|
Name |
Accession |
Description |
Interval |
E-value |
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
1-538 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 976.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 1 MAKELKFSEDARSKMKAGVDKLANTVKTTIGPKGRNVVLEQSYGAPTITNDGVTIAKAIELEDHFENMGAKLVAEVASKT 80
Cdd:PRK00013 1 MAKDIKFGEDARRKLLRGVNKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDPFENMGAQLVKEVASKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 81 NDIAGDGTTTATVLTQAIVAEGLKNVTAGANPVGIRTGIEKATAAAVKKLHEMSHTVSTKAEIAQIASISASN-EEVGEL 159
Cdd:PRK00013 81 NDVAGDGTTTATVLAQAIVREGLKNVAAGANPMDLKRGIDKAVEAAVEELKKISKPVEDKEEIAQVATISANGdEEIGKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 160 IAEAMDKVGNDGVITIEESKGIETTLDVVEGMQFDRGYMSQYMVTDNDKMEANLDNPYILITDKKISNIQDVLPVLQSVV 239
Cdd:PRK00013 161 IAEAMEKVGKEGVITVEESKGFETELEVVEGMQFDRGYLSPYFVTDPEKMEAELENPYILITDKKISNIQDLLPVLEQVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 240 EQGRALLIIADDITGEALPTLVLNKMRGTFNVVAVKAPGFGDRRKAQLEDIAVLTGGTVITEDLGLNLKDVTIDQLGQAS 319
Cdd:PRK00013 241 QSGKPLLIIAEDVEGEALATLVVNKLRGTLKVVAVKAPGFGDRRKAMLEDIAILTGGTVISEELGLKLEDATLEDLGQAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 320 KVNVSKDNTTIVEGSGDKNAVATRVDIIKQQIAETTSDFDREKLQERLAKLAGGVAVINVGAATETELKERKYRIEDALN 399
Cdd:PRK00013 321 KVVVTKDNTTIVDGAGDKEAIKARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATEVEMKEKKDRVEDALH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 400 ATRAAVEEGFVSGGGTALVNAISAVTALSEV-GDVQTGINTVIKALEAPVRQIVENAGFEGSVIVNKLKEQ-VEGFGYNA 477
Cdd:PRK00013 401 ATRAAVEEGIVPGGGVALLRAAPALEALKGLnGDEATGINIVLRALEAPLRQIAENAGLEGSVVVEKVKNGkGKGYGYNA 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2538675531 478 ATNEWVDMIAAGIVDPTKVTRSALQNAASVSALLLTTEAVVAELPS-DDAASAMPQGGMPGM 538
Cdd:PRK00013 481 ATGEYVDMIEAGIIDPTKVTRSALQNAASVAGLLLTTEAVVADKPEkKAAAPPMGGGGMGGM 542
|
|
| GroEL |
cd03344 |
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ... |
3-520 |
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: 860.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 3 KELKFSEDARSKMKAGVDKLANTVKTTIGPKGRNVVLEQSYGAPTITNDGVTIAKAIELEDHFENMGAKLVAEVASKTND 82
Cdd:cd03344 1 KDIKFGEEARKALLRGVNKLADAVKVTLGPKGRNVVIEKSFGSPKITKDGVTVAKEIELEDPFENMGAQLVKEVASKTND 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 83 IAGDGTTTATVLTQAIVAEGLKNVTAGANPVGIRTGIEKATAAAVKKLHEMSHTVSTKAEIAQIASISASN-EEVGELIA 161
Cdd:cd03344 81 VAGDGTTTATVLARAIIKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKPVKTKEEIAQVATISANGdEEIGELIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 162 EAMDKVGNDGVITIEESKGIETTLDVVEGMQFDRGYMSQYMVTDNDKMEANLDNPYILITDKKISNIQDVLPVLQSVVEQ 241
Cdd:cd03344 161 EAMEKVGKDGVITVEEGKTLETELEVVEGMQFDRGYLSPYFVTDPEKMEVELENPYILLTDKKISSIQELLPILELVAKA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 242 GRALLIIADDITGEALPTLVLNKMRGTFNVVAVKAPGFGDRRKAQLEDIAVLTGGTVITEDLGLNLKDVTIDQLGQASKV 321
Cdd:cd03344 241 GRPLLIIAEDVEGEALATLVVNKLRGGLKVCAVKAPGFGDRRKAMLEDIAILTGGTVISEELGLKLEDVTLEDLGRAKKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 322 NVSKDNTTIVEGSGDKNAVATRVDIIKQQIAETTSDFDREKLQERLAKLAGGVAVINVGAATETELKERKYRIEDALNAT 401
Cdd:cd03344 321 VVTKDDTTIIGGAGDKAAIKARIAQIRKQIEETTSDYDKEKLQERLAKLSGGVAVIKVGGATEVELKEKKDRVEDALNAT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 402 RAAVEEGFVSGGGTALVNAISAVTAL-SEVGDVQTGINTVIKALEAPVRQIVENAGFEGSVIVNKLKEQVEGFGYNAATN 480
Cdd:cd03344 401 RAAVEEGIVPGGGVALLRASPALDKLkALNGDEKLGIEIVRRALEAPLRQIAENAGVDGSVVVEKVLESPDGFGYDAATG 480
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 2538675531 481 EWVDMIAAGIVDPTKVTRSALQNAASVSALLLTTEAVVAE 520
Cdd:cd03344 481 EYVDMIEAGIIDPTKVVRSALQNAASVASLLLTTEALVVD 520
|
|
| groEL |
PRK12849 |
chaperonin GroEL; Reviewed |
1-539 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237230 Cd Length: 542 Bit Score: 854.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 1 MAKELKFSEDARSKMKAGVDKLANTVKTTIGPKGRNVVLEQSYGAPTITNDGVTIAKAIELEDHFENMGAKLVAEVASKT 80
Cdd:PRK12849 1 MAKIIKFDEEARRALERGVNKLADAVKVTLGPKGRNVVIDKSFGAPTITKDGVSIAKEIELEDPFENLGAQLVKEVASKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 81 NDIAGDGTTTATVLTQAIVAEGLKNVTAGANPVGIRTGIEKATAAAVKKLHEMSHTVSTKAEIAQIASISASN-EEVGEL 159
Cdd:PRK12849 81 NDVAGDGTTTATVLAQALVQEGLKNVAAGANPMDLKRGIDKAVEAVVEELKALARPVSGSEEIAQVATISANGdEEIGEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 160 IAEAMDKVGNDGVITIEESKGIETTLDVVEGMQFDRGYMSQYMVTDNDKMEANLDNPYILITDKKISNIQDVLPVLQSVV 239
Cdd:PRK12849 161 IAEAMEKVGKDGVITVEESKTLETELEVTEGMQFDRGYLSPYFVTDPERMEAVLEDPLILLTDKKISSLQDLLPLLEKVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 240 EQGRALLIIADDITGEALPTLVLNKMRGTFNVVAVKAPGFGDRRKAQLEDIAVLTGGTVITEDLGLNLKDVTIDQLGQAS 319
Cdd:PRK12849 241 QSGKPLLIIAEDVEGEALATLVVNKLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGLKLEEVTLDDLGRAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 320 KVNVSKDNTTIVEGSGDKNAVATRVDIIKQQIAETTSDFDREKLQERLAKLAGGVAVINVGAATETELKERKYRIEDALN 399
Cdd:PRK12849 321 RVTITKDNTTIVDGAGDKEAIEARVAQIRRQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATEVELKERKDRVEDALN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 400 ATRAAVEEGFVSGGGTALVNAISAVTALSEV-GDVQTGINTVIKALEAPVRQIVENAGFEGSVIVNKLKEQVEGFGYNAA 478
Cdd:PRK12849 401 ATRAAVEEGIVPGGGVALLRAAKALDELAGLnGDQAAGVEIVRRALEAPLRQIAENAGLDGSVVVAKVLELEDGFGFNAA 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2538675531 479 TNEWVDMIAAGIVDPTKVTRSALQNAASVSALLLTTEAVVAELPSDDAASA-MPQGGMPGMM 539
Cdd:PRK12849 481 TGEYGDLIAAGIIDPVKVTRSALQNAASVAGLLLTTEALVADKPEEEDPPGgMGGMGGMGHM 542
|
|
| GroEL |
TIGR02348 |
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ... |
2-522 |
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: 840.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 2 AKELKFSEDARSKMKAGVDKLANTVKTTIGPKGRNVVLEQSYGAPTITNDGVTIAKAIELEDHFENMGAKLVAEVASKTN 81
Cdd:TIGR02348 1 AKQIKFDEEARKALLRGVDKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDKFENMGAQLVKEVASKTN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 82 DIAGDGTTTATVLTQAIVAEGLKNVTAGANPVGIRTGIEKATAAAVKKLHEMSHTVSTKAEIAQIASISASN-EEVGELI 160
Cdd:TIGR02348 81 DVAGDGTTTATVLAQAIVKEGLKNVAAGANPIELKRGIEKAVEAVVEELKKLSKPVKGKKEIAQVATISANNdEEIGSLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 161 AEAMDKVGNDGVITIEESKGIETTLDVVEGMQFDRGYMSQYMVTDNDKMEANLDNPYILITDKKISNIQDVLPVLQSVVE 240
Cdd:TIGR02348 161 AEAMEKVGKDGVITVEESKSLETELEVVEGMQFDRGYISPYFVTDAEKMEVELENPYILITDKKISNIKDLLPLLEKVAQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 241 QGRALLIIADDITGEALPTLVLNKMRGTFNVVAVKAPGFGDRRKAQLEDIAVLTGGTVITEDLGLNLKDVTIDQLGQASK 320
Cdd:TIGR02348 241 SGKPLLIIAEDVEGEALATLVVNKLRGTLNVCAVKAPGFGDRRKAMLEDIAILTGGQVISEELGLKLEEVTLDDLGKAKK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 321 VNVSKDNTTIVEGSGDKNAVATRVDIIKQQIAETTSDFDREKLQERLAKLAGGVAVINVGAATETELKERKYRIEDALNA 400
Cdd:TIGR02348 321 VTVDKDNTTIVEGAGDKAAIKARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATETEMKEKKLRIEDALNA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 401 TRAAVEEGFVSGGGTALVNAISAVTALSEVG-DVQTGINTVIKALEAPVRQIVENAGFEGSVIVNKLKEQVEGFGYNAAT 479
