|
Name |
Accession |
Description |
Interval |
E-value |
| GroEL |
cd03344 |
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ... |
4-525 |
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: 609.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 4 KNICYRDVIIKQIKKGLQDTTNILSLTLGPRGKNIVLWDKTSKPQIINDGTSIINKINNQNFVEHIGQFLVKDVIFNVND 83
Cdd:cd03344 1 KDIKFGEEARKALLRGVNKLADAVKVTLGPKGRNVVIEKSFGSPKITKDGVTVAKEIELEDPFENMGAQLVKEVASKTND 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 84 SVGDGTSTTGILTGNVLSRGLSLIHSGYTPYFFSNGIFKCTNILLNKLYKISWPLNNNKDILNIATNSSGGDKLLGKLIV 163
Cdd:cd03344 81 VAGDGTTTATVLARAIIKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKPVKTKEEIAQVATISANGDEEIGELIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 164 NAYKRVGTDGLISIETSDKNDTSLIVYGGLQIDRGYVSHKFINNFKNSTCEYNDSAILVTDLPIDSIKQAAAIMQSILQI 243
Cdd:cd03344 161 EAMEKVGKDGVITVEEGKTLETELEVVEGMQFDRGYLSPYFVTDPEKMEVELENPYILLTDKKISSIQELLPILELVAKA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 244 DKPLLIISDTISKKCLNAFLVNNKEKNIKICAVKIPSFGSYRKSILQDISIATGASFYSSDSGMKLKNLKPEDFGSLRKC 323
Cdd:cd03344 241 GRPLLIIAEDVEGEALATLVVNKLRGGLKVCAVKAPGFGDRRKAMLEDIAILTGGTVISEELGLKLEDVTLEDLGRAKKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 324 IVSENNCTLISKNRFKNQIKSRIDYLEKLLSSTDSTFETNLLSERIAKLSGGIAVIRVGAPTELELIDKKLRLEDAKNAT 403
Cdd:cd03344 321 VVTKDDTTIIGGAGDKAAIKARIAQIRKQIEETTSDYDKEKLQERLAKLSGGVAVIKVGGATEVELKEKKDRVEDALNAT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 404 FSAVTQGVVTGSAVSLVHLSNFLKYFMALssCMEESLGMQLLRKSIVVPNRNIILNSDEDGYLMEKKIVNYPFEIGYDAE 483
Cdd:cd03344 401 RAAVEEGIVPGGGVALLRASPALDKLKAL--NGDEKLGIEIVRRALEAPLRQIAENAGVDGSVVVEKVLESPDGFGYDAA 478
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 75756309 484 YKCLTNLVGEGVVDPSLLLYNSLISLCKISSVLMHTQAVISK 525
Cdd:cd03344 479 TGEYVDMIEAGIIDPTKVVRSALQNAASVASLLLTTEALVVD 520
|
|
| GroEL |
TIGR02348 |
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ... |
4-526 |
2.91e-129 |
|
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: 387.42 E-value: 2.91e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 4 KNICYRDVIIKQIKKGLQDTTNILSLTLGPRGKNIVLWDKTSKPQIINDGTSIINKINNQNFVEHIGQFLVKDVIFNVND 83
Cdd:TIGR02348 2 KQIKFDEEARKALLRGVDKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDKFENMGAQLVKEVASKTND 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 84 SVGDGTSTTGILTGNVLSRGLSLIHSGYTPYFFSNGIFKCTNILLNKLYKISWPLNNNKDILNIATNSSGGDKLLGKLIV 163
Cdd:TIGR02348 82 VAGDGTTTATVLAQAIVKEGLKNVAAGANPIELKRGIEKAVEAVVEELKKLSKPVKGKKEIAQVATISANNDEEIGSLIA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 164 NAYKRVGTDGLISIETSDKNDTSLIVYGGLQIDRGYVSHKFINNFKNSTCEYNDSAILVTDLPIDSIKQAAAIMQSILQI 243
Cdd:TIGR02348 162 EAMEKVGKDGVITVEESKSLETELEVVEGMQFDRGYISPYFVTDAEKMEVELENPYILITDKKISNIKDLLPLLEKVAQS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 244 DKPLLIISDTISKKCLnAFLVNNKEKNI-KICAVKIPSFGSYRKSILQDISIATGASFYSSDSGMKLKNLKPEDFGSLRK 322
Cdd:TIGR02348 242 GKPLLIIAEDVEGEAL-ATLVVNKLRGTlNVCAVKAPGFGDRRKAMLEDIAILTGGQVISEELGLKLEEVTLDDLGKAKK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 323 CIVSENNCTLISKNRFKNQIKSRIDYLEKLLSSTDSTFETNLLSERIAKLSGGIAVIRVGAPTELELIDKKLRLEDAKNA 402
Cdd:TIGR02348 321 VTVDKDNTTIVEGAGDKAAIKARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATETEMKEKKLRIEDALNA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 403 TFSAVTQGVVTGSAVSLVHLSNFLKYFMALSScmEESLGMQLLRKSIVVPNRNIILNSDEDGYLMEKKIVNYPFEIGYDA 482
Cdd:TIGR02348 401 TRAAVEEGIVPGGGVALLRAAAALEGLKGDGE--DEAIGIDIVKRALEAPLRQIAENAGLDGAVVAEKVKELKGNFGFNA 478
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 75756309 483 EYKCLTNLVGEGVVDPSLLLYNSLISLCKISSVLMHTQAVISKR 526
Cdd:TIGR02348 479 ATGEYEDLVEAGIIDPTKVTRSALQNAASIAGLLLTTEAVVADK 522
|
|
| groEL |
CHL00093 |
chaperonin GroEL |
4-523 |
1.69e-128 |
|
chaperonin GroEL
Pssm-ID: 177025 Cd Length: 529 Bit Score: 385.61 E-value: 1.69e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 4 KNICYRDVIIKQIKKGLQDTTNILSLTLGPRGKNIVLWDKTSKPQIINDGTSIINKINNQNFVEHIGQFLVKDVIFNVND 83
Cdd:CHL00093 3 KKILYQDNARRALERGMDILAEAVSVTLGPKGRNVVLEKKYGSPQIVNDGVTIAKEIELEDHIENTGVALIRQAASKTND 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 84 SVGDGTSTTGILTGNVLSRGLSLIHSGYTPYFFSNGIFKCTNILLNKLYKISWPLNNNKDILNIATNSSGGDKLLGKLIV 163
Cdd:CHL00093 83 VAGDGTTTATVLAYAIVKQGMKNVAAGANPISLKRGIEKATQYVVSQIAEYARPVEDIQAITQVASISAGNDEEVGSMIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 164 NAYKRVGTDGLISIETSDKNDTSLIVYGGLQIDRGYVSHKFINNFKNSTCEYNDSAILVTDLPIDSIKQA-AAIMQSILQ 242
