|
Name |
Accession |
Description |
Interval |
E-value |
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
1-527 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 959.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 1 MAKDLKFSEDARQAMLRGVDKLANAVKVTIGPKGRNVVLDKDYTTPLITNDGVTIAKEIELEDPYENMGAKLVQEVANKT 80
Cdd:PRK00013 1 MAKDIKFGEDARRKLLRGVNKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDPFENMGAQLVKEVASKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 81 NEIAGDGTTTATVLAQSMIQEGLKNVTSGANPVGLRQGIDKAVQVAIEALHEISQKVENKNEIAQVGAISA-ADEEIGRY 159
Cdd:PRK00013 81 NDVAGDGTTTATVLAQAIVREGLKNVAAGANPMDLKRGIDKAVEAAVEELKKISKPVEDKEEIAQVATISAnGDEEIGKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 160 ISEAMDKVGNDGVITIEESNGFNTELEVVEGMQFDRGYQSPYMVTDSDKMIAELERPYILVTDKKITSFQDILPLLEQVV 239
Cdd:PRK00013 161 IAEAMEKVGKEGVITVEESKGFETELEVVEGMQFDRGYLSPYFVTDPEKMEAELENPYILITDKKISNIQDLLPVLEQVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 240 QSSRPILIVADEVEGDALTNIVLNRMRGTFTAVAVKAPGFGDRRKAMLEDLAILTGAQVITDDLGLELKDASLDMLGTAN 319
Cdd:PRK00013 241 QSGKPLLIIAEDVEGEALATLVVNKLRGTLKVVAVKAPGFGDRRKAMLEDIAILTGGTVISEELGLKLEDATLEDLGQAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 320 KVEVTKDHTTVVDGNGDENNIDARVGQIKAQIEETDSEFDKEKLQERLAKLAGGVAVIKVGAASETELKERKLRIEDALN 399
Cdd:PRK00013 321 KVVVTKDNTTIVDGAGDKEAIKARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATEVEMKEKKDRVEDALH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 400 STRAAVEEGIVAGGGTALVNIYQKVSEIK-AEGDVETGVNIVLQALQAPVRQIAENAGLEGSIIVERLKHAE-AGVGFNA 477
Cdd:PRK00013 401 ATRAAVEEGIVPGGGVALLRAAPALEALKgLNGDEATGINIVLRALEAPLRQIAENAGLEGSVVVEKVKNGKgKGYGYNA 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 488432175 478 ATNEWVNMLEEGIVDPTKVTRSALQHAASVAAMFLTTEAVVASIPEPENN 527
Cdd:PRK00013 481 ATGEYVDMIEAGIIDPTKVTRSALQNAASVAGLLLTTEAVVADKPEKKAA 530
|
|
| GroEL |
cd03344 |
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ... |
3-519 |
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: 860.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 3 KDLKFSEDARQAMLRGVDKLANAVKVTIGPKGRNVVLDKDYTTPLITNDGVTIAKEIELEDPYENMGAKLVQEVANKTNE 82
Cdd:cd03344 1 KDIKFGEEARKALLRGVNKLADAVKVTLGPKGRNVVIEKSFGSPKITKDGVTVAKEIELEDPFENMGAQLVKEVASKTND 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 83 IAGDGTTTATVLAQSMIQEGLKNVTSGANPVGLRQGIDKAVQVAIEALHEISQKVENKNEIAQVGAISA-ADEEIGRYIS 161
Cdd:cd03344 81 VAGDGTTTATVLARAIIKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKPVKTKEEIAQVATISAnGDEEIGELIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 162 EAMDKVGNDGVITIEESNGFNTELEVVEGMQFDRGYQSPYMVTDSDKMIAELERPYILVTDKKITSFQDILPLLEQVVQS 241
Cdd:cd03344 161 EAMEKVGKDGVITVEEGKTLETELEVVEGMQFDRGYLSPYFVTDPEKMEVELENPYILLTDKKISSIQELLPILELVAKA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 242 SRPILIVADEVEGDALTNIVLNRMRGTFTAVAVKAPGFGDRRKAMLEDLAILTGAQVITDDLGLELKDASLDMLGTANKV 321
Cdd:cd03344 241 GRPLLIIAEDVEGEALATLVVNKLRGGLKVCAVKAPGFGDRRKAMLEDIAILTGGTVISEELGLKLEDVTLEDLGRAKKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 322 EVTKDHTTVVDGNGDENNIDARVGQIKAQIEETDSEFDKEKLQERLAKLAGGVAVIKVGAASETELKERKLRIEDALNST 401
Cdd:cd03344 321 VVTKDDTTIIGGAGDKAAIKARIAQIRKQIEETTSDYDKEKLQERLAKLSGGVAVIKVGGATEVELKEKKDRVEDALNAT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 402 RAAVEEGIVAGGGTALVNIYQKVSEIKAE-GDVETGVNIVLQALQAPVRQIAENAGLEGSIIVERLKHAEAGVGFNAATN 480
Cdd:cd03344 401 RAAVEEGIVPGGGVALLRASPALDKLKALnGDEKLGIEIVRRALEAPLRQIAENAGVDGSVVVEKVLESPDGFGYDAATG 480
|
490 500 510
....*....|....*....|....*....|....*....
gi 488432175 481 EWVNMLEEGIVDPTKVTRSALQHAASVAAMFLTTEAVVA 519
Cdd:cd03344 481 EYVDMIEAGIIDPTKVVRSALQNAASVASLLLTTEALVV 519
|
|
| groEL |
PRK12849 |
chaperonin GroEL; Reviewed |
1-526 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237230 Cd Length: 542 Bit Score: 859.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 1 MAKDLKFSEDARQAMLRGVDKLANAVKVTIGPKGRNVVLDKDYTTPLITNDGVTIAKEIELEDPYENMGAKLVQEVANKT 80
Cdd:PRK12849 1 MAKIIKFDEEARRALERGVNKLADAVKVTLGPKGRNVVIDKSFGAPTITKDGVSIAKEIELEDPFENLGAQLVKEVASKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 81 NEIAGDGTTTATVLAQSMIQEGLKNVTSGANPVGLRQGIDKAVQVAIEALHEISQKVENKNEIAQVGAISA-ADEEIGRY 159
Cdd:PRK12849 81 NDVAGDGTTTATVLAQALVQEGLKNVAAGANPMDLKRGIDKAVEAVVEELKALARPVSGSEEIAQVATISAnGDEEIGEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 160 ISEAMDKVGNDGVITIEESNGFNTELEVVEGMQFDRGYQSPYMVTDSDKMIAELERPYILVTDKKITSFQDILPLLEQVV 239
Cdd:PRK12849 161 IAEAMEKVGKDGVITVEESKTLETELEVTEGMQFDRGYLSPYFVTDPERMEAVLEDPLILLTDKKISSLQDLLPLLEKVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 240 QSSRPILIVADEVEGDALTNIVLNRMRGTFTAVAVKAPGFGDRRKAMLEDLAILTGAQVITDDLGLELKDASLDMLGTAN 319
Cdd:PRK12849 241 QSGKPLLIIAEDVEGEALATLVVNKLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGLKLEEVTLDDLGRAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 320 KVEVTKDHTTVVDGNGDENNIDARVGQIKAQIEETDSEFDKEKLQERLAKLAGGVAVIKVGAASETELKERKLRIEDALN 399
Cdd:PRK12849 321 RVTITKDNTTIVDGAGDKEAIEARVAQIRRQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATEVELKERKDRVEDALN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 400 STRAAVEEGIVAGGGTALVNIYQKVSEIK-AEGDVETGVNIVLQALQAPVRQIAENAGLEGSIIVERLKHAEAGVGFNAA 478
Cdd:PRK12849 401 ATRAAVEEGIVPGGGVALLRAAKALDELAgLNGDQAAGVEIVRRALEAPLRQIAENAGLDGSVVVAKVLELEDGFGFNAA 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 488432175 479 TNEWVNMLEEGIVDPTKVTRSALQHAASVAAMFLTTEAVVASIPEPEN 526
Cdd:PRK12849 481 TGEYGDLIAAGIIDPVKVTRSALQNAASVAGLLLTTEALVADKPEEED 528
|
|
| GroEL |
TIGR02348 |
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ... |
2-523 |
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: 830.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 2 AKDLKFSEDARQAMLRGVDKLANAVKVTIGPKGRNVVLDKDYTTPLITNDGVTIAKEIELEDPYENMGAKLVQEVANKTN 81
Cdd:TIGR02348 1 AKQIKFDEEARKALLRGVDKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDKFENMGAQLVKEVASKTN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 82 EIAGDGTTTATVLAQSMIQEGLKNVTSGANPVGLRQGIDKAVQVAIEALHEISQKVENKNEIAQVGAISA-ADEEIGRYI 160
Cdd:TIGR02348 81 DVAGDGTTTATVLAQAIVKEGLKNVAAGANPIELKRGIEKAVEAVVEELKKLSKPVKGKKEIAQVATISAnNDEEIGSLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 161 SEAMDKVGNDGVITIEESNGFNTELEVVEGMQFDRGYQSPYMVTDSDKMIAELERPYILVTDKKITSFQDILPLLEQVVQ 240
Cdd:TIGR02348 161 AEAMEKVGKDGVITVEESKSLETELEVVEGMQFDRGYISPYFVTDAEKMEVELENPYILITDKKISNIKDLLPLLEKVAQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 241 SSRPILIVADEVEGDALTNIVLNRMRGTFTAVAVKAPGFGDRRKAMLEDLAILTGAQVITDDLGLELKDASLDMLGTANK 320
