|
Name |
Accession |
Description |
Interval |
E-value |
| groEL |
PRK12849 |
chaperonin GroEL; Reviewed |
1-529 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237230 Cd Length: 542 Bit Score: 785.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 1 MSKLIEYDETARRAMEVGMDKLADTVRVTLGPRGRHVVLAKAFGGPTVTNDGVTVAREIELEDPFEDLGAQLVKSVATKT 80
Cdd:PRK12849 1 MAKIIKFDEEARRALERGVNKLADAVKVTLGPKGRNVVIDKSFGAPTITKDGVSIAKEIELEDPFENLGAQLVKEVASKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 81 NDVAGDGTTTATILAQALIKGGLRLVAAGVNPIALGVGIGKAADAVSEALLASATPVSGKTGIAQVATVSSR-DEQIGDL 159
Cdd:PRK12849 81 NDVAGDGTTTATVLAQALVQEGLKNVAAGANPMDLKRGIDKAVEAVVEELKALARPVSGSEEIAQVATISANgDEEIGEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 160 VGEAMSKVGHDGVVSVEESSTLGTELEFTEGIGFDKGFLSAYFVTDFDNQQAVLEDALILLHQDKISSLPDLLPLLEKVA 239
Cdd:PRK12849 161 IAEAMEKVGKDGVITVEESKTLETELEVTEGMQFDRGYLSPYFVTDPERMEAVLEDPLILLTDKKISSLQDLLPLLEKVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 240 GTGKPLLIVAEDVEGEALATLVVNAIRKTLKAVAVKGPYFGDRRKAFLEDLAVVTGGQVVNPDAGMVLREVGLEVLGSAR 319
Cdd:PRK12849 241 QSGKPLLIIAEDVEGEALATLVVNKLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGLKLEEVTLDDLGRAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 320 RVVVSKDDTVIVDGGGTAEAVANRAKHLRAEIDKSDSDWDREKLGERLAKLAGGVAVIKVGAATETALKERKESVEDAVA 399
Cdd:PRK12849 321 RVTITKDNTTIVDGAGDKEAIEARVAQIRRQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATEVELKERKDRVEDALN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 400 AAKAAVEEGIVPGGGASLIHqARKALTELrASLTGDEVLGVDVFSEALAAPLFWIAANAGLDGSVVVNKVSELPAGHGLN 479
Cdd:PRK12849 401 ATRAAVEEGIVPGGGVALLR-AAKALDEL-AGLNGDQAAGVEIVRRALEAPLRQIAENAGLDGSVVVAKVLELEDGFGFN 478
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 489513178 480 VNTLSYGDLAADGVIDPVKVTRSAVLNASSVARMVLTTETVVVDKPAKAE 529
Cdd:PRK12849 479 AATGEYGDLIAAGIIDPVKVTRSALQNAASVAGLLLTTEALVADKPEEED 528
|
|
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
1-529 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 705.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 1 MSKLIEYDETARRAMEVGMDKLADTVRVTLGPRGRHVVLAKAFGGPTVTNDGVTVAREIELEDPFEDLGAQLVKSVATKT 80
Cdd:PRK00013 1 MAKDIKFGEDARRKLLRGVNKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDPFENMGAQLVKEVASKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 81 NDVAGDGTTTATILAQALIKGGLRLVAAGVNPIALGVGIGKAADAVSEALLASATPVSGKTGIAQVATVSS-RDEQIGDL 159
Cdd:PRK00013 81 NDVAGDGTTTATVLAQAIVREGLKNVAAGANPMDLKRGIDKAVEAAVEELKKISKPVEDKEEIAQVATISAnGDEEIGKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 160 VGEAMSKVGHDGVVSVEESSTLGTELEFTEGIGFDKGFLSAYFVTDFDNQQAVLEDALILLHQDKISSLPDLLPLLEKVA 239
Cdd:PRK00013 161 IAEAMEKVGKEGVITVEESKGFETELEVVEGMQFDRGYLSPYFVTDPEKMEAELENPYILITDKKISNIQDLLPVLEQVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 240 GTGKPLLIVAEDVEGEALATLVVNAIRKTLKAVAVKGPYFGDRRKAFLEDLAVVTGGQVVNPDAGMVLREVGLEVLGSAR 319
Cdd:PRK00013 241 QSGKPLLIIAEDVEGEALATLVVNKLRGTLKVVAVKAPGFGDRRKAMLEDIAILTGGTVISEELGLKLEDATLEDLGQAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 320 RVVVSKDDTVIVDGGGTAEAVANRAKHLRAEIDKSDSDWDREKLGERLAKLAGGVAVIKVGAATETALKERKESVEDAVA 399
Cdd:PRK00013 321 KVVVTKDNTTIVDGAGDKEAIKARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATEVEMKEKKDRVEDALH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 400 AAKAAVEEGIVPGGGASLIHqARKALTELrASLTGDEVLGVDVFSEALAAPLFWIAANAGLDGSVVVNKV-SELPAGHGL 478
Cdd:PRK00013 401 ATRAAVEEGIVPGGGVALLR-AAPALEAL-KGLNGDEATGINIVLRALEAPLRQIAENAGLEGSVVVEKVkNGKGKGYGY 478
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 489513178 479 NVNTLSYGDLAADGVIDPVKVTRSAVLNASSVARMVLTTETVVVDKPAKAE 529
Cdd:PRK00013 479 NAATGEYVDMIEAGIIDPTKVTRSALQNAASVAGLLLTTEAVVADKPEKKA 529
|
|
| GroEL |
cd03344 |
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ... |
3-523 |
0e+00 |
|
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings, each composed of 7-9 subunits. The symmetry of type I is seven-fold and they are found in eubacteria (GroEL) and in organelles of eubacterial descent (hsp60 and RBP). With the aid of cochaperonin GroES, GroEL encapsulates non-native substrate proteins inside the cavity of the GroEL-ES complex and promotes folding by using energy derived from ATP hydrolysis.
Pssm-ID: 239460 Cd Length: 520 Bit Score: 703.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 3 KLIEYDETARRAMEVGMDKLADTVRVTLGPRGRHVVLAKAFGGPTVTNDGVTVAREIELEDPFEDLGAQLVKSVATKTND 82
Cdd:cd03344 1 KDIKFGEEARKALLRGVNKLADAVKVTLGPKGRNVVIEKSFGSPKITKDGVTVAKEIELEDPFENMGAQLVKEVASKTND 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 83 VAGDGTTTATILAQALIKGGLRLVAAGVNPIALGVGIGKAADAVSEALLASATPVSGKTGIAQVATVSSR-DEQIGDLVG 161
Cdd:cd03344 81 VAGDGTTTATVLARAIIKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKPVKTKEEIAQVATISANgDEEIGELIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 162 EAMSKVGHDGVVSVEESSTLGTELEFTEGIGFDKGFLSAYFVTDFDNQQAVLEDALILLHQDKISSLPDLLPLLEKVAGT 241
Cdd:cd03344 161 EAMEKVGKDGVITVEEGKTLETELEVVEGMQFDRGYLSPYFVTDPEKMEVELENPYILLTDKKISSIQELLPILELVAKA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 242 GKPLLIVAEDVEGEALATLVVNAIRKTLKAVAVKGPYFGDRRKAFLEDLAVVTGGQVVNPDAGMVLREVGLEVLGSARRV 321
Cdd:cd03344 241 GRPLLIIAEDVEGEALATLVVNKLRGGLKVCAVKAPGFGDRRKAMLEDIAILTGGTVISEELGLKLEDVTLEDLGRAKKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 322 VVSKDDTVIVDGGGTAEAVANRAKHLRAEIDKSDSDWDREKLGERLAKLAGGVAVIKVGAATETALKERKESVEDAVAAA 401
Cdd:cd03344 321 VVTKDDTTIIGGAGDKAAIKARIAQIRKQIEETTSDYDKEKLQERLAKLSGGVAVIKVGGATEVELKEKKDRVEDALNAT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 402 KAAVEEGIVPGGGASLIHqARKALTELrASLTGDEVLGVDVFSEALAAPLFWIAANAGLDGSVVVNKVSELPAGHGLNVN 481
Cdd:cd03344 401 RAAVEEGIVPGGGVALLR-ASPALDKL-KALNGDEKLGIEIVRRALEAPLRQIAENAGVDGSVVVEKVLESPDGFGYDAA 478
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 489513178 482 TLSYGDLAADGVIDPVKVTRSAVLNASSVARMVLTTETVVVD 523
Cdd:cd03344 479 TGEYVDMIEAGIIDPTKVVRSALQNAASVASLLLTTEALVVD 520
|
|
| GroEL |
TIGR02348 |
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ... |
2-525 |
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: 647.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 2 SKLIEYDETARRAMEVGMDKLADTVRVTLGPRGRHVVLAKAFGGPTVTNDGVTVAREIELEDPFEDLGAQLVKSVATKTN 81
Cdd:TIGR02348 1 AKQIKFDEEARKALLRGVDKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDKFENMGAQLVKEVASKTN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 82 DVAGDGTTTATILAQALIKGGLRLVAAGVNPIALGVGIGKAADAVSEALLASATPVSGKTGIAQVATVSS-RDEQIGDLV 160
Cdd:TIGR02348 81 DVAGDGTTTATVLAQAIVKEGLKNVAAGANPIELKRGIEKAVEAVVEELKKLSKPVKGKKEIAQVATISAnNDEEIGSLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 161 GEAMSKVGHDGVVSVEESSTLGTELEFTEGIGFDKGFLSAYFVTDFDNQQAVLEDALILLHQDKISSLPDLLPLLEKVAG 240
Cdd:TIGR02348 161 AEAMEKVGKDGVITVEESKSLETELEVVEGMQFDRGYISPYFVTDAEKMEVELENPYILITDKKISNIKDLLPLLEKVAQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 241 TGKPLLIVAEDVEGEALATLVVNAIRKTLKAVAVKGPYFGDRRKAFLEDLAVVTGGQVVNPDAGMVLREVGLEVLGSARR 320
Cdd:TIGR02348 241 SGKPLLIIAEDVEGEALATLVVNKLRGTLNVCAVKAPGFGDRRKAMLEDIAILTGGQVISEELGLKLEEVTLDDLGKAKK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 321 VVVSKDDTVIVDGGGTAEAVANRAKHLRAEIDKSDSDWDREKLGERLAKLAGGVAVIKVGAATETALKERKESVEDAVAA 400
Cdd:TIGR02348 321 VTVDKDNTTIVEGAGDKAAIKARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATETEMKEKKLRIEDALNA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 401 AKAAVEEGIVPGGGASLIHqARKALTELRaSLTGDEVLGVDVFSEALAAPLFWIAANAGLDGSVVVNKVSELPAGHGLNV 480
