|
Name |
Accession |
Description |
Interval |
E-value |
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
1-528 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 862.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 1 MAKEIKFEADARSALAAGVNKLADAVKVTLGPKGRYVALEKSYGAPLITNDGVTVAKEVELEDPIENMGAQLVREVAVKT 80
Cdd:PRK00013 1 MAKDIKFGEDARRKLLRGVNKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDPFENMGAQLVKEVASKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 81 NDVAGDGTTTATLLADVIVSEGLRNVTAGADALGIRRGIQKATDAVVEAIKADATPVSTKEQIANVGTISA-GDAEIGEK 159
Cdd:PRK00013 81 NDVAGDGTTTATVLAQAIVREGLKNVAAGANPMDLKRGIDKAVEAAVEELKKISKPVEDKEEIAQVATISAnGDEEIGKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 160 IAEAMDAVGKDGAISVEESQTFGIDMDIVEGMQYERGYISPYMATDMEKMEAVLSDPYILLTDQKVTNIQDMVPLLEEIM 239
Cdd:PRK00013 161 IAEAMEKVGKEGVITVEESKGFETELEVVEGMQFDRGYLSPYFVTDPEKMEAELENPYILITDKKISNIQDLLPVLEQVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 240 KSGRPLFIVAEDVEGEALATILLNKLRGTFNCVAIKAPGFGDRRKRILEDIAAVTGAQVIDKDFGMTMADARIDMLGHAK 319
Cdd:PRK00013 241 QSGKPLLIIAEDVEGEALATLVVNKLRGTLKVVAVKAPGFGDRRKAMLEDIAILTGGTVISEELGLKLEDATLEDLGQAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 320 TVKVTKDSALIVDGAGDKKAIDDRIGQIKAELERVDSDFDREKLQERLAKLSGGVAVLKVGAATESELKEKKSRIEDALQ 399
Cdd:PRK00013 321 KVVVTKDNTTIVDGAGDKEAIKARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATEVEMKEKKDRVEDALH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 400 ATRAAVEEGIVAGGGVALVGALPALDKVEAADKDEEVGVAIIRKALEAPMRAIAQNAGFEGSVVVERVK-GMATGEGLNC 478
Cdd:PRK00013 401 ATRAAVEEGIVPGGGVALLRAAPALEALKGLNGDEATGINIVLRALEAPLRQIAENAGLEGSVVVEKVKnGKGKGYGYNA 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 496662690 479 ANGEYGNMIEMGVNDPVKVTRTALQSAASVAALILITEATINEIPKDPDP 528
Cdd:PRK00013 481 ATGEYVDMIEAGIIDPTKVTRSALQNAASVAGLLLTTEAVVADKPEKKAA 530
|
|
| GroEL |
cd03344 |
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ... |
3-521 |
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: 803.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 3 KEIKFEADARSALAAGVNKLADAVKVTLGPKGRYVALEKSYGAPLITNDGVTVAKEVELEDPIENMGAQLVREVAVKTND 82
Cdd:cd03344 1 KDIKFGEEARKALLRGVNKLADAVKVTLGPKGRNVVIEKSFGSPKITKDGVTVAKEIELEDPFENMGAQLVKEVASKTND 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 83 VAGDGTTTATLLADVIVSEGLRNVTAGADALGIRRGIQKATDAVVEAIKADATPVSTKEQIANVGTISA-GDAEIGEKIA 161
Cdd:cd03344 81 VAGDGTTTATVLARAIIKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKPVKTKEEIAQVATISAnGDEEIGELIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 162 EAMDAVGKDGAISVEESQTFGIDMDIVEGMQYERGYISPYMATDMEKMEAVLSDPYILLTDQKVTNIQDMVPLLEEIMKS 241
Cdd:cd03344 161 EAMEKVGKDGVITVEEGKTLETELEVVEGMQFDRGYLSPYFVTDPEKMEVELENPYILLTDKKISSIQELLPILELVAKA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 242 GRPLFIVAEDVEGEALATILLNKLRGTFNCVAIKAPGFGDRRKRILEDIAAVTGAQVIDKDFGMTMADARIDMLGHAKTV 321
Cdd:cd03344 241 GRPLLIIAEDVEGEALATLVVNKLRGGLKVCAVKAPGFGDRRKAMLEDIAILTGGTVISEELGLKLEDVTLEDLGRAKKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 322 KVTKDSALIVDGAGDKKAIDDRIGQIKAELERVDSDFDREKLQERLAKLSGGVAVLKVGAATESELKEKKSRIEDALQAT 401
Cdd:cd03344 321 VVTKDDTTIIGGAGDKAAIKARIAQIRKQIEETTSDYDKEKLQERLAKLSGGVAVIKVGGATEVELKEKKDRVEDALNAT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 402 RAAVEEGIVAGGGVALVGALPALDKVEAADKDEEVGVAIIRKALEAPMRAIAQNAGFEGSVVVERVKGMATGEGLNCANG 481
Cdd:cd03344 401 RAAVEEGIVPGGGVALLRASPALDKLKALNGDEKLGIEIVRRALEAPLRQIAENAGVDGSVVVEKVLESPDGFGYDAATG 480
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 496662690 482 EYGNMIEMGVNDPVKVTRTALQSAASVAALILITEATINE 521
Cdd:cd03344 481 EYVDMIEAGIIDPTKVVRSALQNAASVASLLLTTEALVVD 520
|
|
| groEL |
PRK12849 |
chaperonin GroEL; Reviewed |
1-528 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237230 Cd Length: 542 Bit Score: 799.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 1 MAKEIKFEADARSALAAGVNKLADAVKVTLGPKGRYVALEKSYGAPLITNDGVTVAKEVELEDPIENMGAQLVREVAVKT 80
Cdd:PRK12849 1 MAKIIKFDEEARRALERGVNKLADAVKVTLGPKGRNVVIDKSFGAPTITKDGVSIAKEIELEDPFENLGAQLVKEVASKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 81 NDVAGDGTTTATLLADVIVSEGLRNVTAGADALGIRRGIQKATDAVVEAIKADATPVSTKEQIANVGTISA-GDAEIGEK 159
Cdd:PRK12849 81 NDVAGDGTTTATVLAQALVQEGLKNVAAGANPMDLKRGIDKAVEAVVEELKALARPVSGSEEIAQVATISAnGDEEIGEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 160 IAEAMDAVGKDGAISVEESQTFGIDMDIVEGMQYERGYISPYMATDMEKMEAVLSDPYILLTDQKVTNIQDMVPLLEEIM 239
Cdd:PRK12849 161 IAEAMEKVGKDGVITVEESKTLETELEVTEGMQFDRGYLSPYFVTDPERMEAVLEDPLILLTDKKISSLQDLLPLLEKVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 240 KSGRPLFIVAEDVEGEALATILLNKLRGTFNCVAIKAPGFGDRRKRILEDIAAVTGAQVIDKDFGMTMADARIDMLGHAK 319
Cdd:PRK12849 241 QSGKPLLIIAEDVEGEALATLVVNKLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGLKLEEVTLDDLGRAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 320 TVKVTKDSALIVDGAGDKKAIDDRIGQIKAELERVDSDFDREKLQERLAKLSGGVAVLKVGAATESELKEKKSRIEDALQ 399
Cdd:PRK12849 321 RVTITKDNTTIVDGAGDKEAIEARVAQIRRQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATEVELKERKDRVEDALN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 400 ATRAAVEEGIVAGGGVALVGALPALDKVEAADKDEEVGVAIIRKALEAPMRAIAQNAGFEGSVVVERVKGMATGEGLNCA 479
Cdd:PRK12849 401 ATRAAVEEGIVPGGGVALLRAAKALDELAGLNGDQAAGVEIVRRALEAPLRQIAENAGLDGSVVVAKVLELEDGFGFNAA 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 496662690 480 NGEYGNMIEMGVNDPVKVTRTALQSAASVAALILITEATINEIPKDPDP 528
Cdd:PRK12849 481 TGEYGDLIAAGIIDPVKVTRSALQNAASVAGLLLTTEALVADKPEEEDP 529
|
|
| GroEL |
TIGR02348 |
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ... |
2-524 |
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: 755.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 2 AKEIKFEADARSALAAGVNKLADAVKVTLGPKGRYVALEKSYGAPLITNDGVTVAKEVELEDPIENMGAQLVREVAVKTN 81
Cdd:TIGR02348 1 AKQIKFDEEARKALLRGVDKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDKFENMGAQLVKEVASKTN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 82 DVAGDGTTTATLLADVIVSEGLRNVTAGADALGIRRGIQKATDAVVEAIKADATPVSTKEQIANVGTISAG-DAEIGEKI 160
