|
Name |
Accession |
Description |
Interval |
E-value |
| TCP1_eta |
cd03340 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ... |
4-524 |
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: 1036.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 4 QIVLLKEGTDSSQGKPQLVSNINACQSIVDAVRTTLGPRGMDKLIVDAHGKATISNDGATIMKLLEIIHPAAKTLVDIAK 83
Cdd:cd03340 1 PIILLKEGTDTSQGKGQLISNINACQAIADAVRTTLGPRGMDKLIVDGRGKVTISNDGATILKLLDIVHPAAKTLVDIAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 84 SQDAEVGDGTTSVVLLAGEFLKQVKPFVEEGVHPRVIIKAIRKALQLCMEKINEMAVQIVEQSKDQQRALLEKCAATAMS 163
Cdd:cd03340 81 SQDAEVGDGTTSVVVLAGEFLKEAKPFIEDGVHPQIIIRGYRKALQLAIEKIKEIAVNIDKEDKEEQRELLEKCAATALN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 164 SKLIHQQKDFFSRIVVDAVLSLDELLPLNMIGIKKVTGGSLEESQLVSGVAFKKTFSYAGFEMAPKSYDNCKIALLNIEL 243
Cdd:cd03340 161 SKLIASEKEFFAKMVVDAVLSLDDDLDLDMIGIKKVPGGSLEDSQLVNGVAFKKTFSYAGFEQQPKKFKNPKILLLNVEL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 244 ELKAERDNAEIRVDNVKEYQKVVDAEWQILYNKLAKIHESGANVVLSKLPIGDVATQYFADRDIFCAGRVPEEDLKRTMK 323
Cdd:cd03340 241 ELKAEKDNAEVRVEDPEEYQAIVDAEWKIIYDKLEKIVKSGANVVLSKLPIGDLATQYFADRDIFCAGRVPEEDLKRVAQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 324 ACGGAVMTTANDIKPNVLGLCEHFEERQVGGERFNLFQGCPNAKTSTLILRGGAEQFLEETERSLHDAIMIVRRTIKHDS 403
Cdd:cd03340 321 ATGGSIQTTVSNITDDVLGTCGLFEERQVGGERYNIFTGCPKAKTCTIILRGGAEQFIEEAERSLHDAIMIVRRAIKNDS 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 404 VVAGGGAIEMELSKLLRDYSRTIAGKEQLLIAAIAKGLEIIPRQLCDNAGFDATNILNKLRQKHAQG-GQWYGVDINKED 482
Cdd:cd03340 401 VVAGGGAIEMELSKYLRDYSRTIAGKQQLVINAFAKALEIIPRQLCDNAGFDATDILNKLRQKHAQGgGKWYGVDINNEG 480
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 24645179 483 ISDNYEQCVWEPSIIKINALTAAAEAACMILSVDETIKSPKA 524
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 ... |
2-524 |
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: 872.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 2 QPQIVLLKEGTDSSQGKPQLVSNINACQSIVDAVRTTLGPRGMDKLIVDAHGKATISNDGATIMKLLEIIHPAAKTLVDI 81
Cdd:TIGR02345 1 RPTIVLLKEGTDTSQGKGQLISNINACVAIAEALKTTLGPRGMDKLIVGSNGKATISNDGATILKLLDIVHPAAKTLVDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 82 AKSQDAEVGDGTTSVVLLAGEFLKQVKPFVEEGVHPRVIIKAIRKALQLCMEKINEMAVQIVEqSKDQQRALLEKCAATA 161
Cdd:TIGR02345 81 AKSQDAEVGDGTTSVTILAGELLKEAKPFIEEGVHPQLIIRCYREALSLAVEKIKEIAVTIDE-EKGEQRELLEKCAATA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 162 MSSKLIHQQKDFFSRIVVDAVLSLD-ELLPLNMIGIKKVTGGSLEESQLVSGVAFKKTFSYAGFEMAPKSYDNCKIALLN 240
Cdd:TIGR02345 160 LSSKLISHNKEFFSKMIVDAVLSLDrDDLDLKLIGIKKVQGGALEDSQLVNGVAFKKTFSYAGFEQQPKKFANPKILLLN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 241 IELELKAERDNAEIRVDNVKEYQKVVDAEWQILYNKLAKIHESGANVVLSKLPIGDVATQYFADRDIFCAGRVPEEDLKR 320
Cdd:TIGR02345 240 VELELKAEKDNAEIRVEDVEDYQAIVDAEWAIIFRKLEKIVESGANVVLSKLPIGDLATQYFADRDIFCAGRVSAEDLKR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 321 TMKACGGAVMTTANDIKPNVLGLCEHFEERQVGGERFNLFQGCPNAKTSTLILRGGAEQFLEETERSLHDAIMIVRRTIK 400
Cdd:TIGR02345 320 VIKACGGSIQSTTSDLEADVLGTCALFEERQIGSERYNYFTGCPHAKTCTIILRGGAEQFIEEAERSLHDAIMIVRRALK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 401 HDSVVAGGGAIEMELSKLLRDYSRTIAGKEQLLIAAIAKGLEIIPRQLCDNAGFDATNILNKLRQKHAQGGQWYGVDINK 480
Cdd:TIGR02345 400 NKKIVAGGGAIEMELSKCLRDYSKTIDGKQQLIINAFAKALEIIPRQLCENAGFDSIEILNKLRSRHAKGGKWYGVDINT 479
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 24645179 481 EDISDNYEQCVWEPSIIKINALTAAAEAACMILSVDETIKSPKA 524
Cdd:TIGR02345 480 EDIGDNFEAFVWEPALVKINALKAAFEAACTILSVDETITNPKS 523
|
|
| chaperonin_type_I_II |
cd00309 |
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ... |
12-520 |
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: 547.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 12 TDSSQGKPQLVSNINACQSIVDAVRTTLGPRGMDKLIVDAHGKATISNDGATIMKLLEIIHPAAKTLVDIAKSQDAEVGD 91
Cdd:cd00309 1 KEREFGEEARLSNINAAKALADAVKTTLGPKGMDKMLVDSLGDPTITNDGATILKEIEVEHPAAKLLVEVAKSQDDEVGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 92 GTTSVVLLAGEFLKQVKPFVEEGVHPRVIIKAIRKALQLCMEKINEMAVQIVEQSKDQqralLEKCAATAMSSKLIHQQK 171
Cdd:cd00309 81 GTTTVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVPIDVEDREE----LLKVATTSLNSKLVSGGD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 172 DFFSRIVVDAVLSL---DELLPLNMIGIKKVTGGSLEESQLVSGVAFKKTFSYAGFemaPKSYDNCKIALLNIELElkae 248
Cdd:cd00309 157 DFLGELVVDAVLKVgkeNGDVDLGVIRVEKKKGGSLEDSELVVGMVFDKGYLSPYM---PKRLENAKILLLDCKLE---- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 249 rdnaeirvdnvkeyqkvvdaewqilynklakihesgaNVVLSKLPIGDVATQYFADRDIFCAGRVPEEDLKRTMKACGGA 328
Cdd:cd00309 230 -------------------------------------YVVIAEKGIDDEALHYLAKLGIMAVRRVRKEDLERIAKATGAT 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 329 VMTTANDIKPNVLGLCEHFEERQVGGERFNLFQGCPNAKTSTLILRGGAEQFLEETERSLHDAIMIVRRTIKHDSVVAGG 408
Cdd:cd00309 273 IVSRLEDLTPEDLGTAGLVEETKIGDEKYTFIEGCKGGKVATILLRGATEVELDEAERSLHDALCAVRAAVEDGGIVPGG 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 409 GAIEMELSKLLRDYSRTIAGKEQLLIAAIAKGLEIIPRQLCDNAGFDATNILNKLRQKHAQGGQWYGVDINKEDISDNYE 488
Cdd:cd00309 353 GAAEIELSKALEELAKTLPGKEQLGIEAFADALEVIPRTLAENAGLDPIEVVTKLRAKHAEGGGNAGGDVETGEIVDMKE 432
|
490 500 510
....*....|....*....|....*....|..