Cdd:TIGR02348 401 TRAAVEEGIVPGGGVALLR-AAAALEGLK-GDGEDEAIGIDIVKRALEAPLRQIAENAGLDGAVVAEKVKELKGNFGFNA 478
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 489513178 481 NTLSYGDLAADGVIDPVKVTRSAVLNASSVARMVLTTETVVVDKP 525
Cdd:TIGR02348 479 ATGEYEDLVEAGIIDPTKVTRSALQNAASIAGLLLTTEAVVADKP 523
|
|
| groEL |
PRK12850 |
chaperonin GroEL; Reviewed |
1-529 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237231 Cd Length: 544 Bit Score: 634.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 1 MSKLIEYDETARRAMEVGMDKLADTVRVTLGPRGRHVVLAKAFGGPTVTNDGVTVAREIELEDPFEDLGAQLVKSVATKT 80
Cdd:PRK12850 2 AAKEIRFSTDARDRLLRGVNILANAVKVTLGPKGRNVVLEKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVKEVASKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 81 NDVAGDGTTTATILAQALIKGGLRLVAAGVNPIALGVGIGKAADAVSEALLASATPVSGKTGIAQVATVS-SRDEQIGDL 159
Cdd:PRK12850 82 NDLAGDGTTTATVLAQAIVREGAKLVAAGMNPMDLKRGIDLAVAAVVDELKKIAKKVTSSKEIAQVATISaNGDESIGEM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 160 VGEAMSKVGHDGVVSVEESSTLGTELEFTEGIGFDKGFLSAYFVTDFDNQQAVLEDALILLHQDKISSLPDLLPLLEKVA 239
Cdd:PRK12850 162 IAEAMDKVGKEGVITVEEAKTLGTELDVVEGMQFDRGYLSPYFVTNPEKMRAELEDPYILLHEKKISNLQDLLPILEAVV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 240 GTGKPLLIVAEDVEGEALATLVVNAIRKTLKAVAVKGPYFGDRRKAFLEDLAVVTGGQVVNPDAGMVLREVGLEVLGSAR 319
Cdd:PRK12850 242 QSGRPLLIIAEDVEGEALATLVVNKLRGGLKSVAVKAPGFGDRRKAMLEDIAVLTGGQVISEDLGIKLENVTLDMLGRAK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 320 RVVVSKDDTVIVDGGGTAEAVANRAKHLRAEIDKSDSDWDREKLGERLAKLAGGVAVIKVGAATETALKERKESVEDAVA 399
Cdd:PRK12850 322 RVLITKENTTIIDGAGDKKNIEARVKQIRAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKEKKDRVDDALH 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 400 AAKAAVEEGIVPGGGASLIhQARKALTELrASLTGDEVLGVDVFSEALAAPLFWIAANAGLDGSVVVNKVSELPAGHGLN 479
Cdd:PRK12850 402 ATRAAVEEGIVPGGGVALL-RARSALRGL-KGANADETAGIDIVRRALEEPLRQIATNAGFEGSVVVGKVAELPGNFGFN 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 489513178 480 VNTLSYGDLAADGVIDPVKVTRSAVLNASSVARMVLTTETVVVDKPAKAE 529
Cdd:PRK12850 480 AQTGEYGDMVEAGIIDPAKVTRTALQDAASIAALLITTEAMVAEAPKKAA 529
|
|
| GroEL |
COG0459 |
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ... |
1-529 |
0e+00 |
|
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227 Cd Length: 497 Bit Score: 624.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 1 MSKLIEYDETARRAMEVGMDKLADTVRVTLGPRGRHVVLAKAFGGPTVTNDGVTVAREIELEDPFEDLGAQLVKSVATKT 80
Cdd:COG0459 1 MAKQILFGEDARRANIRGVKALADAVKVTLGPKGRNVMLVKSFGDPTITNDGVTIAKEIELEDPFENMGAQLVKEVASKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 81 NDVAGDGTTTATILAQALIKGGLRLVAAGVNPIALGVGIGKAADAVSEALLASATPVSGKTGIAQVATVSSR-DEQIGDL 159
Cdd:COG0459 81 NDEAGDGTTTATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPVDDKEELAQVATISANgDEEIGEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 160 VGEAMSKVGHDGVVSVEESSTLGTELEFTEGIGFDKGFLSAYFVTDFDNQQAVLEDALILLHQDKISSLPDLLPLLEKVA 239
Cdd:COG0459 161 IAEAMEKVGKDGVITVEEGKGLETELEVVEGMQFDKGYLSPYFVTDPEKMPAELENAYILLTDKKISSIQDLLPLLEKVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 240 GTGKPLLIVAEDVEGEALATLVVNAIRKTLKAVAVKGPYFGDRRKAFLEDLAVVTGGQVVNPDAGMVLREVGLEVLGSAR 319
Cdd:COG0459 241 QSGKPLLIIAEDIDGEALATLVVNGIRGVLRVVAVKAPGFGDRRKAMLEDIAILTGGRVISEDLGLKLEDVTLDDLGRAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 320 RVVVSKDDTVIVDGGGTAEAVanrakhlraeidksdsdwdreklgerlaklaggvaVIKVGAATETALKERKESVEDAVA 399
Cdd:COG0459 321 RVEVDKDNTTIVEGAGNPKAI-----------------------------------VILVGAATEVEVKERKRRVEDALH 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 400 AAKAAVEEGIVPGGGASLIHqARKALTELRASLTGDEVLGVDVFSEALAAPLFWIAANAGLDGSVVVNKVSELP-AGHGL 478
Cdd:COG0459 366 ATRAAVEEGIVPGGGAALLR-AARALRELAAKLEGDEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKVRAAKdKGFGF 444
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 489513178 479 NVNTLSYGDLAADGVIDPVKVTRSAVLNASSVARMVLTTETVVVDKPAKAE 529
Cdd:COG0459 445 DAATGEYVDMLEAGVIDPAKVKRSALQNAASVAGLILTTEAVIADKPEKEE 495
|
|
| groEL |
PRK12851 |
chaperonin GroEL; Reviewed |
1-529 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 171770 Cd Length: 541 Bit Score: 604.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 1 MSKLIEYDETARRAMEVGMDKLADTVRVTLGPRGRHVVLAKAFGGPTVTNDGVTVAREIELEDPFEDLGAQLVKSVATKT 80
Cdd:PRK12851 2 AAKEVKFHVEAREKMLRGVNILADAVKVTLGPKGRNVVIDKSFGAPTITNDGVTIAKEIELEDKFENMGAQMVREVASKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 81 NDVAGDGTTTATILAQALIKGGLRLVAAGVNPIALGVGIGKAADAVSEALLASATPVSGKTGIAQVATVSSR-DEQIGDL 159
Cdd:PRK12851 82 NDVAGDGTTTATVLAQAIVREGAKAVAAGANPMDLKRGIDRAVAAVVEELKANARPVTTNAEIAQVATISANgDAEIGRL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 160 VGEAMSKVGHDGVVSVEESSTLGTELEFTEGIGFDKGFLSAYFVTDFDNQQAVLEDALILLHQDKISSLPDLLPLLEKVA 239
Cdd:PRK12851 162 VAEAMEKVGNEGVITVEESKTAETELEVVEGMQFDRGYLSPYFVTDADKMEAELEDPYILIHEKKISNLQDLLPVLEAVV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 240 GTGKPLLIVAEDVEGEALATLVVNAIRKTLKAVAVKGPYFGDRRKAFLEDLAVVTGGQVVNPDAGMVLREVGLEVLGSAR 319
Cdd:PRK12851 242 QSGKPLLIIAEDVEGEALATLVVNKLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGIKLENVTLEQLGRAK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 320 RVVVSKDDTVIVDGGGTAEAVANRAKHLRAEIDKSDSDWDREKLGERLAKLAGGVAVIKVGAATETALKERKESVEDAVA 399
Cdd:PRK12851 322 KVVVEKENTTIIDGAGSKTEIEGRVAQIRAQIEETTSDYDREKLQERLAKLAGGVAVIRVGASTEVEVKEKKDRVDDALH 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 400 AAKAAVEEGIVPGGGASLIhQARKALTELRAsLTGDEVLGVDVFSEALAAPLFWIAANAGLDGSVVVNKVSELPAGHGLN 479
Cdd:PRK12851 402 ATRAAVEEGIVPGGGVALL-RAVKALDKLET-ANGDQRTGVEIVRRALEAPVRQIAENAGAEGSVVVGKLREKPGGYGFN 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 489513178 480 VNTLSYGDLAADGVIDPVKVTRSAVLNASSVARMVLTTETVVVDKPAKAE 529
Cdd:PRK12851 480 AATNEYGDLYAQGVIDPVKVVRTALQNAASVAGLLLTTEAMVAEKPKKEP 529
|
|
| groEL |
CHL00093 |
chaperonin GroEL |
1-525 |
0e+00 |
|
chaperonin GroEL
Pssm-ID: 177025 Cd Length: 529 Bit Score: 573.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 1 MSKLIEYDETARRAMEVGMDKLADTVRVTLGPRGRHVVLAKAFGGPTVTNDGVTVAREIELEDPFEDLGAQLVKSVATKT 80
Cdd:CHL00093 1 MSKKILYQDNARRALERGMDILAEAVSVTLGPKGRNVVLEKKYGSPQIVNDGVTIAKEIELEDHIENTGVALIRQAASKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 81 NDVAGDGTTTATILAQALIKGGLRLVAAGVNPIALGVGIGKAADAVSEALLASATPVSGKTGIAQVATVSS-RDEQIGDL 159
Cdd:CHL00093 81 NDVAGDGTTTATVLAYAIVKQGMKNVAAGANPISLKRGIEKATQYVVSQIAEYARPVEDIQAITQVASISAgNDEEVGSM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 160 VGEAMSKVGHDGVVSVEESSTLGTELEFTEGIGFDKGFLSAYFVTDFDNQQAVLEDALILLHQDKISSLPDLLP-LLEKV 238
Cdd:CHL00093 161 IADAIEKVGREGVISLEEGKSTVTELEITEGMRFEKGFISPYFVTDTERMEVVQENPYILLTDKKITLVQQDLLpILEQV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 239 AGTGKPLLIVAEDVEGEALATLVVNAIRKTLKAVAVKGPYFGDRRKAFLEDLAVVTGGQVVNPDAGMVLREVGLEVLGSA 318
Cdd:CHL00093 241 TKTKRPLLIIAEDVEKEALATLVLNKLRGIVNVVAVRAPGFGDRRKAMLEDIAILTGGQVITEDAGLSLETIQLDLLGQA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 319 RRVVVSKDDTVIVdGGGTAEAVANRAKHLRAEIDKSDSDWDREKLGERLAKLAGGVAVIKVGAATETALKERKESVEDAV 398
Cdd:CHL00093 321 RRIIVTKDSTTII-ADGNEEQVKARCEQLRKQIEIADSSYEKEKLQERLAKLSGGVAVIKVGAATETEMKDKKLRLEDAI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 399 AAAKAAVEEGIVPGGGASLIHQARKALTELRASLTGDEVLGVDVFSEALAAPLFWIAANAGLDGSVVVNKVSELPAGHGL 478
Cdd:CHL00093 400 NATKAAVEEGIVPGGGATLVHLSENLKTWAKNNLKEDELIGALIVARAILAPLKRIAENAGKNGSVIIEKVQEQDFEIGY 479