Cdd:TIGR02348 81 DVAGDGTTTATVLAQAIVKEGLKNVAAGANPIELKRGIEKAVEAVVEELKKLSKPVKGKKEIAQVATISANnDEEIGSLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 161 AEAMDAVGKDGAISVEESQTFGIDMDIVEGMQYERGYISPYMATDMEKMEAVLSDPYILLTDQKVTNIQDMVPLLEEIMK 240
Cdd:TIGR02348 161 AEAMEKVGKDGVITVEESKSLETELEVVEGMQFDRGYISPYFVTDAEKMEVELENPYILITDKKISNIKDLLPLLEKVAQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 241 SGRPLFIVAEDVEGEALATILLNKLRGTFNCVAIKAPGFGDRRKRILEDIAAVTGAQVIDKDFGMTMADARIDMLGHAKT 320
Cdd:TIGR02348 241 SGKPLLIIAEDVEGEALATLVVNKLRGTLNVCAVKAPGFGDRRKAMLEDIAILTGGQVISEELGLKLEEVTLDDLGKAKK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 321 VKVTKDSALIVDGAGDKKAIDDRIGQIKAELERVDSDFDREKLQERLAKLSGGVAVLKVGAATESELKEKKSRIEDALQA 400
Cdd:TIGR02348 321 VTVDKDNTTIVEGAGDKAAIKARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATETEMKEKKLRIEDALNA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 401 TRAAVEEGIVAGGGVALVGALPALDKVEAADKDEEVGVAIIRKALEAPMRAIAQNAGFEGSVVVERVKGMATGEGLNCAN 480
Cdd:TIGR02348 401 TRAAVEEGIVPGGGVALLRAAAALEGLKGDGEDEAIGIDIVKRALEAPLRQIAENAGLDGAVVAEKVKELKGNFGFNAAT 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 496662690 481 GEYGNMIEMGVNDPVKVTRTALQSAASVAALILITEATINEIPK 524
Cdd:TIGR02348 481 GEYEDLVEAGIIDPTKVTRSALQNAASIAGLLLTTEAVVADKPE 524
|
|
| groEL |
PRK12850 |
chaperonin GroEL; Reviewed |
1-528 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237231 Cd Length: 544 Bit Score: 742.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 1 MAKEIKFEADARSALAAGVNKLADAVKVTLGPKGRYVALEKSYGAPLITNDGVTVAKEVELEDPIENMGAQLVREVAVKT 80
Cdd:PRK12850 2 AAKEIRFSTDARDRLLRGVNILANAVKVTLGPKGRNVVLEKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVKEVASKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 81 NDVAGDGTTTATLLADVIVSEGLRNVTAGADALGIRRGIQKATDAVVEAIKADATPVSTKEQIANVGTISA-GDAEIGEK 159
Cdd:PRK12850 82 NDLAGDGTTTATVLAQAIVREGAKLVAAGMNPMDLKRGIDLAVAAVVDELKKIAKKVTSSKEIAQVATISAnGDESIGEM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 160 IAEAMDAVGKDGAISVEESQTFGIDMDIVEGMQYERGYISPYMATDMEKMEAVLSDPYILLTDQKVTNIQDMVPLLEEIM 239
Cdd:PRK12850 162 IAEAMDKVGKEGVITVEEAKTLGTELDVVEGMQFDRGYLSPYFVTNPEKMRAELEDPYILLHEKKISNLQDLLPILEAVV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 240 KSGRPLFIVAEDVEGEALATILLNKLRGTFNCVAIKAPGFGDRRKRILEDIAAVTGAQVIDKDFGMTMADARIDMLGHAK 319
Cdd:PRK12850 242 QSGRPLLIIAEDVEGEALATLVVNKLRGGLKSVAVKAPGFGDRRKAMLEDIAVLTGGQVISEDLGIKLENVTLDMLGRAK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 320 TVKVTKDSALIVDGAGDKKAIDDRIGQIKAELERVDSDFDREKLQERLAKLSGGVAVLKVGAATESELKEKKSRIEDALQ 399
Cdd:PRK12850 322 RVLITKENTTIIDGAGDKKNIEARVKQIRAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKEKKDRVDDALH 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 400 ATRAAVEEGIVAGGGVALVGALPALDKVEAADKDEEVGVAIIRKALEAPMRAIAQNAGFEGSVVVERVKGMATGEGLNCA 479
Cdd:PRK12850 402 ATRAAVEEGIVPGGGVALLRARSALRGLKGANADETAGIDIVRRALEEPLRQIATNAGFEGSVVVGKVAELPGNFGFNAQ 481
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 496662690 480 NGEYGNMIEMGVNDPVKVTRTALQSAASVAALILITEATINEIPKDPDP 528
Cdd:PRK12850 482 TGEYGDMVEAGIIDPAKVTRTALQDAASIAALLITTEAMVAEAPKKAAA 530
|
|
| groEL |
PRK12851 |
chaperonin GroEL; Reviewed |
1-524 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 171770 Cd Length: 541 Bit Score: 699.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 1 MAKEIKFEADARSALAAGVNKLADAVKVTLGPKGRYVALEKSYGAPLITNDGVTVAKEVELEDPIENMGAQLVREVAVKT 80
Cdd:PRK12851 2 AAKEVKFHVEAREKMLRGVNILADAVKVTLGPKGRNVVIDKSFGAPTITNDGVTIAKEIELEDKFENMGAQMVREVASKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 81 NDVAGDGTTTATLLADVIVSEGLRNVTAGADALGIRRGIQKATDAVVEAIKADATPVSTKEQIANVGTISA-GDAEIGEK 159
Cdd:PRK12851 82 NDVAGDGTTTATVLAQAIVREGAKAVAAGANPMDLKRGIDRAVAAVVEELKANARPVTTNAEIAQVATISAnGDAEIGRL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 160 IAEAMDAVGKDGAISVEESQTFGIDMDIVEGMQYERGYISPYMATDMEKMEAVLSDPYILLTDQKVTNIQDMVPLLEEIM 239
Cdd:PRK12851 162 VAEAMEKVGNEGVITVEESKTAETELEVVEGMQFDRGYLSPYFVTDADKMEAELEDPYILIHEKKISNLQDLLPVLEAVV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 240 KSGRPLFIVAEDVEGEALATILLNKLRGTFNCVAIKAPGFGDRRKRILEDIAAVTGAQVIDKDFGMTMADARIDMLGHAK 319
Cdd:PRK12851 242 QSGKPLLIIAEDVEGEALATLVVNKLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGIKLENVTLEQLGRAK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 320 TVKVTKDSALIVDGAGDKKAIDDRIGQIKAELERVDSDFDREKLQERLAKLSGGVAVLKVGAATESELKEKKSRIEDALQ 399
Cdd:PRK12851 322 KVVVEKENTTIIDGAGSKTEIEGRVAQIRAQIEETTSDYDREKLQERLAKLAGGVAVIRVGASTEVEVKEKKDRVDDALH 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 400 ATRAAVEEGIVAGGGVALVGALPALDKVEAADKDEEVGVAIIRKALEAPMRAIAQNAGFEGSVVVERVKGMATGEGLNCA 479
Cdd:PRK12851 402 ATRAAVEEGIVPGGGVALLRAVKALDKLETANGDQRTGVEIVRRALEAPVRQIAENAGAEGSVVVGKLREKPGGYGFNAA 481
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 496662690 480 NGEYGNMIEMGVNDPVKVTRTALQSAASVAALILITEATINEIPK 524
Cdd:PRK12851 482 TNEYGDLYAQGVIDPVKVVRTALQNAASVAGLLLTTEAMVAEKPK 526
|
|
| GroEL |
COG0459 |
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ... |
1-528 |
0e+00 |
|
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227 Cd Length: 497 Bit Score: 699.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 1 MAKEIKFEADARSALAAGVNKLADAVKVTLGPKGRYVALEKSYGAPLITNDGVTVAKEVELEDPIENMGAQLVREVAVKT 80
Cdd:COG0459 1 MAKQILFGEDARRANIRGVKALADAVKVTLGPKGRNVMLVKSFGDPTITNDGVTIAKEIELEDPFENMGAQLVKEVASKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 81 NDVAGDGTTTATLLADVIVSEGLRNVTAGADALGIRRGIQKATDAVVEAIKADATPVSTKEQIANVGTISA-GDAEIGEK 159
Cdd:COG0459 81 NDEAGDGTTTATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPVDDKEELAQVATISAnGDEEIGEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 160 IAEAMDAVGKDGAISVEESQTFGIDMDIVEGMQYERGYISPYMATDMEKMEAVLSDPYILLTDQKVTNIQDMVPLLEEIM 239
Cdd:COG0459 161 IAEAMEKVGKDGVITVEEGKGLETELEVVEGMQFDKGYLSPYFVTDPEKMPAELENAYILLTDKKISSIQDLLPLLEKVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 240 KSGRPLFIVAEDVEGEALATILLNKLRGTFNCVAIKAPGFGDRRKRILEDIAAVTGAQVIDKDFGMTMADARIDMLGHAK 319
Cdd:COG0459 241 QSGKPLLIIAEDIDGEALATLVVNGIRGVLRVVAVKAPGFGDRRKAMLEDIAILTGGRVISEDLGLKLEDVTLDDLGRAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 320 TVKVTKDSALIVDGAGDKKAIddrigqikaelervdsdfdreklqerlaklsggvaVLKVGAATESELKEKKSRIEDALQ 399
