|
Name |
Accession |
Description |
Interval |
E-value |
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
1-537 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 978.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 1 MVKQLKFSEDARQAMLRGVDQLANAVKVTIGPKGRNVVLDKEFTAPLITNDGVTIAKEIELEDPYENMGAKLVQEVANKT 80
Cdd:PRK00013 1 MAKDIKFGEDARRKLLRGVNKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDPFENMGAQLVKEVASKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 81 NEIAGDGTTTATVLAQAMIQEGLKNVTSGANPVGLRQGIDKAVKVAVEALHENSQKVENKNEIAQVGAISA-ADEEIGRY 159
Cdd:PRK00013 81 NDVAGDGTTTATVLAQAIVREGLKNVAAGANPMDLKRGIDKAVEAAVEELKKISKPVEDKEEIAQVATISAnGDEEIGKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 160 ISEAMEKVGNDGVITIEESNGLNTELEVVEGMQFDRGYQSPYMVTDSDKMVAELERPYILVTDKKISSFQDILPLLEQVV 239
Cdd:PRK00013 161 IAEAMEKVGKEGVITVEESKGFETELEVVEGMQFDRGYLSPYFVTDPEKMEAELENPYILITDKKISNIQDLLPVLEQVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 240 QSNRPILIVADEVEGDALTNIVLNRMRGTFTAVAVKAPGFGDRRKAMLEDLAILTGAQVITDDLGLDLKDASIDMLGTAS 319
Cdd:PRK00013 241 QSGKPLLIIAEDVEGEALATLVVNKLRGTLKVVAVKAPGFGDRRKAMLEDIAILTGGTVISEELGLKLEDATLEDLGQAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 320 KVEVTKDNTTVVDGDGDENSIDARVSQLKSQIEETESDFDREKLQERLAKLAGGVAVIKVGAASETELKERKLRIEDALN 399
Cdd:PRK00013 321 KVVVTKDNTTIVDGAGDKEAIKARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATEVEMKEKKDRVEDALH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 400 STRAAVEEGIVAGGGTALVNVYQKVSEIE-AEGDIETGVNIVLKALTAPVRQIAENAGLEGSVIVERLKNAEP-GVGFNA 477
Cdd:PRK00013 401 ATRAAVEEGIVPGGGVALLRAAPALEALKgLNGDEATGINIVLRALEAPLRQIAENAGLEGSVVVEKVKNGKGkGYGYNA 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446162787 478 ATNEWVNMLEAGIVDPTKVTRSALQHAASVAAMFLTTEAVVASIPEKNNDQPNM--GGMPGM 537
Cdd:PRK00013 481 ATGEYVDMIEAGIIDPTKVTRSALQNAASVAGLLLTTEAVVADKPEKKAAAPPMggGGMGGM 542
|
|
| groEL |
PRK12849 |
chaperonin GroEL; Reviewed |
1-537 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237230 Cd Length: 542 Bit Score: 876.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 1 MVKQLKFSEDARQAMLRGVDQLANAVKVTIGPKGRNVVLDKEFTAPLITNDGVTIAKEIELEDPYENMGAKLVQEVANKT 80
Cdd:PRK12849 1 MAKIIKFDEEARRALERGVNKLADAVKVTLGPKGRNVVIDKSFGAPTITKDGVSIAKEIELEDPFENLGAQLVKEVASKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 81 NEIAGDGTTTATVLAQAMIQEGLKNVTSGANPVGLRQGIDKAVKVAVEALHENSQKVENKNEIAQVGAISA-ADEEIGRY 159
Cdd:PRK12849 81 NDVAGDGTTTATVLAQALVQEGLKNVAAGANPMDLKRGIDKAVEAVVEELKALARPVSGSEEIAQVATISAnGDEEIGEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 160 ISEAMEKVGNDGVITIEESNGLNTELEVVEGMQFDRGYQSPYMVTDSDKMVAELERPYILVTDKKISSFQDILPLLEQVV 239
Cdd:PRK12849 161 IAEAMEKVGKDGVITVEESKTLETELEVTEGMQFDRGYLSPYFVTDPERMEAVLEDPLILLTDKKISSLQDLLPLLEKVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 240 QSNRPILIVADEVEGDALTNIVLNRMRGTFTAVAVKAPGFGDRRKAMLEDLAILTGAQVITDDLGLDLKDASIDMLGTAS 319
Cdd:PRK12849 241 QSGKPLLIIAEDVEGEALATLVVNKLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGLKLEEVTLDDLGRAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 320 KVEVTKDNTTVVDGDGDENSIDARVSQLKSQIEETESDFDREKLQERLAKLAGGVAVIKVGAASETELKERKLRIEDALN 399
Cdd:PRK12849 321 RVTITKDNTTIVDGAGDKEAIEARVAQIRRQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATEVELKERKDRVEDALN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 400 STRAAVEEGIVAGGGTALVNVYQKVSEIE-AEGDIETGVNIVLKALTAPVRQIAENAGLEGSVIVERLKNAEPGVGFNAA 478
Cdd:PRK12849 401 ATRAAVEEGIVPGGGVALLRAAKALDELAgLNGDQAAGVEIVRRALEAPLRQIAENAGLDGSVVVAKVLELEDGFGFNAA 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 446162787 479 TNEWVNMLEAGIVDPTKVTRSALQHAASVAAMFLTTEAVVASIPEKNNDQPNMGGMPGM 537
Cdd:PRK12849 481 TGEYGDLIAAGIIDPVKVTRSALQNAASVAGLLLTTEALVADKPEEEDPPGGMGGMGGM 539
|
|
| 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: 868.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 3 KQLKFSEDARQAMLRGVDQLANAVKVTIGPKGRNVVLDKEFTAPLITNDGVTIAKEIELEDPYENMGAKLVQEVANKTNE 82
Cdd:cd03344 1 KDIKFGEEARKALLRGVNKLADAVKVTLGPKGRNVVIEKSFGSPKITKDGVTVAKEIELEDPFENMGAQLVKEVASKTND 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 83 IAGDGTTTATVLAQAMIQEGLKNVTSGANPVGLRQGIDKAVKVAVEALHENSQKVENKNEIAQVGAISA-ADEEIGRYIS 161
Cdd:cd03344 81 VAGDGTTTATVLARAIIKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKPVKTKEEIAQVATISAnGDEEIGELIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 162 EAMEKVGNDGVITIEESNGLNTELEVVEGMQFDRGYQSPYMVTDSDKMVAELERPYILVTDKKISSFQDILPLLEQVVQS 241
Cdd:cd03344 161 EAMEKVGKDGVITVEEGKTLETELEVVEGMQFDRGYLSPYFVTDPEKMEVELENPYILLTDKKISSIQELLPILELVAKA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 242 NRPILIVADEVEGDALTNIVLNRMRGTFTAVAVKAPGFGDRRKAMLEDLAILTGAQVITDDLGLDLKDASIDMLGTASKV 321
Cdd:cd03344 241 GRPLLIIAEDVEGEALATLVVNKLRGGLKVCAVKAPGFGDRRKAMLEDIAILTGGTVISEELGLKLEDVTLEDLGRAKKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 322 EVTKDNTTVVDGDGDENSIDARVSQLKSQIEETESDFDREKLQERLAKLAGGVAVIKVGAASETELKERKLRIEDALNST 401
Cdd:cd03344 321 VVTKDDTTIIGGAGDKAAIKARIAQIRKQIEETTSDYDKEKLQERLAKLSGGVAVIKVGGATEVELKEKKDRVEDALNAT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 402 RAAVEEGIVAGGGTALVNVYQKVSEIEAE-GDIETGVNIVLKALTAPVRQIAENAGLEGSVIVERLKNAEPGVGFNAATN 480
Cdd:cd03344 401 RAAVEEGIVPGGGVALLRASPALDKLKALnGDEKLGIEIVRRALEAPLRQIAENAGVDGSVVVEKVLESPDGFGYDAATG 480
|
490 500 510
....*....|....*....|....*....|....*....