Cdd:TIGR02348 401 TRAAVEEGIVPGGGVALLRAAAALEGLKGDGeDEAIGIDIVKRALEAPLRQIAENAGLDGAVVAEKVKELKGNFGFNAAT 480
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 2538675531 480 NEWVDMIAAGIVDPTKVTRSALQNAASVSALLLTTEAVVAELP 522
Cdd:TIGR02348 481 GEYEDLVEAGIIDPTKVTRSALQNAASIAGLLLTTEAVVADKP 523
|
|
| groEL |
PRK12850 |
chaperonin GroEL; Reviewed |
1-539 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237231 Cd Length: 544 Bit Score: 795.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 1 MAKELKFSEDARSKMKAGVDKLANTVKTTIGPKGRNVVLEQSYGAPTITNDGVTIAKAIELEDHFENMGAKLVAEVASKT 80
Cdd:PRK12850 2 AAKEIRFSTDARDRLLRGVNILANAVKVTLGPKGRNVVLEKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVKEVASKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 81 NDIAGDGTTTATVLTQAIVAEGLKNVTAGANPVGIRTGIEKATAAAVKKLHEMSHTVSTKAEIAQIASISASNEE-VGEL 159
Cdd:PRK12850 82 NDLAGDGTTTATVLAQAIVREGAKLVAAGMNPMDLKRGIDLAVAAVVDELKKIAKKVTSSKEIAQVATISANGDEsIGEM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 160 IAEAMDKVGNDGVITIEESKGIETTLDVVEGMQFDRGYMSQYMVTDNDKMEANLDNPYILITDKKISNIQDVLPVLQSVV 239
Cdd:PRK12850 162 IAEAMDKVGKEGVITVEEAKTLGTELDVVEGMQFDRGYLSPYFVTNPEKMRAELEDPYILLHEKKISNLQDLLPILEAVV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 240 EQGRALLIIADDITGEALPTLVLNKMRGTFNVVAVKAPGFGDRRKAQLEDIAVLTGGTVITEDLGLNLKDVTIDQLGQAS 319
Cdd:PRK12850 242 QSGRPLLIIAEDVEGEALATLVVNKLRGGLKSVAVKAPGFGDRRKAMLEDIAVLTGGQVISEDLGIKLENVTLDMLGRAK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 320 KVNVSKDNTTIVEGSGDKNAVATRVDIIKQQIAETTSDFDREKLQERLAKLAGGVAVINVGAATETELKERKYRIEDALN 399
Cdd:PRK12850 322 RVLITKENTTIIDGAGDKKNIEARVKQIRAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKEKKDRVDDALH 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 400 ATRAAVEEGFVSGGGTALVNAISAVTALSEV-GDVQTGINTVIKALEAPVRQIVENAGFEGSVIVNKLKEQVEGFGYNAA 478
Cdd:PRK12850 402 ATRAAVEEGIVPGGGVALLRARSALRGLKGAnADETAGIDIVRRALEEPLRQIATNAGFEGSVVVGKVAELPGNFGFNAQ 481
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2538675531 479 TNEWVDMIAAGIVDPTKVTRSALQNAASVSALLLTTEAVVAELPSDDAASAMPQGGMPGMM 539
Cdd:PRK12850 482 TGEYGDMVEAGIIDPAKVTRTALQDAASIAALLITTEAMVAEAPKKAAAAAAGPGPGMGGM 542
|
|
| GroEL |
COG0459 |
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ... |
1-527 |
0e+00 |
|
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227 Cd Length: 497 Bit Score: 765.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 1 MAKELKFSEDARSKMKAGVDKLANTVKTTIGPKGRNVVLEQSYGAPTITNDGVTIAKAIELEDHFENMGAKLVAEVASKT 80
Cdd:COG0459 1 MAKQILFGEDARRANIRGVKALADAVKVTLGPKGRNVMLVKSFGDPTITNDGVTIAKEIELEDPFENMGAQLVKEVASKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 81 NDIAGDGTTTATVLTQAIVAEGLKNVTAGANPVGIRTGIEKATAAAVKKLHEMSHTVSTKAEIAQIASISASN-EEVGEL 159
Cdd:COG0459 81 NDEAGDGTTTATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPVDDKEELAQVATISANGdEEIGEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 160 IAEAMDKVGNDGVITIEESKGIETTLDVVEGMQFDRGYMSQYMVTDNDKMEANLDNPYILITDKKISNIQDVLPVLQSVV 239
Cdd:COG0459 161 IAEAMEKVGKDGVITVEEGKGLETELEVVEGMQFDKGYLSPYFVTDPEKMPAELENAYILLTDKKISSIQDLLPLLEKVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 240 EQGRALLIIADDITGEALPTLVLNKMRGTFNVVAVKAPGFGDRRKAQLEDIAVLTGGTVITEDLGLNLKDVTIDQLGQAS 319
Cdd:COG0459 241 QSGKPLLIIAEDIDGEALATLVVNGIRGVLRVVAVKAPGFGDRRKAMLEDIAILTGGRVISEDLGLKLEDVTLDDLGRAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 320 KVNVSKDNTTIVEGSGDKNAVatrvdiikqqiaettsdfdreklqerlaklaggvaVINVGAATETELKERKYRIEDALN 399
Cdd:COG0459 321 RVEVDKDNTTIVEGAGNPKAI-----------------------------------VILVGAATEVEVKERKRRVEDALH 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 400 ATRAAVEEGFVSGGGTALVNAISAVTALSEV--GDVQTGINTVIKALEAPVRQIVENAGFEGSVIVNKLKEQ-VEGFGYN 476
Cdd:COG0459 366 ATRAAVEEGIVPGGGAALLRAARALRELAAKleGDEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKVRAAkDKGFGFD 445
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 2538675531 477 AATNEWVDMIAAGIVDPTKVTRSALQNAASVSALLLTTEAVVAELPSDDAA 527
Cdd:COG0459 446 AATGEYVDMLEAGVIDPAKVKRSALQNAASVAGLILTTEAVIADKPEKEEA 496
|
|
| groEL |
PRK12851 |
chaperonin GroEL; Reviewed |
1-538 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 171770 Cd Length: 541 Bit Score: 740.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 1 MAKELKFSEDARSKMKAGVDKLANTVKTTIGPKGRNVVLEQSYGAPTITNDGVTIAKAIELEDHFENMGAKLVAEVASKT 80
Cdd:PRK12851 2 AAKEVKFHVEAREKMLRGVNILADAVKVTLGPKGRNVVIDKSFGAPTITNDGVTIAKEIELEDKFENMGAQMVREVASKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 81 NDIAGDGTTTATVLTQAIVAEGLKNVTAGANPVGIRTGIEKATAAAVKKLHEMSHTVSTKAEIAQIASISASN-EEVGEL 159
Cdd:PRK12851 82 NDVAGDGTTTATVLAQAIVREGAKAVAAGANPMDLKRGIDRAVAAVVEELKANARPVTTNAEIAQVATISANGdAEIGRL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 160 IAEAMDKVGNDGVITIEESKGIETTLDVVEGMQFDRGYMSQYMVTDNDKMEANLDNPYILITDKKISNIQDVLPVLQSVV 239
Cdd:PRK12851 162 VAEAMEKVGNEGVITVEESKTAETELEVVEGMQFDRGYLSPYFVTDADKMEAELEDPYILIHEKKISNLQDLLPVLEAVV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 240 EQGRALLIIADDITGEALPTLVLNKMRGTFNVVAVKAPGFGDRRKAQLEDIAVLTGGTVITEDLGLNLKDVTIDQLGQAS 319
Cdd:PRK12851 242 QSGKPLLIIAEDVEGEALATLVVNKLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGIKLENVTLEQLGRAK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 320 KVNVSKDNTTIVEGSGDKNAVATRVDIIKQQIAETTSDFDREKLQERLAKLAGGVAVINVGAATETELKERKYRIEDALN 399
Cdd:PRK12851 322 KVVVEKENTTIIDGAGSKTEIEGRVAQIRAQIEETTSDYDREKLQERLAKLAGGVAVIRVGASTEVEVKEKKDRVDDALH 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 400 ATRAAVEEGFVSGGGTALVNAISAVTALSEV-GDVQTGINTVIKALEAPVRQIVENAGFEGSVIVNKLKEQVEGFGYNAA 478
Cdd:PRK12851 402 ATRAAVEEGIVPGGGVALLRAVKALDKLETAnGDQRTGVEIVRRALEAPVRQIAENAGAEGSVVVGKLREKPGGYGFNAA 481
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 479 TNEWVDMIAAGIVDPTKVTRSALQNAASVSALLLTTEAVVAELPSDDAASAMPQGGMPGM 538
Cdd:PRK12851 482 TNEYGDLYAQGVIDPVKVVRTALQNAASVAGLLLTTEAMVAEKPKKEPAPPAPPGGGMDF 541
|
|
| groEL |
PRK12852 |
chaperonin GroEL; Reviewed |
1-539 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237232 Cd Length: 545 Bit Score: 720.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 1 MAKELKFSEDARSKMKAGVDKLANTVKTTIGPKGRNVVLEQSYGAPTITNDGVTIAKAIELEDHFENMGAKLVAEVASKT 80
Cdd:PRK12852 2 AAKDVKFSGDARDRMLRGVDILANAVKVTLGPKGRNVVIEKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVREVASKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 81 NDIAGDGTTTATVLTQAIVAEGLKNVTAGANPVGIRTGIEKATAAAVKKLHEMSHTVSTKAEIAQIASISAS-NEEVGEL 159
Cdd:PRK12852 82 NDLAGDGTTTATVLAQAIVREGAKAVAAGMNPMDLKRGIDIAVAAVVKDIEKRAKPVASSAEIAQVGTISANgDAAIGKM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 160 IAEAMDKVGNDGVITIEESKGIETTLDVVEGMQFDRGYMSQYMVTDNDKMEANLDNPYILITDKKISNIQDVLPVLQSVV 239
Cdd:PRK12852 162 IAQAMQKVGNEGVITVEENKSLETEVDIVEGMKFDRGYLSPYFVTNAEKMTVELDDAYILLHEKKLSGLQAMLPVLEAVV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 240 EQGRALLIIADDITGEALPTLVLNKMRGTFNVVAVKAPGFGDRRKAQLEDIAVLTGGTVITEDLGLNLKDVTIDQLGQAS 319
Cdd:PRK12852 242 QSGKPLLIIAEDVEGEALATLVVNRLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGQLISEDLGIKLENVTLKMLGRAK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 320 KVNVSKDNTTIVEGSGDKNAVATRVDIIKQQIAETTSDFDREKLQERLAKLAGGVAVINVGAATETELKERKYRIEDALN 399
