 529
Cdd:PRK14104 481 SQTGEYGNLVSKGIIDPTKVVRTAIQNAASVAALLITTEAMVAELPKKGG 530
|
|
| PLN03167 |
PLN03167 |
Chaperonin-60 beta subunit; Provisional |
2-526 |
0e+00 |
|
Chaperonin-60 beta subunit; Provisional
Pssm-ID: 215611 [Multi-domain] Cd Length: 600 Bit Score: 549.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 2 AAKDVKFGND--ARVKMLRGVNVLADAVKVTLGPKGRNVVLDKSFGAPTITKDGVSVAREIELEDKFENMGAQMVKEVAS 79
Cdd:PLN03167 55 AAKELHFNKDgsAIKKLQAGVNKLADLVGVTLGPKGRNVVLESKYGSPKIVNDGVTVAKEVELEDPVENIGAKLVRQAAA 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 80 KANDAAGDGTTTATVLAQAIVNEGLKAVAAGMNPMDLKRGIDKAVVAAVEELKALSVPCSDSKaIAQVGTISANSDETVG 159
Cdd:PLN03167 135 KTNDLAGDGTTTSVVLAQGLIAEGVKVVAAGANPVQITRGIEKTAKALVKELKKMSKEVEDSE-LADVAAVSAGNNYEVG 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 160 KLIAEAMDKVGKEGVITVEDGTGLEDELDVVEGMQFDRGYLSPYFINKPDTGAVELESPFILLADKKISNIREMLPVLEA 239
Cdd:PLN03167 214 NMIAEAMSKVGRKGVVTLEEGKSAENNLYVVEGMQFDRGYISPYFVTDSEKMSVEYDNCKLLLVDKKITNARDLIGILED 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 240 VAKAGKPLVIIAEDVEGEALATLVVNTMRGIVKVAAVKAPGFGDRRKAMLQDIATLTGGTVISEEIGMELEKATLEDLGQ 319
Cdd:PLN03167 294 AIRGGYPLLIIAEDIEQEALATLVVNKLRGSLKIAALKAPGFGERKSQYLDDIAILTGGTVIREEVGLSLDKVGKEVLGT 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 320 AKRVVINKDTTTIIDGVGEESAIQGRVAQIRKQIEEATSDYDREKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVDDA 399
Cdd:PLN03167 374 AAKVVLTKDTTTIVGDGSTQEAVNKRVAQIKNLIEAAEQDYEKEKLNERIAKLSGGVAVIQVGAQTETELKEKKLRVEDA 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 400 LHATRAAVEEGVVAGGGVALVRVAAKLAGL--TGQNEDQNVGIKVALRAMEAPLRQIVSNAGEEPSVVANNVKAGDG-NY 476
Cdd:PLN03167 454 LNATKAAVEEGIVVGGGCTLLRLASKVDAIkdTLENDEQKVGADIVKRALSYPLKLIAKNAGVNGSVVSEKVLSNDNpKF 533
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1993607497 477 GYNAATEEYGNMIDFGILDPTKVTRSALQYAASVAGLMITTECMVTDLPK 526
Cdd:PLN03167 534 GYNAATGKYEDLMAAGIIDPTKVVRCCLEHAASVAKTFLTSDCVVVEIKE 583
|
|
| chaperonin_type_I_II |
cd00309 |
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ... |
4-522 |
8.91e-153 |
|
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: 445.33 E-value: 8.91e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 4 KDVKFGNDARVKMLRGVNVLADAVKVTLGPKGRNVVLDKSFGAPTITKDGVSVAREIELEdkfeNMGAQMVKEVASKAND 83
Cdd:cd00309 1 KEREFGEEARLSNINAAKALADAVKTTLGPKGMDKMLVDSLGDPTITNDGATILKEIEVE----HPAAKLLVEVAKSQDD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 84 AAGDGTTTATVLAQAIVNEGLKAVAAGMNPMDLKRGIDKAVVAAVEELKALSVP--CSDSKAIAQVGTISANS------D 155
Cdd:cd00309 77 EVGDGTTTVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVPidVEDREELLKVATTSLNSklvsggD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 156 ETVGKLIAEAMDKVGKE------GVITVEDGTG---LEDELdvVEGMQFDRGYLSPYFInkpdtgaVELESPFILLADKK 226