Cdd:TIGR02348 241 SGKPLLIIAEDVEGEALATLVVNKLRGTLNVCAVKAPGFGDRRKAMLEDIAILTGGQVISEELGLKLEEVTLDDLGKAKK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 321 VEVTKDHTTVVDGNGDENNIDARVGQIKAQIEETDSEFDKEKLQERLAKLAGGVAVIKVGAASETELKERKLRIEDALNS 400
Cdd:TIGR02348 321 VTVDKDNTTIVEGAGDKAAIKARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATETEMKEKKLRIEDALNA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 401 TRAAVEEGIVAGGGTALVNIYQKVSEIKAEG-DVETGVNIVLQALQAPVRQIAENAGLEGSIIVERLKHAEAGVGFNAAT 479
Cdd:TIGR02348 401 TRAAVEEGIVPGGGVALLRAAAALEGLKGDGeDEAIGIDIVKRALEAPLRQIAENAGLDGAVVAEKVKELKGNFGFNAAT 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 488432175 480 NEWVNMLEEGIVDPTKVTRSALQHAASVAAMFLTTEAVVASIPE 523
Cdd:TIGR02348 481 GEYEDLVEAGIIDPTKVTRSALQNAASIAGLLLTTEAVVADKPE 524
|
|
| groEL |
PRK12850 |
chaperonin GroEL; Reviewed |
1-523 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237231 Cd Length: 544 Bit Score: 794.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 1 MAKDLKFSEDARQAMLRGVDKLANAVKVTIGPKGRNVVLDKDYTTPLITNDGVTIAKEIELEDPYENMGAKLVQEVANKT 80
Cdd:PRK12850 2 AAKEIRFSTDARDRLLRGVNILANAVKVTLGPKGRNVVLEKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVKEVASKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 81 NEIAGDGTTTATVLAQSMIQEGLKNVTSGANPVGLRQGIDKAVQVAIEALHEISQKVENKNEIAQVGAISA-ADEEIGRY 159
Cdd:PRK12850 82 NDLAGDGTTTATVLAQAIVREGAKLVAAGMNPMDLKRGIDLAVAAVVDELKKIAKKVTSSKEIAQVATISAnGDESIGEM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 160 ISEAMDKVGNDGVITIEESNGFNTELEVVEGMQFDRGYQSPYMVTDSDKMIAELERPYILVTDKKITSFQDILPLLEQVV 239
Cdd:PRK12850 162 IAEAMDKVGKEGVITVEEAKTLGTELDVVEGMQFDRGYLSPYFVTNPEKMRAELEDPYILLHEKKISNLQDLLPILEAVV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 240 QSSRPILIVADEVEGDALTNIVLNRMRGTFTAVAVKAPGFGDRRKAMLEDLAILTGAQVITDDLGLELKDASLDMLGTAN 319
Cdd:PRK12850 242 QSGRPLLIIAEDVEGEALATLVVNKLRGGLKSVAVKAPGFGDRRKAMLEDIAVLTGGQVISEDLGIKLENVTLDMLGRAK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 320 KVEVTKDHTTVVDGNGDENNIDARVGQIKAQIEETDSEFDKEKLQERLAKLAGGVAVIKVGAASETELKERKLRIEDALN 399
Cdd:PRK12850 322 RVLITKENTTIIDGAGDKKNIEARVKQIRAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKEKKDRVDDALH 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 400 STRAAVEEGIVAGGGTALVNIYQKVSEIK-AEGDVETGVNIVLQALQAPVRQIAENAGLEGSIIVERLKHAEAGVGFNAA 478
Cdd:PRK12850 402 ATRAAVEEGIVPGGGVALLRARSALRGLKgANADETAGIDIVRRALEEPLRQIATNAGFEGSVVVGKVAELPGNFGFNAQ 481
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 488432175 479 TNEWVNMLEEGIVDPTKVTRSALQHAASVAAMFLTTEAVVASIPE 523
Cdd:PRK12850 482 TGEYGDMVEAGIIDPAKVTRTALQDAASIAALLITTEAMVAEAPK 526
|
|
| GroEL |
COG0459 |
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ... |
1-525 |
0e+00 |
|
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227 Cd Length: 497 Bit Score: 754.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 1 MAKDLKFSEDARQAMLRGVDKLANAVKVTIGPKGRNVVLDKDYTTPLITNDGVTIAKEIELEDPYENMGAKLVQEVANKT 80
Cdd:COG0459 1 MAKQILFGEDARRANIRGVKALADAVKVTLGPKGRNVMLVKSFGDPTITNDGVTIAKEIELEDPFENMGAQLVKEVASKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 81 NEIAGDGTTTATVLAQSMIQEGLKNVTSGANPVGLRQGIDKAVQVAIEALHEISQKVENKNEIAQVGAISAA-DEEIGRY 159
Cdd:COG0459 81 NDEAGDGTTTATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPVDDKEELAQVATISANgDEEIGEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 160 ISEAMDKVGNDGVITIEESNGFNTELEVVEGMQFDRGYQSPYMVTDSDKMIAELERPYILVTDKKITSFQDILPLLEQVV 239
Cdd:COG0459 161 IAEAMEKVGKDGVITVEEGKGLETELEVVEGMQFDKGYLSPYFVTDPEKMPAELENAYILLTDKKISSIQDLLPLLEKVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 240 QSSRPILIVADEVEGDALTNIVLNRMRGTFTAVAVKAPGFGDRRKAMLEDLAILTGAQVITDDLGLELKDASLDMLGTAN 319
Cdd:COG0459 241 QSGKPLLIIAEDIDGEALATLVVNGIRGVLRVVAVKAPGFGDRRKAMLEDIAILTGGRVISEDLGLKLEDVTLDDLGRAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 320 KVEVTKDHTTVVDGNGDENNIdarvgqikaqieetdsefdkeklqerlaklaggvaVIKVGAASETELKERKLRIEDALN 399
Cdd:COG0459 321 RVEVDKDNTTIVEGAGNPKAI-----------------------------------VILVGAATEVEVKERKRRVEDALH 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 400 STRAAVEEGIVAGGGTALVNIYQKVSEI--KAEGDVETGVNIVLQALQAPVRQIAENAGLEGSIIVERLKHAE-AGVGFN 476
Cdd:COG0459 366 ATRAAVEEGIVPGGGAALLRAARALRELaaKLEGDEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKVRAAKdKGFGFD 445
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 488432175 477 AATNEWVNMLEEGIVDPTKVTRSALQHAASVAAMFLTTEAVVASIPEPE 525
Cdd:COG0459 446 AATGEYVDMLEAGVIDPAKVKRSALQNAASVAGLILTTEAVIADKPEKE 494
|
|
| groEL |
PRK12851 |
chaperonin GroEL; Reviewed |
1-525 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 171770 Cd Length: 541 Bit Score: 742.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 1 MAKDLKFSEDARQAMLRGVDKLANAVKVTIGPKGRNVVLDKDYTTPLITNDGVTIAKEIELEDPYENMGAKLVQEVANKT 80
Cdd:PRK12851 2 AAKEVKFHVEAREKMLRGVNILADAVKVTLGPKGRNVVIDKSFGAPTITNDGVTIAKEIELEDKFENMGAQMVREVASKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 81 NEIAGDGTTTATVLAQSMIQEGLKNVTSGANPVGLRQGIDKAVQVAIEALHEISQKVENKNEIAQVGAISA-ADEEIGRY 159
Cdd:PRK12851 82 NDVAGDGTTTATVLAQAIVREGAKAVAAGANPMDLKRGIDRAVAAVVEELKANARPVTTNAEIAQVATISAnGDAEIGRL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 160 ISEAMDKVGNDGVITIEESNGFNTELEVVEGMQFDRGYQSPYMVTDSDKMIAELERPYILVTDKKITSFQDILPLLEQVV 239
Cdd:PRK12851 162 VAEAMEKVGNEGVITVEESKTAETELEVVEGMQFDRGYLSPYFVTDADKMEAELEDPYILIHEKKISNLQDLLPVLEAVV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 240 QSSRPILIVADEVEGDALTNIVLNRMRGTFTAVAVKAPGFGDRRKAMLEDLAILTGAQVITDDLGLELKDASLDMLGTAN 319
Cdd:PRK12851 242 QSGKPLLIIAEDVEGEALATLVVNKLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGIKLENVTLEQLGRAK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 320 KVEVTKDHTTVVDGNGDENNIDARVGQIKAQIEETDSEFDKEKLQERLAKLAGGVAVIKVGAASETELKERKLRIEDALN 399
Cdd:PRK12851 322 KVVVEKENTTIIDGAGSKTEIEGRVAQIRAQIEETTSDYDREKLQERLAKLAGGVAVIRVGASTEVEVKEKKDRVDDALH 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 400 STRAAVEEGIVAGGGTALVNIYQKVSEIK-AEGDVETGVNIVLQALQAPVRQIAENAGLEGSIIVERLKHAEAGVGFNAA 478
Cdd:PRK12851 402 ATRAAVEEGIVPGGGVALLRAVKALDKLEtANGDQRTGVEIVRRALEAPVRQIAENAGAEGSVVVGKLREKPGGYGFNAA 481
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 488432175 479 TNEWVNMLEEGIVDPTKVTRSALQHAASVAAMFLTTEAVVASIPEPE 525
Cdd:PRK12851 482 TNEYGDLYAQGVIDPVKVVRTALQNAASVAGLLLTTEAMVAEKPKKE 528
|
|
| groEL |
PRK12852 |
chaperonin GroEL; Reviewed |
1-525 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237232 Cd Length: 545 Bit Score: 700.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 1 MAKDLKFSEDARQAMLRGVDKLANAVKVTIGPKGRNVVLDKDYTTPLITNDGVTIAKEIELEDPYENMGAKLVQEVANKT 80
Cdd:PRK12852 2 AAKDVKFSGDARDRMLRGVDILANAVKVTLGPKGRNVVIEKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVREVASKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 81 NEIAGDGTTTATVLAQSMIQEGLKNVTSGANPVGLRQGIDKAVQVAIEALHEISQKVENKNEIAQVGAISA-ADEEIGRY 159
