|
Name |
Accession |
Description |
Interval |
E-value |
| groEL |
CHL00093 |
chaperonin GroEL |
1-526 |
0e+00 |
|
chaperonin GroEL
Pssm-ID: 177025 Cd Length: 529 Bit Score: 984.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 1 MAKRIIYNENARRALEKGIDILAEAVAVTLGPKGRNVVLEKKFGAPQIVNDGVTIAKEIELEDHIENTGVSLIRQAASKT 80
Cdd:CHL00093 1 MSKKILYQDNARRALERGMDILAEAVSVTLGPKGRNVVLEKKYGSPQIVNDGVTIAKEIELEDHIENTGVALIRQAASKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 81 NDAAGDGTTTATVLAHAIVKEGLRNVAAGANAIQLKRGIDKATAFLVDKIAEHARPVEDSKAIAQVGSISAGNDEEVGQM 160
Cdd:CHL00093 81 NDVAGDGTTTATVLAYAIVKQGMKNVAAGANPISLKRGIEKATQYVVSQIAEYARPVEDIQAITQVASISAGNDEEVGSM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 161 IAEAMDKVGKEGVISLEEGKSMTTELEITEGMRFDKGYISPYFATDAERMEAVFDDPYILLTDKKIALV-QDLVPVLEQV 239
Cdd:CHL00093 161 IADAIEKVGREGVISLEEGKSTVTELEITEGMRFEKGFISPYFVTDTERMEVVQENPYILLTDKKITLVqQDLLPILEQV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 240 ARQGKPLVIIAEDIEKEALATLVVNRLRGVLNVAAVKAPGFGDRRKAMLEDIAVLTGGQVITEDAGLKLENTKLDSLGKA 319
Cdd:CHL00093 241 TKTKRPLLIIAEDVEKEALATLVLNKLRGIVNVVAVRAPGFGDRRKAMLEDIAILTGGQVITEDAGLSLETIQLDLLGQA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 320 RRITITKDNTTVVAEGNEAAVKARCEQIRRQMDETESSYDKEKLQERLAKLSGGVAVVKVGAATETEMKDKKLRLEDAIN 399
Cdd:CHL00093 321 RRIIVTKDSTTIIADGNEEQVKARCEQLRKQIEIADSSYEKEKLQERLAKLSGGVAVIKVGAATETEMKDKKLRLEDAIN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 400 ATKAAVEEGIVPGGGTTLAHLAPHLEEWANKTLTSEELTGALIVARALPAPLKRIAENAGQNGAVIAERVKEKEFNVGFN 479
Cdd:CHL00093 401 ATKAAVEEGIVPGGGATLVHLSENLKTWAKNNLKEDELIGALIVARAILAPLKRIAENAGKNGSVIIEKVQEQDFEIGYN 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 950121894 480 ASTNEFVDMLAAGIVDPAKVTRSALQNAASIAGMVLTTECIVVDKPE 526
Cdd:CHL00093 481 AANNKFVNMYEAGIIDPAKVTRSALQNAASIASMILTTECIIVDKKE 527
|
|
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
1-529 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 949.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 1 MAKRIIYNENARRALEKGIDILAEAVAVTLGPKGRNVVLEKKFGAPQIVNDGVTIAKEIELEDHIENTGVSLIRQAASKT 80
Cdd:PRK00013 1 MAKDIKFGEDARRKLLRGVNKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDPFENMGAQLVKEVASKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 81 NDAAGDGTTTATVLAHAIVKEGLRNVAAGANAIQLKRGIDKATAFLVDKIAEHARPVEDSKAIAQVGSISAGNDEEVGQM 160
Cdd:PRK00013 81 NDVAGDGTTTATVLAQAIVREGLKNVAAGANPMDLKRGIDKAVEAAVEELKKISKPVEDKEEIAQVATISANGDEEIGKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 161 IAEAMDKVGKEGVISLEEGKSMTTELEITEGMRFDKGYISPYFATDAERMEAVFDDPYILLTDKKIALVQDLVPVLEQVA 240
Cdd:PRK00013 161 IAEAMEKVGKEGVITVEESKGFETELEVVEGMQFDRGYLSPYFVTDPEKMEAELENPYILITDKKISNIQDLLPVLEQVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 241 RQGKPLVIIAEDIEKEALATLVVNRLRGVLNVAAVKAPGFGDRRKAMLEDIAVLTGGQVITEDAGLKLENTKLDSLGKAR 320
Cdd:PRK00013 241 QSGKPLLIIAEDVEGEALATLVVNKLRGTLKVVAVKAPGFGDRRKAMLEDIAILTGGTVISEELGLKLEDATLEDLGQAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 321 RITITKDNTTVV-AEGNEAAVKARCEQIRRQMDETESSYDKEKLQERLAKLSGGVAVVKVGAATETEMKDKKLRLEDAIN 399
Cdd:PRK00013 321 KVVVTKDNTTIVdGAGDKEAIKARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATEVEMKEKKDRVEDALH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 400 ATKAAVEEGIVPGGGTTLAHLAPHLEEwaNKTLTSEELTGALIVARALPAPLKRIAENAGQNGAVIAERVKE-KEFNVGF 478
Cdd:PRK00013 401 ATRAAVEEGIVPGGGVALLRAAPALEA--LKGLNGDEATGINIVLRALEAPLRQIAENAGLEGSVVVEKVKNgKGKGYGY 478
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 950121894 479 NASTNEFVDMLAAGIVDPAKVTRSALQNAASIAGMVLTTECIVVDKPEPKE 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: 872.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 3 KRIIYNENARRALEKGIDILAEAVAVTLGPKGRNVVLEKKFGAPQIVNDGVTIAKEIELEDHIENTGVSLIRQAASKTND 82
Cdd:cd03344 1 KDIKFGEEARKALLRGVNKLADAVKVTLGPKGRNVVIEKSFGSPKITKDGVTVAKEIELEDPFENMGAQLVKEVASKTND 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 83 AAGDGTTTATVLAHAIVKEGLRNVAAGANAIQLKRGIDKATAFLVDKIAEHARPVEDSKAIAQVGSISAGNDEEVGQMIA 162
Cdd:cd03344 81 VAGDGTTTATVLARAIIKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKPVKTKEEIAQVATISANGDEEIGELIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 163 EAMDKVGKEGVISLEEGKSMTTELEITEGMRFDKGYISPYFATDAERMEAVFDDPYILLTDKKIALVQDLVPVLEQVARQ 242
Cdd:cd03344 161 EAMEKVGKDGVITVEEGKTLETELEVVEGMQFDRGYLSPYFVTDPEKMEVELENPYILLTDKKISSIQELLPILELVAKA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 243 GKPLVIIAEDIEKEALATLVVNRLRGVLNVAAVKAPGFGDRRKAMLEDIAVLTGGQVITEDAGLKLENTKLDSLGKARRI 322
Cdd:cd03344 241 GRPLLIIAEDVEGEALATLVVNKLRGGLKVCAVKAPGFGDRRKAMLEDIAILTGGTVISEELGLKLEDVTLEDLGRAKKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 323 TITKDNTTVVA-EGNEAAVKARCEQIRRQMDETESSYDKEKLQERLAKLSGGVAVVKVGAATETEMKDKKLRLEDAINAT 401
Cdd:cd03344 321 VVTKDDTTIIGgAGDKAAIKARIAQIRKQIEETTSDYDKEKLQERLAKLSGGVAVIKVGGATEVELKEKKDRVEDALNAT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 402 KAAVEEGIVPGGGTTLAHLAPHLEEWanKTLTSEELTGALIVARALPAPLKRIAENAGQNGAVIAERVKEKEFNVGFNAS 481
Cdd:cd03344 401 RAAVEEGIVPGGGVALLRASPALDKL--KALNGDEKLGIEIVRRALEAPLRQIAENAGVDGSVVVEKVLESPDGFGYDAA 478
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 950121894 482 TNEFVDMLAAGIVDPAKVTRSALQNAASIAGMVLTTECIVVD 523
Cdd:cd03344 479 TGEYVDMIEAGIIDPTKVVRSALQNAASVASLLLTTEALVVD 520
|
|
| groEL |
PRK12849 |
chaperonin GroEL; Reviewed |
1-529 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237230 Cd Length: 542 Bit Score: 859.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 1 MAKRIIYNENARRALEKGIDILAEAVAVTLGPKGRNVVLEKKFGAPQIVNDGVTIAKEIELEDHIENTGVSLIRQAASKT 80
Cdd:PRK12849 1 MAKIIKFDEEARRALERGVNKLADAVKVTLGPKGRNVVIDKSFGAPTITKDGVSIAKEIELEDPFENLGAQLVKEVASKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 81 NDAAGDGTTTATVLAHAIVKEGLRNVAAGANAIQLKRGIDKATAFLVDKIAEHARPVEDSKAIAQVGSISAGNDEEVGQM 160
Cdd:PRK12849 81 NDVAGDGTTTATVLAQALVQEGLKNVAAGANPMDLKRGIDKAVEAVVEELKALARPVSGSEEIAQVATISANGDEEIGEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 161 IAEAMDKVGKEGVISLEEGKSMTTELEITEGMRFDKGYISPYFATDAERMEAVFDDPYILLTDKKIALVQDLVPVLEQVA 240
Cdd:PRK12849 161 IAEAMEKVGKDGVITVEESKTLETELEVTEGMQFDRGYLSPYFVTDPERMEAVLEDPLILLTDKKISSLQDLLPLLEKVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 241 RQGKPLVIIAEDIEKEALATLVVNRLRGVLNVAAVKAPGFGDRRKAMLEDIAVLTGGQVITEDAGLKLENTKLDSLGKAR 320
Cdd:PRK12849 241 QSGKPLLIIAEDVEGEALATLVVNKLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGLKLEEVTLDDLGRAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 321 RITITKDNTTVVA-EGNEAAVKARCEQIRRQMDETESSYDKEKLQERLAKLSGGVAVVKVGAATETEMKDKKLRLEDAIN 399