gi 446162787 481 EWVNMLEAGIVDPTKVTRSALQHAASVAAMFLTTEAVVA 519
Cdd:cd03344 481 EYVDMIEAGIIDPTKVVRSALQNAASVASLLLTTEALVV 519
|
|
| GroEL |
TIGR02348 |
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ... |
3-523 |
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: 838.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 3 KQLKFSEDARQAMLRGVDQLANAVKVTIGPKGRNVVLDKEFTAPLITNDGVTIAKEIELEDPYENMGAKLVQEVANKTNE 82
Cdd:TIGR02348 2 KQIKFDEEARKALLRGVDKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDKFENMGAQLVKEVASKTND 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 83 IAGDGTTTATVLAQAMIQEGLKNVTSGANPVGLRQGIDKAVKVAVEALHENSQKVENKNEIAQVGAISA-ADEEIGRYIS 161
Cdd:TIGR02348 82 VAGDGTTTATVLAQAIVKEGLKNVAAGANPIELKRGIEKAVEAVVEELKKLSKPVKGKKEIAQVATISAnNDEEIGSLIA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 162 EAMEKVGNDGVITIEESNGLNTELEVVEGMQFDRGYQSPYMVTDSDKMVAELERPYILVTDKKISSFQDILPLLEQVVQS 241
Cdd:TIGR02348 162 EAMEKVGKDGVITVEESKSLETELEVVEGMQFDRGYISPYFVTDAEKMEVELENPYILITDKKISNIKDLLPLLEKVAQS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 242 NRPILIVADEVEGDALTNIVLNRMRGTFTAVAVKAPGFGDRRKAMLEDLAILTGAQVITDDLGLDLKDASIDMLGTASKV 321
Cdd:TIGR02348 242 GKPLLIIAEDVEGEALATLVVNKLRGTLNVCAVKAPGFGDRRKAMLEDIAILTGGQVISEELGLKLEEVTLDDLGKAKKV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 322 EVTKDNTTVVDGDGDENSIDARVSQLKSQIEETESDFDREKLQERLAKLAGGVAVIKVGAASETELKERKLRIEDALNST 401
Cdd:TIGR02348 322 TVDKDNTTIVEGAGDKAAIKARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATETEMKEKKLRIEDALNAT 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 402 RAAVEEGIVAGGGTALVNVYQKVSEIEAEG-DIETGVNIVLKALTAPVRQIAENAGLEGSVIVERLKNAEPGVGFNAATN 480
Cdd:TIGR02348 402 RAAVEEGIVPGGGVALLRAAAALEGLKGDGeDEAIGIDIVKRALEAPLRQIAENAGLDGAVVAEKVKELKGNFGFNAATG 481
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 446162787 481 EWVNMLEAGIVDPTKVTRSALQHAASVAAMFLTTEAVVASIPE 523
Cdd:TIGR02348 482 EYEDLVEAGIIDPTKVTRSALQNAASIAGLLLTTEAVVADKPE 524
|
|
| groEL |
PRK12850 |
chaperonin GroEL; Reviewed |
1-537 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237231 Cd Length: 544 Bit Score: 807.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 1 MVKQLKFSEDARQAMLRGVDQLANAVKVTIGPKGRNVVLDKEFTAPLITNDGVTIAKEIELEDPYENMGAKLVQEVANKT 80
Cdd:PRK12850 2 AAKEIRFSTDARDRLLRGVNILANAVKVTLGPKGRNVVLEKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVKEVASKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 81 NEIAGDGTTTATVLAQAMIQEGLKNVTSGANPVGLRQGIDKAVKVAVEALHENSQKVENKNEIAQVGAISA-ADEEIGRY 159
Cdd:PRK12850 82 NDLAGDGTTTATVLAQAIVREGAKLVAAGMNPMDLKRGIDLAVAAVVDELKKIAKKVTSSKEIAQVATISAnGDESIGEM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 160 ISEAMEKVGNDGVITIEESNGLNTELEVVEGMQFDRGYQSPYMVTDSDKMVAELERPYILVTDKKISSFQDILPLLEQVV 239
Cdd:PRK12850 162 IAEAMDKVGKEGVITVEEAKTLGTELDVVEGMQFDRGYLSPYFVTNPEKMRAELEDPYILLHEKKISNLQDLLPILEAVV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 240 QSNRPILIVADEVEGDALTNIVLNRMRGTFTAVAVKAPGFGDRRKAMLEDLAILTGAQVITDDLGLDLKDASIDMLGTAS 319
Cdd:PRK12850 242 QSGRPLLIIAEDVEGEALATLVVNKLRGGLKSVAVKAPGFGDRRKAMLEDIAVLTGGQVISEDLGIKLENVTLDMLGRAK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 320 KVEVTKDNTTVVDGDGDENSIDARVSQLKSQIEETESDFDREKLQERLAKLAGGVAVIKVGAASETELKERKLRIEDALN 399
Cdd:PRK12850 322 RVLITKENTTIIDGAGDKKNIEARVKQIRAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKEKKDRVDDALH 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 400 STRAAVEEGIVAGGGTALVNVYQKVSEIE-AEGDIETGVNIVLKALTAPVRQIAENAGLEGSVIVERLKNAEPGVGFNAA 478
Cdd:PRK12850 402 ATRAAVEEGIVPGGGVALLRARSALRGLKgANADETAGIDIVRRALEEPLRQIATNAGFEGSVVVGKVAELPGNFGFNAQ 481
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446162787 479 TNEWVNMLEAGIVDPTKVTRSALQHAASVAAMFLTTEAVVASIPEKNNDQ--PNMGGMPGM 537
Cdd:PRK12850 482 TGEYGDMVEAGIIDPAKVTRTALQDAASIAALLITTEAMVAEAPKKAAAAaaGPGPGMGGM 542
|
|
| 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: 763.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 1 MVKQLKFSEDARQAMLRGVDQLANAVKVTIGPKGRNVVLDKEFTAPLITNDGVTIAKEIELEDPYENMGAKLVQEVANKT 80
Cdd:COG0459 1 MAKQILFGEDARRANIRGVKALADAVKVTLGPKGRNVMLVKSFGDPTITNDGVTIAKEIELEDPFENMGAQLVKEVASKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 81 NEIAGDGTTTATVLAQAMIQEGLKNVTSGANPVGLRQGIDKAVKVAVEALHENSQKVENKNEIAQVGAISAA-DEEIGRY 159
Cdd:COG0459 81 NDEAGDGTTTATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPVDDKEELAQVATISANgDEEIGEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 160 ISEAMEKVGNDGVITIEESNGLNTELEVVEGMQFDRGYQSPYMVTDSDKMVAELERPYILVTDKKISSFQDILPLLEQVV 239
Cdd:COG0459 161 IAEAMEKVGKDGVITVEEGKGLETELEVVEGMQFDKGYLSPYFVTDPEKMPAELENAYILLTDKKISSIQDLLPLLEKVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 240 QSNRPILIVADEVEGDALTNIVLNRMRGTFTAVAVKAPGFGDRRKAMLEDLAILTGAQVITDDLGLDLKDASIDMLGTAS 319
Cdd:COG0459 241 QSGKPLLIIAEDIDGEALATLVVNGIRGVLRVVAVKAPGFGDRRKAMLEDIAILTGGRVISEDLGLKLEDVTLDDLGRAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 320 KVEVTKDNTTVVDGDGDENSIdarvsqlksqieetesdfdreklqerlaklaggvaVIKVGAASETELKERKLRIEDALN 399
Cdd:COG0459 321 RVEVDKDNTTIVEGAGNPKAI-----------------------------------VILVGAATEVEVKERKRRVEDALH 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 400 STRAAVEEGIVAGGGTALVNVYQKVSEI--EAEGDIETGVNIVLKALTAPVRQIAENAGLEGSVIVERLKNAE-PGVGFN 476
Cdd:COG0459 366 ATRAAVEEGIVPGGGAALLRAARALRELaaKLEGDEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKVRAAKdKGFGFD 445
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 446162787 477 AATNEWVNMLEAGIVDPTKVTRSALQHAASVAAMFLTTEAVVASIPEKN 525
Cdd:COG0459 446 AATGEYVDMLEAGVIDPAKVKRSALQNAASVAGLILTTEAVIADKPEKE 494
|
|
| groEL |
PRK12851 |
chaperonin GroEL; Reviewed |
1-537 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 171770 Cd Length: 541 Bit Score: 749.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 1 MVKQLKFSEDARQAMLRGVDQLANAVKVTIGPKGRNVVLDKEFTAPLITNDGVTIAKEIELEDPYENMGAKLVQEVANKT 80