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 489513178 479 NVNTLSYGDLAADGVIDPVKVTRSAVLNASSVARMVLTTETVVVDKP 525
Cdd:CHL00093 480 NAANNKFVNMYEAGIIDPAKVTRSALQNAASIASMILTTECIIVDKK 526
|
|
| PTZ00114 |
PTZ00114 |
Heat shock protein 60; Provisional |
2-527 |
0e+00 |
|
Heat shock protein 60; Provisional
Pssm-ID: 185455 Cd Length: 555 Bit Score: 550.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 2 SKLIEYDETARRAMEVGMDKLADTVRVTLGPRGRHVVLAKAFGGPTVTNDGVTVAREIELEDPFEDLGAQLVKSVATKTN 81
Cdd:PTZ00114 14 GKEIRFGDEARQSLLKGIERLADAVAVTLGPKGRNVIIEQEYGSPKITKDGVTVAKAIEFSDRFENVGAQLIRQVASKTN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 82 DVAGDGTTTATILAQALIKGGLRLVAAGVNPIALGVGIGKAADAVSEALLASATPVSGKTGIAQVATVSSR-DEQIGDLV 160
Cdd:PTZ00114 94 DKAGDGTTTATILARAIFREGCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQSRPVKTKEDILNVATISANgDVEIGSLI 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 161 GEAMSKVGHDGVVSVEESSTLGTELEFTEGIGFDKGFLSAYFVTDFDNQQAVLEDALILLHQDKISSLPDLLPLLEKVAG 240
Cdd:PTZ00114 174 ADAMDKVGKDGTITVEDGKTLEDELEVVEGMSFDRGYISPYFVTNEKTQKVELENPLILVTDKKISSIQSILPILEHAVK 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 241 TGKPLLIVAEDVEGEALATLVVNAIRKTLKAVAVKGPYFGDRRKAFLEDLAVVTGGQVVNPDA-GMVLREVGLEVLGSAR 319
Cdd:PTZ00114 254 NKRPLLIIAEDVEGEALQTLIINKLRGGLKVCAVKAPGFGDNRKDILQDIAVLTGATVVSEDNvGLKLDDFDPSMLGSAK 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 320 RVVVSKDDTVIVDGGGTAEAVANRAKHLRAEIDKSDSDWDREKLGERLAKLAGGVAVIKVGAATETALKERKESVEDAVA 399
Cdd:PTZ00114 334 KVTVTKDETVILTGGGDKAEIKERVELLRSQIERTTSEYDKEKLKERLAKLSGGVAVIKVGGASEVEVNEKKDRIEDALN 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 400 AAKAAVEEGIVPGGGASLIHqARKALTELRA--SLTGDEVLGVDVFSEALAAPLFWIAANAGLDGSVVVNKVSEL-PAGH 476
Cdd:PTZ00114 414 ATRAAVEEGIVPGGGVALLR-ASKLLDKLEEdnELTPDQRTGVKIVRNALRLPTKQIAENAGVEGAVVVEKILEKkDPSF 492
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 489513178 477 GLNVNTLSYGDLAADGVIDPVKVTRSAVLNASSVARMVLTTETVVVDKPAK 527
Cdd:PTZ00114 493 GYDAQTGEYVNMFEAGIIDPTKVVRSALVDAASVASLMLTTEAAIVDLPKE 543
|
|
| groEL |
PRK12852 |
chaperonin GroEL; Reviewed |
1-529 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237232 Cd Length: 545 Bit Score: 527.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 1 MSKLIEYDETARRAMEVGMDKLADTVRVTLGPRGRHVVLAKAFGGPTVTNDGVTVAREIELEDPFEDLGAQLVKSVATKT 80
Cdd:PRK12852 2 AAKDVKFSGDARDRMLRGVDILANAVKVTLGPKGRNVVIEKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVREVASKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 81 NDVAGDGTTTATILAQALIKGGLRLVAAGVNPIALGVGIGKAADAVSEALLASATPVSGKTGIAQVATVSSR-DEQIGDL 159
Cdd:PRK12852 82 NDLAGDGTTTATVLAQAIVREGAKAVAAGMNPMDLKRGIDIAVAAVVKDIEKRAKPVASSAEIAQVGTISANgDAAIGKM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 160 VGEAMSKVGHDGVVSVEESSTLGTELEFTEGIGFDKGFLSAYFVTDFDNQQAVLEDALILLHQDKISSLPDLLPLLEKVA 239
Cdd:PRK12852 162 IAQAMQKVGNEGVITVEENKSLETEVDIVEGMKFDRGYLSPYFVTNAEKMTVELDDAYILLHEKKLSGLQAMLPVLEAVV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 240 GTGKPLLIVAEDVEGEALATLVVNAIRKTLKAVAVKGPYFGDRRKAFLEDLAVVTGGQVVNPDAGMVLREVGLEVLGSAR 319
Cdd:PRK12852 242 QSGKPLLIIAEDVEGEALATLVVNRLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGQLISEDLGIKLENVTLKMLGRAK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 320 RVVVSKDDTVIVDGGGTAEAVANRAKHLRAEIDKSDSDWDREKLGERLAKLAGGVAVIKVGAATETALKERKESVEDAVA 399
Cdd:PRK12852 322 KVVIDKENTTIVNGAGKKADIEARVGQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKEKKDRVEDALN 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 400 AAKAAVEEGIVPGGGASLIhQARKALTELrASLTGDEVLGVDVFSEALAAPLFWIAANAGLDGSVVVNKVSELPA-GHGL 478
Cdd:PRK12852 402 ATRAAVQEGIVPGGGVALL-RAKKAVGRI-NNDNADVQAGINIVLKALEAPIRQIAENAGVEGSIVVGKILENKSeTFGF 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 489513178 479 NVNTLSYGDLAADGVIDPVKVTRSAVLNASSVARMVLTTETVVVDKPAKAE 529
Cdd:PRK12852 480 DAQTEEYVDMVAKGIIDPAKVVRTALQDAASVAGLLVTTEAMVAELPKKDA 530
|
|
| PRK14104 |
PRK14104 |
chaperonin GroEL; Provisional |
2-528 |
3.12e-158 |
|
chaperonin GroEL; Provisional
Pssm-ID: 172594 Cd Length: 546 Bit Score: 462.19 E-value: 3.12e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 2 SKLIEYDETARRAMEVGMDKLADTVRVTLGPRGRHVVLAKAFGGPTVTNDGVTVAREIELEDPFEDLGAQLVKSVATKTN 81
Cdd:PRK14104 3 AKEVKFGVDARDRMLRGVDILANAVKVTLGPKGRNVVLDKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVREVASKSA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 82 DVAGDGTTTATILAQALIKGGLRLVAAGVNPIALGVGIGKAADAVSEALLASATPVSGKTGIAQVATVSSR-DEQIGDLV 160
Cdd:PRK14104 83 DAAGDGTTTATVLAQAIVREGAKSVAAGMNPMDLKRGIDLAVEAVVADLVKNSKKVTSNDEIAQVGTISANgDAEIGKFL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 161 GEAMSKVGHDGVVSVEESSTLGTELEFTEGIGFDKGFLSAYFVTDFDNQQAVLEDALILLHQDKISSLPDLLPLLEKVAG 240
Cdd:PRK14104 163 ADAMKKVGNEGVITVEEAKSLETELDVVEGMQFDRGYISPYFVTNADKMRVEMDDAYILINEKKLSSLNELLPLLEAVVQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 241 TGKPLLIVAEDVEGEALATLVVNAIRKTLKAVAVKGPYFGDRRKAFLEDLAVVTGGQVVNPDAGMVLREVGLEVLGSARR 320
Cdd:PRK14104 243 TGKPLVIVAEDVEGEALATLVVNRLRGGLKVAAVKAPGFGDRRKAMLQDIAILTGGQAISEDLGIKLENVTLQMLGRAKK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 321 VVVSKDDTVIVDGGGTAEAVANRAKHLRAEIDKSDSDWDREKLGERLAKLAGGVAVIKVGAATETALKERKESVEDAVAA 400
Cdd:PRK14104 323 VMIDKENTTIVNGAGKKADIEARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKERKDRVDDAMHA 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 401 AKAAVEEGIVPGGGASLIhQARKALTELRASlTGDEVLGVDVFSEALAAPLFWIAANAGLDGSVVVNKVSELPA-GHGLN 479
Cdd:PRK14104 403 TRAAVEEGIVPGGGVALL-RASEQLKGIKTK-NDDQKTGVEIVRKALSAPARQIAINAGEDGSVIVGKILEKEQySYGFD 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 489513178 480 VNTLSYGDLAADGVIDPVKVTRSAVLNASSVARMVLTTETVVVDKPAKA 528
Cdd:PRK14104 481 SQTGEYGNLVSKGIIDPTKVVRTAIQNAASVAALLITTEAMVAELPKKG 529
|
|
| PLN03167 |
PLN03167 |
Chaperonin-60 beta subunit; Provisional |
8-523 |
6.93e-144 |
|
Chaperonin-60 beta subunit; Provisional
Pssm-ID: 215611 [Multi-domain] Cd Length: 600 Bit Score: 427.42 E-value: 6.93e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 8 DETARRAMEVGMDKLADTVRVTLGPRGRHVVLAKAFGGPTVTNDGVTVAREIELEDPFEDLGAQLVKSVATKTNDVAGDG 87
Cdd:PLN03167 64 DGSAIKKLQAGVNKLADLVGVTLGPKGRNVVLESKYGSPKIVNDGVTVAKEVELEDPVENIGAKLVRQAAAKTNDLAGDG 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 88 TTTATILAQALIKGGLRLVAAGVNPIALGVGIGKAADAVSEALLASATPVSgKTGIAQVATVSS-RDEQIGDLVGEAMSK 166
Cdd:PLN03167 144 TTTSVVLAQGLIAEGVKVVAAGANPVQITRGIEKTAKALVKELKKMSKEVE-DSELADVAAVSAgNNYEVGNMIAEAMSK 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 167 VGHDGVVSVEESSTLGTELEFTEGIGFDKGFLSAYFVTDFDNQQAVLEDALILLHQDKISSLPDLLPLLEKVAGTGKPLL 246
Cdd:PLN03167 223 VGRKGVVTLEEGKSAENNLYVVEGMQFDRGYISPYFVTDSEKMSVEYDNCKLLLVDKKITNARDLIGILEDAIRGGYPLL 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 247 IVAEDVEGEALATLVVNAIRKTLKAVAVKGPYFGDRRKAFLEDLAVVTGGQVVNPDAGMVLREVGLEVLGSARRVVVSKD 326
Cdd:PLN03167 303 IIAEDIEQEALATLVVNKLRGSLKIAALKAPGFGERKSQYLDDIAILTGGTVIREEVGLSLDKVGKEVLGTAAKVVLTKD 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 327 DTVIVDGGGTAEAVANRAKHLRAEIDKSDSDWDREKLGERLAKLAGGVAVIKVGAATETALKERKESVEDAVAAAKAAVE 406
Cdd:PLN03167 383 TTTIVGDGSTQEAVNKRVAQIKNLIEAAEQDYEKEKLNERIAKLSGGVAVIQVGAQTETELKEKKLRVEDALNATKAAVE 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 407 EGIVPGGGASLIHQARKaLTELRASLTGDE-VLGVDVFSEALAAPLFWIAANAGLDGSVVVNKV-SELPAGHGLNVNTLS 484
Cdd:PLN03167 463 EGIVVGGGCTLLRLASK-VDAIKDTLENDEqKVGADIVKRALSYPLKLIAKNAGVNGSVVSEKVlSNDNPKFGYNAATGK 541
|
490 500 510
....*....|....*....|....*....|....*....
