|
Name |
Accession |
Description |
Interval |
E-value |
| GroEL |
cd03344 |
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ... |
36-557 |
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: 692.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 36 KRILYGKDSREKLQAGIDKLADAVSITLGPRGRNVVLAEK-DTIKVINDGVTIAKSIELPDTIENAGATLIQEVAIKMNE 114
Cdd:cd03344 1 KDIKFGEEARKALLRGVNKLADAVKVTLGPKGRNVVIEKSfGSPKITKDGVTVAKEIELEDPFENMGAQLVKEVASKTND 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 115 SAGDGTTTAIILAREMIKAGSLAIAFGANAVSVKNGMNKTVKELVRVLQMKSIPVQGKNDIKAVASISAGNDEFVGNLIA 194
Cdd:cd03344 81 VAGDGTTTATVLARAIIKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKPVKTKEEIAQVATISANGDEEIGELIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 195 ETVEKIGPDGVISIESSSTSETSVIVEEGMKFDKGYMSPHFITNQEKSTVEFDKAKILVTDQKITSAKELVPLLEKTSQL 274
Cdd:cd03344 161 EAMEKVGKDGVITVEEGKTLETELEVVEGMQFDRGYLSPYFVTDPEKMEVELENPYILLTDKKISSIQELLPILELVAKA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 275 SVPLLIIAEDISAEVLEILVVNKKQGLINVAVVKCPGMLDGKKALLQDIALMTGADYLSGDLGMSLMGATSDQLGVSRRV 354
Cdd:cd03344 241 GRPLLIIAEDVEGEALATLVVNKLRGGLKVCAVKAPGFGDRRKAMLEDIAILTGGTVISEELGLKLEDVTLEDLGRAKKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 355 VITANSTTIVADASTKPEIQARIAQMKKDLAETDNSYLSKKIAERIAKLTGGVAVIKVGGHTETELEDRKLRIEDAKNAT 434
Cdd:cd03344 321 VVTKDDTTIIGGAGDKAAIKARIAQIRKQIEETTSDYDKEKLQERLAKLSGGVAVIKVGGATEVELKEKKDRVEDALNAT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 435 FAAMREGIVPGGGATYIHLldeIPRIKKNLMEDSYEQIGADIVAMALTAPAMAIATNAGVDGSVVVQKTRELEWRSGYNA 514
Cdd:cd03344 401 RAAVEEGIVPGGGVALLRA---SPALDKLKALNGDEKLGIEIVRRALEAPLRQIAENAGVDGSVVVEKVLESPDGFGYDA 477
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 15239580 515 MSGKYEDLLNAGIADPCRVSRFALQNAVSVAGIILTTQAVLVE 557
Cdd:cd03344 478 ATGEYVDMIEAGIIDPTKVVRSALQNAASVASLLLTTEALVVD 520
|
|
| groEL |
PRK12849 |
chaperonin GroEL; Reviewed |
35-564 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237230 Cd Length: 542 Bit Score: 614.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 35 AKRILYGKDSREKLQAGIDKLADAVSITLGPRGRNVVLaEKD--TIKVINDGVTIAKSIELPDTIENAGATLIQEVAIKM 112
Cdd:PRK12849 2 AKIIKFDEEARRALERGVNKLADAVKVTLGPKGRNVVI-DKSfgAPTITKDGVSIAKEIELEDPFENLGAQLVKEVASKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 113 NESAGDGTTTAIILAREMIKAGSLAIAFGANAVSVKNGMNKTVKELVRVLQMKSIPVQGKNDIKAVASISAGNDEFVGNL 192
Cdd:PRK12849 81 NDVAGDGTTTATVLAQALVQEGLKNVAAGANPMDLKRGIDKAVEAVVEELKALARPVSGSEEIAQVATISANGDEEIGEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 193 IAETVEKIGPDGVISIESSSTSETSVIVEEGMKFDKGYMSPHFITNQEKSTVEFDKAKILVTDQKITSAKELVPLLEKTS 272
Cdd:PRK12849 161 IAEAMEKVGKDGVITVEESKTLETELEVTEGMQFDRGYLSPYFVTDPERMEAVLEDPLILLTDKKISSLQDLLPLLEKVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 273 QLSVPLLIIAEDISAEVLEILVVNKKQGLINVAVVKCPGMLDGKKALLQDIALMTGADYLSGDLGMSLMGATSDQLGVSR 352
Cdd:PRK12849 241 QSGKPLLIIAEDVEGEALATLVVNKLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGLKLEEVTLDDLGRAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 353 RVVITANSTTIVADASTKPEIQARIAQMKKDLAETDNSYLSKKIAERIAKLTGGVAVIKVGGHTETELEDRKLRIEDAKN 432
Cdd:PRK12849 321 RVTITKDNTTIVDGAGDKEAIEARVAQIRRQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATEVELKERKDRVEDALN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 433 ATFAAMREGIVPGGGATYIHLLDEIpRIKKNLMEDsyEQIGADIVAMALTAPAMAIATNAGVDGSVVVQKTRELEWRSGY 512
Cdd:PRK12849 401 ATRAAVEEGIVPGGGVALLRAAKAL-DELAGLNGD--QAAGVEIVRRALEAPLRQIAENAGLDGSVVVAKVLELEDGFGF 477
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 15239580 513 NAMSGKYEDLLNAGIADPCRVSRFALQNAVSVAGIILTTQAVLVEKIKQPKP 564
Cdd:PRK12849 478 NAATGEYGDLIAAGIIDPVKVTRSALQNAASVAGLLLTTEALVADKPEEEDP 529
|
|
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
35-571 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 601.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 35 AKRILYGKDSREKLQAGIDKLADAVSITLGPRGRNVVLAEK-DTIKVINDGVTIAKSIELPDTIENAGATLIQEVAIKMN 113
Cdd:PRK00013 2 AKDIKFGEDARRKLLRGVNKLADAVKVTLGPKGRNVVLEKSfGAPTITKDGVTVAKEIELEDPFENMGAQLVKEVASKTN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 114 ESAGDGTTTAIILAREMIKAGSLAIAFGANAVSVKNGMNKTVKELVRVLQMKSIPVQGKNDIKAVASISAGNDEFVGNLI 193
Cdd:PRK00013 82 DVAGDGTTTATVLAQAIVREGLKNVAAGANPMDLKRGIDKAVEAAVEELKKISKPVEDKEEIAQVATISANGDEEIGKLI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 194 AETVEKIGPDGVISIESSSTSETSVIVEEGMKFDKGYMSPHFITNQEKSTVEFDKAKILVTDQKITSAKELVPLLEKTSQ 273
Cdd:PRK00013 162 AEAMEKVGKEGVITVEESKGFETELEVVEGMQFDRGYLSPYFVTDPEKMEAELENPYILITDKKISNIQDLLPVLEQVAQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 274 LSVPLLIIAEDISAEVLEILVVNKKQGLINVAVVKCPGMLDGKKALLQDIALMTGADYLSGDLGMSLMGATSDQLGVSRR 353