Cdd:PRK12852 322 KVVIDKENTTIVNGAGKKADIEARVGQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKEKKDRVEDALN 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 400 ATRAAVEEGFVSGGGTALVNAISAVTALSEVG-DVQTGINTVIKALEAPVRQIVENAGFEGSVIVNKLKE-QVEGFGYNA 477
Cdd:PRK12852 402 ATRAAVQEGIVPGGGVALLRAKKAVGRINNDNaDVQAGINIVLKALEAPIRQIAENAGVEGSIVVGKILEnKSETFGFDA 481
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2538675531 478 ATNEWVDMIAAGIVDPTKVTRSALQNAASVSALLLTTEAVVAELPSDDAASAMPQGGMPGMM 539
Cdd:PRK12852 482 QTEEYVDMVAKGIIDPAKVVRTALQDAASVAGLLVTTEAMVAELPKKDAAPAMPAGGGMGGM 543
|
|
| PTZ00114 |
PTZ00114 |
Heat shock protein 60; Provisional |
2-535 |
0e+00 |
|
Heat shock protein 60; Provisional
Pssm-ID: 185455 Cd Length: 555 Bit Score: 688.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 2 AKELKFSEDARSKMKAGVDKLANTVKTTIGPKGRNVVLEQSYGAPTITNDGVTIAKAIELEDHFENMGAKLVAEVASKTN 81
Cdd:PTZ00114 14 GKEIRFGDEARQSLLKGIERLADAVAVTLGPKGRNVIIEQEYGSPKITKDGVTVAKAIEFSDRFENVGAQLIRQVASKTN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 82 DIAGDGTTTATVLTQAIVAEGLKNVTAGANPVGIRTGIEKATAAAVKKLHEMSHTVSTKAEIAQIASISASN-EEVGELI 160
Cdd:PTZ00114 94 DKAGDGTTTATILARAIFREGCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQSRPVKTKEDILNVATISANGdVEIGSLI 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 161 AEAMDKVGNDGVITIEESKGIETTLDVVEGMQFDRGYMSQYMVTDNDKMEANLDNPYILITDKKISNIQDVLPVLQSVVE 240
Cdd:PTZ00114 174 ADAMDKVGKDGTITVEDGKTLEDELEVVEGMSFDRGYISPYFVTNEKTQKVELENPLILVTDKKISSIQSILPILEHAVK 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 241 QGRALLIIADDITGEALPTLVLNKMRGTFNVVAVKAPGFGDRRKAQLEDIAVLTGGTVITED-LGLNLKDVTIDQLGQAS 319
Cdd:PTZ00114 254 NKRPLLIIAEDVEGEALQTLIINKLRGGLKVCAVKAPGFGDNRKDILQDIAVLTGATVVSEDnVGLKLDDFDPSMLGSAK 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 320 KVNVSKDNTTIVEGSGDKNAVATRVDIIKQQIAETTSDFDREKLQERLAKLAGGVAVINVGAATETELKERKYRIEDALN 399
Cdd:PTZ00114 334 KVTVTKDETVILTGGGDKAEIKERVELLRSQIERTTSEYDKEKLKERLAKLSGGVAVIKVGGASEVEVNEKKDRIEDALN 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 400 ATRAAVEEGFVSGGGTALVNAISAVTALSE----VGDVQTGINTVIKALEAPVRQIVENAGFEGSVIVNKLKE-QVEGFG 474
Cdd:PTZ00114 414 ATRAAVEEGIVPGGGVALLRASKLLDKLEEdnelTPDQRTGVKIVRNALRLPTKQIAENAGVEGAVVVEKILEkKDPSFG 493
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2538675531 475 YNAATNEWVDMIAAGIVDPTKVTRSALQNAASVSALLLTTEAVVAELPSDDAAS-AMPQGGM 535
Cdd:PTZ00114 494 YDAQTGEYVNMFEAGIIDPTKVVRSALVDAASVASLMLTTEAAIVDLPKEKKKNkNSAAPPM 555
|
|
| groEL |
CHL00093 |
chaperonin GroEL |
1-520 |
0e+00 |
|
chaperonin GroEL
Pssm-ID: 177025 Cd Length: 529 Bit Score: 674.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 1 MAKELKFSEDARSKMKAGVDKLANTVKTTIGPKGRNVVLEQSYGAPTITNDGVTIAKAIELEDHFENMGAKLVAEVASKT 80
Cdd:CHL00093 1 MSKKILYQDNARRALERGMDILAEAVSVTLGPKGRNVVLEKKYGSPQIVNDGVTIAKEIELEDHIENTGVALIRQAASKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 81 NDIAGDGTTTATVLTQAIVAEGLKNVTAGANPVGIRTGIEKATAAAVKKLHEMSHTVSTKAEIAQIASISASN-EEVGEL 159
Cdd:CHL00093 81 NDVAGDGTTTATVLAYAIVKQGMKNVAAGANPISLKRGIEKATQYVVSQIAEYARPVEDIQAITQVASISAGNdEEVGSM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 160 IAEAMDKVGNDGVITIEESKGIETTLDVVEGMQFDRGYMSQYMVTDNDKMEANLDNPYILITDKKISNI-QDVLPVLQSV 238
Cdd:CHL00093 161 IADAIEKVGREGVISLEEGKSTVTELEITEGMRFEKGFISPYFVTDTERMEVVQENPYILLTDKKITLVqQDLLPILEQV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 239 VEQGRALLIIADDITGEALPTLVLNKMRGTFNVVAVKAPGFGDRRKAQLEDIAVLTGGTVITEDLGLNLKDVTIDQLGQA 318
Cdd:CHL00093 241 TKTKRPLLIIAEDVEKEALATLVLNKLRGIVNVVAVRAPGFGDRRKAMLEDIAILTGGQVITEDAGLSLETIQLDLLGQA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 319 SKVNVSKDNTTIVeGSGDKNAVATRVDIIKQQIAETTSDFDREKLQERLAKLAGGVAVINVGAATETELKERKYRIEDAL 398
Cdd:CHL00093 321 RRIIVTKDSTTII-ADGNEEQVKARCEQLRKQIEIADSSYEKEKLQERLAKLSGGVAVIKVGAATETEMKDKKLRLEDAI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 399 NATRAAVEEGFVSGGGTALVNAISAVTALSE---VGDVQTGINTVIKALEAPVRQIVENAGFEGSVIVNKLKEQVEGFGY 475
Cdd:CHL00093 400 NATKAAVEEGIVPGGGATLVHLSENLKTWAKnnlKEDELIGALIVARAILAPLKRIAENAGKNGSVIIEKVQEQDFEIGY 479
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 2538675531 476 NAATNEWVDMIAAGIVDPTKVTRSALQNAASVSALLLTTEAVVAE 520
Cdd:CHL00093 480 NAANNKFVNMYEAGIIDPAKVTRSALQNAASIASMILTTECIIVD 524
|
|
| PRK14104 |
PRK14104 |
chaperonin GroEL; Provisional |
2-538 |
0e+00 |
|
chaperonin GroEL; Provisional
Pssm-ID: 172594 Cd Length: 546 Bit Score: 600.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 2 AKELKFSEDARSKMKAGVDKLANTVKTTIGPKGRNVVLEQSYGAPTITNDGVTIAKAIELEDHFENMGAKLVAEVASKTN 81
Cdd:PRK14104 3 AKEVKFGVDARDRMLRGVDILANAVKVTLGPKGRNVVLDKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVREVASKSA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 82 DIAGDGTTTATVLTQAIVAEGLKNVTAGANPVGIRTGIEKATAAAVKKLHEMSHTVSTKAEIAQIASISAS-NEEVGELI 160
Cdd:PRK14104 83 DAAGDGTTTATVLAQAIVREGAKSVAAGMNPMDLKRGIDLAVEAVVADLVKNSKKVTSNDEIAQVGTISANgDAEIGKFL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 161 AEAMDKVGNDGVITIEESKGIETTLDVVEGMQFDRGYMSQYMVTDNDKMEANLDNPYILITDKKISNIQDVLPVLQSVVE 240
Cdd:PRK14104 163 ADAMKKVGNEGVITVEEAKSLETELDVVEGMQFDRGYISPYFVTNADKMRVEMDDAYILINEKKLSSLNELLPLLEAVVQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 241 QGRALLIIADDITGEALPTLVLNKMRGTFNVVAVKAPGFGDRRKAQLEDIAVLTGGTVITEDLGLNLKDVTIDQLGQASK 320
Cdd:PRK14104 243 TGKPLVIVAEDVEGEALATLVVNRLRGGLKVAAVKAPGFGDRRKAMLQDIAILTGGQAISEDLGIKLENVTLQMLGRAKK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 321 VNVSKDNTTIVEGSGDKNAVATRVDIIKQQIAETTSDFDREKLQERLAKLAGGVAVINVGAATETELKERKYRIEDALNA 400
Cdd:PRK14104 323 VMIDKENTTIVNGAGKKADIEARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKERKDRVDDAMHA 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 401 TRAAVEEGFVSGGGTALVNAISAVTAL-SEVGDVQTGINTVIKALEAPVRQIVENAGFEGSVIVNKLKEQVE-GFGYNAA 478
Cdd:PRK14104 403 TRAAVEEGIVPGGGVALLRASEQLKGIkTKNDDQKTGVEIVRKALSAPARQIAINAGEDGSVIVGKILEKEQySYGFDSQ 482
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2538675531 479 TNEWVDMIAAGIVDPTKVTRSALQNAASVSALLLTTEAVVAELPSDDAASA--MPQGGMPGM 538
Cdd:PRK14104 483 TGEYGNLVSKGIIDPTKVVRTAIQNAASVAALLITTEAMVAELPKKGGAGPamPPGGGMGGM 544
|
|
| PLN03167 |
PLN03167 |
Chaperonin-60 beta subunit; Provisional |
2-529 |
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 2538675531 2 AKELKFSED--ARSKMKAGVDKLANTVKTTIGPKGRNVVLEQSYGAPTITNDGVTIAKAIELEDHFENMGAKLVAEVASK 79
Cdd:PLN03167 56 AKELHFNKDgsAIKKLQAGVNKLADLVGVTLGPKGRNVVLESKYGSPKIVNDGVTVAKEVELEDPVENIGAKLVRQAAAK 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 80 TNDIAGDGTTTATVLTQAIVAEGLKNVTAGANPVGIRTGIEKATAAAVKKLHEMSHTVStKAEIAQIASISA-SNEEVGE 158
Cdd:PLN03167 136 TNDLAGDGTTTSVVLAQGLIAEGVKVVAAGANPVQITRGIEKTAKALVKELKKMSKEVE-DSELADVAAVSAgNNYEVGN 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 159 LIAEAMDKVGNDGVITIEESKGIETTLDVVEGMQFDRGYMSQYMVTDNDKMEANLDNPYILITDKKISNIQDVLPVLQSV 238
Cdd:PLN03167 215 MIAEAMSKVGRKGVVTLEEGKSAENNLYVVEGMQFDRGYISPYFVTDSEKMSVEYDNCKLLLVDKKITNARDLIGILEDA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 239 VEQGRALLIIADDITGEALPTLVLNKMRGTFNVVAVKAPGFGDRRKAQLEDIAVLTGGTVITEDLGLNLKDVTIDQLGQA 318