gi 24645179 489 QCVWEPSIIKINALTAAAEAACMILSVDETIK 520
Cdd:cd00309 433 AGIIDPLKVKRQALKSATEAASLILTIDDIIV 464
|
|
| Cpn60_TCP1 |
pfam00118 |
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ... |
31-520 |
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: 529.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 31 IVDAVRTTLGPRGMDKLIVDAHGKATISNDGATIMKLLEIIHPAAKTLVDIAKSQDAEVGDGTTSVVLLAGEFLKQVKPF 110
Cdd:pfam00118 1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELEIQHPAAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEEAEKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 111 VEEGVHPRVIIKAIRKALQLCMEKINEMAVQIVEQSKDQQralLEKCAATAMSSKLIHQQKDFFSRIVVDAVLSL---DE 187
Cdd:pfam00118 81 LAAGVHPTTIIEGYEKALEKALEILDSIISIPVEDVDRED---LLKVARTSLSSKIISRESDFLAKLVVDAVLAIpknDG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 188 LLPLNMIGIKKVTGGSLEESQLVSGVAFKKTFSYagfEMAPKSYDNCKIALLNIELELKAERDNAEIRVDNVKEYQKVVD 267
Cdd:pfam00118 158 SFDLGNIGVVKILGGSLEDSELVDGVVLDKGPLH---PDMPKRLENAKVLLLNCSLEYEKTETKATVVLSDAEQLERFLK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 268 AEWQILYNKLAKIHESGANVVLSKLPIGDVATQYFADRDIFCAGRVPEEDLKRTMKACGGAVMTTANDIKPNVLGLCEHF 347
Cdd:pfam00118 235 AEEEQILEIVEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMALRRVKKRDLERLAKATGARAVSSLDDLTPDDLGTAGKV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 348 EERQVGGERFNLFQGCPNAKTSTLILRGGAEQFLEETERSLHDAIMIVRRTIKHDSVVAGGGAIEMELSKLLRDYSRTIA 427
Cdd:pfam00118 315 EEEKIGDEKYTFIEGCKSPKAATILLRGATDHVLDEIERSIHDALCVVKNAIEDPRVVPGGGAVEMELARALREYAKSVS 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 428 GKEQLLIAAIAKGLEIIPRQLCDNAGFDATNILNKLRQKHAQGGQWYGVDINKEDISDNYEQCVWEPSIIKINALTAAAE 507
Cdd:pfam00118 395 GKEQLAIEAFAEALEVIPKTLAENAGLDPIEVLAELRAAHASGEKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKSATE 474
|
490
....*....|...
gi 24645179 508 AACMILSVDETIK 520
Cdd:pfam00118 475 AASTILRIDDIIK 487
|
|
| thermosome_beta |
NF041083 |
thermosome subunit beta; |
2-521 |
4.03e-162 |
|
thermosome subunit beta;
Pssm-ID: 469010 Cd Length: 519 Bit Score: 471.36 E-value: 4.03e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 2 QPqIVLLKEGTDSSQGKPQLVSNINACQSIVDAVRTTLGPRGMDKLIVDAHGKATISNDGATIMKLLEIIHPAAKTLVDI 81
Cdd:NF041083 1 QP-VLILKEGTQRTKGRDAQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDIVITNDGATILKEMDVQHPAAKMLVEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 82 AKSQDAEVGDGTTSVVLLAGEFLKQVKPFVEEGVHPRVIIKAIRKALQLCMEKINEMAVQIveqsKDQQRALLEKCAATA 161
Cdd:NF041083 80 AKTQDDEVGDGTTTAVVLAGELLKKAEELLDQNIHPTIIANGYRLAAEKAIEILDEIAEKV----DPDDRETLKKIAETS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 162 MSSKLIHQQKDFFSRIVVDAVLSLDEL------LPLNMIGIKKVTGGSLEESQLVSGVAFKKTFSYAGFemaPKSYDNCK 235
Cdd:NF041083 156 LTSKGVEEARDYLAEIAVKAVKQVAEKrdgkyyVDLDNIQIEKKHGGSIEDTQLIYGIVIDKEVVHPGM---PKRVENAK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 236 IALLNIELELKAERDNAEIRVDNVKEYQKVVDAEWQILYNKLAKIHESGANVVLSKLPIGDVATQYFADRDIFCAGRVPE 315
Cdd:NF041083 233 IALLDAPLEVKKTEIDAEIRITDPDQLQKFLDQEEKMLKEMVDKIKATGANVVFCQKGIDDLAQHYLAKAGILAVRRVKK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 316 EDLKRTMKACGGAVMTTANDIKPNVLGLCEHFEERQVGGERFNLFQGCPNAKTSTLILRGGAEQFLEETERSLHDAIMIV 395
Cdd:NF041083 313 SDMEKLAKATGARIVTNIDDLTPEDLGYAELVEERKVGDDKMVFVEGCKNPKAVTILIRGGTEHVVDEAERALEDALSVV 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 396 RRTIKHDSVVAGGGAIEMELSKLLRDYSRTIAGKEQLLIAAIAKGLEIIPRQLCDNAGFDATNILNKLRQKHAQGGQWYG 475
Cdd:NF041083 393 ADAVEDGKIVAGGGAPEVELAKRLREYAATVGGREQLAVEAFAEALEIIPRTLAENAGLDPIDILVKLRSAHEKGKKWAG 472
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 24645179 476 VDINKEDISDNYEQCVWEPSIIKINALTAAAEAACMILSVDETIKS 521
Cdd:NF041083 473 INVFTGEVVDMWELGVIEPLRVKTQAIKSATEAATMILRIDDVIAA 518
|
|
| thermosome_alpha |
NF041082 |
thermosome subunit alpha; |
2-521 |
1.52e-160 |
|
thermosome subunit alpha;
Pssm-ID: 469009 Cd Length: 518 Bit Score: 467.05 E-value: 1.52e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 2 QPqIVLLKEGTDSSQGKPQLVSNINACQSIVDAVRTTLGPRGMDKLIVDAHGKATISNDGATIMKLLEIIHPAAKTLVDI 81
Cdd:NF041082 1 QP-ILILKEGTQRTSGRDAQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDVVITNDGVTILKEMDIEHPAAKMIVEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 82 AKSQDAEVGDGTTSVVLLAGEFLKQVKPFVEEGVHPRVIIKAIRKALQLCMEKINEMAVQIveqsKDQQRALLEKCAATA 161
Cdd:NF041082 80 AKTQDDEVGDGTTTAVVLAGELLKKAEELLDQDIHPTIIAEGYRLAAEKALEILDEIAIKV----DPDDKETLKKIAATA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 162 MSSKLIHQQKDFFSRIVVDAVLSLDE-----LLPLNMIGIKKVTGGSLEESQLVSGVAFKKTFSYAGfeMaPKSYDNCKI 236