Cdd:PRK00013 242 SGKPLLIIAEDVEGEALATLVVNKLRGTLKVVAVKAPGFGDRRKAMLEDIAILTGGTVISEELGLKLEDATLEDLGQAKK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 354 VVITANSTTIVADASTKPEIQARIAQMKKDLAETDNSYLSKKIAERIAKLTGGVAVIKVGGHTETELEDRKLRIEDAKNA 433
Cdd:PRK00013 322 VVVTKDNTTIVDGAGDKEAIKARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATEVEMKEKKDRVEDALHA 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 434 TFAAMREGIVPGGGATYIHLldeIPRIKKNLMEDSYEQIGADIVAMALTAPAMAIATNAGVDGSVVVQKTRELE-WRSGY 512
Cdd:PRK00013 402 TRAAVEEGIVPGGGVALLRA---APALEALKGLNGDEATGINIVLRALEAPLRQIAENAGLEGSVVVEKVKNGKgKGYGY 478
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 15239580 513 NAMSGKYEDLLNAGIADPCRVSRFALQNAVSVAGIILTTQAVLVEKiKQPKPAVPQVPG 571
Cdd:PRK00013 479 NAATGEYVDMIEAGIIDPTKVTRSALQNAASVAGLLLTTEAVVADK-PEKKAAAPPMGG 536
|
|
| GroEL |
TIGR02348 |
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ... |
35-558 |
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: 585.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 35 AKRILYGKDSREKLQAGIDKLADAVSITLGPRGRNVVLAEK-DTIKVINDGVTIAKSIELPDTIENAGATLIQEVAIKMN 113
Cdd:TIGR02348 1 AKQIKFDEEARKALLRGVDKLADAVKVTLGPKGRNVVLEKSfGAPTITKDGVTVAKEIELEDKFENMGAQLVKEVASKTN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 114 ESAGDGTTTAIILAREMIKAGSLAIAFGANAVSVKNGMNKTVKELVRVLQMKSIPVQGKNDIKAVASISAGNDEFVGNLI 193
Cdd:TIGR02348 81 DVAGDGTTTATVLAQAIVKEGLKNVAAGANPIELKRGIEKAVEAVVEELKKLSKPVKGKKEIAQVATISANNDEEIGSLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 194 AETVEKIGPDGVISIESSSTSETSVIVEEGMKFDKGYMSPHFITNQEKSTVEFDKAKILVTDQKITSAKELVPLLEKTSQ 273
Cdd:TIGR02348 161 AEAMEKVGKDGVITVEESKSLETELEVVEGMQFDRGYISPYFVTDAEKMEVELENPYILITDKKISNIKDLLPLLEKVAQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 274 LSVPLLIIAEDISAEVLEILVVNKKQGLINVAVVKCPGMLDGKKALLQDIALMTGADYLSGDLGMSLMGATSDQLGVSRR 353
Cdd:TIGR02348 241 SGKPLLIIAEDVEGEALATLVVNKLRGTLNVCAVKAPGFGDRRKAMLEDIAILTGGQVISEELGLKLEEVTLDDLGKAKK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 354 VVITANSTTIVADASTKPEIQARIAQMKKDLAETDNSYLSKKIAERIAKLTGGVAVIKVGGHTETELEDRKLRIEDAKNA 433
Cdd:TIGR02348 321 VTVDKDNTTIVEGAGDKAAIKARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATETEMKEKKLRIEDALNA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 434 TFAAMREGIVPGGGATYIHLLDEIPRIKKNLMEdsyEQIGADIVAMALTAPAMAIATNAGVDGSVVVQKTRELEWRSGYN 513
Cdd:TIGR02348 401 TRAAVEEGIVPGGGVALLRAAAALEGLKGDGED---EAIGIDIVKRALEAPLRQIAENAGLDGAVVAEKVKELKGNFGFN 477
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 15239580 514 AMSGKYEDLLNAGIADPCRVSRFALQNAVSVAGIILTTQAVLVEK 558
Cdd:TIGR02348 478 AATGEYEDLVEAGIIDPTKVTRSALQNAASIAGLLLTTEAVVADK 522
|
|
| groEL |
CHL00093 |
chaperonin GroEL |
35-560 |
0e+00 |
|
chaperonin GroEL
Pssm-ID: 177025 Cd Length: 529 Bit Score: 562.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 35 AKRILYGKDSREKLQAGIDKLADAVSITLGPRGRNVVLAEK-DTIKVINDGVTIAKSIELPDTIENAGATLIQEVAIKMN 113
Cdd:CHL00093 2 SKKILYQDNARRALERGMDILAEAVSVTLGPKGRNVVLEKKyGSPQIVNDGVTIAKEIELEDHIENTGVALIRQAASKTN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 114 ESAGDGTTTAIILAREMIKAGSLAIAFGANAVSVKNGMNKTVKELVRVLQMKSIPVQGKNDIKAVASISAGNDEFVGNLI 193
Cdd:CHL00093 82 DVAGDGTTTATVLAYAIVKQGMKNVAAGANPISLKRGIEKATQYVVSQIAEYARPVEDIQAITQVASISAGNDEEVGSMI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 194 AETVEKIGPDGVISIESSSTSETSVIVEEGMKFDKGYMSPHFITNQEKSTVEFDKAKILVTDQKITSAK-ELVPLLEKTS 272
Cdd:CHL00093 162 ADAIEKVGREGVISLEEGKSTVTELEITEGMRFEKGFISPYFVTDTERMEVVQENPYILLTDKKITLVQqDLLPILEQVT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 273 QLSVPLLIIAEDISAEVLEILVVNKKQGLINVAVVKCPGMLDGKKALLQDIALMTGADYLSGDLGMSLMGATSDQLGVSR 352
Cdd:CHL00093 242 KTKRPLLIIAEDVEKEALATLVLNKLRGIVNVVAVRAPGFGDRRKAMLEDIAILTGGQVITEDAGLSLETIQLDLLGQAR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 353 RVVITANSTTIVADASTKpEIQARIAQMKKDLAETDNSYLSKKIAERIAKLTGGVAVIKVGGHTETELEDRKLRIEDAKN 432
Cdd:CHL00093 322 RIIVTKDSTTIIADGNEE-QVKARCEQLRKQIEIADSSYEKEKLQERLAKLSGGVAVIKVGAATETEMKDKKLRLEDAIN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 433 ATFAAMREGIVPGGGATYIHLLDEIPR-IKKNLMEDsyEQIGADIVAMALTAPAMAIATNAGVDGSVVVQKTRELEWRSG 511
Cdd:CHL00093 401 ATKAAVEEGIVPGGGATLVHLSENLKTwAKNNLKED--ELIGALIVARAILAPLKRIAENAGKNGSVIIEKVQEQDFEIG 478
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 15239580 512 YNAMSGKYEDLLNAGIADPCRVSRFALQNAVSVAGIILTTQAVLVEKIK 560
Cdd:CHL00093 479 YNAANNKFVNMYEAGIIDPAKVTRSALQNAASIASMILTTECIIVDKKE 527
|
|
| GroEL |
COG0459 |
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ... |
35-565 |
0e+00 |
|