Cdd:PLN03167 295 IRGGYPLLIIAEDIEQEALATLVVNKLRGSLKIAALKAPGFGERKSQYLDDIAILTGGTVIREEVGLSLDKVGKEVLGTA 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 319 SKVNVSKDNTTIVEGSGDKNAVATRVDIIKQQIAETTSDFDREKLQERLAKLAGGVAVINVGAATETELKERKYRIEDAL 398
Cdd:PLN03167 375 AKVVLTKDTTTIVGDGSTQEAVNKRVAQIKNLIEAAEQDYEKEKLNERIAKLSGGVAVIQVGAQTETELKEKKLRVEDAL 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 399 NATRAAVEEGFVSGGGTALVNAISAVTALSEVGDVQ---TGINTVIKALEAPVRQIVENAGFEGSVIVNK-LKEQVEGFG 474
Cdd:PLN03167 455 NATKAAVEEGIVVGGGCTLLRLASKVDAIKDTLENDeqkVGADIVKRALSYPLKLIAKNAGVNGSVVSEKvLSNDNPKFG 534
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 2538675531 475 YNAATNEWVDMIAAGIVDPTKVTRSALQNAASVSALLLTTEAVVAELPSDDAASA 529
Cdd:PLN03167 535 YNAATGKYEDLMAAGIIDPTKVVRCCLEHAASVAKTFLTSDCVVVEIKEPEPVPA 589
|
|
| chaperonin_type_I_II |
cd00309 |
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ... |
3-519 |
5.52e-150 |
|
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: 438.02 E-value: 5.52e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 3 KELKFSEDARSKMKAGVDKLANTVKTTIGPKGRNVVLEQSYGAPTITNDGVTIAKAIELEdhfeNMGAKLVAEVASKTND 82
Cdd:cd00309 1 KEREFGEEARLSNINAAKALADAVKTTLGPKGMDKMLVDSLGDPTITNDGATILKEIEVE----HPAAKLLVEVAKSQDD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 83 IAGDGTTTATVLTQAIVAEGLKNVTAGANPVGIRTGIEKATAAAVKKLHEMS--HTVSTKAEIAQIASISAS-------N 153
Cdd:cd00309 77 EVGDGTTTVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAvpIDVEDREELLKVATTSLNsklvsggD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 154 EEVGELIAEAMDKVG------NDGVITIEESKG---IETTLdvVEGMQFDRGYMSQYmvtdndkMEANLDNPYILITDKK 224
Cdd:cd00309 157 DFLGELVVDAVLKVGkengdvDLGVIRVEKKKGgslEDSEL--VVGMVFDKGYLSPY-------MPKRLENAKILLLDCK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 225 ISNiqdvlpvlqsvveqgralLIIADD-ITGEALPTLVLNkmrgtfNVVAVKApgfgdRRKAQLEDIAVLTGGTVITEdl 303
Cdd:cd00309 228 LEY------------------VVIAEKgIDDEALHYLAKL------GIMAVRR-----VRKEDLERIAKATGATIVSR-- 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 304 glnLKDVTIDQLGQASKVNVSK----DNTTIVEGSGdknavatrvdiikqqiaettsdfdreklqerlaklaGGVAVINV 379
Cdd:cd00309 277 ---LEDLTPEDLGTAGLVEETKigdeKYTFIEGCKG------------------------------------GKVATILL 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 380 GAATETELKERKYRIEDALNATRAAVEE-GFVSGGGTALVNAISAVTALSEV--GDVQTGINTVIKALEAPVRQIVENAG 456
Cdd:cd00309 318 RGATEVELDEAERSLHDALCAVRAAVEDgGIVPGGGAAEIELSKALEELAKTlpGKEQLGIEAFADALEVIPRTLAENAG 397
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2538675531 457 FEGSVIVNKLKEQVEGFGYNAA----TNEWVDMIAAGIVDPTKVTRSALQNAASVSALLLTTEAVVA 519
Cdd:cd00309 398 LDPIEVVTKLRAKHAEGGGNAGgdveTGEIVDMKEAGIIDPLKVKRQALKSATEAASLILTIDDIIV 464
|
|
| Cpn60_TCP1 |
pfam00118 |
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ... |
22-518 |
1.25e-86 |
|
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: 276.01 E-value: 1.25e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 22 LANTVKTTIGPKGRNVVLEQSYGAPTITNDGVTIAKAIELEdhfeNMGAKLVAEVASKTNDIAGDGTTTATVLTQAIVAE 101
Cdd:pfam00118 1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELEIQ----HPAAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 102 GLKNVTAGANPVGIRTGIEKATAAAVKKLHEM---SHTVSTKAEIAQIASISASN-------EEVGELIAEA-------- 163
Cdd:pfam00118 77 AEKLLAAGVHPTTIIEGYEKALEKALEILDSIisiPVEDVDREDLLKVARTSLSSkiisresDFLAKLVVDAvlaipknd 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 164 -MDKVGNDGVITIEESKGIETTLdvVEGMQFDRGYMSQYMVTDndkmeanLDNPYILITDKKISNIQD------------ 230
Cdd:pfam00118 157 gSFDLGNIGVVKILGGSLEDSEL--VDGVVLDKGPLHPDMPKR-------LENAKVLLLNCSLEYEKTetkatvvlsdae 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 231 ------------VLPVLQSVVEQGRALLIIADDITGEALPTLVLNKMRGTFNVvavkapgfgdrRKAQLEDIAVLTGGTV 298
Cdd:pfam00118 228 qlerflkaeeeqILEIVEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMALRRV-----------KKRDLERLAKATGARA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 299 ITedlglNLKDVTIDQLGQASKV---NVSKDNTTIVEGSGDknavatrvdiikqqiaettsdfdreklqerlaklaGGVA 375
Cdd:pfam00118 297 VS-----SLDDLTPDDLGTAGKVeeeKIGDEKYTFIEGCKS-----------------------------------PKAA 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 376 VINVGAATETELKERKYRIEDALNATRAAVEE-GFVSGGG---TALVNAISAvTALSEVGDVQTGINTVIKALEAPVRQI 451
Cdd:pfam00118 337 TILLRGATDHVLDEIERSIHDALCVVKNAIEDpRVVPGGGaveMELARALRE-YAKSVSGKEQLAIEAFAEALEVIPKTL 415
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2538675531 452 VENAGFEGSVIVNKLK-EQVEG---FGYNAATNEWVDMIAAGIVDPTKVTRSALQNAASVSALLLTTEAVV 518
Cdd:pfam00118 416 AENAGLDPIEVLAELRaAHASGekhAGIDVETGEIIDMKEAGVVDPLKVKRQALKSATEAASTILRIDDII 486
|
|
| chaperonin_like |
cd03333 |
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ... |
140-407 |
6.46e-40 |
|
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: 143.76 E-value: 6.46e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 140 KAEIAQIASISAS------NEEVGELIAEAMDKVG------NDGVITIEESKG---IETTLdvVEGMQFDRGYMSQYMvt 204
Cdd:cd03333 1 RELLLQVATTSLNsklsswDDFLGKLVVDAVLKVGpdnrmdDLGVIKVEKIPGgslEDSEL--VVGVVFDKGYASPYM-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 205 dndkmEANLDNPYILITDKKISNiqdvlpvlqsvveqgralLIIADD-ITGEALPTLVLNkmrgtfNVVAVKApgfgdRR 283
Cdd:cd03333 77 -----PKRLENAKILLLDCPLEY------------------VVIAEKgIDDLALHYLAKA------GIMAVRR-----VK 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 284 KAQLEDIAVLTGGTVITEdlglnLKDVTIDQLGQASKVNVSKD----NTTIVEGSGdknavatrvdiikqqiaettsdfd 359
Cdd:cd03333 123 KEDLERIARATGATIVSS-----LEDLTPEDLGTAELVEETKIgeekLTFIEGCKG------------------------ 173
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2538675531 360 reklqerlaklaGGVAVINVGAATETELKERKYRIEDALNATRAAVEE 407
Cdd:cd03333 174 ------------GKAATILLRGATEVELDEVKRSLHDALCAVRAAVEE 209
|
|
| cpn60 |
cd03343 |
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ... |
9-519 |
9.18e-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: 122.76 E-value: 9.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 9 EDARSKMKAGVDKLANTVKTTIGPKGRNVVLEQSYGAPTITNDGVTIAKAIELedhfENMGAKLVAEVASKTNDIAGDGT 88
Cdd:cd03343 14 RDAQRMNIAAAKAVAEAVRTTLGPKGMDKMLVDSLGDVTITNDGATILKEMDI----EHPAAKMLVEVAKTQDEEVGDGT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 89 TTATVLTQAIVAEGLKNVTAGANPVGIRTGIEKATAAAVKKLHEMSHTVSTKAE-----IAQIASISASNEEVGELIAEa 163
Cdd:cd03343 90 TTAVVLAGELLEKAEDLLDQNIHPTVIIEGYRLAAEKALELLDEIAIKVDPDDKdtlrkIAKTSLTGKGAEAAKDKLAD- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 164 mdkVGNDGVITIEESKGIETTLDV-------VEGMQFDRGYMSQYMVTD----NDKMEANLDNPYILITDKKIS------ 226
Cdd:cd03343 169 ---LVVDAVLQVAEKRDGKYVVDLdnikiekKTGGSVDDTELIRGIVIDkevvHPGMPKRVENAKIALLDAPLEvkktei 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 227 ----NIQDVLPVLQSVVEQGRALLIIADDITGEALPTLVLNKmrGTFNVVA---VKAPGFGDRR--KAQLEDIAVLTGGT 297
Cdd:cd03343 246 dakiRITSPDQLQAFLEQEEAMLKEMVDKIADTGANVVFCQK--GIDDLAQhylAKAGILAVRRvkKSDMEKLARATGAK 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 298 VITedlglNLKDVTIDQLGQASKV---NVSKDNTTIVEgsGDKNAVAtrVDIIkqqiaettsdfdreklqerlakLAGGv 374