Cdd:COG0459 321 RVEVDKDNTTIVEGAGNPKAI-----------------------------------VILVGAATEVEVKERKRRVEDALH 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 400 ATRAAVEEGIVAGGGVALVGALPALDKVEA-ADKDEEVGVAIIRKALEAPMRAIAQNAGFEGSVVVERVKGMA-TGEGLN 477
Cdd:COG0459 366 ATRAAVEEGIVPGGGAALLRAARALRELAAkLEGDEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKVRAAKdKGFGFD 445
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 496662690 478 CANGEYGNMIEMGVNDPVKVTRTALQSAASVAALILITEATINEIPKDPDP 528
Cdd:COG0459 446 AATGEYVDMLEAGVIDPAKVKRSALQNAASVAGLILTTEAVIADKPEKEEA 496
|
|
| PTZ00114 |
PTZ00114 |
Heat shock protein 60; Provisional |
2-528 |
0e+00 |
|
Heat shock protein 60; Provisional
Pssm-ID: 185455 Cd Length: 555 Bit Score: 661.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 2 AKEIKFEADARSALAAGVNKLADAVKVTLGPKGRYVALEKSYGAPLITNDGVTVAKEVELEDPIENMGAQLVREVAVKTN 81
Cdd:PTZ00114 14 GKEIRFGDEARQSLLKGIERLADAVAVTLGPKGRNVIIEQEYGSPKITKDGVTVAKAIEFSDRFENVGAQLIRQVASKTN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 82 DVAGDGTTTATLLADVIVSEGLRNVTAGADALGIRRGIQKATDAVVEAIKADATPVSTKEQIANVGTISA-GDAEIGEKI 160
Cdd:PTZ00114 94 DKAGDGTTTATILARAIFREGCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQSRPVKTKEDILNVATISAnGDVEIGSLI 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 161 AEAMDAVGKDGAISVEESQTFGIDMDIVEGMQYERGYISPYMATDMEKMEAVLSDPYILLTDQKVTNIQDMVPLLEEIMK 240
Cdd:PTZ00114 174 ADAMDKVGKDGTITVEDGKTLEDELEVVEGMSFDRGYISPYFVTNEKTQKVELENPLILVTDKKISSIQSILPILEHAVK 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 241 SGRPLFIVAEDVEGEALATILLNKLRGTFNCVAIKAPGFGDRRKRILEDIAAVTGAQVIDKDF-GMTMADARIDMLGHAK 319
Cdd:PTZ00114 254 NKRPLLIIAEDVEGEALQTLIINKLRGGLKVCAVKAPGFGDNRKDILQDIAVLTGATVVSEDNvGLKLDDFDPSMLGSAK 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 320 TVKVTKDSALIVDGAGDKKAIDDRIGQIKAELERVDSDFDREKLQERLAKLSGGVAVLKVGAATESELKEKKSRIEDALQ 399
Cdd:PTZ00114 334 KVTVTKDETVILTGGGDKAEIKERVELLRSQIERTTSEYDKEKLKERLAKLSGGVAVIKVGGASEVEVNEKKDRIEDALN 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 400 ATRAAVEEGIVAGGGVALVGALPALDKVEA---ADKDEEVGVAIIRKALEAPMRAIAQNAGFEGSVVVERVKGMATGE-G 475
Cdd:PTZ00114 414 ATRAAVEEGIVPGGGVALLRASKLLDKLEEdneLTPDQRTGVKIVRNALRLPTKQIAENAGVEGAVVVEKILEKKDPSfG 493
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 496662690 476 LNCANGEYGNMIEMGVNDPVKVTRTALQSAASVAALILITEATINEIPKDPDP 528
Cdd:PTZ00114 494 YDAQTGEYVNMFEAGIIDPTKVVRSALVDAASVASLMLTTEAAIVDLPKEKKK 546
|
|
| groEL |
PRK12852 |
chaperonin GroEL; Reviewed |
1-528 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237232 Cd Length: 545 Bit Score: 638.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 1 MAKEIKFEADARSALAAGVNKLADAVKVTLGPKGRYVALEKSYGAPLITNDGVTVAKEVELEDPIENMGAQLVREVAVKT 80
Cdd:PRK12852 2 AAKDVKFSGDARDRMLRGVDILANAVKVTLGPKGRNVVIEKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVREVASKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 81 NDVAGDGTTTATLLADVIVSEGLRNVTAGADALGIRRGIQKATDAVVEAIKADATPVSTKEQIANVGTISA-GDAEIGEK 159
Cdd:PRK12852 82 NDLAGDGTTTATVLAQAIVREGAKAVAAGMNPMDLKRGIDIAVAAVVKDIEKRAKPVASSAEIAQVGTISAnGDAAIGKM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 160 IAEAMDAVGKDGAISVEESQTFGIDMDIVEGMQYERGYISPYMATDMEKMEAVLSDPYILLTDQKVTNIQDMVPLLEEIM 239
Cdd:PRK12852 162 IAQAMQKVGNEGVITVEENKSLETEVDIVEGMKFDRGYLSPYFVTNAEKMTVELDDAYILLHEKKLSGLQAMLPVLEAVV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 240 KSGRPLFIVAEDVEGEALATILLNKLRGTFNCVAIKAPGFGDRRKRILEDIAAVTGAQVIDKDFGMTMADARIDMLGHAK 319
Cdd:PRK12852 242 QSGKPLLIIAEDVEGEALATLVVNRLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGQLISEDLGIKLENVTLKMLGRAK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 320 TVKVTKDSALIVDGAGDKKAIDDRIGQIKAELERVDSDFDREKLQERLAKLSGGVAVLKVGAATESELKEKKSRIEDALQ 399
Cdd:PRK12852 322 KVVIDKENTTIVNGAGKKADIEARVGQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKEKKDRVEDALN 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 400 ATRAAVEEGIVAGGGVALVGALPALDKVEAADKDEEVGVAIIRKALEAPMRAIAQNAGFEGSVVVERV-KGMATGEGLNC 478
Cdd:PRK12852 402 ATRAAVQEGIVPGGGVALLRAKKAVGRINNDNADVQAGINIVLKALEAPIRQIAENAGVEGSIVVGKIlENKSETFGFDA 481
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 496662690 479 ANGEYGNMIEMGVNDPVKVTRTALQSAASVAALILITEATINEIPKDPDP 528
Cdd:PRK12852 482 QTEEYVDMVAKGIIDPAKVVRTALQDAASVAGLLVTTEAMVAELPKKDAA 531
|
|
| groEL |
CHL00093 |
chaperonin GroEL |
1-519 |
0e+00 |
|
chaperonin GroEL
Pssm-ID: 177025 Cd Length: 529 Bit Score: 629.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 1 MAKEIKFEADARSALAAGVNKLADAVKVTLGPKGRYVALEKSYGAPLITNDGVTVAKEVELEDPIENMGAQLVREVAVKT 80
Cdd:CHL00093 1 MSKKILYQDNARRALERGMDILAEAVSVTLGPKGRNVVLEKKYGSPQIVNDGVTIAKEIELEDHIENTGVALIRQAASKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 81 NDVAGDGTTTATLLADVIVSEGLRNVTAGADALGIRRGIQKATDAVVEAIKADATPVSTKEQIANVGTISAG-DAEIGEK 159
Cdd:CHL00093 81 NDVAGDGTTTATVLAYAIVKQGMKNVAAGANPISLKRGIEKATQYVVSQIAEYARPVEDIQAITQVASISAGnDEEVGSM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 160 IAEAMDAVGKDGAISVEESQTFGIDMDIVEGMQYERGYISPYMATDMEKMEAVLSDPYILLTDQKVTNI-QDMVPLLEEI 238
Cdd:CHL00093 161 IADAIEKVGREGVISLEEGKSTVTELEITEGMRFEKGFISPYFVTDTERMEVVQENPYILLTDKKITLVqQDLLPILEQV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 239 MKSGRPLFIVAEDVEGEALATILLNKLRGTFNCVAIKAPGFGDRRKRILEDIAAVTGAQVIDKDFGMTMADARIDMLGHA 318
Cdd:CHL00093 241 TKTKRPLLIIAEDVEKEALATLVLNKLRGIVNVVAVRAPGFGDRRKAMLEDIAILTGGQVITEDAGLSLETIQLDLLGQA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 319 KTVKVTKDSALIVdGAGDKKAIDDRIGQIKAELERVDSDFDREKLQERLAKLSGGVAVLKVGAATESELKEKKSRIEDAL 398
Cdd:CHL00093 321 RRIIVTKDSTTII-ADGNEEQVKARCEQLRKQIEIADSSYEKEKLQERLAKLSGGVAVIKVGAATETEMKDKKLRLEDAI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 399 QATRAAVEEGIVAGGGVALVG-ALPALDKVEAADKDEE-VGVAIIRKALEAPMRAIAQNAGFEGSVVVERVKGMATGEGL 476
Cdd:CHL00093 400 NATKAAVEEGIVPGGGATLVHlSENLKTWAKNNLKEDElIGALIVARAILAPLKRIAENAGKNGSVIIEKVQEQDFEIGY 479
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 496662690 477 NCANGEYGNMIEMGVNDPVKVTRTALQSAASVAALILITEATI 519
Cdd:CHL00093 480 NAANNKFVNMYEAGIIDPAKVTRSALQNAASIASMILTTECII 522
|
|
| PRK14104 |
PRK14104 |
chaperonin GroEL; Provisional |
2-524 |
0e+00 |
|
chaperonin GroEL; Provisional
