|
Name |
Accession |
Description |
Interval |
E-value |
| GroEL |
cd03344 |
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ... |
25-548 |
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: 860.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 25 KELKFGVEGRASLLKGVETLAEAVAATLGPKGRNVLIEQPFGPPKITKDGVTVAKSIVLKDKFENMGAKLLQEVASKTNE 104
Cdd:cd03344 1 KDIKFGEEARKALLRGVNKLADAVKVTLGPKGRNVVIEKSFGSPKITKDGVTVAKEIELEDPFENMGAQLVKEVASKTND 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 105 AAGDGTTSATVLGRAIFTESVKNVAAGCNPMDLRRGSQVAVEKVIEFLSANKKEITTSEEIAQVATISANGDSHVGKLLA 184
Cdd:cd03344 81 VAGDGTTTATVLARAIIKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKPVKTKEEIAQVATISANGDEEIGELIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 185 SAMEKVGKEGVITIREGRTLEDELEVTEGMRFDRGFISPYFITDPKSSKVEFEKPLLLLSEKKISSIQDILPALEISNQS 264
Cdd:cd03344 161 EAMEKVGKDGVITVEEGKTLETELEVVEGMQFDRGYLSPYFVTDPEKMEVELENPYILLTDKKISSIQELLPILELVAKA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 265 RRPLLIIAEDVDGEALAACILNKLRGQVKVCAVKAPGFGDNRKNTIGDIAVLTGGTVFTEELDLKPEQCTIENLGSCDSI 344
Cdd:cd03344 241 GRPLLIIAEDVEGEALATLVVNKLRGGLKVCAVKAPGFGDRRKAMLEDIAILTGGTVISEELGLKLEDVTLEDLGRAKKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 345 TVTKEDTVILNGSGPKEAIQERIEQIKGSIDITTTNsYEKEKLQERLAKLSGGVAVIRVGGASEVEVGEKKDRYDDALNA 424
Cdd:cd03344 321 VVTKDDTTIIGGAGDKAAIKARIAQIRKQIEETTSD-YDKEKLQERLAKLSGGVAVIKVGGATEVELKEKKDRVEDALNA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 425 TRAAVEEGILPGGGTALVKASRVLDEVVVDNFDQKLGVDIIRKAITRPAKQIIENAGEEGSVIIGKLIDEygdDFAKGYD 504
Cdd:cd03344 400 TRAAVEEGIVPGGGVALLRASPALDKLKALNGDEKLGIEIVRRALEAPLRQIAENAGVDGSVVVEKVLES---PDGFGYD 476
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 6323288 505 ASKSEYTDMLATGIIDPFKVVRSGLVDASGVASLLATTEVAIVD 548
Cdd:cd03344 477 AATGEYVDMIEAGIIDPTKVVRSALQNAASVASLLLTTEALVVD 520
|
|
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
25-548 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 800.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 25 KELKFGVEGRASLLKGVETLAEAVAATLGPKGRNVLIEQPFGPPKITKDGVTVAKSIVLKDKFENMGAKLLQEVASKTNE 104
Cdd:PRK00013 3 KDIKFGEDARRKLLRGVNKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDPFENMGAQLVKEVASKTND 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 105 AAGDGTTSATVLGRAIFTESVKNVAAGCNPMDLRRGSQVAVEKVIEFLSANKKEITTSEEIAQVATISANGDSHVGKLLA 184
Cdd:PRK00013 83 VAGDGTTTATVLAQAIVREGLKNVAAGANPMDLKRGIDKAVEAAVEELKKISKPVEDKEEIAQVATISANGDEEIGKLIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 185 SAMEKVGKEGVITIREGRTLEDELEVTEGMRFDRGFISPYFITDPKSSKVEFEKPLLLLSEKKISSIQDILPALEISNQS 264
Cdd:PRK00013 163 EAMEKVGKEGVITVEESKGFETELEVVEGMQFDRGYLSPYFVTDPEKMEAELENPYILITDKKISNIQDLLPVLEQVAQS 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 265 RRPLLIIAEDVDGEALAACILNKLRGQVKVCAVKAPGFGDNRKNTIGDIAVLTGGTVFTEELDLKPEQCTIENLGSCDSI 344
Cdd:PRK00013 243 GKPLLIIAEDVEGEALATLVVNKLRGTLKVVAVKAPGFGDRRKAMLEDIAILTGGTVISEELGLKLEDATLEDLGQAKKV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 345 TVTKEDTVILNGSGPKEAIQERIEQIKGSIDiTTTNSYEKEKLQERLAKLSGGVAVIRVGGASEVEVGEKKDRYDDALNA 424
Cdd:PRK00013 323 VVTKDNTTIVDGAGDKEAIKARVAQIKAQIE-ETTSDYDREKLQERLAKLAGGVAVIKVGAATEVEMKEKKDRVEDALHA 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 425 TRAAVEEGILPGGGTALVKASRVLDEVVVDNFDQKLGVDIIRKAITRPAKQIIENAGEEGSVIIGKLIDEYGDDFakGYD 504
Cdd:PRK00013 402 TRAAVEEGIVPGGGVALLRAAPALEALKGLNGDEATGINIVLRALEAPLRQIAENAGLEGSVVVEKVKNGKGKGY--GYN 479
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 6323288 505 ASKSEYTDMLATGIIDPFKVVRSGLVDASGVASLLATTEVAIVD 548
Cdd:PRK00013 480 AATGEYVDMIEAGIIDPTKVTRSALQNAASVAGLLLTTEAVVAD 523
|
|
| PTZ00114 |
PTZ00114 |
Heat shock protein 60; Provisional |
18-548 |
0e+00 |
|
Heat shock protein 60; Provisional
Pssm-ID: 185455 Cd Length: 555 Bit Score: 796.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 18 RRAYSSHKELKFGVEGRASLLKGVETLAEAVAATLGPKGRNVLIEQPFGPPKITKDGVTVAKSIVLKDKFENMGAKLLQE 97
Cdd:PTZ00114 8 SRYRFKGKEIRFGDEARQSLLKGIERLADAVAVTLGPKGRNVIIEQEYGSPKITKDGVTVAKAIEFSDRFENVGAQLIRQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 98 VASKTNEAAGDGTTSATVLGRAIFTESVKNVAAGCNPMDLRRGSQVAVEKVIEFLSANKKEITTSEEIAQVATISANGDS 177
Cdd:PTZ00114 88 VASKTNDKAGDGTTTATILARAIFREGCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQSRPVKTKEDILNVATISANGDV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 178 HVGKLLASAMEKVGKEGVITIREGRTLEDELEVTEGMRFDRGFISPYFITDPKSSKVEFEKPLLLLSEKKISSIQDILPA 257
Cdd:PTZ00114 168 EIGSLIADAMDKVGKDGTITVEDGKTLEDELEVVEGMSFDRGYISPYFVTNEKTQKVELENPLILVTDKKISSIQSILPI 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 258 LEISNQSRRPLLIIAEDVDGEALAACILNKLRGQVKVCAVKAPGFGDNRKNTIGDIAVLTGGTVFTEE-LDLKPEQCTIE 336
Cdd:PTZ00114 248 LEHAVKNKRPLLIIAEDVEGEALQTLIINKLRGGLKVCAVKAPGFGDNRKDILQDIAVLTGATVVSEDnVGLKLDDFDPS 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 337 NLGSCDSITVTKEDTVILNGSGPKEAIQERIEQIKGSIDITTTNsYEKEKLQERLAKLSGGVAVIRVGGASEVEVGEKKD 416
