|
Name |
Accession |
Description |
Interval |
E-value |
| groEL |
CHL00093 |
chaperonin GroEL |
1-528 |
0e+00 |
|
chaperonin GroEL
Pssm-ID: 177025 Cd Length: 529 Bit Score: 955.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 1 MAKRIIYNEQARRALERGIDILAESVAVTLGPKGRNVVLEKKFGAPQIINDGVTIAKEIELEDHIENTGVALIRQAASKT 80
Cdd:CHL00093 1 MSKKILYQDNARRALERGMDILAEAVSVTLGPKGRNVVLEKKYGSPQIVNDGVTIAKEIELEDHIENTGVALIRQAASKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 81 NDAAGDGTTTATVLAHAMVKAGLRNVAAGANAITLKKGIDKATEFLVGKIEENSKPISDSTAIAQCGTIAAGNDEEVGEM 160
Cdd:CHL00093 81 NDVAGDGTTTATVLAYAIVKQGMKNVAAGANPISLKRGIEKATQYVVSQIAEYARPVEDIQAITQVASISAGNDEEVGSM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 161 IANAMDKVGKEGVISLEEGKSMTTELEVTEGMRFDKGYISPYFATDTERMEAVLDEPYILLTDKKIALV-QDLVPVLEQI 239
Cdd:CHL00093 161 IADAIEKVGREGVISLEEGKSTVTELEITEGMRFEKGFISPYFVTDTERMEVVQENPYILLTDKKITLVqQDLLPILEQV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 240 AKTGKPLVIIAEDIEKEALATLVVNRLRGVLNVAAVKAPGFGDRRKAMLEDMAVLTNGQLITEDAGLKLENATLEMLGTG 319
Cdd:CHL00093 241 TKTKRPLLIIAEDVEKEALATLVLNKLRGIVNVVAVRAPGFGDRRKAMLEDIAILTGGQVITEDAGLSLETIQLDLLGQA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 320 RRITINKETTTIVAEGNEKAVNSRCDQIKKQMEETDSSYDKEKLQERLAKLAGGVAVIKVGAATETEMKDKKLRLEDAIN 399
Cdd:CHL00093 321 RRIIVTKDSTTIIADGNEEQVKARCEQLRKQIEIADSSYEKEKLQERLAKLSGGVAVIKVGAATETEMKDKKLRLEDAIN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 400 ATKAAVEEGIVPGGGTTLAHLAPILKEWADATLSGEELIGANIVEASLTAPLMRIAENAGSNGAVIAENVKSKPFNDGFN 479
Cdd:CHL00093 401 ATKAAVEEGIVPGGGATLVHLSENLKTWAKNNLKEDELIGALIVARAILAPLKRIAENAGKNGSVIIEKVQEQDFEIGYN 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 500144914 480 AATGEYVDMSSAGIVDPAKVTRSGLQNAASIAGMVLTTECIVADMPEKK 528
Cdd:CHL00093 481 AANNKFVNMYEAGIIDPAKVTRSALQNAASIASMILTTECIIVDKKESS 529
|
|
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
1-540 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 935.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 1 MAKRIIYNEQARRALERGIDILAESVAVTLGPKGRNVVLEKKFGAPQIINDGVTIAKEIELEDHIENTGVALIRQAASKT 80
Cdd:PRK00013 1 MAKDIKFGEDARRKLLRGVNKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDPFENMGAQLVKEVASKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 81 NDAAGDGTTTATVLAHAMVKAGLRNVAAGANAITLKKGIDKATEFLVGKIEENSKPISDSTAIAQCGTIAAGNDEEVGEM 160
Cdd:PRK00013 81 NDVAGDGTTTATVLAQAIVREGLKNVAAGANPMDLKRGIDKAVEAAVEELKKISKPVEDKEEIAQVATISANGDEEIGKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 161 IANAMDKVGKEGVISLEEGKSMTTELEVTEGMRFDKGYISPYFATDTERMEAVLDEPYILLTDKKIALVQDLVPVLEQIA 240
Cdd:PRK00013 161 IAEAMEKVGKEGVITVEESKGFETELEVVEGMQFDRGYLSPYFVTDPEKMEAELENPYILITDKKISNIQDLLPVLEQVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 241 KTGKPLVIIAEDIEKEALATLVVNRLRGVLNVAAVKAPGFGDRRKAMLEDMAVLTNGQLITEDAGLKLENATLEMLGTGR 320
Cdd:PRK00013 241 QSGKPLLIIAEDVEGEALATLVVNKLRGTLKVVAVKAPGFGDRRKAMLEDIAILTGGTVISEELGLKLEDATLEDLGQAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 321 RITINKETTTIV-AEGNEKAVNSRCDQIKKQMEETDSSYDKEKLQERLAKLAGGVAVIKVGAATETEMKDKKLRLEDAIN 399
Cdd:PRK00013 321 KVVVTKDNTTIVdGAGDKEAIKARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATEVEMKEKKDRVEDALH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 400 ATKAAVEEGIVPGGGTTLAHLAPILKEwaDATLSGEELIGANIVEASLTAPLMRIAENAGSNGAVIAENVK-SKPFNDGF 478
Cdd:PRK00013 401 ATRAAVEEGIVPGGGVALLRAAPALEA--LKGLNGDEATGINIVLRALEAPLRQIAENAGLEGSVVVEKVKnGKGKGYGY 478
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500144914 479 NAATGEYVDMSSAGIVDPAKVTRSGLQNAASIAGMVLTTECIVADMPEKKESAPA-GAPGMGG 540
Cdd:PRK00013 479 NAATGEYVDMIEAGIIDPTKVTRSALQNAASVAGLLLTTEAVVADKPEKKAAAPPmGGGGMGG 541
|
|
| 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: 850.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 3 KRIIYNEQARRALERGIDILAESVAVTLGPKGRNVVLEKKFGAPQIINDGVTIAKEIELEDHIENTGVALIRQAASKTND 82
Cdd:cd03344 1 KDIKFGEEARKALLRGVNKLADAVKVTLGPKGRNVVIEKSFGSPKITKDGVTVAKEIELEDPFENMGAQLVKEVASKTND 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 83 AAGDGTTTATVLAHAMVKAGLRNVAAGANAITLKKGIDKATEFLVGKIEENSKPISDSTAIAQCGTIAAGNDEEVGEMIA 162
Cdd:cd03344 81 VAGDGTTTATVLARAIIKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKPVKTKEEIAQVATISANGDEEIGELIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 163 NAMDKVGKEGVISLEEGKSMTTELEVTEGMRFDKGYISPYFATDTERMEAVLDEPYILLTDKKIALVQDLVPVLEQIAKT 242
Cdd:cd03344 161 EAMEKVGKDGVITVEEGKTLETELEVVEGMQFDRGYLSPYFVTDPEKMEVELENPYILLTDKKISSIQELLPILELVAKA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 243 GKPLVIIAEDIEKEALATLVVNRLRGVLNVAAVKAPGFGDRRKAMLEDMAVLTNGQLITEDAGLKLENATLEMLGTGRRI 322
Cdd:cd03344 241 GRPLLIIAEDVEGEALATLVVNKLRGGLKVCAVKAPGFGDRRKAMLEDIAILTGGTVISEELGLKLEDVTLEDLGRAKKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 323 TINKETTTIVA-EGNEKAVNSRCDQIKKQMEETDSSYDKEKLQERLAKLAGGVAVIKVGAATETEMKDKKLRLEDAINAT 401
Cdd:cd03344 321 VVTKDDTTIIGgAGDKAAIKARIAQIRKQIEETTSDYDKEKLQERLAKLSGGVAVIKVGGATEVELKEKKDRVEDALNAT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 402 KAAVEEGIVPGGGTTLAHLAPILKEWadATLSGEELIGANIVEASLTAPLMRIAENAGSNGAVIAENVKSKPFNDGFNAA 481
Cdd:cd03344 401 RAAVEEGIVPGGGVALLRASPALDKL--KALNGDEKLGIEIVRRALEAPLRQIAENAGVDGSVVVEKVLESPDGFGYDAA 478
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 500144914 482 TGEYVDMSSAGIVDPAKVTRSGLQNAASIAGMVLTTECIVAD 523
Cdd:cd03344 479 TGEYVDMIEAGIIDPTKVVRSALQNAASVASLLLTTEALVVD 520
|
|
| groEL |
PRK12849 |
chaperonin GroEL; Reviewed |
1-540 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237230 Cd Length: 542 Bit Score: 847.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 1 MAKRIIYNEQARRALERGIDILAESVAVTLGPKGRNVVLEKKFGAPQIINDGVTIAKEIELEDHIENTGVALIRQAASKT 80
Cdd:PRK12849 1 MAKIIKFDEEARRALERGVNKLADAVKVTLGPKGRNVVIDKSFGAPTITKDGVSIAKEIELEDPFENLGAQLVKEVASKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 81 NDAAGDGTTTATVLAHAMVKAGLRNVAAGANAITLKKGIDKATEFLVGKIEENSKPISDSTAIAQCGTIAAGNDEEVGEM 160