Cdd:NF041082 156 MTGKGAEAAKDKLADLVVDAVKAVAEkdggyNVDLDNIKVEKKVGGSIEDSELVEGVVIDKERVHPG--M-PKRVENAKI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 237 ALLNIELELKAERDNAEIRVDNVKEYQKVVDAEWQILYNKLAKIHESGANVVLSKLPIGDVATQYFADRDIFCAGRVPEE 316
Cdd:NF041082 233 ALLDAPLEVKKTEIDAKISITDPDQLQAFLDQEEKMLKEMVDKIADSGANVVFCQKGIDDLAQHYLAKEGILAVRRVKKS 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 317 DLKRTMKACGGAVMTTANDIKPNVLGLCEHFEERQVGGERFNLFQGCPNAKTSTLILRGGAEQFLEETERSLHDAIMIVR 396
Cdd:NF041082 313 DMEKLAKATGARIVTSIDDLSPEDLGYAGLVEERKVGGDKMIFVEGCKNPKAVTILLRGGTEHVVDEVERALEDALRVVR 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 397 RTIKHDSVVAGGGAIEMELSKLLRDYSRTIAGKEQLLIAAIAKGLEIIPRQLCDNAGFDATNILNKLRQKHAQGGQWYGV 476
Cdd:NF041082 393 VVLEDGKVVAGGGAPEVELALRLREYAASVGGREQLAIEAFAEALEIIPRTLAENAGLDPIDALVELRSAHEKGNKTAGL 472
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 24645179 477 DINKEDISDNYEQCVWEPSIIKINALTAAAEAACMILSVDETIKS 521
Cdd:NF041082 473 DVYTGKVVDMLEIGVVEPLRVKTQAIKSATEAAVMILRIDDVIAA 517
|
|
| cpn60 |
cd03343 |
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ... |
5-521 |
3.85e-158 |
|
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: 460.96 E-value: 3.85e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 5 IVLLKEGTDSSQGKPQLVSNINACQSIVDAVRTTLGPRGMDKLIVDAHGKATISNDGATIMKLLEIIHPAAKTLVDIAKS 84
Cdd:cd03343 1 VLILKEGTQRTSGRDAQRMNIAAAKAVAEAVRTTLGPKGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 85 QDAEVGDGTTSVVLLAGEFLKQVKPFVEEGVHPRVIIKAIRKALQLCMEKINEMAVQIVEQSKDqqraLLEKCAATAMSS 164
Cdd:cd03343 81 QDEEVGDGTTTAVVLAGELLEKAEDLLDQNIHPTVIIEGYRLAAEKALELLDEIAIKVDPDDKD----TLRKIAKTSLTG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 165 KLIHQQKDFFSRIVVDAVLSLDELLP------LNMIGIKKVTGGSLEESQLVSGVAFKKTFSYAGFemaPKSYDNCKIAL 238
Cdd:cd03343 157 KGAEAAKDKLADLVVDAVLQVAEKRDgkyvvdLDNIKIEKKTGGSVDDTELIRGIVIDKEVVHPGM---PKRVENAKIAL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 239 LNIELELKAERDNAEIRVDNVKEYQKVVDAEWQILYNKLAKIHESGANVVLSKLPIGDVATQYFADRDIFCAGRVPEEDL 318
Cdd:cd03343 234 LDAPLEVKKTEIDAKIRITSPDQLQAFLEQEEAMLKEMVDKIADTGANVVFCQKGIDDLAQHYLAKAGILAVRRVKKSDM 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 319 KRTMKACGGAVMTTANDIKPNVLGLCEHFEERQVGGERFNLFQGCPNAKTSTLILRGGAEQFLEETERSLHDAIMIVRRT 398
Cdd:cd03343 314 EKLARATGAKIVTNIDDLTPEDLGEAELVEERKVGDDKMVFVEGCKNPKAVTILLRGGTEHVVDELERALEDALRVVADA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 399 IKHDSVVAGGGAIEMELSKLLRDYSRTIAGKEQLLIAAIAKGLEIIPRQLCDNAGFDATNILNKLRQKHAQGGQWYGVDI 478
Cdd:cd03343 394 LEDGKVVAGGGAVEIELAKRLREYARSVGGREQLAVEAFADALEEIPRTLAENAGLDPIDTLVELRAAHEKGNKNAGLDV 473
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 24645179 479 NKEDISDNYEQCVWEPSIIKINALTAAAEAACMILSVDETIKS 521
Cdd:cd03343 474 YTGEVVDMLEKGVIEPLRVKKQAIKSATEAATMILRIDDVIAA 516
|
|
| thermosome_arch |
TIGR02339 |
thermosome, various subunits, archaeal; Thermosome is the name given to the archaeal rather ... |
5-519 |
2.80e-153 |
|
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: 448.75 E-value: 2.80e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 5 IVLLKEGTDSSQGKPQLVSNINACQSIVDAVRTTLGPRGMDKLIVDAHGKATISNDGATIMKLLEIIHPAAKTLVDIAKS 84
Cdd:TIGR02339 2 VFILKEGTQRTSGRDAQRNNIAAAKAVAEAVKSTLGPRGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 85 QDAEVGDGTTSVVLLAGEFLKQVKPFVEEGVHPRVIIKAIRKALQLCMEKINEMAVQIVEQSKDqqraLLEKCAATAMSS 164
Cdd:TIGR02339 82 QDEEVGDGTTTAVVLAGELLEKAEDLLEQDIHPTVIIEGYRKAAEKALEIIDEIATKISPEDRD----LLKKIAYTSLTS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 165 KLIHQQ-KDFFSRIVVDAVLSLDELLP-------LNMIGIKKVTGGSLEESQLVSGVAFKKTFSYAGFemaPKSYDNCKI 236
Cdd:TIGR02339 158 KASAEVaKDKLADLVVEAVKQVAELRGdgkyyvdLDNIKIVKKKGGSIEDTELVEGIVVDKEVVHPGM---PKRVENAKI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 237 ALLNIELELKAERDNAEIRVDNVKEYQKVVDAEWQILYNKLAKIHESGANVVLSKLPIGDVATQYFADRDIFCAGRVPEE 316
Cdd:TIGR02339 235 ALLDAPLEVEKTEIDAKIRITDPDQIKKFLDQEEAMLKEMVDKIASAGANVVICQKGIDDVAQHYLAKAGILAVRRVKKS 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 317 DLKRTMKACGGAVMTTANDIKPNVLGLCEHFEERQVGGERFNLFQGCPNAKTSTLILRGGAEQFLEETERSLHDAIMIVR 396
Cdd:TIGR02339 315 DIEKLARATGARIVSSIDEITESDLGYAELVEERKVGEDKMVFVEGCKNPKAVTILLRGGTEHVVDELERSIQDALHVVA 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 397 RTIKHDSVVAGGGAIEMELSKLLRDYSRTIAGKEQLLIAAIAKGLEIIPRQLCDNAGFDATNILNKLRQKHAQGGQWYGV 476
Cdd:TIGR02339 395 NALEDGKIVAGGGAVEIELALRLRSYARSVGGREQLAIEAFADALEEIPRILAENAGLDPIDALVDLRAKHEKGNKNAGI 474
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 24645179 477 DINKEDISDNYEQCVWEPSIIKINALTAAAEAACMILSVDETI 519