Pssm-ID: 172594 Cd Length: 546 Bit Score: 544.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 2 AKEIKFEADARSALAAGVNKLADAVKVTLGPKGRYVALEKSYGAPLITNDGVTVAKEVELEDPIENMGAQLVREVAVKTN 81
Cdd:PRK14104 3 AKEVKFGVDARDRMLRGVDILANAVKVTLGPKGRNVVLDKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVREVASKSA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 82 DVAGDGTTTATLLADVIVSEGLRNVTAGADALGIRRGIQKATDAVVEAIKADATPVSTKEQIANVGTISA-GDAEIGEKI 160
Cdd:PRK14104 83 DAAGDGTTTATVLAQAIVREGAKSVAAGMNPMDLKRGIDLAVEAVVADLVKNSKKVTSNDEIAQVGTISAnGDAEIGKFL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 161 AEAMDAVGKDGAISVEESQTFGIDMDIVEGMQYERGYISPYMATDMEKMEAVLSDPYILLTDQKVTNIQDMVPLLEEIMK 240
Cdd:PRK14104 163 ADAMKKVGNEGVITVEEAKSLETELDVVEGMQFDRGYISPYFVTNADKMRVEMDDAYILINEKKLSSLNELLPLLEAVVQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 241 SGRPLFIVAEDVEGEALATILLNKLRGTFNCVAIKAPGFGDRRKRILEDIAAVTGAQVIDKDFGMTMADARIDMLGHAKT 320
Cdd:PRK14104 243 TGKPLVIVAEDVEGEALATLVVNRLRGGLKVAAVKAPGFGDRRKAMLQDIAILTGGQAISEDLGIKLENVTLQMLGRAKK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 321 VKVTKDSALIVDGAGDKKAIDDRIGQIKAELERVDSDFDREKLQERLAKLSGGVAVLKVGAATESELKEKKSRIEDALQA 400
Cdd:PRK14104 323 VMIDKENTTIVNGAGKKADIEARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKERKDRVDDAMHA 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 401 TRAAVEEGIVAGGGVALVGALPALDKVEAADKDEEVGVAIIRKALEAPMRAIAQNAGFEGSVVVERV-KGMATGEGLNCA 479
Cdd:PRK14104 403 TRAAVEEGIVPGGGVALLRASEQLKGIKTKNDDQKTGVEIVRKALSAPARQIAINAGEDGSVIVGKIlEKEQYSYGFDSQ 482
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 496662690 480 NGEYGNMIEMGVNDPVKVTRTALQSAASVAALILITEATINEIPK 524
Cdd:PRK14104 483 TGEYGNLVSKGIIDPTKVVRTAIQNAASVAALLITTEAMVAELPK 527
|
|
| PLN03167 |
PLN03167 |
Chaperonin-60 beta subunit; Provisional |
2-528 |
3.53e-169 |
|
Chaperonin-60 beta subunit; Provisional
Pssm-ID: 215611 [Multi-domain] Cd Length: 600 Bit Score: 492.13 E-value: 3.53e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 2 AKEIKFEAD--ARSALAAGVNKLADAVKVTLGPKGRYVALEKSYGAPLITNDGVTVAKEVELEDPIENMGAQLVREVAVK 79
Cdd:PLN03167 56 AKELHFNKDgsAIKKLQAGVNKLADLVGVTLGPKGRNVVLESKYGSPKIVNDGVTVAKEVELEDPVENIGAKLVRQAAAK 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 80 TNDVAGDGTTTATLLADVIVSEGLRNVTAGADALGIRRGIQKATDAVVEAIKADATPVSTKEqIANVGTISAGDA-EIGE 158
Cdd:PLN03167 136 TNDLAGDGTTTSVVLAQGLIAEGVKVVAAGANPVQITRGIEKTAKALVKELKKMSKEVEDSE-LADVAAVSAGNNyEVGN 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 159 KIAEAMDAVGKDGAISVEESQTFGIDMDIVEGMQYERGYISPYMATDMEKMEAVLSDPYILLTDQKVTNIQDMVPLLEEI 238
Cdd:PLN03167 215 MIAEAMSKVGRKGVVTLEEGKSAENNLYVVEGMQFDRGYISPYFVTDSEKMSVEYDNCKLLLVDKKITNARDLIGILEDA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 239 MKSGRPLFIVAEDVEGEALATILLNKLRGTFNCVAIKAPGFGDRRKRILEDIAAVTGAQVIDKDFGMTMADARIDMLGHA 318
Cdd:PLN03167 295 IRGGYPLLIIAEDIEQEALATLVVNKLRGSLKIAALKAPGFGERKSQYLDDIAILTGGTVIREEVGLSLDKVGKEVLGTA 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 319 KTVKVTKDSALIVDGAGDKKAIDDRIGQIKAELERVDSDFDREKLQERLAKLSGGVAVLKVGAATESELKEKKSRIEDAL 398
Cdd:PLN03167 375 AKVVLTKDTTTIVGDGSTQEAVNKRVAQIKNLIEAAEQDYEKEKLNERIAKLSGGVAVIQVGAQTETELKEKKLRVEDAL 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 399 QATRAAVEEGIVAGGGVALVGALPALDKV-EAADKDEE-VGVAIIRKALEAPMRAIAQNAGFEGSVVVERVKGMATGE-G 475
Cdd:PLN03167 455 NATKAAVEEGIVVGGGCTLLRLASKVDAIkDTLENDEQkVGADIVKRALSYPLKLIAKNAGVNGSVVSEKVLSNDNPKfG 534
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 496662690 476 LNCANGEYGNMIEMGVNDPVKVTRTALQSAASVAALILITEATINEIpKDPDP 528
Cdd:PLN03167 535 YNAATGKYEDLMAAGIIDPTKVVRCCLEHAASVAKTFLTSDCVVVEI-KEPEP 586
|
|
| chaperonin_type_I_II |
cd00309 |
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ... |
3-519 |
4.14e-128 |
|
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: 382.16 E-value: 4.14e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 3 KEIKFEADARSALAAGVNKLADAVKVTLGPKGRYVALEKSYGAPLITNDGVTVAKEVEledpIENMGAQLVREVAVKTND 82
Cdd:cd00309 1 KEREFGEEARLSNINAAKALADAVKTTLGPKGMDKMLVDSLGDPTITNDGATILKEIE----VEHPAAKLLVEVAKSQDD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 83 VAGDGTTTATLLADVIVSEGLRNVTAGADALGIRRGIQKATDAVVEAIKADATP--VSTKEQIANVGTISAG-------D 153
Cdd:cd00309 77 EVGDGTTTVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVPidVEDREELLKVATTSLNsklvsggD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 154 AEIGEKIAEAMDAVGK------DGAISVEESQTfGIDMD--IVEGMQYERGYISPYmatdmekMEAVLSDPYILLTDQKV 225
Cdd:cd00309 157 DFLGELVVDAVLKVGKengdvdLGVIRVEKKKG-GSLEDseLVVGMVFDKGYLSPY-------MPKRLENAKILLLDCKL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 226 TNIqdmvplleeimksgrplfIVAED-VEGEALATilLNKLrgtfNCVAIKApgfgdRRKRILEDIAAVTGAQVIdkdfg 304
Cdd:cd00309 229 EYV------------------VIAEKgIDDEALHY--LAKL----GIMAVRR-----VRKEDLERIAKATGATIV----- 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 305 MTMADARIDMLGHAKTVKVTK----DSALIVDGAGdkkaiddrigqikaelervdsdfdreklqerlaklsGGVAVLKVG 380
Cdd:cd00309 275 SRLEDLTPEDLGTAGLVEETKigdeKYTFIEGCKG------------------------------------GKVATILLR 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 381 AATESELKEKKSRIEDALQATRAAVEE-GIVAGGGVALVGALPALDKVEAADK-DEEVGVAIIRKALEAPMRAIAQNAGF 458
Cdd:cd00309 319 GATEVELDEAERSLHDALCAVRAAVEDgGIVPGGGAAEIELSKALEELAKTLPgKEQLGIEAFADALEVIPRTLAENAGL 398
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496662690 459 EGSVVVERVKGMATGE----GLNCANGEYGNMIEMGVNDPVKVTRTALQSAASVAALILITEATI 519
Cdd:cd00309 399 DPIEVVTKLRAKHAEGggnaGGDVETGEIVDMKEAGIIDPLKVKRQALKSATEAASLILTIDDII 463
|
|
| Cpn60_TCP1 |
pfam00118 |
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ... |
22-519 |
4.43e-73 |
|
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: 240.95 E-value: 4.43e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 22 LADAVKVTLGPKGRYVALEKSYGAPLITNDGVTVAKEVELEDPIenmgAQLVREVAVKTNDVAGDGTTTATLLADVIVSE 101
Cdd:pfam00118 1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELEIQHPA----AKLLVEAAKAQDEEVGDGTTTVVVLAGELLEE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 102 GLRNVTAGADALGIRRGIQKATDAVVEAIKA-DATPVS--TKEQIANVGTISAG------DAE-IGEKIAEAMDA----- 166
