|
Name |
Accession |
Description |
Interval |
E-value |
| TCP1_eta |
cd03340 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ... |
8-525 |
0e+00 |
|
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: 1032.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 8 PIVLLKEGTDTSQGLPQLISNINACCAIVDTVRTTLGPRGMDKLIYQSERQVTISNDGATVMKLLDIVHPAARTLVDIAK 87
Cdd:cd03340 1 PIILLKEGTDTSQGKGQLISNINACQAIADAVRTTLGPRGMDKLIVDGRGKVTISNDGATILKLLDIVHPAAKTLVDIAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 88 SQDSEVGDGTTSVVILAGEFLKAAKPFLEEGIHPQIIIRAFRSACELAKQKIQELSVDIK---PENMREFLEKCASTSMN 164
Cdd:cd03340 81 SQDAEVGDGTTSVVVLAGEFLKEAKPFIEDGVHPQIIIRGYRKALQLAIEKIKEIAVNIDkedKEEQRELLEKCAATALN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 165 SKLIASHKQFFSKMVVDAVQLLDDNIDLDMIGIKKESGGGLGDSQFIAGAAFKRTFFYAGFEQQPKHIKNPKVLCLNIEL 244
Cdd:cd03340 161 SKLIASEKEFFAKMVVDAVLSLDDDLDLDMIGIKKVPGGSLEDSQLVNGVAFKKTFSYAGFEQQPKKFKNPKILLLNVEL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 245 ELKAEKDNAEIRISDPTKYQSLVNAEWKLFFDKLEAIHASGVNVVLSKLAIGDLATQFFADKNMFCAGRVPDDDIRRVCR 324
Cdd:cd03340 241 ELKAEKDNAEVRVEDPEEYQAIVDAEWKIIYDKLEKIVKSGANVVLSKLPIGDLATQYFADRDIFCAGRVPEEDLKRVAQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 325 ATGAAIQNTTSNIIPDVIGTCDLFEEVQVGGQRYNLFTGCTMTQTATIILRGGGEQFIDEAERSLHDSIMIVRRARKHRS 404
Cdd:cd03340 321 ATGGSIQTTVSNITDDVLGTCGLFEERQVGGERYNIFTGCPKAKTCTIILRGGAEQFIEEAERSLHDAIMIVRRAIKNDS 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 405 VVAGGGAIEMEVSKYLRDYSLSIEGKKQLLINAFAKALEVIPRQIADNAGFDSTDILNQLRQKHAQGE-KWFGVDIVNEG 483
Cdd:cd03340 401 VVAGGGAIEMELSKYLRDYSRTIAGKQQLVINAFAKALEIIPRQLCDNAGFDATDILNKLRQKHAQGGgKWYGVDINNEG 480
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 66802602 484 ICDTYESAIWEPSLVKLNSIVAATEATCLILSVDETVQNNQA 525
Cdd:cd03340 481 IADNFEAFVWEPSLVKINALTAATEAACLILSVDETIKNPKS 522
|
|
| chap_CCT_eta |
TIGR02345 |
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ... |
6-525 |
0e+00 |
|
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: 846.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 6 RPPIVLLKEGTDTSQGLPQLISNINACCAIVDTVRTTLGPRGMDKLIYQSERQVTISNDGATVMKLLDIVHPAARTLVDI 85
Cdd:TIGR02345 1 RPTIVLLKEGTDTSQGKGQLISNINACVAIAEALKTTLGPRGMDKLIVGSNGKATISNDGATILKLLDIVHPAAKTLVDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 86 AKSQDSEVGDGTTSVVILAGEFLKAAKPFLEEGIHPQIIIRAFRSACELAKQKIQELSVDIKPEN--MREFLEKCASTSM 163
Cdd:TIGR02345 81 AKSQDAEVGDGTTSVTILAGELLKEAKPFIEEGVHPQLIIRCYREALSLAVEKIKEIAVTIDEEKgeQRELLEKCAATAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 164 NSKLIASHKQFFSKMVVDAVQLLDDN-IDLDMIGIKKESGGGLGDSQFIAGAAFKRTFFYAGFEQQPKHIKNPKVLCLNI 242
Cdd:TIGR02345 161 SSKLISHNKEFFSKMIVDAVLSLDRDdLDLKLIGIKKVQGGALEDSQLVNGVAFKKTFSYAGFEQQPKKFANPKILLLNV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 243 ELELKAEKDNAEIRISDPTKYQSLVNAEWKLFFDKLEAIHASGVNVVLSKLAIGDLATQFFADKNMFCAGRVPDDDIRRV 322
Cdd:TIGR02345 241 ELELKAEKDNAEIRVEDVEDYQAIVDAEWAIIFRKLEKIVESGANVVLSKLPIGDLATQYFADRDIFCAGRVSAEDLKRV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 323 CRATGAAIQNTTSNIIPDVIGTCDLFEEVQVGGQRYNLFTGCTMTQTATIILRGGGEQFIDEAERSLHDSIMIVRRARKH 402
Cdd:TIGR02345 321 IKACGGSIQSTTSDLEADVLGTCALFEERQIGSERYNYFTGCPHAKTCTIILRGGAEQFIEEAERSLHDAIMIVRRALKN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 403 RSVVAGGGAIEMEVSKYLRDYSLSIEGKKQLLINAFAKALEVIPRQIADNAGFDSTDILNQLRQKHAQGEKWFGVDIVNE 482
Cdd:TIGR02345 401 KKIVAGGGAIEMELSKCLRDYSKTIDGKQQLIINAFAKALEIIPRQLCENAGFDSIEILNKLRSRHAKGGKWYGVDINTE 480
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 66802602 483 GICDTYESAIWEPSLVKLNSIVAATEATCLILSVDETVQNNQA 525
Cdd:TIGR02345 481 DIGDNFEAFVWEPALVKINALKAAFEAACTILSVDETITNPKS 523
|
|
| chaperonin_type_I_II |
cd00309 |
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ... |
16-520 |
0e+00 |
|
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: 573.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 16 TDTSQGLPQLISNINACCAIVDTVRTTLGPRGMDKLIYQSERQVTISNDGATVMKLLDIVHPAARTLVDIAKSQDSEVGD 95
Cdd:cd00309 1 KEREFGEEARLSNINAAKALADAVKTTLGPKGMDKMLVDSLGDPTITNDGATILKEIEVEHPAAKLLVEVAKSQDDEVGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 96 GTTSVVILAGEFLKAAKPFLEEGIHPQIIIRAFRSACELAKQKIQELSVDIKPENmREFLEKCASTSMNSKLIASHKQFF 175
Cdd:cd00309 81 GTTTVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVPIDVED-REELLKVATTSLNSKLVSGGDDFL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 176 SKMVVDAVQLL---DDNIDLDMIGIKKESGGGLGDSQFIAGAAFKRTFFYAGFeqqPKHIKNPKVLCLNIELElkaekdn 252
Cdd:cd00309 160 GELVVDAVLKVgkeNGDVDLGVIRVEKKKGGSLEDSELVVGMVFDKGYLSPYM---PKRLENAKILLLDCKLE------- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 253 aeirisdptkyqslvnaewklffdkleaihasgvNVVLSKLAIGDLATQFFADKNMFCAGRVPDDDIRRVCRATGAAIQN 332
Cdd:cd00309 230 ----------------------------------YVVIAEKGIDDEALHYLAKLGIMAVRRVRKEDLERIAKATGATIVS 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 333 TTSNIIPDVIGTCDLFEEVQVGGQRYNLFTGCTMTQTATIILRGGGEQFIDEAERSLHDSIMIVRRARKHRSVVAGGGAI 412
Cdd:cd00309 276 RLEDLTPEDLGTAGLVEETKIGDEKYTFIEGCKGGKVATILLRGATEVELDEAERSLHDALCAVRAAVEDGGIVPGGGAA 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 413 EMEVSKYLRDYSLSIEGKKQLLINAFAKALEVIPRQIADNAGFDSTDILNQLRQKHAQGEKWFGVDIVNEGICDTYESAI 492
Cdd:cd00309 356 EIELSKALEELAKTLPGKEQLGIEAFADALEVIPRTLAENAGLDPIEVVTKLRAKHAEGGGNAGGDVETGEIVDMKEAGI 435
|
490 500
....*....|....*....|....*...
gi 66802602 493 WEPSLVKLNSIVAATEATCLILSVDETV 520
Cdd:cd00309 436 IDPLKVKRQALKSATEAASLILTIDDII 463
|
|
| Cpn60_TCP1 |
pfam00118 |
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ... |
35-520 |
0e+00 |
|
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: 547.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 35 IVDTVRTTLGPRGMDKLIYQSERQVTISNDGATVMKLLDIVHPAARTLVDIAKSQDSEVGDGTTSVVILAGEFLKAAKPF 114
Cdd:pfam00118 1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELEIQHPAAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEEAEKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 115 LEEGIHPQIIIRAFRSACELAKQKIQE-LSVDIKPENmREFLEKCASTSMNSKLIASHKQFFSKMVVDAVQLLDDN---I 190
Cdd:pfam00118 81 LAAGVHPTTIIEGYEKALEKALEILDSiISIPVEDVD-REDLLKVARTSLSSKIISRESDFLAKLVVDAVLAIPKNdgsF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 191 DLDMIGIKKESGGGLGDSQFIAGAAFKRTFFYagfEQQPKHIKNPKVLCLNIELELKAEKDNAEIRISDPTKYQSLVNAE 270
Cdd:pfam00118 160 DLGNIGVVKILGGSLEDSELVDGVVLDKGPLH---PDMPKRLENAKVLLLNCSLEYEKTETKATVVLSDAEQLERFLKAE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 271 WKLFFDKLEAIHASGVNVVLSKLAIGDLATQFFADKNMFCAGRVPDDDIRRVCRATGAAIQNTTSNIIPDVIGTCDLFEE 350
Cdd:pfam00118 237 EEQILEIVEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMALRRVKKRDLERLAKATGARAVSSLDDLTPDDLGTAGKVEE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 351 VQVGGQRYNLFTGCTMTQTATIILRGGGEQFIDEAERSLHDSIMIVRRARKHRSVVAGGGAIEMEVSKYLRDYSLSIEGK 430
Cdd:pfam00118 317 EKIGDEKYTFIEGCKSPKAATILLRGATDHVLDEIERSIHDALCVVKNAIEDPRVVPGGGAVEMELARALREYAKSVSGK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 431 KQLLINAFAKALEVIPRQIADNAGFDSTDILNQLRQKHAQGEKWFGVDIVNEGICDTYESAIWEPSLVKLNSIVAATEAT 510
Cdd:pfam00118 397 EQLAIEAFAEALEVIPKTLAENAGLDPIEVLAELRAAHASGEKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKSATEAA 476
|
490
....*....|
gi 66802602 511 CLILSVDETV 520
Cdd:pfam00118 477 STILRIDDII 486
|
|
| thermosome_beta |
NF041083 |
thermosome subunit beta; |
8-518 |
2.86e-170 |
|
thermosome subunit beta;
Pssm-ID: 469010 Cd Length: 519 Bit Score: 492.54 E-value: 2.86e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 8 PIVLLKEGTDTSQGLPQLISNINACCAIVDTVRTTLGPRGMDKLIYQSERQVTISNDGATVMKLLDIVHPAARTLVDIAK 87
Cdd:NF041083 2 PVLILKEGTQRTKGRDAQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDIVITNDGATILKEMDVQHPAAKMLVEVAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 88 SQDSEVGDGTTSVVILAGEFLKAAKPFLEEGIHPQIIIRAFRSACELAKQKIQELSVDIKPENmREFLEKCASTSMNSKL 167
Cdd:NF041083 82 TQDDEVGDGTTTAVVLAGELLKKAEELLDQNIHPTIIANGYRLAAEKAIEILDEIAEKVDPDD-RETLKKIAETSLTSKG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 168 IASHKQFFSKMVVDAVQLLDD------NIDLDMIGIKKESGGGLGDSQFIAGAAFKRTFFYAGFeqqPKHIKNPKVLCLN 241
Cdd:NF041083 161 VEEARDYLAEIAVKAVKQVAEkrdgkyYVDLDNIQIEKKHGGSIEDTQLIYGIVIDKEVVHPGM---PKRVENAKIALLD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 242 IELELKAEKDNAEIRISDPTKYQSLVNAEWKLFFDKLEAIHASGVNVVLSKLAIGDLATQFFADKNMFCAGRVPDDDIRR 321
Cdd:NF041083 238 APLEVKKTEIDAEIRITDPDQLQKFLDQEEKMLKEMVDKIKATGANVVFCQKGIDDLAQHYLAKAGILAVRRVKKSDMEK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 322 VCRATGAAIQNTTSNIIPDVIGTCDLFEEVQVGGQRYNLFTGCTMTQTATIILRGGGEQFIDEAERSLHDSIMIVRRARK 401
Cdd:NF041083 318 LAKATGARIVTNIDDLTPEDLGYAELVEERKVGDDKMVFVEGCKNPKAVTILIRGGTEHVVDEAERALEDALSVVADAVE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 402 HRSVVAGGGAIEMEVSKYLRDYSLSIEGKKQLLINAFAKALEVIPRQIADNAGFDSTDILNQLRQKHAQGEKWFGVDIVN 481
Cdd:NF041083 398 DGKIVAGGGAPEVELAKRLREYAATVGGREQLAVEAFAEALEIIPRTLAENAGLDPIDILVKLRSAHEKGKKWAGINVFT 477
|
490 500 510
....*....|....*....|....*....|....*..