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227 Cd Length: 497 Bit Score: 531.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 35 AKRILYGKDSREKLQAGIDKLADAVSITLGPRGRNVVLAEK-DTIKVINDGVTIAKSIELPDTIENAGATLIQEVAIKMN 113
Cdd:COG0459 2 AKQILFGEDARRANIRGVKALADAVKVTLGPKGRNVMLVKSfGDPTITNDGVTIAKEIELEDPFENMGAQLVKEVASKTN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 114 ESAGDGTTTAIILAREMIKAGSLAIAFGANAVSVKNGMNKTVKELVRVLQMKSIPVQGKNDIKAVASISAGNDEFVGNLI 193
Cdd:COG0459 82 DEAGDGTTTATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPVDDKEELAQVATISANGDEEIGELI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 194 AETVEKIGPDGVISIESSSTSETSVIVEEGMKFDKGYMSPHFITNQEKSTVEFDKAKILVTDQKITSAKELVPLLEKTSQ 273
Cdd:COG0459 162 AEAMEKVGKDGVITVEEGKGLETELEVVEGMQFDKGYLSPYFVTDPEKMPAELENAYILLTDKKISSIQDLLPLLEKVAQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 274 LSVPLLIIAEDISAEVLEILVVNKKQGLINVAVVKCPGMLDGKKALLQDIALMTGADYLSGDLGMSLMGATSDQLGVSRR 353
Cdd:COG0459 242 SGKPLLIIAEDIDGEALATLVVNGIRGVLRVVAVKAPGFGDRRKAMLEDIAILTGGRVISEDLGLKLEDVTLDDLGRAKR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 354 VVITANSTTIVADASTKPEIqariaqmkkdlaetdnsylskkiaeriakltggvaVIKVGGHTETELEDRKLRIEDAKNA 433
Cdd:COG0459 322 VEVDKDNTTIVEGAGNPKAI-----------------------------------VILVGAATEVEVKERKRRVEDALHA 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 434 TFAAMREGIVPGGGATYIHLLDEIPRIKKNLMEDsyEQIGADIVAMALTAPAMAIATNAGVDGSVVVQKTRELEWRS-GY 512
Cdd:COG0459 367 TRAAVEEGIVPGGGAALLRAARALRELAAKLEGD--EQLGIEIVARALEAPLRQIAENAGLDGSVVVEKVRAAKDKGfGF 444
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 15239580 513 NAMSGKYEDLLNAGIADPCRVSRFALQNAVSVAGIILTTQAVLVEKIKQPKPA 565
Cdd:COG0459 445 DAATGEYVDMLEAGVIDPAKVKRSALQNAASVAGLILTTEAVIADKPEKEEAA 497
|
|
| groEL |
PRK12850 |
chaperonin GroEL; Reviewed |
35-567 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237231 Cd Length: 544 Bit Score: 525.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 35 AKRILYGKDSREKLQAGIDKLADAVSITLGPRGRNVVLAEKDTIKVI-NDGVTIAKSIELPDTIENAGATLIQEVAIKMN 113
Cdd:PRK12850 3 AKEIRFSTDARDRLLRGVNILANAVKVTLGPKGRNVVLEKSFGAPRItKDGVTVAKEIELEDKFENMGAQMVKEVASKTN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 114 ESAGDGTTTAIILAREMIKAGSLAIAFGANAVSVKNGMNKTVKELVRVLQMKSIPVQGKNDIKAVASISAGNDEFVGNLI 193
Cdd:PRK12850 83 DLAGDGTTTATVLAQAIVREGAKLVAAGMNPMDLKRGIDLAVAAVVDELKKIAKKVTSSKEIAQVATISANGDESIGEMI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 194 AETVEKIGPDGVISIESSSTSETSVIVEEGMKFDKGYMSPHFITNQEKSTVEFDKAKILVTDQKITSAKELVPLLEKTSQ 273
Cdd:PRK12850 163 AEAMDKVGKEGVITVEEAKTLGTELDVVEGMQFDRGYLSPYFVTNPEKMRAELEDPYILLHEKKISNLQDLLPILEAVVQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 274 LSVPLLIIAEDISAEVLEILVVNKKQGLINVAVVKCPGMLDGKKALLQDIALMTGADYLSGDLGMSLMGATSDQLGVSRR 353
Cdd:PRK12850 243 SGRPLLIIAEDVEGEALATLVVNKLRGGLKSVAVKAPGFGDRRKAMLEDIAVLTGGQVISEDLGIKLENVTLDMLGRAKR 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 354 VVITANSTTIVADASTKPEIQARIAQMKKDLAETDNSYLSKKIAERIAKLTGGVAVIKVGGHTETELEDRKLRIEDAKNA 433
Cdd:PRK12850 323 VLITKENTTIIDGAGDKKNIEARVKQIRAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKEKKDRVDDALHA 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 434 TFAAMREGIVPGGGatyIHLLDEIPRIKKNLMEDSYEQIGADIVAMALTAPAMAIATNAGVDGSVVVQKTRELEWRSGYN 513
Cdd:PRK12850 403 TRAAVEEGIVPGGG---VALLRARSALRGLKGANADETAGIDIVRRALEEPLRQIATNAGFEGSVVVGKVAELPGNFGFN 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 15239580 514 AMSGKYEDLLNAGIADPCRVSRFALQNAVSVAGIILTTQAVLVEKIKQPKPAVP 567
Cdd:PRK12850 480 AQTGEYGDMVEAGIIDPAKVTRTALQDAASIAALLITTEAMVAEAPKKAAAAAA 533
|
|
| PTZ00114 |
PTZ00114 |
Heat shock protein 60; Provisional |
25-564 |
0e+00 |
|
Heat shock protein 60; Provisional
Pssm-ID: 185455 Cd Length: 555 Bit Score: 523.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 25 PRKFSVVRAGAKRILYGKDSREKLQAGIDKLADAVSITLGPRGRNVVLAEKD-TIKVINDGVTIAKSIELPDTIENAGAT 103
Cdd:PTZ00114 4 KMFSSRYRFKGKEIRFGDEARQSLLKGIERLADAVAVTLGPKGRNVIIEQEYgSPKITKDGVTVAKAIEFSDRFENVGAQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 104 LIQEVAIKMNESAGDGTTTAIILAREMIKAGSLAIAFGANAVSVKNGMNKTVKELVRVLQMKSIPVQGKNDIKAVASISA 183
Cdd:PTZ00114 84 LIRQVASKTNDKAGDGTTTATILARAIFREGCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQSRPVKTKEDILNVATISA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 184 GNDEFVGNLIAETVEKIGPDGVISIESSSTSETSVIVEEGMKFDKGYMSPHFITNQEKSTVEFDKAKILVTDQKITSAKE 263
Cdd:PTZ00114 164 NGDVEIGSLIADAMDKVGKDGTITVEDGKTLEDELEVVEGMSFDRGYISPYFVTNEKTQKVELENPLILVTDKKISSIQS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 264 LVPLLEKTSQLSVPLLIIAEDISAEVLEILVVNKKQGLINVAVVKCPGMLDGKKALLQDIALMTGADYLSGD-LGMSLMG 342