Cdd:cd00309 157 DFLGELVVDAVLKVGKEngdvdlGVIRVEKKKGgslEDSEL--VVGMVFDKGYLSPYMP-------KRLENAKILLLDCK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 227 ISNiremlpvleavakagkplVIIAED-VEGEALATLVVNtmrgivKVAAVKApgfgdRRKAMLQDIATLTGGTVISeei 305
Cdd:cd00309 228 LEY------------------VVIAEKgIDDEALHYLAKL------GIMAVRR-----VRKEDLERIAKATGATIVS--- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 306 gmELEKATLEDLGQAKRVVINK----DTTTIIDGVGeesaiqgrvaqirkqieeatsdydreklqervaklaGGVAVIKV 381
Cdd:cd00309 276 --RLEDLTPEDLGTAGLVEETKigdeKYTFIEGCKG------------------------------------GKVATILL 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 382 GAATEVEMKEKKARVDDALHATRAAVEE-GVVAGGGVALVRVAAKLAGL-TGQNEDQNVGIKVALRAMEAPLRQIVSNAG 459
Cdd:cd00309 318 RGATEVELDEAERSLHDALCAVRAAVEDgGIVPGGGAAEIELSKALEELaKTLPGKEQLGIEAFADALEVIPRTLAENAG 397
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1993607497 460 EEPSVVANNVKA----GDGNYGYNAATEEYGNMIDFGILDPTKVTRSALQYAASVAGLMITTECMVT 522
Cdd:cd00309 398 LDPIEVVTKLRAkhaeGGGNAGGDVETGEIVDMKEAGIIDPLKVKRQALKSATEAASLILTIDDIIV 464
|
|
| Cpn60_TCP1 |
pfam00118 |
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ... |
23-521 |
1.59e-78 |
|
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: 255.20 E-value: 1.59e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 23 LADAVKVTLGPKGRNVVLDKSFGAPTITKDGVSVAREIELEDKfenmGAQMVKEVASKANDAAGDGTTTATVLAQAIVNE 102
Cdd:pfam00118 1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELEIQHP----AAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 103 GLKAVAAGMNPMDLKRGIDKAVVAAVEELKA-LSVPCS--DSKAIAQVGTISANSD------ETVGKLIAEA-------- 165
Cdd:pfam00118 77 AEKLLAAGVHPTTIIEGYEKALEKALEILDSiISIPVEdvDREDLLKVARTSLSSKiisresDFLAKLVVDAvlaipknd 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 166 -MDKVGKEGVITVEdGTGLEDeLDVVEGMQFDRGYLSPYFINKpdtgaveLESPFILLADKKISNIRE------------ 232
Cdd:pfam00118 157 gSFDLGNIGVVKIL-GGSLED-SELVDGVVLDKGPLHPDMPKR-------LENAKVLLLNCSLEYEKTetkatvvlsdae 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 233 ------------MLPVLEAVAKAGKPLVIIAEDVEGEALATLVVNTMRGIVKVaavkapgfgdrRKAMLQDIATLTGGTV 300
Cdd:pfam00118 228 qlerflkaeeeqILEIVEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMALRRV-----------KKRDLERLAKATGARA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 301 ISeeigmELEKATLEDLGQAKRV---VINKDTTTIIDGVGEesaiqgrvaqirkqieeatsdydreklqervaklaGGVA 377
Cdd:pfam00118 297 VS-----SLDDLTPDDLGTAGKVeeeKIGDEKYTFIEGCKS-----------------------------------PKAA 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 378 VIKVGAATEVEMKEKKARVDDALHATRAAVEE-GVVAGGGVALVRVAAKLAGL-TGQNEDQNVGIKVALRAMEAPLRQIV 455
Cdd:pfam00118 337 TILLRGATDHVLDEIERSIHDALCVVKNAIEDpRVVPGGGAVEMELARALREYaKSVSGKEQLAIEAFAEALEVIPKTLA 416
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 456 SNAGEEPSVVANNVKA----GDGNYGYNAATEEYGNMIDFGILDPTKVTRSALQYAASVAGLMITTECMV 521
Cdd:pfam00118 417 ENAGLDPIEVLAELRAahasGEKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKSATEAASTILRIDDII 486
|
|
| chaperonin_like |
cd03333 |
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ... |
142-409 |
2.73e-42 |
|
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: 150.31 E-value: 2.73e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 142 KAIAQVGTISANS-----DETVGKLIAEAMDKVGKE------GVITVEDGTG---LEDELdvVEGMQFDRGYLSPYFInk 207
Cdd:cd03333 2 ELLLQVATTSLNSklsswDDFLGKLVVDAVLKVGPDnrmddlGVIKVEKIPGgslEDSEL--VVGVVFDKGYASPYMP-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 208 pdtgaVELESPFILLADKKISNiremlpvleavakagkplVIIAED-VEGEALATLVVNtmrgivKVAAVKApgfgdRRK 286
Cdd:cd03333 78 -----KRLENAKILLLDCPLEY------------------VVIAEKgIDDLALHYLAKA------GIMAVRR-----VKK 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 287 AMLQDIATLTGGTVISeeigmELEKATLEDLGQAKRVVINK---DTTTIIDGVGEesaiqgrvaqirkqieeatsdydre 363
Cdd:cd03333 124 EDLERIARATGATIVS-----SLEDLTPEDLGTAELVEETKigeEKLTFIEGCKG------------------------- 173
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1993607497 364 klqervaklaGGVAVIKVGAATEVEMKEKKARVDDALHATRAAVEE 409
Cdd:cd03333 174 ----------GKAATILLRGATEVELDEVKRSLHDALCAVRAAVEE 209
|
|
| cpn60 |
cd03343 |
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ... |
9-515 |
6.04e-24 |
|
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: 105.42 E-value: 6.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 9 GNDARVKMLRGVNVLADAVKVTLGPKGRNVVLDKSFGAPTITKDGVSVAREIELedkfENMGAQMVKEVASKANDAAGDG 88
Cdd:cd03343 13 GRDAQRMNIAAAKAVAEAVRTTLGPKGMDKMLVDSLGDVTITNDGATILKEMDI----EHPAAKMLVEVAKTQDEEVGDG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 89 TTTATVLAQAIVNEGLKAVAAGMNPMDLKRGIDKAVVAAVEELKALSVPCSDS-----KAIAQVGTISANSDETVGKLIA 163
Cdd:cd03343 89 TTTAVVLAGELLEKAEDLLDQNIHPTVIIEGYRLAAEKALELLDEIAIKVDPDdkdtlRKIAKTSLTGKGAEAAKDKLAD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 164 EAMDKV--------GKEGV----ITVEDGTGLE-DELDVVEGMQFDRGYL-----------------SPYFINKPDTGA- 212
Cdd:cd03343 169 LVVDAVlqvaekrdGKYVVdldnIKIEKKTGGSvDDTELIRGIVIDKEVVhpgmpkrvenakialldAPLEVKKTEIDAk 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 213 VELESPFILLA--DKKISNIREMlpvLEAVAKAGKPLVIIAEDVEGEALATLvvnTMRGIVKVAAVKapgfgdrrKAMLQ 290
Cdd:cd03343 249 IRITSPDQLQAflEQEEAMLKEM---VDKIADTGANVVFCQKGIDDLAQHYL---AKAGILAVRRVK--------KSDME 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 291 DIATLTGGTVISeeigmELEKATLEDLGQAKRVVINKdtttiidgVGEESAIqgrvaqirkQIEEatsdydreklqervA 370
Cdd:cd03343 315 KLARATGAKIVT-----NIDDLTPEDLGEAELVEERK--------VGDDKMV---------FVEG--------------C 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 371 KLAGGVAVIKVGaATEVEMKEKKARVDDALHATRAAVEEG-VVAGGGVALVRVAAKLagltgQNEDQNVGIKVAL----- 444
Cdd:cd03343 359 KNPKAVTILLRG-GTEHVVDELERALEDALRVVADALEDGkVVAGGGAVEIELAKRL-----REYARSVGGREQLaveaf 432