gi 489513178 485 YGDLAADGVIDPVKVTRSAVLNASSVARMVLTTETVVVD 523
Cdd:PLN03167 542 YEDLMAAGIIDPTKVVRCCLEHAASVAKTFLTSDCVVVE 580
|
|
| chaperonin_type_I_II |
cd00309 |
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ... |
3-522 |
4.44e-119 |
|
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: 359.05 E-value: 4.44e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 3 KLIEYDETARRAMEVGMDKLADTVRVTLGPRGRHVVLAKAFGGPTVTNDGVTVAREIELEDPfedlGAQLVKSVATKTND 82
Cdd:cd00309 1 KEREFGEEARLSNINAAKALADAVKTTLGPKGMDKMLVDSLGDPTITNDGATILKEIEVEHP----AAKLLVEVAKSQDD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 83 VAGDGTTTATILAQALIKGGLRLVAAGVNPIALGVGIGKAADAVSEALLASATP--VSGKTGIAQVATVSSR-------D 153
Cdd:cd00309 77 EVGDGTTTVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVPidVEDREELLKVATTSLNsklvsggD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 154 EQIGDLVGEAMSKVGH------DGVVSVEES---STLGTELEftEGIGFDKGFLSAYFvtdfdnqQAVLEDALILLHQDK 224
Cdd:cd00309 157 DFLGELVVDAVLKVGKengdvdLGVIRVEKKkggSLEDSELV--VGMVFDKGYLSPYM-------PKRLENAKILLLDCK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 225 ISslpdllpllekvagtgkpLLIVAED-VEGEALATLVVnairktLKAVAVKgpyfgDRRKAFLEDLAVVTGGQVVNPda 303
Cdd:cd00309 228 LE------------------YVVIAEKgIDDEALHYLAK------LGIMAVR-----RVRKEDLERIAKATGATIVSR-- 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 304 gmvLREVGLEVLGSARRVVVSK----DDTVIVDGGGtaeavanrakhlraeidksdsdwdreklgerlaklaGGVAVIKV 379
Cdd:cd00309 277 ---LEDLTPEDLGTAGLVEETKigdeKYTFIEGCKG------------------------------------GKVATILL 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 380 GAATETALKERKESVE-DAVAAAKAAVEEGIVPGGGASLIHqARKALTELRASLTGDEVLGVDVFSEALAAPLFWIAANA 458
Cdd:cd00309 318 RGATEVELDEAERSLHdALCAVRAAVEDGGIVPGGGAAEIE-LSKALEELAKTLPGKEQLGIEAFADALEVIPRTLAENA 396
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489513178 459 GLDGSVVVNKVSELPAG----HGLNVNTLSYGDLAADGVIDPVKVTRSAVLNASSVARMVLTTETVVV 522
Cdd:cd00309 397 GLDPIEVVTKLRAKHAEgggnAGGDVETGEIVDMKEAGIIDPLKVKRQALKSATEAASLILTIDDIIV 464
|
|
| Cpn60_TCP1 |
pfam00118 |
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ... |
22-524 |
7.38e-65 |
|
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: 219.00 E-value: 7.38e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 22 LADTVRVTLGPRGRHVVLAKAFGGPTVTNDGVTVAREIELEDPfedlGAQLVKSVATKTNDVAGDGTTTATILAQALIKG 101
Cdd:pfam00118 1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELEIQHP----AAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 102 GLRLVAAGVNPIALGVGIGKAADAVSEALLA----SATPVSGKTgIAQVATVSSR-------DEQIGDLVGEAMS----- 165
Cdd:pfam00118 77 AEKLLAAGVHPTTIIEGYEKALEKALEILDSiisiPVEDVDRED-LLKVARTSLSskiisreSDFLAKLVVDAVLaipkn 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 166 ----KVGHDGVVSVEESSTLGTELEftEGIGFDKGFLSAYFVTDfdnqqavLEDALILLHQDKISSLPDLLPLL------ 235
Cdd:pfam00118 156 dgsfDLGNIGVVKILGGSLEDSELV--DGVVLDKGPLHPDMPKR-------LENAKVLLLNCSLEYEKTETKATvvlsda 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 236 ------------------EKVAGTGKPLLIVAEDVEGEALATLVVNAIRkTLKAVavkgpyfgdrRKAFLEDLAVVTGGQ 297
Cdd:pfam00118 227 eqlerflkaeeeqileivEKIIDSGVNVVVCQKGIDDLALHFLAKNGIM-ALRRV----------KKRDLERLAKATGAR 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 298 VVNPDAGMVlrevgLEVLGSARRV---VVSKDDTVIVDGGgtaeavanrakhlraeidksdsdwdreklgerlakLAGGV 374
Cdd:pfam00118 296 AVSSLDDLT-----PDDLGTAGKVeeeKIGDEKYTFIEGC-----------------------------------KSPKA 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 375 AVIKVGAATETALKERKESVE-DAVAAAKAAVEEGIVPGGGASLIHQARKaLTELRASLTGDEVLGVDVFSEALAAPLFW 453
Cdd:pfam00118 336 ATILLRGATDHVLDEIERSIHdALCVVKNAIEDPRVVPGGGAVEMELARA-LREYAKSVSGKEQLAIEAFAEALEVIPKT 414
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489513178 454 IAANAGLDGSVVVNKVSELPAG----HGLNVNTLSYGDLAADGVIDPVKVTRSAVLNASSVARMVLTTETVVVDK 524
Cdd:pfam00118 415 LAENAGLDPIEVLAELRAAHASgekhAGIDVETGEIIDMKEAGVVDPLKVKRQALKSATEAASTILRIDDIIKAK 489
|
|
| cpn60 |
cd03343 |
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ... |
22-515 |
7.01e-25 |
|
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: 108.12 E-value: 7.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 22 LADTVRVTLGPRGRHVVLAKAFGGPTVTNDGVTVAREIELEDPfedlGAQLVKSVATKTNDVAGDGTTTATILAQALIKG 101
Cdd:cd03343 27 VAEAVRTTLGPKGMDKMLVDSLGDVTITNDGATILKEMDIEHP----AAKMLVEVAKTQDEEVGDGTTTAVVLAGELLEK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 102 GLRLVAAGVNPIALGVGIGKAADAVSEALLASATPVS----------GKTGIAQVATVSSRDeQIGDLVGEAMSKVGHDG 171
Cdd:cd03343 103 AEDLLDQNIHPTVIIEGYRLAAEKALELLDEIAIKVDpddkdtlrkiAKTSLTGKGAEAAKD-KLADLVVDAVLQVAEKR 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 172 ------------VVSVEESSTLGTELefTEGIGFDKGFLSayfvtdfDNQQAVLEDALILLHQDKISS------------ 227
Cdd:cd03343 182 dgkyvvdldnikIEKKTGGSVDDTEL--IRGIVIDKEVVH-------PGMPKRVENAKIALLDAPLEVkkteidakirit 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 228 ------------LPDLLPLLEKVAGTGKPLLIVAEDVEGEA---LATLVVNAIRKtlkavaVKgpyfgdrrKAFLEDLAV 292
Cdd:cd03343 253 spdqlqafleqeEAMLKEMVDKIADTGANVVFCQKGIDDLAqhyLAKAGILAVRR------VK--------KSDMEKLAR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 293 VTGGQVVNPdagmvLREVGLEVLGSARRVV---VSKDDTVIVDGGGTAEAVA----NRAKHLRAEIDKSDSDwdreklge 365
Cdd:cd03343 319 ATGAKIVTN-----IDDLTPEDLGEAELVEerkVGDDKMVFVEGCKNPKAVTillrGGTEHVVDELERALED-------- 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 366 rlaklagGVAVIKVgaatetALKERKesvedavaaakaaveegIVPGGGASLIHQARKaLTELRASLTGDEVLGVDVFSE 445
Cdd:cd03343 386 -------ALRVVAD------ALEDGK-----------------VVAGGGAVEIELAKR-LREYARSVGGREQLAVEAFAD 434
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489513178 446 ALAAPLFWIAANAGLDGsvvVNKVSELPAGH-------GLNVNTLSYGDLAADGVIDPVKVTRSAVLNASSVARMVL 515