Cdd:PTZ00114 244 ILPILEHAVKNKRPLLIIAEDVEGEALQTLIINKLRGGLKVCAVKAPGFGDNRKDILQDIAVLTGATVVSEDnVGLKLDD 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 343 ATSDQLGVSRRVVITANSTTIVADASTKPEIQARIAQMKKDLAETDNSYLSKKIAERIAKLTGGVAVIKVGGHTETELED 422
Cdd:PTZ00114 324 FDPSMLGSAKKVTVTKDETVILTGGGDKAEIKERVELLRSQIERTTSEYDKEKLKERLAKLSGGVAVIKVGGASEVEVNE 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 423 RKLRIEDAKNATFAAMREGIVPGGGATYIHLLDEIPRIKKNLMEDSYEQIGADIVAMALTAPAMAIATNAGVDGSVVVQK 502
Cdd:PTZ00114 404 KKDRIEDALNATRAAVEEGIVPGGGVALLRASKLLDKLEEDNELTPDQRTGVKIVRNALRLPTKQIAENAGVEGAVVVEK 483
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15239580 503 TRELEWRS-GYNAMSGKYEDLLNAGIADPCRVSRFALQNAVSVAGIILTTQAVLVEKIKQPKP 564
Cdd:PTZ00114 484 ILEKKDPSfGYDAQTGEYVNMFEAGIIDPTKVVRSALVDAASVASLMLTTEAAIVDLPKEKKK 546
|
|
| groEL |
PRK12851 |
chaperonin GroEL; Reviewed |
35-571 |
6.43e-176 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 171770 Cd Length: 541 Bit Score: 508.51 E-value: 6.43e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 35 AKRILYGKDSREKLQAGIDKLADAVSITLGPRGRNVVLAEKDTIKVI-NDGVTIAKSIELPDTIENAGATLIQEVAIKMN 113
Cdd:PRK12851 3 AKEVKFHVEAREKMLRGVNILADAVKVTLGPKGRNVVIDKSFGAPTItNDGVTIAKEIELEDKFENMGAQMVREVASKTN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 114 ESAGDGTTTAIILAREMIKAGSLAIAFGANAVSVKNGMNKTVKELVRVLQMKSIPVQGKNDIKAVASISAGNDEFVGNLI 193
Cdd:PRK12851 83 DVAGDGTTTATVLAQAIVREGAKAVAAGANPMDLKRGIDRAVAAVVEELKANARPVTTNAEIAQVATISANGDAEIGRLV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 194 AETVEKIGPDGVISIESSSTSETSVIVEEGMKFDKGYMSPHFITNQEKSTVEFDKAKILVTDQKITSAKELVPLLEKTSQ 273
Cdd:PRK12851 163 AEAMEKVGNEGVITVEESKTAETELEVVEGMQFDRGYLSPYFVTDADKMEAELEDPYILIHEKKISNLQDLLPVLEAVVQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 274 LSVPLLIIAEDISAEVLEILVVNKKQGLINVAVVKCPGMLDGKKALLQDIALMTGADYLSGDLGMSLMGATSDQLGVSRR 353
Cdd:PRK12851 243 SGKPLLIIAEDVEGEALATLVVNKLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGIKLENVTLEQLGRAKK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 354 VVITANSTTIVADASTKPEIQARIAQMKKDLAETDNSYLSKKIAERIAKLTGGVAVIKVGGHTETELEDRKLRIEDAKNA 433
Cdd:PRK12851 323 VVVEKENTTIIDGAGSKTEIEGRVAQIRAQIEETTSDYDREKLQERLAKLAGGVAVIRVGASTEVEVKEKKDRVDDALHA 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 434 TFAAMREGIVPGGGatyIHLLDEIPRIKKNLMEDSYEQIGADIVAMALTAPAMAIATNAGVDGSVVVQKTRELEWRSGYN 513
Cdd:PRK12851 403 TRAAVEEGIVPGGG---VALLRAVKALDKLETANGDQRTGVEIVRRALEAPVRQIAENAGAEGSVVVGKLREKPGGYGFN 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 15239580 514 AMSGKYEDLLNAGIADPCRVSRFALQNAVSVAGIILTTQAVLVEKIKQPKPAVPQVPG 571
Cdd:PRK12851 480 AATNEYGDLYAQGVIDPVKVVRTALQNAASVAGLLLTTEAMVAEKPKKEPAPPAPPGG 537
|
|
| PLN03167 |
PLN03167 |
Chaperonin-60 beta subunit; Provisional |
1-570 |
7.96e-161 |
|
Chaperonin-60 beta subunit; Provisional
Pssm-ID: 215611 [Multi-domain] Cd Length: 600 Bit Score: 472.10 E-value: 7.96e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 1 MFAVSPSSFSPTTISPRRSGQRNEPRKFSVVRAGAKRILYGKDSR--EKLQAGIDKLADAVSITLGPRGRNVVLAEK-DT 77
Cdd:PLN03167 22 SDNRLSSFASISSSSFGRRQSVRLRRSRSPKVKAAKELHFNKDGSaiKKLQAGVNKLADLVGVTLGPKGRNVVLESKyGS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 78 IKVINDGVTIAKSIELPDTIENAGATLIQEVAIKMNESAGDGTTTAIILAREMIKAGSLAIAFGANAVSVKNGMNKTVKE 157
Cdd:PLN03167 102 PKIVNDGVTVAKEVELEDPVENIGAKLVRQAAAKTNDLAGDGTTTSVVLAQGLIAEGVKVVAAGANPVQITRGIEKTAKA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 158 LVRVLQMKSIPVQgKNDIKAVASISAGNDEFVGNLIAETVEKIGPDGVISIESSSTSETSVIVEEGMKFDKGYMSPHFIT 237
Cdd:PLN03167 182 LVKELKKMSKEVE-DSELADVAAVSAGNNYEVGNMIAEAMSKVGRKGVVTLEEGKSAENNLYVVEGMQFDRGYISPYFVT 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 238 NQEKSTVEFDKAKILVTDQKITSAKELVPLLEKTSQLSVPLLIIAEDISAEVLEILVVNKKQGLINVAVVKCPGMLDGKK 317
Cdd:PLN03167 261 DSEKMSVEYDNCKLLLVDKKITNARDLIGILEDAIRGGYPLLIIAEDIEQEALATLVVNKLRGSLKIAALKAPGFGERKS 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 318 ALLQDIALMTGADYLSGDLGMSLMGATSDQLGVSRRVVITANSTTIVADASTKPEIQARIAQMKKDLAETDNSYLSKKIA 397
Cdd:PLN03167 341 QYLDDIAILTGGTVIREEVGLSLDKVGKEVLGTAAKVVLTKDTTTIVGDGSTQEAVNKRVAQIKNLIEAAEQDYEKEKLN 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 398 ERIAKLTGGVAVIKVGGHTETELEDRKLRIEDAKNATFAAMREGIVPGGGATYIHLLDEIPRIKKNLMEDSyEQIGADIV 477
Cdd:PLN03167 421 ERIAKLSGGVAVIQVGAQTETELKEKKLRVEDALNATKAAVEEGIVVGGGCTLLRLASKVDAIKDTLENDE-QKVGADIV 499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 478 AMALTAPAMAIATNAGVDGSVVVQKTRELE-WRSGYNAMSGKYEDLLNAGIADPCRVSRFALQNAVSVAGIILTTQAVLV 556
Cdd:PLN03167 500 KRALSYPLKLIAKNAGVNGSVVSEKVLSNDnPKFGYNAATGKYEDLMAAGIIDPTKVVRCCLEHAASVAKTFLTSDCVVV 579
|
570
....*....|....