Cdd:PRK12849 321 RVTITKDNTTIVDgAGDKEAIEARVAQIRRQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATEVELKERKDRVEDALN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 400 ATKAAVEEGIVPGGGTTLAHLAPHLEEwaNKTLTSEELTGALIVARALPAPLKRIAENAGQNGAVIAERVKEKEFNVGFN 479
Cdd:PRK12849 401 ATRAAVEEGIVPGGGVALLRAAKALDE--LAGLNGDQAAGVEIVRRALEAPLRQIAENAGLDGSVVVAKVLELEDGFGFN 478
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 950121894 480 ASTNEFVDMLAAGIVDPAKVTRSALQNAASIAGMVLTTECIVVDKPEPKE 529
Cdd:PRK12849 479 AATGEYGDLIAAGIIDPVKVTRSALQNAASVAGLLLTTEALVADKPEEED 528
|
|
| 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: 850.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 2 AKRIIYNENARRALEKGIDILAEAVAVTLGPKGRNVVLEKKFGAPQIVNDGVTIAKEIELEDHIENTGVSLIRQAASKTN 81
Cdd:TIGR02348 1 AKQIKFDEEARKALLRGVDKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDKFENMGAQLVKEVASKTN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 82 DAAGDGTTTATVLAHAIVKEGLRNVAAGANAIQLKRGIDKATAFLVDKIAEHARPVEDSKAIAQVGSISAGNDEEVGQMI 161
Cdd:TIGR02348 81 DVAGDGTTTATVLAQAIVKEGLKNVAAGANPIELKRGIEKAVEAVVEELKKLSKPVKGKKEIAQVATISANNDEEIGSLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 162 AEAMDKVGKEGVISLEEGKSMTTELEITEGMRFDKGYISPYFATDAERMEAVFDDPYILLTDKKIALVQDLVPVLEQVAR 241
Cdd:TIGR02348 161 AEAMEKVGKDGVITVEESKSLETELEVVEGMQFDRGYISPYFVTDAEKMEVELENPYILITDKKISNIKDLLPLLEKVAQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 242 QGKPLVIIAEDIEKEALATLVVNRLRGVLNVAAVKAPGFGDRRKAMLEDIAVLTGGQVITEDAGLKLENTKLDSLGKARR 321
Cdd:TIGR02348 241 SGKPLLIIAEDVEGEALATLVVNKLRGTLNVCAVKAPGFGDRRKAMLEDIAILTGGQVISEELGLKLEEVTLDDLGKAKK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 322 ITITKDNTTVVAE-GNEAAVKARCEQIRRQMDETESSYDKEKLQERLAKLSGGVAVVKVGAATETEMKDKKLRLEDAINA 400
Cdd:TIGR02348 321 VTVDKDNTTIVEGaGDKAAIKARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATETEMKEKKLRIEDALNA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 401 TKAAVEEGIVPGGGTTLAHLAPHLEEWanKTLTSEELTGALIVARALPAPLKRIAENAGQNGAVIAERVKEKEFNVGFNA 480
Cdd:TIGR02348 401 TRAAVEEGIVPGGGVALLRAAAALEGL--KGDGEDEAIGIDIVKRALEAPLRQIAENAGLDGAVVAEKVKELKGNFGFNA 478
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 950121894 481 STNEFVDMLAAGIVDPAKVTRSALQNAASIAGMVLTTECIVVDKPE 526
Cdd:TIGR02348 479 ATGEYEDLVEAGIIDPTKVTRSALQNAASIAGLLLTTEAVVADKPE 524
|
|
| groEL |
PRK12850 |
chaperonin GroEL; Reviewed |
1-529 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237231 Cd Length: 544 Bit Score: 758.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 1 MAKRIIYNENARRALEKGIDILAEAVAVTLGPKGRNVVLEKKFGAPQIVNDGVTIAKEIELEDHIENTGVSLIRQAASKT 80
Cdd:PRK12850 2 AAKEIRFSTDARDRLLRGVNILANAVKVTLGPKGRNVVLEKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVKEVASKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 81 NDAAGDGTTTATVLAHAIVKEGLRNVAAGANAIQLKRGIDKATAFLVDKIAEHARPVEDSKAIAQVGSISAGNDEEVGQM 160
Cdd:PRK12850 82 NDLAGDGTTTATVLAQAIVREGAKLVAAGMNPMDLKRGIDLAVAAVVDELKKIAKKVTSSKEIAQVATISANGDESIGEM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 161 IAEAMDKVGKEGVISLEEGKSMTTELEITEGMRFDKGYISPYFATDAERMEAVFDDPYILLTDKKIALVQDLVPVLEQVA 240
Cdd:PRK12850 162 IAEAMDKVGKEGVITVEEAKTLGTELDVVEGMQFDRGYLSPYFVTNPEKMRAELEDPYILLHEKKISNLQDLLPILEAVV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 241 RQGKPLVIIAEDIEKEALATLVVNRLRGVLNVAAVKAPGFGDRRKAMLEDIAVLTGGQVITEDAGLKLENTKLDSLGKAR 320
Cdd:PRK12850 242 QSGRPLLIIAEDVEGEALATLVVNKLRGGLKSVAVKAPGFGDRRKAMLEDIAVLTGGQVISEDLGIKLENVTLDMLGRAK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 321 RITITKDNTTVV-AEGNEAAVKARCEQIRRQMDETESSYDKEKLQERLAKLSGGVAVVKVGAATETEMKDKKLRLEDAIN 399
Cdd:PRK12850 322 RVLITKENTTIIdGAGDKKNIEARVKQIRAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKEKKDRVDDALH 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 400 ATKAAVEEGIVPGGGTTLAHLAPHLEewANKTLTSEELTGALIVARALPAPLKRIAENAGQNGAVIAERVKEKEFNVGFN 479
Cdd:PRK12850 402 ATRAAVEEGIVPGGGVALLRARSALR--GLKGANADETAGIDIVRRALEEPLRQIATNAGFEGSVVVGKVAELPGNFGFN 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 950121894 480 ASTNEFVDMLAAGIVDPAKVTRSALQNAASIAGMVLTTECIVVDKPEPKE 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: 750.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 1 MAKRIIYNENARRALEKGIDILAEAVAVTLGPKGRNVVLEKKFGAPQIVNDGVTIAKEIELEDHIENTGVSLIRQAASKT 80
Cdd:COG0459 1 MAKQILFGEDARRANIRGVKALADAVKVTLGPKGRNVMLVKSFGDPTITNDGVTIAKEIELEDPFENMGAQLVKEVASKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 81 NDAAGDGTTTATVLAHAIVKEGLRNVAAGANAIQLKRGIDKATAFLVDKIAEHARPVEDSKAIAQVGSISAGNDEEVGQM 160
Cdd:COG0459 81 NDEAGDGTTTATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPVDDKEELAQVATISANGDEEIGEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 161 IAEAMDKVGKEGVISLEEGKSMTTELEITEGMRFDKGYISPYFATDAERMEAVFDDPYILLTDKKIALVQDLVPVLEQVA 240
Cdd:COG0459 161 IAEAMEKVGKDGVITVEEGKGLETELEVVEGMQFDKGYLSPYFVTDPEKMPAELENAYILLTDKKISSIQDLLPLLEKVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 241 RQGKPLVIIAEDIEKEALATLVVNRLRGVLNVAAVKAPGFGDRRKAMLEDIAVLTGGQVITEDAGLKLENTKLDSLGKAR 320
Cdd:COG0459 241 QSGKPLLIIAEDIDGEALATLVVNGIRGVLRVVAVKAPGFGDRRKAMLEDIAILTGGRVISEDLGLKLEDVTLDDLGRAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 321 RITITKDNTTVVAE-GNEAAVkarceqirrqmdetessydkeklqerlaklsggvaVVKVGAATETEMKDKKLRLEDAIN 399
Cdd:COG0459 321 RVEVDKDNTTIVEGaGNPKAI-----------------------------------VILVGAATEVEVKERKRRVEDALH 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 400 ATKAAVEEGIVPGGGTTLAHLAPHLEEWANKtLTSEELTGALIVARALPAPLKRIAENAGQNGAVIAERVKE-KEFNVGF 478
Cdd:COG0459 366 ATRAAVEEGIVPGGGAALLRAARALRELAAK-LEGDEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKVRAaKDKGFGF 444
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 950121894 479 NASTNEFVDMLAAGIVDPAKVTRSALQNAASIAGMVLTTECIVVDKPEPKE 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: 721.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 1 MAKRIIYNENARRALEKGIDILAEAVAVTLGPKGRNVVLEKKFGAPQIVNDGVTIAKEIELEDHIENTGVSLIRQAASKT 80
Cdd:PRK12851 2 AAKEVKFHVEAREKMLRGVNILADAVKVTLGPKGRNVVIDKSFGAPTITNDGVTIAKEIELEDKFENMGAQMVREVASKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 81 NDAAGDGTTTATVLAHAIVKEGLRNVAAGANAIQLKRGIDKATAFLVDKIAEHARPVEDSKAIAQVGSISAGNDEEVGQM 160
Cdd:PRK12851 82 NDVAGDGTTTATVLAQAIVREGAKAVAAGANPMDLKRGIDRAVAAVVEELKANARPVTTNAEIAQVATISANGDAEIGRL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 161 IAEAMDKVGKEGVISLEEGKSMTTELEITEGMRFDKGYISPYFATDAERMEAVFDDPYILLTDKKIALVQDLVPVLEQVA 240