Cdd:PRK12852 82 NDLAGDGTTTATVLAQAIVREGAKAVAAGMNPMDLKRGIDIAVAAVVKDIEKRAKPVASSAEIAQVGTISAnGDAAIGKM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 160 ISEAMDKVGNDGVITIEESNGFNTELEVVEGMQFDRGYQSPYMVTDSDKMIAELERPYILVTDKKITSFQDILPLLEQVV 239
Cdd:PRK12852 162 IAQAMQKVGNEGVITVEENKSLETEVDIVEGMKFDRGYLSPYFVTNAEKMTVELDDAYILLHEKKLSGLQAMLPVLEAVV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 240 QSSRPILIVADEVEGDALTNIVLNRMRGTFTAVAVKAPGFGDRRKAMLEDLAILTGAQVITDDLGLELKDASLDMLGTAN 319
Cdd:PRK12852 242 QSGKPLLIIAEDVEGEALATLVVNRLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGQLISEDLGIKLENVTLKMLGRAK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 320 KVEVTKDHTTVVDGNGDENNIDARVGQIKAQIEETDSEFDKEKLQERLAKLAGGVAVIKVGAASETELKERKLRIEDALN 399
Cdd:PRK12852 322 KVVIDKENTTIVNGAGKKADIEARVGQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKEKKDRVEDALN 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 400 STRAAVEEGIVAGGGTALVNIYQKVSEIK-AEGDVETGVNIVLQALQAPVRQIAENAGLEGSIIVER-LKHAEAGVGFNA 477
Cdd:PRK12852 402 ATRAAVQEGIVPGGGVALLRAKKAVGRINnDNADVQAGINIVLKALEAPIRQIAENAGVEGSIVVGKiLENKSETFGFDA 481
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 488432175 478 ATNEWVNMLEEGIVDPTKVTRSALQHAASVAAMFLTTEAVVASIPEPE 525
Cdd:PRK12852 482 QTEEYVDMVAKGIIDPAKVVRTALQDAASVAGLLVTTEAMVAELPKKD 529
|
|
| PTZ00114 |
PTZ00114 |
Heat shock protein 60; Provisional |
2-526 |
0e+00 |
|
Heat shock protein 60; Provisional
Pssm-ID: 185455 Cd Length: 555 Bit Score: 698.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 2 AKDLKFSEDARQAMLRGVDKLANAVKVTIGPKGRNVVLDKDYTTPLITNDGVTIAKEIELEDPYENMGAKLVQEVANKTN 81
Cdd:PTZ00114 14 GKEIRFGDEARQSLLKGIERLADAVAVTLGPKGRNVIIEQEYGSPKITKDGVTVAKAIEFSDRFENVGAQLIRQVASKTN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 82 EIAGDGTTTATVLAQSMIQEGLKNVTSGANPVGLRQGIDKAVQVAIEALHEISQKVENKNEIAQVGAISA-ADEEIGRYI 160
Cdd:PTZ00114 94 DKAGDGTTTATILARAIFREGCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQSRPVKTKEDILNVATISAnGDVEIGSLI 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 161 SEAMDKVGNDGVITIEESNGFNTELEVVEGMQFDRGYQSPYMVTDSDKMIAELERPYILVTDKKITSFQDILPLLEQVVQ 240
Cdd:PTZ00114 174 ADAMDKVGKDGTITVEDGKTLEDELEVVEGMSFDRGYISPYFVTNEKTQKVELENPLILVTDKKISSIQSILPILEHAVK 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 241 SSRPILIVADEVEGDALTNIVLNRMRGTFTAVAVKAPGFGDRRKAMLEDLAILTGAQVITDD-LGLELKDASLDMLGTAN 319
Cdd:PTZ00114 254 NKRPLLIIAEDVEGEALQTLIINKLRGGLKVCAVKAPGFGDNRKDILQDIAVLTGATVVSEDnVGLKLDDFDPSMLGSAK 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 320 KVEVTKDHTTVVDGNGDENNIDARVGQIKAQIEETDSEFDKEKLQERLAKLAGGVAVIKVGAASETELKERKLRIEDALN 399
Cdd:PTZ00114 334 KVTVTKDETVILTGGGDKAEIKERVELLRSQIERTTSEYDKEKLKERLAKLSGGVAVIKVGGASEVEVNEKKDRIEDALN 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 400 STRAAVEEGIVAGGGTALVNIYQKVSEIK----AEGDVETGVNIVLQALQAPVRQIAENAGLEGSIIVER-LKHAEAGVG 474
Cdd:PTZ00114 414 ATRAAVEEGIVPGGGVALLRASKLLDKLEedneLTPDQRTGVKIVRNALRLPTKQIAENAGVEGAVVVEKiLEKKDPSFG 493
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 488432175 475 FNAATNEWVNMLEEGIVDPTKVTRSALQHAASVAAMFLTTEAVVASIPEPEN 526
Cdd:PTZ00114 494 YDAQTGEYVNMFEAGIIDPTKVVRSALVDAASVASLMLTTEAAIVDLPKEKK 545
|
|
| groEL |
CHL00093 |
chaperonin GroEL |
1-523 |
0e+00 |
|
chaperonin GroEL
Pssm-ID: 177025 Cd Length: 529 Bit Score: 685.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 1 MAKDLKFSEDARQAMLRGVDKLANAVKVTIGPKGRNVVLDKDYTTPLITNDGVTIAKEIELEDPYENMGAKLVQEVANKT 80
Cdd:CHL00093 1 MSKKILYQDNARRALERGMDILAEAVSVTLGPKGRNVVLEKKYGSPQIVNDGVTIAKEIELEDHIENTGVALIRQAASKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 81 NEIAGDGTTTATVLAQSMIQEGLKNVTSGANPVGLRQGIDKAVQVAIEALHEISQKVENKNEIAQVGAISAA-DEEIGRY 159
Cdd:CHL00093 81 NDVAGDGTTTATVLAYAIVKQGMKNVAAGANPISLKRGIEKATQYVVSQIAEYARPVEDIQAITQVASISAGnDEEVGSM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 160 ISEAMDKVGNDGVITIEESNGFNTELEVVEGMQFDRGYQSPYMVTDSDKMIAELERPYILVTDKKITSF-QDILPLLEQV 238
Cdd:CHL00093 161 IADAIEKVGREGVISLEEGKSTVTELEITEGMRFEKGFISPYFVTDTERMEVVQENPYILLTDKKITLVqQDLLPILEQV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 239 VQSSRPILIVADEVEGDALTNIVLNRMRGTFTAVAVKAPGFGDRRKAMLEDLAILTGAQVITDDLGLELKDASLDMLGTA 318
Cdd:CHL00093 241 TKTKRPLLIIAEDVEKEALATLVLNKLRGIVNVVAVRAPGFGDRRKAMLEDIAILTGGQVITEDAGLSLETIQLDLLGQA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 319 NKVEVTKDHTTVVdGNGDENNIDARVGQIKAQIEETDSEFDKEKLQERLAKLAGGVAVIKVGAASETELKERKLRIEDAL 398
Cdd:CHL00093 321 RRIIVTKDSTTII-ADGNEEQVKARCEQLRKQIEIADSSYEKEKLQERLAKLSGGVAVIKVGAATETEMKDKKLRLEDAI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 399 NSTRAAVEEGIVAGGGTALVNIYQKV---SEIKAEGDVETGVNIVLQALQAPVRQIAENAGLEGSIIVERLKHAEAGVGF 475
Cdd:CHL00093 400 NATKAAVEEGIVPGGGATLVHLSENLktwAKNNLKEDELIGALIVARAILAPLKRIAENAGKNGSVIIEKVQEQDFEIGY 479
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 488432175 476 NAATNEWVNMLEEGIVDPTKVTRSALQHAASVAAMFLTTEAVVASIPE 523
Cdd:CHL00093 480 NAANNKFVNMYEAGIIDPAKVTRSALQNAASIASMILTTECIIVDKKE 527
|
|
| PRK14104 |
PRK14104 |
chaperonin GroEL; Provisional |
2-523 |
0e+00 |
|
chaperonin GroEL; Provisional
Pssm-ID: 172594 Cd Length: 546 Bit Score: 605.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 2 AKDLKFSEDARQAMLRGVDKLANAVKVTIGPKGRNVVLDKDYTTPLITNDGVTIAKEIELEDPYENMGAKLVQEVANKTN 81
Cdd:PRK14104 3 AKEVKFGVDARDRMLRGVDILANAVKVTLGPKGRNVVLDKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVREVASKSA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 82 EIAGDGTTTATVLAQSMIQEGLKNVTSGANPVGLRQGIDKAVQVAIEALHEISQKVENKNEIAQVGAISA-ADEEIGRYI 160
Cdd:PRK14104 83 DAAGDGTTTATVLAQAIVREGAKSVAAGMNPMDLKRGIDLAVEAVVADLVKNSKKVTSNDEIAQVGTISAnGDAEIGKFL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 161 SEAMDKVGNDGVITIEESNGFNTELEVVEGMQFDRGYQSPYMVTDSDKMIAELERPYILVTDKKITSFQDILPLLEQVVQ 240
Cdd:PRK14104 163 ADAMKKVGNEGVITVEEAKSLETELDVVEGMQFDRGYISPYFVTNADKMRVEMDDAYILINEKKLSSLNELLPLLEAVVQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 241 SSRPILIVADEVEGDALTNIVLNRMRGTFTAVAVKAPGFGDRRKAMLEDLAILTGAQVITDDLGLELKDASLDMLGTANK 320
Cdd:PRK14104 243 TGKPLVIVAEDVEGEALATLVVNRLRGGLKVAAVKAPGFGDRRKAMLQDIAILTGGQAISEDLGIKLENVTLQMLGRAKK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 321 VEVTKDHTTVVDGNGDENNIDARVGQIKAQIEETDSEFDKEKLQERLAKLAGGVAVIKVGAASETELKERKLRIEDALNS 400
Cdd:PRK14104 323 VMIDKENTTIVNGAGKKADIEARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKERKDRVDDAMHA 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 401 TRAAVEEGIVAGGGTALVNIYQKVSEIKAEG-DVETGVNIVLQALQAPVRQIAENAGLEGSIIVER-LKHAEAGVGFNAA 478