Cdd:pfam00118 77 AEKLLAAGVHPTTIIEGYEKALEKALEILDSiISIPVEdvDREDLLKVARTSLSskiisrESDfLAKLVVDAVLAipknd 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 167 ----VGKDGAISVEESQtfGIDMDIVEGMQYERGYISPYMATDMEkmeavlsDPYILLTDQKVTNIQD------------ 230
Cdd:pfam00118 157 gsfdLGNIGVVKILGGS--LEDSELVDGVVLDKGPLHPDMPKRLE-------NAKVLLLNCSLEYEKTetkatvvlsdae 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 231 ------------MVPLLEEIMKSGRPLFIVAEDVEGEALATILLNKLRGTFNCvaikapgfgdrRKRILEDIAAVTGAQV 298
Cdd:pfam00118 228 qlerflkaeeeqILEIVEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMALRRV-----------KKRDLERLAKATGARA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 299 IDKDFGMTMADaridmLGHAKTVKVTKDSalivdgagdkkaiDDRIGQIKaelervdsdfdreklqerlAKLSGGVAVLK 378
Cdd:pfam00118 297 VSSLDDLTPDD-----LGTAGKVEEEKIG-------------DEKYTFIE-------------------GCKSPKAATIL 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 379 VGAATESELKEKKSRIEDALQATRAAVEE-GIVAGGGVALVGALPALDKVEAADKDEE-VGVAIIRKALEAPMRAIAQNA 456
Cdd:pfam00118 340 LRGATDHVLDEIERSIHDALCVVKNAIEDpRVVPGGGAVEMELARALREYAKSVSGKEqLAIEAFAEALEVIPKTLAENA 419
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496662690 457 GFEGSVVVERVKGM-ATGE---GLNCANGEYGNMIEMGVNDPVKVTRTALQSAASVAALILITEATI 519
Cdd:pfam00118 420 GLDPIEVLAELRAAhASGEkhaGIDVETGEIIDMKEAGVVDPLKVKRQALKSATEAASTILRIDDII 486
|
|
| chaperonin_like |
cd03333 |
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ... |
140-407 |
2.24e-29 |
|
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: 114.87 E-value: 2.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 140 KEQIANVGTISAG------DAEIGEKIAEAMDAVGKD------GAISVEESQTfGIDMD--IVEGMQYERGYISPYMATD 205
Cdd:cd03333 1 RELLLQVATTSLNsklsswDDFLGKLVVDAVLKVGPDnrmddlGVIKVEKIPG-GSLEDseLVVGVVFDKGYASPYMPKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 206 MEkmeavlsDPYILLTDQKVTNIqdmvplleeimksgrplfIVAED-VEGEALATilLNKLrgtfNCVAIKApgfgdRRK 284
Cdd:cd03333 80 LE-------NAKILLLDCPLEYV------------------VIAEKgIDDLALHY--LAKA----GIMAVRR-----VKK 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 285 RILEDIAAVTGAQVIdkdfgMTMADARIDMLGHAKTVKVTKDSA----LIVDGAGdkkaiddrigqikaelervdsdfdr 360
Cdd:cd03333 124 EDLERIARATGATIV-----SSLEDLTPEDLGTAELVEETKIGEekltFIEGCKG------------------------- 173
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 496662690 361 eklqerlaklsGGVAVLKVGAATESELKEKKSRIEDALQATRAAVEE 407
Cdd:cd03333 174 -----------GKAATILLRGATEVELDEVKRSLHDALCAVRAAVEE 209
|
|
| thermosome_beta |
NF041083 |
thermosome subunit beta; |
22-513 |
2.75e-23 |
|
thermosome subunit beta;
Pssm-ID: 469010 Cd Length: 519 Bit Score: 103.11 E-value: 2.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 22 LADAVKVTLGPKGRYVALEKSYGAPLITNDGVTVAKEVELEDPienmGAQLVREVAVKTNDVAGDGTTTATLLADVIV-- 99
Cdd:NF041083 29 VAEAVRTTLGPKGMDKMLVDSLGDIVITNDGATILKEMDVQHP----AAKMLVEVAKTQDDEVGDGTTTAVVLAGELLkk 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 100 SEGL--RNVTAGADALGIRRGIQKATDAVVE-AIKADATPVSTKEQIANVGTISAGDAEIGEKIAE-AMDAVgkdGAISV 175
Cdd:NF041083 105 AEELldQNIHPTIIANGYRLAAEKAIEILDEiAEKVDPDDRETLKKIAETSLTSKGVEEARDYLAEiAVKAV---KQVAE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 176 EESQTFGIDMD----------------IVEGMQYERGYISPYM--------------ATDMEK----MEAVLSDPYIL-- 219
Cdd:NF041083 182 KRDGKYYVDLDniqiekkhggsiedtqLIYGIVIDKEVVHPGMpkrvenakialldaPLEVKKteidAEIRITDPDQLqk 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 220 LTDQKVTNIQDMVpllEEIMKSGRPLFIVA---EDVEGEALAtillnklrgtfncvaiKAPGFGDRR--KRILEDIAAVT 294
Cdd:NF041083 262 FLDQEEKMLKEMV---DKIKATGANVVFCQkgiDDLAQHYLA----------------KAGILAVRRvkKSDMEKLAKAT 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 295 GAQVIDKDFGMTMADaridmLGHAKTV---KVTKDSALIVDGAGDKKAiddrigqikaelervdsdfdreklqerlakls 371
Cdd:NF041083 323 GARIVTNIDDLTPED-----LGYAELVeerKVGDDKMVFVEGCKNPKA-------------------------------- 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 372 ggVAVLkVGAATESELKEKKSRIEDALQATRAAVEEG-IVAGGGVALVGAlpALDKVEAADK---DEEVGVAIIRKALEA 447
Cdd:NF041083 366 --VTIL-IRGGTEHVVDEAERALEDALSVVADAVEDGkIVAGGGAPEVEL--AKRLREYAATvggREQLAVEAFAEALEI 440
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 448 PMRAIAQNAGFEG-SVVVERVKGMATGE---GLNCANGEYGNMIEMGVNDPVKVTRTALQSAASVAALIL 513
Cdd:NF041083 441 IPRTLAENAGLDPiDILVKLRSAHEKGKkwaGINVFTGEVVDMWELGVIEPLRVKTQAIKSATEAATMIL 510
|
|
| cpn60 |
cd03343 |
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ... |
10-513 |
2.39e-21 |
|
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: 97.33 E-value: 2.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 10 DARSALAAGVNKLADAVKVTLGPKGRYVALEKSYGAPLITNDGVTVAKEVELEDPienmGAQLVREVAVKTNDVAGDGTT 89
Cdd:cd03343 15 DAQRMNIAAAKAVAEAVRTTLGPKGMDKMLVDSLGDVTITNDGATILKEMDIEHP----AAKMLVEVAKTQDEEVGDGTT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 90 TATLLADVIV--SEGL--RNVTAGADALGIRRGIQKATDAVVE-AIKADATPVSTKEQIANVGTISAGDAEIGEKIAE-A 163
Cdd:cd03343 91 TAVVLAGELLekAEDLldQNIHPTVIIEGYRLAAEKALELLDEiAIKVDPDDKDTLRKIAKTSLTGKGAEAAKDKLADlV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 164 MDAV-----GKDGA-------ISVEESQTFGI-DMDIVEGMQYERGYISPYMA--------------------------- 203
Cdd:cd03343 171 VDAVlqvaeKRDGKyvvdldnIKIEKKTGGSVdDTELIRGIVIDKEVVHPGMPkrvenakialldaplevkkteidakir 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 204 -TDMEKMEAVLsdpyilltDQKVTNIQDMVpllEEIMKSGRPLFIVAEDVEGeaLATILLNKlRGTFncvAIKapgfgdR 282
Cdd:cd03343 251 iTSPDQLQAFL--------EQEEAMLKEMV---DKIADTGANVVFCQKGIDD--LAQHYLAK-AGIL---AVR------R 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 283 RKRI-LEDIAAVTGAQVIDkdfgmTMADARIDMLGHAKTV---KVTKDSALIVDGAGDKKAiddrigqikaelervdsdf 358
Cdd:cd03343 308 VKKSdMEKLARATGAKIVT-----NIDDLTPEDLGEAELVeerKVGDDKMVFVEGCKNPKA------------------- 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 359 dreklqerlaklsggVAVLKVGaATESELKEKKSRIEDALQATRAAVEEG-IVAGGGVALVGAlpALDKVEAADK---DE 434
Cdd:cd03343 364 ---------------VTILLRG-GTEHVVDELERALEDALRVVADALEDGkVVAGGGAVEIEL--AKRLREYARSvggRE 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 435 EVGVAIIRKALEAPMRAIAQNAGFEG-SVVVERVKGMATGE---GLNCANGEYGNMIEMGVNDPVKVTRTALQSAASVAA 510
Cdd:cd03343 426 QLAVEAFADALEEIPRTLAENAGLDPiDTLVELRAAHEKGNknaGLDVYTGEVVDMLEKGVIEPLRVKKQAIKSATEAAT 505
|
...