Cdd:cd03343 324 IVT-----NIDDLTPEDLGEAELVeerKVGDDKMVFVE--GCKNPKA--VTIL----------------------LRGG- 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 375 avinvgaaTETELKERKYRIEDALNATRAAVEEG-FVSGGGTALVNAISAVT--ALSEVGDVQTGINTVIKALEAPVRQI 451
Cdd:cd03343 372 --------TEHVVDELERALEDALRVVADALEDGkVVAGGGAVEIELAKRLReyARSVGGREQLAVEAFADALEEIPRTL 443
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2538675531 452 VENAGFEGSVIVNKLK----EQVEGFGYNAATNEWVDMIAAGIVDPTKVTRSALQNAASVSALLLTTEAVVA 519
Cdd:cd03343 444 AENAGLDPIDTLVELRaaheKGNKNAGLDVYTGEVVDMLEKGVIEPLRVKKQAIKSATEAATMILRIDDVIA 515
|
|
| thermosome_beta |
NF041083 |
thermosome subunit beta; |
22-519 |
5.47e-28 |
|
thermosome subunit beta;
Pssm-ID: 469010 Cd Length: 519 Bit Score: 117.36 E-value: 5.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 22 LANTVKTTIGPKGRNVVLEQSYGAPTITNDGVTIAKAIELedhfENMGAKLVAEVASKTNDIAGDGTTTATVLTQAIVAE 101
Cdd:NF041083 29 VAEAVRTTLGPKGMDKMLVDSLGDIVITNDGATILKEMDV----QHPAAKMLVEVAKTQDDEVGDGTTTAVVLAGELLKK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 102 GLKNVTAGANPVGIRTGIEKATAAAVKKLHEMSHTVSTKAE-----IAQIASISASNEEVGELIAEamdkVGNDGVITIE 176
Cdd:NF041083 105 AEELLDQNIHPTIIANGYRLAAEKAIEILDEIAEKVDPDDRetlkkIAETSLTSKGVEEARDYLAE----IAVKAVKQVA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 177 ESKGIETTLDV------------VEGMQFDRGymsqyMVTDNDK----MEANLDNPYILITDKKI--------SNIQDVL 232
Cdd:NF041083 181 EKRDGKYYVDLdniqiekkhggsIEDTQLIYG-----IVIDKEVvhpgMPKRVENAKIALLDAPLevkkteidAEIRITD 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 233 P-VLQSVVEQGRALL------IIA------------DDITGEALPTlvlnkmRGTFNVVAVKapgfgdrrKAQLEDIAVL 293
Cdd:NF041083 256 PdQLQKFLDQEEKMLkemvdkIKAtganvvfcqkgiDDLAQHYLAK------AGILAVRRVK--------KSDMEKLAKA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 294 TGGTVITedlglNLKDVTIDQLGQASKV---NVSKDNTTIVEGSGDKNAVAtrvdiikqqiaettsdfdreklqerlakl 370
Cdd:NF041083 322 TGARIVT-----NIDDLTPEDLGYAELVeerKVGDDKMVFVEGCKNPKAVT----------------------------- 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 371 aggvavINVGAATETELKERKYRIEDALNATRAAVEEGFVSGGGTALVNAISAVT---ALSEVGDVQTGINTVIKALEAP 447
Cdd:NF041083 368 ------ILIRGGTEHVVDEAERALEDALSVVADAVEDGKIVAGGGAPEVELAKRLreyAATVGGREQLAVEAFAEALEII 441
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2538675531 448 VRQIVENAGFEGSVIVNKLKEQVE----GFGYNAATNEWVDMIAAGIVDPTKVTRSALQNAASVSALLLTTEAVVA 519
Cdd:NF041083 442 PRTLAENAGLDPIDILVKLRSAHEkgkkWAGINVFTGEVVDMWELGVIEPLRVKTQAIKSATEAATMILRIDDVIA 517
|
|
| thermosome_alpha |
NF041082 |
thermosome subunit alpha; |
22-519 |
1.15e-27 |
|
thermosome subunit alpha;
Pssm-ID: 469009 Cd Length: 518 Bit Score: 116.52 E-value: 1.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 22 LANTVKTTIGPKGRNVVLEQSYGAPTITNDGVTIAKAIELedhfENMGAKLVAEVASKTNDIAGDGTTTATVLTQAIVAE 101
Cdd:NF041082 29 VAEAVRTTLGPKGMDKMLVDSLGDVVITNDGVTILKEMDI----EHPAAKMIVEVAKTQDDEVGDGTTTAVVLAGELLKK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 102 GLKNVTAGANPVGIRTGIEKATAAAVKKLHEMSHTVSTK-----AEIAQIA----SISASNEEVGELIAEA----MDKVG 168
Cdd:NF041082 105 AEELLDQDIHPTIIAEGYRLAAEKALEILDEIAIKVDPDdketlKKIAATAmtgkGAEAAKDKLADLVVDAvkavAEKDG 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 169 NDGV----ITIEESKG--IETTlDVVEGMQFDRGYMSQYM--VTDNDKMeANLDNPyILI----TDKKIsNIQDVLPVLQ 236
Cdd:NF041082 185 GYNVdldnIKVEKKVGgsIEDS-ELVEGVVIDKERVHPGMpkRVENAKI-ALLDAP-LEVkkteIDAKI-SITDPDQLQA 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 237 SVVEQGRALLIIADDI--TGEalptlvlnkmrgtfNVVAV-------------KAPGFGDRR--KAQLEDIAVLTGGTVI 299
Cdd:NF041082 261 FLDQEEKMLKEMVDKIadSGA--------------NVVFCqkgiddlaqhylaKEGILAVRRvkKSDMEKLAKATGARIV 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 300 TedlglNLKDVTIDQLGQASKV---NVSKDNTTIVEGSgdKNAVAtrVDIIkqqiaettsdfdreklqerlakLAGGvav 376
Cdd:NF041082 327 T-----SIDDLSPEDLGYAGLVeerKVGGDKMIFVEGC--KNPKA--VTIL----------------------LRGG--- 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 377 invgaaTETELKERKYRIEDALNATRAAVEEGFVSGGGTALVNAISavTALSEVGDV-----QTGINTVIKALEAPVRQI 451
Cdd:NF041082 373 ------TEHVVDEVERALEDALRVVRVVLEDGKVVAGGGAPEVELA--LRLREYAASvggreQLAIEAFAEALEIIPRTL 444
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2538675531 452 VENAGFEGSVIVNKLKEQVEG----FGYNAATNEWVDMIAAGIVDPTKVTRSALQNAASVSALLLTTEAVVA 519
Cdd:NF041082 445 AENAGLDPIDALVELRSAHEKgnktAGLDVYTGKVVDMLEIGVVEPLRVKTQAIKSATEAAVMILRIDDVIA 516
|
|
| TCP1_eta |
cd03340 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ... |
21-512 |
6.74e-19 |
|
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: 89.65 E-value: 6.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 21 KLANTVKTTIGPKGRNVVLEQSYGAPTITNDGVTIAKAIELedhfENMGAKLVAEVASKTNDIAGDGTTTATVLTQAIVA 100
Cdd:cd03340 27 AIADAVRTTLGPRGMDKLIVDGRGKVTISNDGATILKLLDI----VHPAAKTLVDIAKSQDAEVGDGTTSVVVLAGEFLK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 101 EGLKNVTAGANPVGIRTGIEKATAAAVKKLHEMSHTVSTKAE------IAQIAS-------ISASNEEVGELIAEAMDKV 167
Cdd:cd03340 103 EAKPFIEDGVHPQIIIRGYRKALQLAIEKIKEIAVNIDKEDKeeqrelLEKCAAtalnsklIASEKEFFAKMVVDAVLSL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 168 GND---GVITIEESKG--IETTLdVVEGMQFDR-----GYMSQYMVTDNDK---------MEANLDNPYILITDKKIsni 228
Cdd:cd03340 183 DDDldlDMIGIKKVPGgsLEDSQ-LVNGVAFKKtfsyaGFEQQPKKFKNPKilllnveleLKAEKDNAEVRVEDPEE--- 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 229 qdvlpvLQSVVEQGRAllIIADDitgealptlvLNKMRGT-FNVVAVKAP-G------FGDRR--------KAQLEDIAV 292
Cdd:cd03340 259 ------YQAIVDAEWK--IIYDK----------LEKIVKSgANVVLSKLPiGdlatqyFADRDifcagrvpEEDLKRVAQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 293 LTGGTVITEdlGLNLKDVTIDQLGQASKVNVSKDNTTIVEGSGDKNAVAtrvdII-----KQQIAETtsdfdreklqerl 367
Cdd:cd03340 321 ATGGSIQTT--VSNITDDVLGTCGLFEERQVGGERYNIFTGCPKAKTCT----IIlrggaEQFIEEA------------- 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 368 aklaggvavinvgaatetelkERKyrIEDALNATRAAVEEGFVSGGGTALVNAISAVT---ALSEVGDVQTGINTVIKAL 444
Cdd:cd03340 382 ---------------------ERS--LHDAIMIVRRAIKNDSVVAGGGAIEMELSKYLrdySRTIAGKQQLVINAFAKAL 438
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2538675531 445 EAPVRQIVENAGFEGSVIVNKLKEQ-----VEGFGYNAATNEWVDMIAAGIVDPTKVTRSALQNAASVSALLL 512
Cdd:cd03340 439 EIIPRQLCDNAGFDATDILNKLRQKhaqggGKWYGVDINNEGIADNFEAFVWEPSLVKINALTAATEAACLIL 511
|
|
| chap_CCT_eta |
TIGR02345 |
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ... |
21-518 |
1.68e-18 |
|
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: 88.66 E-value: 1.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 21 KLANTVKTTIGPKGRNVVLEQSYGAPTITNDGVTIAKAIELedhfENMGAKLVAEVASKTNDIAGDGTTTATVLTQAIVA 100
Cdd:TIGR02345 29 AIAEALKTTLGPRGMDKLIVGSNGKATISNDGATILKLLDI----VHPAAKTLVDIAKSQDAEVGDGTTSVTILAGELLK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 101 EGLKNVTAGANPVGIRTGIEKATAAAVKKLHEMSHTV-STKAEIAQIAS-----------ISASNEEVGELIAEAMDKVG 168
Cdd:TIGR02345 105 EAKPFIEEGVHPQLIIRCYREALSLAVEKIKEIAVTIdEEKGEQRELLEkcaatalssklISHNKEFFSKMIVDAVLSLD 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 169 ND----GVITIEESKG--IETTLdVVEGMQFDR-----GYMSQYMVTDNDK---------MEANLDNPYILITDKKisni 228