Cdd:TIGR02339 475 NVFTGEIEDMLELGVIEPLRVKEQAIKSATEAATMILRIDDVI 517
|
|
| TCP1_alpha |
cd03335 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ... |
13-520 |
1.10e-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: 411.68 E-value: 1.10e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 13 DSSQGKPQLVSNINACQSIVDAVRTTLGPRGMDKLIVDAHGKATISNDGATIMKLLEIIHPAAKTLVDIAKSQDAEVGDG 92
Cdd:cd03335 2 ERTSGQDVRTQNVTAAMAIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDKEVGDG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 93 TTSVVLLAGEFLKQVKPFVEEGVHPRVIIKAIRKALQLCMEKINE-MAVQIVEQSKDqqraLLEKCAATAMSSKLIHQQK 171
Cdd:cd03335 82 TTSVVIIAAELLKRANELVKQKIHPTTIISGYRLACKEAVKYIKEhLSISVDNLGKE----SLINVAKTSMSSKIIGADS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 172 DFFSRIVVDAVLSL-------DELLPLNMIGIKKVTGGSLEESQLVSGVAFKKTFsyAGFEMaPKSYDNCKIALLNIELE 244
Cdd:cd03335 158 DFFANMVVDAILAVkttnekgKTKYPIKAVNILKAHGKSAKESYLVNGYALNCTR--ASQGM-PTRVKNAKIACLDFNLQ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 245 LKAERDNAEIRVDNVKEYQKVVDAEWQILYNKLAKIHESGANVVLSKLPIGDVATQYFADRDIFCAGRVPEEDLKRTMKA 324
Cdd:cd03335 235 KTKMKLGVQVVVTDPEKLEKIRQRESDITKERIKKILAAGANVVLTTGGIDDMCLKYFVEAGAMAVRRVKKEDLRRIAKA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 325 CGGAVMTTANDIK------PNVLGLCEHFEERQVGGERFNLFQGCPNAKTSTLILRGGAEQFLEETERSLHDAIMIVRRT 398
Cdd:cd03335 315 TGATLVSTLANLEgeetfdPSYLGEAEEVVQERIGDDELILIKGTKKRSSASIILRGANDFMLDEMERSLHDALCVVKRT 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 399 IKHDSVVAGGGAIEMELSKLLRDYSRTIAGKEQLLIAAIAKGLEIIPRQLCDNAGFDATNILNKLRQKHA--------QG 470
Cdd:cd03335 395 LESNSVVPGGGAVETALSIYLENFATTLGSREQLAIAEFAEALLVIPKTLAVNAAKDATELVAKLRAYHAaaqvkpdkKH 474
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 24645179 471 GQWYGVDINKEDISDNYEQCVWEPSIIKINALTAAAEAACMILSVDETIK 520
Cdd:cd03335 475 LKWYGLDLINGKVRDNLEAGVLEPTVSKIKSLKFATEAAITILRIDDLIK 524
|
|
| chap_CCT_alpha |
TIGR02340 |
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ... |
11-523 |
7.29e-135 |
|
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: 402.18 E-value: 7.29e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 11 GTDSSQGKPQLVSNINACQSIVDAVRTTLGPRGMDKLIVDAHGKATISNDGATIMKLLEIIHPAAKTLVDIAKSQDAEVG 90
Cdd:TIGR02340 4 GGERTSGQDVRTQNVTAAMAIANIVKTSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDREVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 91 DGTTSVVLLAGEFLKQVKPFVEEGVHPRVIIKAIRKALQLCMEKINE-MAVQIVEQSKDQqralLEKCAATAMSSKLIHQ 169
Cdd:TIGR02340 84 DGTTSVVIIAAELLKRADELVKNKIHPTSVISGYRLACKEAVKYIKEnLSVSVDELGREA----LINVAKTSMSSKIIGL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 170 QKDFFSRIVVDAVLSL-------DELLPLNMIGIKKVTGGSLEESQLVSGVAFKKTFsyAGFEMaPKSYDNCKIALLNIE 242
Cdd:TIGR02340 160 DSDFFSNIVVDAVLAVkttnengETKYPIKAINILKAHGKSARESMLVKGYALNCTV--ASQQM-PKRIKNAKIACLDFN 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 243 LELKAERDNAEIRVDNVKEYQKVVDAEWQILYNKLAKIHESGANVVLSKLPIGDVATQYFADRDIFCAGRVPEEDLKRTM 322
Cdd:TIGR02340 237 LQKAKMALGVQIVVDDPEKLEQIRQREADITKERIKKILDAGANVVLTTGGIDDMCLKYFVEAGAMGVRRCKKEDLKRIA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 323 KACGGAVMTTANDIK------PNVLGLCEHFEERQVGGERFNLFQGCPNAKTSTLILRGGAEQFLEETERSLHDAIMIVR 396
Cdd:TIGR02340 317 KATGATLVSTLADLEgeetfeASYLGFADEVVQERIADDECILIKGTKKRKSASIILRGANDFMLDEMERSLHDALCVVK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 397 RTIKHDSVVAGGGAIEMELSKLLRDYSRTIAGKEQLLIAAIAKGLEIIPRQLCDNAGFDATNILNKLRQKHA-------- 468
Cdd:TIGR02340 397 RTLESNSVVPGGGAVEAALSIYLENFATTLGSREQLAIAEFARALLIIPKTLAVNAAKDSTELVAKLRAYHAaaqlkpek 476
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 24645179 469 QGGQWYGVDINKEDISDNYEQCVWEPSIIKINALTAAAEAACMILSVDETIKSPK 523
Cdd:TIGR02340 477 KHLKWYGLDLVNGKIRDNKEAGVLEPTVSKVKSLKFATEAAITILRIDDLIKLNP 531
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
3-521 |
7.05e-119 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 360.88 E-value: 7.05e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 3 PQIvlLKEGTDSSQGKPQLVSNINACQSIVDAVRTTLGPRGMDKLIVDAH-----GKATISNDGATIMKLLEIIHPAAKT 77
Cdd:PTZ00212 8 PQV--LKQGAQEEKGETARLQSFVGAIAVADLVKTTLGPKGMDKILQPMSegprsGNVTVTNDGATILKSVWLDNPAAKI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 78 LVDIAKSQDAEVGDGTTSVVLLAGEFLKQVKPFVEEGVHPRVIIKAIRKALQLCMEKINEMAVQiVEQSKDQQRALLEKC 157
Cdd:PTZ00212 86 LVDISKTQDEEVGDGTTSVVVLAGELLREAEKLLDQKIHPQTIIEGWRMALDVARKALEEIAFD-HGSDEEKFKEDLLNI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 158 AATAMSSKLIHQQKDFFSRIVVDAVLSLDELLPLNMIGIKKVTGGSLEESQLVSGVAFKKTFSYAgfemAPKSYDNCKIA 237