gi 496662690 511 LIL 513
Cdd:cd03343 506 MIL 508
|
|
| chap_CCT_epsi |
TIGR02343 |
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ... |
10-513 |
1.56e-12 |
|
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: 69.83 E-value: 1.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 10 DARSALAAGVNKLADAVKVTLGPKGRYVALEKSYGAPLITNDGVTVAKEVELEDPIenmgAQLVREVAVKTNDVAGDGTT 89
Cdd:TIGR02343 27 EAKKSNIAAAKSVASILRTSLGPKGMDKMLISPDGDITVTNDGATILSQMDVDNQI----AKLMVELSKSQDDEIGDGTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 90 TATLLADVIVSEGLRNVTAGADALGIRRGIQKATDAVVEAIKADATPVSTKEQIANVgTISAGDAEIGEKIA----EAMD 165
Cdd:TIGR02343 103 GVVVLAGALLEQAEELLDKGIHPIKIADGFEEAARIAVEHLEEISDEISADNNNREP-LIQAAKTSLGSKIVskchRRFA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 166 AVGKDGAISVEESQTFGIDMDIVE----------------GMQYERGYISPYMATDMEKME-AVLSDPY---ILLTDQK- 224
Cdd:TIGR02343 182 EIAVDAVLNVADMERRDVDFDLIKvegkvggsledtklikGIIIDKDFSHPQMPKEVEDAKiAILTCPFeppKPKTKHKl 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 225 -VTNIQDMVPL-----------LEEIMKSGRPLFIVAEDVEGEALATILLNKLRgtfncvAIKAPGFGDrrkriLEDIAA 292
Cdd:TIGR02343 262 dISSVEEYKKLqkyeqqkfkemIDDIKKSGANLVICQWGFDDEANHLLLQNDLP------AVRWVGGQE-----LELIAI 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 293 VTGAQVIDKdfgmtMADARIDMLGHAKTVK-----VTKDSALIVDGAGDKKAiddrigqikaelervdsdfdreklqerl 367
Cdd:TIGR02343 331 ATGGRIVPR-----FQELSKDKLGKAGLVReisfgTTKDRMLVIEQCKNSKA---------------------------- 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 368 aklsggVAVLkVGAATESELKEKKSRIEDALQATRAAVEEG-IVAGGGVALVGALPALDkvEAADKDEEVGVAIIR---K 443
Cdd:TIGR02343 378 ------VTIF-IRGGNKMIIEEAKRSIHDALCVVRNLIKDSrIVYGGGAAEISCSLAVS--QEADKYPGVEQYAIRafaD 448
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496662690 444 ALEAPMRAIAQNAGFEGSVVVERVKGMATGE-----GLNCANGEYGNMIEMGVNDPVKVTRTALQSAASVAALIL 513
Cdd:TIGR02343 449 ALETIPMALAENSGLDPIGTLSTLKSLQLKEknpnlGVDCLGYGTNDMKEQFVFETLIGKKQQILLATQLVRMIL 523
|
|
| TCP1_delta |
cd03338 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ... |
22-513 |
5.41e-12 |
|
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.
Pssm-ID: 239454 [Multi-domain] Cd Length: 515 Bit Score: 68.08 E-value: 5.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 22 LADAVKVTLGPKGRYVALEKSYGAPLITNDGVTVAKEVELEDPIENMGAQLvrevaVKTNDV-AGDGTTTATLLADVIVS 100
Cdd:cd03338 20 VADAIRTSLGPRGMDKMIQTGKGEVIITNDGATILKQMSVLHPAAKMLVEL-----SKAQDIeAGDGTTSVVVLAGALLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 101 EGLRNVTAGADALGIRRGIQKATDAVVEAIKADATPVSTKE-----QIANVGTISAGDAEIGEKIAE-AMDAVGKDGAIS 174
Cdd:cd03338 95 ACESLLKKGIHPTVISESFQIAAKKAVEILDSMSIPVDLNDresliKSATTSLNSKVVSQYSSLLAPiAVDAVLKVIDPA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 175 VEES---------QTFG---IDMDIVEGMQY-ERGYISPYMATDMEK-----MEAVLSDPYillTDQK----VTNIQDMV 232
Cdd:cd03338 175 TATNvdlkdirivKKLGgtiEDTELVDGLVFtQKASKKAGGPTRIEKakiglIQFCLSPPK---TDMDnnivVNDYAQMD 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 233 PLLEE-----------IMKSGRPLFIVAEDVEGEA---LATILLNKLrgtfNCVAIKapgfgDRRKRILEDIAAVTGAQV 298
Cdd:cd03338 252 RILREerkyilnmckkIKKSGCNVLLIQKSILRDAvsdLALHFLAKL----KIMVVK-----DIEREEIEFICKTIGCKP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 299 IDKDFGMTMadariDMLGHAKTVkvtkdsalivdgagdkkaiddrigqikaelERVDSDFDREKLQERLAKLSGGVAVLk 378
Cdd:cd03338 323 VASIDHFTE-----DKLGSADLV------------------------------EEVSLGDGKIVKITGVKNPGKTVTIL- 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 379 VGAATESELKEKKSRIEDALQATRAAVEE-GIVAGGGVALVGAlpALDKVEAADKDEEVGVAIIR---KALEAPMRAIAQ 454
Cdd:cd03338 367 VRGSNKLVLDEAERSLHDALCVIRCLVKKrALIPGGGAPEIEI--ALQLSEWARTLTGVEQYCVRafaDALEVIPYTLAE 444
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496662690 455 NAGFEG-SVVVERVKGMATGE---GLNCANGEYGNMIEMGVNDPVKVTRTALQSAASVAALIL 513
Cdd:cd03338 445 NAGLNPiSIVTELRNRHAQGEknaGINVRKGAITNILEENVVQPLLVSTSAITLATETVRMIL 507
|
|
| chap_CCT_eta |
TIGR02345 |
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ... |
21-519 |
1.47e-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: 1.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 21 KLADAVKVTLGPKGRYVALEKSYGAPLITNDGVTVAKEVELEDPIenmgAQLVREVAVKTNDVAGDGTTTATLLADVIVS 100
Cdd:TIGR02345 29 AIAEALKTTLGPRGMDKLIVGSNGKATISNDGATILKLLDIVHPA----AKTLVDIAKSQDAEVGDGTTSVTILAGELLK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 101 EGLRNVTAGADALGIRRGIQKATDAVVEAIKADATPVSTK--------EQIANVGTISAGDAEIGEKIAE-AMDAVgKDG 171
Cdd:TIGR02345 105 EAKPFIEEGVHPQLIIRCYREALSLAVEKIKEIAVTIDEEkgeqrellEKCAATALSSKLISHNKEFFSKmIVDAV-LSL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 172 AISVEESQTFGI---------DMDIVEGMQYERGYisPYMAtdMEKMEAVLSDPYILLTDQKVtniqdmvplleEIMKSG 242
Cdd:TIGR02345 184 DRDDLDLKLIGIkkvqggaleDSQLVNGVAFKKTF--SYAG--FEQQPKKFANPKILLLNVEL-----------ELKAEK 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 243 RPLFIVAEDVEG-----EALATILLNKLRGTF----NCVAIKAPgFGDRRKRILEDIAAVTGAQVIDKDFGMTMADARID 313
Cdd:TIGR02345 249 DNAEIRVEDVEDyqaivDAEWAIIFRKLEKIVesgaNVVLSKLP-IGDLATQYFADRDIFCAGRVSAEDLKRVIKACGGS 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 314 MLGhakTVKVTKDSALivdgaGDKKAIDDRigQIKAElervdsdfdREKLQERLAKLSGGVAVLKVGAatESELKEKKSR 393
Cdd:TIGR02345 328 IQS---TTSDLEADVL-----GTCALFEER--QIGSE---------RYNYFTGCPHAKTCTIILRGGA--EQFIEEAERS 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 394 IEDALQATRAAVEEGIVAGGGVALVGALPAL--DKVEAADKDEEVGVAIIRKALEAPMRAIAQNAGFEGSVVVERVKGM- 470
Cdd:TIGR02345 387 LHDAIMIVRRALKNKKIVAGGGAIEMELSKClrDYSKTIDGKQQLIINAFAKALEIIPRQLCENAGFDSIEILNKLRSRh 466
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 496662690 471 ATG---EGLNCANGEYGNMIEMGVNDPVKVTRTALQSAASVAALILITEATI 519
Cdd:TIGR02345 467 AKGgkwYGVDINTEDIGDNFEAFVWEPALVKINALKAAFEAACTILSVDETI 518
|
|
| TCP1_eta |
cd03340 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ... |
21-519 |
3.64e-11 |
|
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.