gi 15239580 557 EkIKQPKPAVPQVP 570
Cdd:PLN03167 580 E-IKEPEPVPAGNP 592
|
|
| groEL |
PRK12852 |
chaperonin GroEL; Reviewed |
35-572 |
1.06e-159 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237232 Cd Length: 545 Bit Score: 467.40 E-value: 1.06e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 35 AKRILYGKDSREKLQAGIDKLADAVSITLGPRGRNVVLAEK-DTIKVINDGVTIAKSIELPDTIENAGATLIQEVAIKMN 113
Cdd:PRK12852 3 AKDVKFSGDARDRMLRGVDILANAVKVTLGPKGRNVVIEKSfGAPRITKDGVTVAKEIELEDKFENMGAQMVREVASKTN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 114 ESAGDGTTTAIILAREMIKAGSLAIAFGANAVSVKNGMNKTVKELVRVLQMKSIPVQGKNDIKAVASISAGNDEFVGNLI 193
Cdd:PRK12852 83 DLAGDGTTTATVLAQAIVREGAKAVAAGMNPMDLKRGIDIAVAAVVKDIEKRAKPVASSAEIAQVGTISANGDAAIGKMI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 194 AETVEKIGPDGVISIESSSTSETSVIVEEGMKFDKGYMSPHFITNQEKSTVEFDKAKILVTDQKITSAKELVPLLEKTSQ 273
Cdd:PRK12852 163 AQAMQKVGNEGVITVEENKSLETEVDIVEGMKFDRGYLSPYFVTNAEKMTVELDDAYILLHEKKLSGLQAMLPVLEAVVQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 274 LSVPLLIIAEDISAEVLEILVVNKKQGLINVAVVKCPGMLDGKKALLQDIALMTGADYLSGDLGMSLMGATSDQLGVSRR 353
Cdd:PRK12852 243 SGKPLLIIAEDVEGEALATLVVNRLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGQLISEDLGIKLENVTLKMLGRAKK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 354 VVITANSTTIVADASTKPEIQARIAQMKKDLAETDNSYLSKKIAERIAKLTGGVAVIKVGGHTETELEDRKLRIEDAKNA 433
Cdd:PRK12852 323 VVIDKENTTIVNGAGKKADIEARVGQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKEKKDRVEDALNA 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 434 TFAAMREGIVPGGGATYIHLLDEIPRIKKnlmEDSYEQIGADIVAMALTAPAMAIATNAGVDGSVVVQKTRELEWRS-GY 512
Cdd:PRK12852 403 TRAAVQEGIVPGGGVALLRAKKAVGRINN---DNADVQAGINIVLKALEAPIRQIAENAGVEGSIVVGKILENKSETfGF 479
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15239580 513 NAMSGKYEDLLNAGIADPCRVSRFALQNAVSVAGIILTTQAVLVEK-IKQPKPAVPQVPGI 572
Cdd:PRK12852 480 DAQTEEYVDMVAKGIIDPAKVVRTALQDAASVAGLLVTTEAMVAELpKKDAAPAMPAGGGM 540
|
|
| PRK14104 |
PRK14104 |
chaperonin GroEL; Provisional |
35-571 |
4.50e-147 |
|
chaperonin GroEL; Provisional
Pssm-ID: 172594 Cd Length: 546 Bit Score: 434.84 E-value: 4.50e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 35 AKRILYGKDSREKLQAGIDKLADAVSITLGPRGRNVVLAEK-DTIKVINDGVTIAKSIELPDTIENAGATLIQEVAIKMN 113
Cdd:PRK14104 3 AKEVKFGVDARDRMLRGVDILANAVKVTLGPKGRNVVLDKSfGAPRITKDGVTVAKEIELEDKFENMGAQMVREVASKSA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 114 ESAGDGTTTAIILAREMIKAGSLAIAFGANAVSVKNGMNKTVKELVRVLQMKSIPVQGKNDIKAVASISAGNDEFVGNLI 193
Cdd:PRK14104 83 DAAGDGTTTATVLAQAIVREGAKSVAAGMNPMDLKRGIDLAVEAVVADLVKNSKKVTSNDEIAQVGTISANGDAEIGKFL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 194 AETVEKIGPDGVISIESSSTSETSVIVEEGMKFDKGYMSPHFITNQEKSTVEFDKAKILVTDQKITSAKELVPLLEKTSQ 273
Cdd:PRK14104 163 ADAMKKVGNEGVITVEEAKSLETELDVVEGMQFDRGYISPYFVTNADKMRVEMDDAYILINEKKLSSLNELLPLLEAVVQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 274 LSVPLLIIAEDISAEVLEILVVNKKQGLINVAVVKCPGMLDGKKALLQDIALMTGADYLSGDLGMSLMGATSDQLGVSRR 353
Cdd:PRK14104 243 TGKPLVIVAEDVEGEALATLVVNRLRGGLKVAAVKAPGFGDRRKAMLQDIAILTGGQAISEDLGIKLENVTLQMLGRAKK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 354 VVITANSTTIVADASTKPEIQARIAQMKKDLAETDNSYLSKKIAERIAKLTGGVAVIKVGGHTETELEDRKLRIEDAKNA 433
Cdd:PRK14104 323 VMIDKENTTIVNGAGKKADIEARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKERKDRVDDAMHA 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 434 TFAAMREGIVPGGGATYIHLLDEIPRIKknlMEDSYEQIGADIVAMALTAPAMAIATNAGVDGSVVVQKTRELEWRS-GY 512
Cdd:PRK14104 403 TRAAVEEGIVPGGGVALLRASEQLKGIK---TKNDDQKTGVEIVRKALSAPARQIAINAGEDGSVIVGKILEKEQYSyGF 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 15239580 513 NAMSGKYEDLLNAGIADPCRVSRFALQNAVSVAGIILTTQAVLVEKIKQPKPAVPQVPG 571
Cdd:PRK14104 480 DSQTGEYGNLVSKGIIDPTKVVRTAIQNAASVAALLITTEAMVAELPKKGGAGPAMPPG 538
|
|
| chaperonin_type_I_II |
cd00309 |
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ... |
36-556 |
1.05e-110 |
|
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: 338.63 E-value: 1.05e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 36 KRILYGKDSREKLQAGIDKLADAVSITLGPRGRNVVLAEKD-TIKVINDGVTIAKSIElpdtIENAGATLIQEVAIKMNE 114
Cdd:cd00309 1 KEREFGEEARLSNINAAKALADAVKTTLGPKGMDKMLVDSLgDPTITNDGATILKEIE----VEHPAAKLLVEVAKSQDD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 115 SAGDGTTTAIILAREMIKAGSLAIAFGANAVSVKNGMNKTVKELVRVLQMKSIP--VQGKNDIKAVASISAG------ND 186
Cdd:cd00309 77 EVGDGTTTVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVPidVEDREELLKVATTSLNsklvsgGD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 187 EFVGNLIAETVEKIGPDGVISIE-------SSSTSETSVIVEEGMKFDKGYMSPHFitnqeksTVEFDKAKILVTDQKIT 259
Cdd:cd00309 157 DFLGELVVDAVLKVGKENGDVDLgvirvekKKGGSLEDSELVVGMVFDKGYLSPYM-------PKRLENAKILLLDCKLE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 260 SakelvpllektsqlsvplLIIAED-ISAEVLEILVVNkkqgliNVAVVKCPgmldgKKALLQDIALMTGADYLSgdlgm 338
Cdd:cd00309 230 Y------------------VVIAEKgIDDEALHYLAKL------GIMAVRRV-----RKEDLERIAKATGATIVS----- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 339 SLMGATSDQLGVSRRVVITA----NSTTIVADAStkpeiqariaqmkkdlaetdnsylskkiaeriakltGGVAVIKVGG 414
Cdd:cd00309 276 RLEDLTPEDLGTAGLVEETKigdeKYTFIEGCKG------------------------------------GKVATILLRG 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 415 HTETELEDRKLRIEDAKNATFAAMRE-GIVPGGGATYIHLLDEIPRIKKNLMEDsyEQIGADIVAMALTAPAMAIATNAG 493
Cdd:cd00309 320 ATEVELDEAERSLHDALCAVRAAVEDgGIVPGGGAAEIELSKALEELAKTLPGK--EQLGIEAFADALEVIPRTLAENAG 397