Cdd:CHL00093 163 DAIEKVGREGVISLEEGKSTVTELEITEGMRFEKGFISPYFVTDTERMEVVQENPYILLTDKKITLVQQDlLPILEQVTK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 243 IDKPLLIISDTISKKCLNAFLVNNKEKNIKICAVKIPSFGSYRKSILQDISIATGASFYSSDSGMKLKNLKPEDFGSLRK 322
Cdd:CHL00093 243 TKRPLLIIAEDVEKEALATLVLNKLRGIVNVVAVRAPGFGDRRKAMLEDIAILTGGQVITEDAGLSLETIQLDLLGQARR 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 323 CIVSENNCTLISKNRfKNQIKSRIDYLEKLLSSTDSTFETNLLSERIAKLSGGIAVIRVGAPTELELIDKKLRLEDAKNA 402
Cdd:CHL00093 323 IIVTKDSTTIIADGN-EEQVKARCEQLRKQIEIADSSYEKEKLQERLAKLSGGVAVIKVGAATETEMKDKKLRLEDAINA 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 403 TFSAVTQGVVTGSAVSLVHLSNFLKYFMALSSCMEESLGMQLLRKSIVVPNRNIILNSDEDGYLMEKKIVNYPFEIGYDA 482
Cdd:CHL00093 402 TKAAVEEGIVPGGGATLVHLSENLKTWAKNNLKEDELIGALIVARAILAPLKRIAENAGKNGSVIIEKVQEQDFEIGYNA 481
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 75756309 483 EYKCLTNLVGEGVVDPSLLLYNSLISLCKISSVLMHTQAVI 523
Cdd:CHL00093 482 ANNKFVNMYEAGIIDPAKVTRSALQNAASIASMILTTECII 522
|
|
| PTZ00114 |
PTZ00114 |
Heat shock protein 60; Provisional |
14-523 |
3.09e-127 |
|
Heat shock protein 60; Provisional
Pssm-ID: 185455 Cd Length: 555 Bit Score: 383.49 E-value: 3.09e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 14 KQIKKGLQDTTNILSLTLGPRGKNIVLWDKTSKPQIINDGTSIINKINNQNFVEHIGQFLVKDVIFNVNDSVGDGTSTTG 93
Cdd:PTZ00114 25 QSLLKGIERLADAVAVTLGPKGRNVIIEQEYGSPKITKDGVTVAKAIEFSDRFENVGAQLIRQVASKTNDKAGDGTTTAT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 94 ILTGNVLSRGLSLIHSGYTPYFFSNGIFKCTNILLNKLYKISWPLNNNKDILNIATNSSGGDKLLGKLIVNAYKRVGTDG 173
Cdd:PTZ00114 105 ILARAIFREGCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQSRPVKTKEDILNVATISANGDVEIGSLIADAMDKVGKDG 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 174 LISIETSDKNDTSLIVYGGLQIDRGYVSHKFINNFKNSTCEYNDSAILVTDLPIDSIKQAAAIMQSILQIDKPLLIISDT 253
Cdd:PTZ00114 185 TITVEDGKTLEDELEVVEGMSFDRGYISPYFVTNEKTQKVELENPLILVTDKKISSIQSILPILEHAVKNKRPLLIIAED 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 254 ISKKCLNAFLVNNKEKNIKICAVKIPSFGSYRKSILQDISIATGASFYSSDS-GMKLKNLKPEDFGSLRKCIVSENNCTL 332
Cdd:PTZ00114 265 VEGEALQTLIINKLRGGLKVCAVKAPGFGDNRKDILQDIAVLTGATVVSEDNvGLKLDDFDPSMLGSAKKVTVTKDETVI 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 333 ISKNRFKNQIKSRIDYLEKLLSSTDSTFETNLLSERIAKLSGGIAVIRVGAPTELELIDKKLRLEDAKNATFSAVTQGVV 412
Cdd:PTZ00114 345 LTGGGDKAEIKERVELLRSQIERTTSEYDKEKLKERLAKLSGGVAVIKVGGASEVEVNEKKDRIEDALNATRAAVEEGIV 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 413 TGSAVSLVHLSNFLKYFMALSSC-MEESLGMQLLRKSIVVPNRNIILNSDEDGYLMEKKIVNY-PFEIGYDAEYKCLTNL 490
Cdd:PTZ00114 425 PGGGVALLRASKLLDKLEEDNELtPDQRTGVKIVRNALRLPTKQIAENAGVEGAVVVEKILEKkDPSFGYDAQTGEYVNM 504
|
490 500 510
....*....|....*....|....*....|...
gi 75756309 491 VGEGVVDPSLLLYNSLISLCKISSVLMHTQAVI 523
Cdd:PTZ00114 505 FEAGIIDPTKVVRSALVDAASVASLMLTTEAAI 537
|
|
| groEL |
PRK12849 |
chaperonin GroEL; Reviewed |
16-526 |
1.38e-123 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237230 Cd Length: 542 Bit Score: 373.37 E-value: 1.38e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 16 IKKGLQDTTNILSLTLGPRGKNIVLWDKTSKPQIINDGTSIINKINNQNFVEHIGQFLVKDVIFNVNDSVGDGTSTTGIL 95
Cdd:PRK12849 15 LERGVNKLADAVKVTLGPKGRNVVIDKSFGAPTITKDGVSIAKEIELEDPFENLGAQLVKEVASKTNDVAGDGTTTATVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 96 TGNVLSRGLSLIHSGYTPYFFSNGIFKCTNILLNKLYKISWPLNNNKDILNIATNSSGGDKLLGKLIVNAYKRVGTDGLI 175
Cdd:PRK12849 95 AQALVQEGLKNVAAGANPMDLKRGIDKAVEAVVEELKALARPVSGSEEIAQVATISANGDEEIGELIAEAMEKVGKDGVI 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 176 SIETSDKNDTSLIVYGGLQIDRGYVSHKFINNFKNSTCEYNDSAILVTDLPIDSIKQAAAIMQSILQIDKPLLIISDTIS 255
Cdd:PRK12849 175 TVEESKTLETELEVTEGMQFDRGYLSPYFVTDPERMEAVLEDPLILLTDKKISSLQDLLPLLEKVAQSGKPLLIIAEDVE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 256 KKCLNAFLVNNKEKNIKICAVKIPSFGSYRKSILQDISIATGASFYSSDSGMKLKNLKPEDFGSLRKCIVSENNCTLISK 335
Cdd:PRK12849 255 GEALATLVVNKLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGLKLEEVTLDDLGRAKRVTITKDNTTIVDG 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 336 NRFKNQIKSRIDYLEKLLSSTDSTFETNLLSERIAKLSGGIAVIRVGAPTELELIDKKLRLEDAKNATFSAVTQGVVTGS 415
Cdd:PRK12849 335 AGDKEAIEARVAQIRRQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATEVELKERKDRVEDALNATRAAVEEGIVPGG 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 416 AVSLVHLSNFLKYFMALSScmEESLGMQLLRKSIVVPNRNIILNSDEDGYLMEKKIVNYPFEIGYDA---EYkclTNLVG 492
Cdd:PRK12849 415 GVALLRAAKALDELAGLNG--DQAAGVEIVRRALEAPLRQIAENAGLDGSVVVAKVLELEDGFGFNAatgEY---GDLIA 489
|
490 500 510
....*....|....*....|....*....|....