Pssm-ID: 239456 [Multi-domain] Cd Length: 522 Bit Score: 65.39 E-value: 3.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 21 KLADAVKVTLGPKGRYVALEKSYGAPLITNDGVTVAKEVELEDPienmGAQLVREVAVKTNDVAGDGTTTATLLADVIVS 100
Cdd:cd03340 27 AIADAVRTTLGPRGMDKLIVDGRGKVTISNDGATILKLLDIVHP----AAKTLVDIAKSQDAEVGDGTTSVVVLAGEFLK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 101 EGLRNVTAGADALGIRRGIQKATDAVVEAIKADATPVS--------------------------TKEQIANVGTisagDA 154
Cdd:cd03340 103 EAKPFIEDGVHPQIIIRGYRKALQLAIEKIKEIAVNIDkedkeeqrellekcaatalnskliasEKEFFAKMVV----DA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 155 --EIGEKIAEAMDAVGKDGAISVEESQtfgidmdIVEGMQYER-----GYispymatdmEKMEAVLSDPYILLTD----- 222
Cdd:cd03340 179 vlSLDDDLDLDMIGIKKVPGGSLEDSQ-------LVNGVAFKKtfsyaGF---------EQQPKKFKNPKILLLNvelel 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 223 -----------QKVTNIQDMVPL--------LEEIMKSGrplfivaedvegealATILLNKLrgTFNCVAIKApgFGDRR 283
Cdd:cd03340 243 kaekdnaevrvEDPEEYQAIVDAewkiiydkLEKIVKSG---------------ANVVLSKL--PIGDLATQY--FADRD 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 284 ----KRILED----IAAVTGAQVIDKDFGMTmadaridmlghaktvkvtkdsalivdgagdkkaiDDRIGQIkAELERVD 355
Cdd:cd03340 304 ifcaGRVPEEdlkrVAQATGGSIQTTVSNIT----------------------------------DDVLGTC-GLFEERQ 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 356 SDFDREKLQERLAKLSGGVAVLKVGAatESELKEKKSRIEDALQATRAAVEEG-IVAGGGvALVGALPAL--DKVEAADK 432
Cdd:cd03340 349 VGGERYNIFTGCPKAKTCTIILRGGA--EQFIEEAERSLHDAIMIVRRAIKNDsVVAGGG-AIEMELSKYlrDYSRTIAG 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 433 DEEVGVAIIRKALEAPMRAIAQNAGFEGSVVVERV-----KGMATGEGLNCANGEYGNMIEMGVNDPVKVTRTALQSAAS 507
Cdd:cd03340 426 KQQLVINAFAKALEIIPRQLCDNAGFDATDILNKLrqkhaQGGGKWYGVDINNEGIADNFEAFVWEPSLVKINALTAATE 505
|
570
....*....|..
gi 496662690 508 VAALILITEATI 519
Cdd:cd03340 506 AACLILSVDETI 517
|
|
| chap_CCT_delta |
TIGR02342 |
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ... |
8-513 |
9.00e-10 |
|
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: 60.95 E-value: 9.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 8 EADARSALAAGVNKLADAVKVTLGPKGRYVALEKSYGAPLITNDGVTVAKEVELEDPIenmgAQLVREVAVKTNDVAGDG 87
Cdd:TIGR02342 7 PQDVRTSNIVAAKAVADAIRTSLGPKGMDKMIQDGKGEVIITNDGATILKQMAVLHPA----AKMLVELSKAQDIEAGDG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 88 TTTATLLADVIVSEGLRNVTAGADALGIRRGIQKATDAVVEAIKADATPVSTKE-QIANVGTISAGDAEIGEKIAEAMDA 166
Cdd:TIGR02342 83 TTSVVILAGALLGACERLLNKGIHPTIISESFQSAADEAIKILDEMSIPVDLSDrEQLLKSATTSLSSKVVSQYSSLLAP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 167 VGKDGAISVEESQTF-GIDMDIVEGMQYERGYISpymatDMEKMEAVLSDPYILLTDQKVTNIQDM-VPLLEEIMKSGRP 244
Cdd:TIGR02342 163 LAVDAVLKVIDPENAkNVDLNDIKVVKKLGGTID-----DTELIEGLVFTQKASKSAGGPTRIEKAkIGLIQFQISPPKT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 245 lfivaeDVEgealatillnklrgtfNCVAIKAPGFGDR-----RKRILEDIAAV--TGAQV--IDKDFgmtMADARIDML 315
Cdd:TIGR02342 238 ------DME----------------NQIIVNDYAQMDRvlkeeRAYILNIVKKIkkTGCNVllIQKSI---LRDAVNDLA 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 316 GH---AKTVKVTKD-----SALIVDGAGDKKAID------DRIGqiKAEL-ERVDSDFDREKLQERLAKLSGGVAVLKVG 380
Cdd:TIGR02342 293 LHflaKMKIMVVKDiereeIEFICKTIGCKPIASidhftaDKLG--SAELvEEVDSDGGKIIKITGIQNAGKTVTVVVRG 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 381 aATESELKEKKSRIEDALQATRAAVEE-GIVAGGGVALVGAlpALDKVEAADKDEEVGVAIIR---KALEAPMRAIAQNA 456
Cdd:TIGR02342 371 -SNKLVIDEAERSLHDALCVIRCLVKKrGLIAGGGAPEIEI--ARRLSKYARTMKGVESYCVRafaDALEVIPYTLAENA 447
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496662690 457 GFEG-SVVVERVKGMATGE---GLNCANGEYGNMIEMGVNDPVKVTRTALQSAASVAALIL 513
Cdd:TIGR02342 448 GLNPiKVVTELRNRHANGEktaGISVRKGGITNMLEEHVLQPLLVTTSAITLASETVRSIL 508
|
|
| chap_CCT_beta |
TIGR02341 |
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ... |
10-524 |
2.54e-08 |
|
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT beta chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.