gi 66802602 482 EGICDTYESAIWEPSLVKLNSIVAATEATCLILSVDE 518
Cdd:NF041083 478 GEVVDMWELGVIEPLRVKTQAIKSATEAATMILRIDD 514
|
|
| thermosome_alpha |
NF041082 |
thermosome subunit alpha; |
8-517 |
1.20e-166 |
|
thermosome subunit alpha;
Pssm-ID: 469009 Cd Length: 518 Bit Score: 483.23 E-value: 1.20e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 8 PIVLLKEGTDTSQGLPQLISNINACCAIVDTVRTTLGPRGMDKLIYQSERQVTISNDGATVMKLLDIVHPAARTLVDIAK 87
Cdd:NF041082 2 PILILKEGTQRTSGRDAQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDVVITNDGVTILKEMDIEHPAAKMIVEVAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 88 SQDSEVGDGTTSVVILAGEFLKAAKPFLEEGIHPQIIIRAFRSACELAKQKIQELSVDIKPENmREFLEKCASTSMNSKL 167
Cdd:NF041082 82 TQDDEVGDGTTTAVVLAGELLKKAEELLDQDIHPTIIAEGYRLAAEKALEILDEIAIKVDPDD-KETLKKIAATAMTGKG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 168 IASHKQFFSKMVVDAVQLLDD-----NIDLDMIGIKKESGGGLGDSQFIAGAAFKRTFFYAGFeqqPKHIKNPKVLCLNI 242
Cdd:NF041082 161 AEAAKDKLADLVVDAVKAVAEkdggyNVDLDNIKVEKKVGGSIEDSELVEGVVIDKERVHPGM---PKRVENAKIALLDA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 243 ELELKAEKDNAEIRISDPTKYQSLVNAEWKLFFDKLEAIHASGVNVVLSKLAIGDLATQFFADKNMFCAGRVPDDDIRRV 322
Cdd:NF041082 238 PLEVKKTEIDAKISITDPDQLQAFLDQEEKMLKEMVDKIADSGANVVFCQKGIDDLAQHYLAKEGILAVRRVKKSDMEKL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 323 CRATGAAIQNTTSNIIPDVIGTCDLFEEVQVGGQRYNLFTGCTMTQTATIILRGGGEQFIDEAERSLHDSIMIVRRARKH 402
Cdd:NF041082 318 AKATGARIVTSIDDLSPEDLGYAGLVEERKVGGDKMIFVEGCKNPKAVTILLRGGTEHVVDEVERALEDALRVVRVVLED 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 403 RSVVAGGGAIEMEVSKYLRDYSLSIEGKKQLLINAFAKALEVIPRQIADNAGFDSTDILNQLRQKHAQGEKWFGVDIVNE 482
Cdd:NF041082 398 GKVVAGGGAPEVELALRLREYAASVGGREQLAIEAFAEALEIIPRTLAENAGLDPIDALVELRSAHEKGNKTAGLDVYTG 477
|
490 500 510
....*....|....*....|....*....|....*
gi 66802602 483 GICDTYESAIWEPSLVKLNSIVAATEATCLILSVD 517
Cdd:NF041082 478 KVVDMLEIGVVEPLRVKTQAIKSATEAAVMILRID 512
|
|
| cpn60 |
cd03343 |
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ... |
9-518 |
1.43e-166 |
|
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: 482.92 E-value: 1.43e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 9 IVLLKEGTDTSQGLPQLISNINACCAIVDTVRTTLGPRGMDKLIYQSERQVTISNDGATVMKLLDIVHPAARTLVDIAKS 88
Cdd:cd03343 1 VLILKEGTQRTSGRDAQRMNIAAAKAVAEAVRTTLGPKGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 89 QDSEVGDGTTSVVILAGEFLKAAKPFLEEGIHPQIIIRAFRSACELAKQKIQELSVDIKPENmREFLEKCASTSMNSKLI 168
Cdd:cd03343 81 QDEEVGDGTTTAVVLAGELLEKAEDLLDQNIHPTVIIEGYRLAAEKALELLDEIAIKVDPDD-KDTLRKIAKTSLTGKGA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 169 ASHKQFFSKMVVDAVQLLDD------NIDLDMIGIKKESGGGLGDSQFIAGAAFKRTFFYagfEQQPKHIKNPKVLCLNI 242
Cdd:cd03343 160 EAAKDKLADLVVDAVLQVAEkrdgkyVVDLDNIKIEKKTGGSVDDTELIRGIVIDKEVVH---PGMPKRVENAKIALLDA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 243 ELELKAEKDNAEIRISDPTKYQSLVNAEWKLFFDKLEAIHASGVNVVLSKLAIGDLATQFFADKNMFCAGRVPDDDIRRV 322
Cdd:cd03343 237 PLEVKKTEIDAKIRITSPDQLQAFLEQEEAMLKEMVDKIADTGANVVFCQKGIDDLAQHYLAKAGILAVRRVKKSDMEKL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 323 CRATGAAIQNTTSNIIPDVIGTCDLFEEVQVGGQRYNLFTGCTMTQTATIILRGGGEQFIDEAERSLHDSIMIVRRARKH 402
Cdd:cd03343 317 ARATGAKIVTNIDDLTPEDLGEAELVEERKVGDDKMVFVEGCKNPKAVTILLRGGTEHVVDELERALEDALRVVADALED 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 403 RSVVAGGGAIEMEVSKYLRDYSLSIEGKKQLLINAFAKALEVIPRQIADNAGFDSTDILNQLRQKHAQGEKWFGVDIVNE 482
Cdd:cd03343 397 GKVVAGGGAVEIELAKRLREYARSVGGREQLAVEAFADALEEIPRTLAENAGLDPIDTLVELRAAHEKGNKNAGLDVYTG 476
|
490 500 510
....*....|....*....|....*....|....*.
gi 66802602 483 GICDTYESAIWEPSLVKLNSIVAATEATCLILSVDE 518
Cdd:cd03343 477 EVVDMLEKGVIEPLRVKKQAIKSATEAATMILRIDD 512
|
|
| thermosome_arch |
TIGR02339 |
thermosome, various subunits, archaeal; Thermosome is the name given to the archaeal rather ... |
8-520 |
1.15e-161 |
|
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: 470.32 E-value: 1.15e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 8 PIVLLKEGTDTSQGLPQLISNINACCAIVDTVRTTLGPRGMDKLIYQSERQVTISNDGATVMKLLDIVHPAARTLVDIAK 87
Cdd:TIGR02339 1 PVFILKEGTQRTSGRDAQRNNIAAAKAVAEAVKSTLGPRGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 88 SQDSEVGDGTTSVVILAGEFLKAAKPFLEEGIHPQIIIRAFRSACELAKQKIQELSVDIKPENmREFLEKCASTSMNSKL 167
Cdd:TIGR02339 81 TQDEEVGDGTTTAVVLAGELLEKAEDLLEQDIHPTVIIEGYRKAAEKALEIIDEIATKISPED-RDLLKKIAYTSLTSKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 168 IASH-KQFFSKMVVDAV----QLLDD---NIDLDMIGIKKESGGGLGDSQFIAGAAFKRTFFYAGFeqqPKHIKNPKVLC 239
Cdd:TIGR02339 160 SAEVaKDKLADLVVEAVkqvaELRGDgkyYVDLDNIKIVKKKGGSIEDTELVEGIVVDKEVVHPGM---PKRVENAKIAL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 240 LNIELELKAEKDNAEIRISDPTKYQSLVNAEWKLFFDKLEAIHASGVNVVLSKLAIGDLATQFFADKNMFCAGRVPDDDI 319
Cdd:TIGR02339 237 LDAPLEVEKTEIDAKIRITDPDQIKKFLDQEEAMLKEMVDKIASAGANVVICQKGIDDVAQHYLAKAGILAVRRVKKSDI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 320 RRVCRATGAAIQNTTSNIIPDVIGTCDLFEEVQVGGQRYNLFTGCTMTQTATIILRGGGEQFIDEAERSLHDSIMIVRRA 399
Cdd:TIGR02339 317 EKLARATGARIVSSIDEITESDLGYAELVEERKVGEDKMVFVEGCKNPKAVTILLRGGTEHVVDELERSIQDALHVVANA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 400 RKHRSVVAGGGAIEMEVSKYLRDYSLSIEGKKQLLINAFAKALEVIPRQIADNAGFDSTDILNQLRQKHAQGEKWFGVDI 479
Cdd:TIGR02339 397 LEDGKIVAGGGAVEIELALRLRSYARSVGGREQLAIEAFADALEEIPRILAENAGLDPIDALVDLRAKHEKGNKNAGINV 476
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 66802602 480 VNEGICDTYESAIWEPSLVKLNSIVAATEATCLILSVDETV 520
Cdd:TIGR02339 477 FTGEIEDMLELGVIEPLRVKEQAIKSATEAATMILRIDDVI 517
|
|
| TCP1_alpha |
cd03335 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ... |
28-518 |
2.01e-138 |
|
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: 411.29 E-value: 2.01e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 28 NINACCAIVDTVRTTLGPRGMDKLIYQSERQVTISNDGATVMKLLDIVHPAARTLVDIAKSQDSEVGDGTTSVVILAGEF 107
Cdd:cd03335 13 NVTAAMAIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDKEVGDGTTSVVIIAAEL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 108 LKAAKPFLEEGIHPQIIIRAFRSACELAKQKIQElSVDIKPENM-REFLEKCASTSMNSKLIASHKQFFSKMVVDA---V 183
Cdd:cd03335 93 LKRANELVKQKIHPTTIISGYRLACKEAVKYIKE-HLSISVDNLgKESLINVAKTSMSSKIIGADSDFFANMVVDAilaV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 184 QLLDDNID----LDMIGIKKESGGGLGDSQFIAGAAFKRTffyAGFEQQPKHIKNPKVLCLNIELELKAEKDNAEIRISD 259
Cdd:cd03335 172 KTTNEKGKtkypIKAVNILKAHGKSAKESYLVNGYALNCT---RASQGMPTRVKNAKIACLDFNLQKTKMKLGVQVVVTD 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 260 PTKYQSLVNAEWKLFFDKLEAIHASGVNVVLSKLAIGDLATQFFADKNMFCAGRVPDDDIRRVCRATGAAIQNTTSNII- 338
Cdd:cd03335 249 PEKLEKIRQRESDITKERIKKILAAGANVVLTTGGIDDMCLKYFVEAGAMAVRRVKKEDLRRIAKATGATLVSTLANLEg 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 339 -----PDVIGTCDLFEEVQVGGQRYNLFTGCTMTQTATIILRGGGEQFIDEAERSLHDSIMIVRRARKHRSVVAGGGAIE 413
Cdd:cd03335 329 eetfdPSYLGEAEEVVQERIGDDELILIKGTKKRSSASIILRGANDFMLDEMERSLHDALCVVKRTLESNSVVPGGGAVE 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 414 MEVSKYLRDYSLSIEGKKQLLINAFAKALEVIPRQIADNAGFDSTDILNQLRQKHA--------QGEKWFGVDIVNEGIC 485
Cdd:cd03335 409 TALSIYLENFATTLGSREQLAIAEFAEALLVIPKTLAVNAAKDATELVAKLRAYHAaaqvkpdkKHLKWYGLDLINGKVR 488
|
490 500 510
....*....|....*....|....*....|...