gi 75756309 493 EGVVDPSLLLYNSLISLCKISSVLMHTQAVISKR 526
Cdd:PRK12849 490 AGIIDPVKVTRSALQNAASVAGLLLTTEALVADK 523
|
|
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
14-523 |
1.82e-119 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 362.90 E-value: 1.82e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 14 KQIK------KGLQDTTNILS----LTLGPRGKNIVLWDKTSKPQIINDGTSIINKINNQNFVEHIGQFLVKDVIFNVND 83
Cdd:PRK00013 3 KDIKfgedarRKLLRGVNKLAdavkVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDPFENMGAQLVKEVASKTND 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 84 SVGDGTSTTGILTGNVLSRGLSLIHSGYTPYFFSNGIFKCTNILLNKLYKISWPLNNNKDILNIATNSSGGDKLLGKLIV 163
Cdd:PRK00013 83 VAGDGTTTATVLAQAIVREGLKNVAAGANPMDLKRGIDKAVEAAVEELKKISKPVEDKEEIAQVATISANGDEEIGKLIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 164 NAYKRVGTDGLISIETSDKNDTSLIVYGGLQIDRGYVSHKFINNFKNSTCEYNDSAILVTDLPIDSIKQAAAIMQSILQI 243
Cdd:PRK00013 163 EAMEKVGKEGVITVEESKGFETELEVVEGMQFDRGYLSPYFVTDPEKMEAELENPYILITDKKISNIQDLLPVLEQVAQS 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 244 DKPLLIISDTISKKCLNAFLVNNKEKNIKICAVKIPSFGSYRKSILQDISIATGASFYSSDSGMKLKNLKPEDFGSLRKC 323
Cdd:PRK00013 243 GKPLLIIAEDVEGEALATLVVNKLRGTLKVVAVKAPGFGDRRKAMLEDIAILTGGTVISEELGLKLEDATLEDLGQAKKV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 324 IVSENNCTLISKNRFKNQIKSRIDYLEKLLSSTDSTFETNLLSERIAKLSGGIAVIRVGAPTELELIDKKLRLEDAKNAT 403
Cdd:PRK00013 323 VVTKDNTTIVDGAGDKEAIKARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATEVEMKEKKDRVEDALHAT 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 404 FSAVTQGVVTGSAVSLVHLSNFLKYFMALSScmEESLGMQLLRKSIVVPNRNIILNSDEDGYLMEKKIVNY-PFEIGYDA 482
Cdd:PRK00013 403 RAAVEEGIVPGGGVALLRAAPALEALKGLNG--DEATGINIVLRALEAPLRQIAENAGLEGSVVVEKVKNGkGKGYGYNA 480
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 75756309 483 EYKCLTNLVGEGVVDPSLLLYNSLISLCKISSVLMHTQAVI 523
Cdd:PRK00013 481 ATGEYVDMIEAGIIDPTKVTRSALQNAASVAGLLLTTEAVV 521
|
|
| groEL |
PRK12850 |
chaperonin GroEL; Reviewed |
1-523 |
6.17e-116 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237231 Cd Length: 544 Bit Score: 354.02 E-value: 6.17e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 1 MKIKNICYRDVIIKQIKKGLQDTTNILSLTLGPRGKNIVLWDKTSKPQIINDGTSIINKINNQNFVEHIGQFLVKDVIFN 80
Cdd:PRK12850 1 MAAKEIRFSTDARDRLLRGVNILANAVKVTLGPKGRNVVLEKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVKEVASK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 81 VNDSVGDGTSTTGILTGNVLSRGLSLIHSGYTPYFFSNGIFKCTNILLNKLYKISWPLNNNKDILNIATNSSGGDKLLGK 160
Cdd:PRK12850 81 TNDLAGDGTTTATVLAQAIVREGAKLVAAGMNPMDLKRGIDLAVAAVVDELKKIAKKVTSSKEIAQVATISANGDESIGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 161 LIVNAYKRVGTDGLISIETSDKNDTSLIVYGGLQIDRGYVSHKFINNFKNSTCEYNDSAILVTDLPIDSIKQAAAIMQSI 240
Cdd:PRK12850 161 MIAEAMDKVGKEGVITVEEAKTLGTELDVVEGMQFDRGYLSPYFVTNPEKMRAELEDPYILLHEKKISNLQDLLPILEAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 241 LQIDKPLLIISDTISKKCLNAFLVNNKEKNIKICAVKIPSFGSYRKSILQDISIATGASFYSSDSGMKLKNLKPEDFGSL 320
Cdd:PRK12850 241 VQSGRPLLIIAEDVEGEALATLVVNKLRGGLKSVAVKAPGFGDRRKAMLEDIAVLTGGQVISEDLGIKLENVTLDMLGRA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 321 RKCIVSENNCTLISKNRFKNQIKSRIDYLEKLLSSTDSTFETNLLSERIAKLSGGIAVIRVGAPTELELIDKKLRLEDAK 400
Cdd:PRK12850 321 KRVLITKENTTIIDGAGDKKNIEARVKQIRAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKEKKDRVDDAL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 401 NATFSAVTQGVVTGSAVSLVHLSNFLKYFMALSScmEESLGMQLLRKSIVVPNRNIILNSDEDGYLMEKKIVNYPFEIGY 480
Cdd:PRK12850 401 HATRAAVEEGIVPGGGVALLRARSALRGLKGANA--DETAGIDIVRRALEEPLRQIATNAGFEGSVVVGKVAELPGNFGF 478
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 75756309 481 DAEYKCLTNLVGEGVVDPSLLLYNSLISLCKISSVLMHTQAVI 523
Cdd:PRK12850 479 NAQTGEYGDMVEAGIIDPAKVTRTALQDAASIAALLITTEAMV 521
|
|
| groEL |
PRK12851 |
chaperonin GroEL; Reviewed |
1-524 |
8.55e-116 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 171770 Cd Length: 541 Bit Score: 353.66 E-value: 8.55e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 1 MKIKNICYRDVIIKQIKKGLQDTTNILSLTLGPRGKNIVLWDKTSKPQIINDGTSIINKINNQNFVEHIGQFLVKDVIFN 80
Cdd:PRK12851 1 MAAKEVKFHVEAREKMLRGVNILADAVKVTLGPKGRNVVIDKSFGAPTITNDGVTIAKEIELEDKFENMGAQMVREVASK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 81 VNDSVGDGTSTTGILTGNVLSRGLSLIHSGYTPYFFSNGIFKCTNILLNKLYKISWPLNNNKDILNIATNSSGGDKLLGK 160
Cdd:PRK12851 81 TNDVAGDGTTTATVLAQAIVREGAKAVAAGANPMDLKRGIDRAVAAVVEELKANARPVTTNAEIAQVATISANGDAEIGR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 161 LIVNAYKRVGTDGLISIETSDKNDTSLIVYGGLQIDRGYVSHKFINNFKNSTCEYNDSAILVTDLPIDSIKQAAAIMQSI 240
Cdd:PRK12851 161 LVAEAMEKVGNEGVITVEESKTAETELEVVEGMQFDRGYLSPYFVTDADKMEAELEDPYILIHEKKISNLQDLLPVLEAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 241 LQIDKPLLIISDTISKKCLNAFLVNNKEKNIKICAVKIPSFGSYRKSILQDISIATGASFYSSDSGMKLKNLKPEDFGSL 320
Cdd:PRK12851 241 VQSGKPLLIIAEDVEGEALATLVVNKLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGIKLENVTLEQLGRA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 321 RKCIVSENNCTLISKNRFKNQIKSRIDYLEKLLSSTDSTFETNLLSERIAKLSGGIAVIRVGAPTELELIDKKLRLEDAK 400
Cdd:PRK12851 321 KKVVVEKENTTIIDGAGSKTEIEGRVAQIRAQIEETTSDYDREKLQERLAKLAGGVAVIRVGASTEVEVKEKKDRVDDAL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 401 NATFSAVTQGVVTGSAVSLVHLSNFLKYFMALSScmEESLGMQLLRKSIVVPNRNIILNSDEDGYLMEKKIVNYPFEIGY 480
Cdd:PRK12851 401 HATRAAVEEGIVPGGGVALLRAVKALDKLETANG--DQRTGVEIVRRALEAPVRQIAENAGAEGSVVVGKLREKPGGYGF 478
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 75756309 481 DAEYKCLTNLVGEGVVDPSLLLYNSLISLCKISSVLMHTQAVIS 524