Cdd:PTZ00212 165 ARTTLSSKLLTVEKDHFAKLAVDAVLRLKGSGNLDYIQIIKKPGGTLRDSYLEDGFILEKKIGVG----QPKRLENCKIL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 238 LLNIELEL-KAERDNAEIRVDNVKEYQKVVDAEWQILYNKLAKIHESGANVVLSKLPIGDVATQYFADRDIFCAGRVPEE 316
Cdd:PTZ00212 241 VANTPMDTdKIKIYGAKVKVDSMEKVAEIEAAEKEKMKNKVDKILAHGCNVFINRQLIYNYPEQLFAEAGIMAIEHADFD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 317 DLKRTMKACGGAVMTTANDIKPNVLGLCEHFEERQVGGERFNLFQGCPNAKTSTLILRGGAEQFLEETERSLHDAIMIVR 396
Cdd:PTZ00212 321 GMERLAAALGAEIVSTFDTPEKVKLGHCDLIEEIMIGEDKLIRFSGCAKGEACTIVLRGASTHILDEAERSLHDALCVLS 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 397 RTIKHDSVVAGGGAIEMELSKLLRDYSRTIAGKEQLLIAAIAKGLEIIPRQLCDNAGFDATNILNKLRQKHAQGGQWYGV 476
Cdd:PTZ00212 401 QTVKDTRVVLGGGCSEMLMANAVEELAKKVEGKKSLAIEAFAKALRQIPTIIADNGGYDSAELVSKLRAEHYKGNKTAGI 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 24645179 477 DINKEDISDNYEQCVWEPSIIKINALTAAAEAACMILSVDETIKS 521
Cdd:PTZ00212 481 DMEKGTVGDMKELGITESYKVKLSQLCSATEAAEMILRVDDIIRC 525
|
|
| TCP1_beta |
cd03336 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ... |
8-520 |
4.48e-113 |
|
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: 345.47 E-value: 4.48e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 8 LKEGTDSSQGKPQLVSNINACQSIVDAVRTTLGPRGMDKLI--VDAHGKATISNDGATIMKLLEIIHPAAKTLVDIAKSQ 85
Cdd:cd03336 2 LKDGAQEEKGETARLSSFVGAIAIGDLVKTTLGPKGMDKILqsVGRSGGVTVTNDGATILKSIGVDNPAAKVLVDISKVQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 86 DAEVGDGTTSVVLLAGEFLKQVKPFVEEGVHPRVIIKAIRKALQLCMEKINEMAVQiVEQSKDQQRALLEKCAATAMSSK 165
Cdd:cd03336 82 DDEVGDGTTSVTVLAAELLREAEKLVAQKIHPQTIIEGYRMATAAAREALLSSAVD-HSSDEEAFREDLLNIARTTLSSK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 166 LIHQQKDFFSRIVVDAVLSLDELLPLNMIGIKKVTGGSLEESQLVSGVAFKKTFSYAgfemAPKSYDNCKIALLNIELEL 245
Cdd:cd03336 161 ILTQDKEHFAELAVDAVLRLKGSGNLDAIQIIKKLGGSLKDSYLDEGFLLDKKIGVN----QPKRIENAKILIANTPMDT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 246 -KAERDNAEIRVDNVKEYQKVVDAEWQILYNKLAKIHESGANVVLSKLPIGDVATQYFADRDIFCAGRVPEEDLKRTMKA 324
Cdd:cd03336 237 dKIKIFGAKVRVDSTAKVAEIEEAEKEKMKNKVEKILKHGINCFINRQLIYNYPEQLFADAGIMAIEHADFDGVERLALV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 325 CGGAVMTTANDIKPNVLGLCEHFEERQVGGERFNLFQGCPNAKTSTLILRGGAEQFLEETERSLHDAIMIVRRTIKHDSV 404
Cdd:cd03336 317 TGGEIASTFDHPELVKLGTCKLIEEIMIGEDKLIRFSGVAAGEACTIVLRGASQQILDEAERSLHDALCVLAQTVKDTRV 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 405 VAGGGAIEMELSKLLRDYSRTIAGKEQLLIAAIAKGLEIIPRQLCDNAGFDATNILNKLRQKHAQGGQWYGVDINKEDIS 484
Cdd:cd03336 397 VLGGGCSEMLMAKAVEELAKKTPGKKSLAIEAFAKALRQLPTIIADNAGYDSAELVAQLRAAHYNGNTTAGLDMRKGTVG 476
|
490 500 510
....*....|....*....|....*....|....*.
gi 24645179 485 DNYEQCVWEPSIIKINALTAAAEAACMILSVDETIK 520
Cdd:cd03336 477 DMKELGITESFKVKRQVLLSASEAAEMILRVDDIIK 512
|
|
| TCP1_delta |
cd03338 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ... |
22-519 |
2.00e-112 |
|
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: 343.88 E-value: 2.00e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 22 VSNINACQSIVDAVRTTLGPRGMDKLIVDAHGKATISNDGATIMKLLEIIHPAAKTLVDIAKSQDAEVGDGTTSVVLLAG 101
Cdd:cd03338 11 LSNIQAAKAVADAIRTSLGPRGMDKMIQTGKGEVIITNDGATILKQMSVLHPAAKMLVELSKAQDIEAGDGTTSVVVLAG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 102 EFLKQVKPFVEEGVHPRVIIKAIRKALQLCMEKINEMAVQIveqsKDQQRALLEKCAATAMSSKLIHQQKDFFSRIVVDA 181
Cdd:cd03338 91 ALLSACESLLKKGIHPTVISESFQIAAKKAVEILDSMSIPV----DLNDRESLIKSATTSLNSKVVSQYSSLLAPIAVDA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 182 VLSL-----DELLPLNMIGIKKVTGGSLEESQLVSGVAFKKTFSYAGfeMAPKSYDNCKIALLNIELE-LKAERDNAEIr 255
Cdd:cd03338 167 VLKVidpatATNVDLKDIRIVKKLGGTIEDTELVDGLVFTQKASKKA--GGPTRIEKAKIGLIQFCLSpPKTDMDNNIV- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 256 vdnVKEYQ---KVVDAEWQILYNKLAKIHESGANVVL---SKL--PIGDVATQYFADRDIFCAGRVPEEDLKRTMKACGG 327
Cdd:cd03338 244 ---VNDYAqmdRILREERKYILNMCKKIKKSGCNVLLiqkSILrdAVSDLALHFLAKLKIMVVKDIEREEIEFICKTIGC 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 328 AVMTTANDIKPNVLGLCEHFEERQVGGERFNLFQGCPNA-KTSTLILRGGAEQFLEETERSLHDAIMIVRRTIKHDSVVA 406
Cdd:cd03338 321 KPVASIDHFTEDKLGSADLVEEVSLGDGKIVKITGVKNPgKTVTILVRGSNKLVLDEAERSLHDALCVIRCLVKKRALIP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 407 GGGAIEMELSKLLRDYSRTIAGKEQLLIAAIAKGLEIIPRQLCDNAGFDATNILNKLRQKHAQGGQWYGVDINKEDISDN 486
Cdd:cd03338 401 GGGAPEIEIALQLSEWARTLTGVEQYCVRAFADALEVIPYTLAENAGLNPISIVTELRNRHAQGEKNAGINVRKGAITNI 480
|
490 500 510
....*....|....*....|....*....|...