Cdd:PRK12851 2 AAKEVKFHVEAREKMLRGVNILADAVKVTLGPKGRNVVIDKSFGAPTITNDGVTIAKEIELEDKFENMGAQMVREVASKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 81 NEIAGDGTTTATVLAQAMIQEGLKNVTSGANPVGLRQGIDKAVKVAVEALHENSQKVENKNEIAQVGAISA-ADEEIGRY 159
Cdd:PRK12851 82 NDVAGDGTTTATVLAQAIVREGAKAVAAGANPMDLKRGIDRAVAAVVEELKANARPVTTNAEIAQVATISAnGDAEIGRL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 160 ISEAMEKVGNDGVITIEESNGLNTELEVVEGMQFDRGYQSPYMVTDSDKMVAELERPYILVTDKKISSFQDILPLLEQVV 239
Cdd:PRK12851 162 VAEAMEKVGNEGVITVEESKTAETELEVVEGMQFDRGYLSPYFVTDADKMEAELEDPYILIHEKKISNLQDLLPVLEAVV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 240 QSNRPILIVADEVEGDALTNIVLNRMRGTFTAVAVKAPGFGDRRKAMLEDLAILTGAQVITDDLGLDLKDASIDMLGTAS 319
Cdd:PRK12851 242 QSGKPLLIIAEDVEGEALATLVVNKLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGIKLENVTLEQLGRAK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 320 KVEVTKDNTTVVDGDGDENSIDARVSQLKSQIEETESDFDREKLQERLAKLAGGVAVIKVGAASETELKERKLRIEDALN 399
Cdd:PRK12851 322 KVVVEKENTTIIDGAGSKTEIEGRVAQIRAQIEETTSDYDREKLQERLAKLAGGVAVIRVGASTEVEVKEKKDRVDDALH 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 400 STRAAVEEGIVAGGGTALVNVYQKVSEIE-AEGDIETGVNIVLKALTAPVRQIAENAGLEGSVIVERLKNAEPGVGFNAA 478
Cdd:PRK12851 402 ATRAAVEEGIVPGGGVALLRAVKALDKLEtANGDQRTGVEIVRRALEAPVRQIAENAGAEGSVVVGKLREKPGGYGFNAA 481
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 446162787 479 TNEWVNMLEAGIVDPTKVTRSALQHAASVAAMFLTTEAVVASIPEKNNDQPNMGGmPGM 537
Cdd:PRK12851 482 TNEYGDLYAQGVIDPVKVVRTALQNAASVAGLLLTTEAMVAEKPKKEPAPPAPPG-GGM 539
|
|
| PTZ00114 |
PTZ00114 |
Heat shock protein 60; Provisional |
3-535 |
0e+00 |
|
Heat shock protein 60; Provisional
Pssm-ID: 185455 Cd Length: 555 Bit Score: 714.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 3 KQLKFSEDARQAMLRGVDQLANAVKVTIGPKGRNVVLDKEFTAPLITNDGVTIAKEIELEDPYENMGAKLVQEVANKTNE 82
Cdd:PTZ00114 15 KEIRFGDEARQSLLKGIERLADAVAVTLGPKGRNVIIEQEYGSPKITKDGVTVAKAIEFSDRFENVGAQLIRQVASKTND 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 83 IAGDGTTTATVLAQAMIQEGLKNVTSGANPVGLRQGIDKAVKVAVEALHENSQKVENKNEIAQVGAISA-ADEEIGRYIS 161
Cdd:PTZ00114 95 KAGDGTTTATILARAIFREGCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQSRPVKTKEDILNVATISAnGDVEIGSLIA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 162 EAMEKVGNDGVITIEESNGLNTELEVVEGMQFDRGYQSPYMVTDSDKMVAELERPYILVTDKKISSFQDILPLLEQVVQS 241
Cdd:PTZ00114 175 DAMDKVGKDGTITVEDGKTLEDELEVVEGMSFDRGYISPYFVTNEKTQKVELENPLILVTDKKISSIQSILPILEHAVKN 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 242 NRPILIVADEVEGDALTNIVLNRMRGTFTAVAVKAPGFGDRRKAMLEDLAILTGAQVITDD-LGLDLKDASIDMLGTASK 320
Cdd:PTZ00114 255 KRPLLIIAEDVEGEALQTLIINKLRGGLKVCAVKAPGFGDNRKDILQDIAVLTGATVVSEDnVGLKLDDFDPSMLGSAKK 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 321 VEVTKDNTTVVDGDGDENSIDARVSQLKSQIEETESDFDREKLQERLAKLAGGVAVIKVGAASETELKERKLRIEDALNS 400
Cdd:PTZ00114 335 VTVTKDETVILTGGGDKAEIKERVELLRSQIERTTSEYDKEKLKERLAKLSGGVAVIKVGGASEVEVNEKKDRIEDALNA 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 401 TRAAVEEGIVAGGGTALVNVYQKVSEIE----AEGDIETGVNIVLKALTAPVRQIAENAGLEGSVIVER-LKNAEPGVGF 475
Cdd:PTZ00114 415 TRAAVEEGIVPGGGVALLRASKLLDKLEedneLTPDQRTGVKIVRNALRLPTKQIAENAGVEGAVVVEKiLEKKDPSFGY 494
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 476 NAATNEWVNMLEAGIVDPTKVTRSALQHAASVAAMFLTTEAVVASIPEKNNDQPNMGGMP 535
Cdd:PTZ00114 495 DAQTGEYVNMFEAGIIDPTKVVRSALVDAASVASLMLTTEAAIVDLPKEKKKNKNSAAPP 554
|
|
| groEL |
PRK12852 |
chaperonin GroEL; Reviewed |
1-537 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237232 Cd Length: 545 Bit Score: 709.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 1 MVKQLKFSEDARQAMLRGVDQLANAVKVTIGPKGRNVVLDKEFTAPLITNDGVTIAKEIELEDPYENMGAKLVQEVANKT 80
Cdd:PRK12852 2 AAKDVKFSGDARDRMLRGVDILANAVKVTLGPKGRNVVIEKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVREVASKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 81 NEIAGDGTTTATVLAQAMIQEGLKNVTSGANPVGLRQGIDKAVKVAVEALHENSQKVENKNEIAQVGAISA-ADEEIGRY 159
Cdd:PRK12852 82 NDLAGDGTTTATVLAQAIVREGAKAVAAGMNPMDLKRGIDIAVAAVVKDIEKRAKPVASSAEIAQVGTISAnGDAAIGKM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 160 ISEAMEKVGNDGVITIEESNGLNTELEVVEGMQFDRGYQSPYMVTDSDKMVAELERPYILVTDKKISSFQDILPLLEQVV 239
Cdd:PRK12852 162 IAQAMQKVGNEGVITVEENKSLETEVDIVEGMKFDRGYLSPYFVTNAEKMTVELDDAYILLHEKKLSGLQAMLPVLEAVV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 240 QSNRPILIVADEVEGDALTNIVLNRMRGTFTAVAVKAPGFGDRRKAMLEDLAILTGAQVITDDLGLDLKDASIDMLGTAS 319
Cdd:PRK12852 242 QSGKPLLIIAEDVEGEALATLVVNRLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGQLISEDLGIKLENVTLKMLGRAK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 320 KVEVTKDNTTVVDGDGDENSIDARVSQLKSQIEETESDFDREKLQERLAKLAGGVAVIKVGAASETELKERKLRIEDALN 399
Cdd:PRK12852 322 KVVIDKENTTIVNGAGKKADIEARVGQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKEKKDRVEDALN 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 400 STRAAVEEGIVAGGGTALVNVYQKVSEIE-AEGDIETGVNIVLKALTAPVRQIAENAGLEGSVIVER-LKNAEPGVGFNA 477
Cdd:PRK12852 402 ATRAAVQEGIVPGGGVALLRAKKAVGRINnDNADVQAGINIVLKALEAPIRQIAENAGVEGSIVVGKiLENKSETFGFDA 481
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 478 ATNEWVNMLEAGIVDPTKVTRSALQHAASVAAMFLTTEAVVASIPEKnNDQPNMGGMPGM 537
Cdd:PRK12852 482 QTEEYVDMVAKGIIDPAKVVRTALQDAASVAGLLVTTEAMVAELPKK-DAAPAMPAGGGM 540
|
|
| groEL |
CHL00093 |
chaperonin GroEL |
1-525 |
0e+00 |
|
chaperonin GroEL
Pssm-ID: 177025 Cd Length: 529 Bit Score: 693.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 1 MVKQLKFSEDARQAMLRGVDQLANAVKVTIGPKGRNVVLDKEFTAPLITNDGVTIAKEIELEDPYENMGAKLVQEVANKT 80
Cdd:CHL00093 1 MSKKILYQDNARRALERGMDILAEAVSVTLGPKGRNVVLEKKYGSPQIVNDGVTIAKEIELEDHIENTGVALIRQAASKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 81 NEIAGDGTTTATVLAQAMIQEGLKNVTSGANPVGLRQGIDKAVKVAVEALHENSQKVENKNEIAQVGAISAA-DEEIGRY 159
Cdd:CHL00093 81 NDVAGDGTTTATVLAYAIVKQGMKNVAAGANPISLKRGIEKATQYVVSQIAEYARPVEDIQAITQVASISAGnDEEVGSM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 160 ISEAMEKVGNDGVITIEESNGLNTELEVVEGMQFDRGYQSPYMVTDSDKMVAELERPYILVTDKKISSF-QDILPLLEQV 238