Cdd:PTZ00114 328 MLGSAKKVTVTKDETVILTGGGDKAEIKERVELLRSQIERTTSE-YDKEKLKERLAKLSGGVAVIKVGGASEVEVNEKKD 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 417 RYDDALNATRAAVEEGILPGGGTALVKASRVLDEVVVDNF---DQKLGVDIIRKAITRPAKQIIENAGEEGSVIIGKLID 493
Cdd:PTZ00114 407 RIEDALNATRAAVEEGIVPGGGVALLRASKLLDKLEEDNEltpDQRTGVKIVRNALRLPTKQIAENAGVEGAVVVEKILE 486
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 6323288 494 eyGDDFAKGYDASKSEYTDMLATGIIDPFKVVRSGLVDASGVASLLATTEVAIVD 548
Cdd:PTZ00114 487 --KKDPSFGYDAQTGEYVNMFEAGIIDPTKVVRSALVDAASVASLMLTTEAAIVD 539
|
|
| groEL |
PRK12849 |
chaperonin GroEL; Reviewed |
25-548 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237230 Cd Length: 542 Bit Score: 745.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 25 KELKFGVEGRASLLKGVETLAEAVAATLGPKGRNVLIEQPFGPPKITKDGVTVAKSIVLKDKFENMGAKLLQEVASKTNE 104
Cdd:PRK12849 3 KIIKFDEEARRALERGVNKLADAVKVTLGPKGRNVVIDKSFGAPTITKDGVSIAKEIELEDPFENLGAQLVKEVASKTND 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 105 AAGDGTTSATVLGRAIFTESVKNVAAGCNPMDLRRGSQVAVEKVIEFLSANKKEITTSEEIAQVATISANGDSHVGKLLA 184
Cdd:PRK12849 83 VAGDGTTTATVLAQALVQEGLKNVAAGANPMDLKRGIDKAVEAVVEELKALARPVSGSEEIAQVATISANGDEEIGELIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 185 SAMEKVGKEGVITIREGRTLEDELEVTEGMRFDRGFISPYFITDPKSSKVEFEKPLLLLSEKKISSIQDILPALEISNQS 264
Cdd:PRK12849 163 EAMEKVGKDGVITVEESKTLETELEVTEGMQFDRGYLSPYFVTDPERMEAVLEDPLILLTDKKISSLQDLLPLLEKVAQS 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 265 RRPLLIIAEDVDGEALAACILNKLRGQVKVCAVKAPGFGDNRKNTIGDIAVLTGGTVFTEELDLKPEQCTIENLGSCDSI 344
Cdd:PRK12849 243 GKPLLIIAEDVEGEALATLVVNKLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGLKLEEVTLDDLGRAKRV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 345 TVTKEDTVILNGSGPKEAIQERIEQIKGSIDITTTNsYEKEKLQERLAKLSGGVAVIRVGGASEVEVGEKKDRYDDALNA 424
Cdd:PRK12849 323 TITKDNTTIVDGAGDKEAIEARVAQIRRQIEETTSD-YDREKLQERLAKLAGGVAVIKVGAATEVELKERKDRVEDALNA 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 425 TRAAVEEGILPGGGTALVKASRVLDEVVVDNFDQKLGVDIIRKAITRPAKQIIENAGEEGSVIIGKLIDEygdDFAKGYD 504
Cdd:PRK12849 402 TRAAVEEGIVPGGGVALLRAAKALDELAGLNGDQAAGVEIVRRALEAPLRQIAENAGLDGSVVVAKVLEL---EDGFGFN 478
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 6323288 505 ASKSEYTDMLATGIIDPFKVVRSGLVDASGVASLLATTEVAIVD 548
Cdd:PRK12849 479 AATGEYGDLIAAGIIDPVKVTRSALQNAASVAGLLLTTEALVAD 522
|
|
| groEL |
PRK12850 |
chaperonin GroEL; Reviewed |
25-548 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237231 Cd Length: 544 Bit Score: 721.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 25 KELKFGVEGRASLLKGVETLAEAVAATLGPKGRNVLIEQPFGPPKITKDGVTVAKSIVLKDKFENMGAKLLQEVASKTNE 104
Cdd:PRK12850 4 KEIRFSTDARDRLLRGVNILANAVKVTLGPKGRNVVLEKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVKEVASKTND 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 105 AAGDGTTSATVLGRAIFTESVKNVAAGCNPMDLRRGSQVAVEKVIEFLSANKKEITTSEEIAQVATISANGDSHVGKLLA 184
Cdd:PRK12850 84 LAGDGTTTATVLAQAIVREGAKLVAAGMNPMDLKRGIDLAVAAVVDELKKIAKKVTSSKEIAQVATISANGDESIGEMIA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 185 SAMEKVGKEGVITIREGRTLEDELEVTEGMRFDRGFISPYFITDPKSSKVEFEKPLLLLSEKKISSIQDILPALEISNQS 264
Cdd:PRK12850 164 EAMDKVGKEGVITVEEAKTLGTELDVVEGMQFDRGYLSPYFVTNPEKMRAELEDPYILLHEKKISNLQDLLPILEAVVQS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 265 RRPLLIIAEDVDGEALAACILNKLRGQVKVCAVKAPGFGDNRKNTIGDIAVLTGGTVFTEELDLKPEQCTIENLGSCDSI 344
Cdd:PRK12850 244 GRPLLIIAEDVEGEALATLVVNKLRGGLKSVAVKAPGFGDRRKAMLEDIAVLTGGQVISEDLGIKLENVTLDMLGRAKRV 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 345 TVTKEDTVILNGSGPKEAIQERIEQIKGSIDITTTNsYEKEKLQERLAKLSGGVAVIRVGGASEVEVGEKKDRYDDALNA 424
Cdd:PRK12850 324 LITKENTTIIDGAGDKKNIEARVKQIRAQIEETTSD-YDREKLQERLAKLAGGVAVIRVGGATEVEVKEKKDRVDDALHA 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 425 TRAAVEEGILPGGGTALVKASRVLDEVVVDNFDQKLGVDIIRKAITRPAKQIIENAGEEGSVIIGKLIDEYGDdfaKGYD 504
Cdd:PRK12850 403 TRAAVEEGIVPGGGVALLRARSALRGLKGANADETAGIDIVRRALEEPLRQIATNAGFEGSVVVGKVAELPGN---FGFN 479
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 6323288 505 ASKSEYTDMLATGIIDPFKVVRSGLVDASGVASLLATTEVAIVD 548
Cdd:PRK12850 480 AQTGEYGDMVEAGIIDPAKVTRTALQDAASIAALLITTEAMVAE 523
|
|
| GroEL |
TIGR02348 |
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ... |
25-548 |
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: 718.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 25 KELKFGVEGRASLLKGVETLAEAVAATLGPKGRNVLIEQPFGPPKITKDGVTVAKSIVLKDKFENMGAKLLQEVASKTNE 104
Cdd:TIGR02348 2 KQIKFDEEARKALLRGVDKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDKFENMGAQLVKEVASKTND 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 105 AAGDGTTSATVLGRAIFTESVKNVAAGCNPMDLRRGSQVAVEKVIEFLSANKKEITTSEEIAQVATISANGDSHVGKLLA 184
Cdd:TIGR02348 82 VAGDGTTTATVLAQAIVKEGLKNVAAGANPIELKRGIEKAVEAVVEELKKLSKPVKGKKEIAQVATISANNDEEIGSLIA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 185 SAMEKVGKEGVITIREGRTLEDELEVTEGMRFDRGFISPYFITDPKSSKVEFEKPLLLLSEKKISSIQDILPALEISNQS 264