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1993607497 445 -RAMEAPLRQIVSNAGEEPSVVANNVKA----GDGNYGYNAATEEYGNMIDFGILDPTKVTRSALQyAASVAGLMI 515
Cdd:cd03343 433 aDALEEIPRTLAENAGLDPIDTLVELRAahekGNKNAGLDVYTGEVVDMLEKGVIEPLRVKKQAIK-SATEAATMI 507
|
|
| TCP1_delta |
cd03338 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ... |
10-508 |
2.06e-14 |
|
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: 75.79 E-value: 2.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 10 NDARVKMLRGVNVLADAVKVTLGPKGRNVVLDKSFGAPTITKDGVSVAREIELEdkfeNMGAQMVKEVaSKAND-AAGDG 88
Cdd:cd03338 7 ADVRLSNIQAAKAVADAIRTSLGPRGMDKMIQTGKGEVIITNDGATILKQMSVL----HPAAKMLVEL-SKAQDiEAGDG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 89 TTTATVLAQAIVNEGLKAVAAGMNPMDLKRGIDKAVVAAVEELKALSVPCS--DSKAIAQVGTISANS------DETVGK 160
Cdd:cd03338 82 TTSVVVLAGALLSACESLLKKGIHPTVISESFQIAAKKAVEILDSMSIPVDlnDRESLIKSATTSLNSkvvsqySSLLAP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 161 LIAEAMDKVGKEGVITVED-----------GTGLEDELdvVEGM----QFDRGYLSPYFINKPDTGAV---------ELE 216
Cdd:cd03338 162 IAVDAVLKVIDPATATNVDlkdirivkklgGTIEDTEL--VDGLvftqKASKKAGGPTRIEKAKIGLIqfclsppktDMD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 217 SPFIL----LADKKISNIRE-MLPVLEAVAKAGKPLVIIAEDVEGEALATLVVNTMRGIvKVAAVKapgfgDRRKAMLQD 291
Cdd:cd03338 240 NNIVVndyaQMDRILREERKyILNMCKKIKKSGCNVLLIQKSILRDAVSDLALHFLAKL-KIMVVK-----DIEREEIEF 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 292 IATLTGGTVISeeigmELEKATLEDLGQAKRVvinkdtttiidgvgeesaiqgrvaqirkqiEEATSDYDREKLQERVAK 371
Cdd:cd03338 314 ICKTIGCKPVA-----SIDHFTEDKLGSADLV------------------------------EEVSLGDGKIVKITGVKN 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 372 LAGGVAVIkVGAATEVEMKEKKARVDDALHATRAAVEE-GVVAGGGVALVRVAAKLAGLTGQNEDQNV-GIKVALRAMEA 449
Cdd:cd03338 359 PGKTVTIL-VRGSNKLVLDEAERSLHDALCVIRCLVKKrALIPGGGAPEIEIALQLSEWARTLTGVEQyCVRAFADALEV 437
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1993607497 450 PLRQIVSNAGEEP-SVVA---NNVKAGDGNYGYNAATEEYGNMIDFGILDPTKVTRSALQYAA 508
Cdd:cd03338 438 IPYTLAENAGLNPiSIVTelrNRHAQGEKNAGINVRKGAITNILEENVVQPLLVSTSAITLAT 500
|
|
| chap_CCT_eta |
TIGR02345 |
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ... |
17-515 |
4.12e-12 |
|
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: 68.63 E-value: 4.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 17 LRGVNVLADAVKVTLGPKGRNVVLDKSFGAPTITKDGVSVAREIELedkfENMGAQMVKEVASKANDAAGDGTTTATVLA 96
Cdd:TIGR02345 24 INACVAIAEALKTTLGPRGMDKLIVGSNGKATISNDGATILKLLDI----VHPAAKTLVDIAKSQDAEVGDGTTSVTILA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 97 QAIVNEGLKAVAAGMNPMDLKRGIDKAVVAAVEELKALSVPCSDSK-----------AIAQVGTISANSDETVGKLIAEA 165
Cdd:TIGR02345 100 GELLKEAKPFIEEGVHPQLIIRCYREALSLAVEKIKEIAVTIDEEKgeqrellekcaATALSSKLISHNKEFFSKMIVDA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 166 MDKVGKE-------GVITVEDGTgLEDELdVVEGMQFDRGYLSPYFINKPdtgavelespfilladKKISNIREMLPVLE 238