gi 66802602 486 DTYESAIWEPSLVKLNSIVAATEATCLILSVDE 518
Cdd:cd03335 489 DNLEAGVLEPTVSKIKSLKFATEAAITILRIDD 521
|
|
| chap_CCT_alpha |
TIGR02340 |
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ... |
28-527 |
1.23e-131 |
|
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: 394.47 E-value: 1.23e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 28 NINACCAIVDTVRTTLGPRGMDKLIYQSERQVTISNDGATVMKLLDIVHPAARTLVDIAKSQDSEVGDGTTSVVILAGEF 107
Cdd:TIGR02340 17 NVTAAMAIANIVKTSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDREVGDGTTSVVIIAAEL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 108 LKAAKPFLEEGIHPQIIIRAFRSACELAKQKIQElSVDIKPENM-REFLEKCASTSMNSKLIASHKQFFSKMVVDA---V 183
Cdd:TIGR02340 97 LKRADELVKNKIHPTSVISGYRLACKEAVKYIKE-NLSVSVDELgREALINVAKTSMSSKIIGLDSDFFSNIVVDAvlaV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 184 QLLDDNID----LDMIGIKKESGGGLGDSQFIAGAAFKRTffyAGFEQQPKHIKNPKVLCLNIELELKAEKDNAEIRISD 259
Cdd:TIGR02340 176 KTTNENGEtkypIKAINILKAHGKSARESMLVKGYALNCT---VASQQMPKRIKNAKIACLDFNLQKAKMALGVQIVVDD 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 260 PTKYQSLVNAEWKLFFDKLEAIHASGVNVVLSKLAIGDLATQFFADKNMFCAGRVPDDDIRRVCRATGAAIQNTTSNI-- 337
Cdd:TIGR02340 253 PEKLEQIRQREADITKERIKKILDAGANVVLTTGGIDDMCLKYFVEAGAMGVRRCKKEDLKRIAKATGATLVSTLADLeg 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 338 ----IPDVIGTCDLFEEVQVGGQRYNLFTGCTMTQTATIILRGGGEQFIDEAERSLHDSIMIVRRARKHRSVVAGGGAIE 413
Cdd:TIGR02340 333 eetfEASYLGFADEVVQERIADDECILIKGTKKRKSASIILRGANDFMLDEMERSLHDALCVVKRTLESNSVVPGGGAVE 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 414 MEVSKYLRDYSLSIEGKKQLLINAFAKALEVIPRQIADNAGFDSTDILNQLRQKHA--------QGEKWFGVDIVNEGIC 485
Cdd:TIGR02340 413 AALSIYLENFATTLGSREQLAIAEFARALLIIPKTLAVNAAKDSTELVAKLRAYHAaaqlkpekKHLKWYGLDLVNGKIR 492
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 66802602 486 DTYESAIWEPSLVKLNSIVAATEATCLILSVDETVQNNQAEQ 527
Cdd:TIGR02340 493 DNKEAGVLEPTVSKVKSLKFATEAAITILRIDDLIKLNPEQS 534
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
12-522 |
1.48e-131 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 394.01 E-value: 1.48e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 12 LKEGTDTSQGLPQLISNINACCAIVDTVRTTLGPRGMDKLI-----YQSERQVTISNDGATVMKLLDIVHPAARTLVDIA 86
Cdd:PTZ00212 11 LKQGAQEEKGETARLQSFVGAIAVADLVKTTLGPKGMDKILqpmseGPRSGNVTVTNDGATILKSVWLDNPAAKILVDIS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 87 KSQDSEVGDGTTSVVILAGEFLKAAKPFLEEGIHPQIIIRAFRSACELAKQKIQELSVD--IKPENMREFLEKCASTSMN 164
Cdd:PTZ00212 91 KTQDEEVGDGTTSVVVLAGELLREAEKLLDQKIHPQTIIEGWRMALDVARKALEEIAFDhgSDEEKFKEDLLNIARTTLS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 165 SKLIASHKQFFSKMVVDAVQLLDDNIDLDMIGIKKESGGGLGDSQFIAGAAFKRTFFYAgfeqQPKHIKNPKVLCLNIEL 244
Cdd:PTZ00212 171 SKLLTVEKDHFAKLAVDAVLRLKGSGNLDYIQIIKKPGGTLRDSYLEDGFILEKKIGVG----QPKRLENCKILVANTPM 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 245 EL-KAEKDNAEIRISDPTKYQSLVNAEWKLFFDKLEAIHASGVNVVLSKLAIGDLATQFFADKNMFCAGRVPDDDIRRVC 323
Cdd:PTZ00212 247 DTdKIKIYGAKVKVDSMEKVAEIEAAEKEKMKNKVDKILAHGCNVFINRQLIYNYPEQLFAEAGIMAIEHADFDGMERLA 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 324 RATGAAIQNTTSNIIPDVIGTCDLFEEVQVGGQRYNLFTGCTMTQTATIILRGGGEQFIDEAERSLHDSIMIVRRARKHR 403
Cdd:PTZ00212 327 AALGAEIVSTFDTPEKVKLGHCDLIEEIMIGEDKLIRFSGCAKGEACTIVLRGASTHILDEAERSLHDALCVLSQTVKDT 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 404 SVVAGGGAIEMEVSKYLRDYSLSIEGKKQLLINAFAKALEVIPRQIADNAGFDSTDILNQLRQKHAQGEKWFGVDIVNEG 483
Cdd:PTZ00212 407 RVVLGGGCSEMLMANAVEELAKKVEGKKSLAIEAFAKALRQIPTIIADNGGYDSAELVSKLRAEHYKGNKTAGIDMEKGT 486
|
490 500 510
....*....|....*....|....*....|....*....
gi 66802602 484 ICDTYESAIWEPSLVKLNSIVAATEATCLILSVDETVQN 522
Cdd:PTZ00212 487 VGDMKELGITESYKVKLSQLCSATEAAEMILRVDDIIRC 525
|
|
| TCP1_delta |
cd03338 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ... |
27-520 |
1.48e-131 |
|
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: 393.19 E-value: 1.48e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 27 SNINACCAIVDTVRTTLGPRGMDKLIYQSERQVTISNDGATVMKLLDIVHPAARTLVDIAKSQDSEVGDGTTSVVILAGE 106
Cdd:cd03338 12 SNIQAAKAVADAIRTSLGPRGMDKMIQTGKGEVIITNDGATILKQMSVLHPAAKMLVELSKAQDIEAGDGTTSVVVLAGA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 107 FLKAAKPFLEEGIHPQIIIRAFRSACELAKQKIQELSVDIKPENmREFLEKCASTSMNSKLIASHKQFFSKMVVDAVQLL 186
Cdd:cd03338 92 LLSACESLLKKGIHPTVISESFQIAAKKAVEILDSMSIPVDLND-RESLIKSATTSLNSKVVSQYSSLLAPIAVDAVLKV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 187 DD-----NIDLDMIGIKKESGGGLGDSQFIAGAAFKRTFFYAGfeQQPKHIKNPKVLClnIELELKAEKDNAE--IRISD 259
Cdd:cd03338 171 IDpatatNVDLKDIRIVKKLGGTIEDTELVDGLVFTQKASKKA--GGPTRIEKAKIGL--IQFCLSPPKTDMDnnIVVND 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 260 PTKYQSLVNAEWKLFFDKLEAIHASGVNVVL---SKL--AIGDLATQFFADKNMFCAGRVPDDDIRRVCRATGAAIQNTT 334
Cdd:cd03338 247 YAQMDRILREERKYILNMCKKIKKSGCNVLLiqkSILrdAVSDLALHFLAKLKIMVVKDIEREEIEFICKTIGCKPVASI 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 335 SNIIPDVIGTCDLFEEVQVGGQRYNLFTGCTMT-QTATIILRGGGEQFIDEAERSLHDSIMIVRRARKHRSVVAGGGAIE 413
Cdd:cd03338 327 DHFTEDKLGSADLVEEVSLGDGKIVKITGVKNPgKTVTILVRGSNKLVLDEAERSLHDALCVIRCLVKKRALIPGGGAPE 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 414 MEVSKYLRDYSLSIEGKKQLLINAFAKALEVIPRQIADNAGFDSTDILNQLRQKHAQGEKWFGVDIVNEGICDTYESAIW 493
Cdd:cd03338 407 IEIALQLSEWARTLTGVEQYCVRAFADALEVIPYTLAENAGLNPISIVTELRNRHAQGEKNAGINVRKGAITNILEENVV 486
|
490 500
....*....|....*....|....*..
gi 66802602 494 EPSLVKLNSIVAATEATCLILSVDETV 520
Cdd:cd03338 487 QPLLVSTSAITLATETVRMILKIDDIV 513
|
|
| TCP1_beta |
cd03336 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ... |
12-521 |
9.01e-130 |
|
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: 389.00 E-value: 9.01e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 12 LKEGTDTSQGLPQLISNINACCAIVDTVRTTLGPRGMDKlIYQS---ERQVTISNDGATVMKLLDIVHPAARTLVDIAKS 88
Cdd:cd03336 2 LKDGAQEEKGETARLSSFVGAIAIGDLVKTTLGPKGMDK-ILQSvgrSGGVTVTNDGATILKSIGVDNPAAKVLVDISKV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 89 QDSEVGDGTTSVVILAGEFLKAAKPFLEEGIHPQIIIRAFRSACELAKQKIQELSVDIK--PENMREFLEKCASTSMNSK 166
Cdd:cd03336 81 QDDEVGDGTTSVTVLAAELLREAEKLVAQKIHPQTIIEGYRMATAAAREALLSSAVDHSsdEEAFREDLLNIARTTLSSK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 167 LIASHKQFFSKMVVDAVQLLDDNIDLDMIGIKKESGGGLGDSQFIAGAAFKRTFFYAgfeqQPKHIKNPKVLCLNIELEL 246
Cdd:cd03336 161 ILTQDKEHFAELAVDAVLRLKGSGNLDAIQIIKKLGGSLKDSYLDEGFLLDKKIGVN----QPKRIENAKILIANTPMDT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 247 -KAEKDNAEIRISDPTKYQSLVNAEWKLFFDKLEAIHASGVNVVLSKLAIGDLATQFFADKNMFCAGRVPDDDIRRVCRA 325
Cdd:cd03336 237 dKIKIFGAKVRVDSTAKVAEIEEAEKEKMKNKVEKILKHGINCFINRQLIYNYPEQLFADAGIMAIEHADFDGVERLALV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 326 TGAAIQNTTSNIIPDVIGTCDLFEEVQVGGQRYNLFTGCTMTQTATIILRGGGEQFIDEAERSLHDSIMIVRRARKHRSV 405
Cdd:cd03336 317 TGGEIASTFDHPELVKLGTCKLIEEIMIGEDKLIRFSGVAAGEACTIVLRGASQQILDEAERSLHDALCVLAQTVKDTRV 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 406 VAGGGAIEMEVSKYLRDYSLSIEGKKQLLINAFAKALEVIPRQIADNAGFDSTDILNQLRQKHAQGEKWFGVDIVNEGIC 485
Cdd:cd03336 397 VLGGGCSEMLMAKAVEELAKKTPGKKSLAIEAFAKALRQLPTIIADNAGYDSAELVAQLRAAHYNGNTTAGLDMRKGTVG 476
|
490 500 510
....*....|....*....|....*....|....*.