Cdd:TIGR02348 162 EAMEKVGKDGVITVEESKSLETELEVVEGMQFDRGYISPYFVTDAEKMEVELENPYILITDKKISNIKDLLPLLEKVAQS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 265 RRPLLIIAEDVDGEALAACILNKLRGQVKVCAVKAPGFGDNRKNTIGDIAVLTGGTVFTEELDLKPEQCTIENLGSCDSI 344
Cdd:TIGR02348 242 GKPLLIIAEDVEGEALATLVVNKLRGTLNVCAVKAPGFGDRRKAMLEDIAILTGGQVISEELGLKLEEVTLDDLGKAKKV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 345 TVTKEDTVILNGSGPKEAIQERIEQIKGSIDITTTnSYEKEKLQERLAKLSGGVAVIRVGGASEVEVGEKKDRYDDALNA 424
Cdd:TIGR02348 322 TVDKDNTTIVEGAGDKAAIKARVAQIKAQIEETTS-DYDREKLQERLAKLAGGVAVIKVGAATETEMKEKKLRIEDALNA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 425 TRAAVEEGILPGGGTALVKASRVLDEVVVDNFDQKLGVDIIRKAITRPAKQIIENAGEEGSVIIGKLIDEYGDdfaKGYD 504
Cdd:TIGR02348 401 TRAAVEEGIVPGGGVALLRAAAALEGLKGDGEDEAIGIDIVKRALEAPLRQIAENAGLDGAVVAEKVKELKGN---FGFN 477
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 6323288 505 ASKSEYTDMLATGIIDPFKVVRSGLVDASGVASLLATTEVAIVD 548
Cdd:TIGR02348 478 AATGEYEDLVEAGIIDPTKVTRSALQNAASIAGLLLTTEAVVAD 521
|
|
| groEL |
PRK12851 |
chaperonin GroEL; Reviewed |
23-548 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 171770 Cd Length: 541 Bit Score: 666.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 23 SHKELKFGVEGRASLLKGVETLAEAVAATLGPKGRNVLIEQPFGPPKITKDGVTVAKSIVLKDKFENMGAKLLQEVASKT 102
Cdd:PRK12851 2 AAKEVKFHVEAREKMLRGVNILADAVKVTLGPKGRNVVIDKSFGAPTITNDGVTIAKEIELEDKFENMGAQMVREVASKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 103 NEAAGDGTTSATVLGRAIFTESVKNVAAGCNPMDLRRGSQVAVEKVIEFLSANKKEITTSEEIAQVATISANGDSHVGKL 182
Cdd:PRK12851 82 NDVAGDGTTTATVLAQAIVREGAKAVAAGANPMDLKRGIDRAVAAVVEELKANARPVTTNAEIAQVATISANGDAEIGRL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 183 LASAMEKVGKEGVITIREGRTLEDELEVTEGMRFDRGFISPYFITDPKSSKVEFEKPLLLLSEKKISSIQDILPALEISN 262
Cdd:PRK12851 162 VAEAMEKVGNEGVITVEESKTAETELEVVEGMQFDRGYLSPYFVTDADKMEAELEDPYILIHEKKISNLQDLLPVLEAVV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 263 QSRRPLLIIAEDVDGEALAACILNKLRGQVKVCAVKAPGFGDNRKNTIGDIAVLTGGTVFTEELDLKPEQCTIENLGSCD 342
Cdd:PRK12851 242 QSGKPLLIIAEDVEGEALATLVVNKLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGIKLENVTLEQLGRAK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 343 SITVTKEDTVILNGSGPKEAIQERIEQIKGSIDiTTTNSYEKEKLQERLAKLSGGVAVIRVGGASEVEVGEKKDRYDDAL 422
Cdd:PRK12851 322 KVVVEKENTTIIDGAGSKTEIEGRVAQIRAQIE-ETTSDYDREKLQERLAKLAGGVAVIRVGASTEVEVKEKKDRVDDAL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 423 NATRAAVEEGILPGGGTALVKASRVLDEVVVDNFDQKLGVDIIRKAITRPAKQIIENAGEEGSVIIGKLIDEYGDdfaKG 502
Cdd:PRK12851 401 HATRAAVEEGIVPGGGVALLRAVKALDKLETANGDQRTGVEIVRRALEAPVRQIAENAGAEGSVVVGKLREKPGG---YG 477
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 6323288 503 YDASKSEYTDMLATGIIDPFKVVRSGLVDASGVASLLATTEVAIVD 548
Cdd:PRK12851 478 FNAATNEYGDLYAQGVIDPVKVVRTALQNAASVAGLLLTTEAMVAE 523
|
|
| groEL |
PRK12852 |
chaperonin GroEL; Reviewed |
23-548 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237232 Cd Length: 545 Bit Score: 665.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 23 SHKELKFGVEGRASLLKGVETLAEAVAATLGPKGRNVLIEQPFGPPKITKDGVTVAKSIVLKDKFENMGAKLLQEVASKT 102
Cdd:PRK12852 2 AAKDVKFSGDARDRMLRGVDILANAVKVTLGPKGRNVVIEKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVREVASKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 103 NEAAGDGTTSATVLGRAIFTESVKNVAAGCNPMDLRRGSQVAVEKVIEFLSANKKEITTSEEIAQVATISANGDSHVGKL 182
Cdd:PRK12852 82 NDLAGDGTTTATVLAQAIVREGAKAVAAGMNPMDLKRGIDIAVAAVVKDIEKRAKPVASSAEIAQVGTISANGDAAIGKM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 183 LASAMEKVGKEGVITIREGRTLEDELEVTEGMRFDRGFISPYFITDPKSSKVEFEKPLLLLSEKKISSIQDILPALEISN 262
Cdd:PRK12852 162 IAQAMQKVGNEGVITVEENKSLETEVDIVEGMKFDRGYLSPYFVTNAEKMTVELDDAYILLHEKKLSGLQAMLPVLEAVV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 263 QSRRPLLIIAEDVDGEALAACILNKLRGQVKVCAVKAPGFGDNRKNTIGDIAVLTGGTVFTEELDLKPEQCTIENLGSCD 342
Cdd:PRK12852 242 QSGKPLLIIAEDVEGEALATLVVNRLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGQLISEDLGIKLENVTLKMLGRAK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 343 SITVTKEDTVILNGSGPKEAIQERIEQIKGSIDITTTNsYEKEKLQERLAKLSGGVAVIRVGGASEVEVGEKKDRYDDAL 422
Cdd:PRK12852 322 KVVIDKENTTIVNGAGKKADIEARVGQIKAQIEETTSD-YDREKLQERLAKLAGGVAVIRVGGATEVEVKEKKDRVEDAL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 423 NATRAAVEEGILPGGGTALVKASRVLDEVVVDNFDQKLGVDIIRKAITRPAKQIIENAGEEGSVIIGKLIDEYGDDFakG 502
Cdd:PRK12852 401 NATRAAVQEGIVPGGGVALLRAKKAVGRINNDNADVQAGINIVLKALEAPIRQIAENAGVEGSIVVGKILENKSETF--G 478
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 6323288 503 YDASKSEYTDMLATGIIDPFKVVRSGLVDASGVASLLATTEVAIVD 548
Cdd:PRK12852 479 FDAQTEEYVDMVAKGIIDPAKVVRTALQDAASVAGLLVTTEAMVAE 524
|
|
| GroEL |
COG0459 |
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ... |
25-548 |
0e+00 |
|
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227 Cd Length: 497 Bit Score: 640.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 25 KELKFGVEGRASLLKGVETLAEAVAATLGPKGRNVLIEQPFGPPKITKDGVTVAKSIVLKDKFENMGAKLLQEVASKTNE 104