Cdd:PRK14104 403 TRAAVEEGIVPGGGVALLRASEQLKGIKTKNdDQKTGVEIVRKALSAPARQIAINAGEDGSVIVGKiLEKEQYSYGFDSQ 482
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 488432175 479 TNEWVNMLEEGIVDPTKVTRSALQHAASVAAMFLTTEAVVASIPE 523
Cdd:PRK14104 483 TGEYGNLVSKGIIDPTKVVRTAIQNAASVAALLITTEAMVAELPK 527
|
|
| PLN03167 |
PLN03167 |
Chaperonin-60 beta subunit; Provisional |
2-525 |
0e+00 |
|
Chaperonin-60 beta subunit; Provisional
Pssm-ID: 215611 [Multi-domain] Cd Length: 600 Bit Score: 541.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 2 AKDLKFSED--ARQAMLRGVDKLANAVKVTIGPKGRNVVLDKDYTTPLITNDGVTIAKEIELEDPYENMGAKLVQEVANK 79
Cdd:PLN03167 56 AKELHFNKDgsAIKKLQAGVNKLADLVGVTLGPKGRNVVLESKYGSPKIVNDGVTVAKEVELEDPVENIGAKLVRQAAAK 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 80 TNEIAGDGTTTATVLAQSMIQEGLKNVTSGANPVGLRQGIDKAVQVAIEALHEISQKVENkNEIAQVGAISAADE-EIGR 158
Cdd:PLN03167 136 TNDLAGDGTTTSVVLAQGLIAEGVKVVAAGANPVQITRGIEKTAKALVKELKKMSKEVED-SELADVAAVSAGNNyEVGN 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 159 YISEAMDKVGNDGVITIEESNGFNTELEVVEGMQFDRGYQSPYMVTDSDKMIAELERPYILVTDKKITSFQDILPLLEQV 238
Cdd:PLN03167 215 MIAEAMSKVGRKGVVTLEEGKSAENNLYVVEGMQFDRGYISPYFVTDSEKMSVEYDNCKLLLVDKKITNARDLIGILEDA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 239 VQSSRPILIVADEVEGDALTNIVLNRMRGTFTAVAVKAPGFGDRRKAMLEDLAILTGAQVITDDLGLELKDASLDMLGTA 318
Cdd:PLN03167 295 IRGGYPLLIIAEDIEQEALATLVVNKLRGSLKIAALKAPGFGERKSQYLDDIAILTGGTVIREEVGLSLDKVGKEVLGTA 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 319 NKVEVTKDHTTVVDGNGDENNIDARVGQIKAQIEETDSEFDKEKLQERLAKLAGGVAVIKVGAASETELKERKLRIEDAL 398
Cdd:PLN03167 375 AKVVLTKDTTTIVGDGSTQEAVNKRVAQIKNLIEAAEQDYEKEKLNERIAKLSGGVAVIQVGAQTETELKEKKLRVEDAL 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 399 NSTRAAVEEGIVAGGGTALVNIYQKVSEIKA--EGDVE-TGVNIVLQALQAPVRQIAENAGLEGSIIVER-LKHAEAGVG 474
Cdd:PLN03167 455 NATKAAVEEGIVVGGGCTLLRLASKVDAIKDtlENDEQkVGADIVKRALSYPLKLIAKNAGVNGSVVSEKvLSNDNPKFG 534
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 488432175 475 FNAATNEWVNMLEEGIVDPTKVTRSALQHAASVAAMFLTTEAVVASIPEPE 525
Cdd:PLN03167 535 YNAATGKYEDLMAAGIIDPTKVVRCCLEHAASVAKTFLTSDCVVVEIKEPE 585
|
|
| chaperonin_type_I_II |
cd00309 |
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ... |
3-519 |
5.71e-148 |
|
chaperonin families, type I and type II. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings, each composed of 7-9 subunits. There are 2 main chaperonin groups. The symmetry of type I is seven-fold and they are found in eubacteria (GroEL) and in organelles of eubacterial descent (hsp60 and RBP). The symmetry of type II is eight- or nine-fold and they are found in archea (thermosome), thermophilic bacteria (TF55) and in the eukaryotic cytosol (CTT). Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis.
Pssm-ID: 238189 Cd Length: 464 Bit Score: 433.01 E-value: 5.71e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 3 KDLKFSEDARQAMLRGVDKLANAVKVTIGPKGRNVVLDKDYTTPLITNDGVTIAKEIELEdpyeNMGAKLVQEVANKTNE 82
Cdd:cd00309 1 KEREFGEEARLSNINAAKALADAVKTTLGPKGMDKMLVDSLGDPTITNDGATILKEIEVE----HPAAKLLVEVAKSQDD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 83 IAGDGTTTATVLAQSMIQEGLKNVTSGANPVGLRQGIDKAVQVAIEALHEISQK--VENKNEIAQVGAISAA-------D 153
Cdd:cd00309 77 EVGDGTTTVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVPidVEDREELLKVATTSLNsklvsggD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 154 EEIGRYISEAMDKVG------NDGVITIEESNGFN-TELEVVEGMQFDRGYQSPYmvtdsdkMIAELERPYILVTDKKit 226
Cdd:cd00309 157 DFLGELVVDAVLKVGkengdvDLGVIRVEKKKGGSlEDSELVVGMVFDKGYLSPY-------MPKRLENAKILLLDCK-- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 227 sfqdilplLEQVVqssrpilIVADEVEGDALTNIVLNRMrgtftaVAVKApgfgdRRKAMLEDLAILTGAQVITddlglE 306
Cdd:cd00309 228 --------LEYVV-------IAEKGIDDEALHYLAKLGI------MAVRR-----VRKEDLERIAKATGATIVS-----R 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 307 LKDASLDMLGTANKVEVTK----DHTTVVDGNGdennidarvgqikaqieetdsefdkeklqerlaklaGGVAVIKVGAA 382
Cdd:cd00309 277 LEDLTPEDLGTAGLVEETKigdeKYTFIEGCKG------------------------------------GKVATILLRGA 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 383 SETELKERKLRIEDALNSTRAAVEE-GIVAGGGTALVNIYQKVSEIKA--EGDVETGVNIVLQALQAPVRQIAENAGLEG 459
Cdd:cd00309 321 TEVELDEAERSLHDALCAVRAAVEDgGIVPGGGAAEIELSKALEELAKtlPGKEQLGIEAFADALEVIPRTLAENAGLDP 400
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488432175 460 SIIVERL--KHAEAG--VGFNAATNEWVNMLEEGIVDPTKVTRSALQHAASVAAMFLTTEAVVA 519
Cdd:cd00309 401 IEVVTKLraKHAEGGgnAGGDVETGEIVDMKEAGIIDPLKVKRQALKSATEAASLILTIDDIIV 464
|
|
| Cpn60_TCP1 |
pfam00118 |
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ... |
22-521 |
1.65e-88 |
|
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: 281.01 E-value: 1.65e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 22 LANAVKVTIGPKGRNVVLDKDYTTPLITNDGVTIAKEIELEDPYenmgAKLVQEVANKTNEIAGDGTTTATVLAQSMIQE 101
Cdd:pfam00118 1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELEIQHPA----AKLLVEAAKAQDEEVGDGTTTVVVLAGELLEE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 102 GLKNVTSGANPVGLRQGIDKAVQVAIEAL---HEISQKVENKNEIAQVGAISAA-------DEEIGRYISEA-------- 163
Cdd:pfam00118 77 AEKLLAAGVHPTTIIEGYEKALEKALEILdsiISIPVEDVDREDLLKVARTSLSskiisreSDFLAKLVVDAvlaipknd 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 164 -MDKVGNDGVITIEESNGFNTELevVEGMQFDRGYQSPymvtdsdKMIAELERPYILVTDKKITSFQD------------ 230
Cdd:pfam00118 157 gSFDLGNIGVVKILGGSLEDSEL--VDGVVLDKGPLHP-------DMPKRLENAKVLLLNCSLEYEKTetkatvvlsdae 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 231 ------------ILPLLEQVVQSSRPILIVADEVEGDALTNIVLNRMRGTFTAvavkapgfgdrRKAMLEDLAILTGAQV 298
Cdd:pfam00118 228 qlerflkaeeeqILEIVEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMALRRV-----------KKRDLERLAKATGARA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 299 ITDdlgleLKDASLDMLGTANKVEVTK---DHTTVVDGNGDennidarvgqikaqieetdsefdkeklqerlaklaGGVA 375
Cdd:pfam00118 297 VSS-----LDDLTPDDLGTAGKVEEEKigdEKYTFIEGCKS-----------------------------------PKAA 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 376 VIKVGAASETELKERKLRIEDALNSTRAAVEE-GIVAGGGTALVNIYQKVSEIKA--EGDVETGVNIVLQALQAPVRQIA 452
Cdd:pfam00118 337 TILLRGATDHVLDEIERSIHDALCVVKNAIEDpRVVPGGGAVEMELARALREYAKsvSGKEQLAIEAFAEALEVIPKTLA 416
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488432175 453 ENAGLEGSIIVERLKHA----EAGVGFNAATNEWVNMLEEGIVDPTKVTRSALQHAASVAAMFLTTEAVVASI 521
Cdd:pfam00118 417 ENAGLDPIEVLAELRAAhasgEKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKSATEAASTILRIDDIIKAK 489
|
|
| chaperonin_like |
cd03333 |
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ... |
140-407 |
4.99e-37 |
|