gi 66802602 486 DTYESAIWEPSLVKLNSIVAATEATCLILSVDETVQ 521
Cdd:cd03336 477 DMKELGITESFKVKRQVLLSASEAAEMILRVDDIIK 512
|
|
| chap_CCT_delta |
TIGR02342 |
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ... |
27-520 |
1.20e-123 |
|
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: 373.35 E-value: 1.20e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 27 SNINACCAIVDTVRTTLGPRGMDKLIYQSERQVTISNDGATVMKLLDIVHPAARTLVDIAKSQDSEVGDGTTSVVILAGE 106
Cdd:TIGR02342 13 SNIVAAKAVADAIRTSLGPKGMDKMIQDGKGEVIITNDGATILKQMAVLHPAAKMLVELSKAQDIEAGDGTTSVVILAGA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 107 FLKAAKPFLEEGIHPQIIIRAFRSACELAKQKIQELSVDIKPENmREFLEKCASTSMNSKLIASHKQFFSKMVVDAVQLL 186
Cdd:TIGR02342 93 LLGACERLLNKGIHPTIISESFQSAADEAIKILDEMSIPVDLSD-REQLLKSATTSLSSKVVSQYSSLLAPLAVDAVLKV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 187 DD-----NIDLDMIGIKKESGGGLGDSQFIAGAAFKRTFFYAgfEQQPKHIKNPKVLClnIELELKAEKDNAE--IRISD 259
Cdd:TIGR02342 172 IDpenakNVDLNDIKVVKKLGGTIDDTELIEGLVFTQKASKS--AGGPTRIEKAKIGL--IQFQISPPKTDMEnqIIVND 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 260 PTKYQSLVNAEWKLFFDKLEAIHASGVNVVL---SKL--AIGDLATQFFADKNMFCAGRVPDDDIRRVCRATGAAIQNTT 334
Cdd:TIGR02342 248 YAQMDRVLKEERAYILNIVKKIKKTGCNVLLiqkSILrdAVNDLALHFLAKMKIMVVKDIEREEIEFICKTIGCKPIASI 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 335 SNIIPDVIGTCDLFEEVQVGGQRYNLFTGC-TMTQTATIILRGGGEQFIDEAERSLHDSIMIVRRARKHRSVVAGGGAIE 413
Cdd:TIGR02342 328 DHFTADKLGSAELVEEVDSDGGKIIKITGIqNAGKTVTVVVRGSNKLVIDEAERSLHDALCVIRCLVKKRGLIAGGGAPE 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 414 MEVSKYLRDYSLSIEGKKQLLINAFAKALEVIPRQIADNAGFDSTDILNQLRQKHAQGEKWFGVDIVNEGICDTYESAIW 493
Cdd:TIGR02342 408 IEIARRLSKYARTMKGVESYCVRAFADALEVIPYTLAENAGLNPIKVVTELRNRHANGEKTAGISVRKGGITNMLEEHVL 487
|
490 500
....*....|....*....|....*..
gi 66802602 494 EPSLVKLNSIVAATEATCLILSVDETV 520
Cdd:TIGR02342 488 QPLLVTTSAITLASETVRSILKIDDIV 514
|
|
| TCP1_gamma |
cd03337 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ... |
8-520 |
2.12e-120 |
|
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.
Pssm-ID: 239453 [Multi-domain] Cd Length: 480 Bit Score: 363.54 E-value: 2.12e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 8 PIVLLKEGTDTSQGLPQLISNINACCAIVDTVRTTLGPRGMDKLIYQSERQVTISNDGATVMKLLDIVHPAARTLVDIAK 87
Cdd:cd03337 1 PVLVLNQNTKRESGRKAQLGNIQAAKTVADVIRTCLGPRAMLKMLLDPMGGIVLTNDGNAILREIDVAHPAAKSMIELSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 88 SQDSEVGDGTTSVVILAGEFLKAAKPFLEEGIHPQIIIRAFRSACELAKQKIQELSVDIKPENmREFLEKCASTSMNSKL 167
Cdd:cd03337 81 TQDEEVGDGTTSVIILAGEILAVAEPFLERGIHPTVIIKAYRKALEDALKILEEISIPVDVND-RAQMLKIIKSCIGTKF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 168 IASHKQFFSKMVVDAVQL--LDDNIDLDMIGIK------KESGGGLGDSQFIAGAAFKRTFFYAGFEqqpKHIKNPKVLC 239
Cdd:cd03337 160 VSRWSDLMCNLALDAVKTvaVEENGRKKEIDIKryakveKIPGGEIEDSRVLDGVMLNKDVTHPKMR---RRIENPRIVL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 240 LNIELElkaekdnaeirisdptkYqslvnaewklffdkleaihasgvnVVLSKLAIGDLATQFFADKNMFCAGRVPDDDI 319
Cdd:cd03337 237 LDCPLE-----------------Y------------------------LVITEKGVSDLAQHYLVKAGITALRRVRKTDN 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 320 RRVCRATGAAIQNTTSNIIPDVIGTCDLFEEVQVGGQRY-NLFTGCTMTQTATIILRGGGEQFIDEAERSLHDSIMIVRR 398
Cdd:cd03337 276 NRIARACGATIVNRPEELTESDVGTGAGLFEVKKIGDEYfTFITECKDPKACTILLRGASKDVLNEVERNLQDAMAVARN 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 399 ARKHRSVVAGGGAIEMEVSKYLRDYSLSIEGKKQLLINAFAKALEVIPRQIADNAGFDSTDILNQLRQKHAQGEK-WFGV 477
Cdd:cd03337 356 IILNPKLVPGGGATEMAVSHALSEKAKSIEGVEQWPYKAVASALEVIPRTLAQNCGANVIRTLTELRAKHAQGENsTWGI 435
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 66802602 478 DIVNEGICDTYESAIWEPSLVKLNSIVAATEATCLILSVDETV 520
Cdd:cd03337 436 DGETGDIVDMKELGIWDPLAVKAQTYKTAIEAACMLLRIDDIV 478
|
|
| chap_CCT_gamma |
TIGR02344 |
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ... |
8-520 |
1.77e-115 |
|
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: 352.50 E-value: 1.77e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 8 PIVLLKEGTDTSQGLPQLISNINACCAIVDTVRTTLGPRGMDKLIYQSERQVTISNDGATVMKLLDIVHPAARTLVDIAK 87
Cdd:TIGR02344 1 PVLVLNQNTKRESGRKAQLSNIQAAKAVADIIRTCLGPRSMLKMLLDPMGGIVMTNDGNAILREIDVAHPAAKSMIELSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 88 SQDSEVGDGTTSVVILAGEFLKAAKPFLEEGIHPQIIIRAFRSACELAKQKIQELSVDIKPENmREFLEKCASTSMNSKL 167
Cdd:TIGR02344 81 TQDEEVGDGTTSVIILAGEMLSVAEPFLEQNIHPTVIIRAYRKALDDALSVLEEISIPVDVND-DAAMLKLIQSCIGTKF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 168 IASHKQFFSKMVVDAVQ--LLDDN----IDLD-MIGIKKESGGGLGDSQFIAGAAFKRTFFYagfeqqPK---HIKNPKV 237
Cdd:TIGR02344 160 VSRWSDLMCDLALDAVRtvQRDENgrkeIDIKrYAKVEKIPGGDIEDSCVLKGVMINKDVTH------PKmrrYIENPRI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 238 LCLNIELELKAEKDNAEIRISDPTKYQSLVNAEWKLFFDKLEAIHASGVNVVLSKLAIGDLATQFFADKNMFCAGRVPDD 317
Cdd:TIGR02344 234 VLLDCPLEYKKGESQTNIEITKEEDWNRILQMEEEYVQLMCEDIIAVKPDLVITEKGVSDLAQHYLLKANITAIRRVRKT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 318 DIRRVCRATGAAIQNTTSNIIPDVIGT-CDLFEEVQVGGQRYNLFTGCTMTQTATIILRGGGEQFIDEAERSLHDSIMIV 396
Cdd:TIGR02344 314 DNNRIARACGATIVNRPEELRESDVGTgCGLFEVKKIGDEYFTFITECKDPKACTILLRGASKDILNEVERNLQDAMAVA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 397 RRARKHRSVVAGGGAIEMEVSKYLRDYSLSIEGKKQLLINAFAKALEVIPRQIADNAGFDSTDILNQLRQKHAQGEK-WF 475
Cdd:TIGR02344 394 RNVLLDPKLVPGGGATEMAVSVALTEKSKKLEGVEQWPYRAVADALEIIPRTLAQNCGANVIRTLTELRAKHAQENNcTW 473
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 66802602 476 GVDIVNEGICDTYESAIWEPSLVKLNSIVAATEATCLILSVDETV 520
Cdd:TIGR02344 474 GIDGETGKIVDMKEKGIWEPLAVKLQTYKTAIESACLLLRIDDIV 518
|
|
| TCP1_theta |
cd03341 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ... |
23-520 |
4.89e-107 |
|
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: 328.80 E-value: 4.89e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 23 PQLISNINACCAIVDTVRTTLGPRGMDKLIYQSERQVTISNDGATVMKLLDIVHPAARTLVDIAKSQDSEVGDGTTSVVI 102
Cdd:cd03341 8 EAVLRNIEACKELSQITRTSYGPNGMNKMVINHLEKLFVTSDAATILRELEVQHPAAKLLVMASQMQEEEIGDGTNLVVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 103 LAGEFLKAAKPFLEEGIHPQIIIRAFRSACELAKQKIQELSVDiKPENMREF--LEKCASTSMNSKLIaSHKQFFSKMVV 180
Cdd:cd03341 88 LAGELLEKAEELLRMGLHPSEIIEGYEKALKKALEILEELVVY-KIEDLRNKeeVSKALKTAIASKQY-GNEDFLSPLVA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 181 DA-VQLLDDNI---DLDMIGIKKESGGGLGDSQFIAGAAFKRtffyaGFEQQPKHIKNPKVLCLNIELELkaekdnaeir 256
Cdd:cd03341 166 EAcISVLPENIgnfNVDNIRVVKILGGSLEDSKVVRGMVFKR-----EPEGSVKRVKKAKVAVFSCPFDI---------- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 257 isdptkyqslvnaewklffdkleaihasGVNVVLSKLAIGDLAtQFFADKNMFCAGRVPDD-DIRRVCRATGAAIQNTTS 335
Cdd:cd03341 231 ----------------------------GVNVIVAGGSVGDLA-LHYCNKYGIMVIKINSKfELRRLCRTVGATPLPRLG 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 336 NIIPDVIGTCDLFEEVQVGGQRYNLFTGC-TMTQTATIILRGGGEQFIDEAERSLHDSIMIVRRARKHRSVVAGGGAIEM 414
Cdd:cd03341 282 APTPEEIGYCDSVYVEEIGDTKVVVFRQNkEDSKIATIVLRGATQNILDDVERAIDDGVNVFKSLTKDGRFVPGAGATEI 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 415 EVSKYLRDYSLSIEGKKQLLINAFAKALEVIPRQIADNAGFDSTDILNQLRQKHAQGEKWFGVDIV--NEGICDTYESAI 492
Cdd:cd03341 362 ELAKKLKEYGEKTPGLEQYAIKKFAEAFEVVPRTLAENAGLDATEVLSELYAAHQKGNKSAGVDIEsgDEGTKDAKEAGI 441
|
490 500
....*....|....*....|....*...