Cdd:CHL00093 161 IADAIEKVGREGVISLEEGKSTVTELEITEGMRFEKGFISPYFVTDTERMEVVQENPYILLTDKKITLVqQDLLPILEQV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 239 VQSNRPILIVADEVEGDALTNIVLNRMRGTFTAVAVKAPGFGDRRKAMLEDLAILTGAQVITDDLGLDLKDASIDMLGTA 318
Cdd:CHL00093 241 TKTKRPLLIIAEDVEKEALATLVLNKLRGIVNVVAVRAPGFGDRRKAMLEDIAILTGGQVITEDAGLSLETIQLDLLGQA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 319 SKVEVTKDNTTVVdGDGDENSIDARVSQLKSQIEETESDFDREKLQERLAKLAGGVAVIKVGAASETELKERKLRIEDAL 398
Cdd:CHL00093 321 RRIIVTKDSTTII-ADGNEEQVKARCEQLRKQIEIADSSYEKEKLQERLAKLSGGVAVIKVGAATETEMKDKKLRLEDAI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 399 NSTRAAVEEGIVAGGGTALVNVYQKV---SEIEAEGDIETGVNIVLKALTAPVRQIAENAGLEGSVIVERLKNAEPGVGF 475
Cdd:CHL00093 400 NATKAAVEEGIVPGGGATLVHLSENLktwAKNNLKEDELIGALIVARAILAPLKRIAENAGKNGSVIIEKVQEQDFEIGY 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 446162787 476 NAATNEWVNMLEAGIVDPTKVTRSALQHAASVAAMFLTTEAVVASIPEKN 525
Cdd:CHL00093 480 NAANNKFVNMYEAGIIDPAKVTRSALQNAASIASMILTTECIIVDKKESS 529
|
|
| PRK14104 |
PRK14104 |
chaperonin GroEL; Provisional |
3-537 |
0e+00 |
|
chaperonin GroEL; Provisional
Pssm-ID: 172594 Cd Length: 546 Bit Score: 625.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 3 KQLKFSEDARQAMLRGVDQLANAVKVTIGPKGRNVVLDKEFTAPLITNDGVTIAKEIELEDPYENMGAKLVQEVANKTNE 82
Cdd:PRK14104 4 KEVKFGVDARDRMLRGVDILANAVKVTLGPKGRNVVLDKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVREVASKSAD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 83 IAGDGTTTATVLAQAMIQEGLKNVTSGANPVGLRQGIDKAVKVAVEALHENSQKVENKNEIAQVGAISA-ADEEIGRYIS 161
Cdd:PRK14104 84 AAGDGTTTATVLAQAIVREGAKSVAAGMNPMDLKRGIDLAVEAVVADLVKNSKKVTSNDEIAQVGTISAnGDAEIGKFLA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 162 EAMEKVGNDGVITIEESNGLNTELEVVEGMQFDRGYQSPYMVTDSDKMVAELERPYILVTDKKISSFQDILPLLEQVVQS 241
Cdd:PRK14104 164 DAMKKVGNEGVITVEEAKSLETELDVVEGMQFDRGYISPYFVTNADKMRVEMDDAYILINEKKLSSLNELLPLLEAVVQT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 242 NRPILIVADEVEGDALTNIVLNRMRGTFTAVAVKAPGFGDRRKAMLEDLAILTGAQVITDDLGLDLKDASIDMLGTASKV 321
Cdd:PRK14104 244 GKPLVIVAEDVEGEALATLVVNRLRGGLKVAAVKAPGFGDRRKAMLQDIAILTGGQAISEDLGIKLENVTLQMLGRAKKV 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 322 EVTKDNTTVVDGDGDENSIDARVSQLKSQIEETESDFDREKLQERLAKLAGGVAVIKVGAASETELKERKLRIEDALNST 401
Cdd:PRK14104 324 MIDKENTTIVNGAGKKADIEARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKERKDRVDDAMHAT 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 402 RAAVEEGIVAGGGTALVNVYQKVSEIEAEGDIE-TGVNIVLKALTAPVRQIAENAGLEGSVIVER-LKNAEPGVGFNAAT 479
Cdd:PRK14104 404 RAAVEEGIVPGGGVALLRASEQLKGIKTKNDDQkTGVEIVRKALSAPARQIAINAGEDGSVIVGKiLEKEQYSYGFDSQT 483
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 446162787 480 NEWVNMLEAGIVDPTKVTRSALQHAASVAAMFLTTEAVVASIPEKNNDQPNMGGMPGM 537
Cdd:PRK14104 484 GEYGNLVSKGIIDPTKVVRTAIQNAASVAALLITTEAMVAELPKKGGAGPAMPPGGGM 541
|
|
| PLN03167 |
PLN03167 |
Chaperonin-60 beta subunit; Provisional |
3-535 |
0e+00 |
|
Chaperonin-60 beta subunit; Provisional
Pssm-ID: 215611 [Multi-domain] Cd Length: 600 Bit Score: 540.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 3 KQLKFSED--ARQAMLRGVDQLANAVKVTIGPKGRNVVLDKEFTAPLITNDGVTIAKEIELEDPYENMGAKLVQEVANKT 80
Cdd:PLN03167 57 KELHFNKDgsAIKKLQAGVNKLADLVGVTLGPKGRNVVLESKYGSPKIVNDGVTVAKEVELEDPVENIGAKLVRQAAAKT 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 81 NEIAGDGTTTATVLAQAMIQEGLKNVTSGANPVGLRQGIDKAVKVAVEALHENSQKVENkNEIAQVGAISAADE-EIGRY 159
Cdd:PLN03167 137 NDLAGDGTTTSVVLAQGLIAEGVKVVAAGANPVQITRGIEKTAKALVKELKKMSKEVED-SELADVAAVSAGNNyEVGNM 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 160 ISEAMEKVGNDGVITIEESNGLNTELEVVEGMQFDRGYQSPYMVTDSDKMVAELERPYILVTDKKISSFQDILPLLEQVV 239
Cdd:PLN03167 216 IAEAMSKVGRKGVVTLEEGKSAENNLYVVEGMQFDRGYISPYFVTDSEKMSVEYDNCKLLLVDKKITNARDLIGILEDAI 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 240 QSNRPILIVADEVEGDALTNIVLNRMRGTFTAVAVKAPGFGDRRKAMLEDLAILTGAQVITDDLGLDLKDASIDMLGTAS 319
Cdd:PLN03167 296 RGGYPLLIIAEDIEQEALATLVVNKLRGSLKIAALKAPGFGERKSQYLDDIAILTGGTVIREEVGLSLDKVGKEVLGTAA 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 320 KVEVTKDNTTVVDGDGDENSIDARVSQLKSQIEETESDFDREKLQERLAKLAGGVAVIKVGAASETELKERKLRIEDALN 399
Cdd:PLN03167 376 KVVLTKDTTTIVGDGSTQEAVNKRVAQIKNLIEAAEQDYEKEKLNERIAKLSGGVAVIQVGAQTETELKEKKLRVEDALN 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 400 STRAAVEEGIVAGGGTALVNVYQKVSEIEA--EGDIE-TGVNIVLKALTAPVRQIAENAGLEGSVIVER-LKNAEPGVGF 475
Cdd:PLN03167 456 ATKAAVEEGIVVGGGCTLLRLASKVDAIKDtlENDEQkVGADIVKRALSYPLKLIAKNAGVNGSVVSEKvLSNDNPKFGY 535
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 476 NAATNEWVNMLEAGIVDPTKVTRSALQHAASVAAMFLTTEAVVASIPEKnndQPNMGGMP 535
Cdd:PLN03167 536 NAATGKYEDLMAAGIIDPTKVVRCCLEHAASVAKTFLTSDCVVVEIKEP---EPVPAGNP 592
|
|
| chaperonin_type_I_II |
cd00309 |
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ... |
3-519 |
8.53e-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: 432.24 E-value: 8.53e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 3 KQLKFSEDARQAMLRGVDQLANAVKVTIGPKGRNVVLDKEFTAPLITNDGVTIAKEIELEdpyeNMGAKLVQEVANKTNE 82
Cdd:cd00309 1 KEREFGEEARLSNINAAKALADAVKTTLGPKGMDKMLVDSLGDPTITNDGATILKEIEVE----HPAAKLLVEVAKSQDD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 83 IAGDGTTTATVLAQAMIQEGLKNVTSGANPVGLRQGIDKAVKVAVEALHENSQK--VENKNEIAQVGAISAA-------D 153
Cdd:cd00309 77 EVGDGTTTVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVPidVEDREELLKVATTSLNsklvsggD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 154 EEIGRYISEAMEKVG------NDGVITIEESNGLN-TELEVVEGMQFDRGYQSPYMVTdsdkmvaELERPYILVTDKKIS 226
Cdd:cd00309 157 DFLGELVVDAVLKVGkengdvDLGVIRVEKKKGGSlEDSELVVGMVFDKGYLSPYMPK-------RLENAKILLLDCKLE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 227 sfqdilplleqvvqsnrPILIVADEVEGDALTNIVLNRMrgtftaVAVKApgfgdRRKAMLEDLAILTGAQVITddlglD 306