Cdd:TIGR02345 185 RDdldlKLIGIKKVQGgaLEDSQ-LVNGVAFKKtfsyaGFEQQPKKFANPKilllnveleLKAEKDNAEIRVEDVE---- 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 229 qdvlpVLQSVVEQGRALLIIADDITGEALPTLVLNKMrgtfnvvavkapGFGDRRKAQLEDIAVLTGGTVITEDLGlnlk 308
Cdd:TIGR02345 260 -----DYQAIVDAEWAIIFRKLEKIVESGANVVLSKL------------PIGDLATQYFADRDIFCAGRVSAEDLK---- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 309 dvtidqlgqaskvnvskdntTIVEGSGdkNAVATRVDIIKQQIAETTSDFDREKL-QERLAKLAGGVaviNVGAAT---- 383
Cdd:TIGR02345 319 --------------------RVIKACG--GSIQSTTSDLEADVLGTCALFEERQIgSERYNYFTGCP---HAKTCTiilr 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 384 ---ETELKERKYRIEDALNATRAAVEEGFVSGGGTALVNAISAVT---ALSEVGDVQTGINTVIKALEAPVRQIVENAGF 457
Cdd:TIGR02345 374 ggaEQFIEEAERSLHDAIMIVRRALKNKKIVAGGGAIEMELSKCLrdySKTIDGKQQLIINAFAKALEIIPRQLCENAGF 453
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2538675531 458 EGSVIVNKLK----EQVEGFGYNAATNEWVDMIAAGIVDPTKVTRSALQNAASVSALLLTTEAVV 518
Cdd:TIGR02345 454 DSIEILNKLRsrhaKGGKWYGVDINTEDIGDNFEAFVWEPALVKINALKAAFEAACTILSVDETI 518
|
|
| TCP1_delta |
cd03338 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ... |
22-525 |
1.50e-17 |
|
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: 85.42 E-value: 1.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 22 LANTVKTTIGPKGRNVVLEQSYGAPTITNDGVTIAKAIELeDHfenMGAKLVAEVaSKTNDI-AGDGTTTATVLTQAIVA 100
Cdd:cd03338 20 VADAIRTSLGPRGMDKMIQTGKGEVIITNDGATILKQMSV-LH---PAAKMLVEL-SKAQDIeAGDGTTSVVVLAGALLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 101 EGLKNVTAGANPVGIRTGIEKATAAAVKKLHEMSHTVS--TKAEIAQIASISASNEEV---GELIAE-AMD---KVGNDG 171
Cdd:cd03338 95 ACESLLKKGIHPTVISESFQIAAKKAVEILDSMSIPVDlnDRESLIKSATTSLNSKVVsqySSLLAPiAVDavlKVIDPA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 172 VITIEESKGIE-------TTLD--VVEGMQFDRGYM-----------------------------SQYMVTDNDKMEANL 213
Cdd:cd03338 175 TATNVDLKDIRivkklggTIEDteLVDGLVFTQKASkkaggptriekakigliqfclsppktdmdNNIVVNDYAQMDRIL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 214 --DNPYILITDKKIsniqdvlpvlqsvVEQGRALLIIADDITGEALPTL---VLNKMrgtfNVVAVKapgfgDRRKAQLE 288
Cdd:cd03338 255 reERKYILNMCKKI-------------KKSGCNVLLIQKSILRDAVSDLalhFLAKL----KIMVVK-----DIEREEIE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 289 DIAVLTGGTVITedlglNLKDVTIDQLGQASKV-NVSKDNTTIVEGSGDKNAVATrvdiikqqiaettsdfdreklqerl 367
Cdd:cd03338 313 FICKTIGCKPVA-----SIDHFTEDKLGSADLVeEVSLGDGKIVKITGVKNPGKT------------------------- 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 368 aklaggVAVInVGAATETELKERKYRIEDALNATRAAVEEGFVSGGGTALVNAISavTALSEVGDVQTGINTVI-----K 442
Cdd:cd03338 363 ------VTIL-VRGSNKLVLDEAERSLHDALCVIRCLVKKRALIPGGGAPEIEIA--LQLSEWARTLTGVEQYCvrafaD 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 443 ALEAPVRQIVENAGFEGSVIVNKLKEQ-VEG---FGYNAATNEWVDMIAAGIVDPTKVtrsalqnaaSVSALLLTTEAVV 518
Cdd:cd03338 434 ALEVIPYTLAENAGLNPISIVTELRNRhAQGeknAGINVRKGAITNILEENVVQPLLV---------STSAITLATETVR 504
|
....*..
gi 2538675531 519 AELPSDD 525
Cdd:cd03338 505 MILKIDD 511
|
|
| chap_CCT_epsi |
TIGR02343 |
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ... |
17-519 |
4.36e-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: 81.00 E-value: 4.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 17 AGVDKLANTVKTTIGPKGRNVVLEQSYGAPTITNDGVTIAKAIELEDHFenmgAKLVAEVASKTNDIAGDGTTTATVLTQ 96
Cdd:TIGR02343 34 AAAKSVASILRTSLGPKGMDKMLISPDGDITVTNDGATILSQMDVDNQI----AKLMVELSKSQDDEIGDGTTGVVVLAG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 97 AIVAEGLKNVTAGANPVGIRTGIEKATAAAVKKLHEMSHTVS---------TKAEIAQIAS--ISASNEEVGELIAEA-- 163
Cdd:TIGR02343 110 ALLEQAEELLDKGIHPIKIADGFEEAARIAVEHLEEISDEISadnnnreplIQAAKTSLGSkiVSKCHRRFAEIAVDAvl 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 164 --MDKVGND---GVITIEESKG--IETTlDVVEGMQFDRGYMSQYMVTD-NDKMEANLDNPY---ILITDKK--ISNIQD 230
Cdd:TIGR02343 190 nvADMERRDvdfDLIKVEGKVGgsLEDT-KLIKGIIIDKDFSHPQMPKEvEDAKIAILTCPFeppKPKTKHKldISSVEE 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 231 -----------VLPVLQSVVEQGRALLIIADDITGEALPTLVLNkmrgtfNVVAVKAPGfgdrrKAQLEDIAVLTGGTVI 299
Cdd:TIGR02343 269 ykklqkyeqqkFKEMIDDIKKSGANLVICQWGFDDEANHLLLQN------DLPAVRWVG-----GQELELIAIATGGRIV 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 300 TEdlglnLKDVTIDQLGQASKV-----NVSKDNTTIVEGSGDKNAVAtrvdiikqqiaettsdfdreklqerlaklaggv 374
Cdd:TIGR02343 338 PR-----FQELSKDKLGKAGLVreisfGTTKDRMLVIEQCKNSKAVT--------------------------------- 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 375 avINVGAATETELKERKYRIEDALNATRAAVEEG-FVSGGGTAlvnAISAVTALSEVGDVQTG-----INTVIKALEAPV 448
Cdd:TIGR02343 380 --IFIRGGNKMIIEEAKRSIHDALCVVRNLIKDSrIVYGGGAA---EISCSLAVSQEADKYPGveqyaIRAFADALETIP 454
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2538675531 449 RQIVENAGFE-----GSVIVNKLKEQVEGFGYNAATNEWVDMIAAGIVDPTKVTRSALQNAASVSALLLTTEAVVA 519
Cdd:TIGR02343 455 MALAENSGLDpigtlSTLKSLQLKEKNPNLGVDCLGYGTNDMKEQFVFETLIGKKQQILLATQLVRMILKIDDVIS 530
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
9-134 |
2.11e-14 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 75.84 E-value: 2.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 9 EDARSKMKAGVDKLANTVKTTIGPKGRNVVLE-----QSYGAPTITNDGVTIAKAIELEdhfeNMGAKLVAEVASKTNDI 83
Cdd:PTZ00212 21 ETARLQSFVGAIAVADLVKTTLGPKGMDKILQpmsegPRSGNVTVTNDGATILKSVWLD----NPAAKILVDISKTQDEE 96
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2538675531 84 AGDGTTTATVLTQAIVAEGLKNVTAGANPVGIRTGIEKATAAAVKKLHEMS 134
Cdd:PTZ00212 97 VGDGTTSVVVLAGELLREAEKLLDQKIHPQTIIEGWRMALDVARKALEEIA 147
|
|
| TCP1_epsilon |
cd03339 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ... |
22-142 |
2.17e-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: 2.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 22 LANTVKTTIGPKGRNVVLEQSYGAPTITNDGVTIAKAIELEDHFenmgAKLVAEVASKTNDIAGDGTTTATVLTQAIVAE 101
Cdd:cd03339 35 VANILRTSLGPRGMDKILVSPDGEVTVTNDGATILEKMDVDHQI----AKLLVELSKSQDDEIGDGTTGVVVLAGALLEQ 110
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2538675531 102 GLKNVTAGANPVGIRTGIEKATAAAVKKLHEMSHTVSTKAE 142
Cdd:cd03339 111 AEKLLDRGIHPIRIADGYEQACKIAVEHLEEIADKIEFSPD 151
|
|
| TCP1_beta |
cd03336 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ... |
9-142 |
2.27e-14 |
|
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: 75.44 E-value: 2.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 9 EDARSKMKAGVDKLANTVKTTIGPKGRNVVLEQSY--GAPTITNDGVTIAKAIeledHFENMGAKLVAEVASKTNDIAGD 86
Cdd:cd03336 12 ETARLSSFVGAIAIGDLVKTTLGPKGMDKILQSVGrsGGVTVTNDGATILKSI----GVDNPAAKVLVDISKVQDDEVGD 87
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2538675531 87 GTTTATVLTQAIVAEGLKNVTAGANPVGIRTGIEKATAAAVKKLHEMSHTVSTKAE 142
Cdd:cd03336 88 GTTSVTVLAAELLREAEKLVAQKIHPQTIIEGYRMATAAAREALLSSAVDHSSDEE 143
|
|
| chap_CCT_delta |
TIGR02342 |
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ... |
22-152 |
1.27e-12 |
|
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: 70.20 E-value: 1.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 22 LANTVKTTIGPKGRNVVLEQSYGAPTITNDGVTIAKAIELEdhfeNMGAKLVAEVaSKTNDI-AGDGTTTATVLTQAIVA 100