gi 66802602 493 WEPSLVKLNSIVAATEATCLILSVDETV 520
Cdd:cd03341 442 FDHLATKKWAIKLATEAAVTVLRVDQII 469
|
|
| TCP1_epsilon |
cd03339 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ... |
8-520 |
2.69e-102 |
|
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: 318.47 E-value: 2.69e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 8 PIVLLKEGTDTS--QGLPQLISNINACCAIVDTVRTTLGPRGMDKLIYQSERQVTISNDGATVMKLLDIVHPAARTLVDI 85
Cdd:cd03339 6 PFIIVREQEKKKrlKGLEAHKSHILAAKSVANILRTSLGPRGMDKILVSPDGEVTVTNDGATILEKMDVDHQIAKLLVEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 86 AKSQDSEVGDGTTSVVILAGEFLKAAKPFLEEGIHPQIIIRAFRSACELAKQKIQELS--VDIKPENmREFLEKCASTSM 163
Cdd:cd03339 86 SKSQDDEIGDGTTGVVVLAGALLEQAEKLLDRGIHPIRIADGYEQACKIAVEHLEEIAdkIEFSPDN-KEPLIQTAMTSL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 164 NSKLIASHKQFFSKMVVDAVQLLDD----NIDLDMIGIKKESGGGLGDSQFIAGAAFKRTFFYAgfeQQPKHIKNPKVLC 239
Cdd:cd03339 165 GSKIVSRCHRQFAEIAVDAVLSVADlerkDVNFELIKVEGKVGGRLEDTKLVKGIVIDKDFSHP---QMPKEVKDAKIAI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 240 LNIELELKAEKDNAEIRISDPTKYQSLVNAEWKLFFDKLEAIHASGVNVVLSKLAIGDLATQFFADKNMFCAGRVPDDDI 319
Cdd:cd03339 242 LTCPFEPPKPKTKHKLDITSVEDYKKLQEYEQKYFREMVEQVKDAGANLVICQWGFDDEANHLLLQNGLPAVRWVGGVEI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 320 RRVCRATGAAIQNTTSNIIPDVIGTCDLFEEVQVGG--QRYNLFTGCTMTQTATIILRGGGEQFIDEAERSLHDSIMIVR 397
Cdd:cd03339 322 ELIAIATGGRIVPRFEDLSPEKLGKAGLVREISFGTtkDKMLVIEGCPNSKAVTIFIRGGNKMIIEEAKRSLHDALCVVR 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 398 RARKHRSVVAGGGAIEMEVSKYLRDYSLSIEGKKQLLINAFAKALEVIPRQIADNAGFDSTDILNQLRQKH-AQGEKWFG 476
Cdd:cd03339 402 NLIRDNRIVYGGGAAEISCSLAVEKAADKCSGIEQYAMRAFADALESIPLALAENSGLNPIETLSEVKARQvKEKNPHLG 481
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 66802602 477 VDIVNEGICDTYESAIWEPSLVKLNSIVAATEATCLILSVDETV 520
Cdd:cd03339 482 IDCLGRGTNDMKEQKVFETLISKKQQILLATQVVKMILKIDDVI 525
|
|
| chap_CCT_theta |
TIGR02346 |
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ... |
11-537 |
1.95e-101 |
|
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: 316.27 E-value: 1.95e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 11 LLKEGTDTSQGLP-QLISNINACCAIVDTVRTTLGPRGMDKLIYQSERQVTISNDGATVMKLLDIVHPAARTLVDIAKSQ 89
Cdd:TIGR02346 5 LLKEGYRHFSGLEeAVIKNIEACKELSQITRTSLGPNGMNKMVINHLEKLFVTNDAATILRELEVQHPAAKLLVMASEMQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 90 DSEVGDGTTSVVILAGEFLKAAKPFLEEGIHPQIIIRAFRSACELAKQKIQELSVD-IKPENMREFLEKCASTSMNSKLI 168
Cdd:TIGR02346 85 ENEIGDGTNLVLVLAGELLNKAEELIRMGLHPSEIIKGYEMALKKAMEILEELVVWeVKDLRDKDELIKALKASISSKQY 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 169 aSHKQFFSKMVVDAVQLL----DDNIDLDMIGIKKESGGGLGDSQFIAGAAFKRTffyagFEQQPKHIKNPKVLCLNIEL 244
Cdd:TIGR02346 165 -GNEDFLAQLVAQACSTVlpknPQNFNVDNIRVCKILGGSLSNSEVLKGMVFNRE-----AEGSVKSVKNAKVAVFSCPL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 245 ELKAEKDNAEIRISDPTKYQSLVNAEWKLFFDKLEAIHASGVNVVLSKLAIGDLAtQFFADKNMFCAGRVPDD-DIRRVC 323
Cdd:TIGR02346 239 DTATTETKGTVLIHNAEELLNYSKGEENQIEAMIKAIADSGVNVIVTGGSVGDMA-LHYLNKYNIMVLKIPSKfELRRLC 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 324 RATGAAIQNTTSNIIPDVIGTCDLFEEVQVGGQRYNLFTGC-TMTQTATIILRGGGEQFIDEAERSLHDSIMIVRRARKH 402
Cdd:TIGR02346 318 KTVGATPLPRLGAPTPEEIGYVDSVYVSEIGGDKVTVFKQEnGDSKISTIILRGSTDNLLDDIERAIDDGVNTVKALVKD 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 403 RSVVAGGGAIEMEVSKYLRDYSLSIEGKKQLLINAFAKALEVIPRQIADNAGFDSTDILNQLRQKHAQGEKWFGVDIVNE 482
Cdd:TIGR02346 398 GRLLPGAGATEIELASRLTKYGEKLPGLDQYAIKKFAEAFEIIPRTLAENAGLNANEVIPKLYAAHKKGNKSKGIDIEAE 477
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 66802602 483 --GICDTYESAIWEPSLVKLNSIVAATEATCLILSVDETVQNNQAeqaqAGPQINNQ 537
Cdd:TIGR02346 478 sdGVKDASEAGIYDMLATKKWAIKLATEAAVTVLRVDQIIMAKPA----GGPKPPQG 530
|
|
| chap_CCT_beta |
TIGR02341 |
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ... |
11-521 |
1.09e-100 |
|
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: 314.10 E-value: 1.09e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 11 LLKEGTDTSQGLPQLISNINACCAIVDTVRTTLGPRGMDKLIYQSERQVTI--SNDGATVMKLLDIVHPAARTLVDIAKS 88
Cdd:TIGR02341 2 IFKDGADEERAENARLSSFVGAIAIGDLVKSTLGPKGMDKILQSSSSDASImvTNDGATILKSIGVDNPAAKVLVDMSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 89 QDSEVGDGTTSVVILAGEFLKAAKPFLEEGIHPQIIIRAFRSACELAKQKIQELSVD--IKPENMREFLEKCASTSMNSK 166
Cdd:TIGR02341 82 QDDEVGDGTTSVTVLAAELLREAEKLINQKIHPQTIIAGYREATKAARDALLKSAVDngSDEVKFRQDLMNIARTTLSSK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 167 LIASHKQFFSKMVVDAVQLLDDNIDLDMIGIKKESGGGLGDSQFIAGAAFKRTFFYagfeQQPKHIKNPKVLCLNIELEL 246
Cdd:TIGR02341 162 ILSQHKDHFAQLAVDAVLRLKGSGNLEAIQIIKKLGGSLADSYLDEGFLLDKKIGV----NQPKRIENAKILIANTGMDT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 247 -KAEKDNAEIRISDPTKYQSLVNAEWKLFFDKLEAIHASGVNVVLSKLAIGDLATQFFADKNMFCAGRVPDDDIRRVCRA 325
Cdd:TIGR02341 238 dKVKIFGSRVRVDSTAKVAELEHAEKEKMKEKVEKILKHGINCFINRQLIYNYPEQLFADAGVMAIEHADFEGVERLALV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 326 TGAAIQNTTSNIIPDVIGTCDLFEEVQVGGQRYNLFTGCTMTQTATIILRGGGEQFIDEAERSLHDSIMIVRRARKHRSV 405
Cdd:TIGR02341 318 TGGEIVSTFDHPELVKLGSCDLIEEIMIGEDKLLKFSGVKLGEACTIVLRGATQQILDEAERSLHDALCVLSQTVKESRT 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 406 VAGGGAIEMEVSKYLRDYSLSIEGKKQLLINAFAKALEVIPRQIADNAGFDSTDILNQLRQKHAQGEKWFGVDIVNEGIC 485
Cdd:TIGR02341 398 VLGGGCSEMLMSKAVTQEAQRTPGKEALAVEAFARALRQLPTIIADNAGFDSAELVAQLRAAHYNGNTTMGLDMNEGTIA 477
|
490 500 510
....*....|....*....|....*....|....*.
gi 66802602 486 DTYESAIWEPSLVKLNSIVAATEATCLILSVDETVQ 521
Cdd:TIGR02341 478 DMRQLGITESYKVKRAVVSSAAEAAEVILRVDNIIK 513
|
|
| chap_CCT_epsi |
TIGR02343 |
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ... |
3-522 |
5.27e-96 |
|
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: 302.49 E-value: 5.27e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 3 QMIRPPIVLLKEGTDTSQ-GLPQLISNINACCAIVDTVRTTLGPRGMDKLIYQSERQVTISNDGATVMKLLDIVHPAART 81
Cdd:TIGR02343 6 EYGRPFIIIKDQDNKKRLkGLEAKKSNIAAAKSVASILRTSLGPKGMDKMLISPDGDITVTNDGATILSQMDVDNQIAKL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 82 LVDIAKSQDSEVGDGTTSVVILAGEFLKAAKPFLEEGIHPQIIIRAFRSACELAKQKIQELSVDIK-PENMREFLEKCAS 160
Cdd:TIGR02343 86 MVELSKSQDDEIGDGTTGVVVLAGALLEQAEELLDKGIHPIKIADGFEEAARIAVEHLEEISDEISaDNNNREPLIQAAK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 161 TSMNSKLIASHKQFFSKMVVDAVQLLDD----NIDLDMIGIKKESGGGLGDSQFIAGAAFKRTFFYAgfeQQPKHIKNPK 236
Cdd:TIGR02343 166 TSLGSKIVSKCHRRFAEIAVDAVLNVADmerrDVDFDLIKVEGKVGGSLEDTKLIKGIIIDKDFSHP---QMPKEVEDAK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 237 VLCLNIELELKAEKDNAEIRISDPTKYQSLVNAEWKLFFDKLEAIHASGVNVVLSKLAIGDLATQFFADKNMFCAGRVPD 316
Cdd:TIGR02343 243 IAILTCPFEPPKPKTKHKLDISSVEEYKKLQKYEQQKFKEMIDDIKKSGANLVICQWGFDDEANHLLLQNDLPAVRWVGG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 317 DDIRRVCRATGAAIQNTTSNIIPDVIGTCDLFEEVQVG--GQRYNLFTGCTMTQTATIILRGGGEQFIDEAERSLHDSIM 394
Cdd:TIGR02343 323 QELELIAIATGGRIVPRFQELSKDKLGKAGLVREISFGttKDRMLVIEQCKNSKAVTIFIRGGNKMIIEEAKRSIHDALC 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 395 IVRRARKHRSVVAGGGAIEMEVSKYLRDYSLSIEGKKQLLINAFAKALEVIPRQIADNAGFDSTDILNQLRQKHAQGEKW 474
Cdd:TIGR02343 403 VVRNLIKDSRIVYGGGAAEISCSLAVSQEADKYPGVEQYAIRAFADALETIPMALAENSGLDPIGTLSTLKSLQLKEKNP 482
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 66802602 475 F-GVDIVNEGICDTYESAIWEPSLVKLNSIVAATEATCLILSVDETVQN 522
Cdd:TIGR02343 483 NlGVDCLGYGTNDMKEQFVFETLIGKKQQILLATQLVRMILKIDDVISP 531
|
|
| GroEL |
COG0459 |
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ... |
27-520 |
2.62e-95 |
|
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227 Cd Length: 497 Bit Score: 299.30 E-value: 2.62e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 27 SNINACCAIVDTVRTTLGPRGMDKLIYQSERQVTISNDGATVMKLLDIVHP----AARTLVDIAKSQDSEVGDGTTSVVI 102
Cdd:COG0459 14 ANIRGVKALADAVKVTLGPKGRNVMLVKSFGDPTITNDGVTIAKEIELEDPfenmGAQLVKEVASKTNDEAGDGTTTATV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 103 LAGEFLKAAKPFLEEGIHPQIIIRAFRSACELAKQKIQELSVDIKPenmREFLEKCASTSMNSKliashkQFFSKMVVDA 182
Cdd:COG0459 94 LAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPVDD---KEELAQVATISANGD------EEIGELIAEA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 183 VQLLDDNIDldmigIKKESGGGLG-DSQFIAGAAFKRTF----FYAGFEQQPKHIKNPKVLCLNIELELKAEkdnaeiri 257
Cdd:COG0459 165 MEKVGKDGV-----ITVEEGKGLEtELEVVEGMQFDKGYlspyFVTDPEKMPAELENAYILLTDKKISSIQD-------- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 258 sdptkyqslvnaewklFFDKLEAIHASGVNVVLSKLAIGDLATQFFADKNMF-----CAGRVPD------DDIRRVCRAT 326
Cdd:COG0459 232 ----------------LLPLLEKVAQSGKPLLIIAEDIDGEALATLVVNGIRgvlrvVAVKAPGfgdrrkAMLEDIAILT 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 327 GA-AIQN----TTSNIIPDVIGTCDLfeeVQVGGQRYNLFTGCTMTQTATIILRGGGEQFIDEAERSLHDSIMIVRRARK 401
Cdd:COG0459 296 GGrVISEdlglKLEDVTLDDLGRAKR---VEVDKDNTTIVEGAGNPKAIVILVGAATEVEVKERKRRVEDALHATRAAVE 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 402 HRsVVAGGGAIEMEVSKYLRDYSLSIEGKKQLLINAFAKALEVIPRQIADNAGFDSTDILNQLRqkhAQGEKWFGVDIVN 481
Cdd:COG0459 373 EG-IVPGGGAALLRAARALRELAAKLEGDEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKVR---AAKDKGFGFDAAT 448
|
490 500 510
....*....|....*....|....*....|....*....