Cdd:PRK12851 162 VAEAMEKVGNEGVITVEESKTAETELEVVEGMQFDRGYLSPYFVTDADKMEAELEDPYILIHEKKISNLQDLLPVLEAVV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 241 RQGKPLVIIAEDIEKEALATLVVNRLRGVLNVAAVKAPGFGDRRKAMLEDIAVLTGGQVITEDAGLKLENTKLDSLGKAR 320
Cdd:PRK12851 242 QSGKPLLIIAEDVEGEALATLVVNKLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGIKLENVTLEQLGRAK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 321 RITITKDNTTVV-AEGNEAAVKARCEQIRRQMDETESSYDKEKLQERLAKLSGGVAVVKVGAATETEMKDKKLRLEDAIN 399
Cdd:PRK12851 322 KVVVEKENTTIIdGAGSKTEIEGRVAQIRAQIEETTSDYDREKLQERLAKLAGGVAVIRVGASTEVEVKEKKDRVDDALH 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 400 ATKAAVEEGIVPGGGTTLAHLAPHLEEwaNKTLTSEELTGALIVARALPAPLKRIAENAGQNGAVIAERVKEKEFNVGFN 479
Cdd:PRK12851 402 ATRAAVEEGIVPGGGVALLRAVKALDK--LETANGDQRTGVEIVRRALEAPVRQIAENAGAEGSVVVGKLREKPGGYGFN 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 950121894 480 ASTNEFVDMLAAGIVDPAKVTRSALQNAASIAGMVLTTECIVVDKPEPKE 529
Cdd:PRK12851 480 AATNEYGDLYAQGVIDPVKVVRTALQNAASVAGLLLTTEAMVAEKPKKEP 529
|
|
| PTZ00114 |
PTZ00114 |
Heat shock protein 60; Provisional |
2-529 |
0e+00 |
|
Heat shock protein 60; Provisional
Pssm-ID: 185455 Cd Length: 555 Bit Score: 710.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 2 AKRIIYNENARRALEKGIDILAEAVAVTLGPKGRNVVLEKKFGAPQIVNDGVTIAKEIELEDHIENTGVSLIRQAASKTN 81
Cdd:PTZ00114 14 GKEIRFGDEARQSLLKGIERLADAVAVTLGPKGRNVIIEQEYGSPKITKDGVTVAKAIEFSDRFENVGAQLIRQVASKTN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 82 DAAGDGTTTATVLAHAIVKEGLRNVAAGANAIQLKRGIDKATAFLVDKIAEHARPVEDSKAIAQVGSISAGNDEEVGQMI 161
Cdd:PTZ00114 94 DKAGDGTTTATILARAIFREGCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQSRPVKTKEDILNVATISANGDVEIGSLI 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 162 AEAMDKVGKEGVISLEEGKSMTTELEITEGMRFDKGYISPYFATDAERMEAVFDDPYILLTDKKIALVQDLVPVLEQVAR 241
Cdd:PTZ00114 174 ADAMDKVGKDGTITVEDGKTLEDELEVVEGMSFDRGYISPYFVTNEKTQKVELENPLILVTDKKISSIQSILPILEHAVK 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 242 QGKPLVIIAEDIEKEALATLVVNRLRGVLNVAAVKAPGFGDRRKAMLEDIAVLTGGQVITEDA-GLKLENTKLDSLGKAR 320
Cdd:PTZ00114 254 NKRPLLIIAEDVEGEALQTLIINKLRGGLKVCAVKAPGFGDNRKDILQDIAVLTGATVVSEDNvGLKLDDFDPSMLGSAK 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 321 RITITKDNTTVV-AEGNEAAVKARCEQIRRQMDETESSYDKEKLQERLAKLSGGVAVVKVGAATETEMKDKKLRLEDAIN 399
Cdd:PTZ00114 334 KVTVTKDETVILtGGGDKAEIKERVELLRSQIERTTSEYDKEKLKERLAKLSGGVAVIKVGGASEVEVNEKKDRIEDALN 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 400 ATKAAVEEGIVPGGGTTLAHLAPHLEEWAN-KTLTSEELTGALIVARALPAPLKRIAENAGQNGAVIAERVKE-KEFNVG 477
Cdd:PTZ00114 414 ATRAAVEEGIVPGGGVALLRASKLLDKLEEdNELTPDQRTGVKIVRNALRLPTKQIAENAGVEGAVVVEKILEkKDPSFG 493
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 950121894 478 FNASTNEFVDMLAAGIVDPAKVTRSALQNAASIAGMVLTTECIVVDKPEPKE 529
Cdd:PTZ00114 494 YDAQTGEYVNMFEAGIIDPTKVVRSALVDAASVASLMLTTEAAIVDLPKEKK 545
|
|
| groEL |
PRK12852 |
chaperonin GroEL; Reviewed |
1-526 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237232 Cd Length: 545 Bit Score: 666.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 1 MAKRIIYNENARRALEKGIDILAEAVAVTLGPKGRNVVLEKKFGAPQIVNDGVTIAKEIELEDHIENTGVSLIRQAASKT 80
Cdd:PRK12852 2 AAKDVKFSGDARDRMLRGVDILANAVKVTLGPKGRNVVIEKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVREVASKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 81 NDAAGDGTTTATVLAHAIVKEGLRNVAAGANAIQLKRGIDKATAFLVDKIAEHARPVEDSKAIAQVGSISAGNDEEVGQM 160
Cdd:PRK12852 82 NDLAGDGTTTATVLAQAIVREGAKAVAAGMNPMDLKRGIDIAVAAVVKDIEKRAKPVASSAEIAQVGTISANGDAAIGKM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 161 IAEAMDKVGKEGVISLEEGKSMTTELEITEGMRFDKGYISPYFATDAERMEAVFDDPYILLTDKKIALVQDLVPVLEQVA 240
Cdd:PRK12852 162 IAQAMQKVGNEGVITVEENKSLETEVDIVEGMKFDRGYLSPYFVTNAEKMTVELDDAYILLHEKKLSGLQAMLPVLEAVV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 241 RQGKPLVIIAEDIEKEALATLVVNRLRGVLNVAAVKAPGFGDRRKAMLEDIAVLTGGQVITEDAGLKLENTKLDSLGKAR 320
Cdd:PRK12852 242 QSGKPLLIIAEDVEGEALATLVVNRLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGQLISEDLGIKLENVTLKMLGRAK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 321 RITITKDNTTVV-AEGNEAAVKARCEQIRRQMDETESSYDKEKLQERLAKLSGGVAVVKVGAATETEMKDKKLRLEDAIN 399
Cdd:PRK12852 322 KVVIDKENTTIVnGAGKKADIEARVGQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKEKKDRVEDALN 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 400 ATKAAVEEGIVPGGGTTLAHLAPHLEEWANKtlTSEELTGALIVARALPAPLKRIAENAGQNGAVIAERVKE-KEFNVGF 478
Cdd:PRK12852 402 ATRAAVQEGIVPGGGVALLRAKKAVGRINND--NADVQAGINIVLKALEAPIRQIAENAGVEGSIVVGKILEnKSETFGF 479
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 950121894 479 NASTNEFVDMLAAGIVDPAKVTRSALQNAASIAGMVLTTECIVVDKPE 526
Cdd:PRK12852 480 DAQTEEYVDMVAKGIIDPAKVVRTALQDAASVAGLLVTTEAMVAELPK 527
|
|
| PLN03167 |
PLN03167 |
Chaperonin-60 beta subunit; Provisional |
2-528 |
0e+00 |
|
Chaperonin-60 beta subunit; Provisional
Pssm-ID: 215611 [Multi-domain] Cd Length: 600 Bit Score: 586.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 2 AKRIIYNEN--ARRALEKGIDILAEAVAVTLGPKGRNVVLEKKFGAPQIVNDGVTIAKEIELEDHIENTGVSLIRQAASK 79
Cdd:PLN03167 56 AKELHFNKDgsAIKKLQAGVNKLADLVGVTLGPKGRNVVLESKYGSPKIVNDGVTVAKEVELEDPVENIGAKLVRQAAAK 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 80 TNDAAGDGTTTATVLAHAIVKEGLRNVAAGANAIQLKRGIDKATAFLVDKIAEHARPVEDSKaIAQVGSISAGNDEEVGQ 159
Cdd:PLN03167 136 TNDLAGDGTTTSVVLAQGLIAEGVKVVAAGANPVQITRGIEKTAKALVKELKKMSKEVEDSE-LADVAAVSAGNNYEVGN 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 160 MIAEAMDKVGKEGVISLEEGKSMTTELEITEGMRFDKGYISPYFATDAERMEAVFDDPYILLTDKKIALVQDLVPVLEQV 239
Cdd:PLN03167 215 MIAEAMSKVGRKGVVTLEEGKSAENNLYVVEGMQFDRGYISPYFVTDSEKMSVEYDNCKLLLVDKKITNARDLIGILEDA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 240 ARQGKPLVIIAEDIEKEALATLVVNRLRGVLNVAAVKAPGFGDRRKAMLEDIAVLTGGQVITEDAGLKLENTKLDSLGKA 319
Cdd:PLN03167 295 IRGGYPLLIIAEDIEQEALATLVVNKLRGSLKIAALKAPGFGERKSQYLDDIAILTGGTVIREEVGLSLDKVGKEVLGTA 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 320 RRITITKDNTTVVAEGN-EAAVKARCEQIRRQMDETESSYDKEKLQERLAKLSGGVAVVKVGAATETEMKDKKLRLEDAI 398
Cdd:PLN03167 375 AKVVLTKDTTTIVGDGStQEAVNKRVAQIKNLIEAAEQDYEKEKLNERIAKLSGGVAVIQVGAQTETELKEKKLRVEDAL 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 399 NATKAAVEEGIVPGGGTTLAHLAPHLEEWANKTLTSEELTGALIVARALPAPLKRIAENAGQNGAVIAERVKEKE-FNVG 477
Cdd:PLN03167 455 NATKAAVEEGIVVGGGCTLLRLASKVDAIKDTLENDEQKVGADIVKRALSYPLKLIAKNAGVNGSVVSEKVLSNDnPKFG 534
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 950121894 478 FNASTNEFVDMLAAGIVDPAKVTRSALQNAASIAGMVLTTECIVVDKPEPK 528