Cdd:TIGR02345 180 VLSLDRDdldlkliGIKKVQGGA-LEDSQ-LVNGVAFKKTFSYAGFEQQP----------------KKFANPKILLLNVE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 239 AVAKAGKPLV-IIAEDVEG-----EALATLVVNTMRGIV----KVAAVKAPgFGDRRKAMLQDIATLTGGTVISEEIgme 308
Cdd:TIGR02345 242 LELKAEKDNAeIRVEDVEDyqaivDAEWAIIFRKLEKIVesgaNVVLSKLP-IGDLATQYFADRDIFCAGRVSAEDL--- 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 309 lekatledlgqaKRVVinkdtttiiDGVGeeSAIQGRVAQIRKQIEEATSDYDREKL-QERVAKLAGG-----VAVIKVG 382
Cdd:TIGR02345 318 ------------KRVI---------KACG--GSIQSTTSDLEADVLGTCALFEERQIgSERYNYFTGCphaktCTIILRG 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 383 AATEVeMKEKKARVDDALHATRAAVE-EGVVAGGGVALVRVAAKLAGLTGQNEDQNVGIKVAL-RAMEAPLRQIVSNAGE 460
Cdd:TIGR02345 375 GAEQF-IEEAERSLHDAIMIVRRALKnKKIVAGGGAIEMELSKCLRDYSKTIDGKQQLIINAFaKALEIIPRQLCENAGF 453
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1993607497 461 EPSVVANNVKA----GDGNYGYNAATEEYGNMIDFGILDPTKVTRSALQYAASVAGLMI 515
Cdd:TIGR02345 454 DSIEILNKLRSrhakGGKWYGVDINTEDIGDNFEAFVWEPALVKINALKAAFEAACTIL 512
|
|
| TCP1_beta |
cd03336 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ... |
9-143 |
7.70e-12 |
|
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.
Pssm-ID: 239452 [Multi-domain] Cd Length: 517 Bit Score: 67.74 E-value: 7.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 9 GNDARVKMLRGVNVLADAVKVTLGPKGRNVVL--DKSFGAPTITKDGVSVAREIELEdkfeNMGAQMVKEVASKANDAAG 86
Cdd:cd03336 11 GETARLSSFVGAIAIGDLVKTTLGPKGMDKILqsVGRSGGVTVTNDGATILKSIGVD----NPAAKVLVDISKVQDDEVG 86
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1993607497 87 DGTTTATVLAQAIVNEGLKAVAAGMNPMDLKRGIDKAVVAAVEELKALSVPCSDSKA 143
Cdd:cd03336 87 DGTTSVTVLAAELLREAEKLVAQKIHPQTIIEGYRMATAAAREALLSSAVDHSSDEE 143
|
|
| chap_CCT_delta |
TIGR02342 |
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ... |
10-507 |
2.57e-11 |
|
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: 65.96 E-value: 2.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 10 NDARVKMLRGVNVLADAVKVTLGPKGRNVVLDKSFGAPTITKDGVSVAREIELEdkfeNMGAQMVKEVaSKAND-AAGDG 88
Cdd:TIGR02342 8 QDVRTSNIVAAKAVADAIRTSLGPKGMDKMIQDGKGEVIITNDGATILKQMAVL----HPAAKMLVEL-SKAQDiEAGDG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 89 TTTATVLAQAIVNEGLKAVAAGMNPMDLKRGIDKAVVAAVEELKALSVPC--SDSKAIAQVGTISANSD----------- 155
Cdd:TIGR02342 83 TTSVVILAGALLGACERLLNKGIHPTIISESFQSAADEAIKILDEMSIPVdlSDREQLLKSATTSLSSKvvsqyssllap 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 156 ---ETVGKLIAEAMDK-VGKEGVITVEDGTGLEDELDVVEGMQFDRGYL----SPYFINKPDTGAVElespFILLADKK- 226
Cdd:TIGR02342 163 lavDAVLKVIDPENAKnVDLNDIKVVKKLGGTIDDTELIEGLVFTQKASksagGPTRIEKAKIGLIQ----FQISPPKTd 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 227 ------ISNIREM-----------LPVLEAVAKAGKPLVIIAEDVEGEALATLVVNTMRGIvKVAAVKapgfgDRRKAML 289