Cdd:PRK12849 81 NDVAGDGTTTATVLAQALVQEGLKNVAAGANPMDLKRGIDKAVEAVVEELKALARPVSGSEEIAQVATISANGDEEIGEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 161 IANAMDKVGKEGVISLEEGKSMTTELEVTEGMRFDKGYISPYFATDTERMEAVLDEPYILLTDKKIALVQDLVPVLEQIA 240
Cdd:PRK12849 161 IAEAMEKVGKDGVITVEESKTLETELEVTEGMQFDRGYLSPYFVTDPERMEAVLEDPLILLTDKKISSLQDLLPLLEKVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 241 KTGKPLVIIAEDIEKEALATLVVNRLRGVLNVAAVKAPGFGDRRKAMLEDMAVLTNGQLITEDAGLKLENATLEMLGTGR 320
Cdd:PRK12849 241 QSGKPLLIIAEDVEGEALATLVVNKLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGLKLEEVTLDDLGRAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 321 RITINKETTTIVA-EGNEKAVNSRCDQIKKQMEETDSSYDKEKLQERLAKLAGGVAVIKVGAATETEMKDKKLRLEDAIN 399
Cdd:PRK12849 321 RVTITKDNTTIVDgAGDKEAIEARVAQIRRQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATEVELKERKDRVEDALN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 400 ATKAAVEEGIVPGGGTTLAHLAPILKEwaDATLSGEELIGANIVEASLTAPLMRIAENAGSNGAVIAENVKSKPFNDGFN 479
Cdd:PRK12849 401 ATRAAVEEGIVPGGGVALLRAAKALDE--LAGLNGDQAAGVEIVRRALEAPLRQIAENAGLDGSVVVAKVLELEDGFGFN 478
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500144914 480 AATGEYVDMSSAGIVDPAKVTRSGLQNAASIAGMVLTTECIVADMPEkKESAPAGAPGMGG 540
Cdd:PRK12849 479 AATGEYGDLIAAGIIDPVKVTRSALQNAASVAGLLLTTEALVADKPE-EEDPPGGMGGMGG 538
|
|
| GroEL |
TIGR02348 |
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ... |
2-526 |
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: 826.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 2 AKRIIYNEQARRALERGIDILAESVAVTLGPKGRNVVLEKKFGAPQIINDGVTIAKEIELEDHIENTGVALIRQAASKTN 81
Cdd:TIGR02348 1 AKQIKFDEEARKALLRGVDKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDKFENMGAQLVKEVASKTN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 82 DAAGDGTTTATVLAHAMVKAGLRNVAAGANAITLKKGIDKATEFLVGKIEENSKPISDSTAIAQCGTIAAGNDEEVGEMI 161
Cdd:TIGR02348 81 DVAGDGTTTATVLAQAIVKEGLKNVAAGANPIELKRGIEKAVEAVVEELKKLSKPVKGKKEIAQVATISANNDEEIGSLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 162 ANAMDKVGKEGVISLEEGKSMTTELEVTEGMRFDKGYISPYFATDTERMEAVLDEPYILLTDKKIALVQDLVPVLEQIAK 241
Cdd:TIGR02348 161 AEAMEKVGKDGVITVEESKSLETELEVVEGMQFDRGYISPYFVTDAEKMEVELENPYILITDKKISNIKDLLPLLEKVAQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 242 TGKPLVIIAEDIEKEALATLVVNRLRGVLNVAAVKAPGFGDRRKAMLEDMAVLTNGQLITEDAGLKLENATLEMLGTGRR 321
Cdd:TIGR02348 241 SGKPLLIIAEDVEGEALATLVVNKLRGTLNVCAVKAPGFGDRRKAMLEDIAILTGGQVISEELGLKLEEVTLDDLGKAKK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 322 ITINKETTTIVAE-GNEKAVNSRCDQIKKQMEETDSSYDKEKLQERLAKLAGGVAVIKVGAATETEMKDKKLRLEDAINA 400
Cdd:TIGR02348 321 VTVDKDNTTIVEGaGDKAAIKARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATETEMKEKKLRIEDALNA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 401 TKAAVEEGIVPGGGTTLAHLAPILKEWadATLSGEELIGANIVEASLTAPLMRIAENAGSNGAVIAENVKSKPFNDGFNA 480
Cdd:TIGR02348 401 TRAAVEEGIVPGGGVALLRAAAALEGL--KGDGEDEAIGIDIVKRALEAPLRQIAENAGLDGAVVAEKVKELKGNFGFNA 478
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 500144914 481 ATGEYVDMSSAGIVDPAKVTRSGLQNAASIAGMVLTTECIVADMPE 526
Cdd:TIGR02348 479 ATGEYEDLVEAGIIDPTKVTRSALQNAASIAGLLLTTEAVVADKPE 524
|
|
| groEL |
PRK12850 |
chaperonin GroEL; Reviewed |
1-540 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237231 Cd Length: 544 Bit Score: 751.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 1 MAKRIIYNEQARRALERGIDILAESVAVTLGPKGRNVVLEKKFGAPQIINDGVTIAKEIELEDHIENTGVALIRQAASKT 80
Cdd:PRK12850 2 AAKEIRFSTDARDRLLRGVNILANAVKVTLGPKGRNVVLEKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVKEVASKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 81 NDAAGDGTTTATVLAHAMVKAGLRNVAAGANAITLKKGIDKATEFLVGKIEENSKPISDSTAIAQCGTIAAGNDEEVGEM 160
Cdd:PRK12850 82 NDLAGDGTTTATVLAQAIVREGAKLVAAGMNPMDLKRGIDLAVAAVVDELKKIAKKVTSSKEIAQVATISANGDESIGEM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 161 IANAMDKVGKEGVISLEEGKSMTTELEVTEGMRFDKGYISPYFATDTERMEAVLDEPYILLTDKKIALVQDLVPVLEQIA 240
Cdd:PRK12850 162 IAEAMDKVGKEGVITVEEAKTLGTELDVVEGMQFDRGYLSPYFVTNPEKMRAELEDPYILLHEKKISNLQDLLPILEAVV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 241 KTGKPLVIIAEDIEKEALATLVVNRLRGVLNVAAVKAPGFGDRRKAMLEDMAVLTNGQLITEDAGLKLENATLEMLGTGR 320
Cdd:PRK12850 242 QSGRPLLIIAEDVEGEALATLVVNKLRGGLKSVAVKAPGFGDRRKAMLEDIAVLTGGQVISEDLGIKLENVTLDMLGRAK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 321 RITINKETTTIV-AEGNEKAVNSRCDQIKKQMEETDSSYDKEKLQERLAKLAGGVAVIKVGAATETEMKDKKLRLEDAIN 399
Cdd:PRK12850 322 RVLITKENTTIIdGAGDKKNIEARVKQIRAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKEKKDRVDDALH 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 400 ATKAAVEEGIVPGGGTTLAHLAPILKEWADATlsGEELIGANIVEASLTAPLMRIAENAGSNGAVIAENVKSKPFNDGFN 479
Cdd:PRK12850 402 ATRAAVEEGIVPGGGVALLRARSALRGLKGAN--ADETAGIDIVRRALEEPLRQIATNAGFEGSVVVGKVAELPGNFGFN 479
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500144914 480 AATGEYVDMSSAGIVDPAKVTRSGLQNAASIAGMVLTTECIVADMPEKKESAPAG-APGMGG 540
Cdd:PRK12850 480 AQTGEYGDMVEAGIIDPAKVTRTALQDAASIAALLITTEAMVAEAPKKAAAAAAGpGPGMGG 541
|
|
| GroEL |
COG0459 |
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ... |
1-531 |
0e+00 |
|
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227 Cd Length: 497 Bit Score: 728.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 1 MAKRIIYNEQARRALERGIDILAESVAVTLGPKGRNVVLEKKFGAPQIINDGVTIAKEIELEDHIENTGVALIRQAASKT 80
Cdd:COG0459 1 MAKQILFGEDARRANIRGVKALADAVKVTLGPKGRNVMLVKSFGDPTITNDGVTIAKEIELEDPFENMGAQLVKEVASKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 81 NDAAGDGTTTATVLAHAMVKAGLRNVAAGANAITLKKGIDKATEFLVGKIEENSKPISDSTAIAQCGTIAAGNDEEVGEM 160