Cdd:PRK12851 479 NAATNEYGDLYAQGVIDPVKVVRTALQNAASVAGLLLTTEAMVA 522
|
|
| PRK14104 |
PRK14104 |
chaperonin GroEL; Provisional |
18-525 |
2.36e-104 |
|
chaperonin GroEL; Provisional
Pssm-ID: 172594 Cd Length: 546 Bit Score: 324.29 E-value: 2.36e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 18 KGLQDTTNILSLTLGPRGKNIVLWDKTSKPQIINDGTSIINKINNQNFVEHIGQFLVKDVIFNVNDSVGDGTSTTGILTG 97
Cdd:PRK14104 18 RGVDILANAVKVTLGPKGRNVVLDKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVREVASKSADAAGDGTTTATVLAQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 98 NVLSRGLSLIHSGYTPYFFSNGIFKCTNILLNKLYKISWPLNNNKDILNIATNSSGGDKLLGKLIVNAYKRVGTDGLISI 177
Cdd:PRK14104 98 AIVREGAKSVAAGMNPMDLKRGIDLAVEAVVADLVKNSKKVTSNDEIAQVGTISANGDAEIGKFLADAMKKVGNEGVITV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 178 ETSDKNDTSLIVYGGLQIDRGYVSHKFINNFKNSTCEYNDSAILVTDLPIDSIKQAAAIMQSILQIDKPLLIISDTISKK 257
Cdd:PRK14104 178 EEAKSLETELDVVEGMQFDRGYISPYFVTNADKMRVEMDDAYILINEKKLSSLNELLPLLEAVVQTGKPLVIVAEDVEGE 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 258 CLNAFLVNNKEKNIKICAVKIPSFGSYRKSILQDISIATGASFYSSDSGMKLKNLKPEDFGSLRKCIVSENNCTLISKNR 337
Cdd:PRK14104 258 ALATLVVNRLRGGLKVAAVKAPGFGDRRKAMLQDIAILTGGQAISEDLGIKLENVTLQMLGRAKKVMIDKENTTIVNGAG 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 338 FKNQIKSRIDYLEKLLSSTDSTFETNLLSERIAKLSGGIAVIRVGAPTELELIDKKLRLEDAKNATFSAVTQGVVTGSAV 417
Cdd:PRK14104 338 KKADIEARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKERKDRVDDAMHATRAAVEEGIVPGGGV 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 418 SLVHLSNFLKYFMALSScmEESLGMQLLRKSIVVPNRNIILNSDEDGYLMEKKIV-NYPFEIGYDAEYKCLTNLVGEGVV 496
Cdd:PRK14104 418 ALLRASEQLKGIKTKND--DQKTGVEIVRKALSAPARQIAINAGEDGSVIVGKILeKEQYSYGFDSQTGEYGNLVSKGII 495
|
490 500
....*....|....*....|....*....
gi 75756309 497 DPSLLLYNSLISLCKISSVLMHTQAVISK 525
Cdd:PRK14104 496 DPTKVVRTAIQNAASVAALLITTEAMVAE 524
|
|
| groEL |
PRK12852 |
chaperonin GroEL; Reviewed |
1-525 |
2.45e-102 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237232 Cd Length: 545 Bit Score: 319.10 E-value: 2.45e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 1 MKIKNICYRDVIIKQIKKGLQDTTNILSLTLGPRGKNIVLWDKTSKPQIINDGTSIINKINNQNFVEHIGQFLVKDVIFN 80
Cdd:PRK12852 1 MAAKDVKFSGDARDRMLRGVDILANAVKVTLGPKGRNVVIEKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVREVASK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 81 VNDSVGDGTSTTGILTGNVLSRGLSLIHSGYTPYFFSNGIFKCTNILLNKLYKISWPLNNNKDILNIATNSSGGDKLLGK 160
Cdd:PRK12852 81 TNDLAGDGTTTATVLAQAIVREGAKAVAAGMNPMDLKRGIDIAVAAVVKDIEKRAKPVASSAEIAQVGTISANGDAAIGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 161 LIVNAYKRVGTDGLISIETSDKNDTSLIVYGGLQIDRGYVSHKFINNFKNSTCEYNDSAILVTDLPIDSIKQAAAIMQSI 240
Cdd:PRK12852 161 MIAQAMQKVGNEGVITVEENKSLETEVDIVEGMKFDRGYLSPYFVTNAEKMTVELDDAYILLHEKKLSGLQAMLPVLEAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 241 LQIDKPLLIISDTISKKCLNAFLVNNKEKNIKICAVKIPSFGSYRKSILQDISIATGASFYSSDSGMKLKNLKPEDFGSL 320
Cdd:PRK12852 241 VQSGKPLLIIAEDVEGEALATLVVNRLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGQLISEDLGIKLENVTLKMLGRA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 321 RKCIVSENNCTLISKNRFKNQIKSRIDYLEKLLSSTDSTFETNLLSERIAKLSGGIAVIRVGAPTELELIDKKLRLEDAK 400
Cdd:PRK12852 321 KKVVIDKENTTIVNGAGKKADIEARVGQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKEKKDRVEDAL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 401 NATFSAVTQGVVTGSAVSLVHLSNFLKYFMALSScmEESLGMQLLRKSIVVPNRNIILNSDEDGYLMEKKIV-NYPFEIG 479
Cdd:PRK12852 401 NATRAAVQEGIVPGGGVALLRAKKAVGRINNDNA--DVQAGINIVLKALEAPIRQIAENAGVEGSIVVGKILeNKSETFG 478
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 75756309 480 YDAEYKCLTNLVGEGVVDPSLLLYNSLISLCKISSVLMHTQAVISK 525
Cdd:PRK12852 479 FDAQTEEYVDMVAKGIIDPAKVVRTALQDAASVAGLLVTTEAMVAE 524
|
|
| GroEL |
COG0459 |
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ... |
30-526 |
4.30e-101 |
|
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227 Cd Length: 497 Bit Score: 313.94 E-value: 4.30e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 30 TLGPRGKNIVLWDKTSKPQIINDGTSIINKINNQNFVEHIGQFLVKDVIFNVNDSVGDGTSTTGILTGNVLSRGLSLIHS 109
Cdd:COG0459 29 TLGPKGRNVMLVKSFGDPTITNDGVTIAKEIELEDPFENMGAQLVKEVASKTNDEAGDGTTTATVLAGALLKEGLKLVAA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 110 GYTPYFFSNGIFKCTNILLNKLYKISWPLNNNKDILNIATNSSGGDKLLGKLIVNAYKRVGTDGLISIETSDKNDTSLIV 189
Cdd:COG0459 109 GANPTDIKRGIDKAVEKAVEELKKIAKPVDDKEELAQVATISANGDEEIGELIAEAMEKVGKDGVITVEEGKGLETELEV 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 190 YGGLQIDRGYVSHKFINNFKNSTCEYNDSAILVTDLPIDSIKQAAAIMQSILQIDKPLLIISDTISKKCLNAFLVNNKEK 269
Cdd:COG0459 189 VEGMQFDKGYLSPYFVTDPEKMPAELENAYILLTDKKISSIQDLLPLLEKVAQSGKPLLIIAEDIDGEALATLVVNGIRG 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 270 NIKICAVKIPSFGSYRKSILQDISIATGASFYSSDSGMKLKNLKPEDFGSLRKCIVSENNCTLISKNRFKNQIksridyl 349
Cdd:COG0459 269 VLRVVAVKAPGFGDRRKAMLEDIAILTGGRVISEDLGLKLEDVTLDDLGRAKRVEVDKDNTTIVEGAGNPKAI------- 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 350 ekllsstdstfetnllseriaklsggiaVIRVGAPTELELIDKKLRLEDAKNATFSAVTQGVVTGSAVSLVHLSNFL-KY 428
Cdd:COG0459 342 ----------------------------VILVGAATEVEVKERKRRVEDALHATRAAVEEGIVPGGGAALLRAARALrEL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 429 FMALSScmEESLGMQLLRKSIVVPNRNIILNSDEDGY-----LMEKKIVNYpfeiGYDAEYKCLTNLVGEGVVDPSLLLY 503
Cdd:COG0459 394 AAKLEG--DEQLGIEIVARALEAPLRQIAENAGLDGSvvvekVRAAKDKGF----GFDAATGEYVDMLEAGVIDPAKVKR 467
|
490 500
....*....|....*....|...