Cdd:COG0459 3 KQILFGEDARRANIRGVKALADAVKVTLGPKGRNVMLVKSFGDPTITNDGVTIAKEIELEDPFENMGAQLVKEVASKTND 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 105 AAGDGTTSATVLGRAIFTESVKNVAAGCNPMDLRRGSQVAVEKVIEFLSANKKEITTSEEIAQVATISANGDSHVGKLLA 184
Cdd:COG0459 83 EAGDGTTTATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPVDDKEELAQVATISANGDEEIGELIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 185 SAMEKVGKEGVITIREGRTLEDELEVTEGMRFDRGFISPYFITDPKSSKVEFEKPLLLLSEKKISSIQDILPALEISNQS 264
Cdd:COG0459 163 EAMEKVGKDGVITVEEGKGLETELEVVEGMQFDKGYLSPYFVTDPEKMPAELENAYILLTDKKISSIQDLLPLLEKVAQS 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 265 RRPLLIIAEDVDGEALAACILNKLRGQVKVCAVKAPGFGDNRKNTIGDIAVLTGGTVFTEELDLKPEQCTIENLGSCDSI 344
Cdd:COG0459 243 GKPLLIIAEDIDGEALATLVVNGIRGVLRVVAVKAPGFGDRRKAMLEDIAILTGGRVISEDLGLKLEDVTLDDLGRAKRV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 345 TVTKEDTVILNGSGPKEAIqerieqikgsiditttnsyekeklqerlaklsggvaVIRVGGASEVEVGEKKDRYDDALNA 424
Cdd:COG0459 323 EVDKDNTTIVEGAGNPKAI------------------------------------VILVGAATEVEVKERKRRVEDALHA 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 425 TRAAVEEGILPGGGTALVKASRVLDEVV--VDNfDQKLGVDIIRKAITRPAKQIIENAGEEGSVIIGKLIDEYGDDFakG 502
Cdd:COG0459 367 TRAAVEEGIVPGGGAALLRAARALRELAakLEG-DEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKVRAAKDKGF--G 443
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 6323288 503 YDASKSEYTDMLATGIIDPFKVVRSGLVDASGVASLLATTEVAIVD 548
Cdd:COG0459 444 FDAATGEYVDMLEAGVIDPAKVKRSALQNAASVAGLILTTEAVIAD 489
|
|
| PRK14104 |
PRK14104 |
chaperonin GroEL; Provisional |
23-548 |
0e+00 |
|
chaperonin GroEL; Provisional
Pssm-ID: 172594 Cd Length: 546 Bit Score: 603.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 23 SHKELKFGVEGRASLLKGVETLAEAVAATLGPKGRNVLIEQPFGPPKITKDGVTVAKSIVLKDKFENMGAKLLQEVASKT 102
Cdd:PRK14104 2 SAKEVKFGVDARDRMLRGVDILANAVKVTLGPKGRNVVLDKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVREVASKS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 103 NEAAGDGTTSATVLGRAIFTESVKNVAAGCNPMDLRRGSQVAVEKVIEFLSANKKEITTSEEIAQVATISANGDSHVGKL 182
Cdd:PRK14104 82 ADAAGDGTTTATVLAQAIVREGAKSVAAGMNPMDLKRGIDLAVEAVVADLVKNSKKVTSNDEIAQVGTISANGDAEIGKF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 183 LASAMEKVGKEGVITIREGRTLEDELEVTEGMRFDRGFISPYFITDPKSSKVEFEKPLLLLSEKKISSIQDILPALEISN 262
Cdd:PRK14104 162 LADAMKKVGNEGVITVEEAKSLETELDVVEGMQFDRGYISPYFVTNADKMRVEMDDAYILINEKKLSSLNELLPLLEAVV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 263 QSRRPLLIIAEDVDGEALAACILNKLRGQVKVCAVKAPGFGDNRKNTIGDIAVLTGGTVFTEELDLKPEQCTIENLGSCD 342
Cdd:PRK14104 242 QTGKPLVIVAEDVEGEALATLVVNRLRGGLKVAAVKAPGFGDRRKAMLQDIAILTGGQAISEDLGIKLENVTLQMLGRAK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 343 SITVTKEDTVILNGSGPKEAIQERIEQIKGSIDiTTTNSYEKEKLQERLAKLSGGVAVIRVGGASEVEVGEKKDRYDDAL 422
Cdd:PRK14104 322 KVMIDKENTTIVNGAGKKADIEARVAQIKAQIE-ETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKERKDRVDDAM 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 423 NATRAAVEEGILPGGGTALVKASRVLDEVVVDNFDQKLGVDIIRKAITRPAKQIIENAGEEGSVIIGKLIDEygDDFAKG 502
Cdd:PRK14104 401 HATRAAVEEGIVPGGGVALLRASEQLKGIKTKNDDQKTGVEIVRKALSAPARQIAINAGEDGSVIVGKILEK--EQYSYG 478
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 6323288 503 YDASKSEYTDMLATGIIDPFKVVRSGLVDASGVASLLATTEVAIVD 548
Cdd:PRK14104 479 FDSQTGEYGNLVSKGIIDPTKVVRTAIQNAASVAALLITTEAMVAE 524
|
|
| groEL |
CHL00093 |
chaperonin GroEL |
34-548 |
0e+00 |
|
chaperonin GroEL
Pssm-ID: 177025 Cd Length: 529 Bit Score: 603.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 34 RASLLKGVETLAEAVAATLGPKGRNVLIEQPFGPPKITKDGVTVAKSIVLKDKFENMGAKLLQEVASKTNEAAGDGTTSA 113
Cdd:CHL00093 12 RRALERGMDILAEAVSVTLGPKGRNVVLEKKYGSPQIVNDGVTIAKEIELEDHIENTGVALIRQAASKTNDVAGDGTTTA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 114 TVLGRAIFTESVKNVAAGCNPMDLRRGSQVAVEKVIEFLSANKKEITTSEEIAQVATISANGDSHVGKLLASAMEKVGKE 193
Cdd:CHL00093 92 TVLAYAIVKQGMKNVAAGANPISLKRGIEKATQYVVSQIAEYARPVEDIQAITQVASISAGNDEEVGSMIADAIEKVGRE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 194 GVITIREGRTLEDELEVTEGMRFDRGFISPYFITDPKSSKVEFEKPLLLLSEKKISSI-QDILPALEISNQSRRPLLIIA 272
Cdd:CHL00093 172 GVISLEEGKSTVTELEITEGMRFEKGFISPYFVTDTERMEVVQENPYILLTDKKITLVqQDLLPILEQVTKTKRPLLIIA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 273 EDVDGEALAACILNKLRGQVKVCAVKAPGFGDNRKNTIGDIAVLTGGTVFTEELDLKPEQCTIENLGSCDSITVTKEDTV 352
Cdd:CHL00093 252 EDVEKEALATLVLNKLRGIVNVVAVRAPGFGDRRKAMLEDIAILTGGQVITEDAGLSLETIQLDLLGQARRIIVTKDSTT 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 353 ILNgSGPKEAIQERIEQIKGSIDITTTnSYEKEKLQERLAKLSGGVAVIRVGGASEVEVGEKKDRYDDALNATRAAVEEG 432
Cdd:CHL00093 332 IIA-DGNEEQVKARCEQLRKQIEIADS-SYEKEKLQERLAKLSGGVAVIKVGAATETEMKDKKLRLEDAINATKAAVEEG 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 433 ILPGGGTALVKASRVLDEVVVDNF--DQKLGVDIIRKAITRPAKQIIENAGEEGSVIIGKLIDEygdDFAKGYDASKSEY 510
Cdd:CHL00093 410 IVPGGGATLVHLSENLKTWAKNNLkeDELIGALIVARAILAPLKRIAENAGKNGSVIIEKVQEQ---DFEIGYNAANNKF 486
|
490 500 510
....*....|....*....|....*....|....*...