gi 66802602 482 EGICDTYESAIWEPSLVKLNSIVAATEATCLILSVDETV 520
Cdd:COG0459 449 GEYVDMLEAGVIDPAKVKRSALQNAASVAGLILTTEAVI 487
|
|
| chap_CCT_zeta |
TIGR02347 |
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ... |
25-518 |
1.33e-75 |
|
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: 248.88 E-value: 1.33e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 25 LISNINACCAIVDTVRTTLGPRGMDKLIYQSERQVTISNDGATVMKLLDIVHPAARTLVDIAKSQDSEVGDGTTSVVILA 104
Cdd:TIGR02347 18 LMMNINAARGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEMQIQHPTASMIARAATAQDDITGDGTTSTVLLI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 105 GEFLKAAKPFLEEGIHPQIIIRAFRSACELAKQKIQELSVDIKPENMREFLEKCASTSMNSKLIASHKQFFSKMVVDAVQ 184
Cdd:TIGR02347 98 GELLKQAERYILEGVHPRIITEGFEIARKEALQFLDKFKVKKEDEVDREFLLNVARTSLRTKLPADLADQLTEIVVDAVL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 185 LL---DDNIDLDMIGIKKESGGGLGDSQFIAGAAFKRTFFYAGFeqqPKHIKNPKVLCLNIELELKAEKDNAEIRISDPT 261
Cdd:TIGR02347 178 AIkkdGEDIDLFMVEIMEMKHKSATDTTLIRGLVLDHGARHPDM---PRRVKNAYILTCNVSLEYEKTEVNSGFFYSSAE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 262 KYQSLVNAEWKLFFDKLEAI---------HASGVN-VVLSKLAIGDLATQFFADKNMFCAGRVPDDDIRRVCRATGAAIQ 331
Cdd:TIGR02347 255 QREKLVKAERKFVDDRVKKIielkkkvcgKSPDKGfVVINQKGIDPPSLDLLAKEGIMALRRAKRRNMERLTLACGGEAL 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 332 NTTSNIIPDVIGTCDLFEEVQVGGQRYNLFTGCTMTQTATIILRGGGEQFIDEAERSLHDSIMIVRRARKHRSVVAGGGA 411
Cdd:TIGR02347 335 NSVEDLTPECLGWAGLVYETTIGEEKYTFIEECKNPKSCTILIKGPNDHTIAQIKDAVRDGLRAVKNAIEDKCVVPGAGA 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 412 IEMEVSKYLRDYSLSIEGKKQLLINAFAKALEVIPRQIADNAGFDSTDILNQLRQKHAQGEKWFGVDIVNEGICDTYESA 491
Cdd:TIGR02347 415 FEIAAYRHLKEYKKSVKGKAKLGVEAFANALLVIPKTLAENSGFDAQDTLVKLEDEHDEGGEVVGVDLNTGEPIDPEIKG 494
|
490 500
....*....|....*....|....*..
gi 66802602 492 IWEPSLVKLNSIVAATEATCLILSVDE 518
Cdd:TIGR02347 495 IWDNYRVKKQLIQSATVIASQLLLVDE 521
|
|
| TCP1_zeta |
cd03342 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
28-518 |
2.31e-73 |
|
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: 241.78 E-value: 2.31e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 28 NINACCAIVDTVRTTLGPRGMDKLIYQSERQVTISNDGATVMKLLDIVHPAARTLVDIAKSQDSEVGDGTTSVVILAGEF 107
Cdd:cd03342 17 NISAAKGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLSEMQIQHPTASMIARAATAQDDITGDGTTSNVLLIGEL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 108 LKAAKPFLEEGIHPQIIIRAFRSACELAKQKIQELSVDIKPENMREFLEKCASTSMNSKLIASHKQFFSKMVVDAVQLL- 186
Cdd:cd03342 97 LKQAERYIQEGVHPRIITEGFELAKNKALKFLESFKVPVEIDTDRELLLSVARTSLRTKLHADLADQLTEIVVDAVLAIy 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 187 --DDNIDLDMIGIKKESGGGLGDSQFIAGAAFKRtffyaGFEQ--QPKHIKNPKVLCLNIELELkaEKdnaeirisdptk 262
Cdd:cd03342 177 kpDEPIDLHMVEIMQMQHKSDSDTKLIRGLVLDH-----GARHpdMPKRVENAYILTCNVSLEY--EK------------ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 263 yqSLVNAEwklFFDKleaihasgvnVVLSKLAIGDLATQFFADKNMFCAGRVPDDDIRRVCRATGAAIQNTTSNIIPDVI 342
Cdd:cd03342 238 --TEVNSG---FFYS----------VVINQKGIDPPSLDMLAKEGILALRRAKRRNMERLTLACGGVAMNSVDDLSPECL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 343 GTCDLFEEVQVGGQRYNLFTGCTMTQTATIILRGGGEQFIDEAERSLHDSIMIVRRARKHRSVVAGGGAIEMEVSKYLRD 422
Cdd:cd03342 303 GYAGLVYERTLGEEKYTFIEGVKNPKSCTILIKGPNDHTITQIKDAIRDGLRAVKNAIEDKCVVPGAGAFEVALYAHLKE 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 423 YSLSIEGKKQLLINAFAKALEVIPRQIADNAGFDSTDILNQLRQKHAQGEKWFGVDIVNEGICDTYESAIWEPSLVKLNS 502
Cdd:cd03342 383 FKKSVKGKAKLGVQAFADALLVIPKTLAENSGLDVQETLVKLQDEYAEGGQVGGVDLDTGEPMDPESEGIWDNYSVKRQI 462
|
490
....*....|....*.
gi 66802602 503 IVAATEATCLILSVDE 518
Cdd:cd03342 463 LHSATVIASQLLLVDE 478
|
|
| chaperonin_like |
cd03333 |
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ... |
152-402 |
2.58e-64 |
|
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: 208.86 E-value: 2.58e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 152 REFLEKCASTSMNSKlIASHKQFFSKMVVDAVQLLDD---NIDLDMIGIKKESGGGLGDSQFIAGAAFKRTFFYAGFeqq 228
Cdd:cd03333 1 RELLLQVATTSLNSK-LSSWDDFLGKLVVDAVLKVGPdnrMDDLGVIKVEKIPGGSLEDSELVVGVVFDKGYASPYM--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 229 PKHIKNPKVLCLNIELElkaekdnaeirisdptkyqslvnaewklffdkleaihasgvNVVLSKLAIGDLATQFFADKNM 308
Cdd:cd03333 77 PKRLENAKILLLDCPLE-----------------------------------------YVVIAEKGIDDLALHYLAKAGI 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 309 FCAGRVPDDDIRRVCRATGAAIQNTTSNIIPDVIGTCDLFEEVQVGGQRYNLFTGCTMTQTATIILRGGGEQFIDEAERS 388
Cdd:cd03333 116 MAVRRVKKEDLERIARATGATIVSSLEDLTPEDLGTAELVEETKIGEEKLTFIEGCKGGKAATILLRGATEVELDEVKRS 195
|
250
....*....|....
gi 66802602 389 LHDSIMIVRRARKH 402
Cdd:cd03333 196 LHDALCAVRAAVEE 209
|
|
| PTZ00114 |
PTZ00114 |
Heat shock protein 60; Provisional |
35-515 |
7.23e-15 |
|
Heat shock protein 60; Provisional
Pssm-ID: 185455 Cd Length: 555 Bit Score: 77.26 E-value: 7.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 35 IVDTVRTTLGPRGMDKLIYQSERQVTISNDGATVMKLLDIVHPA----ARTLVDIAKSQDSEVGDGTTSVVILAGEFLKA 110
Cdd:PTZ00114 34 LADAVAVTLGPKGRNVIIEQEYGSPKITKDGVTVAKAIEFSDRFenvgAQLIRQVASKTNDKAGDGTTTATILARAIFRE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 111 AKPFLEEGIHPQIIIRAFRSACELAKQKIQELSvdiKPENMREFLEKCASTSMN-----SKLIAshkQFFSKMVVDAVql 185
Cdd:PTZ00114 114 GCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQS---RPVKTKEDILNVATISANgdveiGSLIA---DAMDKVGKDGT-- 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 186 lddnidldmigIKKESGGGLGDS-QFIAGAAFKRTFFyagfeqQPKHIKNPKvlclnielELKAEKDNAEIRISDP--TK 262
Cdd:PTZ00114 186 -----------ITVEDGKTLEDElEVVEGMSFDRGYI------SPYFVTNEK--------TQKVELENPLILVTDKkiSS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 263 YQSLVNAewklffdkLEAIHASGVNVVL-----SKLAIGDLATQFFADKNMFCAGRVP------DDDIRRVCRATGAAIQ 331
Cdd:PTZ00114 241 IQSILPI--------LEHAVKNKRPLLIiaedvEGEALQTLIINKLRGGLKVCAVKAPgfgdnrKDILQDIAVLTGATVV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 332 NTTS------NIIPDVIGTCDLF-----EEVQVGGQRY------------NLFTGCT--------------MTQTATIIL 374
Cdd:PTZ00114 313 SEDNvglkldDFDPSMLGSAKKVtvtkdETVILTGGGDkaeikervellrSQIERTTseydkeklkerlakLSGGVAVIK 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 375 RGGGEQF-IDEAERSLHDSIMIVRRARKhRSVVAGGGAIEMEVSKYLrDY---SLSIEGKKQLLINAFAKALEVIPRQIA 450
Cdd:PTZ00114 393 VGGASEVeVNEKKDRIEDALNATRAAVE-EGIVPGGGVALLRASKLL-DKleeDNELTPDQRTGVKIVRNALRLPTKQIA 470
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66802602 451 DNAGFDSTDILNQLRQKhaqGEKWFGVDIVNEGICDTYESAIWEPSLVKLNSIVAATEATCLILS 515
Cdd:PTZ00114 471 ENAGVEGAVVVEKILEK---KDPSFGYDAQTGEYVNMFEAGIIDPTKVVRSALVDAASVASLMLT 532
|
|
| GroEL |
cd03344 |
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ... |
34-514 |
8.98e-14 |
|
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: 73.64 E-value: 8.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 34 AIVDTVRTTLGPRGMDKLIYQSERQVTISNDGATVMK---LLDIVHPAARTLV-DIAKSQDSEVGDGTTSVVILAGEFLK 109
Cdd:cd03344 19 KLADAVKVTLGPKGRNVVIEKSFGSPKITKDGVTVAKeieLEDPFENMGAQLVkEVASKTNDVAGDGTTTATVLARAIIK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 110 AAKPFLEEGIHPQIIIRAFRSACELAKQKIQELSVDIKPENMrefLEKCASTSmnskliASHKQFFSKMVVDAVQLLDDN 189
Cdd:cd03344 99 EGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKPVKTKEE---IAQVATIS------ANGDEEIGELIAEAMEKVGKD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 190 --IDLdmigikkESGGGLGDS-QFIAGAAFKRTFFyagfeqQPKHIKNPKvlclnielELKAEKDNAEIRISDP--TKYQ 264
Cdd:cd03344 170 gvITV-------EEGKTLETElEVVEGMQFDRGYL------SPYFVTDPE--------KMEVELENPYILLTDKkiSSIQ 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 265 SLVNAewklffdkLEAIHASGVNVV----------LSKLAIGDLATQF---------FAD--KNMFcagrvpdDDIRRVc 323
Cdd:cd03344 229 ELLPI--------LELVAKAGRPLLiiaedvegeaLATLVVNKLRGGLkvcavkapgFGDrrKAML-------EDIAIL- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 324 raTGA-----AIQNTTSNIIPDVIGTCdlfEEVQVggqrynlftgctmTQTATIILRGGG---------EQFIDEAERSL 389
Cdd:cd03344 293 --TGGtviseELGLKLEDVTLEDLGRA---KKVVV-------------TKDDTTIIGGAGdkaaikariAQIRKQIEETT 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 390 HD---------------SIMIVR---------RARKHR--------------SVVAGGGAIEMEVSKYLrDYSLSIEGKK 431
Cdd:cd03344 355 SDydkeklqerlaklsgGVAVIKvggatevelKEKKDRvedalnatraaveeGIVPGGGVALLRASPAL-DKLKALNGDE 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 432 QLLINAFAKALEVIPRQIADNAGFDSTDILNQLRqKHAQGekwFGVDIVNEGICDTYESAIWEPSLVKLNSIVAATEATC 511
Cdd:cd03344 434 KLGIEIVRRALEAPLRQIAENAGVDGSVVVEKVL-ESPDG---FGYDAATGEYVDMIEAGIIDPTKVVRSALQNAASVAS 509
|
...