Cdd:cd00309 230 -----------------YVVIAEKGIDDEALHYLAKLGI------MAVRR-----VRKEDLERIAKATGATIVS-----R 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 307 LKDASIDMLGTASKVEVTK----DNTTVVDGDGdensidarvsqlksqieetesdfdreklqerlaklaGGVAVIKVGAA 382
Cdd:cd00309 277 LEDLTPEDLGTAGLVEETKigdeKYTFIEGCKG------------------------------------GKVATILLRGA 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 383 SETELKERKLRIEDALNSTRAAVEE-GIVAGGGTALVNVYQKVSEI--EAEGDIETGVNIVLKALTAPVRQIAENAGLEG 459
Cdd:cd00309 321 TEVELDEAERSLHDALCAVRAAVEDgGIVPGGGAAEIELSKALEELakTLPGKEQLGIEAFADALEVIPRTLAENAGLDP 400
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446162787 460 SVIVERLKNAEPGVGFNAA----TNEWVNMLEAGIVDPTKVTRSALQHAASVAAMFLTTEAVVA 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 |
1.88e-85 |
|
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: 272.92 E-value: 1.88e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 22 LANAVKVTIGPKGRNVVLDKEFTAPLITNDGVTIAKEIELEDPYenmgAKLVQEVANKTNEIAGDGTTTATVLAQAMIQE 101
Cdd:pfam00118 1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELEIQHPA----AKLLVEAAKAQDEEVGDGTTTVVVLAGELLEE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 102 GLKNVTSGANPVGLRQGIDKAVKVAVEALHENSQ---KVENKNEIAQVGAISAA-------DEEIGRYISEAME------ 165
Cdd:pfam00118 77 AEKLLAAGVHPTTIIEGYEKALEKALEILDSIISipvEDVDREDLLKVARTSLSskiisreSDFLAKLVVDAVLaipknd 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 166 ---KVGNDGVITIEESNGLNTELevVEGMQFDRGYQSPymvtdsdKMVAELERPYILVTDKKISSFQD------------ 230
Cdd:pfam00118 157 gsfDLGNIGVVKILGGSLEDSEL--VDGVVLDKGPLHP-------DMPKRLENAKVLLLNCSLEYEKTetkatvvlsdae 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 231 ------------ILPLLEQVVQSNRPILIVADEVEGDALTNIVLNRMRGTFTAvavkapgfgdrRKAMLEDLAILTGAQV 298
Cdd:pfam00118 228 qlerflkaeeeqILEIVEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMALRRV-----------KKRDLERLAKATGARA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 299 ITddlglDLKDASIDMLGTASKVEVTK---DNTTVVDGDGDensidarvsqlksqieetesdfdreklqerlaklaGGVA 375
Cdd:pfam00118 297 VS-----SLDDLTPDDLGTAGKVEEEKigdEKYTFIEGCKS-----------------------------------PKAA 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 376 VIKVGAASETELKERKLRIEDALNSTRAAVEE-GIVAGGGTALVNVYQKVSEI--EAEGDIETGVNIVLKALTAPVRQIA 452
Cdd:pfam00118 337 TILLRGATDHVLDEIERSIHDALCVVKNAIEDpRVVPGGGAVEMELARALREYakSVSGKEQLAIEAFAEALEVIPKTLA 416
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446162787 453 ENAGLEGSVIVERLKNA----EPGVGFNAATNEWVNMLEAGIVDPTKVTRSALQHAASVAAMFLTTEAVVASI 521
Cdd:pfam00118 417 ENAGLDPIEVLAELRAAhasgEKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKSATEAASTILRIDDIIKAK 489
|
|
| chaperonin_like |
cd03333 |
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ... |
140-407 |
5.92e-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: 135.67 E-value: 5.92e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 140 KNEIAQVGAISAA------DEEIGRYISEAMEKVG------NDGVITIEESNGLN-TELEVVEGMQFDRGYQSPYMVTds 206
Cdd:cd03333 1 RELLLQVATTSLNsklsswDDFLGKLVVDAVLKVGpdnrmdDLGVIKVEKIPGGSlEDSELVVGVVFDKGYASPYMPK-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 207 dkmvaELERPYILVTDKKISsfqdilplleqvvqsnrPILIVADEVEGDALTNIVLNRMrgtftaVAVKApgfgdRRKAM 286
Cdd:cd03333 79 -----RLENAKILLLDCPLE-----------------YVVIAEKGIDDLALHYLAKAGI------MAVRR-----VKKED 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 287 LEDLAILTGAQVITddlglDLKDASIDMLGTASKVEVTKD----NTTVVDGDGdensidarvsqlksqieetesdfdrek 362
Cdd:cd03333 126 LERIARATGATIVS-----SLEDLTPEDLGTAELVEETKIgeekLTFIEGCKG--------------------------- 173
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 446162787 363 lqerlaklaGGVAVIKVGAASETELKERKLRIEDALNSTRAAVEE 407
Cdd:cd03333 174 ---------GKAATILLRGATEVELDEVKRSLHDALCAVRAAVEE 209
|
|
| cpn60 |
cd03343 |
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ... |
9-520 |
6.12e-30 |
|
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: 123.14 E-value: 6.12e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 9 EDARQAMLRGVDQLANAVKVTIGPKGRNVVLDKEFTAPLITNDGVTIAKEIELEDPyenmGAKLVQEVANKTNEIAGDGT 88
Cdd:cd03343 14 RDAQRMNIAAAKAVAEAVRTTLGPKGMDKMLVDSLGDVTITNDGATILKEMDIEHP----AAKMLVEVAKTQDEEVGDGT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 89 TTATVLAQAMIQEGLKNVTSGANPVGLRQGIDKAVKVAVEALHENSQKVENKNE-----IAQVGAISAADEEIGRYISE- 162
Cdd:cd03343 90 TTAVVLAGELLEKAEDLLDQNIHPTVIIEGYRLAAEKALELLDEIAIKVDPDDKdtlrkIAKTSLTGKGAEAAKDKLADl 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 163 ------AMEKVGNDGV------ITIEESNG---LNTELevVEGMQFDRGYQSPYM---VTDSDKMVA----ELERPYIlV 220
Cdd:cd03343 170 vvdavlQVAEKRDGKYvvdldnIKIEKKTGgsvDDTEL--IRGIVIDKEVVHPGMpkrVENAKIALLdaplEVKKTEI-D 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 221 TDKKISSFQDILPLLEQvvQSNrpilIVADEVEGDALT--NIVL-----NRMRGTFTAvavKAPGFGDRR--KAMLEDLA 291
Cdd:cd03343 247 AKIRITSPDQLQAFLEQ--EEA----MLKEMVDKIADTgaNVVFcqkgiDDLAQHYLA---KAGILAVRRvkKSDMEKLA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 292 ILTGAQVITddlglDLKDASIDMLGTASKVEVTKdnttvvdgDGDENSIdarvsqlksQIEEtesdfdreklqerlAKLA 371
Cdd:cd03343 318 RATGAKIVT-----NIDDLTPEDLGEAELVEERK--------VGDDKMV---------FVEG--------------CKNP 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 372 GGVAVIKVGaASETELKERKLRIEDALNSTRAAVEEG-IVAGGGTALVNVYQKVSEIEA--EGDIETGVNIVLKALTAPV 448
Cdd:cd03343 362 KAVTILLRG-GTEHVVDELERALEDALRVVADALEDGkVVAGGGAVEIELAKRLREYARsvGGREQLAVEAFADALEEIP 440
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446162787 449 RQIAENAGLEG-SVIVE-RLKNAEPG--VGFNAATNEWVNMLEAGIVDPTKVTRSALQHAASVAAMFLTTEAVVAS 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 |
1.72e-16 |
|
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: 82.33 E-value: 1.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 22 LANAVKVTIGPKGrnvvLDKEFTAP----LITNDGVTIAKEIELEDPyenmGAKLVQEVANKTNEIAGDGTTTATVLAQA 97
Cdd:cd03338 20 VADAIRTSLGPRG----MDKMIQTGkgevIITNDGATILKQMSVLHP----AAKMLVELSKAQDIEAGDGTTSVVVLAGA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 98 MIQEGLKNVTSGANPVGLRQGIDKAVKVAVEALHENSQKVENKNEIAQV-GAISAADEEIGRYISEAMEKVGNDGVITIE 176