Cdd:TIGR02342 239 menqiiVNDYAQMdrvlkeerayiLNIVKKIKKTGCNVLLIQKSILRDAVNDLALHFLAKM-KIMVVK-----DIEREEI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 290 QDIATLTGGTVISeeigmELEKATLEDLGQAKRVvinkdtttiidgvgeesaiqgrvaqirkqiEEATSDYDREKLQERV 369
Cdd:TIGR02342 313 EFICKTIGCKPIA-----SIDHFTADKLGSAELV------------------------------EEVDSDGGKIIKITGI 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 370 AKLAGGVAVIKVGaATEVEMKEKKARVDDALHATRAAVEE-GVVAGGGVALVRVAAKLAGLTGQNEDQNVGIKVAL-RAM 447
Cdd:TIGR02342 358 QNAGKTVTVVVRG-SNKLVIDEAERSLHDALCVIRCLVKKrGLIAGGGAPEIEIARRLSKYARTMKGVESYCVRAFaDAL 436
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1993607497 448 EAPLRQIVSNAGEEP-SVVA---NNVKAGDGNYGYNAATEEYGNMIDFGILDPTKVTRSALQYA 507
Cdd:TIGR02342 437 EVIPYTLAENAGLNPiKVVTelrNRHANGEKTAGISVRKGGITNMLEEHVLQPLLVTTSAITLA 500
|
|
| TCP1_eta |
cd03340 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ... |
22-137 |
1.74e-10 |
|
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.
Pssm-ID: 239456 [Multi-domain] Cd Length: 522 Bit Score: 63.46 E-value: 1.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 22 VLADAVKVTLGPKGRNVVLDKSFGAPTITKDGVSVAREIELEdkfeNMGAQMVKEVASKANDAAGDGTTTATVLAQAIVN 101
Cdd:cd03340 27 AIADAVRTTLGPRGMDKLIVDGRGKVTISNDGATILKLLDIV----HPAAKTLVDIAKSQDAEVGDGTTSVVVLAGEFLK 102
|
90 100 110
....*....|....*....|....*....|....*.
gi 1993607497 102 EGLKAVAAGMNPMDLKRGIDKAVVAAVEELKALSVP 137
Cdd:cd03340 103 EAKPFIEDGVHPQIIIRGYRKALQLAIEKIKEIAVN 138
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
9-136 |
2.27e-10 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 63.12 E-value: 2.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 9 GNDARVKMLRGVNVLADAVKVTLGPKGRNVVLDKSFGAP-----TITKDGVSVAREIELEdkfeNMGAQMVKEVASKAND 83
Cdd:PTZ00212 20 GETARLQSFVGAIAVADLVKTTLGPKGMDKILQPMSEGPrsgnvTVTNDGATILKSVWLD----NPAAKILVDISKTQDE 95
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1993607497 84 AAGDGTTTATVLAQAIVNEGLKAVAAGMNPMDLKRGIDKAVVAAVEELKALSV 136
Cdd:PTZ00212 96 EVGDGTTSVVVLAGELLREAEKLLDQKIHPQTIIEGWRMALDVARKALEEIAF 148
|
|
| chap_CCT_epsi |
TIGR02343 |
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ... |
9-141 |
2.52e-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: 62.90 E-value: 2.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 9 GNDARVKMLRGVNVLADAVKVTLGPKGRNVVLDKSFGAPTITKDGVSVAREIELEDKFenmgAQMVKEVASKANDAAGDG 88
Cdd:TIGR02343 25 GLEAKKSNIAAAKSVASILRTSLGPKGMDKMLISPDGDITVTNDGATILSQMDVDNQI----AKLMVELSKSQDDEIGDG 100
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1993607497 89 TTTATVLAQAIVNEGLKAVAAGMNPMDLKRGIDKAVVAAVEELKALSVPCSDS 141
Cdd:TIGR02343 101 TTGVVVLAGALLEQAEELLDKGIHPIKIADGFEEAARIAVEHLEEISDEISAD 153
|
|
| chap_CCT_beta |
TIGR02341 |
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ... |
9-143 |
4.86e-10 |
|
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT beta chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.