gi 24645179 487 YEQCVWEPSIIKINALTAAAEAACMILSVDETI 519
Cdd:cd03338 481 LEENVVQPLLVSTSAITLATETVRMILKIDDIV 513
|
|
| chap_CCT_delta |
TIGR02342 |
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ... |
16-521 |
6.15e-111 |
|
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: 340.22 E-value: 6.15e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 16 QGKPQLV--SNINACQSIVDAVRTTLGPRGMDKLIVDAHGKATISNDGATIMKLLEIIHPAAKTLVDIAKSQDAEVGDGT 93
Cdd:TIGR02342 4 KDKPQDVrtSNIVAAKAVADAIRTSLGPKGMDKMIQDGKGEVIITNDGATILKQMAVLHPAAKMLVELSKAQDIEAGDGT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 94 TSVVLLAGEFLKQVKPFVEEGVHPRVIIKAIRKALQLCMEKINEMAVQiVEQSkdqQRALLEKCAATAMSSKLIHQQKDF 173
Cdd:TIGR02342 84 TSVVILAGALLGACERLLNKGIHPTIISESFQSAADEAIKILDEMSIP-VDLS---DREQLLKSATTSLSSKVVSQYSSL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 174 FSRIVVDAVLSL-----DELLPLNMIGIKKVTGGSLEESQLVSGVAFKKTFSYAgfEMAPKSYDNCKIALLNIELEL-KA 247
Cdd:TIGR02342 160 LAPLAVDAVLKVidpenAKNVDLNDIKVVKKLGGTIDDTELIEGLVFTQKASKS--AGGPTRIEKAKIGLIQFQISPpKT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 248 ERDNaEIRVDNVKEYQKVVDAEWQILYNKLAKIHESGANVVLSKLPI-----GDVATQYFADRDIFCAGRVPEEDLKRTM 322
Cdd:TIGR02342 238 DMEN-QIIVNDYAQMDRVLKEERAYILNIVKKIKKTGCNVLLIQKSIlrdavNDLALHFLAKMKIMVVKDIEREEIEFIC 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 323 KACGGAVMTTANDIKPNVLGLCEHFEERQVGGERFNLFQGCPNA-KTSTLILRGGAEQFLEETERSLHDAIMIVRRTIKH 401
Cdd:TIGR02342 317 KTIGCKPIASIDHFTADKLGSAELVEEVDSDGGKIIKITGIQNAgKTVTVVVRGSNKLVIDEAERSLHDALCVIRCLVKK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 402 DSVVAGGGAIEMELSKLLRDYSRTIAGKEQLLIAAIAKGLEIIPRQLCDNAGFDATNILNKLRQKHAQGGQWYGVDINKE 481
Cdd:TIGR02342 397 RGLIAGGGAPEIEIARRLSKYARTMKGVESYCVRAFADALEVIPYTLAENAGLNPIKVVTELRNRHANGEKTAGISVRKG 476
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 24645179 482 DISDNYEQCVWEPSIIKINALTAAAEAACMILSVDETIKS 521
Cdd:TIGR02342 477 GITNMLEEHVLQPLLVTTSAITLASETVRSILKIDDIVFT 516
|
|
| TCP1_gamma |
cd03337 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ... |
4-519 |
2.58e-107 |
|
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: 329.64 E-value: 2.58e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 4 QIVLLKEGTDSSQGKPQLVSNINACQSIVDAVRTTLGPRGMDKLIVDAHGKATISNDGATIMKLLEIIHPAAKTLVDIAK 83
Cdd:cd03337 1 PVLVLNQNTKRESGRKAQLGNIQAAKTVADVIRTCLGPRAMLKMLLDPMGGIVLTNDGNAILREIDVAHPAAKSMIELSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 84 SQDAEVGDGTTSVVLLAGEFLKQVKPFVEEGVHPRVIIKAIRKALQLCMEKINEMAVQIVEQSKDQqralLEKCAATAMS 163
Cdd:cd03337 81 TQDEEVGDGTTSVIILAGEILAVAEPFLERGIHPTVIIKAYRKALEDALKILEEISIPVDVNDRAQ----MLKIIKSCIG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 164 SKLIHQQKDFFSRIVVDAV--LSLDELLPLNMIGIK------KVTGGSLEESQLVSGVAFKKTFSYAGFEmapKSYDNCK 235
Cdd:cd03337 157 TKFVSRWSDLMCNLALDAVktVAVEENGRKKEIDIKryakveKIPGGEIEDSRVLDGVMLNKDVTHPKMR---RRIENPR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 236 IALLNIELelkaerdnaeirvdnvkEYqkVVdaewqilynklakIHESGanvvlsklpIGDVATQYFADRDIFCAGRVPE 315
Cdd:cd03337 234 IVLLDCPL-----------------EY--LV-------------ITEKG---------VSDLAQHYLVKAGITALRRVRK 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 316 EDLKRTMKACGGAVMTTANDIKPNVLGL-CEHFEERQVGGERFNLFQGCPNAKTSTLILRGGAEQFLEETERSLHDAIMI 394
Cdd:cd03337 273 TDNNRIARACGATIVNRPEELTESDVGTgAGLFEVKKIGDEYFTFITECKDPKACTILLRGASKDVLNEVERNLQDAMAV 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 395 VRRTIKHDSVVAGGGAIEMELSKLLRDYSRTIAGKEQLLIAAIAKGLEIIPRQLCDNAGFDATNILNKLRQKHAQGGQ-W 473
Cdd:cd03337 353 ARNIILNPKLVPGGGATEMAVSHALSEKAKSIEGVEQWPYKAVASALEVIPRTLAQNCGANVIRTLTELRAKHAQGENsT 432
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 24645179 474 YGVDINKEDISDNYEQCVWEPSIIKINALTAAAEAACMILSVDETI 519
Cdd:cd03337 433 WGIDGETGDIVDMKELGIWDPLAVKAQTYKTAIEAACMLLRIDDIV 478
|
|
| chap_CCT_gamma |
TIGR02344 |
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ... |
5-519 |
9.38e-106 |
|
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: 327.08 E-value: 9.38e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 5 IVLLKEGTDSSQGKPQLVSNINACQSIVDAVRTTLGPRGMDKLIVDAHGKATISNDGATIMKLLEIIHPAAKTLVDIAKS 84
Cdd:TIGR02344 2 VLVLNQNTKRESGRKAQLSNIQAAKAVADIIRTCLGPRSMLKMLLDPMGGIVMTNDGNAILREIDVAHPAAKSMIELSRT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 85 QDAEVGDGTTSVVLLAGEFLKQVKPFVEEGVHPRVIIKAIRKALQLCMEKINEMAVQIVEQSKDQQRALLEKCAATamss 164
Cdd:TIGR02344 82 QDEEVGDGTTSVIILAGEMLSVAEPFLEQNIHPTVIIRAYRKALDDALSVLEEISIPVDVNDDAAMLKLIQSCIGT---- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 165 KLIHQQKDFFSRIVVDAVLSLD-ELLPLNMIGIK------KVTGGSLEESQLVSGVAFKKTFSYagfemaPK---SYDNC 234
Cdd:TIGR02344 158 KFVSRWSDLMCDLALDAVRTVQrDENGRKEIDIKryakveKIPGGDIEDSCVLKGVMINKDVTH------PKmrrYIENP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 235 KIALLNIELELKAERDNAEIRVDNVKEYQKVVDAEWQILYNKLAKIHESGANVVLSKLPIGDVATQYFADRDIFCAGRVP 314
Cdd:TIGR02344 232 RIVLLDCPLEYKKGESQTNIEITKEEDWNRILQMEEEYVQLMCEDIIAVKPDLVITEKGVSDLAQHYLLKANITAIRRVR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 315 EEDLKRTMKACGGAVMTTANDIKPNVLGL-CEHFEERQVGGERFNLFQGCPNAKTSTLILRGGAEQFLEETERSLHDAIM 393
Cdd:TIGR02344 312 KTDNNRIARACGATIVNRPEELRESDVGTgCGLFEVKKIGDEYFTFITECKDPKACTILLRGASKDILNEVERNLQDAMA 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 394 IVRRTIKHDSVVAGGGAIEMELSKLLRDYSRTIAGKEQLLIAAIAKGLEIIPRQLCDNAGFDATNILNKLRQKHAQGG-Q 472