gi 75756309 504 NSLISLCKISSVLMHTQAVISKR 526
Cdd:COG0459 468 SALQNAASVAGLILTTEAVIADK 490
|
|
| PLN03167 |
PLN03167 |
Chaperonin-60 beta subunit; Provisional |
13-499 |
2.81e-91 |
|
Chaperonin-60 beta subunit; Provisional
Pssm-ID: 215611 [Multi-domain] Cd Length: 600 Bit Score: 291.83 E-value: 2.81e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 13 IKQIKKGLQDTTNILSLTLGPRGKNIVLWDKTSKPQIINDGTSIINKINNQNFVEHIGQFLVKDVIFNVNDSVGDGTSTT 92
Cdd:PLN03167 68 IKKLQAGVNKLADLVGVTLGPKGRNVVLESKYGSPKIVNDGVTVAKEVELEDPVENIGAKLVRQAAAKTNDLAGDGTTTS 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 93 GILTGNVLSRGLSLIHSGYTPYFFSNGIFKCTNILLNKLYKISWPLNNNkDILNIATNSSGGDKLLGKLIVNAYKRVGTD 172
Cdd:PLN03167 148 VVLAQGLIAEGVKVVAAGANPVQITRGIEKTAKALVKELKKMSKEVEDS-ELADVAAVSAGNNYEVGNMIAEAMSKVGRK 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 173 GLISIETSDKNDTSLIVYGGLQIDRGYVSHKFINNFKNSTCEYNDSAILVTDLPIDSIKQAAAIMQSILQIDKPLLIISD 252
Cdd:PLN03167 227 GVVTLEEGKSAENNLYVVEGMQFDRGYISPYFVTDSEKMSVEYDNCKLLLVDKKITNARDLIGILEDAIRGGYPLLIIAE 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 253 TISKKCLNAFLVNNKEKNIKICAVKIPSFGSYRKSILQDISIATGASFYSSDSGMKLKNLKPEDFGSLRKCIVSENNCTL 332
Cdd:PLN03167 307 DIEQEALATLVVNKLRGSLKIAALKAPGFGERKSQYLDDIAILTGGTVIREEVGLSLDKVGKEVLGTAAKVVLTKDTTTI 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 333 ISKNRFKNQIKSRIDYLEKLLSSTDSTFETNLLSERIAKLSGGIAVIRVGAPTELELIDKKLRLEDAKNATFSAVTQGVV 412
Cdd:PLN03167 387 VGDGSTQEAVNKRVAQIKNLIEAAEQDYEKEKLNERIAKLSGGVAVIQVGAQTETELKEKKLRVEDALNATKAAVEEGIV 466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 413 TGSAVSLVHLSNFLKYFMALSSCMEESLGMQLLRKSIVVPNRNIILNSDEDGYLM-EKKIVNYPFEIGYDAEYKCLTNLV 491
Cdd:PLN03167 467 VGGGCTLLRLASKVDAIKDTLENDEQKVGADIVKRALSYPLKLIAKNAGVNGSVVsEKVLSNDNPKFGYNAATGKYEDLM 546
|
....*...