Cdd:COG0459 81 NDEAGDGTTTATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPVDDKEELAQVATISANGDEEIGEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 161 IANAMDKVGKEGVISLEEGKSMTTELEVTEGMRFDKGYISPYFATDTERMEAVLDEPYILLTDKKIALVQDLVPVLEQIA 240
Cdd:COG0459 161 IAEAMEKVGKDGVITVEEGKGLETELEVVEGMQFDKGYLSPYFVTDPEKMPAELENAYILLTDKKISSIQDLLPLLEKVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 241 KTGKPLVIIAEDIEKEALATLVVNRLRGVLNVAAVKAPGFGDRRKAMLEDMAVLTNGQLITEDAGLKLENATLEMLGTGR 320
Cdd:COG0459 241 QSGKPLLIIAEDIDGEALATLVVNGIRGVLRVVAVKAPGFGDRRKAMLEDIAILTGGRVISEDLGLKLEDVTLDDLGRAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 321 RITINKETTTIVAE-GNEKAVnsrcdqikkqmeetdssydkeklqerlaklaggvaVIKVGAATETEMKDKKLRLEDAIN 399
Cdd:COG0459 321 RVEVDKDNTTIVEGaGNPKAI-----------------------------------VILVGAATEVEVKERKRRVEDALH 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 400 ATKAAVEEGIVPGGGTTLAHLAPILKEWAdATLSGEELIGANIVEASLTAPLMRIAENAGSNGAVIAENVKSKP-FNDGF 478
Cdd:COG0459 366 ATRAAVEEGIVPGGGAALLRAARALRELA-AKLEGDEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKVRAAKdKGFGF 444
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 500144914 479 NAATGEYVDMSSAGIVDPAKVTRSGLQNAASIAGMVLTTECIVADMPEKKESA 531
Cdd:COG0459 445 DAATGEYVDMLEAGVIDPAKVKRSALQNAASVAGLILTTEAVIADKPEKEEAA 497
|
|
| groEL |
PRK12851 |
chaperonin GroEL; Reviewed |
1-542 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 171770 Cd Length: 541 Bit Score: 706.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 1 MAKRIIYNEQARRALERGIDILAESVAVTLGPKGRNVVLEKKFGAPQIINDGVTIAKEIELEDHIENTGVALIRQAASKT 80
Cdd:PRK12851 2 AAKEVKFHVEAREKMLRGVNILADAVKVTLGPKGRNVVIDKSFGAPTITNDGVTIAKEIELEDKFENMGAQMVREVASKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 81 NDAAGDGTTTATVLAHAMVKAGLRNVAAGANAITLKKGIDKATEFLVGKIEENSKPISDSTAIAQCGTIAAGNDEEVGEM 160
Cdd:PRK12851 82 NDVAGDGTTTATVLAQAIVREGAKAVAAGANPMDLKRGIDRAVAAVVEELKANARPVTTNAEIAQVATISANGDAEIGRL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 161 IANAMDKVGKEGVISLEEGKSMTTELEVTEGMRFDKGYISPYFATDTERMEAVLDEPYILLTDKKIALVQDLVPVLEQIA 240
Cdd:PRK12851 162 VAEAMEKVGNEGVITVEESKTAETELEVVEGMQFDRGYLSPYFVTDADKMEAELEDPYILIHEKKISNLQDLLPVLEAVV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 241 KTGKPLVIIAEDIEKEALATLVVNRLRGVLNVAAVKAPGFGDRRKAMLEDMAVLTNGQLITEDAGLKLENATLEMLGTGR 320
Cdd:PRK12851 242 QSGKPLLIIAEDVEGEALATLVVNKLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGIKLENVTLEQLGRAK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 321 RITINKETTTIV-AEGNEKAVNSRCDQIKKQMEETDSSYDKEKLQERLAKLAGGVAVIKVGAATETEMKDKKLRLEDAIN 399
Cdd:PRK12851 322 KVVVEKENTTIIdGAGSKTEIEGRVAQIRAQIEETTSDYDREKLQERLAKLAGGVAVIRVGASTEVEVKEKKDRVDDALH 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 400 ATKAAVEEGIVPGGGTTLAHLAPILKEwaDATLSGEELIGANIVEASLTAPLMRIAENAGSNGAVIAENVKSKPFNDGFN 479
Cdd:PRK12851 402 ATRAAVEEGIVPGGGVALLRAVKALDK--LETANGDQRTGVEIVRRALEAPVRQIAENAGAEGSVVVGKLREKPGGYGFN 479
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500144914 480 AATGEYVDMSSAGIVDPAKVTRSGLQNAASIAGMVLTTECIVADMPEKKESAPAgAPGMGGDF 542
Cdd:PRK12851 480 AATNEYGDLYAQGVIDPVKVVRTALQNAASVAGLLLTTEAMVAEKPKKEPAPPA-PPGGGMDF 541
|
|
| PTZ00114 |
PTZ00114 |
Heat shock protein 60; Provisional |
2-538 |
0e+00 |
|
Heat shock protein 60; Provisional
Pssm-ID: 185455 Cd Length: 555 Bit Score: 683.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 2 AKRIIYNEQARRALERGIDILAESVAVTLGPKGRNVVLEKKFGAPQIINDGVTIAKEIELEDHIENTGVALIRQAASKTN 81
Cdd:PTZ00114 14 GKEIRFGDEARQSLLKGIERLADAVAVTLGPKGRNVIIEQEYGSPKITKDGVTVAKAIEFSDRFENVGAQLIRQVASKTN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 82 DAAGDGTTTATVLAHAMVKAGLRNVAAGANAITLKKGIDKATEFLVGKIEENSKPISDSTAIAQCGTIAAGNDEEVGEMI 161
Cdd:PTZ00114 94 DKAGDGTTTATILARAIFREGCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQSRPVKTKEDILNVATISANGDVEIGSLI 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 162 ANAMDKVGKEGVISLEEGKSMTTELEVTEGMRFDKGYISPYFATDTERMEAVLDEPYILLTDKKIALVQDLVPVLEQIAK 241
Cdd:PTZ00114 174 ADAMDKVGKDGTITVEDGKTLEDELEVVEGMSFDRGYISPYFVTNEKTQKVELENPLILVTDKKISSIQSILPILEHAVK 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 242 TGKPLVIIAEDIEKEALATLVVNRLRGVLNVAAVKAPGFGDRRKAMLEDMAVLTNGQLITEDA-GLKLENATLEMLGTGR 320
Cdd:PTZ00114 254 NKRPLLIIAEDVEGEALQTLIINKLRGGLKVCAVKAPGFGDNRKDILQDIAVLTGATVVSEDNvGLKLDDFDPSMLGSAK 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 321 RITINKETTTIV-AEGNEKAVNSRCDQIKKQMEETDSSYDKEKLQERLAKLAGGVAVIKVGAATETEMKDKKLRLEDAIN 399
Cdd:PTZ00114 334 KVTVTKDETVILtGGGDKAEIKERVELLRSQIERTTSEYDKEKLKERLAKLSGGVAVIKVGGASEVEVNEKKDRIEDALN 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 400 ATKAAVEEGIVPGGGTTLAHLAPILKEWA-DATLSGEELIGANIVEASLTAPLMRIAENAGSNGAVIAENVK-SKPFNDG 477
Cdd:PTZ00114 414 ATRAAVEEGIVPGGGVALLRASKLLDKLEeDNELTPDQRTGVKIVRNALRLPTKQIAENAGVEGAVVVEKILeKKDPSFG 493
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500144914 478 FNAATGEYVDMSSAGIVDPAKVTRSGLQNAASIAGMVLTTECIVADMPEKKESAPAGAPGM 538
Cdd:PTZ00114 494 YDAQTGEYVNMFEAGIIDPTKVVRSALVDAASVASLMLTTEAAIVDLPKEKKKNKNSAAPP 554
|
|
| groEL |
PRK12852 |
chaperonin GroEL; Reviewed |
1-544 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237232 Cd Length: 545 Bit Score: 659.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 1 MAKRIIYNEQARRALERGIDILAESVAVTLGPKGRNVVLEKKFGAPQIINDGVTIAKEIELEDHIENTGVALIRQAASKT 80
Cdd:PRK12852 2 AAKDVKFSGDARDRMLRGVDILANAVKVTLGPKGRNVVIEKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVREVASKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 81 NDAAGDGTTTATVLAHAMVKAGLRNVAAGANAITLKKGIDKATEFLVGKIEENSKPISDSTAIAQCGTIAAGNDEEVGEM 160
Cdd:PRK12852 82 NDLAGDGTTTATVLAQAIVREGAKAVAAGMNPMDLKRGIDIAVAAVVKDIEKRAKPVASSAEIAQVGTISANGDAAIGKM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 161 IANAMDKVGKEGVISLEEGKSMTTELEVTEGMRFDKGYISPYFATDTERMEAVLDEPYILLTDKKIALVQDLVPVLEQIA 240