Cdd:TIGR02342 21 VADAIRTSLGPKGMDKMIQDGKGEVIITNDGATILKQMAVL----HPAAKMLVEL-SKAQDIeAGDGTTSVVILAGALLG 95
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2538675531 101 EGLKNVTAGANPVGIRTGIEKATAAAVKKLHEMSHTVSTKAEIAQIASISAS 152
Cdd:TIGR02342 96 ACERLLNKGIHPTIISESFQSAADEAIKILDEMSIPVDLSDREQLLKSATTS 147
|
|
| chap_CCT_alpha |
TIGR02340 |
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ... |
9-532 |
2.09e-12 |
|
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: 69.36 E-value: 2.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 9 EDARSKMKAGVDKLANTVKTTIGPKGRNVVLEQSYGAPTITNDGVTIAKAIELEDHfenmGAKLVAEVASKTNDIAGDGT 88
Cdd:TIGR02340 11 QDVRTQNVTAAMAIANIVKTSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHP----AAKILVELAQLQDREVGDGT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 89 TTATVLTQAIVAEGLKNVTAGANPVGIRTGIEKATAAAVKKLHE-MSHTVST--KAEIAQIASISASNEEVGeLIAEAMD 165
Cdd:TIGR02340 87 TSVVIIAAELLKRADELVKNKIHPTSVISGYRLACKEAVKYIKEnLSVSVDElgREALINVAKTSMSSKIIG-LDSDFFS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 166 KVGNDGVITIEESKGIETTLDVVEGM-------------QFDRGYMSQYMVTDNdKMEANLDNPYILITDKKISNIQDVL 232
Cdd:TIGR02340 166 NIVVDAVLAVKTTNENGETKYPIKAInilkahgksaresMLVKGYALNCTVASQ-QMPKRIKNAKIACLDFNLQKAKMAL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 233 PVlQSVVEQGRALLIIAD---DITGEALPTL------VLNKMRGTFNVVA---VKAPGFGDRR--KAQLEDIAVLTGGTV 298
Cdd:TIGR02340 245 GV-QIVVDDPEKLEQIRQreaDITKERIKKIldaganVVLTTGGIDDMCLkyfVEAGAMGVRRckKEDLKRIAKATGATL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 299 ITEDLGLNlKDVTID--QLGQASKV---NVSKDNTTIVEGSGDKNAVAtrvdIIkqqiaettsdfdreklqerlakLAGg 373
Cdd:TIGR02340 324 VSTLADLE-GEETFEasYLGFADEVvqeRIADDECILIKGTKKRKSAS----II----------------------LRG- 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 374 vavinvgaATETELKERKYRIEDALNATRAAVEEGFVSGGGTALVNAISAVT---ALSEVGDVQTGINTVIKALEAPVRQ 450
Cdd:TIGR02340 376 --------ANDFMLDEMERSLHDALCVVKRTLESNSVVPGGGAVEAALSIYLenfATTLGSREQLAIAEFARALLIIPKT 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 451 IVENAGFEGSVIVNKL------------KEQVEGFGYNAATNEWVDMIAAGIVDPTKVTRSALQNAasvsallltTEAVV 518
Cdd:TIGR02340 448 LAVNAAKDSTELVAKLrayhaaaqlkpeKKHLKWYGLDLVNGKIRDNKEAGVLEPTVSKVKSLKFA---------TEAAI 518
|
570
....*....|....
gi 2538675531 519 AELPSDDAASAMPQ 532
Cdd:TIGR02340 519 TILRIDDLIKLNPE 532
|
|
| chap_CCT_beta |
TIGR02341 |
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ... |
8-522 |
9.12e-12 |
|
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: 67.58 E-value: 9.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 8 SEDARSKMKAGVDKLANTVKTTIGPKGRNVVLEQ--SYGAPTITNDGVTIAKAIELEdhfeNMGAKLVAEVASKTNDIAG 85
Cdd:TIGR02341 12 AENARLSSFVGAIAIGDLVKSTLGPKGMDKILQSssSDASIMVTNDGATILKSIGVD----NPAAKVLVDMSKVQDDEVG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 86 DGTTTATVLTQAIVAEGLKNVTAGANPVGIRTGIEKATAAAVKKLHEMS-----HTVSTKAEIAQIASISASNeevgELI 160
Cdd:TIGR02341 88 DGTTSVTVLAAELLREAEKLINQKIHPQTIIAGYREATKAARDALLKSAvdngsDEVKFRQDLMNIARTTLSS----KIL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 161 AEAMDKVGNDGVITIEESKGiETTLDVVEGMQFDRGYMSqymvtdndkmEANLDNPYILitDKKISNIQdvlpvlQSVVE 240
Cdd:TIGR02341 164 SQHKDHFAQLAVDAVLRLKG-SGNLEAIQIIKKLGGSLA----------DSYLDEGFLL--DKKIGVNQ------PKRIE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 241 QGRALliiaddITGEALPTLVLNKMRGTFNV-----VAVKAPGFGDRRKAQLEDIAVLTGGTVITEDLGLNLKdvtiDQL 315
Cdd:TIGR02341 225 NAKIL------IANTGMDTDKVKIFGSRVRVdstakVAELEHAEKEKMKEKVEKILKHGINCFINRQLIYNYP----EQL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 316 GQASKVNVSKdnttivegSGDKNAVATRVDIIKQQIAETTSDFDREKL------------QERLAKL----AGGVAVINV 379
Cdd:TIGR02341 295 FADAGVMAIE--------HADFEGVERLALVTGGEIVSTFDHPELVKLgscdlieeimigEDKLLKFsgvkLGEACTIVL 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 380 GAATETELKERKYRIEDALNATRAAVEEG-FVSGGGTALVNAISAVT--ALSEVGDVQTGINTVIKALEAPVRQIVENAG 456
Cdd:TIGR02341 367 RGATQQILDEAERSLHDALCVLSQTVKESrTVLGGGCSEMLMSKAVTqeAQRTPGKEALAVEAFARALRQLPTIIADNAG 446
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 457 FEGSVIVNKLK----EQVEGFGYNAATNEWVDMIAAGIVDPTKVTRSALQNAASVSALLLTTEAVVAELP 522
Cdd:TIGR02341 447 FDSAELVAQLRaahyNGNTTMGLDMNEGTIADMRQLGITESYKVKRAVVSSAAEAAEVILRVDNIIKAAP 516
|
|
| TCP1_theta |
cd03341 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ... |
21-518 |
1.39e-11 |
|
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: 66.48 E-value: 1.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 21 KLANTVKTTIGPKGRNVVLEQSYGAPTITNDGVTIAKAIEledhFENMGAKLVAEvASKTNDI-AGDGTTTATVLTQAIV 99
Cdd:cd03341 19 ELSQITRTSYGPNGMNKMVINHLEKLFVTSDAATILRELE----VQHPAAKLLVM-ASQMQEEeIGDGTNLVVVLAGELL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 100 --AEGLknVTAGANPVGIRTGIEKATAAAVKKLHEMS-HTVSTKAEIAQIASI--------SASNEEV-GELIAEAM--- 164
Cdd:cd03341 94 ekAEEL--LRMGLHPSEIIEGYEKALKKALEILEELVvYKIEDLRNKEEVSKAlktaiaskQYGNEDFlSPLVAEACisv 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 165 --DKVGNDGVITIEESK----GIETTlDVVEGMQFDRgymsqymvtdndkmeanldNPYILITDKKISNIQdvlpVLQSV 238
Cdd:cd03341 172 lpENIGNFNVDNIRVVKilggSLEDS-KVVRGMVFKR-------------------EPEGSVKRVKKAKVA----VFSCP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 239 VEQGRALLIIADDITGEALPtlVLNKmrgtFNVVAVKAPGfgdrrKAQLEDIAVLTGGTVITedlglNLKDVTIDQLGQA 318
Cdd:cd03341 228 FDIGVNVIVAGGSVGDLALH--YCNK----YGIMVIKINS-----KFELRRLCRTVGATPLP-----RLGAPTPEEIGYC 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 319 SKVNVSK---DNTTIVEGSGDKNAVATrvdiikqqiaettsdfdreklqerlaklaggvavINVGAATETELKERKYRIE 395
Cdd:cd03341 292 DSVYVEEigdTKVVVFRQNKEDSKIAT----------------------------------IVLRGATQNILDDVERAID 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 396 DALNATRAAVEEG-FVSGGGTAlvnAISAVTALSEVGDVQTGINT-VIK----ALEAPVRQIVENAGFEGSVIVNKL--- 466
Cdd:cd03341 338 DGVNVFKSLTKDGrFVPGAGAT---EIELAKKLKEYGEKTPGLEQyAIKkfaeAFEVVPRTLAENAGLDATEVLSELyaa 414
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 2538675531 467 ---KEQVEGFGYNAATNEWVDMIAAGIVDPTKVTRSALQNAASVSALLLTTEAVV 518
Cdd:cd03341 415 hqkGNKSAGVDIESGDEGTKDAKEAGIFDHLATKKWAIKLATEAAVTVLRVDQII 469
|
|
| chap_CCT_theta |
TIGR02346 |
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ... |
9-534 |
1.73e-11 |
|
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: 66.66 E-value: 1.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 9 EDARSKMKAGVDKLANTVKTTIGPKGRNVVLEQSYGAPTITNDGVTIAKAIELEdhfeNMGAKLVAEVASKTNDIAGDGT 88
Cdd:TIGR02346 17 EEAVIKNIEACKELSQITRTSLGPNGMNKMVINHLEKLFVTNDAATILRELEVQ----HPAAKLLVMASEMQENEIGDGT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 89 TTATVLTQAIVAEGLKNVTAGANPVGIRTGIEKATAAAVKKLHEMS----HTVSTKAEI-----AQIASISASNEEV-GE 158
Cdd:TIGR02346 93 NLVLVLAGELLNKAEELIRMGLHPSEIIKGYEMALKKAMEILEELVvwevKDLRDKDELikalkASISSKQYGNEDFlAQ 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 159 LIAEAM-----DKVGNDGVITIEESK----GIETTlDVVEGMQFDRGYMSQYMVTDNDKMeANLDNPY-ILITDKK---- 224
Cdd:TIGR02346 173 LVAQACstvlpKNPQNFNVDNIRVCKilggSLSNS-EVLKGMVFNREAEGSVKSVKNAKV-AVFSCPLdTATTETKgtvl 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 225 ISNIQDVLPVLQSVVEQGRALL-IIADD-----ITGEALPTLVLNKMRgTFNVVAVKAPGfgdrrKAQLEDIAVLTGGTV 298