gi 66802602 512 LIL 514
Cdd:cd03344 510 LLL 512
|
|
| Fab1_TCP |
cd03334 |
TCP-1 like domain of the eukaryotic phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinase Fab1. ... |
197-377 |
3.13e-12 |
|
TCP-1 like domain of the eukaryotic phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinase Fab1. Fab1p is important for vacuole size regulation, presumably by modulating PtdIns(3,5)P2 effector activity. In the human homolog p235/PIKfyve deletion of this domain leads to loss of catalytic activity. However no exact function this domain has been defined. In general, chaperonins are involved in productive folding of proteins.
Pssm-ID: 239450 [Multi-domain] Cd Length: 261 Bit Score: 66.86 E-value: 3.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 197 IKKESGGGLGDSQFIAGAAFKRTffyAGFEQQPKHIKNPKVLCLNIELELKaekdnaeiriSDPTKYQSL--VNAEWKLF 274
Cdd:cd03334 52 IKKIPGGSPSDSEVVDGVVFTKN---VAHKRMPSKIKNPRILLLQGPLEYQ----------RVENKLLSLdpVILQEKEY 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 275 FDKLEA-IHASGVNVVLSKLAIGDLATQFFADKNMFCAGRVPDDDIRRVCRATGAAI-QNTTSNIIPDVIGTCDLFEE-- 350
Cdd:cd03334 119 LKNLVSrIVALRPDVILVEKSVSRIAQDLLLEAGITLVLNVKPSVLERISRCTGADIiSSMDDLLTSPKLGTCESFRVrt 198
|
170 180 190
....*....|....*....|....*....|
gi 66802602 351 -VQVGGQRYNL--FTGCTMTQTATIILRGG 377
Cdd:cd03334 199 yVEEHGRSKTLmfFEGCPKELGCTILLRGG 228
|
|
| groEL |
PRK12852 |
chaperonin GroEL; Reviewed |
35-532 |
3.50e-10 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237232 Cd Length: 545 Bit Score: 62.55 E-value: 3.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 35 IVDTVRTTLGPRGMDKLIYQSERQVTISNDGATVMKLLDIV----HPAARTLVDIAKSQDSEVGDGTTSVVILAGEFLKA 110
Cdd:PRK12852 23 LANAVKVTLGPKGRNVVIEKSFGAPRITKDGVTVAKEIELEdkfeNMGAQMVREVASKTNDLAGDGTTTATVLAQAIVRE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 111 AKPFLEEGIHPQIIIRAFRSACELAKQKIQELSvdiKPENMREFLEKCASTSMNS-----KLIAshkQFFSKMVVDAVQL 185
Cdd:PRK12852 103 GAKAVAAGMNPMDLKRGIDIAVAAVVKDIEKRA---KPVASSAEIAQVGTISANGdaaigKMIA---QAMQKVGNEGVIT 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 186 LDDNIDLDMigikkesggglgDSQFIAGAAFKRTFFyagfeqQPKHIKNPKvlclnielELKAEKDNAEIRISDP--TKY 263
Cdd:PRK12852 177 VEENKSLET------------EVDIVEGMKFDRGYL------SPYFVTNAE--------KMTVELDDAYILLHEKklSGL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 264 QSLVNAewklffdkLEAIHASG---------------VNVVLSKL------------AIGDLATQFFADKNMFCAGRVPD 316
Cdd:PRK12852 231 QAMLPV--------LEAVVQSGkplliiaedvegealATLVVNRLrgglkvaavkapGFGDRRKAMLEDIAILTGGQLIS 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 317 DD---------IRRVCRATGAAIQNTTSNIIPDVIGTCDLFEEV-QVGGQ---------RYNLFTGCTMTQTATIILRGG 377
Cdd:PRK12852 303 EDlgiklenvtLKMLGRAKKVVIDKENTTIVNGAGKKADIEARVgQIKAQieettsdydREKLQERLAKLAGGVAVIRVG 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 378 GEQFI------DEAERSLHDSimivrRARKHRSVVAGGGAIEMEVSKYLRDYSlSIEGKKQLLINAFAKALEVIPRQIAD 451
Cdd:PRK12852 383 GATEVevkekkDRVEDALNAT-----RAAVQEGIVPGGGVALLRAKKAVGRIN-NDNADVQAGINIVLKALEAPIRQIAE 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 452 NAGFDSTDILNQLRQKHAQGekwFGVDIVNEGICDTYESAIWEPSLVKLNSIVAATEATCLILSVDETVQNNQAEQAQ-A 530
Cdd:PRK12852 457 NAGVEGSIVVGKILENKSET---FGFDAQTEEYVDMVAKGIIDPAKVVRTALQDAASVAGLLVTTEAMVAELPKKDAApA 533
|
..
gi 66802602 531 GP 532
Cdd:PRK12852 534 MP 535
|
|
| groEL |
CHL00093 |
chaperonin GroEL |
35-527 |
1.62e-08 |
|
chaperonin GroEL
Pssm-ID: 177025 Cd Length: 529 Bit Score: 57.04 E-value: 1.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 35 IVDTVRTTLGPRGMDKLIYQSERQVTISNDGATVMKLLDIVHPAART---LVDIAKSQDSEV-GDGTTSVVILAGEFLKA 110
Cdd:CHL00093 22 LAEAVSVTLGPKGRNVVLEKKYGSPQIVNDGVTIAKEIELEDHIENTgvaLIRQAASKTNDVaGDGTTTATVLAYAIVKQ 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 111 AKPFLEEGIHPQIIIRAFRSACELAKQKIQELSVDIkpENMREfLEKCASTSmnskliASHKQFFSKMVVDAVQLL--DD 188
Cdd:CHL00093 102 GMKNVAAGANPISLKRGIEKATQYVVSQIAEYARPV--EDIQA-ITQVASIS------AGNDEEVGSMIADAIEKVgrEG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 189 NIDLDmigikkESGGGLGDSQFIAGAAFKRTFFYAGFEQQPKHI----KNPKVLCLNIELELKAEKDNAEIRISDPTKYQ 264
Cdd:CHL00093 173 VISLE------EGKSTVTELEITEGMRFEKGFISPYFVTDTERMevvqENPYILLTDKKITLVQQDLLPILEQVTKTKRP 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 265 SLVNAE-------WKLFFDKLEAIhasgVNVVLSKL-AIGDLATQFFADKNMFCAGRVPDDD---------IRRVCRATG 327
Cdd:CHL00093 247 LLIIAEdvekealATLVLNKLRGI----VNVVAVRApGFGDRRKAMLEDIAILTGGQVITEDaglsletiqLDLLGQARR 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 328 AAIQNTTSNIIPD-----VIGTCD-----------LFEEVQVGGQRYNLFTGctmtqTATIILRGGGEQFIDEAERSLHD 391
Cdd:CHL00093 323 IIVTKDSTTIIADgneeqVKARCEqlrkqieiadsSYEKEKLQERLAKLSGG-----VAVIKVGAATETEMKDKKLRLED 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 392 SIMIVRRARKhRSVVAGGGAIEMEVSKYLRDYSlSIEGKKQLLINAF--AKALEVIPRQIADNAGFDSTDILNQLRQKHA 469
Cdd:CHL00093 398 AINATKAAVE-EGIVPGGGATLVHLSENLKTWA-KNNLKEDELIGALivARAILAPLKRIAENAGKNGSVIIEKVQEQDF 475
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 66802602 470 QgekwFGVDIVNEGICDTYESAIWEPSLVKLNSIVAATEATCLILSVDETVQNNQAEQ 527
Cdd:CHL00093 476 E----IGYNAANNKFVNMYEAGIIDPAKVTRSALQNAASIASMILTTECIIVDKKESS 529
|
|
| groEL |
PRK12851 |
chaperonin GroEL; Reviewed |
34-532 |
2.57e-08 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 171770 Cd Length: 541 Bit Score: 56.67 E-value: 2.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 34 AIVDTVRTTLGPRGMDKLIYQSERQVTISNDGATVMKLLDIVHP----AARTLVDIAKSQDSEVGDGTTSVVILAGEFLK 109
Cdd:PRK12851 22 ILADAVKVTLGPKGRNVVIDKSFGAPTITNDGVTIAKEIELEDKfenmGAQMVREVASKTNDVAGDGTTTATVLAQAIVR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 110 AAKPFLEEGIHPQIIIRAFRSACELAkqkIQELSVDIKPENMREFLEKCASTSmnskliASHKQFFSKMVVDAVqlldDN 189
Cdd:PRK12851 102 EGAKAVAAGANPMDLKRGIDRAVAAV---VEELKANARPVTTNAEIAQVATIS------ANGDAEIGRLVAEAM----EK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 190 IDLDMIGIKKESGGGLGDSQFIAGAAFKRTF----FYAGFEQQPKHIKNPKVLCLNIE----------LELKAEKDNAEI 255
Cdd:PRK12851 169 VGNEGVITVEESKTAETELEVVEGMQFDRGYlspyFVTDADKMEAELEDPYILIHEKKisnlqdllpvLEAVVQSGKPLL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 256 RISDPTKYQSL----VNAEWKLFfdKLEAIHASGvnvvlsklaIGDLATQFFADKNMFCAGRVPDDDIrrvcratGAAIQ 331
Cdd:PRK12851 249 IIAEDVEGEALatlvVNKLRGGL--KVAAVKAPG---------FGDRRKAMLEDIAILTGGTVISEDL-------GIKLE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 332 NTTSniipDVIGTCdlfeevqvggqrynlfTGCTMTQTATIILRGGGEQF------------IDEA----------ER-- 387
Cdd:PRK12851 311 NVTL----EQLGRA----------------KKVVVEKENTTIIDGAGSKTeiegrvaqiraqIEETtsdydreklqERla 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 388 SLHDSIMIVR---------RARKHR--------------SVVAGGGAIEMEVSKYLrDYSLSIEGKKQLLINAFAKALEV 444
Cdd:PRK12851 371 KLAGGVAVIRvgastevevKEKKDRvddalhatraaveeGIVPGGGVALLRAVKAL-DKLETANGDQRTGVEIVRRALEA 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 445 IPRQIADNAGFDSTDILNQLRQKH-------AQGEKwfgVDIVNEGICD---TYESAIwePSLVKLNSIVAATEATclil 514
Cdd:PRK12851 450 PVRQIAENAGAEGSVVVGKLREKPggygfnaATNEY---GDLYAQGVIDpvkVVRTAL--QNAASVAGLLLTTEAM---- 520
|
570
....*....|....*...