gi 6323288 511 TDMLATGIIDPFKVVRSGLVDASGVASLLATTEVAIVD 548
Cdd:CHL00093 487 VNMYEAGIIDPAKVTRSALQNAASIASMILTTECIIVD 524
|
|
| PLN03167 |
PLN03167 |
Chaperonin-60 beta subunit; Provisional |
3-548 |
1.59e-163 |
|
Chaperonin-60 beta subunit; Provisional
Pssm-ID: 215611 [Multi-domain] Cd Length: 600 Bit Score: 479.04 E-value: 1.59e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 3 RSSVVRSRATLRPLLRRAysshKELKFGVEGRA--SLLKGVETLAEAVAATLGPKGRNVLIEQPFGPPKITKDGVTVAKS 80
Cdd:PLN03167 39 RRQSVRLRRSRSPKVKAA----KELHFNKDGSAikKLQAGVNKLADLVGVTLGPKGRNVVLESKYGSPKIVNDGVTVAKE 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 81 IVLKDKFENMGAKLLQEVASKTNEAAGDGTTSATVLGRAIFTESVKNVAAGCNPMDLRRGSQVAVEKVIEFLSANKKEIT 160
Cdd:PLN03167 115 VELEDPVENIGAKLVRQAAAKTNDLAGDGTTTSVVLAQGLIAEGVKVVAAGANPVQITRGIEKTAKALVKELKKMSKEVE 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 161 TSEeIAQVATISANGDSHVGKLLASAMEKVGKEGVITIREGRTLEDELEVTEGMRFDRGFISPYFITDPKSSKVEFEKPL 240
Cdd:PLN03167 195 DSE-LADVAAVSAGNNYEVGNMIAEAMSKVGRKGVVTLEEGKSAENNLYVVEGMQFDRGYISPYFVTDSEKMSVEYDNCK 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 241 LLLSEKKISSIQDILPALEISNQSRRPLLIIAEDVDGEALAACILNKLRGQVKVCAVKAPGFGDNRKNTIGDIAVLTGGT 320
Cdd:PLN03167 274 LLLVDKKITNARDLIGILEDAIRGGYPLLIIAEDIEQEALATLVVNKLRGSLKIAALKAPGFGERKSQYLDDIAILTGGT 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 321 VFTEELDLKPEQCTIENLGSCDSITVTKEDTVILNGSGPKEAIQERIEQIKGSIDItTTNSYEKEKLQERLAKLSGGVAV 400
Cdd:PLN03167 354 VIREEVGLSLDKVGKEVLGTAAKVVLTKDTTTIVGDGSTQEAVNKRVAQIKNLIEA-AEQDYEKEKLNERIAKLSGGVAV 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 401 IRVGGASEVEVGEKKDRYDDALNATRAAVEEGILPGGGTALVKASRVLDEVV--VDNFDQKLGVDIIRKAITRPAKQIIE 478
Cdd:PLN03167 433 IQVGAQTETELKEKKLRVEDALNATKAAVEEGIVVGGGCTLLRLASKVDAIKdtLENDEQKVGADIVKRALSYPLKLIAK 512
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 479 NAGEEGSVIIGKLIDEygDDFAKGYDASKSEYTDMLATGIIDPFKVVRSGLVDASGVASLLATTEVAIVD 548
Cdd:PLN03167 513 NAGVNGSVVSEKVLSN--DNPKFGYNAATGKYEDLMAAGIIDPTKVVRCCLEHAASVAKTFLTSDCVVVE 580
|
|
| chaperonin_type_I_II |
cd00309 |
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ... |
25-547 |
2.35e-139 |
|
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: 412.21 E-value: 2.35e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 25 KELKFGVEGRASLLKGVETLAEAVAATLGPKGRNVLIEQPFGPPKITKDGVTVAKSIvlkdKFENMGAKLLQEVASKTNE 104
Cdd:cd00309 1 KEREFGEEARLSNINAAKALADAVKTTLGPKGMDKMLVDSLGDPTITNDGATILKEI----EVEHPAAKLLVEVAKSQDD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 105 AAGDGTTSATVLGRAIFTESVKNVAAGCNPMDLRRGSQVAVEKVIEFLSANKK--EITTSEEIAQVATISAN------GD 176
Cdd:cd00309 77 EVGDGTTTVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVpiDVEDREELLKVATTSLNsklvsgGD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 177 SHVGKLLASAMEKVGKE------GVITIRE---GRTLEDELEVteGMRFDRGFISPYFitdpkssKVEFEKPLLLLSEKK 247
Cdd:cd00309 157 DFLGELVVDAVLKVGKEngdvdlGVIRVEKkkgGSLEDSELVV--GMVFDKGYLSPYM-------PKRLENAKILLLDCK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 248 ISSiqdilpaleisnqsrrplLIIAED-VDGEALAACILNklrgqvKVCAVKApgfgdNRKNTIGDIAVLTGGTVFTEEL 326
Cdd:cd00309 228 LEY------------------VVIAEKgIDDEALHYLAKL------GIMAVRR-----VRKEDLERIAKATGATIVSRLE 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 327 DLKPEQctienLGSCDSITVTK----EDTVILNGSGpkeaiqerieqikgsiditttnsyekeklqerlaklsGGVAVIR 402
Cdd:cd00309 279 DLTPED-----LGTAGLVEETKigdeKYTFIEGCKG-------------------------------------GKVATIL 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 403 VGGASEVEVGEKKDRYDDALNATRAAVEE-GILPGGGTALVKASRVLDEVVV-DNFDQKLGVDIIRKAITRPAKQIIENA 480
Cdd:cd00309 317 LRGATEVELDEAERSLHDALCAVRAAVEDgGIVPGGGAAEIELSKALEELAKtLPGKEQLGIEAFADALEVIPRTLAENA 396
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6323288 481 GEEGSVIIGKLIDEYGDDFAK-GYDASKSEYTDMLATGIIDPFKVVRSGLVDASGVASLLATTEVAIV 547
Cdd:cd00309 397 GLDPIEVVTKLRAKHAEGGGNaGGDVETGEIVDMKEAGIIDPLKVKRQALKSATEAASLILTIDDIIV 464
|
|
| Cpn60_TCP1 |
pfam00118 |
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ... |
44-548 |
1.86e-71 |
|
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: 237.10 E-value: 1.86e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 44 LAEAVAATLGPKGRNVLIEQPFGPPKITKDGVTVAKSIVLkdkfENMGAKLLQEVASKTNEAAGDGTTSATVLGRAIFTE 123
Cdd:pfam00118 1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELEI----QHPAAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 124 SVKNVAAGCNPMDLRRGSQVAVEKVIEFLSANKK---EITTSEEIAQVATISANGD------SHVGKLLASAMEKVGKE- 193
Cdd:pfam00118 77 AEKLLAAGVHPTTIIEGYEKALEKALEILDSIISipvEDVDREDLLKVARTSLSSKiisresDFLAKLVVDAVLAIPKNd 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 194 --------GVITIREGRTleDELEVTEGMRFDRGFISPYFITDPKSSKV-------EFEKP-----LLLLSEKKISSIQD 253
Cdd:pfam00118 157 gsfdlgniGVVKILGGSL--EDSELVDGVVLDKGPLHPDMPKRLENAKVlllncslEYEKTetkatVVLSDAEQLERFLK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 254 -----ILPALEISNQSRRPLLIIAEDVDGEALAACILNKLRGQVKVcavkapgfgdnRKNTIGDIAVLTGGTVFTEELDL 328
Cdd:pfam00118 235 aeeeqILEIVEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMALRRV-----------KKRDLERLAKATGARAVSSLDDL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 329 KPeqctiENLGSCDSI---TVTKEDTVILNGSgpkeaiqerieqikgsiditttnsyekeklqerlakLSGGVAVIRVGG 405
Cdd:pfam00118 304 TP-----DDLGTAGKVeeeKIGDEKYTFIEGC------------------------------------KSPKAATILLRG 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 406 ASEVEVGEKKDRYDDALNATRAAVEE-GILPGGGTALVKASRVLDEVVV-DNFDQKLGVDIIRKAITRPAKQIIENAGEE 483
Cdd:pfam00118 343 ATDHVLDEIERSIHDALCVVKNAIEDpRVVPGGGAVEMELARALREYAKsVSGKEQLAIEAFAEALEVIPKTLAENAGLD 422
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6323288 484 GSVIIGKLIDEY-GDDFAKGYDASKSEYTDMLATGIIDPFKVVRSGLVDASGVASLLATTEVAIVD 548
Cdd:pfam00118 423 PIEVLAELRAAHaSGEKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKSATEAASTILRIDDIIKA 488
|
|
| chaperonin_like |
cd03333 |
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ... |
163-431 |
2.94e-37 |
|
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings, each composed of 7-9 subunits. There are 2 main chaperonin groups. The symmetry of type I is seven-fold and they are found in eubacteria (GroEL) and in organelles of eubacterial descent (hsp60 and RBP). The symmetry of type II is eight- or nine-fold and they are found in archea (thermosome), thermophilic bacteria (TF55) and in the eukaryotic cytosol (CTT). Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. This superfamily also contains related domains from Fab1-like phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinases that only contain the intermediate and apical domains.