Cdd:cd03343 435 ALEEIPRTLAENAGLDP---IDTLVELRAAHekgnknaGLDVYTGEVVDMLEKGVIEPLRVKKQAIKSATEAATMIL 508
|
|
| thermosome_arch |
TIGR02339 |
thermosome, various subunits, archaeal; Thermosome is the name given to the archaeal rather ... |
22-521 |
2.38e-24 |
|
thermosome, various subunits, archaeal; Thermosome is the name given to the archaeal rather than eukaryotic form of the group II chaperonin (counterpart to the group I chaperonin, GroEL/GroES, in bacterial), a torroidal, ATP-dependent molecular chaperone that assists in the folding or refolding of nascent or denatured proteins. Various homologous subunits, one to five per archaeal genome, may be designated alpha, beta, etc., but phylogenetic analysis does not show distinct alpha subunit and beta subunit lineages traceable to ancient paralogs. [Protein fate, Protein folding and stabilization]
Pssm-ID: 274080 Cd Length: 519 Bit Score: 106.31 E-value: 2.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 22 LADTVRVTLGPRGRHVVLAKAFGGPTVTNDGVTVAREIELEDPfedlGAQLVKSVATKTNDVAGDGTTTATILAQALIKG 101
Cdd:TIGR02339 28 VAEAVKSTLGPRGMDKMLVDSLGDVTITNDGATILKEMDIEHP----AAKMLVEVAKTQDEEVGDGTTTAVVLAGELLEK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 102 GLRLVAAGVNPIALGVGIGKAADAVSEALLASATPVS----------GKTGIAQVATVSSRDEQIGDLVGEAMSKVGH-- 169
Cdd:TIGR02339 104 AEDLLEQDIHPTVIIEGYRKAAEKALEIIDEIATKISpedrdllkkiAYTSLTSKASAEVAKDKLADLVVEAVKQVAElr 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 170 -DGVVSVE------ESSTLGT--ELEFTEGIGFDKGFLSAYFVTDFDNQQAVLEDALILLHQDKISS------------- 227
Cdd:TIGR02339 184 gDGKYYVDldnikiVKKKGGSieDTELVEGIVVDKEVVHPGMPKRVENAKIALLDAPLEVEKTEIDAkiritdpdqikkf 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 228 ----LPDLLPLLEKVAGTGKPLLIVAEDVEGEALATLVVNAIrktlkaVAVKgpyfgDRRKAFLEDLAVVTGGQVVNPda 303
Cdd:TIGR02339 264 ldqeEAMLKEMVDKIASAGANVVICQKGIDDVAQHYLAKAGI------LAVR-----RVKKSDIEKLARATGARIVSS-- 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 304 gmvLREVGLEVLGSARRVV---VSKDDTVIVDGGGTAEAVAnrakhlraeidksdsdwdreklgerlaklaggvavIKVG 380
Cdd:TIGR02339 331 ---IDEITESDLGYAELVEerkVGEDKMVFVEGCKNPKAVT-----------------------------------ILLR 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 381 AATETALKERKESVEDAVAAAKAAVEEG-IVPGGGASLIHQARKaLTELRASLTGDEVLGVDVFSEALAAPLFWIAANAG 459
Cdd:TIGR02339 373 GGTEHVVDELERSIQDALHVVANALEDGkIVAGGGAVEIELALR-LRSYARSVGGREQLAIEAFADALEEIPRILAENAG 451
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489513178 460 LDGsvvVNKVSELPAGH-------GLNVNTLSYGDLAADGVIDPVKVTRSAVLNASSVARMVLTTETVV 521
Cdd:TIGR02339 452 LDP---IDALVDLRAKHekgnknaGINVFTGEIEDMLELGVIEPLRVKEQAIKSATEAATMILRIDDVI 517
|
|
| thermosome_beta |
NF041083 |
thermosome subunit beta; |
22-524 |
3.87e-24 |
|
thermosome subunit beta;
Pssm-ID: 469010 Cd Length: 519 Bit Score: 105.80 E-value: 3.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 22 LADTVRVTLGPRGRHVVLAKAFGGPTVTNDGVTVAREIELEDPfedlGAQLVKSVATKTNDVAGDGTTTATILAQALIKG 101
Cdd:NF041083 29 VAEAVRTTLGPKGMDKMLVDSLGDIVITNDGATILKEMDVQHP----AAKMLVEVAKTQDDEVGDGTTTAVVLAGELLKK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 102 GLRLVAAGVNPIALGVGIGKAADAVSEALLASATPVS----------GKTGIAQVATVSSRDEqIGDLVGEAMSKVGH-- 169
Cdd:NF041083 105 AEELLDQNIHPTIIANGYRLAAEKAIEILDEIAEKVDpddretlkkiAETSLTSKGVEEARDY-LAEIAVKAVKQVAEkr 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 170 DGVVSVEES----------STLGTELefTEGIGFDK----------------GFLSAYF------------VTDFDNQQA 211
Cdd:NF041083 184 DGKYYVDLDniqiekkhggSIEDTQL--IYGIVIDKevvhpgmpkrvenakiALLDAPLevkkteidaeirITDPDQLQK 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 212 VLEDALILLHQdkisslpdllpLLEKVAGTGKPLLIVA---EDVEGEALATLVVNAIRKTlkavavkgpyfgdrRKAFLE 288
Cdd:NF041083 262 FLDQEEKMLKE-----------MVDKIKATGANVVFCQkgiDDLAQHYLAKAGILAVRRV--------------KKSDME 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 289 DLAVVTGGQVVNPdagmvLREVGLEVLGSARRV---VVSKDDTVIVDGGGTAEAVA----NRAKHLRAEIDKSDSDwdre 361
Cdd:NF041083 317 KLAKATGARIVTN-----IDDLTPEDLGYAELVeerKVGDDKMVFVEGCKNPKAVTilirGGTEHVVDEAERALED---- 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 362 klgerlaklaggvAVIKVGAATETAlkerkesvedavaaakaaveeGIVPGGGASLIHQArKALTELRASLTGDEVLGVD 441
Cdd:NF041083 388 -------------ALSVVADAVEDG---------------------KIVAGGGAPEVELA-KRLREYAATVGGREQLAVE 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 442 VFSEALAAPLFWIAANAGLDGsvvVNKVSELPAGH-------GLNVNTLSYGDLAADGVIDPVKVTRSAVLNASSVARMV 514
Cdd:NF041083 433 AFAEALEIIPRTLAENAGLDP---IDILVKLRSAHekgkkwaGINVFTGEVVDMWELGVIEPLRVKTQAIKSATEAATMI 509
|
570
....*....|
gi 489513178 515 LTTETVVVDK 524
Cdd:NF041083 510 LRIDDVIAAK 519
|
|
| chaperonin_like |
cd03333 |
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ... |
143-393 |
1.08e-22 |
|
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: 96.00 E-value: 1.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 143 IAQVATVSSR------DEQIGDLVGEAMSKVGHD------GVVSVEES---STLGTELEftEGIGFDKGFLSAYFVTdfd 207
Cdd:cd03333 4 LLQVATTSLNsklsswDDFLGKLVVDAVLKVGPDnrmddlGVIKVEKIpggSLEDSELV--VGVVFDKGYASPYMPK--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 208 nqqaVLEDALILLHQDKISslpdllpllekvagtgkpLLIVAED-VEGEALATLVVnairktLKAVAVKgpyfgDRRKAF 286
Cdd:cd03333 79 ----RLENAKILLLDCPLE------------------YVVIAEKgIDDLALHYLAK------AGIMAVR-----RVKKED 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 287 LEDLAVVTGGQVVNPdagmvLREVGLEVLGSARRVVVSKD----DTVIVDGGGtaeavanrakhlraeidksdsdwdrek 362
Cdd:cd03333 126 LERIARATGATIVSS-----LEDLTPEDLGTAELVEETKIgeekLTFIEGCKG--------------------------- 173
|
250 260 270
....*....|....*....|....*....|.