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: 136.06 E-value: 4.99e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 140 KNEIAQVGAISAA------DEEIGRYISEAMDKVG------NDGVITIEESNGFN-TELEVVEGMQFDRGYQSPYMvtds 206
Cdd:cd03333 1 RELLLQVATTSLNsklsswDDFLGKLVVDAVLKVGpdnrmdDLGVIKVEKIPGGSlEDSELVVGVVFDKGYASPYM---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 207 dkmIAELERPYILVTDKKitsfqdilplLEQVVqssrpilIVADEVEGDALTNIVLNRMrgtftaVAVKApgfgdRRKAM 286
Cdd:cd03333 77 ---PKRLENAKILLLDCP----------LEYVV-------IAEKGIDDLALHYLAKAGI------MAVRR-----VKKED 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 287 LEDLAILTGAQVITddlglELKDASLDMLGTANKVEVTKDhttvvdgngdennidarvgqikaqIEETDSEFDKEKlqer 366
Cdd:cd03333 126 LERIARATGATIVS-----SLEDLTPEDLGTAELVEETKI------------------------GEEKLTFIEGCK---- 172
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 488432175 367 laklAGGVAVIKVGAASETELKERKLRIEDALNSTRAAVEE 407
Cdd:cd03333 173 ----GGKAATILLRGATEVELDEVKRSLHDALCAVRAAVEE 209
|
|
| cpn60 |
cd03343 |
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ... |
9-520 |
5.96e-32 |
|
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: 128.92 E-value: 5.96e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 9 EDARQAMLRGVDKLANAVKVTIGPKGrnvvLDKDYTTPL----ITNDGVTIAKEIELEDPyenmGAKLVQEVANKTNEIA 84
Cdd:cd03343 14 RDAQRMNIAAAKAVAEAVRTTLGPKG----MDKMLVDSLgdvtITNDGATILKEMDIEHP----AAKMLVEVAKTQDEEV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 85 GDGTTTATVLAQSMIQEGLKNVTSGANPVGLRQGIDKAVQVAIEALHEISQKVENKNE-----IAQVGAISAADEEIGRY 159
Cdd:cd03343 86 GDGTTTAVVLAGELLEKAEDLLDQNIHPTVIIEGYRLAAEKALELLDEIAIKVDPDDKdtlrkIAKTSLTGKGAEAAKDK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 160 ISE-AMDKV-----GNDGVITIEESN--------GFNTELEVVEGMQFDRGYQSPYM---VTDSDKMIA----ELERPYI 218
Cdd:cd03343 166 LADlVVDAVlqvaeKRDGKYVVDLDNikiekktgGSVDDTELIRGIVIDKEVVHPGMpkrVENAKIALLdaplEVKKTEI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 219 lVTDKKITSFQDILPLLEqvvQSSRPILIVADEVEgDALTNIVL-----NRMRGTFTAvavKAPGFGDRR--KAMLEDLA 291
Cdd:cd03343 246 -DAKIRITSPDQLQAFLE---QEEAMLKEMVDKIA-DTGANVVFcqkgiDDLAQHYLA---KAGILAVRRvkKSDMEKLA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 292 ILTGAQVITDdlgleLKDASLDMLGTANKVEVTKDhttvvdgnGDENnidarvgqiKAQIEEtdsefdkeklqerlAKLA 371
Cdd:cd03343 318 RATGAKIVTN-----IDDLTPEDLGEAELVEERKV--------GDDK---------MVFVEG--------------CKNP 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 372 GGVAVIKVGaASETELKERKLRIEDALNSTRAAVEEG-IVAGGGTALVNIYQKVSEI--KAEGDVETGVNIVLQALQAPV 448
Cdd:cd03343 362 KAVTILLRG-GTEHVVDELERALEDALRVVADALEDGkVVAGGGAVEIELAKRLREYarSVGGREQLAVEAFADALEEIP 440
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488432175 449 RQIAENAGLEG-SIIVE-RLKHAEAG--VGFNAATNEWVNMLEEGIVDPTKVTRSALQHAASVAAMFLTTEAVVAS 520
Cdd:cd03343 441 RTLAENAGLDPiDTLVElRAAHEKGNknAGLDVYTGEVVDMLEKGVIEPLRVKKQAIKSATEAATMILRIDDVIAA 516
|
|
| TCP1_delta |
cd03338 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ... |
22-512 |
4.64e-19 |
|
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: 90.04 E-value: 4.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 22 LANAVKVTIGPKGrnvvLDKDYTTP----LITNDGVTIAKEIELEDPyenmGAKLVQEVANKTNEIAGDGTTTATVLAQS 97
Cdd:cd03338 20 VADAIRTSLGPRG----MDKMIQTGkgevIITNDGATILKQMSVLHP----AAKMLVELSKAQDIEAGDGTTSVVVLAGA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 98 MIQEGLKNVTSGANPVGLRQGIDKAVQVAIEALHEISQKVENKNEIAQV-GAISAADEEIGRYISEAMDKVGNDGVITIE 176
Cdd:cd03338 92 LLSACESLLKKGIHPTVISESFQIAAKKAVEILDSMSIPVDLNDRESLIkSATTSLNSKVVSQYSSLLAPIAVDAVLKVI 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 177 ESNGFNT-----------------ELEVVEGMQFDRGYQS------------------------PYM-----VTDSDKM- 209
Cdd:cd03338 172 DPATATNvdlkdirivkklggtieDTELVDGLVFTQKASKkaggptriekakigliqfclsppkTDMdnnivVNDYAQMd 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 210 -IAELERPYILVTDKKITSfqdilplleqvvqSSRPILIVADEVEGDALTNI---VLNRMRgtftAVAVKapgfgDRRKA 285
Cdd:cd03338 252 rILREERKYILNMCKKIKK-------------SGCNVLLIQKSILRDAVSDLalhFLAKLK----IMVVK-----DIERE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 286 MLEDLAILTGAQVITDdlgleLKDASLDMLGTANKVevtkdhttvvdgngdennidarvgqikaqiEETDSEFDKEKLQE 365
Cdd:cd03338 310 EIEFICKTIGCKPVAS-----IDHFTEDKLGSADLV------------------------------EEVSLGDGKIVKIT 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 366 RLAKLAGGVAVIkVGAASETELKERKLRIEDALNSTRAAVEE-GIVAGGGTALVNIYQKVSEikaEGDVETGVNIVL--- 441
Cdd:cd03338 355 GVKNPGKTVTIL-VRGSNKLVLDEAERSLHDALCVIRCLVKKrALIPGGGAPEIEIALQLSE---WARTLTGVEQYCvra 430
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488432175 442 --QALQAPVRQIAENAGLEG-SIIVE-RLKHAEAGV--GFNAATNEWVNMLEEGIVDPTKVTRSALQHAASVAAMFL 512
Cdd:cd03338 431 faDALEVIPYTLAENAGLNPiSIVTElRNRHAQGEKnaGINVRKGAITNILEENVVQPLLVSTSAITLATETVRMIL 507
|
|
| chap_CCT_delta |
TIGR02342 |
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ... |
9-520 |
1.86e-16 |
|
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: 82.14 E-value: 1.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 9 EDARQAMLRGVDKLANAVKVTIGPKGRNVVLDKDYTTPLITNDGVTIAKEIELEDPyenmGAKLVQEVANKTNEIAGDGT 88
Cdd:TIGR02342 8 QDVRTSNIVAAKAVADAIRTSLGPKGMDKMIQDGKGEVIITNDGATILKQMAVLHP----AAKMLVELSKAQDIEAGDGT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 89 TTATVLAQSMIQEGLKNVTSGANPVGLRQGIDKAVQVAIEALHEISQKVENKN-EIAQVGAISAADEEIGRYISEAMDKV 167
Cdd:TIGR02342 84 TSVVILAGALLGACERLLNKGIHPTIISESFQSAADEAIKILDEMSIPVDLSDrEQLLKSATTSLSSKVVSQYSSLLAPL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 168 GNDGVITIEES-NGFNTEL----------------EVVEGMQFDRGYQS------------------------PYM---- 202
Cdd:TIGR02342 164 AVDAVLKVIDPeNAKNVDLndikvvkklggtiddtELIEGLVFTQKASKsaggptriekakigliqfqisppkTDMenqi 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 203 -VTDSDKM--IAELERPYILVTDKKItsfqdilplleqvVQSSRPILIVADEVEGDALTNI---VLNRMRgtftAVAVKa 276
Cdd:TIGR02342 244 iVNDYAQMdrVLKEERAYILNIVKKI-------------KKTGCNVLLIQKSILRDAVNDLalhFLAKMK----IMVVK- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 277 pgfgDRRKAMLEDLAILTGAQVITDDLGLelkdaSLDMLGTANKVE-VTKDHTTVVDGNGDENnidarvgqikaqieetd 355
Cdd:TIGR02342 306 ----DIEREEIEFICKTIGCKPIASIDHF-----TADKLGSAELVEeVDSDGGKIIKITGIQN----------------- 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 356 sefdkeklqerlaklAGGVAVIKVGAASETELKERKLRIEDALNSTRAAVEE-GIVAGGGTALVNIYQKVSEIKAEGDVE 434
Cdd:TIGR02342 360 ---------------AGKTVTVVVRGSNKLVIDEAERSLHDALCVIRCLVKKrGLIAGGGAPEIEIARRLSKYARTMKGV 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 435 TG--VNIVLQALQAPVRQIAENAGLEGSIIVERL--KHA--EAGVGFNAATNEWVNMLEEGIVDPTKVTRSALQHAASVA 508
Cdd:TIGR02342 425 ESycVRAFADALEVIPYTLAENAGLNPIKVVTELrnRHAngEKTAGISVRKGGITNMLEEHVLQPLLVTTSAITLASETV 504
|
570
....*....|..