Cdd:TIGR02344 392 VARNVLLDPKLVPGGGATEMAVSVALTEKSKKLEGVEQWPYRAVADALEIIPRTLAQNCGANVIRTLTELRAKHAQENnC 471
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 24645179 473 WYGVDINKEDISDNYEQCVWEPSIIKINALTAAAEAACMILSVDETI 519
Cdd:TIGR02344 472 TWGIDGETGKIVDMKEKGIWEPLAVKLQTYKTAIESACLLLRIDDIV 518
|
|
| TCP1_epsilon |
cd03339 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ... |
23-520 |
1.15e-100 |
|
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: 313.85 E-value: 1.15e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 23 SNINACQSIVDAVRTTLGPRGMDKLIVDAHGKATISNDGATIMKLLEIIHPAAKTLVDIAKSQDAEVGDGTTSVVLLAGE 102
Cdd:cd03339 27 SHILAAKSVANILRTSLGPRGMDKILVSPDGEVTVTNDGATILEKMDVDHQIAKLLVELSKSQDDEIGDGTTGVVVLAGA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 103 FLKQVKPFVEEGVHPRVIIKAIRKALQLCMEKINEMAvQIVEQSKDqQRALLEKCAATAMSSKLIHQQKDFFSRIVVDAV 182
Cdd:cd03339 107 LLEQAEKLLDRGIHPIRIADGYEQACKIAVEHLEEIA-DKIEFSPD-NKEPLIQTAMTSLGSKIVSRCHRQFAEIAVDAV 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 183 LSLDEL----LPLNMIGIKKVTGGSLEESQLVSGVAFKKTFSYAgfEMaPKSYDNCKIALLNIELELKAERDNAEIRVDN 258
Cdd:cd03339 185 LSVADLerkdVNFELIKVEGKVGGRLEDTKLVKGIVIDKDFSHP--QM-PKEVKDAKIAILTCPFEPPKPKTKHKLDITS 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 259 VKEYQKVVDAEWQILYNKLAKIHESGANVVLSKLPIGDVATQYFADRDIFCAGRVPEEDLKRTMKACGGAVMTTANDIKP 338
Cdd:cd03339 262 VEDYKKLQEYEQKYFREMVEQVKDAGANLVICQWGFDDEANHLLLQNGLPAVRWVGGVEIELIAIATGGRIVPRFEDLSP 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 339 NVLGLCEHFEERQVGG--ERFNLFQGCPNAKTSTLILRGGAEQFLEETERSLHDAIMIVRRTIKHDSVVAGGGAIEMELS 416
Cdd:cd03339 342 EKLGKAGLVREISFGTtkDKMLVIEGCPNSKAVTIFIRGGNKMIIEEAKRSLHDALCVVRNLIRDNRIVYGGGAAEISCS 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 417 KLLRDYSRTIAGKEQLLIAAIAKGLEIIPRQLCDNAGFDATNILNKLRQKHAQGGQ-WYGVDINKEDISDNYEQCVWEPS 495
Cdd:cd03339 422 LAVEKAADKCSGIEQYAMRAFADALESIPLALAENSGLNPIETLSEVKARQVKEKNpHLGIDCLGRGTNDMKEQKVFETL 501
|
490 500
....*....|....*....|....*
gi 24645179 496 IIKINALTAAAEAACMILSVDETIK 520
Cdd:cd03339 502 ISKKQQILLATQVVKMILKIDDVIV 526
|
|
| chap_CCT_epsi |
TIGR02343 |
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ... |
2-521 |
6.17e-94 |
|
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: 296.71 E-value: 6.17e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 2 QPQIVLLKEGTDSSQ-GKPQLVSNINACQSIVDAVRTTLGPRGMDKLIVDAHGKATISNDGATIMKLLEIIHPAAKTLVD 80
Cdd:TIGR02343 9 RPFIIIKDQDNKKRLkGLEAKKSNIAAAKSVASILRTSLGPKGMDKMLISPDGDITVTNDGATILSQMDVDNQIAKLMVE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 81 IAKSQDAEVGDGTTSVVLLAGEFLKQVKPFVEEGVHPRVIIKAIRKALQLCMEKINEMAVQIVEQSKDQQRalLEKCAAT 160
Cdd:TIGR02343 89 LSKSQDDEIGDGTTGVVVLAGALLEQAEELLDKGIHPIKIADGFEEAARIAVEHLEEISDEISADNNNREP--LIQAAKT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 161 AMSSKLIHQQKDFFSRIVVDAVLSLDEL----LPLNMIGIKKVTGGSLEESQLVSGVAFKKTFSYAgfEMaPKSYDNCKI 236
Cdd:TIGR02343 167 SLGSKIVSKCHRRFAEIAVDAVLNVADMerrdVDFDLIKVEGKVGGSLEDTKLIKGIIIDKDFSHP--QM-PKEVEDAKI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 237 ALLNIELELKAERDNAEIRVDNVKEYQKVVDAEWQILYNKLAKIHESGANVVLSKLPIGDVATQYFADRDIFCAGRVPEE 316
Cdd:TIGR02343 244 AILTCPFEPPKPKTKHKLDISSVEEYKKLQKYEQQKFKEMIDDIKKSGANLVICQWGFDDEANHLLLQNDLPAVRWVGGQ 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 317 DLKRTMKACGGAVMTTANDIKPNVLGLCEHFEERQVG--GERFNLFQGCPNAKTSTLILRGGAEQFLEETERSLHDAIMI 394
Cdd:TIGR02343 324 ELELIAIATGGRIVPRFQELSKDKLGKAGLVREISFGttKDRMLVIEQCKNSKAVTIFIRGGNKMIIEEAKRSIHDALCV 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 395 VRRTIKHDSVVAGGGAIEMELSKLLRDYSRTIAGKEQLLIAAIAKGLEIIPRQLCDNAGFDATNILNKLRQKH-AQGGQW 473
Cdd:TIGR02343 404 VRNLIKDSRIVYGGGAAEISCSLAVSQEADKYPGVEQYAIRAFADALETIPMALAENSGLDPIGTLSTLKSLQlKEKNPN 483
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 24645179 474 YGVDINKEDISDNYEQCVWEPSIIKINALTAAAEAACMILSVDETIKS 521
Cdd:TIGR02343 484 LGVDCLGYGTNDMKEQFVFETLIGKKQQILLATQLVRMILKIDDVISP 531
|
|
| chap_CCT_theta |
TIGR02346 |
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ... |
7-525 |
2.29e-93 |
|
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: 295.09 E-value: 2.29e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 7 LLKEGTDSSQG-KPQLVSNINACQSIVDAVRTTLGPRGMDKLIVDAHGKATISNDGATIMKLLEIIHPAAKTLVDIAKSQ 85
Cdd:TIGR02346 5 LLKEGYRHFSGlEEAVIKNIEACKELSQITRTSLGPNGMNKMVINHLEKLFVTNDAATILRELEVQHPAAKLLVMASEMQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 86 DAEVGDGTTSVVLLAGEFLKQVKPFVEEGVHPRVIIKAIRKALQLCMEKINEMAVQIVEQSKDQQRalLEKCAATAMSSK 165
Cdd:TIGR02346 85 ENEIGDGTNLVLVLAGELLNKAEELIRMGLHPSEIIKGYEMALKKAMEILEELVVWEVKDLRDKDE--LIKALKASISSK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 166 LIHQQkDFFSRIVVDAVLSL----DELLPLNMIGIKKVTGGSLEESQLVSGVAFKKTfsyagFEMAPKSYDNCKIALLNI 241
Cdd:TIGR02346 163 QYGNE-DFLAQLVAQACSTVlpknPQNFNVDNIRVCKILGGSLSNSEVLKGMVFNRE-----AEGSVKSVKNAKVAVFSC 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 242 ELELKAERDNAEIRVDNVKEYQKVVDAEWQILYNKLAKIHESGANVVLSKLPIGDVAtQYFADRDIFCAGRVPEE-DLKR 320
Cdd:TIGR02346 237 PLDTATTETKGTVLIHNAEELLNYSKGEENQIEAMIKAIADSGVNVIVTGGSVGDMA-LHYLNKYNIMVLKIPSKfELRR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 321 TMKACGGAVMTTANDIKPNVLGLCEHFEERQVGGERFNLF-QGCPNAKTSTLILRGGAEQFLEETERSLHDAIMIVRRTI 399