gi 489513178 363 lgerlaklaGGVAVIKVGAATETALKERKES 393
Cdd:cd03333 174 ---------GKAATILLRGATEVELDEVKRS 195
|
|
| thermosome_alpha |
NF041082 |
thermosome subunit alpha; |
22-515 |
5.91e-22 |
|
thermosome subunit alpha;
Pssm-ID: 469009 Cd Length: 518 Bit Score: 99.19 E-value: 5.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 22 LADTVRVTLGPRGRHVVLAKAFGGPTVTNDGVTVAREIELEDPfedlGAQLVKSVATKTNDVAGDGTTTATILAQALIKG 101
Cdd:NF041082 29 VAEAVRTTLGPKGMDKMLVDSLGDVVITNDGVTILKEMDIEHP----AAKMIVEVAKTQDDEVGDGTTTAVVLAGELLKK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 102 GLRLVAAGVNPIALGVGIGKAADAVSEALLASATPVSGK-----TGIAQVAT----VSSRDEQIGDLVGEAMSKVGHDG- 171
Cdd:NF041082 105 AEELLDQDIHPTIIAEGYRLAAEKALEILDEIAIKVDPDdketlKKIAATAMtgkgAEAAKDKLADLVVDAVKAVAEKDg 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 172 ----------VVSVEESSTLGTELefTEGIGFDK----------------GFLSAYF------------VTDFDNQQAVL 213
Cdd:NF041082 185 gynvdldnikVEKKVGGSIEDSEL--VEGVVIDKervhpgmpkrvenakiALLDAPLevkkteidakisITDPDQLQAFL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 214 EDALILLHQdkisslpdllpLLEKVAGTGKPLLIVA---EDVEGEALATLVVNAIRKTlkavavkgpyfgdrRKAFLEDL 290
Cdd:NF041082 263 DQEEKMLKE-----------MVDKIADSGANVVFCQkgiDDLAQHYLAKEGILAVRRV--------------KKSDMEKL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 291 AVVTGGQVVNPdagmvLREVGLEVLGSARRVV---VSKDDTVIVDGGGTAEAVA----NRAKHLRAEIDKSDSDwdrekl 363
Cdd:NF041082 318 AKATGARIVTS-----IDDLSPEDLGYAGLVEerkVGGDKMIFVEGCKNPKAVTillrGGTEHVVDEVERALED------ 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 364 gerlaklaggvaVIKVgaaTETALKERKesvedavaaakaaveegIVPGGGASLIHQARKaLTELRASLTGDEVLGVDVF 443
Cdd:NF041082 387 ------------ALRV---VRVVLEDGK-----------------VVAGGGAPEVELALR-LREYAASVGGREQLAIEAF 433
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489513178 444 SEALAAPLFWIAANAGLDGsvvVNKVSELPAGH-------GLNVNTLSYGDLAADGVIDPVKVTRSAVLNASSVARMVL 515
Cdd:NF041082 434 AEALEIIPRTLAENAGLDP---IDALVELRSAHekgnktaGLDVYTGKVVDMLEIGVVEPLRVKTQAIKSATEAAVMIL 509
|
|
| TCP1_beta |
cd03336 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ... |
6-527 |
3.40e-21 |
|
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: 97.01 E-value: 3.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 6 EYDETARRAMEVGMDKLADTVRVTLGPRGRHVVL--AKAFGGPTVTNDGVTVAREIELEDPfedlGAQLVKSVATKTNDV 83
Cdd:cd03336 9 EKGETARLSSFVGAIAIGDLVKTTLGPKGMDKILqsVGRSGGVTVTNDGATILKSIGVDNP----AAKVLVDISKVQDDE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 84 AGDGTTTATILAQALIKGGLRLVAAGVNPIALGVGIGKAADAVSEALLASATPVSG-----KTGIAQVA--TVSSRdeqI 156
Cdd:cd03336 85 VGDGTTSVTVLAAELLREAEKLVAQKIHPQTIIEGYRMATAAAREALLSSAVDHSSdeeafREDLLNIArtTLSSK---I 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 157 GDLVGEAMSKVGHDGVVSVEESstlgTELEFTEGIGFDKG-----FLSAYFVTDFD---NQQAVLEDALIL-----LHQD 223
Cdd:cd03336 162 LTQDKEHFAELAVDAVLRLKGS----GNLDAIQIIKKLGGslkdsYLDEGFLLDKKigvNQPKRIENAKILiantpMDTD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 224 KISSLPDLLplleKVAGTGKplliVAEDVEGEALatlvvNAIRKTLKAVAVKGPYFGDRRKAF----------------- 286
Cdd:cd03336 238 KIKIFGAKV----RVDSTAK----VAEIEEAEKE-----KMKNKVEKILKHGINCFINRQLIYnypeqlfadagimaieh 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 287 -----LEDLAVVTGGQVV----NPDagmvlrevgLEVLGSARRV--VVSKDDTVIVDGG---GTAEAVANR--AKHLRAE 350
Cdd:cd03336 305 adfdgVERLALVTGGEIAstfdHPE---------LVKLGTCKLIeeIMIGEDKLIRFSGvaaGEACTIVLRgaSQQILDE 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 351 IDKSdsdwdrekLGERLAKLAGGVAVIKVgaatetalkerkesvedavaaakaaveegiVPGGGASLIHQArKALTELRA 430
Cdd:cd03336 376 AERS--------LHDALCVLAQTVKDTRV------------------------------VLGGGCSEMLMA-KAVEELAK 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 431 SLTGDEVLGVDVFSEALAAPLFWIAANAGLDGSVVvnkVSELPAGH-------GLNVNTLSYGDLAADGVIDPVKVTRSA 503
Cdd:cd03336 417 KTPGKKSLAIEAFAKALRQLPTIIADNAGYDSAEL---VAQLRAAHyngnttaGLDMRKGTVGDMKELGITESFKVKRQV 493
|
570 580
....*....|....*....|....
gi 489513178 504 VLNASSVARMVLTTETVVVDKPAK 527
Cdd:cd03336 494 LLSASEAAEMILRVDDIIKCAPRK 517
|
|
| TCP1_delta |
cd03338 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ... |
22-515 |
1.10e-15 |
|
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: 79.64 E-value: 1.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 22 LADTVRVTLGPRGRHVVLAKAFGGPTVTNDGVTVAREIELEDPFEDLGAQLvksvaTKTNDV-AGDGTTTATILAQALIK 100
Cdd:cd03338 20 VADAIRTSLGPRGMDKMIQTGKGEVIITNDGATILKQMSVLHPAAKMLVEL-----SKAQDIeAGDGTTSVVVLAGALLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 101 GGLRLVAAGVNPIALGVGIGKAADAVSEALLASATPVS---GKTGIAQVAT------VSSRDEQIGDLVGEAMSKVGHDG 171
Cdd:cd03338 95 ACESLLKKGIHPTVISESFQIAAKKAVEILDSMSIPVDlndRESLIKSATTslnskvVSQYSSLLAPIAVDAVLKVIDPA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 172 VVS------VEESSTLGTELEFTE---GIGFDKGF---------------------LSAYfVTDFDNQQAVLEDALIllh 221
Cdd:cd03338 175 TATnvdlkdIRIVKKLGGTIEDTElvdGLVFTQKAskkaggptriekakigliqfcLSPP-KTDMDNNIVVNDYAQM--- 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 222 qDKISSL--PDLLPLLEKVAGTGKPLLIVAEDVEGEALATLVVNAIRKtLKAVAVKgpyfgDRRKAFLEDLAVVTGGQ-V 298
Cdd:cd03338 251 -DRILREerKYILNMCKKIKKSGCNVLLIQKSILRDAVSDLALHFLAK-LKIMVVK-----DIEREEIEFICKTIGCKpV 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 299 VNPDagmvlrEVGLEVLGSARRV-VVSKDDTVIVDGGGTAEAVANRAKHLRAEidksdsdwDREKLGERLAKLAGGVAVI 377
Cdd:cd03338 324 ASID------HFTEDKLGSADLVeEVSLGDGKIVKITGVKNPGKTVTILVRGS--------NKLVLDEAERSLHDALCVI 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 378 KvgaatetALKERKesvedavaaakaaveeGIVPGGGASLIHQARKaLTELRASLTGDEVLGVDVFSEALAAPLFWIAAN 457
Cdd:cd03338 390 R-------CLVKKR----------------ALIPGGGAPEIEIALQ-LSEWARTLTGVEQYCVRAFADALEVIPYTLAEN 445
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489513178 458 AGLDGsvvVNKVSELPAGH-------GLNVNTLSYGDLAADGVIDPVKVTRSAVLNASSVARMVL 515
Cdd:cd03338 446 AGLNP---ISIVTELRNRHaqgeknaGINVRKGAITNILEENVVQPLLVSTSAITLATETVRMIL 507
|
|
| chap_CCT_beta |
TIGR02341 |
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ... |
6-528 |
1.27e-15 |
|
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: 79.52 E-value: 1.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 6 EYDETARRAMEVGMDKLADTVRVTLGPRGRHVVL--AKAFGGPTVTNDGVTVAREIELEDPfedlGAQLVKSVATKTNDV 83
Cdd:TIGR02341 10 ERAENARLSSFVGAIAIGDLVKSTLGPKGMDKILqsSSSDASIMVTNDGATILKSIGVDNP----AAKVLVDMSKVQDDE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 84 AGDGTTTATILAQALIKGGLRLVAAGVNPIALGVGIGKAADAVSEALLASAT-----PVSGKTGIAQVA--TVSSR---- 152
Cdd:TIGR02341 86 VGDGTTSVTVLAAELLREAEKLINQKIHPQTIIAGYREATKAARDALLKSAVdngsdEVKFRQDLMNIArtTLSSKilsq 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 153 -DEQIGDLVGEAMSKV-GHDGVVSVEESSTLGTELEFTEgigFDKGFLSAYFVTdfDNQQAVLEDALIL-----LHQDKI 225
Cdd:TIGR02341 166 hKDHFAQLAVDAVLRLkGSGNLEAIQIIKKLGGSLADSY---LDEGFLLDKKIG--VNQPKRIENAKILiantgMDTDKV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 226 SSLPDLLplleKVAGTGKplLIVAEDVEGEALATLVVNAIRKTLKAVAVKGPYFGDRRKAF---------------LEDL 290
Cdd:TIGR02341 241 KIFGSRV----RVDSTAK--VAELEHAEKEKMKEKVEKILKHGINCFINRQLIYNYPEQLFadagvmaiehadfegVERL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 291 AVVTGGQVVNpdagmVLREVGLEVLGSAR---RVVVSKDDTVIVDGGGTAEAVANRakhLRAEIDKSDSDWDREkLGERL 367
Cdd:TIGR02341 315 ALVTGGEIVS-----TFDHPELVKLGSCDlieEIMIGEDKLLKFSGVKLGEACTIV---LRGATQQILDEAERS-LHDAL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 368 AKLAggvavikvgaateTALKERKesvedavaaakaaveegIVPGGGASLIHQArKALTELRASLTGDEVLGVDVFSEAL 447
Cdd:TIGR02341 386 CVLS-------------QTVKESR-----------------TVLGGGCSEMLMS-KAVTQEAQRTPGKEALAVEAFARAL 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 448 AAPLFWIAANAGLDGSVVvnkVSELPAGH-------GLNVNTLSYGDLAADGVIDPVKVTRSAVLNASSVARMVLTTETV 520
Cdd:TIGR02341 435 RQLPTIIADNAGFDSAEL---VAQLRAAHyngnttmGLDMNEGTIADMRQLGITESYKVKRAVVSSAAEAAEVILRVDNI 511
|
....*...
gi 489513178 521 VVDKPAKA 528
Cdd:TIGR02341 512 IKAAPRKR 519
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
9-529 |
1.43e-15 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 79.30 E-value: 1.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 9 ETARRAMEVGMDKLADTVRVTLGPRGRHVVLAKAFGGP-----TVTNDGVTVAREIELEDPfedlGAQLVKSVATKTNDV 83
Cdd:PTZ00212 21 ETARLQSFVGAIAVADLVKTTLGPKGMDKILQPMSEGPrsgnvTVTNDGATILKSVWLDNP----AAKILVDISKTQDEE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 84 AGDGTTTATILAQALIKGGLRLVAAGVNPIALGVGIGKAADAVSEALLASATPVSG-----KTGIAQVA--TVSSRdeqI 156
Cdd:PTZ00212 97 VGDGTTSVVVLAGELLREAEKLLDQKIHPQTIIEGWRMALDVARKALEEIAFDHGSdeekfKEDLLNIArtTLSSK---L 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 157 GDLVGEAMSKVGHDGVVSVEESSTLgTELEFTEGIG-------FDKGFLSAYFVTdfDNQQAVLEDALIL-----LHQDK 224
Cdd:PTZ00212 174 LTVEKDHFAKLAVDAVLRLKGSGNL-DYIQIIKKPGgtlrdsyLEDGFILEKKIG--VGQPKRLENCKILvantpMDTDK 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 225 I-----------SSLPDLLPLLEKVAGTGKPLLIVAEDVEGEALATLVVNAIRKTLKAVAVKGPYFGDrrkaF--LEDLA 291
Cdd:PTZ00212 251 IkiygakvkvdsMEKVAEIEAAEKEKMKNKVDKILAHGCNVFINRQLIYNYPEQLFAEAGIMAIEHAD----FdgMERLA 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 292 VVTGGQVV----NPDagmvlrevgLEVLGSARRV--VVSKDDTVIVDGG---GTAEAVANR--AKHLRAEIDKSdsdwdr 360
Cdd:PTZ00212 327 AALGAEIVstfdTPE---------KVKLGHCDLIeeIMIGEDKLIRFSGcakGEACTIVLRgaSTHILDEAERS------ 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 361 ekLGERLAKLAggvavikvgaateTALKERKesvedavaaakaaveegIVPGGGASLIHQArKALTELRASLTGDEVLGV 440
Cdd:PTZ00212 392 --LHDALCVLS-------------QTVKDTR-----------------VVLGGGCSEMLMA-NAVEELAKKVEGKKSLAI 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 441 DVFSEALAAPLFWIAANAGLDGSVVVNKV-SELPAGH---GLNVNTLSYGDLAADGVIDPVKVTRSAVLNASSVARMVLT 516
Cdd:PTZ00212 439 EAFAKALRQIPTIIADNGGYDSAELVSKLrAEHYKGNktaGIDMEKGTVGDMKELGITESYKVKLSQLCSATEAAEMILR 518
|
570
....*....|...