Pssm-ID: 239449 [Multi-domain] Cd Length: 209 Bit Score: 137.21 E-value: 2.94e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 163 EEIAQVATISAN-----GDSHVGKLLASAMEKVGKE------GVITIRE---GRTLEDELEVteGMRFDRGFISPYFitd 228
Cdd:cd03333 2 ELLLQVATTSLNsklssWDDFLGKLVVDAVLKVGPDnrmddlGVIKVEKipgGSLEDSELVV--GVVFDKGYASPYM--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 229 pkssKVEFEKPLLLLSEKKISSiqdilpaleisnqsrrplLIIAED-VDGEALAACILNKlrgqvkVCAVKApgfgdNRK 307
Cdd:cd03333 77 ----PKRLENAKILLLDCPLEY------------------VVIAEKgIDDLALHYLAKAG------IMAVRR-----VKK 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 308 NTIGDIAVLTGGTVFTEELDLKPEQctienLGSCDSITVTK--EDTVILngsgpkeaiqerIEQIKGsiditttnsyeke 385
Cdd:cd03333 124 EDLERIARATGATIVSSLEDLTPED-----LGTAELVEETKigEEKLTF------------IEGCKG------------- 173
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 6323288 386 klqerlaklsGGVAVIRVGGASEVEVGEKKDRYDDALNATRAAVEE 431
Cdd:cd03333 174 ----------GKAATILLRGATEVELDEVKRSLHDALCAVRAAVEE 209
|
|
| cpn60 |
cd03343 |
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ... |
43-539 |
6.32e-14 |
|
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: 74.22 E-value: 6.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 43 TLAEAVAATLGPKGRNVLIEQPFGPPKITKDGVTVAKSIVLkdkfENMGAKLLQEVASKTNEAAGDGTTSATVLGRAIFT 122
Cdd:cd03343 26 AVAEAVRTTLGPKGMDKMLVDSLGDVTITNDGATILKEMDI----EHPAAKMLVEVAKTQDEEVGDGTTTAVVLAGELLE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 123 ESVKNVAAGCNPMDLRRGSQVAVEKVIEFLSANKKEITTSEE-----IAQVATISANGDSHVGKL--------LASAMEK 189
Cdd:cd03343 102 KAEDLLDQNIHPTVIIEGYRLAAEKALELLDEIAIKVDPDDKdtlrkIAKTSLTGKGAEAAKDKLadlvvdavLQVAEKR 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 190 VGKEGV------ITIREGRTLEDElEVTEGMRFDRGFIS---PYFITDPK----SSKVEFEKPlLLLSEKKISSIQDILP 256
Cdd:cd03343 182 DGKYVVdldnikIEKKTGGSVDDT-ELIRGIVIDKEVVHpgmPKRVENAKiallDAPLEVKKT-EIDAKIRITSPDQLQA 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 257 ALEisnQSRRPL--------------LIIAEDVDGeaLAACILNKlRGQVKVCAVKapgfgdnrKNTIGDIAVLTGGTVF 322
Cdd:cd03343 260 FLE---QEEAMLkemvdkiadtganvVFCQKGIDD--LAQHYLAK-AGILAVRRVK--------KSDMEKLARATGAKIV 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 323 TEELDLKPeqctiENLGSCDSITVTK--EDTVILngsgpkeaiqerIEQIKGSIDITttnsyekeklqerlaklsggvav 400
Cdd:cd03343 326 TNIDDLTP-----EDLGEAELVEERKvgDDKMVF------------VEGCKNPKAVT----------------------- 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 401 IRVGGASEVEVGEKKDRYDDALNATRAAVEEG-ILPGGGTALVKASRVLDEvvvdnFDQKLG------VDIIRKAITRPA 473
Cdd:cd03343 366 ILLRGGTEHVVDELERALEDALRVVADALEDGkVVAGGGAVEIELAKRLRE-----YARSVGgreqlaVEAFADALEEIP 440
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6323288 474 KQIIENAGEEGSVIIGKLI--DEYGDDFAkGYDASKSEYTDMLATGIIDPFKVVRSGLVDASGVASLL 539
Cdd:cd03343 441 RTLAENAGLDPIDTLVELRaaHEKGNKNA-GLDVYTGEVVDMLEKGVIEPLRVKKQAIKSATEAATMI 507
|
|
| TCP1_delta |
cd03338 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ... |
44-222 |
5.43e-12 |
|
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.
Pssm-ID: 239454 [Multi-domain] Cd Length: 515 Bit Score: 68.08 E-value: 5.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 44 LAEAVAATLGPKGRNVLIEQPFGPPKITKDGVTVAKSIvlkdKFENMGAKLLQEVASKTNEAAGDGTTSATVLGRAIFTE 123
Cdd:cd03338 20 VADAIRTSLGPRGMDKMIQTGKGEVIITNDGATILKQM----SVLHPAAKMLVELSKAQDIEAGDGTTSVVVLAGALLSA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 124 SVKNVAAGCNPMDLRRGSQVAVEKVIEFLSANKKEITTS--EEIAQVATISANGD--SHVGKLLAS----AMEKVGKEGV 195
Cdd:cd03338 96 CESLLKKGIHPTVISESFQIAAKKAVEILDSMSIPVDLNdrESLIKSATTSLNSKvvSQYSSLLAPiavdAVLKVIDPAT 175
|
170 180 190
....*....|....*....|....*....|....*..