gi 75756309 492 GEGVVDPS 499
Cdd:PLN03167 547 AAGIIDPT 554
|
|
| chaperonin_type_I_II |
cd00309 |
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ... |
4-524 |
6.91e-83 |
|
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: 265.83 E-value: 6.91e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 4 KNICYRDVIIKQIKKGLQDTTNILSLTLGPRGKNIVLWDKTSKPQIINDGTSIINKINnqnfVEHIGQFLVKDVIFNVND 83
Cdd:cd00309 1 KEREFGEEARLSNINAAKALADAVKTTLGPKGMDKMLVDSLGDPTITNDGATILKEIE----VEHPAAKLLVEVAKSQDD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 84 SVGDGTSTTGILTGNVLSRGLSLIHSGYTPYFFSNGIFKCTNILLNKLYKISWP--LNNNKDILNIATNS------SGGD 155
Cdd:cd00309 77 EVGDGTTTVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVPidVEDREELLKVATTSlnsklvSGGD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 156 KLLGKLIVNAYKRVGT------DGLISIE---TSDKNDTSLIVygGLQIDRGYVSHKFinnfknsTCEYNDSAILVTDLP 226
Cdd:cd00309 157 DFLGELVVDAVLKVGKengdvdLGVIRVEkkkGGSLEDSELVV--GMVFDKGYLSPYM-------PKRLENAKILLLDCK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 227 IDsikqaaaimqsilqidkPLLIISDTISKKCLNAFLVNNkeknikICAVKIPsfgsyRKSILQDISIATGASFYSSdsg 306
Cdd:cd00309 228 LE-----------------YVVIAEKGIDDEALHYLAKLG------IMAVRRV-----RKEDLERIAKATGATIVSR--- 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 307 mkLKNLKPEDFGSLRKCIVSEnnctlisknrfknqiksridyleklLSSTDSTFETNllseriaKLSGGIAVIRVGAPTE 386
Cdd:cd00309 277 --LEDLTPEDLGTAGLVEETK-------------------------IGDEKYTFIEG-------CKGGKVATILLRGATE 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 387 LELIDKKLRLEDAKNATFSAVTQ-GVVTGSAVSLVHLSNFLKYFmALSSCMEESLGMQLLRKSIVVPNRNIILNSDEDGY 465
Cdd:cd00309 323 VELDEAERSLHDALCAVRAAVEDgGIVPGGGAAEIELSKALEEL-AKTLPGKEQLGIEAFADALEVIPRTLAENAGLDPI 401
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 75756309 466 LMEKKIVNYPFEIGYDAEYKCLT----NLVGEGVVDPSLLLYNSLISLCKISSVLMHTQAVIS 524
Cdd:cd00309 402 EVVTKLRAKHAEGGGNAGGDVETgeivDMKEAGIIDPLKVKRQALKSATEAASLILTIDDIIV 464
|
|
| Cpn60_TCP1 |
pfam00118 |
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ... |
24-524 |
7.43e-39 |
|
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: 148.50 E-value: 7.43e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 24 TNILSLTLGPRGKNIVLWDKTSKPQIINDGTSIINKINnqnfVEH-IGQFLVkDVIFNVNDSVGDGTSTTGILTGNVLSR 102
Cdd:pfam00118 2 ADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELE----IQHpAAKLLV-EAAKAQDEEVGDGTTTVVVLAGELLEE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 103 GLSLIHSGYTPYFFSNGIFKCTNILLNKLYKI-SWPLNNN--KDILNIATNSSGGD------KLLGKLIVNAYKR----- 168
Cdd:pfam00118 77 AEKLLAAGVHPTTIIEGYEKALEKALEILDSIiSIPVEDVdrEDLLKVARTSLSSKiisresDFLAKLVVDAVLAipknd 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 169 ----VGTDGLISIETSDKNDTSLIvyGGLQIDRGYVSHKFINNFKNstceyndSAILVTDLPIDSIK------------- 231
Cdd:pfam00118 157 gsfdLGNIGVVKILGGSLEDSELV--DGVVLDKGPLHPDMPKRLEN-------AKVLLLNCSLEYEKtetkatvvlsdae 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 232 -----------QAAAIMQSILQIDKPLLIISDTISKKCLnAFLVNNkekniKICAVKIPSfgsyrKSILQDISIATGASF 300
Cdd:pfam00118 228 qlerflkaeeeQILEIVEKIIDSGVNVVVCQKGIDDLAL-HFLAKN-----GIMALRRVK-----KRDLERLAKATGARA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 301 YSSdsgmkLKNLKPEDFGSLRKC---IVSENNCTLISknrfknqiksridylekllsstdstfetnllseriAKLSGGIA 377
Cdd:pfam00118 297 VSS-----LDDLTPDDLGTAGKVeeeKIGDEKYTFIE-----------------------------------GCKSPKAA 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 378 VIRVGAPTELELIDKKLRLEDAKNATFSAVT-QGVVTGSAVSLVHLSNFLKYFMALSSCmEESLGMQLLRKSIVVPNRNI 456
Cdd:pfam00118 337 TILLRGATDHVLDEIERSIHDALCVVKNAIEdPRVVPGGGAVEMELARALREYAKSVSG-KEQLAIEAFAEALEVIPKTL 415
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 75756309 457 ILNSDEDG----YLMEKKIVNYPFEIGYDAEYKCLTNLVGEGVVDPSLLLYNSLISLCKISSVLMHTQAVIS 524
Cdd:pfam00118 416 AENAGLDPievlAELRAAHASGEKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKSATEAASTILRIDDIIK 487
|
|
| cpn60 |
cd03343 |
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ... |
25-318 |
2.29e-10 |
|
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: 63.05 E-value: 2.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 25 NILSLTLGPRGKNIVLWDKTSKPQIINDGTSIINKINnqnfVEHIGQFLVKDVIFNVNDSVGDGTSTTGILTGNVLSRGL 104
Cdd:cd03343 29 EAVRTTLGPKGMDKMLVDSLGDVTITNDGATILKEMD----IEHPAAKMLVEVAKTQDEEVGDGTTTAVVLAGELLEKAE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 105 SLIHSGYTPYFFSNGIFKCTNILLNKLYKISWPLN-NNKDIL-NIATNSSGGD------KLLGKLIVNAYKRVGTDG--- 173
Cdd:cd03343 105 DLLDQNIHPTVIIEGYRLAAEKALELLDEIAIKVDpDDKDTLrKIAKTSLTGKgaeaakDKLADLVVDAVLQVAEKRdgk 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 174 ------LISIETSDK---NDTSLIvyGGLQIDRGYVSHKFINNFKNSTCEYNDSAILVTDLPID---SIKQAAAIMQSIL 241
Cdd:cd03343 185 yvvdldNIKIEKKTGgsvDDTELI--RGIVIDKEVVHPGMPKRVENAKIALLDAPLEVKKTEIDakiRITSPDQLQAFLE 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 242 QIDKPLLIISDTISKKCLNAFLVnnkEKNI-----------KICAVKipsfgSYRKSILQDISIATGASFYSSdsgmkLK 310
Cdd:cd03343 263 QEEAMLKEMVDKIADTGANVVFC---QKGIddlaqhylakaGILAVR-----RVKKSDMEKLARATGAKIVTN-----ID 329
|
....*...
gi 75756309 311 NLKPEDFG 318
Cdd:cd03343 330 DLTPEDLG 337
|
|
| thermosome_arch |
TIGR02339 |
thermosome, various subunits, archaeal; Thermosome is the name given to the archaeal rather ... |
25-318 |
2.62e-10 |
|
thermosome, various subunits, archaeal; Thermosome is the name given to the archaeal rather than eukaryotic form of the group II chaperonin (counterpart to the group I chaperonin, GroEL/GroES, in bacterial), a torroidal, ATP-dependent molecular chaperone that assists in the folding or refolding of nascent or denatured proteins. Various homologous subunits, one to five per archaeal genome, may be designated alpha, beta, etc., but phylogenetic analysis does not show distinct alpha subunit and beta subunit lineages traceable to ancient paralogs. [Protein fate, Protein folding and stabilization]
Pssm-ID: 274080 Cd Length: 519 Bit Score: 62.78 E-value: 2.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 25 NILSLTLGPRGKNIVLWDKTSKPQIINDGTSIINKINnqnfVEHIGQFLVKDVIFNVNDSVGDGTSTTGILTGNVLSRGL 104
Cdd:TIGR02339 30 EAVKSTLGPRGMDKMLVDSLGDVTITNDGATILKEMD----IEHPAAKMLVEVAKTQDEEVGDGTTTAVVLAGELLEKAE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 105 SLIHSGYTPYFFSNGIFKCTNILLNKLYKISWPLN-NNKDIL-NIATNSSGGD-------KLLGKLIVNAYKRVG---TD 172
Cdd:TIGR02339 106 DLLEQDIHPTVIIEGYRKAAEKALEIIDEIATKISpEDRDLLkKIAYTSLTSKasaevakDKLADLVVEAVKQVAelrGD 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 173 G-------LISIET---SDKNDTSLIvyGGLQIDRGYVSHKFINNFKNSTceyndsaILVTDLPID----------SIKQ 232
Cdd:TIGR02339 186 GkyyvdldNIKIVKkkgGSIEDTELV--EGIVVDKEVVHPGMPKRVENAK-------IALLDAPLEvekteidakiRITD 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 233 AAAIMQSILQIDKPLLIISDTISKKCLNAFLVnnkEKNIK-----------ICAVKipsfgSYRKSILQDISIATGASFY 301
Cdd:TIGR02339 257 PDQIKKFLDQEEAMLKEMVDKIASAGANVVIC---QKGIDdvaqhylakagILAVR-----RVKKSDIEKLARATGARIV 328
|
330
....*....|....*..