Cdd:cd03338 92 LLSACESLLKKGIHPTVISESFQIAAKKAVEILDSMSIPVDLNDRESLIkSATTSLNSKVVSQYSSLLAPIAVDAVLKVI 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 177 ESN-----------------GLNTELEVVEGMQFDRGYQS------------------------PYM-----VTDSDKM- 209
Cdd:cd03338 172 DPAtatnvdlkdirivkklgGTIEDTELVDGLVFTQKASKkaggptriekakigliqfclsppkTDMdnnivVNDYAQMd 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 210 -VAELERPYILVTDKKISSfqdilplleqvvqSNRPILIVADEVEGDALTNI---VLNRMRgtftAVAVKapgfgDRRKA 285
Cdd:cd03338 252 rILREERKYILNMCKKIKK-------------SGCNVLLIQKSILRDAVSDLalhFLAKLK----IMVVK-----DIERE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 286 MLEDLAILTGAQVITDDLGLDLkdasiDMLGTASKVevtkdnttvvdgdgdensidarvsqlksqiEETESDFDREKLQE 365
Cdd:cd03338 310 EIEFICKTIGCKPVASIDHFTE-----DKLGSADLV------------------------------EEVSLGDGKIVKIT 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 366 RLAKLAGGVAVIkVGAASETELKERKLRIEDALNSTRAAVEE-GIVAGGGTALVNVYQKVSEieaEGDIETGVN-IVLKA 443
Cdd:cd03338 355 GVKNPGKTVTIL-VRGSNKLVLDEAERSLHDALCVIRCLVKKrALIPGGGAPEIEIALQLSE---WARTLTGVEqYCVRA 430
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446162787 444 LTAPVRQI----AENAGLEGSVIV----ERLKNAEPGVGFNAATNEWVNMLEAGIVDPTKVTRSALQHAASVAAMFL 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 |
6.68e-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: 80.21 E-value: 6.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 9 EDARQAMLRGVDQLANAVKVTIGPKGRNVVLDKEFTAPLITNDGVTIAKEIELEDPyenmGAKLVQEVANKTNEIAGDGT 88
Cdd:TIGR02342 8 QDVRTSNIVAAKAVADAIRTSLGPKGMDKMIQDGKGEVIITNDGATILKQMAVLHP----AAKMLVELSKAQDIEAGDGT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 89 TTATVLAQAMIQEGLKNVTSGANPVGLRQGIDKAVKVAVEALHENSQKVENKN-EIAQVGAISAADEEIGRYISEAMEKV 167
Cdd:TIGR02342 84 TSVVILAGALLGACERLLNKGIHPTIISESFQSAADEAIKILDEMSIPVDLSDrEQLLKSATTSLSSKVVSQYSSLLAPL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 168 GNDGVITIEES-NGLNTEL----------------EVVEGMQFDRGYQS------------------------PYM---- 202
Cdd:TIGR02342 164 AVDAVLKVIDPeNAKNVDLndikvvkklggtiddtELIEGLVFTQKASKsaggptriekakigliqfqisppkTDMenqi 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 203 -VTDSDKM--VAELERPYILVTDKKIssfqdilplleqvVQSNRPILIVADEVEGDALTNI---VLNRMRgtftAVAVKa 276
Cdd:TIGR02342 244 iVNDYAQMdrVLKEERAYILNIVKKI-------------KKTGCNVLLIQKSILRDAVNDLalhFLAKMK----IMVVK- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 277 pgfgDRRKAMLEDLAILTGAQVITDDLGLdlkdaSIDMLGTASKVE-VTKDNTTVVdgdgdensidaRVSQLKSqieete 355
Cdd:TIGR02342 306 ----DIEREEIEFICKTIGCKPIASIDHF-----TADKLGSAELVEeVDSDGGKII-----------KITGIQN------ 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 356 sdfdreklqerlaklAGGVAVIKVGAASETELKERKLRIEDALNSTRAAVEE-GIVAGGGTALVNVYQKVSEI--EAEGD 432
Cdd:TIGR02342 360 ---------------AGKTVTVVVRGSNKLVIDEAERSLHDALCVIRCLVKKrGLIAGGGAPEIEIARRLSKYarTMKGV 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 433 IETGVNIVLKALTAPVRQIAENAGLEGSVIVERLKNA----EPGVGFNAATNEWVNMLEAGIVDPTKVTRSALQHAASVA 508
Cdd:TIGR02342 425 ESYCVRAFADALEVIPYTLAENAGLNPIKVVTELRNRhangEKTAGISVRKGGITNMLEEHVLQPLLVTTSAITLASETV 504
|
570
....*....|..
gi 446162787 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 ... |
10-190 |
8.13e-16 |
|
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: 80.23 E-value: 8.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 10 DARQAMLRGVDQLANAVKVTIGPKGrnvvLDKEFTAP----LITNDGVTIAKEIELEDPYenmgAKLVQEVANKTNEIAG 85
Cdd:TIGR02343 27 EAKKSNIAAAKSVASILRTSLGPKG----MDKMLISPdgdiTVTNDGATILSQMDVDNQI----AKLMVELSKSQDDEIG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 86 DGTTTATVLAQAMIQEGLKNVTSGANPVGLRQGIDKAVKVAVEALHENSQKVENKNEIAQVgAISAADEEIGRYI----S 161
Cdd:TIGR02343 99 DGTTGVVVLAGALLEQAEELLDKGIHPIKIADGFEEAARIAVEHLEEISDEISADNNNREP-LIQAAKTSLGSKIvskcH 177
|
170 180 190
....*....|....*....|....*....|.
gi 446162787 162 EAMEKVGNDGVITIE--ESNGLNTELEVVEG 190
Cdd:TIGR02343 178 RRFAEIAVDAVLNVAdmERRDVDFDLIKVEG 208
|
|
| TCP1_epsilon |
cd03339 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ... |
9-190 |
1.78e-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: 75.80 E-value: 1.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 9 EDARQAMLRGVD----------QLANAVKVTIGPKGrnvvLDKEFTAP----LITNDGVTIAKEIELEDPYenmgAKLVQ 74
Cdd:cd03339 12 EQEKKKRLKGLEahkshilaakSVANILRTSLGPRG----MDKILVSPdgevTVTNDGATILEKMDVDHQI----AKLLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 75 EVANKTNEIAGDGTTTATVLAQAMIQEGLKNVTSGANPVGLRQGIDKAVKVAVEALHENSQKVE----NKNEIAQVGAIS 150
Cdd:cd03339 84 ELSKSQDDEIGDGTTGVVVLAGALLEQAEKLLDRGIHPIRIADGYEQACKIAVEHLEEIADKIEfspdNKEPLIQTAMTS 163
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446162787 151 AADEEIGRYiSEAMEKVGNDGVITIE--ESNGLNTELEVVEG 190
Cdd:cd03339 164 LGSKIVSRC-HRQFAEIAVDAVLSVAdlERKDVNFELIKVEG 204
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
9-135 |
3.70e-13 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 71.98 E-value: 3.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 9 EDARQAMLRGVDQLANAVKVTIGPKGRNVVLDK-----EFTAPLITNDGVTIAKEIELEDPyenmGAKLVQEVANKTNEI 83
Cdd:PTZ00212 21 ETARLQSFVGAIAVADLVKTTLGPKGMDKILQPmsegpRSGNVTVTNDGATILKSVWLDNP----AAKILVDISKTQDEE 96
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 446162787 84 AGDGTTTATVLAQAMIQEGLKNVTSGANPVGLRQGIDKAVKVAVEALHENSQ 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 |
1.10e-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: 70.44 E-value: 1.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 9 EDARQAMLRGVDQLANAVKVTIGPKGRNVVL--DKEFTAPLITNDGVTIAKEIELEDPyenmGAKLVQEVANKTNEIAGD 86
Cdd:cd03336 12 ETARLSSFVGAIAIGDLVKTTLGPKGMDKILqsVGRSGGVTVTNDGATILKSIGVDNP----AAKVLVDISKVQDDEVGD 87
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 446162787 87 GTTTATVLAQAMIQEGLKNVTSGANPVGLRQGIDKAVKVAVEALHENSQ 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 ... |
4-518 |
1.69e-11 |
|
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT eta chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.