gi 6323288 196 ----------ITIREGRTLEDElEVTEGMRFDRGFIS 222
Cdd:cd03338 176 atnvdlkdirIVKKLGGTIEDT-ELVDGLVFTQKASK 211
|
|
| chap_CCT_epsi |
TIGR02343 |
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ... |
30-450 |
3.63e-10 |
|
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: 62.51 E-value: 3.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 30 GVEGRASLLKGVETLAEAVAATLGPKGRNVLIEQPFGPPKITKDGVTvaksIVLKDKFENMGAKLLQEVASKTNEAAGDG 109
Cdd:TIGR02343 25 GLEAKKSNIAAAKSVASILRTSLGPKGMDKMLISPDGDITVTNDGAT----ILSQMDVDNQIAKLMVELSKSQDDEIGDG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 110 TTSATVLGRAIFTESVKNVAAGCNPMDLRRGSQVAVEKVIEFLSANKKEITTSEEIAQV---ATISANGDSHVGKLLASa 186
Cdd:TIGR02343 101 TTGVVVLAGALLEQAEELLDKGIHPIKIADGFEEAARIAVEHLEEISDEISADNNNREPliqAAKTSLGSKIVSKCHRR- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 187 MEKVGKEGVITI-----------------REGRTLEDElEVTEGMRFDRGFISPYFITDPKSSKVE-----FEKPLLLLS 244
Cdd:TIGR02343 180 FAEIAVDAVLNVadmerrdvdfdlikvegKVGGSLEDT-KLIKGIIIDKDFSHPQMPKEVEDAKIAiltcpFEPPKPKTK 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 245 EK-KISSIQDiLPALEISNQSRRPLLIIAEDVDGEALAACI------LNKLRGQVKVCAVKAPGFGDnrkntIGDIAVLT 317
Cdd:TIGR02343 259 HKlDISSVEE-YKKLQKYEQQKFKEMIDDIKKSGANLVICQwgfddeANHLLLQNDLPAVRWVGGQE-----LELIAIAT 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 318 GGTVFTEELDLKPEQctienLGSC-----DSITVTKEDTVIlngsgpkeaiqerIEQIKGSIDITttnsyekeklqerla 392
Cdd:TIGR02343 333 GGRIVPRFQELSKDK-----LGKAglvreISFGTTKDRMLV-------------IEQCKNSKAVT--------------- 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 6323288 393 klsggvavIRVGGASEVEVGEKKDRYDDALNATRAAVEEG-ILPGGGTALVKASRVLDE 450
Cdd:TIGR02343 380 --------IFIRGGNKMIIEEAKRSIHDALCVVRNLIKDSrIVYGGGAAEISCSLAVSQ 430
|
|
| TCP1_beta |
cd03336 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ... |
34-164 |
1.92e-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: 60.04 E-value: 1.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 34 RASLLKGVETLAEAVAATLGPKGRNVlIEQPFGPP---KITKDGVTVAKSIVLkdkfENMGAKLLQEVASKTNEAAGDGT 110
Cdd:cd03336 15 RLSSFVGAIAIGDLVKTTLGPKGMDK-ILQSVGRSggvTVTNDGATILKSIGV----DNPAAKVLVDISKVQDDEVGDGT 89
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 6323288 111 TSATVLGRAIFTESVKNVAAGCNPMDLRRGSQVAVEKVIEFLSANKKEITTSEE 164
Cdd:cd03336 90 TSVTVLAAELLREAEKLVAQKIHPQTIIEGYRMATAAAREALLSSAVDHSSDEE 143
|
|
| chap_CCT_eta |
TIGR02345 |
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ... |
32-163 |
3.17e-09 |
|
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT eta chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.
Pssm-ID: 274086 [Multi-domain] Cd Length: 523 Bit Score: 59.39 E-value: 3.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 32 EGRASLLKGVE---TLAEAVAATLGPKGRNVLIEQPFGPPKITKDGVTVAK--SIVlkdkfeNMGAKLLQEVASKTNEAA 106
Cdd:TIGR02345 15 QGKGQLISNINacvAIAEALKTTLGPRGMDKLIVGSNGKATISNDGATILKllDIV------HPAAKTLVDIAKSQDAEV 88
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 6323288 107 GDGTTSATVLGRAIFTESVKNVAAGCNPMDLRRGSQVAVEKVIEFLSANKKEITTSE 163
Cdd:TIGR02345 89 GDGTTSVTILAGELLKEAKPFIEEGVHPQLIIRCYREALSLAVEKIKEIAVTIDEEK 145
|
|
| chap_CCT_delta |
TIGR02342 |
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ... |
34-152 |
4.34e-09 |
|
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: 59.03 E-value: 4.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 34 RASLLKGVETLAEAVAATLGPKGRNVLIEQPFGPPKITKDGVTVAKSIvlkdKFENMGAKLLQEVASKTNEAAGDGTTSA 113
Cdd:TIGR02342 11 RTSNIVAAKAVADAIRTSLGPKGMDKMIQDGKGEVIITNDGATILKQM----AVLHPAAKMLVELSKAQDIEAGDGTTSV 86
|
90 100 110
....*....|....*....|....*....|....*....
gi 6323288 114 TVLGRAIFTESVKNVAAGCNPMDLRRGSQVAVEKVIEFL 152
Cdd:TIGR02342 87 VILAGALLGACERLLNKGIHPTIISESFQSAADEAIKIL 125
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
34-146 |
1.37e-08 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 57.35 E-value: 1.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 34 RASLLKGVETLAEAVAATLGPKGRNVlIEQPFGP------PKITKDGVTVAKSIVLkdkfENMGAKLLQEVASKTNEAAG 107
Cdd:PTZ00212 24 RLQSFVGAIAVADLVKTTLGPKGMDK-ILQPMSEgprsgnVTVTNDGATILKSVWL----DNPAAKILVDISKTQDEEVG 98
|
90 100 110
....*....|....*....|....*....|....*....
gi 6323288 108 DGTTSATVLGRAIFTESVKNVAAGCNPMDLRRGSQVAVE 146
Cdd:PTZ00212 99 DGTTSVVVLAGELLREAEKLLDQKIHPQTIIEGWRMALD 137
|
|
| TCP1_eta |
cd03340 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ... |
27-151 |
2.45e-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: 56.53 E-value: 2.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 27 LKFGV---EGRASLLKGV---ETLAEAVAATLGPKGRNVLIEQPFGPPKITKDGVTVAK--SIVlkdkfeNMGAKLLQEV 98
Cdd:cd03340 5 LKEGTdtsQGKGQLISNInacQAIADAVRTTLGPRGMDKLIVDGRGKVTISNDGATILKllDIV------HPAAKTLVDI 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 6323288 99 ASKTNEAAGDGTTSATVLGRAIFTESVKNVAAGCNPM----DLRRGSQVAVEKVIEF 151
Cdd:cd03340 79 AKSQDAEVGDGTTSVVVLAGEFLKEAKPFIEDGVHPQiiirGYRKALQLAIEKIKEI 135
|
|
| chap_CCT_beta |
TIGR02341 |
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ... |
30-539 |
3.70e-08 |
|
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: 56.02 E-value: 3.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 30 GVEGRASLLKGVETLAEAVAATLGPKGRNVLIEQ--PFGPPKITKDGVTVAKSIVLkdkfENMGAKLLQEVASKTNEAAG 107
Cdd:TIGR02341 12 AENARLSSFVGAIAIGDLVKSTLGPKGMDKILQSssSDASIMVTNDGATILKSIGV----DNPAAKVLVDMSKVQDDEVG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 108 DGTTSATVLGRAIFTESVKNVAAGCNPMDLRRGSQVAVEKVIEFLSANKKEITTSEEIAQVATISANGDSHVGKLLASAM 187
Cdd:TIGR02341 88 DGTTSVTVLAAELLREAEKLINQKIHPQTIIAGYREATKAARDALLKSAVDNGSDEVKFRQDLMNIARTTLSSKILSQHK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 188 EKVGKEGVITI--REGRTLEDELEVTE--GMRFDRGFISPYFITDPK-----SSKVEFEKPLLLLSEKKISSIQDILPAL 258
Cdd:TIGR02341 168 DHFAQLAVDAVlrLKGSGNLEAIQIIKklGGSLADSYLDEGFLLDKKigvnqPKRIENAKILIANTGMDTDKVKIFGSRV 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 259 EISNQSRRPLLIIAEDVDGEALAACILN-----------------KLRGQVKVCAVKAPGFgdnrkNTIGDIAVLTGGTV 321
Cdd:TIGR02341 248 RVDSTAKVAELEHAEKEKMKEKVEKILKhgincfinrqliynypeQLFADAGVMAIEHADF-----EGVERLALVTGGEI 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 322 FTeELDlKPEQCtieNLGSCDSItvtkEDTVIlngsgpkeaiqerieqikgsiditttnsyekekLQERLAKLSGGVA-- 399
Cdd:TIGR02341 323 VS-TFD-HPELV---KLGSCDLI----EEIMI---------------------------------GEDKLLKFSGVKLge 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 400 --VIRVGGASEVEVGEKKDRYDDALNATRAAVEEG--ILPGGGTALVKASRVLDEVVVDNFDQKLGVDIIRKAITRPAKQ 475
Cdd:TIGR02341 361 acTIVLRGATQQILDEAERSLHDALCVLSQTVKESrtVLGGGCSEMLMSKAVTQEAQRTPGKEALAVEAFARALRQLPTI 440
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6323288 476 IIENAGEEGSVIIGKLIDEYGD-DFAKGYDASKSEYTDMLATGIIDPFKVVRSGLVDASGVASLL 539
Cdd:TIGR02341 441 IADNAGFDSAELVAQLRAAHYNgNTTMGLDMNEGTIADMRQLGITESYKVKRAVVSSAAEAAEVI 505
|
|
| TCP1_epsilon |
cd03339 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ... |
32-164 |
1.30e-06 |
|
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: 51.15 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 32 EGRASLLKGVETL------AEAVAAT----LGPKGRNVLIEQPFGPPKITKDGVTvaksIVLKDKFENMGAKLLQEVASK 101
Cdd:cd03339 13 QEKKKRLKGLEAHkshilaAKSVANIlrtsLGPRGMDKILVSPDGEVTVTNDGAT----ILEKMDVDHQIAKLLVELSKS 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6323288 102 TNEAAGDGTTSATVLGRAIFTESVKNVAAGCNPMDLRRGSQVAVEKVIEFLSANKKEITTSEE 164
Cdd:cd03339 89 QDDEIGDGTTGVVVLAGALLEQAEKLLDRGIHPIRIADGYEQACKIAVEHLEEIADKIEFSPD 151
|
|
| chap_CCT_alpha |
TIGR02340 |
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ... |
26-185 |
2.37e-06 |
|
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT alpha chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.