gi 489513178 517 TETVVVDKPAKAE 529
Cdd:PTZ00212 519 VDDIIRCAPRQRE 531
|
|
| chap_CCT_delta |
TIGR02342 |
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ... |
22-521 |
1.82e-13 |
|
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: 72.89 E-value: 1.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 22 LADTVRVTLGPRGRHVVLAKAFGGPTVTNDGVTVAREIELEDPfedlGAQLVKSVATKTNDVAGDGTTTATILAQALIKG 101
Cdd:TIGR02342 21 VADAIRTSLGPKGMDKMIQDGKGEVIITNDGATILKQMAVLHP----AAKMLVELSKAQDIEAGDGTTSVVILAGALLGA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 102 GLRLVAAGVNPIALGVGIGKAADAVSEALLASATPVS-GKTGIAQVATVSSRDEQIGDLVGEAMSKVGHDGVVSVEESST 180
Cdd:TIGR02342 97 CERLLNKGIHPTIISESFQSAADEAIKILDEMSIPVDlSDREQLLKSATTSLSSKVVSQYSSLLAPLAVDAVLKVIDPEN 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 181 L---------------GT--ELEFTEGIGFDKGFLSA---------------YFV-----TDFDNqQAVLEDaliLLHQD 223
Cdd:TIGR02342 177 AknvdlndikvvkklgGTidDTELIEGLVFTQKASKSaggptriekakigliQFQisppkTDMEN-QIIVND---YAQMD 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 224 KISSLPDL--LPLLEKVAGTGKPLLIVAEDVEGEALATLVVNAIRKtLKAVAVKGPyfgDRrkaflEDLAVVTGGQVVNP 301
Cdd:TIGR02342 253 RVLKEERAyiLNIVKKIKKTGCNVLLIQKSILRDAVNDLALHFLAK-MKIMVVKDI---ER-----EEIEFICKTIGCKP 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 302 DAGmvLREVGLEVLGSARRVV-VSKDDTVIVDGGGtaeaVANRAKHLRAEIDKSDSdwdrEKLGERLAKLAGGVAVIKvg 380
Cdd:TIGR02342 324 IAS--IDHFTADKLGSAELVEeVDSDGGKIIKITG----IQNAGKTVTVVVRGSNK----LVIDEAERSLHDALCVIR-- 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 381 aateTALKERkesvedavaaakaaveeGIVPGGGASLIHQARKaLTELRASLTGDEVLGVDVFSEALAAPLFWIAANAGL 460
Cdd:TIGR02342 392 ----CLVKKR-----------------GLIAGGGAPEIEIARR-LSKYARTMKGVESYCVRAFADALEVIPYTLAENAGL 449
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489513178 461 DGsvvVNKVSELPAGH-------GLNVNTLSYGDLAADGVIDPVKVTRSAVLNASSVARMVLTTETVV 521
Cdd:TIGR02342 450 NP---IKVVTELRNRHangektaGISVRKGGITNMLEEHVLQPLLVTTSAITLASETVRSILKIDDIV 514
|
|
| chap_CCT_epsi |
TIGR02343 |
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ... |
22-130 |
2.50e-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: 69.06 E-value: 2.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 22 LADTVRVTLGPRGRHVVLAKAFGGPTVTNDGVTVAREIELEDPFEDLGAQLVKSvatkTNDVAGDGTTTATILAQALIKG 101
Cdd:TIGR02343 39 VASILRTSLGPKGMDKMLISPDGDITVTNDGATILSQMDVDNQIAKLMVELSKS----QDDEIGDGTTGVVVLAGALLEQ 114
|
90 100
....*....|....*....|....*....
gi 489513178 102 GLRLVAAGVNPIALGVGIGKAADAVSEAL 130
Cdd:TIGR02343 115 AEELLDKGIHPIKIADGFEEAARIAVEHL 143
|
|
| TCP1_epsilon |
cd03339 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ... |
22-138 |
1.85e-11 |
|
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: 66.55 E-value: 1.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 22 LADTVRVTLGPRGRHVVLAKAFGGPTVTNDGVTVAREIELEDPFEDLGAQLVKSvatkTNDVAGDGTTTATILAQALIKG 101
Cdd:cd03339 35 VANILRTSLGPRGMDKILVSPDGEVTVTNDGATILEKMDVDHQIAKLLVELSKS----QDDEIGDGTTGVVVLAGALLEQ 110
|
90 100 110
....*....|....*....|....*....|....*..
gi 489513178 102 GLRLVAAGVNPIALGVGIGKAADAVSEALLASATPVS 138
Cdd:cd03339 111 AEKLLDRGIHPIRIADGYEQACKIAVEHLEEIADKIE 147
|
|
| chap_CCT_eta |
TIGR02345 |
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ... |
21-524 |
1.38e-10 |
|
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: 63.62 E-value: 1.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 21 KLADTVRVTLGPRGRHVVLAKAFGGPTVTNDGVTVAREIELEDPfedlGAQLVKSVATKTNDVAGDGTTTATILAQALIK 100
Cdd:TIGR02345 29 AIAEALKTTLGPRGMDKLIVGSNGKATISNDGATILKLLDIVHP----AAKTLVDIAKSQDAEVGDGTTSVTILAGELLK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 101 GGLRLVAAGVNPIALGVGIGKAADAVSEALLASATPVSGKTG-----IAQVATVSSRDEQIGDlVGEAMSKVGHDGVVSV 175
Cdd:TIGR02345 105 EAKPFIEEGVHPQLIIRCYREALSLAVEKIKEIAVTIDEEKGeqrelLEKCAATALSSKLISH-NKEFFSKMIVDAVLSL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 176 E----ESSTLG---------TELEFTEGIGFDKGFLSAyfvtDFDNQQAVLEDALILLHQDKISSLPDLLPLLEKVAGTG 242
Cdd:TIGR02345 184 DrddlDLKLIGikkvqggalEDSQLVNGVAFKKTFSYA----GFEQQPKKFANPKILLLNVELELKAEKDNAEIRVEDVE 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 243 KPLLIVaeDVEGEALATLVVNAIRKTLKAVAVKGPyFGDRRKAFLEDLAVVTGGQVVNPDAGMVLREVGLEVLGSA---- 318
Cdd:TIGR02345 260 DYQAIV--DAEWAIIFRKLEKIVESGANVVLSKLP-IGDLATQYFADRDIFCAGRVSAEDLKRVIKACGGSIQSTTsdle 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 319 ------------RRVVV-----------SKDDTVIVDGGgtaeavanrAKHLRAEIDKSDSDwdreklgerlaklaggvA 375
Cdd:TIGR02345 337 advlgtcalfeeRQIGSerynyftgcphAKTCTIILRGG---------AEQFIEEAERSLHD-----------------A 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 376 VIKVgaatETALKERKesvedavaaakaaveegIVPGGGASLIhQARKALTELRASLTGDEVLGVDVFSEALAAPLFWIA 455
Cdd:TIGR02345 391 IMIV----RRALKNKK-----------------IVAGGGAIEM-ELSKCLRDYSKTIDGKQQLIINAFAKALEIIPRQLC 448
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489513178 456 ANAGLDGSVVVNKVSELPAG----HGLNVNTLSYGDLAADGVIDPVKVTRSAVLNASSVARMVLTTETVVVDK 524
Cdd:TIGR02345 449 ENAGFDSIEILNKLRSRHAKggkwYGVDINTEDIGDNFEAFVWEPALVKINALKAAFEAACTILSVDETITNP 521
|
|
| TCP1_eta |
cd03340 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ... |
21-141 |
2.36e-10 |
|
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.
Pssm-ID: 239456 [Multi-domain] Cd Length: 522 Bit Score: 63.08 E-value: 2.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 21 KLADTVRVTLGPRGRHVVLAKAFGGPTVTNDGVTVAREIELEDPfedlGAQLVKSVATKTNDVAGDGTTTATILAQALIK 100
Cdd:cd03340 27 AIADAVRTTLGPRGMDKLIVDGRGKVTISNDGATILKLLDIVHP----AAKTLVDIAKSQDAEVGDGTTSVVVLAGEFLK 102
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 489513178 101 GGLRLVAAGVNPIALGVGIGKAADAVSEALLASATPVSGKT 141
Cdd:cd03340 103 EAKPFIEDGVHPQIIIRGYRKALQLAIEKIKEIAVNIDKED 143
|
|
| chap_CCT_alpha |
TIGR02340 |
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ... |
19-182 |
7.57e-10 |
|
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT alpha chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.