Cdd:PLN03167 535 YNAATGKYEDLMAAGIIDPTKVVRCCLEHAASVAKTFLTSDCVVVEIKEPE 585
|
|
| PRK14104 |
PRK14104 |
chaperonin GroEL; Provisional |
2-526 |
0e+00 |
|
chaperonin GroEL; Provisional
Pssm-ID: 172594 Cd Length: 546 Bit Score: 578.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 2 AKRIIYNENARRALEKGIDILAEAVAVTLGPKGRNVVLEKKFGAPQIVNDGVTIAKEIELEDHIENTGVSLIRQAASKTN 81
Cdd:PRK14104 3 AKEVKFGVDARDRMLRGVDILANAVKVTLGPKGRNVVLDKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVREVASKSA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 82 DAAGDGTTTATVLAHAIVKEGLRNVAAGANAIQLKRGIDKATAFLVDKIAEHARPVEDSKAIAQVGSISAGNDEEVGQMI 161
Cdd:PRK14104 83 DAAGDGTTTATVLAQAIVREGAKSVAAGMNPMDLKRGIDLAVEAVVADLVKNSKKVTSNDEIAQVGTISANGDAEIGKFL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 162 AEAMDKVGKEGVISLEEGKSMTTELEITEGMRFDKGYISPYFATDAERMEAVFDDPYILLTDKKIALVQDLVPVLEQVAR 241
Cdd:PRK14104 163 ADAMKKVGNEGVITVEEAKSLETELDVVEGMQFDRGYISPYFVTNADKMRVEMDDAYILINEKKLSSLNELLPLLEAVVQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 242 QGKPLVIIAEDIEKEALATLVVNRLRGVLNVAAVKAPGFGDRRKAMLEDIAVLTGGQVITEDAGLKLENTKLDSLGKARR 321
Cdd:PRK14104 243 TGKPLVIVAEDVEGEALATLVVNRLRGGLKVAAVKAPGFGDRRKAMLQDIAILTGGQAISEDLGIKLENVTLQMLGRAKK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 322 ITITKDNTTVV-AEGNEAAVKARCEQIRRQMDETESSYDKEKLQERLAKLSGGVAVVKVGAATETEMKDKKLRLEDAINA 400
Cdd:PRK14104 323 VMIDKENTTIVnGAGKKADIEARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKERKDRVDDAMHA 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 401 TKAAVEEGIVPGGGTTLAHLAPHLEEWanKTLTSEELTGALIVARALPAPLKRIAENAGQNGAVIAERVKEKE-FNVGFN 479
Cdd:PRK14104 403 TRAAVEEGIVPGGGVALLRASEQLKGI--KTKNDDQKTGVEIVRKALSAPARQIAINAGEDGSVIVGKILEKEqYSYGFD 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 950121894 480 ASTNEFVDMLAAGIVDPAKVTRSALQNAASIAGMVLTTECIVVDKPE 526
Cdd:PRK14104 481 SQTGEYGNLVSKGIIDPTKVVRTAIQNAASVAALLITTEAMVAELPK 527
|
|
| chaperonin_type_I_II |
cd00309 |
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ... |
3-522 |
2.87e-147 |
|
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: 431.08 E-value: 2.87e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 3 KRIIYNENARRALEKGIDILAEAVAVTLGPKGRNVVLEKKFGAPQIVNDGVTIAKEIEledhIENTGVSLIRQAASKTND 82
Cdd:cd00309 1 KEREFGEEARLSNINAAKALADAVKTTLGPKGMDKMLVDSLGDPTITNDGATILKEIE----VEHPAAKLLVEVAKSQDD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 83 AAGDGTTTATVLAHAIVKEGLRNVAAGANAIQLKRGIDKATAFLVDKIAEHARP--VEDSKAIAQVGSISAG------ND 154
Cdd:cd00309 77 EVGDGTTTVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVPidVEDREELLKVATTSLNsklvsgGD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 155 EEVGQMIAEAMDKVGKE------GVISLEEGKSMT---TELEitEGMRFDKGYISPYfatdaerMEAVFDDPYILLTDKK 225
Cdd:cd00309 157 DFLGELVVDAVLKVGKEngdvdlGVIRVEKKKGGSledSELV--VGMVFDKGYLSPY-------MPKRLENAKILLLDCK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 226 IAlvqdlvpvleqvarqgkpLVIIAED-IEKEALATLVvnrlrgVLNVAAVKApgfgdRRKAMLEDIAVLTGGQVITEda 304
Cdd:cd00309 228 LE------------------YVVIAEKgIDDEALHYLA------KLGIMAVRR-----VRKEDLERIAKATGATIVSR-- 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 305 glkLENTKLDSLGKARRITITK----DNTTVVAEGNeaavkarceqirrqmdetessydkeklqerlaklsGGVAVVKVG 380
Cdd:cd00309 277 ---LEDLTPEDLGTAGLVEETKigdeKYTFIEGCKG-----------------------------------GKVATILLR 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 381 AATETEMKDKKLRLEDAINATKAAVEE-GIVPGGGTTLAHLAPHLEEWAnKTLTSEELTGALIVARALPAPLKRIAENAG 459
Cdd:cd00309 319 GATEVELDEAERSLHDALCAVRAAVEDgGIVPGGGAAEIELSKALEELA-KTLPGKEQLGIEAFADALEVIPRTLAENAG 397
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 950121894 460 QNGAVIAERVKEK----EFNVGFNASTNEFVDMLAAGIVDPAKVTRSALQNAASIAGMVLTTECIVV 522
Cdd:cd00309 398 LDPIEVVTKLRAKhaegGGNAGGDVETGEIVDMKEAGIIDPLKVKRQALKSATEAASLILTIDDIIV 464
|
|
| Cpn60_TCP1 |
pfam00118 |
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ... |
22-524 |
4.44e-90 |
|
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: 285.25 E-value: 4.44e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 22 LAEAVAVTLGPKGRNVVLEKKFGAPQIVNDGVTIAKEIEledhIENTGVSLIRQAASKTNDAAGDGTTTATVLAHAIVKE 101
Cdd:pfam00118 1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELE----IQHPAAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 102 GLRNVAAGANAIQLKRGIDKATAFLVDKIAE-HARPVE--DSKAIAQVGSISAGND------EEVGQMIAEA-------- 164
Cdd:pfam00118 77 AEKLLAAGVHPTTIIEGYEKALEKALEILDSiISIPVEdvDREDLLKVARTSLSSKiisresDFLAKLVVDAvlaipknd 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 165 -MDKVGKEGVISLEEGKSMTTELEitEGMRFDKGYISPyfatdaeRMEAVFDDPYILLTDKKI----------------- 226
Cdd:pfam00118 157 gSFDLGNIGVVKILGGSLEDSELV--DGVVLDKGPLHP-------DMPKRLENAKVLLLNCSLeyektetkatvvlsdae 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 227 -------ALVQDLVPVLEQVARQGKPLVIIAEDIEKEALATLVVNRLRGVLNVaavkapgfgdrRKAMLEDIAVLTGGQV 299
Cdd:pfam00118 228 qlerflkAEEEQILEIVEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMALRRV-----------KKRDLERLAKATGARA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 300 ITEDAGLKLENtkldsLGKARRI---TITKDNTTVVAEGneaavkarceqirrqmdetessydkeklqerlakLSGGVAV 376
Cdd:pfam00118 297 VSSLDDLTPDD-----LGTAGKVeeeKIGDEKYTFIEGC----------------------------------KSPKAAT 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 377 VKVGAATETEMKDKKLRLEDAINATKAAVEE-GIVPGGGTTLAHLAPHLEEWAnKTLTSEELTGALIVARALPAPLKRIA 455
Cdd:pfam00118 338 ILLRGATDHVLDEIERSIHDALCVVKNAIEDpRVVPGGGAVEMELARALREYA-KSVSGKEQLAIEAFAEALEVIPKTLA 416
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 950121894 456 ENAGQNG-AVIAE---RVKEKEFNVGFNASTNEFVDMLAAGIVDPAKVTRSALQNAASIAGMVLTTECIVVDK 524
Cdd:pfam00118 417 ENAGLDPiEVLAElraAHASGEKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKSATEAASTILRIDDIIKAK 489
|
|
| chaperonin_like |
cd03333 |
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ... |
141-407 |
3.98e-37 |
|
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings, each composed of 7-9 subunits. There are 2 main chaperonin groups. The symmetry of type I is seven-fold and they are found in eubacteria (GroEL) and in organelles of eubacterial descent (hsp60 and RBP). The symmetry of type II is eight- or nine-fold and they are found in archea (thermosome), thermophilic bacteria (TF55) and in the eukaryotic cytosol (CTT). Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. This superfamily also contains related domains from Fab1-like phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinases that only contain the intermediate and apical domains.