Pssm-ID: 274086 [Multi-domain] Cd Length: 523 Bit Score: 66.71 E-value: 1.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 4 QLKFSEDARQAML------RGVDQLANAVKVTIGPKGRNVVLDKEFTAPLITNDGVTIAKEIELEDPyenmGAKLVQEVA 77
Cdd:TIGR02345 6 LLKEGTDTSQGKGqlisniNACVAIAEALKTTLGPRGMDKLIVGSNGKATISNDGATILKLLDIVHP----AAKTLVDIA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 78 NKTNEIAGDGTTTATVLAQAMIQEGLKNVTSGANPVGLRQGIDKAVKVAVEALHENSQKV-ENKNEIAQV---------- 146
Cdd:TIGR02345 82 KSQDAEVGDGTTSVTILAGELLKEAKPFIEEGVHPQLIIRCYREALSLAVEKIKEIAVTIdEEKGEQRELlekcaatals 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 147 -GAISAADEEIGRYISEAMEKVGND-------GVITIEesNGLNTELEVVEGMQFDR-----GY-QSPYMVTDSD----- 207
Cdd:TIGR02345 162 sKLISHNKEFFSKMIVDAVLSLDRDdldlkliGIKKVQ--GGALEDSQLVNGVAFKKtfsyaGFeQQPKKFANPKillln 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 208 ---KMVAELERPYILVTDKKisSFQDILplleqvvqsnrpilivadevegDALTNIVLNRMRGTFTA----VAVKAPgFG 280
Cdd:TIGR02345 240 velELKAEKDNAEIRVEDVE--DYQAIV----------------------DAEWAIIFRKLEKIVESganvVLSKLP-IG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 281 DRRKAMLEDLAILTGAQVITDDLGldlkdasidmlgtaskvevtkdntTVVDGDGdeNSIDARVSQLKSQIEETESDFDR 360
Cdd:TIGR02345 295 DLATQYFADRDIFCAGRVSAEDLK------------------------RVIKACG--GSIQSTTSDLEADVLGTCALFEE 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 361 EKL-QERLAKLAGG----VAVIKVGAASETELKERKLRIEDALNSTRAAVE-EGIVAGGGTALVNVYQKVSEI--EAEGD 432
Cdd:TIGR02345 349 RQIgSERYNYFTGCphakTCTIILRGGAEQFIEEAERSLHDAIMIVRRALKnKKIVAGGGAIEMELSKCLRDYskTIDGK 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 433 IETGVNIVLKALTAPVRQIAENAGLEGSVIVERLKNAEP------GVGFNAAtnEWVNMLEAGIVDPTKVTRSALQHAAS 506
Cdd:TIGR02345 429 QQLIINAFAKALEIIPRQLCENAGFDSIEILNKLRSRHAkggkwyGVDINTE--DIGDNFEAFVWEPALVKINALKAAFE 506
|
570
....*....|..
gi 446162787 507 VAAMFLTTEAVV 518
Cdd:TIGR02345 507 AACTILSVDETI 518
|
|
| chap_CCT_alpha |
TIGR02340 |
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ... |
9-152 |
1.97e-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: 1.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 9 EDARQAMLRGVDQLANAVKVTIGPKGrnvvLDK-------EFTaplITNDGVTIAKEIELEDPyenmGAKLVQEVANKTN 81
Cdd:TIGR02340 11 QDVRTQNVTAAMAIANIVKTSLGPVG----LDKmlvddigDVT---ITNDGATILKLLEVEHP----AAKILVELAQLQD 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446162787 82 EIAGDGTTTATVLAQAMIQEGLKNVTSGANPVGLRQGIDKAVKVAVEALHENSQKveNKNEIAQVGAISAA 152
Cdd:TIGR02340 80 REVGDGTTSVVIIAAELLKRADELVKNKIHPTSVISGYRLACKEAVKYIKENLSV--SVDELGREALINVA 148
|
|
| TCP1_alpha |
cd03335 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ... |
9-139 |
5.79e-10 |
|
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: 61.53 E-value: 5.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 9 EDARQAMLRGVDQLANAVKVTIGPKGrnvvLDK-------EFTaplITNDGVTIAKEIELEDPyenmGAKLVQEVANKTN 81
Cdd:cd03335 7 QDVRTQNVTAAMAIANIVKSSLGPVG----LDKmlvddigDVT---ITNDGATILKLLEVEHP----AAKILVELAQLQD 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 446162787 82 EIAGDGTTTATVLAQAMIQEGLKNVTSGANPVGLRQGIDKAVKVAVEALHEN-SQKVEN 139
Cdd:cd03335 76 KEVGDGTTSVVIIAAELLKRANELVKQKIHPTTIISGYRLACKEAVKYIKEHlSISVDN 134
|
|
| TCP1_eta |
cd03340 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ... |
4-142 |
9.67e-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: 61.15 E-value: 9.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 4 QLKFSEDARQamlrGVDQL----------ANAVKVTIGPKGRNVVLDKEFTAPLITNDGVTIAKEIELEDPyenmGAKLV 73
Cdd:cd03340 4 LLKEGTDTSQ----GKGQLisninacqaiADAVRTTLGPRGMDKLIVDGRGKVTISNDGATILKLLDIVHP----AAKTL 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446162787 74 QEVANKTNEIAGDGTTTATVLAQAMIQEGLKNVTSGANPVGLRQGIDKAVKVAVEALHENSQKVENKNE 142
Cdd:cd03340 76 VDIAKSQDAEVGDGTTSVVVLAGEFLKEAKPFIEDGVHPQIIIRGYRKALQLAIEKIKEIAVNIDKEDK 144
|
|
| chap_CCT_beta |
TIGR02341 |
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ... |
8-134 |
1.43e-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: 1.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 8 SEDARQAMLRGVDQLANAVKVTIGPKGRNVVL--DKEFTAPLITNDGVTIAKEIELEDPyenmGAKLVQEVANKTNEIAG 85
Cdd:TIGR02341 12 AENARLSSFVGAIAIGDLVKSTLGPKGMDKILqsSSSDASIMVTNDGATILKSIGVDNP----AAKVLVDMSKVQDDEVG 87
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 446162787 86 DGTTTATVLAQAMIQEGLKNVTSGANPVGLRQGIDKAVKVAVEALHENS 134
Cdd:TIGR02341 88 DGTTSVTVLAAELLREAEKLINQKIHPQTIIAGYREATKAARDALLKSA 136
|
|
| TCP1_theta |
cd03341 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ... |
6-146 |
1.59e-09 |
|
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: 60.31 E-value: 1.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 6 KFSEDARQAMLRGVD---QLANAVKVTIGPKGRN--VV--LDKEFtaplITNDGVTIAKEIELEDPyenmGAKLVQEVAN 78
Cdd:cd03341 1 RHYSGLEEAVLRNIEackELSQITRTSYGPNGMNkmVInhLEKLF----VTSDAATILRELEVQHP----AAKLLVMASQ 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446162787 79 KTNEIAGDGTTTATVLAQAMIQEGLKNVTSGANPVGLRQGIDKAVKVAVEALHENS-QKVENKNEIAQV 146
Cdd:cd03341 73 MQEEEIGDGTNLVVVLAGELLEKAEELLRMGLHPSEIIEGYEKALKKALEILEELVvYKIEDLRNKEEV 141
|
|
| chap_CCT_theta |
TIGR02346 |
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ... |
21-195 |
5.78e-09 |
|
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: 58.57 E-value: 5.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 21 QLANAVKVTIGPKGRNVV----LDKEFtaplITNDGVTIAKEIELEDPyenmGAKLVQEVANKTNEIAGDGTTTATVLAQ 96
Cdd:TIGR02346 29 ELSQITRTSLGPNGMNKMvinhLEKLF----VTNDAATILRELEVQHP----AAKLLVMASEMQENEIGDGTNLVLVLAG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 97 AMIQEGLKNVTSGANPVGLRQGIDKAVKVAVEALHE----NSQKVENKNEIAQVGAISAADEEIGRY------ISEAM-- 164
Cdd:TIGR02346 101 ELLNKAEELIRMGLHPSEIIKGYEMALKKAMEILEElvvwEVKDLRDKDELIKALKASISSKQYGNEdflaqlVAQACst 180
|
170 180 190
....*....|....*....|....*....|....*..