Cdd:PRK12852 162 IAQAMQKVGNEGVITVEENKSLETEVDIVEGMKFDRGYLSPYFVTNAEKMTVELDDAYILLHEKKLSGLQAMLPVLEAVV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 241 KTGKPLVIIAEDIEKEALATLVVNRLRGVLNVAAVKAPGFGDRRKAMLEDMAVLTNGQLITEDAGLKLENATLEMLGTGR 320
Cdd:PRK12852 242 QSGKPLLIIAEDVEGEALATLVVNRLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGQLISEDLGIKLENVTLKMLGRAK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 321 RITINKETTTIV-AEGNEKAVNSRCDQIKKQMEETDSSYDKEKLQERLAKLAGGVAVIKVGAATETEMKDKKLRLEDAIN 399
Cdd:PRK12852 322 KVVIDKENTTIVnGAGKKADIEARVGQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKEKKDRVEDALN 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 400 ATKAAVEEGIVPGGGTTLAHLAPILKEWADAtlSGEELIGANIVEASLTAPLMRIAENAGSNGAVIAENV-KSKPFNDGF 478
Cdd:PRK12852 402 ATRAAVQEGIVPGGGVALLRAKKAVGRINND--NADVQAGINIVLKALEAPIRQIAENAGVEGSIVVGKIlENKSETFGF 479
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500144914 479 NAATGEYVDMSSAGIVDPAKVTRSGLQNAASIAGMVLTTECIVADMPEKKESAPAGAPGMGGDFDY 544
Cdd:PRK12852 480 DAQTEEYVDMVAKGIIDPAKVVRTALQDAASVAGLLVTTEAMVAELPKKDAAPAMPAGGGMGGMGF 545
|
|
| PRK14104 |
PRK14104 |
chaperonin GroEL; Provisional |
2-540 |
0e+00 |
|
chaperonin GroEL; Provisional
Pssm-ID: 172594 Cd Length: 546 Bit Score: 580.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 2 AKRIIYNEQARRALERGIDILAESVAVTLGPKGRNVVLEKKFGAPQIINDGVTIAKEIELEDHIENTGVALIRQAASKTN 81
Cdd:PRK14104 3 AKEVKFGVDARDRMLRGVDILANAVKVTLGPKGRNVVLDKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVREVASKSA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 82 DAAGDGTTTATVLAHAMVKAGLRNVAAGANAITLKKGIDKATEFLVGKIEENSKPISDSTAIAQCGTIAAGNDEEVGEMI 161
Cdd:PRK14104 83 DAAGDGTTTATVLAQAIVREGAKSVAAGMNPMDLKRGIDLAVEAVVADLVKNSKKVTSNDEIAQVGTISANGDAEIGKFL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 162 ANAMDKVGKEGVISLEEGKSMTTELEVTEGMRFDKGYISPYFATDTERMEAVLDEPYILLTDKKIALVQDLVPVLEQIAK 241
Cdd:PRK14104 163 ADAMKKVGNEGVITVEEAKSLETELDVVEGMQFDRGYISPYFVTNADKMRVEMDDAYILINEKKLSSLNELLPLLEAVVQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 242 TGKPLVIIAEDIEKEALATLVVNRLRGVLNVAAVKAPGFGDRRKAMLEDMAVLTNGQLITEDAGLKLENATLEMLGTGRR 321
Cdd:PRK14104 243 TGKPLVIVAEDVEGEALATLVVNRLRGGLKVAAVKAPGFGDRRKAMLQDIAILTGGQAISEDLGIKLENVTLQMLGRAKK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 322 ITINKETTTIVAEGNEKA-VNSRCDQIKKQMEETDSSYDKEKLQERLAKLAGGVAVIKVGAATETEMKDKKLRLEDAINA 400
Cdd:PRK14104 323 VMIDKENTTIVNGAGKKAdIEARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKERKDRVDDAMHA 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 401 TKAAVEEGIVPGGGTTLAHLAPILKEWadATLSGEELIGANIVEASLTAPLMRIAENAGSNGAVIAENVKSKP-FNDGFN 479
Cdd:PRK14104 403 TRAAVEEGIVPGGGVALLRASEQLKGI--KTKNDDQKTGVEIVRKALSAPARQIAINAGEDGSVIVGKILEKEqYSYGFD 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500144914 480 AATGEYVDMSSAGIVDPAKVTRSGLQNAASIAGMVLTTECIVADMPEKKESAPA--GAPGMGG 540
Cdd:PRK14104 481 SQTGEYGNLVSKGIIDPTKVVRTAIQNAASVAALLITTEAMVAELPKKGGAGPAmpPGGGMGG 543
|
|
| PLN03167 |
PLN03167 |
Chaperonin-60 beta subunit; Provisional |
2-536 |
0e+00 |
|
Chaperonin-60 beta subunit; Provisional
Pssm-ID: 215611 [Multi-domain] Cd Length: 600 Bit Score: 569.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 2 AKRIIYNE--QARRALERGIDILAESVAVTLGPKGRNVVLEKKFGAPQIINDGVTIAKEIELEDHIENTGVALIRQAASK 79
Cdd:PLN03167 56 AKELHFNKdgSAIKKLQAGVNKLADLVGVTLGPKGRNVVLESKYGSPKIVNDGVTVAKEVELEDPVENIGAKLVRQAAAK 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 80 TNDAAGDGTTTATVLAHAMVKAGLRNVAAGANAITLKKGIDKATEFLVGKIEENSKPISDSTaIAQCGTIAAGNDEEVGE 159
Cdd:PLN03167 136 TNDLAGDGTTTSVVLAQGLIAEGVKVVAAGANPVQITRGIEKTAKALVKELKKMSKEVEDSE-LADVAAVSAGNNYEVGN 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 160 MIANAMDKVGKEGVISLEEGKSMTTELEVTEGMRFDKGYISPYFATDTERMEAVLDEPYILLTDKKIALVQDLVPVLEQI 239
Cdd:PLN03167 215 MIAEAMSKVGRKGVVTLEEGKSAENNLYVVEGMQFDRGYISPYFVTDSEKMSVEYDNCKLLLVDKKITNARDLIGILEDA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 240 AKTGKPLVIIAEDIEKEALATLVVNRLRGVLNVAAVKAPGFGDRRKAMLEDMAVLTNGQLITEDAGLKLENATLEMLGTG 319
Cdd:PLN03167 295 IRGGYPLLIIAEDIEQEALATLVVNKLRGSLKIAALKAPGFGERKSQYLDDIAILTGGTVIREEVGLSLDKVGKEVLGTA 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 320 RRITINKETTTIVAEGN-EKAVNSRCDQIKKQMEETDSSYDKEKLQERLAKLAGGVAVIKVGAATETEMKDKKLRLEDAI 398
Cdd:PLN03167 375 AKVVLTKDTTTIVGDGStQEAVNKRVAQIKNLIEAAEQDYEKEKLNERIAKLSGGVAVIQVGAQTETELKEKKLRVEDAL 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 399 NATKAAVEEGIVPGGGTTLAHLAPILKEWADATLSGEELIGANIVEASLTAPLMRIAENAGSNGAVIAENVKSKP-FNDG 477
Cdd:PLN03167 455 NATKAAVEEGIVVGGGCTLLRLASKVDAIKDTLENDEQKVGADIVKRALSYPLKLIAKNAGVNGSVVSEKVLSNDnPKFG 534
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 500144914 478 FNAATGEYVDMSSAGIVDPAKVTRSGLQNAASIAGMVLTTECIVADMPEkKESAPAGAP 536
Cdd:PLN03167 535 YNAATGKYEDLMAAGIIDPTKVVRCCLEHAASVAKTFLTSDCVVVEIKE-PEPVPAGNP 592
|
|
| chaperonin_type_I_II |
cd00309 |
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ... |
3-522 |
3.65e-141 |
|
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: 415.67 E-value: 3.65e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 3 KRIIYNEQARRALERGIDILAESVAVTLGPKGRNVVLEKKFGAPQIINDGVTIAKEIEledhIENTGVALIRQAASKTND 82
Cdd:cd00309 1 KEREFGEEARLSNINAAKALADAVKTTLGPKGMDKMLVDSLGDPTITNDGATILKEIE----VEHPAAKLLVEVAKSQDD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 83 AAGDGTTTATVLAHAMVKAGLRNVAAGANAITLKKGIDKATEFLVGKIEENSKPI--SDSTAIAQCGTIAAG------ND 154
Cdd:cd00309 77 EVGDGTTTVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVPIdvEDREELLKVATTSLNsklvsgGD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 155 EEVGEMIANAMDKVGKE------GVISLEEGKSMT-TELEVTEGMRFDKGYISPYfatdterMEAVLDEPYILLTDKKIA 227
Cdd:cd00309 157 DFLGELVVDAVLKVGKEngdvdlGVIRVEKKKGGSlEDSELVVGMVFDKGYLSPY-------MPKRLENAKILLLDCKLE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 228 lvqdlvpvleqiaktgkpLVIIAED-IEKEALATLVvnrlrgVLNVAAVKApgfgdRRKAMLEDMAVLTNGQLITEdagl 306