Pssm-ID: 239449 [Multi-domain] Cd Length: 209 Bit Score: 136.44 E-value: 3.98e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 141 KAIAQVGSISAG-----NDEEVGQMIAEAMDKVGKE------GVISLEEGKSMT-TELEITEGMRFDKGYISPYfatdae 208
Cdd:cd03333 2 ELLLQVATTSLNsklssWDDFLGKLVVDAVLKVGPDnrmddlGVIKVEKIPGGSlEDSELVVGVVFDKGYASPY------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 209 rMEAVFDDPYILLTDKKIALVqdlvpvleqvarqgkplvIIAED-IEKEALATLVVnrlrgvLNVAAVKApgfgdRRKAM 287
Cdd:cd03333 76 -MPKRLENAKILLLDCPLEYV------------------VIAEKgIDDLALHYLAK------AGIMAVRR-----VKKED 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 288 LEDIAVLTGGQVITEdaglkLENTKLDSLGKARRITITK--DNTTVVAEGNEaavkarceqirrqmdetessydkeklqe 365
Cdd:cd03333 126 LERIARATGATIVSS-----LEDLTPEDLGTAELVEETKigEEKLTFIEGCK---------------------------- 172
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 950121894 366 rlaklSGGVAVVKVGAATETEMKDKKLRLEDAINATKAAVEE 407
Cdd:cd03333 173 -----GGKAATILLRGATEVELDEVKRSLHDALCAVRAAVEE 209
|
|
| thermosome_beta |
NF041083 |
thermosome subunit beta; |
12-515 |
6.08e-24 |
|
thermosome subunit beta;
Pssm-ID: 469010 Cd Length: 519 Bit Score: 105.42 E-value: 6.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 12 RRALEKGID---ILAEAVAVTLGPKGRNVVLEKKFGAPQIVNDGVTIAKEIEledhIENTGVSLIRQAASKTNDAAGDGT 88
Cdd:NF041083 16 RDAQRNNIMaakAVAEAVRTTLGPKGMDKMLVDSLGDIVITNDGATILKEMD----VQHPAAKMLVEVAKTQDDEVGDGT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 89 TTATVLAHAIVKEGL----RNVAAGANAIQLKRGIDKATAFLvDKIAEHARPVEDS--KAIAQV---GSISAGNDEEVGQ 159
Cdd:NF041083 92 TTAVVLAGELLKKAEelldQNIHPTIIANGYRLAAEKAIEIL-DEIAEKVDPDDREtlKKIAETsltSKGVEEARDYLAE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 160 MIAEAMDKV-----GKEGV----ISLE--EGKSMtTELEITEGMRFDKGYISPyfatdaeRMEAVFDDPYILL------- 221
Cdd:NF041083 171 IAVKAVKQVaekrdGKYYVdldnIQIEkkHGGSI-EDTQLIYGIVIDKEVVHP-------GMPKRVENAKIALldaplev 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 222 ----TDKKI----------------ALVQDLVpvlEQVARQGKPLVIIAEDIEKEA---LATlvvnrlRGVLNVAAVKap 278
Cdd:NF041083 243 kkteIDAEIritdpdqlqkfldqeeKMLKEMV---DKIKATGANVVFCQKGIDDLAqhyLAK------AGILAVRRVK-- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 279 gfgdrrKAMLEDIAVLTGGQVITedaglKLENTKLDSLGKARRIT---ITKDNTTVVaEGNEaAVKARCEQIR----RQM 351
Cdd:NF041083 312 ------KSDMEKLAKATGARIVT-----NIDDLTPEDLGYAELVEerkVGDDKMVFV-EGCK-NPKAVTILIRggteHVV 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 352 DETESSydkeklqerlaklsggvavvkvgaatetemkdkklrLEDAINATKAAVEEG-IVPGGGTTLAHLAPHLEEWAnK 430
Cdd:NF041083 379 DEAERA------------------------------------LEDALSVVADAVEDGkIVAGGGAPEVELAKRLREYA-A 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 431 TLTSEELTGALIVARALPAPLKRIAENAGQN--GAVIAERVKEKEFNV--GFNASTNEFVDMLAAGIVDPAKVTRSALQN 506
Cdd:NF041083 422 TVGGREQLAVEAFAEALEIIPRTLAENAGLDpiDILVKLRSAHEKGKKwaGINVFTGEVVDMWELGVIEPLRVKTQAIKS 501
|
....*....
gi 950121894 507 AASIAGMVL 515
Cdd:NF041083 502 ATEAATMIL 510
|
|
| thermosome_alpha |
NF041082 |
thermosome subunit alpha; |
21-515 |
2.59e-22 |
|
thermosome subunit alpha;
Pssm-ID: 469009 Cd Length: 518 Bit Score: 100.34 E-value: 2.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 21 ILAEAVAVTLGPKGRNVVLEKKFGAPQIVNDGVTIAKEIEledhIENTGVSLIRQAASKTNDAAGDGTTTATVLAHAIVK 100
Cdd:NF041082 28 AVAEAVRTTLGPKGMDKMLVDSLGDVVITNDGVTILKEMD----IEHPAAKMIVEVAKTQDDEVGDGTTTAVVLAGELLK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 101 --EGL--RNVAAGANAIQLKRGIDKATAFLvDKIAEHARPvEDSKAIAQVG--SISAGNDEEVGQMIAE--------AMD 166
Cdd:NF041082 104 kaEELldQDIHPTIIAEGYRLAAEKALEIL-DEIAIKVDP-DDKETLKKIAatAMTGKGAEAAKDKLADlvvdavkaVAE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 167 KVGKEGV----ISLE--EGKSMtTELEITEGMRFDKGYISPyfatdaeRMEAVFDDPYILL-----------TDKKIALV 229
Cdd:NF041082 182 KDGGYNVdldnIKVEkkVGGSI-EDSELVEGVVIDKERVHP-------GMPKRVENAKIALldaplevkkteIDAKISIT 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 230 --QDLVPVLEQVARQGKPLViiaeDIEKEALATLVVNRlRGVLNVAA---VKAPGFGDRR--KAMLEDIAVLTGGQVITe 302
Cdd:NF041082 254 dpDQLQAFLDQEEKMLKEMV----DKIADSGANVVFCQ-KGIDDLAQhylAKEGILAVRRvkKSDMEKLAKATGARIVT- 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 303 daglKLENTKLDSLGKARRIT---ITKDNTTVVaEGNEAAvKARCEQIR----RQMDETESSydkeklqerlaklsggva 375
Cdd:NF041082 328 ----SIDDLSPEDLGYAGLVEerkVGGDKMIFV-EGCKNP-KAVTILLRggteHVVDEVERA------------------ 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 376 vvkvgaatetemkdkklrLEDAINATKAAVEEG-IVPGGGTTLAHLAPHLEEWANKT-----LTSEELTGAL-IVARALp 448
Cdd:NF041082 384 ------------------LEDALRVVRVVLEDGkVVAGGGAPEVELALRLREYAASVggreqLAIEAFAEALeIIPRTL- 444
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 950121894 449 aplkriAENAGQN--GAVIAERVK--EKEFNVGFNASTNEFVDMLAAGIVDPAKVTRSALQNAASIAGMVL 515
Cdd:NF041082 445 ------AENAGLDpiDALVELRSAheKGNKTAGLDVYTGKVVDMLEIGVVEPLRVKTQAIKSATEAAVMIL 509
|
|
| cpn60 |
cd03343 |
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ... |
21-515 |
2.84e-22 |
|
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: 100.03 E-value: 2.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 21 ILAEAVAVTLGPKGRNVVLEKKFGAPQIVNDGVTIAKEIEledhIENTGVSLIRQAASKTNDAAGDGTTTATVLAHAIVK 100
Cdd:cd03343 26 AVAEAVRTTLGPKGMDKMLVDSLGDVTITNDGATILKEMD----IEHPAAKMLVEVAKTQDEEVGDGTTTAVVLAGELLE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 101 --EGL--RNVAAGANAIQLKRGIDKATAfLVDKIAEHARPVEDS--KAIAQVgSISAGNDEEVGQMIAE--------AMD 166
Cdd:cd03343 102 kaEDLldQNIHPTVIIEGYRLAAEKALE-LLDEIAIKVDPDDKDtlRKIAKT-SLTGKGAEAAKDKLADlvvdavlqVAE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 167 KVGKEGVISLE-------EGKSMTtELEITEGMRFDKGYISPyfatdaeRMEAVFDDPYILLTDKKIAL----------- 228
Cdd:cd03343 180 KRDGKYVVDLDnikiekkTGGSVD-DTELIRGIVIDKEVVHP-------GMPKRVENAKIALLDAPLEVkkteidakiri 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 229 --VQDLVPVLEQVARQGKPLViiaeDIEKEALATLVVNRlRGVLNVAA---VKAPGFGDRR--KAMLEDIAVLTGGQVIT 301
Cdd:cd03343 252 tsPDQLQAFLEQEEAMLKEMV----DKIADTGANVVFCQ-KGIDDLAQhylAKAGILAVRRvkKSDMEKLARATGAKIVT 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 302 edaglKLENTKLDSLGKARRITITK--DNTTVVAEGNEAAvKARCEQIR----RQMDETESSydkeklqerlaklsggva 375
Cdd:cd03343 327 -----NIDDLTPEDLGEAELVEERKvgDDKMVFVEGCKNP-KAVTILLRggteHVVDELERA------------------ 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 376 vvkvgaatetemkdkklrLEDAINATKAAVEEG-IVPGGGTTLAHLAPHLEEWANKTLTSEELtGALIVARALPAPLKRI 454
Cdd:cd03343 383 ------------------LEDALRVVADALEDGkVVAGGGAVEIELAKRLREYARSVGGREQL-AVEAFADALEEIPRTL 443
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 950121894 455 AENAGQNG--AVIAERVK--EKEFNVGFNASTNEFVDMLAAGIVDPAKVTRSALQNAASIAGMVL 515