Pssm-ID: 274081 [Multi-domain] Cd Length: 536 Bit Score: 61.27 E-value: 7.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 19 MDKLADTVRVTLGPRGRHVVLAKAFGGPTVTNDGVTVAREIELEDPfedlGAQLVKSVATKTNDVAGDGTTTATILAQAL 98
Cdd:TIGR02340 21 AMAIANIVKTSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHP----AAKILVELAQLQDREVGDGTTSVVIIAAEL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 99 IKGGLRLVAAGVNPIALGVG----IGKAADAVSEALLASATPVsGKTGIAQVATVSSRDEQIGdLVGEAMSKVGHDGVVS 174
Cdd:TIGR02340 97 LKRADELVKNKIHPTSVISGyrlaCKEAVKYIKENLSVSVDEL-GREALINVAKTSMSSKIIG-LDSDFFSNIVVDAVLA 174
|
....*...
gi 489513178 175 VEESSTLG 182
Cdd:TIGR02340 175 VKTTNENG 182
|
|
| TCP1_alpha |
cd03335 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ... |
9-112 |
1.50e-08 |
|
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: 57.29 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 9 ETARRAMEVGMDKLADTVRVTLGPRGRHVVLAKAFGGPTVTNDGVTVAREIELEDPfedlGAQLVKSVATKTNDVAGDGT 88
Cdd:cd03335 7 QDVRTQNVTAAMAIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHP----AAKILVELAQLQDKEVGDGT 82
|
90 100
....*....|....*....|....
gi 489513178 89 TTATILAQALIKGGLRLVAAGVNP 112
Cdd:cd03335 83 TSVVIIAAELLKRANELVKQKIHP 106
|
|
| chap_CCT_zeta |
TIGR02347 |
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ... |
9-130 |
3.72e-08 |
|
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT zeta chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.
Pssm-ID: 274088 [Multi-domain] Cd Length: 531 Bit Score: 55.90 E-value: 3.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 9 ETARR--AMEVGMDK---LADTVRVTLGPRGRHVVLAKAFGGPTVTNDGVTVAREIELEDPfedlGAQLVKSVATKTNDV 83
Cdd:TIGR02347 10 ESLRRdaALMMNINAargLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEMQIQHP----TASMIARAATAQDDI 85
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 489513178 84 AGDGTTTATILAQALIKGGLRLVAAGVNPIALGVGIGKAADAVSEAL 130
Cdd:TIGR02347 86 TGDGTTSTVLLIGELLKQAERYILEGVHPRIITEGFEIARKEALQFL 132
|
|
| chap_CCT_theta |
TIGR02346 |
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ... |
22-526 |
4.11e-07 |
|
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: 52.80 E-value: 4.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 22 LADTVRVTLGPRGRHVVLAKAFGGPTVTNDGVTVAREIELEDPFEDLgaqLVKSVATKTNDVaGDGTTTATILAQALIKG 101
Cdd:TIGR02346 30 LSQITRTSLGPNGMNKMVINHLEKLFVTNDAATILRELEVQHPAAKL---LVMASEMQENEI-GDGTNLVLVLAGELLNK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 102 GLRLVAAGVNPIALGVGIGKAADAVSEAL----LASATPVSGKTGIAQVATVSSRDEQIG------DLVGEAMS-----K 166
Cdd:TIGR02346 106 AEELIRMGLHPSEIIKGYEMALKKAMEILeelvVWEVKDLRDKDELIKALKASISSKQYGnedflaQLVAQACStvlpkN 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 167 VGHDGVVSVEESSTLGTELEFTEgigFDKGFLsayFVTDFDNQQAVLEDALILLHQDKISSLPDLLPllekvagtGKPLL 246
Cdd:TIGR02346 186 PQNFNVDNIRVCKILGGSLSNSE---VLKGMV---FNREAEGSVKSVKNAKVAVFSCPLDTATTETK--------GTVLI 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 247 IVAEDVEG-----EALATLVVNAIRKTLKAVAVKGPYFGDRRKAFLEDLAVVTGG-----------QVVNPDAGMVLREV 310
Cdd:TIGR02346 252 HNAEELLNyskgeENQIEAMIKAIADSGVNVIVTGGSVGDMALHYLNKYNIMVLKipskfelrrlcKTVGATPLPRLGAP 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 311 GLEVLGSARRVVVSK--DDTVIV-----DGGGTAEAVanrakhLRAEIDKSDSDWDReklgerlaKLAGGVAVIKVgaat 383
Cdd:TIGR02346 332 TPEEIGYVDSVYVSEigGDKVTVfkqenGDSKISTII------LRGSTDNLLDDIER--------AIDDGVNTVKA---- 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 384 etALKERKesvedavaaakaaveegIVPGGGASLIHQARKaLTELRASLTGDEVLGVDVFSEALAAPLFWIAANAGLDGS 463
Cdd:TIGR02346 394 --LVKDGR-----------------LLPGAGATEIELASR-LTKYGEKLPGLDQYAIKKFAEAFEIIPRTLAENAGLNAN 453
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489513178 464 VVVNKvseLPAGH-------GLNVNTLSYG--DLAADGVIDPVKVTRSAVLNASSVARMVLTTETVVVDKPA 526
Cdd:TIGR02346 454 EVIPK---LYAAHkkgnkskGIDIEAESDGvkDASEAGIYDMLATKKWAIKLATEAAVTVLRVDQIIMAKPA 522
|
|
| TCP1_gamma |
cd03337 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ... |
22-137 |
4.31e-07 |
|
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.
Pssm-ID: 239453 [Multi-domain] Cd Length: 480 Bit Score: 52.30 E-value: 4.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 22 LADTVRVTLGPRGRHVVLAKAFGGPTVTNDGVTVAREIELEDPfedlGAQLVKSVATKTNDVAGDGTTTATILAQALIKG 101
Cdd:cd03337 28 VADVIRTCLGPRAMLKMLLDPMGGIVLTNDGNAILREIDVAHP----AAKSMIELSRTQDEEVGDGTTSVIILAGEILAV 103
|
90 100 110
....*....|....*....|....*....|....*.
gi 489513178 102 GLRLVAAGVNPIALGVGIGKAADAVSEALLASATPV 137
Cdd:cd03337 104 AEPFLERGIHPTVIIKAYRKALEDALKILEEISIPV 139
|
|
| TCP1_zeta |
cd03342 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
9-137 |
9.41e-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: 9.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 9 ETARR--AMEVGMD---KLADTVRVTLGPRGRHVVLAKAFGGPTVTNDGVTVAREIELEDPFedlgAQLVKSVATKTNDV 83
Cdd:cd03342 6 EVLRRgqALAVNISaakGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLSEMQIQHPT----ASMIARAATAQDDI 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 489513178 84 AGDGTTTATILAQALIKGGLRLVAAGVNPIALGVGIGKAADAVSEALLASATPV 137
Cdd:cd03342 82 TGDGTTSNVLLIGELLKQAERYIQEGVHPRIITEGFELAKNKALKFLESFKVPV 135
|
|
| chap_CCT_gamma |
TIGR02344 |
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ... |
22-95 |
2.11e-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: 50.51 E-value: 2.11e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489513178 22 LADTVRVTLGPRGRHVVLAKAFGGPTVTNDGVTVAREIELEDPfedlGAQLVKSVATKTNDVAGDGTTTATILA 95
Cdd:TIGR02344 28 VADIIRTCLGPRSMLKMLLDPMGGIVMTNDGNAILREIDVAHP----AAKSMIELSRTQDEEVGDGTTSVIILA 97
|
|
| TCP1_zeta |
cd03342 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
408-515 |
2.87e-06 |
|
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.
Pssm-ID: 239458 [Multi-domain] Cd Length: 484 Bit Score: 49.95 E-value: 2.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 408 GIVPGGGASLIhQARKALTELRASLTGDEVLGVDVFSEALAAPLFWIAANAGLDGSVVVNKV----SELPAGHGLNVNTL 483
Cdd:cd03342 364 CVVPGAGAFEV-ALYAHLKEFKKSVKGKAKLGVQAFADALLVIPKTLAENSGLDVQETLVKLqdeyAEGGQVGGVDLDTG 442
|
90 100 110
....*....|....*....|....*....|..
gi 489513178 484 SYGDLAADGVIDPVKVTRSAVLNASSVARMVL 515
Cdd:cd03342 443 EPMDPESEGIWDNYSVKRQILHSATVIASQLL 474
|
|
| TCP1_theta |
cd03341 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ... |
21-524 |
4.36e-05 |
|
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: 46.06 E-value: 4.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 21 KLADTVRVTLGPRGRHVVLAKAFGGPTVTNDGVTVAREIELEDPfedlGAQLVKSVATKTNDVAGDGTTTATILAQALIK 100
Cdd:cd03341 19 ELSQITRTSYGPNGMNKMVINHLEKLFVTSDAATILRELEVQHP----AAKLLVMASQMQEEEIGDGTNLVVVLAGELLE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 101 GGLRLVAAGVNPIALGVGIGKAADAVSEAL--LASATpVSGKTGIAQVATV---------SSRDEQIGDLVGEAMSKVGH 169
Cdd:cd03341 95 KAEELLRMGLHPSEIIEGYEKALKKALEILeeLVVYK-IEDLRNKEEVSKAlktaiaskqYGNEDFLSPLVAEACISVLP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 170 D----------GVV-----SVEESSTLgteleftegigfdKGFLsayFVTDFDNQQAVLEDAlillhqdkisslpdllpl 234
Cdd:cd03341 174 EnignfnvdniRVVkilggSLEDSKVV-------------RGMV---FKREPEGSVKRVKKA------------------ 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 235 leKVA------GTGKPLLIVAEDVEGEALATLvvnairKTLKAVAVKGPY-FGDRRkafledLAVVTGGQVV------NP 301
Cdd:cd03341 220 --KVAvfscpfDIGVNVIVAGGSVGDLALHYC------NKYGIMVIKINSkFELRR------LCRTVGATPLprlgapTP 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 302 DA-GMVlREVGLEVLGSARRVVVSKDD------TVIVDGggtaeAVANRAKHLRAEIDKsdsdwdreklgerlaklagGV 374
Cdd:cd03341 286 EEiGYC-DSVYVEEIGDTKVVVFRQNKedskiaTIVLRG-----ATQNILDDVERAIDD-------------------GV 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513178 375 AVIKVgaatetALKERKesvedavaaakaaveegIVPGGGASLIHQARKaLTELRASLTGDEVLGVDVFSEALAAPLFWI 454
Cdd:cd03341 341 NVFKS------LTKDGR-----------------FVPGAGATEIELAKK-LKEYGEKTPGLEQYAIKKFAEAFEVVPRTL 396
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489513178 455 AANAGLDGSVVvnkVSELPAGH-------GLNV--NTLSYGDLAADGVIDPVKVTRSAVLNASSVARMVLTTETVVVDK 524
Cdd:cd03341 397 AENAGLDATEV---LSELYAAHqkgnksaGVDIesGDEGTKDAKEAGIFDHLATKKWAIKLATEAAVTVLRVDQIIMAK 472
|
|
| |