Cdd:cd00309 230 ------------------YVVIAEKgIDDEALHYLA------KLGIMAVRR-----VRKEDLERIAKATGATIVSR---- 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 307 kLENATLEMLGTGRRITINK----ETTTIVAEGNekavnsrcdqikkqmeetdssydkeklqerlaklaGGVAVIKVGAA 382
Cdd:cd00309 277 -LEDLTPEDLGTAGLVEETKigdeKYTFIEGCKG-----------------------------------GKVATILLRGA 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 383 TETEMKDKKLRLEDAINATKAAVEE-GIVPGGGTTLAHLAPILKEWADaTLSGEELIGANIVEASLTAPLMRIAENAGSN 461
Cdd:cd00309 321 TEVELDEAERSLHDALCAVRAAVEDgGIVPGGGAAEIELSKALEELAK-TLPGKEQLGIEAFADALEVIPRTLAENAGLD 399
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 500144914 462 GAVIAENVKSKPFNDGFNAA----TGEYVDMSSAGIVDPAKVTRSGLQNAASIAGMVLTTECIVA 522
Cdd:cd00309 400 PIEVVTKLRAKHAEGGGNAGgdveTGEIVDMKEAGIIDPLKVKRQALKSATEAASLILTIDDIIV 464
|
|
| Cpn60_TCP1 |
pfam00118 |
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ... |
22-523 |
4.02e-83 |
|
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: 267.15 E-value: 4.02e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 22 LAESVAVTLGPKGRNVVLEKKFGAPQIINDGVTIAKEIEledhIENTGVALIRQAASKTNDAAGDGTTTATVLAHAMVKA 101
Cdd:pfam00118 1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELE----IQHPAAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 102 GLRNVAAGANAITLKKGIDKATEFLVGKIEE----NSKPISDST-----AIAQCGTIAAGNDEEVGEMIANA-------- 164
Cdd:pfam00118 77 AEKLLAAGVHPTTIIEGYEKALEKALEILDSiisiPVEDVDREDllkvaRTSLSSKIISRESDFLAKLVVDAvlaipknd 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 165 -MDKVGKEGVISLEEGKSMTTELEvtEGMRFDKGYISPyfatdteRMEAVLDEPYILLTDKKI----------------- 226
Cdd:pfam00118 157 gSFDLGNIGVVKILGGSLEDSELV--DGVVLDKGPLHP-------DMPKRLENAKVLLLNCSLeyektetkatvvlsdae 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 227 -------ALVQDLVPVLEQIAKTGKPLVIIAEDIEKEALATLVVNRLRGVLNVaavkapgfgdrRKAMLEDMAVLTNGQL 299
Cdd:pfam00118 228 qlerflkAEEEQILEIVEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMALRRV-----------KKRDLERLAKATGARA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 300 ITedaglKLENATLEMLGTGRRI---TINKETTTIVAEGnekavnsrcdqikkqmeetdssydkeklqerlakLAGGVAV 376
Cdd:pfam00118 297 VS-----SLDDLTPDDLGTAGKVeeeKIGDEKYTFIEGC----------------------------------KSPKAAT 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 377 IKVGAATETEMKDKKLRLEDAINATKAAVEE-GIVPGGGTTLAHLAPILKEWADaTLSGEELIGANIVEASLTAPLMRIA 455
Cdd:pfam00118 338 ILLRGATDHVLDEIERSIHDALCVVKNAIEDpRVVPGGGAVEMELARALREYAK-SVSGKEQLAIEAFAEALEVIPKTLA 416
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500144914 456 ENAGSNGAVIAENVKSK----PFNDGFNAATGEYVDMSSAGIVDPAKVTRSGLQNAASIAGMVLTTECIVAD 523
Cdd:pfam00118 417 ENAGLDPIEVLAELRAAhasgEKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKSATEAASTILRIDDIIKA 488
|
|
| chaperonin_like |
cd03333 |
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ... |
143-407 |
2.88e-36 |
|
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: 134.13 E-value: 2.88e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 143 IAQCGTIAAG-----NDEEVGEMIANAMDKVGKE------GVISLEEGKSMT-TELEVTEGMRFDKGYISPYfatdterM 210
Cdd:cd03333 4 LLQVATTSLNsklssWDDFLGKLVVDAVLKVGPDnrmddlGVIKVEKIPGGSlEDSELVVGVVFDKGYASPY-------M 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 211 EAVLDEPYILLTDKKIAlvqdlvpvleqiaktgkpLVIIAED-IEKEALATLVvnrlrgVLNVAAVKApgfgdRRKAMLE 289
Cdd:cd03333 77 PKRLENAKILLLDCPLE------------------YVVIAEKgIDDLALHYLA------KAGIMAVRR-----VKKEDLE 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 290 DMAVLTNGQLITEdaglkLENATLEMLGTGRRITINK--ETTTIVAEGNEKavnsrcdqikkqmeetdssydkeklqerl 367
Cdd:cd03333 128 RIARATGATIVSS-----LEDLTPEDLGTAELVEETKigEEKLTFIEGCKG----------------------------- 173
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 500144914 368 aklaGGVAVIKVGAATETEMKDKKLRLEDAINATKAAVEE 407
Cdd:cd03333 174 ----GKAATILLRGATEVELDEVKRSLHDALCAVRAAVEE 209
|
|
| thermosome_beta |
NF041083 |
thermosome subunit beta; |
9-522 |
1.97e-23 |
|
thermosome subunit beta;
Pssm-ID: 469010 Cd Length: 519 Bit Score: 103.88 E-value: 1.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 9 EQARRALERGID---ILAESVAVTLGPKGRNVVLEKKFGAPQIINDGVTIAKEIEledhIENTGVALIRQAASKTNDAAG 85
Cdd:NF041083 13 TKGRDAQRNNIMaakAVAEAVRTTLGPKGMDKMLVDSLGDIVITNDGATILKEMD----VQHPAAKMLVEVAKTQDDEVG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 86 DGTTTATVLAHAMVKAGL----RNVAAGANAITLKKGIDKATEFLvgkiEENSKPISDS----------TAIAqcGTIAA 151
Cdd:NF041083 89 DGTTTAVVLAGELLKKAEelldQNIHPTIIANGYRLAAEKAIEIL----DEIAEKVDPDdretlkkiaeTSLT--SKGVE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 152 GNDEEVGEMIANAMDKV-----GKEGV----ISLE--EGKSMtTELEVTEGMRFDKGYISPYFATDTERME-AVLDEPY- 218
Cdd:NF041083 163 EARDYLAEIAVKAVKQVaekrdGKYYVdldnIQIEkkHGGSI-EDTQLIYGIVIDKEVVHPGMPKRVENAKiALLDAPLe 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 219 ------------------ILLTDKKIALVQDLVpvlEQIAKTGKPLVIIAEDIEKEA---LATlvvnrlRGVLNVAAVKa 277
Cdd:NF041083 242 vkkteidaeiritdpdqlQKFLDQEEKMLKEMV---DKIKATGANVVFCQKGIDDLAqhyLAK------AGILAVRRVK- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 278 pgfgdrrKAMLEDMAVLTNGQLITedaglKLENATLEMLGTGRRITINK--ETTTIVAEG--NEKAVNsrcdqikkqmee 353
Cdd:NF041083 312 -------KSDMEKLAKATGARIVT-----NIDDLTPEDLGYAELVEERKvgDDKMVFVEGckNPKAVT------------ 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 354 tdssydkeklqerlaklaggvavIKVGAATETEMKDKKLRLEDAINATKAAVEEG-IVPGGGTTLAHLAPILKEWAdATL 432
Cdd:NF041083 368 -----------------------ILIRGGTEHVVDEAERALEDALSVVADAVEDGkIVAGGGAPEVELAKRLREYA-ATV 423
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 433 SGEELIGANIVEASLTAPLMRIAENAGSNGAVIAENVKSKPFND----GFNAATGEYVDMSSAGIVDPAKVTRSGLQNAA 508
Cdd:NF041083 424 GGREQLAVEAFAEALEIIPRTLAENAGLDPIDILVKLRSAHEKGkkwaGINVFTGEVVDMWELGVIEPLRVKTQAIKSAT 503
|
570
....*....|....