Cdd:cd03343 444 AENAGLDPidTLVELRAAheKGNKNAGLDVYTGEVVDMLEKGVIEPLRVKKQAIKSATEAATMIL 508
|
|
| chap_CCT_epsi |
TIGR02343 |
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ... |
5-523 |
2.95e-14 |
|
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: 75.22 E-value: 2.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 5 IIYNENARRALEKGIDIL------AEAVAVT----LGPKGRNVVLEKKFGAPQIVNDGVTIAKEIELEDHIentgVSLIR 74
Cdd:TIGR02343 12 IIIKDQDNKKRLKGLEAKksniaaAKSVASIlrtsLGPKGMDKMLISPDGDITVTNDGATILSQMDVDNQI----AKLMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 75 QAASKTNDAAGDGTTTATVLAHAIVKEGLRNVAAGANAIQLKRGIDKATAFLVDKIAEHARPVEDSK---------AIAQ 145
Cdd:TIGR02343 88 ELSKSQDDEIGDGTTGVVVLAGALLEQAEELLDKGIHPIKIADGFEEAARIAVEHLEEISDEISADNnnrepliqaAKTS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 146 VGS-ISAGNDEEVGQMIAEA----MDKVGKE---GVISLEE---GKSMTTELeiTEGMRFDKGYISPYFATDAERME-AV 213
Cdd:TIGR02343 168 LGSkIVSKCHRRFAEIAVDAvlnvADMERRDvdfDLIKVEGkvgGSLEDTKL--IKGIIIDKDFSHPQMPKEVEDAKiAI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 214 FDDPY---ILLTDKKIALV-------------QDLVPVLEQVARQGKPLVIIAEDIEKEALATLVVNRLRGVLNVAAVKa 277
Cdd:TIGR02343 246 LTCPFeppKPKTKHKLDISsveeykklqkyeqQKFKEMIDDIKKSGANLVICQWGFDDEANHLLLQNDLPAVRWVGGQE- 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 278 pgfgdrrkamLEDIAVLTGGQVITedaglKLENTKLDSLGKARRIT-----ITKDNTTVVAegNEAAVKARCEQIRrqmd 352
Cdd:TIGR02343 325 ----------LELIAIATGGRIVP-----RFQELSKDKLGKAGLVReisfgTTKDRMLVIE--QCKNSKAVTIFIR---- 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 353 etessydkeklqerlaklsGGVAVVkvgaateteMKDKKLRLEDAINATKAAVEEG-IVPGGGTTLAHLAPHLEEWANKt 431
Cdd:TIGR02343 384 -------------------GGNKMI---------IEEAKRSIHDALCVVRNLIKDSrIVYGGGAAEISCSLAVSQEADK- 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 432 LTSEELTGALIVARALPAPLKRIAENAGQN-----GAVIAERVKEKEFNVGFNASTNEFVDMLAAGIVDPAKVTRSALQN 506
Cdd:TIGR02343 435 YPGVEQYAIRAFADALETIPMALAENSGLDpigtlSTLKSLQLKEKNPNLGVDCLGYGTNDMKEQFVFETLIGKKQQILL 514
|
570
....*....|....*..
gi 950121894 507 AASIAGMVLTTECIVVD 523
Cdd:TIGR02343 515 ATQLVRMILKIDDVISP 531
|
|
| TCP1_delta |
cd03338 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ... |
22-521 |
9.17e-11 |
|
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: 64.23 E-value: 9.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 22 LAEAVAVTLGPKGRNVVLEKKFGAPQIVNDGVTIAKEIELEDHIENTGVSLirqaaSKTND-AAGDGTTTATVLAHAIVK 100
Cdd:cd03338 20 VADAIRTSLGPRGMDKMIQTGKGEVIITNDGATILKQMSVLHPAAKMLVEL-----SKAQDiEAGDGTTSVVVLAGALLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 101 EGLRNVAAGANAIQLKRGIDKATAFLVDKIAEHARPVE---------------DSKAIAQVGSISAgndeevgQMIAEAM 165
Cdd:cd03338 95 ACESLLKKGIHPTVISESFQIAAKKAVEILDSMSIPVDlndresliksattslNSKVVSQYSSLLA-------PIAVDAV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 166 DKVGKEGVISLEEGKSM--------TTE-LEITEGMRFDKGYISPyfATDAERMEavfddpyilltDKKIALVQ------ 230
Cdd:cd03338 168 LKVIDPATATNVDLKDIrivkklggTIEdTELVDGLVFTQKASKK--AGGPTRIE-----------KAKIGLIQfclspp 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 231 -----------D--------------LVPVLEQVARQGKPLVIIAEDIEKEALATLVVNRLRGvLNVAAVKapgfgDRRK 285
Cdd:cd03338 235 ktdmdnnivvnDyaqmdrilreerkyILNMCKKIKKSGCNVLLIQKSILRDAVSDLALHFLAK-LKIMVVK-----DIER 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 286 AMLEDIAVLTGGQVITEdaglkLENTKLDSLGKARRITitkdnttvvaegneaavkarceqirrqmdETESSYDKEKLQE 365
Cdd:cd03338 309 EEIEFICKTIGCKPVAS-----IDHFTEDKLGSADLVE-----------------------------EVSLGDGKIVKIT 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 366 RLAKLSGGVAVVkVGAATETEMKDKKLRLEDAINATKAAVEE-GIVPGGGTTLAHLAPHLEEWAnKTLTSEEltgALIV- 443
Cdd:cd03338 355 GVKNPGKTVTIL-VRGSNKLVLDEAERSLHDALCVIRCLVKKrALIPGGGAPEIEIALQLSEWA-RTLTGVE---QYCVr 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 444 --ARALPAPLKRIAENAGQNGAVIAERVKEK----EFNVGFNASTNEFVDMLAAGIVDPAKVTRSALQNAASIAGMVLTT 517
Cdd:cd03338 430 afADALEVIPYTLAENAGLNPISIVTELRNRhaqgEKNAGINVRKGAITNILEENVVQPLLVSTSAITLATETVRMILKI 509
|
....
gi 950121894 518 ECIV 521
Cdd:cd03338 510 DDIV 513
|
|
| chap_CCT_eta |
TIGR02345 |
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ... |
22-524 |
1.28e-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: 1.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 22 LAEAVAVTLGPKGRNVVLEKKFGAPQIVNDGVTIAKEIELEDHIENTGVSLirqaaSKTNDA-AGDGTTTATVLAHAIVK 100
Cdd:TIGR02345 30 IAEALKTTLGPRGMDKLIVGSNGKATISNDGATILKLLDIVHPAAKTLVDI-----AKSQDAeVGDGTTSVTILAGELLK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 101 EGLRNVAAGANAIQLKRGIDKATAFLVDKIAEHARPVEDSK-----------AIAQVGSISAGNDEEVGQMIAEAMDKVG 169
Cdd:TIGR02345 105 EAKPFIEEGVHPQLIIRCYREALSLAVEKIKEIAVTIDEEKgeqrellekcaATALSSKLISHNKEFFSKMIVDAVLSLD 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 170 KEGV------ISLEEGKSMTTELEItEGMRFDKGYISPYFatdaERMEAVFDDPYILLTDKKIALV--QDLVPVLEQVAR 241
Cdd:TIGR02345 185 RDDLdlkligIKKVQGGALEDSQLV-NGVAFKKTFSYAGF----EQQPKKFANPKILLLNVELELKaeKDNAEIRVEDVE 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 242 QGKPLV-----IIAEDIEK--EALATLVVNRlrgvLNVAAVKAPGFGDRRkamlediaVLTGGQVITEDAGlklentkld 314
Cdd:TIGR02345 260 DYQAIVdaewaIIFRKLEKivESGANVVLSK----LPIGDLATQYFADRD--------IFCAGRVSAEDLK--------- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 315 slgkaRRITITKDNTTVVAEGNEAAVKARCEqirrQMDETESSYDKEKLQERLAKLSGGVAVVKVGAatETEMKDKKLRL 394
Cdd:TIGR02345 319 -----RVIKACGGSIQSTTSDLEADVLGTCA----LFEERQIGSERYNYFTGCPHAKTCTIILRGGA--EQFIEEAERSL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 395 EDAINATKAAVE-EGIVPGGGTTLAHLAPHLEEWANKTLTSEELTgALIVARALPAPLKRIAENAGQNGAVIAERVKEK- 472
Cdd:TIGR02345 388 HDAIMIVRRALKnKKIVAGGGAIEMELSKCLRDYSKTIDGKQQLI-INAFAKALEIIPRQLCENAGFDSIEILNKLRSRh 466
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 950121894 473 ---EFNVGFNASTNEFVDMLAAGIVDPAKVTRSALQNAASIAGMVLTTECIVVDK 524
Cdd:TIGR02345 467 akgGKWYGVDINTEDIGDNFEAFVWEPALVKINALKAAFEAACTILSVDETITNP 521
|
|
| TCP1_epsilon |
cd03339 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ... |
5-141 |
5.41e-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: 58.46 E-value: 5.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 5 IIYNENARRALEKGID-----ILA-EAVAVT----LGPKGRNVVLEKKFGAPQIVNDGVTIAKEIELEDHIENTGVSLir 74
Cdd:cd03339 8 IIVREQEKKKRLKGLEahkshILAaKSVANIlrtsLGPRGMDKILVSPDGEVTVTNDGATILEKMDVDHQIAKLLVEL-- 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 950121894 75 qaaSKTNDAA-GDGTTTATVLAHAIVKEGLRNVAAGANAIQLKRGIDKATAFLVDKIAEHARPVEDSK 141
Cdd:cd03339 86 ---SKSQDDEiGDGTTGVVVLAGALLEQAEKLLDRGIHPIRIADGYEQACKIAVEHLEEIADKIEFSP 150
|
|
| TCP1_beta |
cd03336 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ... |
9-107 |
7.64e-08 |
|
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.