Pssm-ID: 274082 Cd Length: 519 Bit Score: 61.80 E-value: 4.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 9 GNDARVKMLRGVNVLADAVKVTLGPKGRNVVL--DKSFGAPTITKDGVSVAREIELEdkfeNMGAQMVKEVASKANDAAG 86
Cdd:TIGR02341 12 AENARLSSFVGAIAIGDLVKSTLGPKGMDKILqsSSSDASIMVTNDGATILKSIGVD----NPAAKVLVDMSKVQDDEVG 87
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1993607497 87 DGTTTATVLAQAIVNEGLKAVAAGMNPMDLKRGIDKAVVAAVEELKALSVPCSDSKA 143
Cdd:TIGR02341 88 DGTTSVTVLAAELLREAEKLINQKIHPQTIIAGYREATKAARDALLKSAVDNGSDEV 144
|
|
| TCP1_epsilon |
cd03339 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ... |
23-142 |
1.53e-08 |
|
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.
Pssm-ID: 239455 Cd Length: 526 Bit Score: 57.31 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 23 LADAVKVTLGPKGRNVVLDKSFGAPTITKDGVSVAREIELEdkfeNMGAQMVKEVASKANDAAGDGTTTATVLAQAIVNE 102
Cdd:cd03339 35 VANILRTSLGPRGMDKILVSPDGEVTVTNDGATILEKMDVD----HQIAKLLVELSKSQDDEIGDGTTGVVVLAGALLEQ 110
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1993607497 103 GLKAVAAGMNPMDLKRGIDKAVVAAVEELKALSVPCSDSK 142
Cdd:cd03339 111 AEKLLDRGIHPIRIADGYEQACKIAVEHLEEIADKIEFSP 150
|
|
| chap_CCT_alpha |
TIGR02340 |
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ... |
9-113 |
5.45e-08 |
|
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: 55.50 E-value: 5.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 9 GNDARVKMLRGVNVLADAVKVTLGPKGRNVVLDKSFGAPTITKDGVSVAREIELEDKfenmGAQMVKEVASKANDAAGDG 88
Cdd:TIGR02340 10 GQDVRTQNVTAAMAIANIVKTSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHP----AAKILVELAQLQDREVGDG 85
|
90 100
....*....|....*....|....*
gi 1993607497 89 TTTATVLAQAIVNEGLKAVAAGMNP 113
Cdd:TIGR02340 86 TTSVVIIAAELLKRADELVKNKIHP 110
|
|
| TCP1_zeta |
cd03342 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
23-137 |
1.29e-06 |
|
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.
Pssm-ID: 239458 [Multi-domain] Cd Length: 484 Bit Score: 51.10 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 23 LADAVKVTLGPKGRNVVLDKSFGAPTITKDGVSVAREIEledkFENMGAQMVKEVASKANDAAGDGTTTATVLAQAIVNE 102
Cdd:cd03342 24 LQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLSEMQ----IQHPTASMIARAATAQDDITGDGTTSNVLLIGELLKQ 99
|
90 100 110
....*....|....*....|....*....|....*
gi 1993607497 103 GLKAVAAGMNPMDLKRGIDKAVVAAVEELKALSVP 137
Cdd:cd03342 100 AERYIQEGVHPRIITEGFELAKNKALKFLESFKVP 134
|
|
| TCP1_gamma |
cd03337 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ... |
23-189 |
2.43e-06 |
|
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: 49.99 E-value: 2.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 23 LADAVKVTLGPKGR-NVVLDKSfGAPTITKDGVSVAREIELEdkfeNMGAQMVKEVASKANDAAGDGTTTATVLAQAIVN 101
Cdd:cd03337 28 VADVIRTCLGPRAMlKMLLDPM-GGIVLTNDGNAILREIDVA----HPAAKSMIELSRTQDEEVGDGTTSVIILAGEILA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 102 EGLKAVAAGMNPMDLKRGIDKAVVAAVEELKALSVPCsDSKAIAQVGTISANSDETvgKLIAEAMDKVGK---EGVITVE 178
Cdd:cd03337 103 VAEPFLERGIHPTVIIKAYRKALEDALKILEEISIPV-DVNDRAQMLKIIKSCIGT--KFVSRWSDLMCNlalDAVKTVA 179
|
170
....*....|..