gi 500144914 509 SIAGMVLTTECIVA 522
Cdd:NF041083 504 EAATMILRIDDVIA 517
|
|
| cpn60 |
cd03343 |
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ... |
21-522 |
6.74e-20 |
|
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: 92.71 E-value: 6.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 21 ILAESVAVTLGPKGRNVVLEKKFGAPQIINDGVTIAKEIEledhIENTGVALIRQAASKTNDAAGDGTTTATVLAHAMVK 100
Cdd:cd03343 26 AVAEAVRTTLGPKGMDKMLVDSLGDVTITNDGATILKEMD----IEHPAAKMLVEVAKTQDEEVGDGTTTAVVLAGELLE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 101 AGLRNVAAGANAITLKKGIDKATEFLVGKIEENSKPISDS----------TAIAqcGTIAAGNDEEVGEMIANAMDKVGK 170
Cdd:cd03343 102 KAEDLLDQNIHPTVIIEGYRLAAEKALELLDEIAIKVDPDdkdtlrkiakTSLT--GKGAEAAKDKLADLVVDAVLQVAE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 171 EG---------VISLE--EGKSMTtELEVTEGMRFDKGYISP----------------------------YFATDTERME 211
Cdd:cd03343 180 KRdgkyvvdldNIKIEkkTGGSVD-DTELIRGIVIDKEVVHPgmpkrvenakialldaplevkkteidakIRITSPDQLQ 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 212 AVLDEpyilltdkKIALVQDLVpvlEQIAKTGKPLVIIAEDIEKEALATLVVnrlRGVLNVAAVKapgfgdrrKAMLEDM 291
Cdd:cd03343 259 AFLEQ--------EEAMLKEMV---DKIADTGANVVFCQKGIDDLAQHYLAK---AGILAVRRVK--------KSDMEKL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 292 AVLTNGQLITedaglKLENATLEMLGTGRRITINK--ETTTIVAEG--NEKAVNsrcdqikkqmeetdssydkeklqerl 367
Cdd:cd03343 317 ARATGAKIVT-----NIDDLTPEDLGEAELVEERKvgDDKMVFVEGckNPKAVT-------------------------- 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 368 aklaggvavIKVGAATETEMKDKKLRLEDAINATKAAVEEG-IVPGGGTTLAHLAPILKEWADaTLSGEELIGANIVEAS 446
Cdd:cd03343 366 ---------ILLRGGTEHVVDELERALEDALRVVADALEDGkVVAGGGAVEIELAKRLREYAR-SVGGREQLAVEAFADA 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 447 LTAPLMRIAENAGSNGAVIAENVKSKPFND----GFNAATGEYVDMSSAGIVDPAKVTRSGLQNAASIAGMVLTTECIVA 522
Cdd:cd03343 436 LEEIPRTLAENAGLDPIDTLVELRAAHEKGnknaGLDVYTGEVVDMLEKGVIEPLRVKKQAIKSATEAATMILRIDDVIA 515
|
|
| thermosome_alpha |
NF041082 |
thermosome subunit alpha; |
21-515 |
7.70e-20 |
|
thermosome subunit alpha;
Pssm-ID: 469009 Cd Length: 518 Bit Score: 92.64 E-value: 7.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 21 ILAESVAVTLGPKGRNVVLEKKFGAPQIINDGVTIAKEIEledhIENTGVALIRQAASKTNDAAGDGTTTATVLAHAMVK 100
Cdd:NF041082 28 AVAEAVRTTLGPKGMDKMLVDSLGDVVITNDGVTILKEMD----IEHPAAKMIVEVAKTQDDEVGDGTTTAVVLAGELLK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 101 AGLRNVAAGANAITLKKGIDKATEFLVGKIEENSKPISDS----------TAIAqcGTIAAGNDEEVGEMIANA----MD 166
Cdd:NF041082 104 KAEELLDQDIHPTIIAEGYRLAAEKALEILDEIAIKVDPDdketlkkiaaTAMT--GKGAEAAKDKLADLVVDAvkavAE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 167 KVGKEGV----ISLE--EGKSMtTELEVTEGMRFDKGYISPyfatdteRMEAVLDEPYILL-----------TDKKI--- 226
Cdd:NF041082 182 KDGGYNVdldnIKVEkkVGGSI-EDSELVEGVVIDKERVHP-------GMPKRVENAKIALldaplevkkteIDAKIsit 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 227 -------------ALVQDLVpvlEQIAKTGKPLVIIAEDIEKEA---LATlvvnrlRGVLNVAAVKapgfgdrrKAMLED 290
Cdd:NF041082 254 dpdqlqafldqeeKMLKEMV---DKIADSGANVVFCQKGIDDLAqhyLAK------EGILAVRRVK--------KSDMEK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 291 MAVLTNGQLITedaglKLENATLEMLGTGRRIT---INKETTTIVaEG--NEKAVNsrcdqikkqmeetdssydkeklqe 365
Cdd:NF041082 317 LAKATGARIVT-----SIDDLSPEDLGYAGLVEerkVGGDKMIFV-EGckNPKAVT------------------------ 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 366 rlaklaggvavIKVGAATETEMKDKKLRLEDAINATKAAVEEG-IVPGGGTTLAHLAPILKEWADaTLSGEELIGANIVE 444
Cdd:NF041082 367 -----------ILLRGGTEHVVDEVERALEDALRVVRVVLEDGkVVAGGGAPEVELALRLREYAA-SVGGREQLAIEAFA 434
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 500144914 445 ASLTAPLMRIAENAGSNGAVIAENVKSK----PFNDGFNAATGEYVDMSSAGIVDPAKVTRSGLQNAASIAGMVL 515
Cdd:NF041082 435 EALEIIPRTLAENAGLDPIDALVELRSAhekgNKTAGLDVYTGKVVDMLEIGVVEPLRVKTQAIKSATEAAVMIL 509
|
|
| chap_CCT_epsi |
TIGR02343 |
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ... |
5-523 |
9.03e-16 |
|
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT epsilon chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.
Pssm-ID: 274084 [Multi-domain] Cd Length: 532 Bit Score: 80.23 E-value: 9.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 5 IIYNEQARRALERGIDIL------AESVAVT----LGPKGRNVVLEKKFGAPQIINDGVTIAKEIELEDHIENtgvaLIR 74
Cdd:TIGR02343 12 IIIKDQDNKKRLKGLEAKksniaaAKSVASIlrtsLGPKGMDKMLISPDGDITVTNDGATILSQMDVDNQIAK----LMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 75 QAASKTNDAAGDGTTTATVLAHAMVKAGLRNVAAGANAITLKKGIDKATEFLVGKIEENSKPISDS-----TAIAQCGT- 148
Cdd:TIGR02343 88 ELSKSQDDEIGDGTTGVVVLAGALLEQAEELLDKGIHPIKIADGFEEAARIAVEHLEEISDEISADnnnrePLIQAAKTs 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 149 ----IAAGNDEEVGEMIANA----MDKVGKE---GVISLEE---GKSMTTELevTEGMRFDKGYISPYFATDTERME-AV 213
Cdd:TIGR02343 168 lgskIVSKCHRRFAEIAVDAvlnvADMERRDvdfDLIKVEGkvgGSLEDTKL--IKGIIIDKDFSHPQMPKEVEDAKiAI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 214 LD---EPYILLTDKKIALV-------------QDLVPVLEQIAKTGKPLVIIAEDIEKEALATLVVNRLRGVLNVAAVKa 277
Cdd:TIGR02343 246 LTcpfEPPKPKTKHKLDISsveeykklqkyeqQKFKEMIDDIKKSGANLVICQWGFDDEANHLLLQNDLPAVRWVGGQE- 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 278 pgfgdrrkamLEDMAVLTNGQLITedaglKLENATLEMLGTGRRI------TINKETTTIVAEGNEKAVNsrcdqikkqm 351
Cdd:TIGR02343 325 ----------LELIAIATGGRIVP-----RFQELSKDKLGKAGLVreisfgTTKDRMLVIEQCKNSKAVT---------- 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 352 eetdssydkeklqerlaklaggvavIKVGAATETEMKDKKLRLEDAINATKAAVEEG-IVPGGGTTLAHLAPILKEWADA 430
Cdd:TIGR02343 380 -------------------------IFIRGGNKMIIEEAKRSIHDALCVVRNLIKDSrIVYGGGAAEISCSLAVSQEADK 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 431 TLSGEELIGANIVEASLTAPlMRIAENAGSN-----GAVIAENVKSKPFNDGFNAATGEYVDMSSAGIVDPAKVTRSGLQ 505
Cdd:TIGR02343 435 YPGVEQYAIRAFADALETIP-MALAENSGLDpigtlSTLKSLQLKEKNPNLGVDCLGYGTNDMKEQFVFETLIGKKQQIL 513
|
570
....*....|....*...