Pssm-ID: 239452 [Multi-domain] Cd Length: 517 Bit Score: 55.03 E-value: 7.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 9 ENARRALEKGIDILAEAVAVTLGPKGRNVVLE--KKFGAPQIVNDGVTIAKEIeledHIENTGVSLIRQAASKTNDAAGD 86
Cdd:cd03336 12 ETARLSSFVGAIAIGDLVKTTLGPKGMDKILQsvGRSGGVTVTNDGATILKSI----GVDNPAAKVLVDISKVQDDEVGD 87
|
90 100
....*....|....*....|.
gi 950121894 87 GTTTATVLAHAIVKEGLRNVA 107
Cdd:cd03336 88 GTTSVTVLAAELLREAEKLVA 108
|
|
| TCP1_eta |
cd03340 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ... |
5-134 |
1.30e-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: 54.22 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 5 IIYNENARRALekgidilAEAVAVTLGPKGRNVVLEKKFGAPQIVNDGVTIAKEIELEDHIENTGVSLirqaaSKTNDA- 83
Cdd:cd03340 18 LISNINACQAI-------ADAVRTTLGPRGMDKLIVDGRGKVTISNDGATILKLLDIVHPAAKTLVDI-----AKSQDAe 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 950121894 84 AGDGTTTATVLAHAIVKEGLRNVAAGANAIQLKRGIDKATAFLVDKIAEHA 134
Cdd:cd03340 86 VGDGTTSVVVLAGEFLKEAKPFIEDGVHPQIIIRGYRKALQLAIEKIKEIA 136
|
|
| chap_CCT_alpha |
TIGR02340 |
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ... |
22-529 |
1.27e-06 |
|
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT alpha chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.
Pssm-ID: 274081 [Multi-domain] Cd Length: 536 Bit Score: 51.26 E-value: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 22 LAEAVAVTLGPKGRNVVLEKKFGAPQIVNDGVTIAKEIELEDHIENTGVSLirqaASKTNDAAGDGTTTATVLAHAIVKE 101
Cdd:TIGR02340 24 IANIVKTSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVEL----AQLQDREVGDGTTSVVIIAAELLKR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 102 GLRNVAAGANAIQLKRG-----------IDKATAFLVDKIAEH-----ARPVEDSKAIAqvgsisaGNDEEVGQMIAEAM 165
Cdd:TIGR02340 100 ADELVKNKIHPTSVISGyrlackeavkyIKENLSVSVDELGREalinvAKTSMSSKIIG-------LDSDFFSNIVVDAV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 166 DKVGKEGvislEEGKSMTTELEI----TEGMRFDKGYISPYFATDAER----MEAVFDDPYILLTD-----KKIAL-VQD 231
Cdd:TIGR02340 173 LAVKTTN----ENGETKYPIKAInilkAHGKSARESMLVKGYALNCTVasqqMPKRIKNAKIACLDfnlqkAKMALgVQI 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 232 LV---PVLEQVaRQgKPLVIIAEDIEK--EALATlVVNRLRGVLNVAA---VKAPGFGDRR--KAMLEDIAVLTGGQVIT 301
Cdd:TIGR02340 249 VVddpEKLEQI-RQ-READITKERIKKilDAGAN-VVLTTGGIDDMCLkyfVEAGAMGVRRckKEDLKRIAKATGATLVS 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 302 EDAGLKLEntkldslgkarrititkdnttvvaEGNEAAVKARCEQIrrqmdETESSYDKEKLQERLAKLSGGVAVVKVGA 381
Cdd:TIGR02340 326 TLADLEGE------------------------ETFEASYLGFADEV-----VQERIADDECILIKGTKKRKSASIILRGA 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 382 atETEMKDKKLR-LEDAINATKAAVEEG-IVPGGGTTLAHLAPHLEEWAnKTLTSEELTGALIVARALPAPLKRIAENAG 459
Cdd:TIGR02340 377 --NDFMLDEMERsLHDALCVVKRTLESNsVVPGGGAVEAALSIYLENFA-TTLGSREQLAIAEFARALLIIPKTLAVNAA 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 460 QNG------------AVIAERVKEKEFNVGFNASTNEFVDMLAAGIVDPAKVTRSALQNAASIAGMVLTTECIVVDKPEP 527
Cdd:TIGR02340 454 KDStelvaklrayhaAAQLKPEKKHLKWYGLDLVNGKIRDNKEAGVLEPTVSKVKSLKFATEAAITILRIDDLIKLNPEQ 533
|
..
gi 950121894 528 KE 529
Cdd:TIGR02340 534 SK 535
|
|
| TCP1_theta |
cd03341 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ... |
374-524 |
2.17e-06 |
|
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: 50.30 E-value: 2.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 374 VAVVKVGAATETEMKDKKLRLEDAINATKAAVEEG-IVPGGGTTLAHLAPHLEEWANKTLTSEELtgALI-VARALPAPL 451
Cdd:cd03341 316 IATIVLRGATQNILDDVERAIDDGVNVFKSLTKDGrFVPGAGATEIELAKKLKEYGEKTPGLEQY--AIKkFAEAFEVVP 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 452 KRIAENAGQNG-----AVIAERVKEKEfNVGFNASTNE--FVDMLAAGIVDPAKVTRSALQNAASIAGMVLTTECIVVDK 524
Cdd:cd03341 394 RTLAENAGLDAtevlsELYAAHQKGNK-SAGVDIESGDegTKDAKEAGIFDHLATKKWAIKLATEAAVTVLRVDQIIMAK 472
|
|
| chap_CCT_delta |
TIGR02342 |
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ... |
22-140 |
5.79e-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: 49.01 E-value: 5.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 22 LAEAVAVTLGPKGRNVVLEKKFGAPQIVNDGVTIAKEIELEDHIENTGVSLirqaaSKTND-AAGDGTTTATVLAHAIVK 100
Cdd:TIGR02342 21 VADAIRTSLGPKGMDKMIQDGKGEVIITNDGATILKQMAVLHPAAKMLVEL-----SKAQDiEAGDGTTSVVILAGALLG 95
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 950121894 101 EGLRNVAAGANAIQLKRGIDKATAFLVDKIAEHARPVEDS 140
Cdd:TIGR02342 96 ACERLLNKGIHPTIISESFQSAADEAIKILDEMSIPVDLS 135
|
|
| chap_CCT_theta |
TIGR02346 |
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ... |
22-525 |
8.94e-06 |
|
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: 48.56 E-value: 8.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 22 LAEAVAVTLGPKGRNVV----LEKKFgapqIVNDGVTIAKEIEledhIENTGVSLIRQAASKTNDAAGDGTTTATVLAHA 97
Cdd:TIGR02346 30 LSQITRTSLGPNGMNKMvinhLEKLF----VTNDAATILRELE----VQHPAAKLLVMASEMQENEIGDGTNLVLVLAGE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 98 IVKEGLRNVAAGANAIQLKRGIDKATAF--------LVDKIAEHARPVEDSKAI-AQVGSISAGNDEEVGQMIAEAM--- 165
Cdd:TIGR02346 102 LLNKAEELIRMGLHPSEIIKGYEMALKKameileelVVWEVKDLRDKDELIKALkASISSKQYGNEDFLAQLVAQACstv 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 166 --DKVGKEGVISLEEGKSMTTEL---EITEGMRFDKgyispyfatdaermeavfdDPYILLTDKKIALVQDLVPVLEQVA 240
Cdd:TIGR02346 182 lpKNPQNFNVDNIRVCKILGGSLsnsEVLKGMVFNR-------------------EAEGSVKSVKNAKVAVFSCPLDTAT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 241 RQGKPLVII--AEDIEkealatlvvNRLRGVLNVAavkapgfgdrrKAMLEDIA------VLTGGQVitEDAGLKLENT- 311
Cdd:TIGR02346 243 TETKGTVLIhnAEELL---------NYSKGEENQI-----------EAMIKAIAdsgvnvIVTGGSV--GDMALHYLNKy 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 312 -----KLDSLGKARRITITKDNTTVVaegneaavkarceQIRRQMDETESSYDKEKLQE---------RLAKLSGGVAVV 377
Cdd:TIGR02346 301 nimvlKIPSKFELRRLCKTVGATPLP-------------RLGAPTPEEIGYVDSVYVSEiggdkvtvfKQENGDSKISTI 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 378 KVGAATETEMKDKKLRLEDAINATKAAVEEG-IVPGGGTTLAHLAPHLEEWANKTLTSEELtGALIVARALPAPLKRIAE 456
Cdd:TIGR02346 368 ILRGSTDNLLDDIERAIDDGVNTVKALVKDGrLLPGAGATEIELASRLTKYGEKLPGLDQY-AIKKFAEAFEIIPRTLAE 446
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 950121894 457 NAGQN-----GAVIAERVK-EKEFNVGFNASTNEFVDMLAAGIVDPAKVTRSALQNAASIAGMVLTTECIVVDKP 525
Cdd:TIGR02346 447 NAGLNaneviPKLYAAHKKgNKSKGIDIEAESDGVKDASEAGIYDMLATKKWAIKLATEAAVTVLRVDQIIMAKP 521