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15239580 494 VDGSVVVQKTRELEWRSGYNA----MSGKYEDLLNAGIADPCRVSRFALQNAVSVAGIILTTQAVLV 556
Cdd:cd00309 398 LDPIEVVTKLRAKHAEGGGNAggdvETGEIVDMKEAGIIDPLKVKRQALKSATEAASLILTIDDIIV 464
|
|
| Cpn60_TCP1 |
pfam00118 |
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ... |
55-558 |
3.31e-74 |
|
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: 244.42 E-value: 3.31e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 55 LADAVSITLGPRGRNVVL-AEKDTIKVINDGVTIAKSIElpdtIENAGATLIQEVAIKMNESAGDGTTTAIILAREMIKA 133
Cdd:pfam00118 1 LADIVRTSLGPKGMDKMLvNSGGDVTVTNDGATILKELE----IQHPAAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 134 GSLAIAFGANAVSVKNGMNKTVKELVRVLQ-MKSIPVQGKN--DIKAVASISAGND------EFVGNLIAETVEKIGPDG 204
Cdd:pfam00118 77 AEKLLAAGVHPTTIIEGYEKALEKALEILDsIISIPVEDVDreDLLKVARTSLSSKiisresDFLAKLVVDAVLAIPKND 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 205 VISIESSSTSETSV-------IVEEGMKFDKGYMSPHFITnqekstvEFDKAKILVTDQKITSAKE-------------- 263
Cdd:pfam00118 157 GSFDLGNIGVVKILggsledsELVDGVVLDKGPLHPDMPK-------RLENAKVLLLNCSLEYEKTetkatvvlsdaeql 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 264 ----------LVPLLEKTSQLSVPLLIIAEDISAEVLEILVVNKKQGLINVavvkcpgmldgKKALLQDIALMTGADYLS 333
Cdd:pfam00118 230 erflkaeeeqILEIVEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMALRRV-----------KKRDLERLAKATGARAVS 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 334 gdlgmSLMGATSDQLGVSRRV---VITANSTTIVADastkpeiqariaqmkkdlaetdnsylskkiaeriaKLTGGVAVI 410
Cdd:pfam00118 299 -----SLDDLTPDDLGTAGKVeeeKIGDEKYTFIEG-----------------------------------CKSPKAATI 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 411 KVGGHTETELEDRKLRIEDAKNATFAAMRE-GIVPGGGATYIHLLDEIPRIKKNLmeDSYEQIGADIVAMALTAPAMAIA 489
Cdd:pfam00118 339 LLRGATDHVLDEIERSIHDALCVVKNAIEDpRVVPGGGAVEMELARALREYAKSV--SGKEQLAIEAFAEALEVIPKTLA 416
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15239580 490 TNAGVDGSVVVQKTREL----EWRSGYNAMSGKYEDLLNAGIADPCRVSRFALQNAVSVAGIILTTQAVLVEK 558
Cdd:pfam00118 417 ENAGLDPIEVLAELRAAhasgEKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKSATEAASTILRIDDIIKAK 489
|
|
| chaperonin_like |
cd03333 |
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ... |
172-440 |
5.72e-24 |
|
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: 99.85 E-value: 5.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 172 KNDIKAVASISAG-----NDEFVGNLIAETVEKIGPDGVISIE-------SSSTSETSVIVEEGMKFDKGYMSPHFITnq 239
Cdd:cd03333 1 RELLLQVATTSLNsklssWDDFLGKLVVDAVLKVGPDNRMDDLgvikvekIPGGSLEDSELVVGVVFDKGYASPYMPK-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 240 ekstvEFDKAKILVTDQKITSakelvpllektsqlsvplLIIAED-ISAEVLEILVVNkkqgliNVAVVKcpgmlDGKKA 318
Cdd:cd03333 79 -----RLENAKILLLDCPLEY------------------VVIAEKgIDDLALHYLAKA------GIMAVR-----RVKKE 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 319 LLQDIALMTGADYLSgdlgmSLMGATSDQLGVSRRVVITansttivadastkpeiqariaqmkkdlaetdnsylsKKIAE 398
Cdd:cd03333 125 DLERIARATGATIVS-----SLEDLTPEDLGTAELVEET------------------------------------KIGEE 163
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 15239580 399 RIAKLTG----GVAVIKVGGHTETELEDRKLRIEDAKNATFAAMRE 440
Cdd:cd03333 164 KLTFIEGckggKAATILLRGATEVELDEVKRSLHDALCAVRAAVEE 209
|
|
| cpn60 |
cd03343 |
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ... |
30-549 |
3.62e-15 |
|
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: 78.46 E-value: 3.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 30 VVRAGAKRIlYGKDSREKLQAGIDKLADAVSITLGPRGRNVVLAEK-DTIKVINDGVTIAKSIElpdtIENAGATLIQEV 108
Cdd:cd03343 3 ILKEGTQRT-SGRDAQRMNIAAAKAVAEAVRTTLGPKGMDKMLVDSlGDVTITNDGATILKEMD----IEHPAAKMLVEV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 109 AIKMNESAGDGTTTAIILAREMIKAGSLAIAFGANAVSVKNGMNKTVKELVRVLQMKSIPVQGKND--IKAVASIS---- 182
Cdd:cd03343 78 AKTQDEEVGDGTTTAVVLAGELLEKAEDLLDQNIHPTVIIEGYRLAAEKALELLDEIAIKVDPDDKdtLRKIAKTSltgk 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 183 --AGNDEFVGNLIAETVEKIGPDGVISIESSSTSETSVIVE----------EGMKFDKGYMSPhfitNQEKStVEfdKAK 250
Cdd:cd03343 158 gaEAAKDKLADLVVDAVLQVAEKRDGKYVVDLDNIKIEKKTggsvddteliRGIVIDKEVVHP----GMPKR-VE--NAK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 251 ILVTDQ-------------KITSAKELVPLLEKTSQLsvpLLIIAEDISAEVLEILVVNK-----------KQGLINVAV 306
Cdd:cd03343 231 IALLDAplevkkteidakiRITSPDQLQAFLEQEEAM---LKEMVDKIADTGANVVFCQKgiddlaqhylaKAGILAVRR 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 307 VkcpgmldgKKALLQDIALMTGADYLSgdlgmSLMGATSDQLGVSrrvvitansttivadastkpeiqariaqmkkDLAE 386
Cdd:cd03343 308 V--------KKSDMEKLARATGAKIVT-----NIDDLTPEDLGEA-------------------------------ELVE 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 387 TDNSYLSKKIAERIAKLTGGVAVIKVGGhTETELEDRKLRIEDAKNATFAAMREG-IVPGGGATYIHLLDEIPRIKKNLm 465
Cdd:cd03343 344 ERKVGDDKMVFVEGCKNPKAVTILLRGG-TEHVVDELERALEDALRVVADALEDGkVVAGGGAVEIELAKRLREYARSV- 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 466 eDSYEQIGADIVAMALTAPAMAIATNAGVDGSVVVQKTR----ELEWRSGYNAMSGKYEDLLNAGIADPCRVSRFALQNA 541
Cdd:cd03343 422 -GGREQLAVEAFADALEEIPRTLAENAGLDPIDTLVELRaaheKGNKNAGLDVYTGEVVDMLEKGVIEPLRVKKQAIKSA 500
|
....*...
gi 15239580 542 VSVAGIIL 549
Cdd:cd03343 501 TEAATMIL 508
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
55-134 |
3.25e-09 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 59.66 E-value: 3.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 55 LADAVSITLGPRGRNVVL------AEKDTIKVINDGVTIAKSIelpdTIENAGATLIQEVAIKMNESAGDGTTTAIILAR 128
Cdd:PTZ00212 34 VADLVKTTLGPKGMDKILqpmsegPRSGNVTVTNDGATILKSV----WLDNPAAKILVDISKTQDEEVGDGTTSVVVLAG 109
|
....*.