Cdd:TIGR02346 251 IHNAEELLNYSKGEENQIEAMIkAIADSgvnviVTGGSVGDMALHYLN-KYNIMVLKIPS-----KFELRRLCKTVGATP 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 299 ItedlgLNLKDVTIDQLGQASKVNVSkdnttivEGSGDKnavatrVDIIKQQiaettsdfdreklqerlaKLAGGVAVIN 378
Cdd:TIGR02346 325 L-----PRLGAPTPEEIGYVDSVYVS-------EIGGDK------VTVFKQE------------------NGDSKISTII 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 379 VGAATETELKERKYRIEDALNATRAAVEEG-FVSGGGTALVNAISAVTALSE--VGDVQTGINTVIKALEAPVRQIVENA 455
Cdd:TIGR02346 369 LRGSTDNLLDDIERAIDDGVNTVKALVKDGrLLPGAGATEIELASRLTKYGEklPGLDQYAIKKFAEAFEIIPRTLAENA 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 456 GFEGSVIVNKL------KEQVEGFGYNAATNEWVDMIAAGIVDPTkvtrsalqnAASVSALLLTTEAVVAELPSDDAASA 529
Cdd:TIGR02346 449 GLNANEVIPKLyaahkkGNKSKGIDIEAESDGVKDASEAGIYDML---------ATKKWAIKLATEAAVTVLRVDQIIMA 519
|
....*
gi 2538675531 530 MPQGG 534
Cdd:TIGR02346 520 KPAGG 524
|
|
| TCP1_alpha |
cd03335 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ... |
9-157 |
8.20e-11 |
|
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: 64.23 E-value: 8.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 9 EDARSKMKAGVDKLANTVKTTIGPKGRNVVLEQSYGAPTITNDGVTIAKAIELEDHfenmGAKLVAEVASKTNDIAGDGT 88
Cdd:cd03335 7 QDVRTQNVTAAMAIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHP----AAKILVELAQLQDKEVGDGT 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2538675531 89 TTATVltqaIVAEGLKN----VTAGANPVGIRTGIEKATAAAVKKLHE-MSHTVST--KAEIAQIASISASNEEVG 157
Cdd:cd03335 83 TSVVI----IAAELLKRanelVKQKIHPTTIISGYRLACKEAVKYIKEhLSISVDNlgKESLINVAKTSMSSKIIG 154
|
|
| TCP1_zeta |
cd03342 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
22-515 |
2.25e-08 |
|
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: 56.50 E-value: 2.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 22 LANTVKTTIGPKGRNVVLEQSYGAPTITNDGVTIAKaielEDHFENMGAKLVAEVASKTNDIAGDGTTTATVLTQAIVAE 101
Cdd:cd03342 24 LQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLS----EMQIQHPTASMIARAATAQDDITGDGTTSNVLLIGELLKQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 102 GLKNVTAGANPVGIRTGIEKATAAAVKKLHEMSHTVSTKAEIAQIASI--SASNEEVGELIAEAMDKVGNDGVITIEESk 179
Cdd:cd03342 100 AERYIQEGVHPRIITEGFELAKNKALKFLESFKVPVEIDTDRELLLSVarTSLRTKLHADLADQLTEIVVDAVLAIYKP- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 180 GIETTLDVVEGMQFDRGYMSQY-----MVTD----NDKMEANLDNPYILITdkkisNIQdvLPVLQSVVEQGRALLIIAD 250
Cdd:cd03342 179 DEPIDLHMVEIMQMQHKSDSDTklirgLVLDhgarHPDMPKRVENAYILTC-----NVS--LEYEKTEVNSGFFYSVVIN 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 251 D--ITGEALPTLVLNkmrgtfNVVAVkapgfgdRR--KAQLEDIAVLTGGTVITedlglNLKDVTIDQLGQASKVNVSK- 325
Cdd:cd03342 252 QkgIDPPSLDMLAKE------GILAL-------RRakRRNMERLTLACGGVAMN-----SVDDLSPECLGYAGLVYERTl 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 326 --DNTTIVEGSGDKNAVATrvdIIKqqiaettsdfdreklqerlaklaggvavinvgAATETELKERKYRIEDALNATRA 403
Cdd:cd03342 314 geEKYTFIEGVKNPKSCTI---LIK--------------------------------GPNDHTITQIKDAIRDGLRAVKN 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 404 AVEEGFVSGGGTALvnAISAVTALSE-----VGDVQTGINTVIKALEAPVRQIVENAGFEG-SVIVNKLKEQVEG---FG 474
Cdd:cd03342 359 AIEDKCVVPGAGAF--EVALYAHLKEfkksvKGKAKLGVQAFADALLVIPKTLAENSGLDVqETLVKLQDEYAEGgqvGG 436
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 2538675531 475 YNAATNEWVDMIAAGIVDPTKVTRSALQNAASV-SALLLTTE 515
Cdd:cd03342 437 VDLDTGEPMDPESEGIWDNYSVKRQILHSATVIaSQLLLVDE 478
|
|
| chap_CCT_zeta |
TIGR02347 |
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ... |
22-133 |
5.36e-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: 52.43 E-value: 5.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 22 LANTVKTTIGPKGRNVVLEQSYGAPTITNDGVTIAKaielEDHFENMGAKLVAEVASKTNDIAGDGTTTATVLTQAIVAE 101
Cdd:TIGR02347 28 LQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLN----EMQIQHPTASMIARAATAQDDITGDGTTSTVLLIGELLKQ 103
|
90 100 110
....*....|....*....|....*....|..
gi 2538675531 102 GLKNVTAGANPVGIRTGIEKATAAAVKKLHEM 133
Cdd:TIGR02347 104 AERYILEGVHPRIITEGFEIARKEALQFLDKF 135
|
|
| chap_CCT_gamma |
TIGR02344 |
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ... |
22-519 |
7.62e-06 |
|
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT gamma chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.
Pssm-ID: 274085 [Multi-domain] Cd Length: 524 Bit Score: 48.58 E-value: 7.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 22 LANTVKTTIGPKGRNVVLEQSYGAPTITNDGVTIAKAIELedhfENMGAKLVAEVASKTNDIAGDGTTTATVLTQAIVAE 101
Cdd:TIGR02344 28 VADIIRTCLGPRSMLKMLLDPMGGIVMTNDGNAILREIDV----AHPAAKSMIELSRTQDEEVGDGTTSVIILAGEMLSV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 102 GLKNVTAGANPVGIRTGIEKATAAAVKKLHEMSHTVSTKAEIAQIASISAS---------NEEVGELIAEAMDKVGNDG- 171
Cdd:TIGR02344 104 AEPFLEQNIHPTVIIRAYRKALDDALSVLEEISIPVDVNDDAAMLKLIQSCigtkfvsrwSDLMCDLALDAVRTVQRDEn 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 172 ---------VITIEESKGIETTLDVVEgmqfdRGYMSQYMVTdNDKMEANLDNPYILITD-----KKISNIQDVlpvlqs 237
Cdd:TIGR02344 184 grkeidikrYAKVEKIPGGDIEDSCVL-----KGVMINKDVT-HPKMRRYIENPRIVLLDcpleyKKGESQTNI------ 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 238 vveqgralliiadDITGEALPTLVLnKMRGTFnvvavkapgfgdrRKAQLEDIAVLTGGTVITEDlglNLKDVTIDQLGQ 317
Cdd:TIGR02344 252 -------------EITKEEDWNRIL-QMEEEY-------------VQLMCEDIIAVKPDLVITEK---GVSDLAQHYLLK 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 318 AskvNVS-------KDNTTIVEGSGdKNAVATRVDIIKQQIAETTSDFDREKLQERL------AKLAGGVAVINVGAATE 384
Cdd:TIGR02344 302 A---NITairrvrkTDNNRIARACG-ATIVNRPEELRESDVGTGCGLFEVKKIGDEYftfiteCKDPKACTILLRGASKD 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 385 TeLKERKYRIEDALNATRAAVEEGFVSGGGTALVNAISAV---TALSEVGDVQTGINTVIKALEAPVRQIVENAGFEGSV 461
Cdd:TIGR02344 378 I-LNEVERNLQDAMAVARNVLLDPKLVPGGGATEMAVSVAlteKSKKLEGVEQWPYRAVADALEIIPRTLAQNCGANVIR 456
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2538675531 462 IVNKLK-----EQVEGFGYNAATNEWVDMIAAGIVDPTKVTRSALQNAASVSALLLTTEAVVA 519
Cdd:TIGR02344 457 TLTELRakhaqENNCTWGIDGETGKIVDMKEKGIWEPLAVKLQTYKTAIESACLLLRIDDIVS 519
|
|
| TCP1_gamma |
cd03337 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ... |
22-228 |
1.69e-05 |
|
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.
Pssm-ID: 239453 [Multi-domain] Cd Length: 480 Bit Score: 47.29 E-value: 1.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 22 LANTVKTTIGPKGRNVVLEQSYGAPTITNDGVTIAKAIELEdhfeNMGAKLVAEVASKTNDIAGDGTTTATVLTQAIVAE 101
Cdd:cd03337 28 VADVIRTCLGPRAMLKMLLDPMGGIVLTNDGNAILREIDVA----HPAAKSMIELSRTQDEEVGDGTTSVIILAGEILAV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538675531 102 GLKNVTAGANPVGIRTGIEKATAAAVKKLHEMSHTV--STKAEIAQIASISASNEEVGELiAEAMDKVGNDGVITIE-ES 178
Cdd:cd03337 104 AEPFLERGIHPTVIIKAYRKALEDALKILEEISIPVdvNDRAQMLKIIKSCIGTKFVSRW-SDLMCNLALDAVKTVAvEE 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2538675531 179 KGIETTLDVVEGMQFDR---GYMSQYMVTD---------NDKMEANLDNP----------YILITDKKISNI 228
Cdd:cd03337 183 NGRKKEIDIKRYAKVEKipgGEIEDSRVLDgvmlnkdvtHPKMRRRIENPrivlldcpleYLVITEKGVSDL 254
|
|
| |