gi 488432175 509 AMFLTTEAVVAS 520
Cdd:TIGR02342 505 RSILKIDDIVFT 516
|
|
| chap_CCT_epsi |
TIGR02343 |
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ... |
10-520 |
1.58e-15 |
|
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: 79.46 E-value: 1.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 10 DARQAMLRGVDKLANAVKVTIGPKGRNVVL---DKDYTtplITNDGVTIAKEIELEDPYenmgAKLVQEVANKTNEIAGD 86
Cdd:TIGR02343 27 EAKKSNIAAAKSVASILRTSLGPKGMDKMLispDGDIT---VTNDGATILSQMDVDNQI----AKLMVELSKSQDDEIGD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 87 GTTTATVLAQSMIQEGLKNVTSGANPVGLRQGIDKAVQVAIEALHEISQKVENKNEIAQVgAISAADEEIGRYI----SE 162
Cdd:TIGR02343 100 GTTGVVVLAGALLEQAEELLDKGIHPIKIADGFEEAARIAVEHLEEISDEISADNNNREP-LIQAAKTSLGSKIvskcHR 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 163 AMDKVGNDGVITIE--ESNGFNTEL--------------EVVEGMQFDRGYQSPYMVTD-SDKMIAELERPY---ILVTD 222
Cdd:TIGR02343 179 RFAEIAVDAVLNVAdmERRDVDFDLikvegkvggsledtKLIKGIIIDKDFSHPQMPKEvEDAKIAILTCPFeppKPKTK 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 223 KK--ITSFQDILPLLEQVVQSSRPILivaDEVEgDALTNIVL---------NRMRGTFTAVAVKAPGFGDrrkamLEDLA 291
Cdd:TIGR02343 259 HKldISSVEEYKKLQKYEQQKFKEMI---DDIK-KSGANLVIcqwgfddeaNHLLLQNDLPAVRWVGGQE-----LELIA 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 292 ILTGAQVITddlglELKDASLDMLGTANKVE-----VTKDHTTVVDgngdennidaRVGQIKAqieetdsefdkeklqer 366
Cdd:TIGR02343 330 IATGGRIVP-----RFQELSKDKLGKAGLVReisfgTTKDRMLVIE----------QCKNSKA----------------- 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 367 laklaggvAVIKVGAASETELKERKLRIEDALNSTRAAVEEG-IVAGGGTALVNIYQKVSEI--KAEGDVETGVNIVLQA 443
Cdd:TIGR02343 378 --------VTIFIRGGNKMIIEEAKRSIHDALCVVRNLIKDSrIVYGGGAAEISCSLAVSQEadKYPGVEQYAIRAFADA 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 444 LQAPVRQIAENAGLE-----GSIIVERLKHAEAGVGFNAATNEWVNMLEEGIVDPTKVTRSALQHAASVAAMFLTTEAVV 518
Cdd:TIGR02343 450 LETIPMALAENSGLDpigtlSTLKSLQLKEKNPNLGVDCLGYGTNDMKEQFVFETLIGKKQQILLATQLVRMILKIDDVI 529
|
..
gi 488432175 519 AS 520
Cdd:TIGR02343 530 SP 531
|
|
| TCP1_epsilon |
cd03339 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ... |
9-190 |
2.46e-14 |
|
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: 75.41 E-value: 2.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 9 EDARQAMLRGVD----------KLANAVKVTIGPKGrnvvLDKDYTTP----LITNDGVTIAKEIELEDPYenmgAKLVQ 74
Cdd:cd03339 12 EQEKKKRLKGLEahkshilaakSVANILRTSLGPRG----MDKILVSPdgevTVTNDGATILEKMDVDHQI----AKLLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 75 EVANKTNEIAGDGTTTATVLAQSMIQEGLKNVTSGANPVGLRQGIDKAVQVAIEALHEISQKVE----NKNEIAQVGAIS 150
Cdd:cd03339 84 ELSKSQDDEIGDGTTGVVVLAGALLEQAEKLLDRGIHPIRIADGYEQACKIAVEHLEEIADKIEfspdNKEPLIQTAMTS 163
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488432175 151 AADEEIGRYiSEAMDKVGNDGVITIE--ESNGFNTELEVVEG 190
Cdd:cd03339 164 LGSKIVSRC-HRQFAEIAVDAVLSVAdlERKDVNFELIKVEG 204
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
9-135 |
1.25e-13 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 73.14 E-value: 1.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 9 EDARQAMLRGVDKLANAVKVTIGPKGRNVVL-----DKDYTTPLITNDGVTIAKEIELEDPyenmGAKLVQEVANKTNEI 83
Cdd:PTZ00212 21 ETARLQSFVGAIAVADLVKTTLGPKGMDKILqpmseGPRSGNVTVTNDGATILKSVWLDNP----AAKILVDISKTQDEE 96
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 488432175 84 AGDGTTTATVLAQSMIQEGLKNVTSGANPVGLRQGIDKAVQVAIEALHEISQ 135
Cdd:PTZ00212 97 VGDGTTSVVVLAGELLREAEKLLDQKIHPQTIIEGWRMALDVARKALEEIAF 148
|
|
| TCP1_beta |
cd03336 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ... |
9-135 |
1.97e-13 |
|
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: 72.75 E-value: 1.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 9 EDARQAMLRGVDKLANAVKVTIGPKGRNVVL--DKDYTTPLITNDGVTIAKEIELEDPyenmGAKLVQEVANKTNEIAGD 86
Cdd:cd03336 12 ETARLSSFVGAIAIGDLVKTTLGPKGMDKILqsVGRSGGVTVTNDGATILKSIGVDNP----AAKVLVDISKVQDDEVGD 87
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 488432175 87 GTTTATVLAQSMIQEGLKNVTSGANPVGLRQGIDKAVQVAIEALHEISQ 135
Cdd:cd03336 88 GTTSVTVLAAELLREAEKLVAQKIHPQTIIEGYRMATAAAREALLSSAV 136
|
|
| chap_CCT_eta |
TIGR02345 |
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ... |
5-518 |
3.33e-13 |
|
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: 72.10 E-value: 3.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 5 LKFSEDARQAML------RGVDKLANAVKVTIGPKGRNVVLDKDYTTPLITNDGVTIAKEIELEDPyenmGAKLVQEVAN 78
Cdd:TIGR02345 7 LKEGTDTSQGKGqlisniNACVAIAEALKTTLGPRGMDKLIVGSNGKATISNDGATILKLLDIVHP----AAKTLVDIAK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 79 KTNEIAGDGTTTATVLAQSMIQEGLKNVTSGANPVGLRQGIDKAVQVAIEALHEISQKVENKN----EIAQVGAISAADE 154
Cdd:TIGR02345 83 SQDAEVGDGTTSVTILAGELLKEAKPFIEEGVHPQLIIRCYREALSLAVEKIKEIAVTIDEEKgeqrELLEKCAATALSS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 155 EIGRYISEAMDKVGNDGVITIEESN-------------GFNTELEVVEGMQFDR-----GY-QSPYMVtdSDKMI----- 210
Cdd:TIGR02345 163 KLISHNKEFFSKMIVDAVLSLDRDDldlkligikkvqgGALEDSQLVNGVAFKKtfsyaGFeQQPKKF--ANPKIlllnv 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 211 -----AELERPYILVTDKKitSFQD--------ILPLLEQVVQSSrpilivadevegdalTNIVLNRMrgtftavavkap 277
Cdd:TIGR02345 241 elelkAEKDNAEIRVEDVE--DYQAivdaewaiIFRKLEKIVESG---------------ANVVLSKL------------ 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 278 GFGDRRKAMLEDLAILTGAQVITDDLGLELKDASLDMLGTAnkvevtkdhttvvdgngdeNNIDARVGQIKAQIEETDSE 357
Cdd:TIGR02345 292 PIGDLATQYFADRDIFCAGRVSAEDLKRVIKACGGSIQSTT-------------------SDLEADVLGTCALFEERQIG 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 358 FDKEKLQERLAKLAGGVAVIKVGAASETELKERKLriEDALNSTRAAVE-EGIVAGGGTALVNIYQKVSEI--KAEGDVE 434
Cdd:TIGR02345 353 SERYNYFTGCPHAKTCTIILRGGAEQFIEEAERSL--HDAIMIVRRALKnKKIVAGGGAIEMELSKCLRDYskTIDGKQQ 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 435 TGVNIVLQALQAPVRQIAENAGLEGSIIVE--RLKHAEAGV--GFNAATNEWVNMLEEGIVDPTKVTRSALQHAASVAAM 510
Cdd:TIGR02345 431 LIINAFAKALEIIPRQLCENAGFDSIEILNklRSRHAKGGKwyGVDINTEDIGDNFEAFVWEPALVKINALKAAFEAACT 510
|
....*...