gi 446162787 165 ---EKVGNDGVITIEESNGLNTEL---EVVEGMQFDR 195
Cdd:TIGR02346 181 vlpKNPQNFNVDNIRVCKILGGSLsnsEVLKGMVFNR 217
|
|
| chap_CCT_gamma |
TIGR02344 |
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ... |
9-524 |
1.01e-07 |
|
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: 54.74 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 9 EDARQAMLRGVDQ---LANAVKVTIGPKGRNVVLDKEFTAPLITNDGVTIAKEIELEDPyenmGAKLVQEVANKTNEIAG 85
Cdd:TIGR02344 12 ESGRKAQLSNIQAakaVADIIRTCLGPRSMLKMLLDPMGGIVMTNDGNAILREIDVAHP----AAKSMIELSRTQDEEVG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 86 DGTTTATVLAQAMIQEGLKNVTSGANPVGLRQGIDKAVKVAVEALHENSQKVENKNEIAQVGAISA--ADEEIGRYiSEA 163
Cdd:TIGR02344 88 DGTTSVIILAGEMLSVAEPFLEQNIHPTVIIRAYRKALDDALSVLEEISIPVDVNDDAAMLKLIQSciGTKFVSRW-SDL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 164 MEKVGNDGVITIEESNGLNTELE-------------------VVEGMQFDRGYQSPymvtdsdKMVAELERPYILVTD-- 222
Cdd:TIGR02344 167 MCDLALDAVRTVQRDENGRKEIDikryakvekipggdiedscVLKGVMINKDVTHP-------KMRRYIENPRIVLLDcp 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 223 ---KKISSFQDILPLLEQvvQSNRPILIVADEVEgdaltnivlnrmrgtftavavkapgfgdrrkAMLEDLAILTGAQVI 299
Cdd:TIGR02344 240 leyKKGESQTNIEITKEE--DWNRILQMEEEYVQ-------------------------------LMCEDIIAVKPDLVI 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 300 TDDlglDLKDASIDMLGTASKVEVTKDNTTvvdgdgDENSIdARVS--QLKSQIEE-TESD-------FDREKL-QERLA 368
Cdd:TIGR02344 287 TEK---GVSDLAQHYLLKANITAIRRVRKT------DNNRI-ARACgaTIVNRPEElRESDvgtgcglFEVKKIgDEYFT 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 369 KLAG----GVAVIKVGAASETELKERKLRIEDALNSTRAAVEEG-IVAGGGTALVNVYQKVSEIEA--EGDIETGVNIVL 441
Cdd:TIGR02344 357 FITEckdpKACTILLRGASKDILNEVERNLQDAMAVARNVLLDPkLVPGGGATEMAVSVALTEKSKklEGVEQWPYRAVA 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 442 KALTAPVRQIAENAGleGSVIVE----RLKNAEPG---VGFNAATNEWVNMLEAGIVDPTKVTRSALQHAASVAAMFLTT 514
Cdd:TIGR02344 437 DALEIIPRTLAQNCG--ANVIRTltelRAKHAQENnctWGIDGETGKIVDMKEKGIWEPLAVKLQTYKTAIESACLLLRI 514
|
570
....*....|
gi 446162787 515 EAVVASIPEK 524
Cdd:TIGR02344 515 DDIVSGVKKK 524
|
|
| TCP1_gamma |
cd03337 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ... |
22-187 |
2.75e-07 |
|
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: 53.07 E-value: 2.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 22 LANAVKVTIGPKGR-NVVLDKeFTAPLITNDGVTIAKEIELEDPyenmGAKLVQEVANKTNEIAGDGTTTATVLAQAMIQ 100
Cdd:cd03337 28 VADVIRTCLGPRAMlKMLLDP-MGGIVLTNDGNAILREIDVAHP----AAKSMIELSRTQDEEVGDGTTSVIILAGEILA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 101 EGLKNVTSGANPVGLRQGIDKAVKVAVEALHENSQKV--ENKNEIAQVGAISAADEEIGRYiSEAMEKVGNDGVITIE-E 177
Cdd:cd03337 103 VAEPFLERGIHPTVIIKAYRKALEDALKILEEISIPVdvNDRAQMLKIIKSCIGTKFVSRW-SDLMCNLALDAVKTVAvE 181
|
170
....*....|
gi 446162787 178 SNGLNTELEV 187
Cdd:cd03337 182 ENGRKKEIDI 191
|
|
| chap_CCT_zeta |
TIGR02347 |
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ... |
22-518 |
9.64e-07 |
|
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT zeta chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.
Pssm-ID: 274088 [Multi-domain] Cd Length: 531 Bit Score: 51.27 E-value: 9.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 22 LANAVKVTIGPKGRNVVLDKEFTAPLITNDGVTIAKEIELEDPYENMGAKlvqeVANKTNEIAGDGTTTATVLAQAMIQE 101
Cdd:TIGR02347 28 LQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEMQIQHPTASMIAR----AATAQDDITGDGTTSTVLLIGELLKQ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 102 GLKNVTSGANPVGLRQGIDKAVKVAVEALHENSQKVENKNE----------------------------IAQVGAISAAD 153
Cdd:TIGR02347 104 AERYILEGVHPRIITEGFEIARKEALQFLDKFKVKKEDEVDrefllnvartslrtklpadladqlteivVDAVLAIKKDG 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 154 EEIGRYISEAMEkvgndgvitIEESNGLNTELevVEGMQFDRGYQSPYMVTDsdkmvaeLERPYILV---------TDKK 224
Cdd:TIGR02347 184 EDIDLFMVEIME---------MKHKSATDTTL--IRGLVLDHGARHPDMPRR-------VKNAYILTcnvsleyekTEVN 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 225 ISSFQDILPLLEQVVQSNR--------PILIVADEVEGDAL-TNIVLNRMRGT--FTAVAVKAPGFGDRRKAM---LEDL 290
Cdd:TIGR02347 246 SGFFYSSAEQREKLVKAERkfvddrvkKIIELKKKVCGKSPdKGFVVINQKGIdpPSLDLLAKEGIMALRRAKrrnMERL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 291 AILTGAQVITddlglDLKDASIDMLGTASKVEvtkdNTTVvdgdGDENSidarvsqlkSQIEETEsdfdreklqerlakl 370
Cdd:TIGR02347 326 TLACGGEALN-----SVEDLTPECLGWAGLVY----ETTI----GEEKY---------TFIEECK--------------- 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 371 AGGVAVIKVGAASETELKERKLRIEDALNSTRAAVEEG-IVAGGGTALVNVYQKVSEIE--AEGDIETGVNIVLKALTAP 447
Cdd:TIGR02347 369 NPKSCTILIKGPNDHTIAQIKDAVRDGLRAVKNAIEDKcVVPGAGAFEIAAYRHLKEYKksVKGKAKLGVEAFANALLVI 448
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446162787 448 VRQIAENAGLEG-----SVIVERLKNAEPgVGFNAATNEWVNMLEAGIVDPTKVTRSALQHAASVAAMFLTTEAVV 518
Cdd:TIGR02347 449 PKTLAENSGFDAqdtlvKLEDEHDEGGEV-VGVDLNTGEPIDPEIKGIWDNYRVKKQLIQSATVIASQLLLVDEVM 523
|
|
| TCP1_zeta |
cd03342 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
22-221 |
1.85e-04 |
|
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: 44.17 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 22 LANAVKVTIGPKGRNVVLDKEFTAPLITNDGVTIAKEIELEDPYENMGAKlvqeVANKTNEIAGDGTTTATVLAQAMIQE 101
Cdd:cd03342 24 LQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLSEMQIQHPTASMIAR----AATAQDDITGDGTTSNVLLIGELLKQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446162787 102 GLKNVTSGANPVGLRQGIDKAVKVAVEALHENSQKVENKN--EIAQVGAISAADEEIGRYISEAMEKVGNDGVITIEESN 179
Cdd:cd03342 100 AERYIQEGVHPRIITEGFELAKNKALKFLESFKVPVEIDTdrELLLSVARTSLRTKLHADLADQLTEIVVDAVLAIYKPD 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446162787 180 ---------------GLNTELEVVEGMQFDRGYQSPYMVTDsdkmvaeLERPYILVT 221
Cdd:cd03342 180 epidlhmveimqmqhKSDSDTKLIRGLVLDHGARHPDMPKR-------VENAYILTC 229
|
|
| |