gi 500144914 506 NAASIAGMVLTTECIVAD 523
Cdd:TIGR02343 514 LATQLVRMILKIDDVISP 531
|
|
| TCP1_delta |
cd03338 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ... |
22-521 |
6.66e-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: 67.70 E-value: 6.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 22 LAESVAVTLGPKGRNVVLEKKFGAPQIINDGVTIAKEIELeDHientGVALIRQAASKTND-AAGDGTTTATVLAHAMVK 100
Cdd:cd03338 20 VADAIRTSLGPRGMDKMIQTGKGEVIITNDGATILKQMSV-LH----PAAKMLVELSKAQDiEAGDGTTSVVVLAGALLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 101 AGLRNVAAGANAITLKKGIDKATEFLVGKIEENSKPIS--------DSTAIAQCGTIAAGNDEEVGEMIANAMDKVGKEG 172
Cdd:cd03338 95 ACESLLKKGIHPTVISESFQIAAKKAVEILDSMSIPVDlndresliKSATTSLNSKVVSQYSSLLAPIAVDAVLKVIDPA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 173 VISLEEGKSM--------TTE-LEVTEGMRFDKGYISPyfATDTERMEavldepyilltDKKIALVQ------------- 230
Cdd:cd03338 175 TATNVDLKDIrivkklggTIEdTELVDGLVFTQKASKK--AGGPTRIE-----------KAKIGLIQfclsppktdmdnn 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 231 ----D--------------LVPVLEQIAKTGKPLVIIAEDIEKEALATLVVNRLRGvLNVAAVKapgfgDRRKAMLEDMA 292
Cdd:cd03338 242 ivvnDyaqmdrilreerkyILNMCKKIKKSGCNVLLIQKSILRDAVSDLALHFLAK-LKIMVVK-----DIEREEIEFIC 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 293 VLTNGQLITEdaglkLENATLEMLGTGRRItinketttivaegnekavnsrcdqikkqmEETDSSYDKEKLQERLAKLAG 372
Cdd:cd03338 316 KTIGCKPVAS-----IDHFTEDKLGSADLV-----------------------------EEVSLGDGKIVKITGVKNPGK 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 373 GVAVIkVGAATETEMKDKKLRLEDAINATKAAVEE-GIVPGGGTTLAHLAPILKEWADaTLSGEE-LIGANIVEASLTAP 450
Cdd:cd03338 362 TVTIL-VRGSNKLVLDEAERSLHDALCVIRCLVKKrALIPGGGAPEIEIALQLSEWAR-TLTGVEqYCVRAFADALEVIP 439
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 500144914 451 LMrIAENAGSNGAVIAENVKSKPF----NDGFNAATGEYVDMSSAGIVDPAKVTRSGLQNAASIAGMVLTTECIV 521
Cdd:cd03338 440 YT-LAENAGLNPISIVTELRNRHAqgekNAGINVRKGAITNILEENVVQPLLVSTSAITLATETVRMILKIDDIV 513
|
|
| TCP1_epsilon |
cd03339 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ... |
5-140 |
1.74e-09 |
|
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: 60.39 E-value: 1.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 5 IIYNEQARRALERGID-----ILA-ESVAVT----LGPKGRNVVLEKKFGAPQIINDGVTIAKEIELEDHIENTGVALir 74
Cdd:cd03339 8 IIVREQEKKKRLKGLEahkshILAaKSVANIlrtsLGPRGMDKILVSPDGEVTVTNDGATILEKMDVDHQIAKLLVEL-- 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 500144914 75 qaaSKTNDAA-GDGTTTATVLAHAMVKAGLRNVAAGANAITLKKGIDKATEFLVGKIEENSKPISDS 140
Cdd:cd03339 86 ---SKSQDDEiGDGTTGVVVLAGALLEQAEKLLDRGIHPIRIADGYEQACKIAVEHLEEIADKIEFS 149
|
|
| chap_CCT_eta |
TIGR02345 |
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ... |
22-515 |
4.02e-09 |
|
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: 59.00 E-value: 4.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 22 LAESVAVTLGPKGRNVVLEKKFGAPQIINDGVTIAKEIELEDHIENTGVALirqaaSKTNDA-AGDGTTTATVLAHAMVK 100
Cdd:TIGR02345 30 IAEALKTTLGPRGMDKLIVGSNGKATISNDGATILKLLDIVHPAAKTLVDI-----AKSQDAeVGDGTTSVTILAGELLK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 101 AGLRNVAAGANAITLKKGIDKATEFLVGKIEENSKPISDSTA-----IAQCGTIA------AGNDEEVGEMIANAMDKVG 169
Cdd:TIGR02345 105 EAKPFIEEGVHPQLIIRCYREALSLAVEKIKEIAVTIDEEKGeqrelLEKCAATAlsskliSHNKEFFSKMIVDAVLSLD 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 170 KEGV------ISLEEGKSMTTELEVtEGMRFDKGYISPYFatdtERMEAVLDEPYILLTDKKIALvqdlvpvleQIAKTG 243
Cdd:TIGR02345 185 RDDLdlkligIKKVQGGALEDSQLV-NGVAFKKTFSYAGF----EQQPKKFANPKILLLNVELEL---------KAEKDN 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 244 KPLVIiaEDIEK-----EALATLVVNRLRGVL----NVAAVKAPgFGDRRKAMLEDMAVLTNGQLITEDAGLKlenatle 314
Cdd:TIGR02345 251 AEIRV--EDVEDyqaivDAEWAIIFRKLEKIVesgaNVVLSKLP-IGDLATQYFADRDIFCAGRVSAEDLKRV------- 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 315 MLGTGRRItinkETTTivaEGNEKAVNSRCdqikKQMEETDSSYDKEKLQERLAKLAGGVAVIKVGAatETEMKDKKLRL 394
Cdd:TIGR02345 321 IKACGGSI----QSTT---SDLEADVLGTC----ALFEERQIGSERYNYFTGCPHAKTCTIILRGGA--EQFIEEAERSL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 395 EDAINATKAAVE-EGIVPGGGTTLAHLAPILKEWAdATLSGEELIGANIVEASLTAPLMRIAENAGSNGAVIAENVKSKP 473
Cdd:TIGR02345 388 HDAIMIVRRALKnKKIVAGGGAIEMELSKCLRDYS-KTIDGKQQLIINAFAKALEIIPRQLCENAGFDSIEILNKLRSRH 466
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 500144914 474 FNDGFNAA----TGEYVDMSSAGIVDPAKVTRSGLQNAASIAGMVL 515
Cdd:TIGR02345 467 AKGGKWYGvdinTEDIGDNFEAFVWEPALVKINALKAAFEAACTIL 512
|
|
| TCP1_eta |
cd03340 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ... |
21-141 |
2.42e-07 |
|
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: 53.45 E-value: 2.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 21 ILAESVAVTLGPKGRNVVLEKKFGAPQIINDGVTIAKEIELEDHIENTGVALirqaaSKTNDA-AGDGTTTATVLAHAMV 99
Cdd:cd03340 27 AIADAVRTTLGPRGMDKLIVDGRGKVTISNDGATILKLLDIVHPAAKTLVDI-----AKSQDAeVGDGTTSVVVLAGEFL 101
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 500144914 100 KAGLRNVAAGANAITLKKGIDKATEFLVGKIEENSKPISDST 141
Cdd:cd03340 102 KEAKPFIEDGVHPQIIIRGYRKALQLAIEKIKEIAVNIDKED 143
|
|
| TCP1_beta |
cd03336 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ... |
9-100 |
1.70e-06 |
|
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: 50.79 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 9 EQARRALERGIDILAESVAVTLGPKGRNVVLE--KKFGAPQIINDGVTIAKEIeledHIENTgVALIRQAASKTND-AAG 85
Cdd:cd03336 12 ETARLSSFVGAIAIGDLVKTTLGPKGMDKILQsvGRSGGVTVTNDGATILKSI----GVDNP-AAKVLVDISKVQDdEVG 86
|
90
....*....|....*
gi 500144914 86 DGTTTATVLAHAMVK 100
Cdd:cd03336 87 DGTTSVTVLAAELLR 101
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
22-134 |
6.94e-06 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 48.87 E-value: 6.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 22 LAESVAVTLGPKGRNVVLEKKFGAPQ-----IINDGVTIAKEIELEDhientGVALIRQAASKTNDA-AGDGTTTATVLA 95
Cdd:PTZ00212 34 VADLVKTTLGPKGMDKILQPMSEGPRsgnvtVTNDGATILKSVWLDN-----PAAKILVDISKTQDEeVGDGTTSVVVLA 108
|
90 100 110
....*....|....*....|....*....|....*....