gi 488432175 511 FLTTEAVV 518
Cdd:TIGR02345 511 ILSVDETI 518
|
|
| TCP1_eta |
cd03340 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ... |
21-142 |
1.32e-11 |
|
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: 66.93 E-value: 1.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 21 KLANAVKVTIGPKGRNVVLDKDYTTPLITNDGVTIAKEIELEDPyenmGAKLVQEVANKTNEIAGDGTTTATVLAQSMIQ 100
Cdd:cd03340 27 AIADAVRTTLGPRGMDKLIVDGRGKVTISNDGATILKLLDIVHP----AAKTLVDIAKSQDAEVGDGTTSVVVLAGEFLK 102
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 488432175 101 EGLKNVTSGANPVGLRQGIDKAVQVAIEALHEISQKVENKNE 142
Cdd:cd03340 103 EAKPFIEDGVHPQIIIRGYRKALQLAIEKIKEIAVNIDKEDK 144
|
|
| chap_CCT_alpha |
TIGR02340 |
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ... |
9-139 |
2.01e-10 |
|
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: 63.20 E-value: 2.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 9 EDARQAMLRGVDKLANAVKVTIGPKGRNVVLDKDYTTPLITNDGVTIAKEIELEDPyenmGAKLVQEVANKTNEIAGDGT 88
Cdd:TIGR02340 11 QDVRTQNVTAAMAIANIVKTSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHP----AAKILVELAQLQDREVGDGT 86
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 488432175 89 TTATVLAQSMIQEGLKNVTSGANPVGLRQGIDKAVQVAIEALHE-ISQKVEN 139
Cdd:TIGR02340 87 TSVVIIAAELLKRADELVKNKIHPTSVISGYRLACKEAVKYIKEnLSVSVDE 138
|
|
| chap_CCT_gamma |
TIGR02344 |
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ... |
9-521 |
8.66e-10 |
|
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: 61.29 E-value: 8.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 9 EDARQAMLRGVDK---LANAVKVTIGPKGRNVVLDKDYTTPLITNDGVTIAKEIELEDPyenmGAKLVQEVANKTNEIAG 85
Cdd:TIGR02344 12 ESGRKAQLSNIQAakaVADIIRTCLGPRSMLKMLLDPMGGIVMTNDGNAILREIDVAHP----AAKSMIELSRTQDEEVG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 86 DGTTTATVLAQSMIQEGLKNVTSGANPVGLRQGIDKAVQVAIEALHEISQKVENKNEIAQVGAISA--ADEEIGRYiSEA 163
Cdd:TIGR02344 88 DGTTSVIILAGEMLSVAEPFLEQNIHPTVIIRAYRKALDDALSVLEEISIPVDVNDDAAMLKLIQSciGTKFVSRW-SDL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 164 MDKVGNDGVITIEESNGFNTELE-------------------VVEGMQFDRGYQSPymvtdsdKMIAELERPYILVTD-- 222
Cdd:TIGR02344 167 MCDLALDAVRTVQRDENGRKEIDikryakvekipggdiedscVLKGVMINKDVTHP-------KMRRYIENPRIVLLDcp 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 223 --------------KKITSFQDILPLLEQVVQ-------SSRPILIVADEVEGDALTNIVLnrmRGTFTAvavkapgFGD 281
Cdd:TIGR02344 240 leykkgesqtnieiTKEEDWNRILQMEEEYVQlmcediiAVKPDLVITEKGVSDLAQHYLL---KANITA-------IRR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 282 RRKAMLEDLAILTGAQVItddlglelkdasldmlgtaNKVEVTKdhttvvdgngdENNIDARVG--QIKAQIEETDSEFD 359
Cdd:TIGR02344 310 VRKTDNNRIARACGATIV-------------------NRPEELR-----------ESDVGTGCGlfEVKKIGDEYFTFIT 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 360 KEKLQERLAKLAGGvavikvgaASETELKERKLRIEDALNSTRAAVEEG-IVAGGGTALVNIYQKVSEI--KAEGDVETG 436
Cdd:TIGR02344 360 ECKDPKACTILLRG--------ASKDILNEVERNLQDAMAVARNVLLDPkLVPGGGATEMAVSVALTEKskKLEGVEQWP 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 437 VNIVLQALQAPVRQIAENAGLE--GSIIVERLKHAEAG---VGFNAATNEWVNMLEEGIVDPTKVTRSALQHAASVAAMF 511
Cdd:TIGR02344 432 YRAVADALEIIPRTLAQNCGANviRTLTELRAKHAQENnctWGIDGETGKIVDMKEKGIWEPLAVKLQTYKTAIESACLL 511
|
570
....*....|
gi 488432175 512 LTTEAVVASI 521
Cdd:TIGR02344 512 LRIDDIVSGV 521
|
|
| TCP1_alpha |
cd03335 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ... |
9-139 |
1.11e-09 |
|
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: 60.76 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 9 EDARQAMLRGVDKLANAVKVTIGPKGRNVVLDKDYTTPLITNDGVTIAKEIELEDPyenmGAKLVQEVANKTNEIAGDGT 88
Cdd:cd03335 7 QDVRTQNVTAAMAIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHP----AAKILVELAQLQDKEVGDGT 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 488432175 89 TTATVLAQSMIQEGLKNVTSGANPVGLRQGIDKAVQVAIEALHE-ISQKVEN 139
Cdd:cd03335 83 TSVVIIAAELLKRANELVKQKIHPTTIISGYRLACKEAVKYIKEhLSISVDN 134
|
|
| chap_CCT_beta |
TIGR02341 |
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ... |
8-130 |
1.46e-09 |
|
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: 60.26 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 8 SEDARQAMLRGVDKLANAVKVTIGPKGRNVVL--DKDYTTPLITNDGVTIAKEIELEDPyenmGAKLVQEVANKTNEIAG 85
Cdd:TIGR02341 12 AENARLSSFVGAIAIGDLVKSTLGPKGMDKILqsSSSDASIMVTNDGATILKSIGVDNP----AAKVLVDMSKVQDDEVG 87
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 488432175 86 DGTTTATVLAQSMIQEGLKNVTSGANPVGLRQGIDKAVQVAIEAL 130
Cdd:TIGR02341 88 DGTTSVTVLAAELLREAEKLINQKIHPQTIIAGYREATKAARDAL 132
|
|
| TCP1_gamma |
cd03337 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ... |
22-187 |
4.76e-09 |
|
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: 58.85 E-value: 4.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 22 LANAVKVTIGPKGR-NVVLDKDYTTpLITNDGVTIAKEIELEDPyenmGAKLVQEVANKTNEIAGDGTTTATVLAQSMIQ 100
Cdd:cd03337 28 VADVIRTCLGPRAMlKMLLDPMGGI-VLTNDGNAILREIDVAHP----AAKSMIELSRTQDEEVGDGTTSVIILAGEILA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 101 EGLKNVTSGANPVGLRQGIDKAVQVAIEALHEISQKVENKNEIAQVGAISAAdeeIG-RYISEAMDKVGN---DGVITIE 176
Cdd:cd03337 103 VAEPFLERGIHPTVIIKAYRKALEDALKILEEISIPVDVNDRAQMLKIIKSC---IGtKFVSRWSDLMCNlalDAVKTVA 179
|
170
....*....|..