gi 15239580 129 EMIKAG 134
Cdd:PTZ00212 110 ELLREA 115
|
|
| TCP1_beta |
cd03336 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ... |
41-132 |
9.89e-09 |
|
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: 57.72 E-value: 9.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 41 GKDSREKLQAGIDKLADAVSITLGPRGRNVVL---AEKDTIKVINDGVTIAKSIelpdTIENAGATLIQEVAIKMNESAG 117
Cdd:cd03336 11 GETARLSSFVGAIAIGDLVKTTLGPKGMDKILqsvGRSGGVTVTNDGATILKSI----GVDNPAAKVLVDISKVQDDEVG 86
|
90
....*....|....*
gi 15239580 118 DGTTTAIILAREMIK 132
Cdd:cd03336 87 DGTTSVTVLAAELLR 101
|
|
| chap_CCT_alpha |
TIGR02340 |
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ... |
41-200 |
2.51e-08 |
|
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: 56.65 E-value: 2.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 41 GKDSREKLQAGIDKLADAVSITLGPRGRNVVLAEK-DTIKVINDGVTIAKSIElpdtIENAGATLIQEVAIKMNESAGDG 119
Cdd:TIGR02340 10 GQDVRTQNVTAAMAIANIVKTSLGPVGLDKMLVDDiGDVTITNDGATILKLLE----VEHPAAKILVELAQLQDREVGDG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 120 TTTAIILAREMIKAGSLAIAFGANAVSVKNGMNKTVKELVRVLQ---MKSIPVQGKNDIKAVA--SISA----GNDEFVG 190
Cdd:TIGR02340 86 TTSVVIIAAELLKRADELVKNKIHPTSVISGYRLACKEAVKYIKenlSVSVDELGREALINVAktSMSSkiigLDSDFFS 165
|
170
....*....|
gi 15239580 191 NLIAETVEKI 200
Cdd:TIGR02340 166 NIVVDAVLAV 175
|
|
| TCP1_delta |
cd03338 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ... |
55-182 |
2.83e-08 |
|
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: 56.53 E-value: 2.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 55 LADAVSITLGPRG--RNVVLAEKDTIkVINDGVTIAKSIELPDTIenagATLIQEVAIKMNESAGDGTTTAIILAREMIK 132
Cdd:cd03338 20 VADAIRTSLGPRGmdKMIQTGKGEVI-ITNDGATILKQMSVLHPA----AKMLVELSKAQDIEAGDGTTSVVVLAGALLS 94
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 15239580 133 AGSLAIAFGANAVSVKNGMNKTVKELVRVLQMKSIPV--QGKNDIKAVASIS 182
Cdd:cd03338 95 ACESLLKKGIHPTVISESFQIAAKKAVEILDSMSIPVdlNDRESLIKSATTS 146
|
|
| chap_CCT_theta |
TIGR02346 |
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ... |
52-565 |
2.93e-08 |
|
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: 56.26 E-value: 2.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 52 IDKLADAVSITLGPRGRN-VVLAEKDTIKVINDGVTIAKSIElpdtIENAGATLIQEVAIKMNESAGDGTTTAIILAREM 130
Cdd:TIGR02346 27 CKELSQITRTSLGPNGMNkMVINHLEKLFVTNDAATILRELE----VQHPAAKLLVMASEMQENEIGDGTNLVLVLAGEL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 131 IKAGSLAIAFGANAVSVKNGMNKTVKELVRVL-QMKSIPVQGKNDIKAV-----ASISA---GNDEFVGNLIAETVEKIG 201
Cdd:TIGR02346 103 LNKAEELIRMGLHPSEIIKGYEMALKKAMEILeELVVWEVKDLRDKDELikalkASISSkqyGNEDFLAQLVAQACSTVL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 202 P--------DGVISIESSSTSETSVIVEEGMKFDKgymsphfitNQEKSTVEFDKAKILV----TDQKITSAKELVpLLE 269
Cdd:TIGR02346 183 PknpqnfnvDNIRVCKILGGSLSNSEVLKGMVFNR---------EAEGSVKSVKNAKVAVfscpLDTATTETKGTV-LIH 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 270 KTSQLsvplliiaEDIS-AEVLEILVVNKKQGLINVAVVKCPGMLDgkkallqDIALMTGADYlsgdlGMSLMGATSD-Q 347
Cdd:TIGR02346 253 NAEEL--------LNYSkGEENQIEAMIKAIADSGVNVIVTGGSVG-------DMALHYLNKY-----NIMVLKIPSKfE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 348 LgvsRRVVITANSTTIVADASTKPEiqariaqmkkDLAETDNSYLSKKIAERIA-----KLTGGVAVIKVGGHTETELED 422
Cdd:TIGR02346 313 L---RRLCKTVGATPLPRLGAPTPE----------EIGYVDSVYVSEIGGDKVTvfkqeNGDSKISTIILRGSTDNLLDD 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 423 RKLRIEDAKNATFAAMREG-IVPGGGATYIHLLDEIPRIKKNlmEDSYEQIGADIVAMALTAPAMAIATNAGVDGSVVVQ 501
Cdd:TIGR02346 380 IERAIDDGVNTVKALVKDGrLLPGAGATEIELASRLTKYGEK--LPGLDQYAIKKFAEAFEIIPRTLAENAGLNANEVIP 457
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 502 KT----RELEWRSGYN--AMSGKYEDLLNAGIADPCRVSRFALQNAVSVAGIILTtqavlVEKIKQPKPA 565
Cdd:TIGR02346 458 KLyaahKKGNKSKGIDieAESDGVKDASEAGIYDMLATKKWAIKLATEAAVTVLR-----VDQIIMAKPA 522
|
|
| TCP1_eta |
cd03340 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ... |
54-133 |
1.08e-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: 54.60 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 54 KLADAVSITLGPRGRN-VVLAEKDTIKVINDGVTIAKsieLPDTIENAGATLIqEVAIKMNESAGDGTTTAIILAREMIK 132
Cdd:cd03340 27 AIADAVRTTLGPRGMDkLIVDGRGKVTISNDGATILK---LLDIVHPAAKTLV-DIAKSQDAEVGDGTTSVVVLAGEFLK 102
|
.
gi 15239580 133 A 133
Cdd:cd03340 103 E 103
|
|
| TCP1_alpha |
cd03335 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ... |
41-200 |
1.23e-07 |
|
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: 54.60 E-value: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 41 GKDSREKLQAGIDKLADAVSITLGPRGRNVVLAekDTI---KVINDGVTIAKSIElpdtIENAGATLIQEVAIKMNESAG 117
Cdd:cd03335 6 GQDVRTQNVTAAMAIANIVKSSLGPVGLDKMLV--DDIgdvTITNDGATILKLLE----VEHPAAKILVELAQLQDKEVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 118 DGTTTAIILAREMIKAGSLAIAFGANAVSVKNGMNKTVKELVRVLQMK-SIPVQ--GKNDIKAVA--SISA----GNDEF 188
Cdd:cd03335 80 DGTTSVVIIAAELLKRANELVKQKIHPTTIISGYRLACKEAVKYIKEHlSISVDnlGKESLINVAktSMSSkiigADSDF 159
|
170
....*....|..
gi 15239580 189 VGNLIAETVEKI 200
Cdd:cd03335 160 FANMVVDAILAV 171
|
|
| chap_CCT_delta |
TIGR02342 |
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ... |
55-174 |
1.23e-07 |
|
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: 54.40 E-value: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 55 LADAVSITLGPRGRNVVLAEKD-TIKVINDGVTIAKSIElpdtIENAGATLIQEVAIKMNESAGDGTTTAIILAREMIKA 133
Cdd:TIGR02342 21 VADAIRTSLGPKGMDKMIQDGKgEVIITNDGATILKQMA----VLHPAAKMLVELSKAQDIEAGDGTTSVVILAGALLGA 96
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 15239580 134 GSLAIAFGANAVSVKNGMNKTVKELVRVLQMKSIPVQGKND 174
Cdd:TIGR02342 97 CERLLNKGIHPTIISESFQSAADEAIKILDEMSIPVDLSDR 137
|
|
| chap_CCT_eta |
TIGR02345 |
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ... |
54-133 |
4.53e-07 |
|
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: 52.45 E-value: 4.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 54 KLADAVSITLGPRGRNVVLAEKDTIKVI-NDGVTIAKsieLPDTIENAGATLIqEVAIKMNESAGDGTTTAIILAREMIK 132
Cdd:TIGR02345 29 AIAEALKTTLGPRGMDKLIVGSNGKATIsNDGATILK---LLDIVHPAAKTLV-DIAKSQDAEVGDGTTSVTILAGELLK 104
|
.
gi 15239580 133 A 133
Cdd:TIGR02345 105 E 105
|
|
| chap_CCT_gamma |
TIGR02344 |
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ... |
55-183 |
1.21e-06 |
|
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT gamma chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.