Pssm-ID: 274081 [Multi-domain] Cd Length: 536 Bit Score: 50.49 E-value: 2.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 26 ELKFGVEGRASLLKGVETLAEAVAATLGPKGRNVLIEQPFGPPKITKDGVTVAKSIvlkdKFENMGAKLLQEVASKTNEA 105
Cdd:TIGR02340 6 ERTSGQDVRTQNVTAAMAIANIVKTSLGPVGLDKMLVDDIGDVTITNDGATILKLL----EVEHPAAKILVELAQLQDRE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 106 AGDGTTSATVLGRAIFTESVKNVAAGCNPMDLRRGSQVAVEKVIEFLSanKKEITTSEEIAQVATISANGDSHVGKLLAS 185
Cdd:TIGR02340 82 VGDGTTSVVIIAAELLKRADELVKNKIHPTSVISGYRLACKEAVKYIK--ENLSVSVDELGREALINVAKTSMSSKIIGL 159
|
|
| TCP1_zeta |
cd03342 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
42-544 |
2.87e-06 |
|
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.
Pssm-ID: 239458 [Multi-domain] Cd Length: 484 Bit Score: 49.95 E-value: 2.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 42 ETLAEAVAATLGPKGRNVLIEQPFGPPKITKDGVTVAKSIvlkdKFENMGAKLLQEVASKTNEAAGDGTTSATVLGRAIF 121
Cdd:cd03342 22 KGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLSEM----QIQHPTASMIARAATAQDDITGDGTTSNVLLIGELL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 122 TESVKNVAAGCNPMDLRRGSQVAVEKVIEFLSANK--KEITTSEEIA-QVATISANGDSHVGklLASAMEKVGKEGVITI 198
Cdd:cd03342 98 KQAERYIQEGVHPRIITEGFELAKNKALKFLESFKvpVEIDTDRELLlSVARTSLRTKLHAD--LADQLTEIVVDAVLAI 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 199 REG---------------RTLEDELEVTEGMRFDRGFISPyfiTDPKSSK----------VEFEKP--------LLLLSE 245
Cdd:cd03342 176 YKPdepidlhmveimqmqHKSDSDTKLIRGLVLDHGARHP---DMPKRVEnayiltcnvsLEYEKTevnsgffySVVINQ 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 246 KKISSiqdilPALeisnqsrrplliiaedvdgEALAACILNKLRgQVKvcavkapgfgdnRKNtIGDIAVLTGGTVFTEE 325
Cdd:cd03342 253 KGIDP-----PSL-------------------DMLAKEGILALR-RAK------------RRN-MERLTLACGGVAMNSV 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 326 LDLKPeqctiENLGSCDSITVTK--ED--TVILNGSGPKEAIQerieQIKGSiditttNSYEKEKLQErlaklsggvaVI 401
Cdd:cd03342 295 DDLSP-----ECLGYAGLVYERTlgEEkyTFIEGVKNPKSCTI----LIKGP------NDHTITQIKD----------AI 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 402 RvggasevevgekkdrydDALNATRAAVEEG-ILPGGGTALVKASRVLDEvVVDNFD--QKLGVDIIRKAITRPAKQIIE 478
Cdd:cd03342 350 R-----------------DGLRAVKNAIEDKcVVPGAGAFEVALYAHLKE-FKKSVKgkAKLGVQAFADALLVIPKTLAE 411
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6323288 479 NAGEEGSVIIGKLIDEYGDDFAK-GYDASKSEYTDMLATGIIDPFKVVRSGLVDASGVAS-LLATTEV 544
Cdd:cd03342 412 NSGLDVQETLVKLQDEYAEGGQVgGVDLDTGEPMDPESEGIWDNYSVKRQILHSATVIASqLLLVDEI 479
|
|
| chap_CCT_zeta |
TIGR02347 |
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ... |
38-152 |
2.35e-05 |
|
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT zeta chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.
Pssm-ID: 274088 [Multi-domain] Cd Length: 531 Bit Score: 47.04 E-value: 2.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 38 LKGVETLAEAVAATLGPKGRNVLIEQPFGPPKITKDGVTVAKSIVLKDKFENMGAKllqeVASKTNEAAGDGTTSATVLG 117
Cdd:TIGR02347 22 INAARGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEMQIQHPTASMIAR----AATAQDDITGDGTTSTVLLI 97
|
90 100 110
....*....|....*....|....*....|....*
gi 6323288 118 RAIFTESVKNVAAGCNPMDLRRGSQVAVEKVIEFL 152
Cdd:TIGR02347 98 GELLKQAERYILEGVHPRIITEGFEIARKEALQFL 132
|
|
| TCP1_alpha |
cd03335 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ... |
30-190 |
1.86e-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: 41.12 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 30 GVEGRASLLKGVETLAEAVAATLGPKGRNVLIEQPFGPPKITKDGVTVAKSIvlkdKFENMGAKLLQEVASKTNEAAGDG 109
Cdd:cd03335 6 GQDVRTQNVTAAMAIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLL----EVEHPAAKILVELAQLQDKEVGDG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323288 110 TTSATVLGRAIFTESVKNVAAGCNPMDLRRGSQVAVEKVIEFLSAN---KKEITTSEEIAQVA-------TISANGDsHV 179
Cdd:cd03335 82 TTSVVIIAAELLKRANELVKQKIHPTTIISGYRLACKEAVKYIKEHlsiSVDNLGKESLINVAktsmsskIIGADSD-FF 160
|
170
....*....|.
gi 6323288 180 GKLLASAMEKV 190
Cdd:cd03335 161 ANMVVDAILAV 171
|
|
| |