gi 488432175 177 -ESNGFNTELEV 187
Cdd:cd03337 180 vEENGRKKEIDI 191
|
|
| TCP1_theta |
cd03341 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ... |
6-518 |
1.26e-08 |
|
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: 57.23 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 6 KFSEDARQAMLRGVD---KLANAVKVTIGPKGRN--VV--LDKDYttplITNDGVTIAKEIELEDPyenmGAKLVQEVAN 78
Cdd:cd03341 1 RHYSGLEEAVLRNIEackELSQITRTSYGPNGMNkmVInhLEKLF----VTSDAATILRELEVQHP----AAKLLVMASQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 79 KTNEIAGDGTTTATVLAQSMIQEGLKNVTSGANPVGLRQGIDKAVQVAIEALHEIS-QKVENKNEIAQV-GAISAAdeeI 156
Cdd:cd03341 73 MQEEEIGDGTNLVVVLAGELLEKAEELLRMGLHPSEIIEGYEKALKKALEILEELVvYKIEDLRNKEEVsKALKTA---I 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 157 GRYISEAMD---KVGNDGVITI--EESNGFN--------------TELEVVEGMQFDRgyqspymvtdsdkmiaELERPY 217
Cdd:cd03341 150 ASKQYGNEDflsPLVAEACISVlpENIGNFNvdnirvvkilggslEDSKVVRGMVFKR----------------EPEGSV 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 218 ILVTDKKITSFQDILPLLEQVVqssrpilIVADEVEGDALTniVLNRmrgtFTAVAVKAPG-FGDRRkamledLAILTGA 296
Cdd:cd03341 214 KRVKKAKVAVFSCPFDIGVNVI-------VAGGSVGDLALH--YCNK----YGIMVIKINSkFELRR------LCRTVGA 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 297 QVITddlglELKDASLDMLGTANKVEVTKDHTTVVdgngdennidarvgqIKAQIEETDSEfdkeklqerlaklaggVAV 376
Cdd:cd03341 275 TPLP-----RLGAPTPEEIGYCDSVYVEEIGDTKV---------------VVFRQNKEDSK----------------IAT 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 377 IKVGAASETELKERKLRIEDALNSTRAAVEEG-IVAGGGTALVNIYQKvseIKAEGDVETG-----VNIVLQALQAPVRQ 450
Cdd:cd03341 319 IVLRGATQNILDDVERAIDDGVNVFKSLTKDGrFVPGAGATEIELAKK---LKEYGEKTPGleqyaIKKFAEAFEVVPRT 395
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488432175 451 IAENAGLEGSIIVERL--KHAE----AGVGFNAATNEWVNMLEEGIVDPTKVTRSALQHAASVAAMFLTTEAVV 518
Cdd:cd03341 396 LAENAGLDATEVLSELyaAHQKgnksAGVDIESGDEGTKDAKEAGIFDHLATKKWAIKLATEAAVTVLRVDQII 469
|
|
| chap_CCT_theta |
TIGR02346 |
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ... |
22-522 |
5.11e-08 |
|
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: 55.49 E-value: 5.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 22 LANAVKVTIGPKGRNVVLDKDYTTPLITNDGVTIAKEIELEDPyenmGAKLVQEVANKTNEIAGDGTTTATVLAQSMIQE 101
Cdd:TIGR02346 30 LSQITRTSLGPNGMNKMVINHLEKLFVTNDAATILRELEVQHP----AAKLLVMASEMQENEIGDGTNLVLVLAGELLNK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 102 GLKNVTSGANPVGLRQGIDKAVQVAIEALHEIS----QKVENKNEIAQVGAISAADEEIGRYisEAMDKVGNDGVITI-- 175
Cdd:TIGR02346 106 AEELIRMGLHPSEIIKGYEMALKKAMEILEELVvwevKDLRDKDELIKALKASISSKQYGNE--DFLAQLVAQACSTVlp 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 176 EESNGFNTEL--------------EVVEGMQFDRgyqspymvtDSDKMIAELERPYILV---------TDKK----ITSF 228
Cdd:TIGR02346 184 KNPQNFNVDNirvckilggslsnsEVLKGMVFNR---------EAEGSVKSVKNAKVAVfscpldtatTETKgtvlIHNA 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 229 QDILPLL---EQVVQSSrpILIVADE-----VEGDALTNIVLNRMRgTFTAVAVKAPGfgdrrKAMLEDLAILTGAQVIt 300
Cdd:TIGR02346 255 EELLNYSkgeENQIEAM--IKAIADSgvnviVTGGSVGDMALHYLN-KYNIMVLKIPS-----KFELRRLCKTVGATPL- 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 301 ddlgLELKDASLDMLGTANKVEVTKdhttvvdgngdennidarVGQIKAQIeetdseFDKEKLQERlaklaggVAVIKVG 380
Cdd:TIGR02346 326 ----PRLGAPTPEEIGYVDSVYVSE------------------IGGDKVTV------FKQENGDSK-------ISTIILR 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 381 AASETELKERKLRIEDALNSTRAAVEEG-IVAGGGTALVNIYQKVSEI--KAEGDVETGVNIVLQALQAPVRQIAENAGL 457
Cdd:TIGR02346 371 GSTDNLLDDIERAIDDGVNTVKALVKDGrLLPGAGATEIELASRLTKYgeKLPGLDQYAIKKFAEAFEIIPRTLAENAGL 450
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488432175 458 EGSIIVERL------KHAEAGVGFNAATNEWVNMLEEGIVDPTKVTRSALQHAASVAAMFLTTEAVVASIP 522
Cdd:TIGR02346 451 NANEVIPKLyaahkkGNKSKGIDIEAESDGVKDASEAGIYDMLATKKWAIKLATEAAVTVLRVDQIIMAKP 521
|
|
| chap_CCT_zeta |
TIGR02347 |
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ... |
22-518 |
5.13e-08 |
|
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: 55.51 E-value: 5.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 22 LANAVKVTIGPKGRNVVLDKDYTTPLITNDGVTIAKEIELEDPYENMGAKlvqeVANKTNEIAGDGTTTATVLAQSMIQE 101
Cdd:TIGR02347 28 LQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEMQIQHPTASMIAR----AATAQDDITGDGTTSTVLLIGELLKQ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 102 GLKNVTSGANPVGLRQGIDKAVQVAIEALHEISQKVENKNE----------------------------IAQVGAISAAD 153
Cdd:TIGR02347 104 AERYILEGVHPRIITEGFEIARKEALQFLDKFKVKKEDEVDrefllnvartslrtklpadladqlteivVDAVLAIKKDG 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 154 EEIGRYISEAMDKVGNdgvitieesngFNTELEVVEGMQFDRGYQSPYM------------------------------- 202
Cdd:TIGR02347 184 EDIDLFMVEIMEMKHK-----------SATDTTLIRGLVLDHGARHPDMprrvknayiltcnvsleyektevnsgffyss 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 203 VTDSDKMiAELERPYILVTDKKITSFQDILplleqvvqssrpilivadeVEGDALTNIVLNRMRGT--FTAVAVKAPGFG 280
Cdd:TIGR02347 253 AEQREKL-VKAERKFVDDRVKKIIELKKKV-------------------CGKSPDKGFVVINQKGIdpPSLDLLAKEGIM 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 281 DRRKAM---LEDLAILTGAQVITDdlgleLKDASLDMLGTANKV---EVTKDHTTVVDGNGDENNIdarvgqikaqieet 354
Cdd:TIGR02347 313 ALRRAKrrnMERLTLACGGEALNS-----VEDLTPECLGWAGLVyetTIGEEKYTFIEECKNPKSC-------------- 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 355 dsefdkeklqerlaklaggvaVIKVGAASETELKERKLRIEDALNSTRAAVEEG-IVAGGGTALVNIYQKVSEIK--AEG 431
Cdd:TIGR02347 374 ---------------------TILIKGPNDHTIAQIKDAVRDGLRAVKNAIEDKcVVPGAGAFEIAAYRHLKEYKksVKG 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 432 DVETGVNIVLQALQAPVRQIAENAGLEgsiIVERL-----KHAEAG--VGFNAATNEWVNMLEEGIVDPTKVTRSALQHA 504
Cdd:TIGR02347 433 KAKLGVEAFANALLVIPKTLAENSGFD---AQDTLvkledEHDEGGevVGVDLNTGEPIDPEIKGIWDNYRVKKQLIQSA 509
|
570
....*....|....
gi 488432175 505 ASVAAMFLTTEAVV 518
Cdd:TIGR02347 510 TVIASQLLLVDEVM 523
|
|
| TCP1_zeta |
cd03342 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
22-512 |
7.59e-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: 48.41 E-value: 7.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 22 LANAVKVTIGPKGRNVVLDKDYTTPLITNDGVTIAKEIELEDPYENMGAKlvqeVANKTNEIAGDGTTTATVLAQSMIQE 101
Cdd:cd03342 24 LQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLSEMQIQHPTASMIAR----AATAQDDITGDGTTSNVLLIGELLKQ 99
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 102 GLKNVTSGANPVGLRQGIDKAVQVAIEALHEISQKVENKN--EIAQVGAISAADEEIGRYISEAMDKVGNDGVITIEESN 179
Cdd:cd03342 100 AERYIQEGVHPRIITEGFELAKNKALKFLESFKVPVEIDTdrELLLSVARTSLRTKLHADLADQLTEIVVDAVLAIYKPD 179
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170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 180 ---------------GFNTELEVVEGMQFDRGYQSPYMVTDsdkmiaeLERPYILVTDKKI--------TSFqdilplLE 236
Cdd:cd03342 180 epidlhmveimqmqhKSDSDTKLIRGLVLDHGARHPDMPKR-------VENAYILTCNVSLeyektevnSGF------FY 246
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250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 237 QVVQSSRPIlivaDEVEGDALT--NIV-LNRMRgtftavavkapgfgdRRKamLEDLAILTGAQVIT--DDLglelkdaS 311
Cdd:cd03342 247 SVVINQKGI----DPPSLDMLAkeGILaLRRAK---------------RRN--MERLTLACGGVAMNsvDDL-------S 298
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330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 312 LDMLGTANKVEVTK---DHTTVVdgngdENNIDARVGQIkaqieetdsefdkeklqerlaklaggvaVIKvgAASETELK 388
Cdd:cd03342 299 PECLGYAGLVYERTlgeEKYTFI-----EGVKNPKSCTI----------------------------LIK--GPNDHTIT 343
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410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432175 389 ERKLRIEDALNSTRAAVEEG-IVAGGGTALVNIYQKVSEIK--AEGDVETGVNIVLQALQAPVRQIAENAGLEgsiIVER 465
Cdd:cd03342 344 QIKDAIRDGLRAVKNAIEDKcVVPGAGAFEVALYAHLKEFKksVKGKAKLGVQAFADALLVIPKTLAENSGLD---VQET 420
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490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 488432175 466 L-----KHAEAG--VGFNAATNEWVNMLEEGIVDPTKVTRSALQHAASVAAMFL 512
Cdd:cd03342 421 LvklqdEYAEGGqvGGVDLDTGEPMDPESEGIWDNYSVKRQILHSATVIASQLL 474
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