Pssm-ID: 274082 Cd Length: 519 Bit Score: 56.41 E-value: 2.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 10 DARSALAAGVNKLADAVKVTLGPKGRYVALEK--SYGAPLITNDGVTVAKEVeledPIENMGAQLVREVAVKTNDVAGDG 87
Cdd:TIGR02341 14 NARLSSFVGAIAIGDLVKSTLGPKGMDKILQSssSDASIMVTNDGATILKSI----GVDNPAAKVLVDMSKVQDDEVGDG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 88 TTTATLLADVIVSEGLRNVTAGADALGIRRGIQKATDAVVEAIKADATPVSTKEQIANVGTISAGDAEIGEKIAE----- 162
Cdd:TIGR02341 90 TTSVTVLAAELLREAEKLINQKIHPQTIIAGYREATKAARDALLKSAVDNGSDEVKFRQDLMNIARTTLSSKILSqhkdh 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 163 ----AMDAVGK-DGAISVEESQTfgidmdivegmqyergyispymatdMEKMEAVLSDPYI---LLTDQKVTNIQDMVPL 234
Cdd:TIGR02341 170 faqlAVDAVLRlKGSGNLEAIQI-------------------------IKKLGGSLADSYLdegFLLDKKIGVNQPKRIE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 235 LEEIMKSGRPLFIVAEDVEGEALATILLNKLRGTFNCVAIKapgFGDRRKRILE-DIAAVTGAQVIDKDFGMTMADARID 313
Cdd:TIGR02341 225 NAKILIANTGMDTDKVKIFGSRVRVDSTAKVAELEHAEKEK---MKEKVEKILKhGINCFINRQLIYNYPEQLFADAGVM 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 314 MLGHAKTVKVTKDSalIVDGAGDKKAIDDrigQIKAELERVDSDFDREKLQERLAKLSGGVA------VLKvgAATESEL 387
Cdd:TIGR02341 302 AIEHADFEGVERLA--LVTGGEIVSTFDH---PELVKLGSCDLIEEIMIGEDKLLKFSGVKLgeactiVLR--GATQQIL 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 388 KEKKSRIEDALQATRAAVEEG-IVAGGGVALVGALPALDkVEAADKD--EEVGVAIIRKALEAPMRAIAQNAGFEGSVVV 464
Cdd:TIGR02341 375 DEAERSLHDALCVLSQTVKESrTVLGGGCSEMLMSKAVT-QEAQRTPgkEALAVEAFARALRQLPTIIADNAGFDSAELV 453
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496662690 465 ERVKGM----ATGEGLNCANGEYGNMIEMGVNDPVKVTRTALQSAASVAALILITEATINEIPK 524
Cdd:TIGR02341 454 AQLRAAhyngNTTMGLDMNEGTIADMRQLGITESYKVKRAVVSSAAEAAEVILRVDNIIKAAPR 517
|
|
| TCP1_beta |
cd03336 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ... |
2-141 |
4.30e-08 |
|
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: 55.80 E-value: 4.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 2 AKEIKFEaDARSALAAGVNKLADAVKVTLGPKGRYVALE--KSYGAPLITNDGVTVAKEVELEDPienmGAQLVREVAVK 79
Cdd:cd03336 6 AQEEKGE-TARLSSFVGAIAIGDLVKTTLGPKGMDKILQsvGRSGGVTVTNDGATILKSIGVDNP----AAKVLVDISKV 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496662690 80 TNDVAGDGTTTATLLADVIVSEGLRNVTAGADALGIRRGIQKATDAVVEAIKADATPVSTKE 141
Cdd:cd03336 81 QDDEVGDGTTSVTVLAAELLREAEKLVAQKIHPQTIIEGYRMATAAAREALLSSAVDHSSDE 142
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
2-142 |
1.80e-07 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 53.88 E-value: 1.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 2 AKEIKFEaDARSALAAGVNKLADAVKVTLGPKGRYVALEKSYGAP-----LITNDGVTVAKEVELEDPienmGAQLVREV 76
Cdd:PTZ00212 15 AQEEKGE-TARLQSFVGAIAVADLVKTTLGPKGMDKILQPMSEGPrsgnvTVTNDGATILKSVWLDNP----AAKILVDI 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496662690 77 AVKTNDVAGDGTTTATLLADVIVSEGLRNVTAGADALGIRRGIQKATDAVVEAIKADATPVSTKEQ 142
Cdd:PTZ00212 90 SKTQDEEVGDGTTSVVVLAGELLREAEKLLDQKIHPQTIIEGWRMALDVARKALEEIAFDHGSDEE 155
|
|
| chap_CCT_zeta |
TIGR02347 |
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ... |
22-208 |
1.84e-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: 53.58 E-value: 1.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 22 LADAVKVTLGPKGRYVALEKSYGAPLITNDGVTVAKEVELEDPIENMGAQlvreVAVKTNDVAGDGTTTATLLADVIVSE 101
Cdd:TIGR02347 28 LQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEMQIQHPTASMIAR----AATAQDDITGDGTTSTVLLIGELLKQ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 102 GLRNVTAGADALGIRRGIQKATDAV---VEAIKADATPVSTKEQIANVGTISAG---DAEIGEKIAE----AMDAVGKDG 171
Cdd:TIGR02347 104 AERYILEGVHPRIITEGFEIARKEAlqfLDKFKVKKEDEVDREFLLNVARTSLRtklPADLADQLTEivvdAVLAIKKDG 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 496662690 172 A----ISVEESQ---TFGIDMDIVEGMQYERGYISPYMATDMEK 208
Cdd:TIGR02347 184 EdidlFMVEIMEmkhKSATDTTLIRGLVLDHGARHPDMPRRVKN 227
|
|
| TCP1_zeta |
cd03342 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
11-192 |
8.55e-07 |
|
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.
Pssm-ID: 239458 [Multi-domain] Cd Length: 484 Bit Score: 51.49 E-value: 8.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 11 ARSALAAGVN-----KLADAVKVTLGPKGRYVALEKSYGAPLITNDGVTVAKEVELEDPIENMGAQlvreVAVKTNDVAG 85
Cdd:cd03342 8 LRRGQALAVNisaakGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLSEMQIQHPTASMIAR----AATAQDDITG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 86 DGTTTATLLADVIVSEGLRNVTAGADALGIRRGIQKATDAVVEAIKADATPVST---KEQIANVGTIS---AGDAEIGEK 159
Cdd:cd03342 84 DGTTSNVLLIGELLKQAERYIQEGVHPRIITEGFELAKNKALKFLESFKVPVEIdtdRELLLSVARTSlrtKLHADLADQ 163
|
170 180 190
....*....|....*....|....*....|....
gi 496662690 160 IAEAM-DAVgkdgaISVEESQTFgIDMDIVEGMQ 192
Cdd:cd03342 164 LTEIVvDAV-----LAIYKPDEP-IDLHMVEIMQ 191
|
|
| chap_CCT_alpha |
TIGR02340 |
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ... |
10-191 |
1.04e-06 |
|
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT alpha chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.
Pssm-ID: 274081 [Multi-domain] Cd Length: 536 Bit Score: 51.26 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 10 DARSALAAGVNKLADAVKVTLGPKGRYVALEKSYGAPLITNDGVTVAKEVELEDPienmGAQLVREVAVKTNDVAGDGTT 89
Cdd:TIGR02340 12 DVRTQNVTAAMAIANIVKTSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHP----AAKILVELAQLQDREVGDGTT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 90 TATLLAdvivSEGLRNvtagADALgIRRGIQKATdaVVEAIKadatpVSTKEQIanvgtisagdAEIGEKIAEAMDAVGK 169
Cdd:TIGR02340 88 SVVIIA----AELLKR----ADEL-VKNKIHPTS--VISGYR-----LACKEAV----------KYIKENLSVSVDELGR 141
|
170 180
....*....|....*....|....*.
gi 496662690 170 DGAISVEE----SQTFGIDMDIVEGM 191
Cdd:TIGR02340 142 EALINVAKtsmsSKIIGLDSDFFSNI 167
|
|
| TCP1_alpha |
cd03335 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ... |
9-119 |
6.92e-06 |
|
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.
Pssm-ID: 239451 Cd Length: 527 Bit Score: 48.82 E-value: 6.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 9 ADARSALAAGVNKLADAVKVTLGPKGRYVALEKSYGAPLITNDGVTVAKEVELEDPienmGAQLVREVAVKTNDVAGDGT 88
Cdd:cd03335 7 QDVRTQNVTAAMAIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHP----AAKILVELAQLQDKEVGDGT 82
|
90 100 110
....*....|....*....|....*....|.
gi 496662690 89 TTATLLAdvivSEGLRNvtagADALgIRRGI 119
Cdd:cd03335 83 TSVVIIA----AELLKR----ANEL-VKQKI 104
|
|
| chap_CCT_gamma |
TIGR02344 |
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ... |
22-151 |
9.22e-05 |
|
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT gamma chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.
Pssm-ID: 274085 [Multi-domain] Cd Length: 524 Bit Score: 45.11 E-value: 9.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 22 LADAVKVTLGPKGRYVALEKSYGAPLITNDGVTVAKEVELEDPienmGAQLVREVAVKTNDVAGDGTTTATLLADVIVSE 101
Cdd:TIGR02344 28 VADIIRTCLGPRSMLKMLLDPMGGIVMTNDGNAILREIDVAHP----AAKSMIELSRTQDEEVGDGTTSVIILAGEMLSV 103
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 496662690 102 GLRNVTAGADALGIRRGIQKATDAVVEAIKADATPVSTKEQIANVGTISA 151
Cdd:TIGR02344 104 AEPFLEQNIHPTVIIRAYRKALDDALSVLEEISIPVDVNDDAAMLKLIQS 153
|
|
| TCP1_gamma |
cd03337 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ... |
22-146 |
1.03e-04 |
|
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: 44.98 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496662690 22 LADAVKVTLGPKGRYVALEKSYGAPLITNDGVTVAKEVELEDPienmGAQLVREVAVKTNDVAGDGTTTATLLADVIVSE 101
Cdd:cd03337 28 VADVIRTCLGPRAMLKMLLDPMGGIVLTNDGNAILREIDVAHP----AAKSMIELSRTQDEEVGDGTTSVIILAGEILAV 103
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 496662690 102 GLRNVTAGADALGIRRGIQKATDAVVEAIKADATPV--STKEQIANV 146
Cdd:cd03337 104 AEPFLERGIHPTVIIKAYRKALEDALKILEEISIPVdvNDRAQMLKI 150
|
|
| |