gi 66802602 515 sVDETVQNNQAEQAQAGP 532
Cdd:PRK12851 521 -VAEKPKKEPAPPAPPGG 537
|
|
| groEL |
PRK12849 |
chaperonin GroEL; Reviewed |
37-486 |
3.44e-08 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237230 Cd Length: 542 Bit Score: 55.97 E-value: 3.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 37 DTVRTTLGPRGMDKLIYQSERQVTISNDGATVMKLLDIVHP----AARTLVDIAKSQDSEVGDGTTSVVILAG----EFL 108
Cdd:PRK12849 24 DAVKVTLGPKGRNVVIDKSFGAPTITKDGVSIAKEIELEDPfenlGAQLVKEVASKTNDVAGDGTTTATVLAQalvqEGL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 109 KAakpfLEEGIHPQIIIRAFRSACELAKQKIQELSVDIKPenmREFLEKCASTSmnskliASHKQFFSKMVVDAVqlldD 188
Cdd:PRK12849 104 KN----VAAGANPMDLKRGIDKAVEAVVEELKALARPVSG---SEEIAQVATIS------ANGDEEIGELIAEAM----E 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 189 NIDLDMIgIKKESGGGLGDS-QFIAGAAFKRTF----FYAGFEQQPKHIKNPKVLCL-----NIE-----LELKAEKDNA 253
Cdd:PRK12849 167 KVGKDGV-ITVEESKTLETElEVTEGMQFDRGYlspyFVTDPERMEAVLEDPLILLTdkkisSLQdllplLEKVAQSGKP 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 254 EIRIS---DPTKYQSL-VNAEWKLFfdKLEAIHASGvnvvlsklaIGDLATQFFADKNMFCAGRVPDDDIrrvcratGAA 329
Cdd:PRK12849 246 LLIIAedvEGEALATLvVNKLRGGL--KVAAVKAPG---------FGDRRKAMLEDIAILTGGTVISEDL-------GLK 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 330 IQNTTsniiPDVIGTCDlfeevQVggqrynlftgcTMTQTATIILRGGGE------------QFIDEA----------ER 387
Cdd:PRK12849 308 LEEVT----LDDLGRAK-----RV-----------TITKDNTTIVDGAGDkeaiearvaqirRQIEETtsdydreklqER 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 388 --SLHDSIMIVR---------RARKHR--------------SVVAGGGAIEMEVSKYLRDYsLSIEGKKQLLINAFAKAL 442
Cdd:PRK12849 368 laKLAGGVAVIKvgaatevelKERKDRvedalnatraaveeGIVPGGGVALLRAAKALDEL-AGLNGDQAAGVEIVRRAL 446
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 66802602 443 EVIPRQIADNAGFDSTDILNQLRqkhaQGEKWFG--------VDIVNEGICD 486
Cdd:PRK12849 447 EAPLRQIAENAGLDGSVVVAKVL----ELEDGFGfnaatgeyGDLIAAGIID 494
|
|
| groEL |
PRK12850 |
chaperonin GroEL; Reviewed |
34-486 |
3.84e-08 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237231 Cd Length: 544 Bit Score: 55.88 E-value: 3.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 34 AIVDTVRTTLGPRGMDKLIYQSERQVTISNDGATVMKLLDIVHP----AARTLVDIAKSQDSEVGDGTTSVVILAGEFLK 109
Cdd:PRK12850 22 ILANAVKVTLGPKGRNVVLEKSFGAPRITKDGVTVAKEIELEDKfenmGAQMVKEVASKTNDLAGDGTTTATVLAQAIVR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 110 AAKPFLEEGIHPQIIIRAFRSACELAKQKIQELSVDIKPenmREFLEKCASTSmnskliASHKQFFSKMVVDAVqllddn 189
Cdd:PRK12850 102 EGAKLVAAGMNPMDLKRGIDLAVAAVVDELKKIAKKVTS---SKEIAQVATIS------ANGDESIGEMIAEAM------ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 190 idlDMIG----IKKESGGGLGDS-QFIAGAAFKR----TFFYAGFEQQPKHIKNPKVLCLNIE----------LELKAEK 250
Cdd:PRK12850 167 ---DKVGkegvITVEEAKTLGTElDVVEGMQFDRgylsPYFVTNPEKMRAELEDPYILLHEKKisnlqdllpiLEAVVQS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 251 DNAEIRISDPTKYQSL----VNAEWKLFfdKLEAIHASGvnvvlsklaIGDLATQFFADKNMFCAGRVPDDDirrvcraT 326
Cdd:PRK12850 244 GRPLLIIAEDVEGEALatlvVNKLRGGL--KSVAVKAPG---------FGDRRKAMLEDIAVLTGGQVISED-------L 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 327 GAAIQNTTSniipDVIGTCDLFeevqvggqrynlftgcTMTQTATIILRGGGEQF------------IDEA--------- 385
Cdd:PRK12850 306 GIKLENVTL----DMLGRAKRV----------------LITKENTTIIDGAGDKKniearvkqiraqIEETtsdydrekl 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 386 -ER--SLHDSIMIVR---------RARKHR--------------SVVAGGGAIEMEVSKYLRDYsLSIEGKKQLLINAFA 439
Cdd:PRK12850 366 qERlaKLAGGVAVIRvggatevevKEKKDRvddalhatraaveeGIVPGGGVALLRARSALRGL-KGANADETAGIDIVR 444
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 66802602 440 KALEVIPRQIADNAGFDSTDILNQLRQK------HAQGEKWfgVDIVNEGICD 486
Cdd:PRK12850 445 RALEEPLRQIATNAGFEGSVVVGKVAELpgnfgfNAQTGEY--GDMVEAGIID 495
|
|
| PRK14104 |
PRK14104 |
chaperonin GroEL; Provisional |
35-532 |
5.08e-08 |
|
chaperonin GroEL; Provisional
Pssm-ID: 172594 Cd Length: 546 Bit Score: 55.81 E-value: 5.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 35 IVDTVRTTLGPRGMDKLIYQSERQVTISNDGATVMKLLDI----VHPAARTLVDIAKSQDSEVGDGTTSVVILAGEFLKA 110
Cdd:PRK14104 23 LANAVKVTLGPKGRNVVLDKSFGAPRITKDGVTVAKEIELedkfENMGAQMVREVASKSADAAGDGTTTATVLAQAIVRE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 111 AKPFLEEGIHPQIIIRAFRSACELAkqkIQELSVDIKPENMREFLEKCASTSMNSkliashKQFFSKMVVDAVQLLDDni 190
Cdd:PRK14104 103 GAKSVAAGMNPMDLKRGIDLAVEAV---VADLVKNSKKVTSNDEIAQVGTISANG------DAEIGKFLADAMKKVGN-- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 191 dlDMIGIKKESGGGLGDSQFIAGAAFKRTFFyagfeqQPKHIKNPKvlclnielELKAEKDNAEIRISDptKYQSLVNAE 270
Cdd:PRK14104 172 --EGVITVEEAKSLETELDVVEGMQFDRGYI------SPYFVTNAD--------KMRVEMDDAYILINE--KKLSSLNEL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 271 WKLffdkLEAIHASG---------------VNVVLSKL------------AIGDLATQFFADKNMFCAGRVPDDD----- 318
Cdd:PRK14104 234 LPL----LEAVVQTGkplvivaedvegealATLVVNRLrgglkvaavkapGFGDRRKAMLQDIAILTGGQAISEDlgikl 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 319 ----IRRVCRATGAAIQNTTSNIIPDVIGTCDL----------FEEVQVGGQRYNLFTGCTMTQTATIILRGGGEQFIDE 384
Cdd:PRK14104 310 envtLQMLGRAKKVMIDKENTTIVNGAGKKADIearvaqikaqIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEV 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 385 AERSLH-DSIMIVRRARKHRSVVAGGGAIEMEVSKYLRDYSLSIEGKKQlLINAFAKALEVIPRQIADNAGFDSTDILNQ 463
Cdd:PRK14104 390 KERKDRvDDAMHATRAAVEEGIVPGGGVALLRASEQLKGIKTKNDDQKT-GVEIVRKALSAPARQIAINAGEDGSVIVGK 468
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 66802602 464 LRQKHAQGekwFGVDIVNEGICDTYESAIWEPSLVKLNSIVAATEATCLILSVDETVQnNQAEQAQAGP 532
Cdd:PRK14104 469 ILEKEQYS---YGFDSQTGEYGNLVSKGIIDPTKVVRTAIQNAASVAALLITTEAMVA-ELPKKGGAGP 533
|
|
| GroEL |
TIGR02348 |
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ... |
34-169 |
1.01e-07 |
|
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: 54.61 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 34 AIVDTVRTTLGPRGMDKLIYQSERQVTISNDGATVMKLLDIVHP----AARTLVDIAKSQDSEVGDGTTSVVILAGEFLK 109
Cdd:TIGR02348 20 KLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDKfenmGAQLVKEVASKTNDVAGDGTTTATVLAQAIVK 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66802602 110 AAKPFLEEGIHPQIIIRAFRSACELAKQKIQELSVDIKPenmREFLEKCASTSMNS-----KLIA 169
Cdd:TIGR02348 100 EGLKNVAAGANPIELKRGIEKAVEAVVEELKKLSKPVKG---KKEIAQVATISANNdeeigSLIA 161
|
|
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
37-169 |
1.92e-06 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 50.51 E-value: 1.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 37 DTVRTTLGPRGMDKLIYQSERQVTISNDGATVMK---LLDIVHPAARTLV-DIAKSQDSEVGDGTTSVVILA----GEFL 108
Cdd:PRK00013 24 DAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKeieLEDPFENMGAQLVkEVASKTNDVAGDGTTTATVLAqaivREGL 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66802602 109 K--AAkpfleeGIHPQIIIRAFRSACELAKQKIQELSvdiKPENMREFLEKCASTSMNS-----KLIA 169
Cdd:PRK00013 104 KnvAA------GANPMDLKRGIDKAVEAAVEELKKIS---KPVEDKEEIAQVATISANGdeeigKLIA 162
|
|
| PLN03167 |
PLN03167 |
Chaperonin-60 beta subunit; Provisional |
35-147 |
8.81e-05 |
|
Chaperonin-60 beta subunit; Provisional
Pssm-ID: 215611 [Multi-domain] Cd Length: 600 Bit Score: 45.30 E-value: 8.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 35 IVDTVRTTLGPRGMDKLIYQSERQVTISNDGATVMK---LLDIVHPAARTLVDIAKSQDSEV-GDGTTSVVILAGEFLKA 110
Cdd:PLN03167 78 LADLVGVTLGPKGRNVVLESKYGSPKIVNDGVTVAKeveLEDPVENIGAKLVRQAAAKTNDLaGDGTTTSVVLAQGLIAE 157
|
90 100 110
....*....|....*....|....*....|....*..
gi 66802602 111 AKPFLEEGIHPQIIIRAFRSACELAKQKIQELSVDIK 147
Cdd:PLN03167 158 GVKVVAAGANPVQITRGIEKTAKALVKELKKMSKEVE 194
|
|
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
405-486 |
1.13e-04 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 44.73 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66802602 405 VVAGGGAIEMEVSKYLRDYSLSiEGKKQLLINAFAKALEVIPRQIADNAGFDSTDILNQLRQKHAQGekwFG-------- 476
Cdd:PRK00013 410 IVPGGGVALLRAAPALEALKGL-NGDEATGINIVLRALEAPLRQIAENAGLEGSVVVEKVKNGKGKG---YGynaatgey 485
|
90
....*....|
gi 66802602 477 VDIVNEGICD 486
Cdd:PRK00013 486 VDMIEAGIID 495
|
|
| |