gi 1993607497 179 DGT-GLEDELDV 189
Cdd:cd03337 180 VEEnGRKKEIDI 191
|
|
| chap_CCT_zeta |
TIGR02347 |
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ... |
23-136 |
2.60e-06 |
|
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: 50.12 E-value: 2.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 23 LADAVKVTLGPKGRNVVLDKSFGAPTITKDGVSVAREIELEdkfeNMGAQMVKEVASKANDAAGDGTTTATVLAQAIVNE 102
Cdd:TIGR02347 28 LQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEMQIQ----HPTASMIARAATAQDDITGDGTTSTVLLIGELLKQ 103
|
90 100 110
....*....|....*....|....*....|....
gi 1993607497 103 GLKAVAAGMNPMDLKRGIDKAVVAAVEELKALSV 136
Cdd:TIGR02347 104 AERYILEGVHPRIITEGFEIARKEALQFLDKFKV 137
|
|
| TCP1_alpha |
cd03335 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ... |
9-113 |
6.29e-06 |
|
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: 48.82 E-value: 6.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 9 GNDARVKMLRGVNVLADAVKVTLGPKGRNVVLDKSFGAPTITKDGVSVAREIELEDKfenmGAQMVKEVASKANDAAGDG 88
Cdd:cd03335 6 GQDVRTQNVTAAMAIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHP----AAKILVELAQLQDKEVGDG 81
|
90 100
....*....|....*....|....*
gi 1993607497 89 TTTATVLAQAIVNEGLKAVAAGMNP 113
Cdd:cd03335 82 TTSVVIIAAELLKRANELVKQKIHP 106
|
|
| chap_CCT_theta |
TIGR02346 |
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ... |
11-136 |
1.07e-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: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 11 DARVKMLRGVNVLADAVKVTLGPKGRNVV----LDKSFgaptITKDGVSVAREIELEdkfeNMGAQMVKEVASKANDAAG 86
Cdd:TIGR02346 18 EAVIKNIEACKELSQITRTSLGPNGMNKMvinhLEKLF----VTNDAATILRELEVQ----HPAAKLLVMASEMQENEIG 89
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1993607497 87 DGTTTATVLAQAIVNEGLKAVAAGMNPMDLKRGIDKAVVAAVEELKALSV 136
Cdd:TIGR02346 90 DGTNLVLVLAGELLNKAEELIRMGLHPSEIIKGYEMALKKAMEILEELVV 139
|
|
| chap_CCT_gamma |
TIGR02344 |
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ... |
23-162 |
1.87e-05 |
|
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: 47.43 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 23 LADAVKVTLGPKGRNVVLDKSFGAPTITKDGVSVAREIELedkfENMGAQMVKEVASKANDAAGDGTTTATVLAQAIVNE 102
Cdd:TIGR02344 28 VADIIRTCLGPRSMLKMLLDPMGGIVMTNDGNAILREIDV----AHPAAKSMIELSRTQDEEVGDGTTSVIILAGEMLSV 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 103 GLKAVAAGMNPMDLKRGIDKAVVAAVEELKALSVPcsdskaiaqvgtISANSDETVGKLI 162
Cdd:TIGR02344 104 AEPFLEQNIHPTVIIRAYRKALDDALSVLEEISIP------------VDVNDDAAMLKLI 151
|
|
| TCP1_theta |
cd03341 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ... |
23-136 |
1.28e-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: 44.52 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993607497 23 LADAVKVTLGPKGRN--VV--LDKSFgaptITKDGVSVAREIEledkFENMGAQMVKEvASKANDA-AGDGTTTATVLAQ 97
Cdd:cd03341 20 LSQITRTSYGPNGMNkmVInhLEKLF----VTSDAATILRELE----VQHPAAKLLVM-ASQMQEEeIGDGTNLVVVLAG 90
|
90 100 110
....*....|....*....|....*....|....*....
gi 1993607497 98 AIVNEGLKAVAAGMNPMDLKRGIDKAVVAAVEELKALSV 136
Cdd:cd03341 91 ELLEKAEELLRMGLHPSEIIEGYEKALKKALEILEELVV 129
|
|
| |