Pssm-ID: 274085 [Multi-domain] Cd Length: 524 Bit Score: 51.28 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 55 LADAVSITLGPRGR-NVVLAEKDTIKVINDGVTIAKSIelpDTIENAGATLIqEVAIKMNESAGDGTTTAIILAREMIKA 133
Cdd:TIGR02344 28 VADIIRTCLGPRSMlKMLLDPMGGIVMTNDGNAILREI---DVAHPAAKSMI-ELSRTQDEEVGDGTTSVIILAGEMLSV 103
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 15239580 134 GSLAIAFGANAVSVKNGMNKTVKELVRVLQMKSIPVQGKNDIKAVASISA 183
Cdd:TIGR02344 104 AEPFLEQNIHPTVIIRAYRKALDDALSVLEEISIPVDVNDDAAMLKLIQS 153
|
|
| chap_CCT_beta |
TIGR02341 |
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ... |
55-139 |
2.96e-06 |
|
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: 49.86 E-value: 2.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 55 LADAVSITLGPRGRNVVL---AEKDTIKVINDGVTIAKSIELpdtiENAGATLIQEVAIKMNESAGDGTTTAIILAREMI 131
Cdd:TIGR02341 26 IGDLVKSTLGPKGMDKILqssSSDASIMVTNDGATILKSIGV----DNPAAKVLVDMSKVQDDEVGDGTTSVTVLAAELL 101
|
....*...
gi 15239580 132 KAGSLAIA 139
Cdd:TIGR02341 102 REAEKLIN 109
|
|
| TCP1_theta |
cd03341 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ... |
54-203 |
3.16e-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: 49.91 E-value: 3.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 54 KLADAVSITLGPRGRN-VVLAEKDTIKVINDGVTIAKSIElpdtIENAGATLIQEVAIKMNESAGDGTTTAIILAREMI- 131
Cdd:cd03341 19 ELSQITRTSYGPNGMNkMVINHLEKLFVTSDAATILRELE----VQHPAAKLLVMASQMQEEEIGDGTNLVVVLAGELLe 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 132 KAGSLaIAFGANAVSVKNGMNKTVKELVRVL-QMKSIPVQGKNDIK--------AVASISAGNDEFVGNLIAETVEKIGP 202
Cdd:cd03341 95 KAEEL-LRMGLHPSEIIEGYEKALKKALEILeELVVYKIEDLRNKEevskalktAIASKQYGNEDFLSPLVAEACISVLP 173
|
.
gi 15239580 203 D 203
Cdd:cd03341 174 E 174
|
|
| TCP1_zeta |
cd03342 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
55-181 |
3.72e-06 |
|
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.
Pssm-ID: 239458 [Multi-domain] Cd Length: 484 Bit Score: 49.56 E-value: 3.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 55 LADAVSITLGPRGRNVVLAEKD-TIKVINDGVTIAKSIelpdTIENAGATLIQEVAIKMNESAGDGTTTAIILAREMIKA 133
Cdd:cd03342 24 LQDVLKTNLGPKGTLKMLVSGAgDIKLTKDGNVLLSEM----QIQHPTASMIARAATAQDDITGDGTTSNVLLIGELLKQ 99
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 15239580 134 GSLAIAFGANAVSVKNGMNKTVKELVRVLQMKSIPVQGKNDIKAVASI 181
Cdd:cd03342 100 AERYIQEGVHPRIITEGFELAKNKALKFLESFKVPVEIDTDRELLLSV 147
|
|
| TCP1_gamma |
cd03337 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ... |
30-174 |
9.97e-06 |
|
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.
Pssm-ID: 239453 [Multi-domain] Cd Length: 480 Bit Score: 48.45 E-value: 9.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 30 VVRAGAKRilygkDSREKLQAGIDK----LADAVSITLGPRGR-NVVLAEKDTIKVINDGVTIAKSIelpdTIENAGATL 104
Cdd:cd03337 4 VLNQNTKR-----ESGRKAQLGNIQaaktVADVIRTCLGPRAMlKMLLDPMGGIVLTNDGNAILREI----DVAHPAAKS 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 105 IQEVAIKMNESAGDGTTTAIILAREMIKAGSLAIAFGANAVSVKNGMNKTVKELVRVLQMKSIPVQGKND 174
Cdd:cd03337 75 MIELSRTQDEEVGDGTTSVIILAGEILAVAEPFLERGIHPTVIIKAYRKALEDALKILEEISIPVDVNDR 144
|
|
| TCP1_epsilon |
cd03339 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ... |
26-127 |
5.42e-05 |
|
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: 46.14 E-value: 5.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 26 RKFSVVR-AGAKRILYGKDSREKLQAGIDKLADAVSITLGPRGRNVVLAEKD-TIKVINDGVTIAKSIElpdtIENAGAT 103
Cdd:cd03339 5 RPFIIVReQEKKKRLKGLEAHKSHILAAKSVANILRTSLGPRGMDKILVSPDgEVTVTNDGATILEKMD----VDHQIAK 80
|
90 100
....*....|....*....|....
gi 15239580 104 LIQEVAIKMNESAGDGTTTAIILA 127
Cdd:cd03339 81 LLVELSKSQDDEIGDGTTGVVVLA 104
|
|
| TCP1_zeta |
cd03342 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
415-559 |
2.63e-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: 43.79 E-value: 2.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 415 HTETELEDRklrIEDAKNATFAAMREG-IVPGGGATYIHLLDEIPRIKKNLMEDSyeQIGADIVAMALTAPAMAIATNAG 493
Cdd:cd03342 340 HTITQIKDA---IRDGLRAVKNAIEDKcVVPGAGAFEVALYAHLKEFKKSVKGKA--KLGVQAFADALLVIPKTLAENSG 414
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 494 VDG-SVVVQKTRELEWRS---GYNAMSGKYEDLLNAGIADPCRVSRFALQNAVSVAgiiltTQAVLVEKI 559
Cdd:cd03342 415 LDVqETLVKLQDEYAEGGqvgGVDLDTGEPMDPESEGIWDNYSVKRQILHSATVIA-----SQLLLVDEI 479
|
|
| chap_CCT_zeta |
TIGR02347 |
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ... |
55-162 |
9.32e-04 |
|
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: 42.03 E-value: 9.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239580 55 LADAVSITLGPRGR-NVVLAEKDTIKVINDGVTIAKSIelpdTIENAGATLIQEVAIKMNESAGDGTTTAIILAREMIKA 133
Cdd:TIGR02347 28 LQDVLKTNLGPKGTlKMLVSGAGDIKLTKDGNVLLNEM----QIQHPTASMIARAATAQDDITGDGTTSTVLLIGELLKQ 103
|
90 100
....*....|....*....|....*....
gi 15239580 134 GSLAIAFGANAVSVKNGMNKTVKELVRVL 162
Cdd:TIGR02347 104 AERYILEGVHPRIITEGFEIARKEALQFL 132
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