gi 75756309 302 SSdsgmkLKNLKPEDFG 318
Cdd:TIGR02339 329 SS-----IDEITESDLG 340
|
|
| chap_CCT_eta |
TIGR02345 |
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ... |
26-143 |
3.20e-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: 62.47 E-value: 3.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 26 ILSLTLGPRGKNIVLWDKTSKPQIINDGTSIINKInnqNFVEHIGQFLVkDVIFNVNDSVGDGTSTTGILTGNVLSRGLS 105
Cdd:TIGR02345 33 ALKTTLGPRGMDKLIVGSNGKATISNDGATILKLL---DIVHPAAKTLV-DIAKSQDAEVGDGTTSVTILAGELLKEAKP 108
|
90 100 110
....*....|....*....|....*....|....*...
gi 75756309 106 LIHSGYTPYFFSNGIFKCTNILLNKLYKISWPLNNNKD 143
Cdd:TIGR02345 109 FIEEGVHPQLIIRCYREALSLAVEKIKEIAVTIDEEKG 146
|
|
| TCP1_epsilon |
cd03339 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ... |
25-184 |
4.18e-10 |
|
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: 62.32 E-value: 4.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 25 NILSLTLGPRGKNIVLWDKTSKPQIINDGTSIINKINNQNfveHIGQFLVkDVIFNVNDSVGDGTSTTGILTGNVLSRGL 104
Cdd:cd03339 37 NILRTSLGPRGMDKILVSPDGEVTVTNDGATILEKMDVDH---QIAKLLV-ELSKSQDDEIGDGTTGVVVLAGALLEQAE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 105 SLIHSGYTPYFFSNGIFKCTNILLNKLYKISWPLN---NNKDILNIATNSSggdklLGKLIVNAYKR----VGTDGLISI 177
Cdd:cd03339 113 KLLDRGIHPIRIADGYEQACKIAVEHLEEIADKIEfspDNKEPLIQTAMTS-----LGSKIVSRCHRqfaeIAVDAVLSV 187
|
....*..
gi 75756309 178 ETSDKND 184
Cdd:cd03339 188 ADLERKD 194
|
|
| thermosome_alpha |
NF041082 |
thermosome subunit alpha; |
30-319 |
4.94e-09 |
|
thermosome subunit alpha;
Pssm-ID: 469009 Cd Length: 518 Bit Score: 58.74 E-value: 4.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 30 TLGPRGKNIVLWDKTSKPQIINDGTSIINKINnqnfVEHIGQFLVKDVIFNVNDSVGDGTSTTGILTGNVLSRGLSLIHS 109
Cdd:NF041082 36 TLGPKGMDKMLVDSLGDVVITNDGVTILKEMD----IEHPAAKMIVEVAKTQDDEVGDGTTTAVVLAGELLKKAEELLDQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 110 GYTPYFFSNGIFKCTNILLNKLYKISWPLN-NNKDIL-NIATNS------SGGDKLLGKLIVNAYKRVG-TDGLISIETS 180
Cdd:NF041082 112 DIHPTIIAEGYRLAAEKALEILDEIAIKVDpDDKETLkKIAATAmtgkgaEAAKDKLADLVVDAVKAVAeKDGGYNVDLD 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 181 D----K------NDTSLIvyGGLQIDRGYVsH----KFINNFKnstceyndsaILVTDLPID----------SIKQAAAI 236
Cdd:NF041082 192 NikveKkvggsiEDSELV--EGVVIDKERV-HpgmpKRVENAK----------IALLDAPLEvkkteidakiSITDPDQL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 237 MQSILQIDKPLLIISDTISKKCLNAFLVnnkEKNI-----------KICAVKipsfgSYRKSILQDISIATGASFYSSds 305
Cdd:NF041082 259 QAFLDQEEKMLKEMVDKIADSGANVVFC---QKGIddlaqhylakeGILAVR-----RVKKSDMEKLAKATGARIVTS-- 328
|
330
....*....|....
gi 75756309 306 gmkLKNLKPEDFGS 319
Cdd:NF041082 329 ---IDDLSPEDLGY 339
|
|
| chap_CCT_epsi |
TIGR02343 |
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ... |
25-187 |
9.50e-09 |
|
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: 57.89 E-value: 9.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 25 NILSLTLGPRGKNIVLWDKTSKPQIINDGTSIINKINNQNfveHIGQFLVKdVIFNVNDSVGDGTSTTGILTGNVLSRGL 104
Cdd:TIGR02343 41 SILRTSLGPKGMDKMLISPDGDITVTNDGATILSQMDVDN---QIAKLMVE-LSKSQDDEIGDGTTGVVVLAGALLEQAE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 105 SLIHSGYTPYFFSNGIFKCTNILLNKLYKISWPL---NNNKDILNIATNSSggdklLGKLIVNAYKR----VGTDGLISI 177
Cdd:TIGR02343 117 ELLDKGIHPIKIADGFEEAARIAVEHLEEISDEIsadNNNREPLIQAAKTS-----LGSKIVSKCHRrfaeIAVDAVLNV 191
|
170
....*....|
gi 75756309 178 ETSDKNDTSL 187
Cdd:TIGR02343 192 ADMERRDVDF 201
|
|
| TCP1_eta |
cd03340 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ... |
21-142 |
4.39e-08 |
|
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: 55.76 E-value: 4.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 21 QDTTNILSLTLGPRGKNIVLWDKTSKPQIINDGTSIINKInnqNFVEHIGQFLVkDVIFNVNDSVGDGTSTTGILTGNVL 100
Cdd:cd03340 26 QAIADAVRTTLGPRGMDKLIVDGRGKVTISNDGATILKLL---DIVHPAAKTLV-DIAKSQDAEVGDGTTSVVVLAGEFL 101
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 75756309 101 SRGLSLIHSGYTPYFFSNGIFKCTNILLNKLYKISWPLNNNK 142
Cdd:cd03340 102 KEAKPFIEDGVHPQIIIRGYRKALQLAIEKIKEIAVNIDKED 143
|
|
| chap_CCT_zeta |
TIGR02347 |
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ... |
18-198 |
2.25e-06 |
|
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: 50.50 E-value: 2.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 18 KGLQDttnILSLTLGPRGKNIVLWDKTSKPQIINDGTSIINKINnqnfVEHIGQFLVKDVIFNVNDSVGDGTSTTGILTG 97
Cdd:TIGR02347 26 RGLQD---VLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEMQ----IQHPTASMIARAATAQDDITGDGTTSTVLLIG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 98 NVLSRGLSLIHSGYTPYFFSNGIFKCTNILLNKL--YKISWPLNNNKDILNIATNSSGGDKL-------LGKLIVNAYKR 168
Cdd:TIGR02347 99 ELLKQAERYILEGVHPRIITEGFEIARKEALQFLdkFKVKKEDEVDREFLLNVARTSLRTKLpadladqLTEIVVDAVLA 178
|
170 180 190
....*....|....*....|....*....|....*....