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
9-102 |
1.47e-05 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 47.72 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 9 ENARRALEKGIDILAEAVAVTLGPKGRNVVLEKKFGAPQ-----IVNDGVTIAKEIELEDhientGVSLIRQAASKTNDA 83
Cdd:PTZ00212 21 ETARLQSFVGAIAVADLVKTTLGPKGMDKILQPMSEGPRsgnvtVTNDGATILKSVWLDN-----PAAKILVDISKTQDE 95
|
90 100
....*....|....*....|
gi 950121894 84 -AGDGTTTATVLAHAIVKEG 102
Cdd:PTZ00212 96 eVGDGTTSVVVLAGELLREA 115
|
|
| TCP1_zeta |
cd03342 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
30-511 |
2.77e-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: 46.87 E-value: 2.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 30 LGPKGRNVVLEKKFGAPQIVNDGVTIAKEIeledHIENTGVSLIRQAASKTNDAAGDGTTTATVLAHAIVKEGLRNVAAG 109
Cdd:cd03342 32 LGPKGTLKMLVSGAGDIKLTKDGNVLLSEM----QIQHPTASMIARAATAQDDITGDGTTSNVLLIGELLKQAERYIQEG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 110 ANAIQLKRGIDKATAFLVDKIAEHARPVEDskaiaqvgsisaGNDEEVGQMIAeamdkvgkegvisleeGKSMTTELeit 189
Cdd:cd03342 108 VHPRIITEGFELAKNKALKFLESFKVPVEI------------DTDRELLLSVA----------------RTSLRTKL--- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 190 egmrfdkgyiSPYFATdaermeavfddpyiLLTDkkialvqDLVPVLEQVARQGKP----LVIIAEDIEKEALATLVVNR 265
Cdd:cd03342 157 ----------HADLAD--------------QLTE-------IVVDAVLAIYKPDEPidlhMVEIMQMQHKSDSDTKLIRG 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 266 LrgVLNvaavkapgFGDRRKAM---LEDIAVLTGgqviteDAGLKLENTKLDSlGKARRITITK------DNTTVVAEGN 336
Cdd:cd03342 206 L--VLD--------HGARHPDMpkrVENAYILTC------NVSLEYEKTEVNS-GFFYSVVINQkgidppSLDMLAKEGI 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 337 EAAVKARceqiRRQMdetessydkeklqERLAKLSGGVAVVKVGAATE----------------------TEMKDKK--- 391
Cdd:cd03342 269 LALRRAK----RRNM-------------ERLTLACGGVAMNSVDDLSPeclgyaglvyertlgeekytfiEGVKNPKsct 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 392 -----------LRLEDAIN----ATKAAVEEG-IVPGGGTTLAHLAPHLEEWAnKTLTSEELTGALIVARALPAPLKRIA 455
Cdd:cd03342 332 ilikgpndhtiTQIKDAIRdglrAVKNAIEDKcVVPGAGAFEVALYAHLKEFK-KSVKGKAKLGVQAFADALLVIPKTLA 410
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 456 ENAGQNG----AVIAERVKEKEFNVGFNASTNEFVDMLAAGIVDPAKVTRSALQNAASIA 511
Cdd:cd03342 411 ENSGLDVqetlVKLQDEYAEGGQVGGVDLDTGEPMDPESEGIWDNYSVKRQILHSATVIA 470
|
|
| chap_CCT_zeta |
TIGR02347 |
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ... |
8-122 |
3.65e-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: 46.27 E-value: 3.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 8 NENARRALEkgiDILAEavavTLGPKGRNVVLEKKFGAPQIVNDGVTIAKEIeledHIENTGVSLIRQAASKTNDAAGDG 87
Cdd:TIGR02347 21 NINAARGLQ---DVLKT----NLGPKGTLKMLVSGAGDIKLTKDGNVLLNEM----QIQHPTASMIARAATAQDDITGDG 89
|
90 100 110
....*....|....*....|....*....|....*
gi 950121894 88 TTTATVLAHAIVKEGLRNVAAGANAIQLKRGIDKA 122
Cdd:TIGR02347 90 TTSTVLLIGELLKQAERYILEGVHPRIITEGFEIA 124
|
|
| chap_CCT_gamma |
TIGR02344 |
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ... |
394-521 |
6.30e-05 |
|
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT gamma chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.
Pssm-ID: 274085 [Multi-domain] Cd Length: 524 Bit Score: 45.50 E-value: 6.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 394 LEDAINATKAAVEEG-IVPGGGTTLAHLAPHLEEWANKTLTSEELTgALIVARALPAPLKRIAENAGQN-----GAVIAE 467
Cdd:TIGR02344 386 LQDAMAVARNVLLDPkLVPGGGATEMAVSVALTEKSKKLEGVEQWP-YRAVADALEIIPRTLAQNCGANvirtlTELRAK 464
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 950121894 468 RVKEKEFNVGFNASTNEFVDMLAAGIVDPAKVTRSALQNAASIAGMVLTTECIV 521
Cdd:TIGR02344 465 HAQENNCTWGIDGETGKIVDMKEKGIWEPLAVKLQTYKTAIESACLLLRIDDIV 518
|
|
| chap_CCT_beta |
TIGR02341 |
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ... |
9-134 |
9.05e-05 |
|
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: 45.24 E-value: 9.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 9 ENARRALEKGIDILAEAVAVTLGPKGRNVVLEK--KFGAPQIVNDGVTIAKEIELEdhieNTGVSLIRQAASKTNDAAGD 86
Cdd:TIGR02341 13 ENARLSSFVGAIAIGDLVKSTLGPKGMDKILQSssSDASIMVTNDGATILKSIGVD----NPAAKVLVDMSKVQDDEVGD 88
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 950121894 87 GTTTATVLAHAIVKEGLRNVAAGANAIQLKRGIDKATAFLVDKIAEHA 134
Cdd:TIGR02341 89 GTTSVTVLAAELLREAEKLINQKIHPQTIIAGYREATKAARDALLKSA 136
|
|
| TCP1_alpha |
cd03335 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ... |
22-510 |
3.64e-03 |
|
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: 39.96 E-value: 3.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 22 LAEAVAVTLGPKGRNVVLEKKFGAPQIVNDGVTIAKEIELEDHIENTGVSLirqaASKTNDAAGDGTTTATVLAHAIVKE 101
Cdd:cd03335 20 IANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVEL----AQLQDKEVGDGTTSVVIIAAELLKR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 102 GLRNVAAGANAIQLKRGIDKATAFLVDKIAEH-ARPVED--SKAIAQVG--SISA---GNDEEV-GQMIAEAMDKV---- 168
Cdd:cd03335 96 ANELVKQKIHPTTIISGYRLACKEAVKYIKEHlSISVDNlgKESLINVAktSMSSkiiGADSDFfANMVVDAILAVkttn 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 169 --GK-----EGV-ISLEEGKSMTTELEItegmrfdKGY-ISPYFAtdAERMEAVFDDPYILLTD-----KKIAL-VQDLV 233
Cdd:cd03335 176 ekGKtkypiKAVnILKAHGKSAKESYLV-------NGYaLNCTRA--SQGMPTRVKNAKIACLDfnlqkTKMKLgVQVVV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 234 ---PVLEQVaRQgKPLVIIAEDIEK--EALATlVVNRLRGVLNVAA---VKAPGFGDRR--KAMLEDIAVLTGGQVITED 303
Cdd:cd03335 247 tdpEKLEKI-RQ-RESDITKERIKKilAAGAN-VVLTTGGIDDMCLkyfVEAGAMAVRRvkKEDLRRIAKATGATLVSTL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 304 AGLKLENT-KLDSLGKARRITITK--DNTTVVAEGNEAAVKARCeqIRR-----QMDETESSydkeklqerlaklsggva 375
Cdd:cd03335 324 ANLEGEETfDPSYLGEAEEVVQERigDDELILIKGTKKRSSASI--ILRgandfMLDEMERS------------------ 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950121894 376 vvkvgaatetemkdkklrLEDAINATKAAVEEG-IVPGGGTTLAHLAPHLEEWAnKTLTSEELTGALIVARALPAPLKRI 454
Cdd:cd03335 384 ------------------LHDALCVVKRTLESNsVVPGGGAVETALSIYLENFA-TTLGSREQLAIAEFAEALLVIPKTL 444
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 950121894 455 AENAGQNG------------AVIAERVKEKEFNVGFNASTNEFVDMLAAGIVDPA----KVTRSALQNAASI 510
Cdd:cd03335 445 AVNAAKDAtelvaklrayhaAAQVKPDKKHLKWYGLDLINGKVRDNLEAGVLEPTvskiKSLKFATEAAITI 516
|
|
| |