gi 500144914 96 HAMVKAGLRNVAAGANAITLKKGIDKATEFLVGKIEENS 134
Cdd:PTZ00212 109 GELLREAEKLLDQKIHPQTIIEGWRMALDVARKALEEIA 147
|
|
| chap_CCT_delta |
TIGR02342 |
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ... |
22-140 |
7.83e-06 |
|
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: 48.63 E-value: 7.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 22 LAESVAVTLGPKGRNVVLEKKFGAPQIINDGVTIAKEIELEDHIENTGVALirqaaSKTND-AAGDGTTTATVLAHAMVK 100
Cdd:TIGR02342 21 VADAIRTSLGPKGMDKMIQDGKGEVIITNDGATILKQMAVLHPAAKMLVEL-----SKAQDiEAGDGTTSVVILAGALLG 95
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 500144914 101 AGLRNVAAGANAITLKKGIDKATEFLVGKIEENSKPISDS 140
Cdd:TIGR02342 96 ACERLLNKGIHPTIISESFQSAADEAIKILDEMSIPVDLS 135
|
|
| TCP1_zeta |
cd03342 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
383-511 |
1.44e-05 |
|
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: 47.64 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 383 TETEMKDKklrLEDAINATKAAVEEG-IVPGGGTTLAHLAPILKEWADaTLSGEELIGANIVEASLTAPLMRIAENAGSN 461
Cdd:cd03342 341 TITQIKDA---IRDGLRAVKNAIEDKcVVPGAGAFEVALYAHLKEFKK-SVKGKAKLGVQAFADALLVIPKTLAENSGLD 416
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 500144914 462 G-----AVIAENVKSKPfNDGFNAATGEYVDMSSAGIVDPAKVTRSGLQNAASIA 511
Cdd:cd03342 417 VqetlvKLQDEYAEGGQ-VGGVDLDTGEPMDPESEGIWDNYSVKRQILHSATVIA 470
|
|
| chap_CCT_zeta |
TIGR02347 |
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ... |
22-208 |
5.52e-05 |
|
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: 45.88 E-value: 5.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 22 LAESVAVTLGPKGRNVVLEKKFGAPQIINDGVTIAKEIeledHIENTGVALIRQAASKTNDAAGDGTTTATVLAHAMVKA 101
Cdd:TIGR02347 28 LQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEM----QIQHPTASMIARAATAQDDITGDGTTSTVLLIGELLKQ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 102 GLRNVAAGANAITLKKGIDKAT--------EFLVGKIEENSKPISDSTAIAQCGT-IAAGNDEEVGEMIANAMDKVGKEG 172
Cdd:TIGR02347 104 AERYILEGVHPRIITEGFEIARkealqfldKFKVKKEDEVDREFLLNVARTSLRTkLPADLADQLTEIVVDAVLAIKKDG 183
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 500144914 173 -------VISLEEGKSMTTELEVTEGMRFDKGYISPYFATDTE 208
Cdd:TIGR02347 184 edidlfmVEIMEMKHKSATDTTLIRGLVLDHGARHPDMPRRVK 226
|
|
| chap_CCT_beta |
TIGR02341 |
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ... |
9-528 |
5.41e-04 |
|
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: 42.54 E-value: 5.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 9 EQARRALERGIDILAESVAVTLGPKGRNVVLEK--KFGAPQIINDGVTIAKEIELEdhieNTGVALIRQAASKTNDAAGD 86
Cdd:TIGR02341 13 ENARLSSFVGAIAIGDLVKSTLGPKGMDKILQSssSDASIMVTNDGATILKSIGVD----NPAAKVLVDMSKVQDDEVGD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 87 GTTTATVLAHAMVKAGLRNVAAGANAITLKKGIDKATEFLVGKIEENSkpisdstaiaqcgtIAAGNDEevgEMIANAMD 166
Cdd:TIGR02341 89 GTTSVTVLAAELLREAEKLINQKIHPQTIIAGYREATKAARDALLKSA--------------VDNGSDE---VKFRQDLM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 167 KVGKEGVIS--LEEGKSMTTELEVTEGMRFdKG-----YISPYFATDTERMEAVLDEPYILltDKKIALVQdlvPVLEQI 239
Cdd:TIGR02341 152 NIARTTLSSkiLSQHKDHFAQLAVDAVLRL-KGsgnleAIQIIKKLGGSLADSYLDEGFLL--DKKIGVNQ---PKRIEN 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 240 AKtgkplVIIAE---DIEKEALATLVVnRLRGVLNVAAVKAPgfgdRRKAMLEDMA--------VLTNGQLITE------ 302
Cdd:TIGR02341 226 AK-----ILIANtgmDTDKVKIFGSRV-RVDSTAKVAELEHA----EKEKMKEKVEkilkhginCFINRQLIYNypeqlf 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 303 -DAG-LKLENATLEmlGTGRRITINKETTTIVAEGNEKAVNSRCDQIKKQMEETDssydkeKLQERLAKLAGGVAVIKVG 380
Cdd:TIGR02341 296 aDAGvMAIEHADFE--GVERLALVTGGEIVSTFDHPELVKLGSCDLIEEIMIGED------KLLKFSGVKLGEACTIVLR 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 381 AATETEMKDKKLRLEDAINATKAAVEEG-IVPGGGTTLAHLAPILKEWADATLSGEELIGANIVEASLTAPLMrIAENAG 459
Cdd:TIGR02341 368 GATQQILDEAERSLHDALCVLSQTVKESrTVLGGGCSEMLMSKAVTQEAQRTPGKEALAVEAFARALRQLPTI-IADNAG 446
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500144914 460 SNGAVIAENVKSKPFND----GFNAATGEYVDMSSAGIVDPAKVTRSGLQNAASIAGMVLTTECIVADMPEKK 528
Cdd:TIGR02341 447 FDSAELVAQLRAAHYNGnttmGLDMNEGTIADMRQLGITESYKVKRAVVSSAAEAAEVILRVDNIIKAAPRKR 519
|
|
| TCP1_zeta |
cd03342 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
30-137 |
6.05e-04 |
|
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.
Pssm-ID: 239458 [Multi-domain] Cd Length: 484 Bit Score: 42.63 E-value: 6.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 30 LGPKGRNVVLEKKFGAPQIINDGVTIAKEIeledHIENTGVALIRQAASKTNDAAGDGTTTATVLAHAMVKAGLRNVAAG 109
Cdd:cd03342 32 LGPKGTLKMLVSGAGDIKLTKDGNVLLSEM----QIQHPTASMIARAATAQDDITGDGTTSNVLLIGELLKQAERYIQEG 107
|
90 100
....*....|....*....|....*...
gi 500144914 110 ANAITLKKGIDKATEFLVGKIEENSKPI 137
Cdd:cd03342 108 VHPRIITEGFELAKNKALKFLESFKVPV 135
|
|
| TCP1_theta |
cd03341 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ... |
374-521 |
6.63e-04 |
|
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: 42.21 E-value: 6.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 374 VAVIKVGAATETEMKDKKLRLEDAINATKAAVEEG-IVPGGGTTLAHLAPILKEWADATLSGEELIGANIVEASLTAPlm 452
Cdd:cd03341 316 IATIVLRGATQNILDDVERAIDDGVNVFKSLTKDGrFVPGAGATEIELAKKLKEYGEKTPGLEQYAIKKFAEAFEVVP-- 393
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 500144914 453 RI-AENAGSNG-----AVIAENVKSKPfNDGFNAATGEY--VDMSSAGIVDPAKVTRSGLQNAASIAGMVLTTECIV 521
Cdd:cd03341 394 RTlAENAGLDAtevlsELYAAHQKGNK-SAGVDIESGDEgtKDAKEAGIFDHLATKKWAIKLATEAAVTVLRVDQII 469
|
|
| chap_CCT_alpha |
TIGR02340 |
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ... |
22-133 |
1.00e-02 |
|
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: 38.55 E-value: 1.00e-02
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144914 22 LAESVAVTLGPKGRNVVLEKKFGAPQIINDGVTIAKEIEledhIENTGVALIRQAASKTNDAAGDGTTTATVLAHAMVKA 101
Cdd:TIGR02340 24 IANIVKTSLGPVGLDKMLVDDIGDVTITNDGATILKLLE----VEHPAAKILVELAQLQDREVGDGTTSVVIIAAELLKR 99
|
90 100 110
....*....|....*....|....*....|..
gi 500144914 102 GLRNVAAGANAITLKKGIDKATEFLVGKIEEN 133
Cdd:TIGR02340 100 ADELVKNKIHPTSVISGYRLACKEAVKYIKEN 131
|
|
| |