gi 75756309 169 VGTDG----LISIETSD-----KNDTSLIvyGGLQIDRG 198
Cdd:TIGR02347 179 IKKDGedidLFMVEIMEmkhksATDTTLI--RGLVLDHG 215
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
25-173 |
5.24e-06 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 49.26 E-value: 5.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 25 NILSLTLGPRGKNIVL-----WDKTSKPQIINDGTSIINKINNQNFVEHIgqfLVkDVIFNVNDSVGDGTSTTGILTGNV 99
Cdd:PTZ00212 36 DLVKTTLGPKGMDKILqpmseGPRSGNVTVTNDGATILKSVWLDNPAAKI---LV-DISKTQDEEVGDGTTSVVVLAGEL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 100 LSRGLSLIHSGYTPYFFSNGIFKCTNILLNKLYKISWPLNNNK-----DILNIA--TNSSggdKLL-------GKLIVNA 165
Cdd:PTZ00212 112 LREAEKLLDQKIHPQTIIEGWRMALDVARKALEEIAFDHGSDEekfkeDLLNIArtTLSS---KLLtvekdhfAKLAVDA 188
|
....*...
gi 75756309 166 YKRVGTDG 173
Cdd:PTZ00212 189 VLRLKGSG 196
|
|
| chap_CCT_gamma |
TIGR02344 |
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ... |
25-160 |
5.04e-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: 45.88 E-value: 5.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 25 NILSLTLGPRGKNIVLWDKTSKPQIINDGTSIINKINnqnfVEHIGQFLVKDVIFNVNDSVGDGTSTTGILTGNVLSRGL 104
Cdd:TIGR02344 30 DIIRTCLGPRSMLKMLLDPMGGIVMTNDGNAILREID----VAHPAAKSMIELSRTQDEEVGDGTTSVIILAGEMLSVAE 105
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 75756309 105 SLIHSGYTPYFFSNGIFKCTNILLNKLYKISWPLN-NNKDILNIATNSSGGDKLLGK 160
Cdd:TIGR02344 106 PFLEQNIHPTVIIRAYRKALDDALSVLEEISIPVDvNDDAAMLKLIQSCIGTKFVSR 162
|
|
| chap_CCT_delta |
TIGR02342 |
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ... |
30-169 |
1.70e-04 |
|
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: 44.39 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 30 TLGPRGKNIVLWDKTSKPQIINDGTSIINKINnqnfVEHIGQFLVKDVIFNVNDSVGDGTSTTGILTGNVLSRGLSLIHS 109
Cdd:TIGR02342 28 SLGPKGMDKMIQDGKGEVIITNDGATILKQMA----VLHPAAKMLVELSKAQDIEAGDGTTSVVILAGALLGACERLLNK 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 75756309 110 GYTPYFFSNGIFKCTNILLNKLYKISWPLN-NNKDILNIATNSSGGDK-------LLGKLIVNAYKRV 169
Cdd:TIGR02342 104 GIHPTIISESFQSAADEAIKILDEMSIPVDlSDREQLLKSATTSLSSKvvsqyssLLAPLAVDAVLKV 171
|
|
| TCP1_theta |
cd03341 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ... |
21-165 |
3.60e-04 |
|
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.
Pssm-ID: 239457 [Multi-domain] Cd Length: 472 Bit Score: 43.36 E-value: 3.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 21 QDTTNILSLTLGPRGKNIVLWDKTSKPQIINDGTSIINKINnqnfVEHIGQFLVKDVIFNVNDSVGDGTSTTGILTGNVL 100
Cdd:cd03341 18 KELSQITRTSYGPNGMNKMVINHLEKLFVTSDAATILRELE----VQHPAAKLLVMASQMQEEEIGDGTNLVVVLAGELL 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 75756309 101 SRGLSLIHSGYTPYFFSNGIFKCTNILLNKL-----YKISwPLNNNKDILN-----IATNSSGGDKLLGKLIVNA 165
Cdd:cd03341 94 EKAEELLRMGLHPSEIIEGYEKALKKALEILeelvvYKIE-DLRNKEEVSKalktaIASKQYGNEDFLSPLVAEA 167
|
|
| TCP1_zeta |
cd03342 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
18-151 |
3.91e-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: 43.02 E-value: 3.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 18 KGLQDttnILSLTLGPRGKNIVLWDKTSKPQIINDGTSIINKINNQnfveHIGQFLVKDVIFNVNDSVGDGTSTTGILTG 97
Cdd:cd03342 22 KGLQD---VLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLSEMQIQ----HPTASMIARAATAQDDITGDGTTSNVLLIG 94
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 75756309 98 NVLSRGLSLIHSGYTPYFFSNGIFKCTNILLNKL--YKISWPLNNNKDIL-NIATNS 151
Cdd:cd03342 95 ELLKQAERYIQEGVHPRIITEGFELAKNKALKFLesFKVPVEIDTDRELLlSVARTS 151
|
|
| chap_CCT_theta |
TIGR02346 |
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ... |
10-159 |
5.51e-04 |
|
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: 42.78 E-value: 5.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 10 DVIIKQIKkGLQDTTNILSLTLGPRGKNIVLWDKTSKPQIINDGTSIINKINnqnfVEHIGQFLVKDVIFNVNDSVGDGT 89
Cdd:TIGR02346 18 EAVIKNIE-ACKELSQITRTSLGPNGMNKMVINHLEKLFVTNDAATILRELE----VQHPAAKLLVMASEMQENEIGDGT 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 75756309 90 STTGILTGNVLSRGLSLIHSGYTPYFFSNGI---FKCTNILLNKLYKISWPLNNNKDILNIATNSSGGDKLLG 159
Cdd:TIGR02346 93 NLVLVLAGELLNKAEELIRMGLHPSEIIKGYemaLKKAMEILEELVVWEVKDLRDKDELIKALKASISSKQYG 165
|
|
| chap_CCT_alpha |
TIGR02340 |
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ... |
25-119 |
5.34e-03 |
|
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: 39.32 E-value: 5.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 25 NILSLTLGPRGKNIVLWDKTSKPQIINDGTSIINKINnqnfVEH-IGQFLVKdvIFNVND-SVGDGTSTTGILTGNVLSR 102
Cdd:TIGR02340 26 NIVKTSLGPVGLDKMLVDDIGDVTITNDGATILKLLE----VEHpAAKILVE--LAQLQDrEVGDGTTSVVIIAAELLKR 99
|
90
....*....|....*..
gi 75756309 103 GLSLIHSGYTPYFFSNG 119
Cdd:TIGR02340 100 ADELVKNKIHPTSVISG 116
|
|
| TCP1_alpha |
cd03335 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ... |
25-113 |
7.92e-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: 38.80 E-value: 7.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75756309 25 NILSLTLGPRGKNIVLWDKTSKPQIINDGTSIINKINnqnfVEH-IGQFLVkDVIFNVNDSVGDGTSTTGILTGNVLSRG 103
Cdd:cd03335 22 NIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLE----VEHpAAKILV-ELAQLQDKEVGDGTTSVVIIAAELLKRA 96
|
90
....*....|
gi 75756309 104 LSLIHSGYTP 113
Cdd:cd03335 97 NELVKQKIHP 106
|
|
| |