Cdd:TIGR02346 316 LCKTVGATPLPRLGAPTPEEIGYVDSVYVSEIGGDKVTVFkQENGDSKISTIILRGSTDNLLDDIERAIDDGVNTVKALV 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 400 KHDSVVAGGGAIEMELSKLLRDYSRTIAGKEQLLIAAIAKGLEIIPRQLCDNAGFDATNILNKLRQKHAQGGQWYGVDIN 479
Cdd:TIGR02346 396 KDGRLLPGAGATEIELASRLTKYGEKLPGLDQYAIKKFAEAFEIIPRTLAENAGLNANEVIPKLYAAHKKGNKSKGIDIE 475
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 24645179 480 KEDIS--DNYEQCVWEPSIIKINALTAAAEAACMILSVDETIKSPKAG 525
Cdd:TIGR02346 476 AESDGvkDASEAGIYDMLATKKWAIKLATEAAVTVLRVDQIIMAKPAG 523
|
|
| TCP1_theta |
cd03341 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ... |
19-519 |
2.59e-93 |
|
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: 292.97 E-value: 2.59e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 19 PQLVSNINACQSIVDAVRTTLGPRGMDKLIVDAHGKATISNDGATIMKLLEIIHPAAKTLVDIAKSQDAEVGDGTTSVVL 98
Cdd:cd03341 8 EAVLRNIEACKELSQITRTSYGPNGMNKMVINHLEKLFVTSDAATILRELEVQHPAAKLLVMASQMQEEEIGDGTNLVVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 99 LAGEFLKQVKPFVEEGVHPRVIIKAIRKALQLCMEKINEMAVQIVEQSKDQQraLLEKCAATAMSSKLIHQQkDFFSRIV 178
Cdd:cd03341 88 LAGELLEKAEELLRMGLHPSEIIEGYEKALKKALEILEELVVYKIEDLRNKE--EVSKALKTAIASKQYGNE-DFLSPLV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 179 VDAVLSldeLLPLNM-------IGIKKVTGGSLEESQLVSGVAFKKtfsyaGFEMAPKSYDNCKIALLNIELELkaerdn 251
Cdd:cd03341 165 AEACIS---VLPENIgnfnvdnIRVVKILGGSLEDSKVVRGMVFKR-----EPEGSVKRVKKAKVAVFSCPFDI------ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 252 aeirvdnvkeyqkvvdaewqilynklakihesGANVVLSKLPIGDVAtQYFADRDIFCAGRVPEE-DLKRTMKACGGAVM 330
Cdd:cd03341 231 --------------------------------GVNVIVAGGSVGDLA-LHYCNKYGIMVIKINSKfELRRLCRTVGATPL 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 331 TTANDIKPNVLGLCEHFEERQVGGERFNLFQGCPNA-KTSTLILRGGAEQFLEETERSLHDAIMIVRRTIKHDSVVAGGG 409
Cdd:cd03341 278 PRLGAPTPEEIGYCDSVYVEEIGDTKVVVFRQNKEDsKIATIVLRGATQNILDDVERAIDDGVNVFKSLTKDGRFVPGAG 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 410 AIEMELSKLLRDYSRTIAGKEQLLIAAIAKGLEIIPRQLCDNAGFDATNILNKLRQKHAQGGQWYGVDINKEDIS--DNY 487
Cdd:cd03341 358 ATEIELAKKLKEYGEKTPGLEQYAIKKFAEAFEVVPRTLAENAGLDATEVLSELYAAHQKGNKSAGVDIESGDEGtkDAK 437
|
490 500 510
....*....|....*....|....*....|..
gi 24645179 488 EQCVWEPSIIKINALTAAAEAACMILSVDETI 519
Cdd:cd03341 438 EAGIFDHLATKKWAIKLATEAAVTVLRVDQII 469
|
|
| chap_CCT_beta |
TIGR02341 |
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ... |
7-521 |
1.79e-92 |
|
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: 292.53 E-value: 1.79e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 7 LLKEGTDSSQGKPQLVSNINACQSIVDAVRTTLGPRGMDKLIVDAHGKATI--SNDGATIMKLLEIIHPAAKTLVDIAKS 84
Cdd:TIGR02341 2 IFKDGADEERAENARLSSFVGAIAIGDLVKSTLGPKGMDKILQSSSSDASImvTNDGATILKSIGVDNPAAKVLVDMSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 85 QDAEVGDGTTSVVLLAGEFLKQVKPFVEEGVHPRVIIKAIRKALQLCMEKINEMAVqivEQSKDQQ--RALLEKCAATAM 162
Cdd:TIGR02341 82 QDDEVGDGTTSVTVLAAELLREAEKLINQKIHPQTIIAGYREATKAARDALLKSAV---DNGSDEVkfRQDLMNIARTTL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 163 SSKLIHQQKDFFSRIVVDAVLSLDELLPLNMIGIKKVTGGSLEESQLVSGVAFKKTFSYagfeMAPKSYDNCKIALLNIE 242
Cdd:TIGR02341 159 SSKILSQHKDHFAQLAVDAVLRLKGSGNLEAIQIIKKLGGSLADSYLDEGFLLDKKIGV----NQPKRIENAKILIANTG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 243 LEL-KAERDNAEIRVDNVKEYQKVVDAEWQILYNKLAKIHESGANVVLSKLPIGDVATQYFADRDIFCAGRVPEEDLKRT 321
Cdd:TIGR02341 235 MDTdKVKIFGSRVRVDSTAKVAELEHAEKEKMKEKVEKILKHGINCFINRQLIYNYPEQLFADAGVMAIEHADFEGVERL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 322 MKACGGAVMTTANDIKPNVLGLCEHFEERQVGGERFNLFQGCPNAKTSTLILRGGAEQFLEETERSLHDAIMIVRRTIKH 401
Cdd:TIGR02341 315 ALVTGGEIVSTFDHPELVKLGSCDLIEEIMIGEDKLLKFSGVKLGEACTIVLRGATQQILDEAERSLHDALCVLSQTVKE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 402 DSVVAGGGAIEMELSKLLRDYSRTIAGKEQLLIAAIAKGLEIIPRQLCDNAGFDATNILNKLRQKHAQGGQWYGVDINKE 481
Cdd:TIGR02341 395 SRTVLGGGCSEMLMSKAVTQEAQRTPGKEALAVEAFARALRQLPTIIADNAGFDSAELVAQLRAAHYNGNTTMGLDMNEG 474
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 24645179 482 DISDNYEQCVWEPSIIKINALTAAAEAACMILSVDETIKS 521
Cdd:TIGR02341 475 TIADMRQLGITESYKVKRAVVSSAAEAAEVILRVDNIIKA 514
|
|
| GroEL |
COG0459 |
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ... |
23-494 |
4.49e-87 |
|
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227 Cd Length: 497 Bit Score: 277.73 E-value: 4.49e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 23 SNINACQSIVDAVRTTLGPRGMDKLIVDAHGKATISNDGATIMKLLEIIHP----AAKTLVDIAKSQDAEVGDGTTSVVL 98
Cdd:COG0459 14 ANIRGVKALADAVKVTLGPKGRNVMLVKSFGDPTITNDGVTIAKEIELEDPfenmGAQLVKEVASKTNDEAGDGTTTATV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 99 LAGEFLKQVKPFVEEGVHPRVIIKAIRKALQLCMEKINEMAVQIveqskdQQRALLEKCAATAMSSKlihqqkDFFSRIV 178
Cdd:COG0459 94 LAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPV------DDKEELAQVATISANGD------EEIGELI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 179 VDAVlsldellplNMIGIKKVT----GGSLE-ESQLVSGVAFKKTFSYAGF----EMAPKSYDNCKIALLNIELElkaer 249
Cdd:COG0459 162 AEAM---------EKVGKDGVItveeGKGLEtELEVVEGMQFDKGYLSPYFvtdpEKMPAELENAYILLTDKKIS----- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 250 dnaeirvdNVKEYQKVVDaewqilynklaKIHESGANVVLSKLPIGDVATQYFADRDIFCAGRVP-----------EEDL 318
Cdd:COG0459 228 --------SIQDLLPLLE-----------KVAQSGKPLLIIAEDIDGEALATLVVNGIRGVLRVVavkapgfgdrrKAML 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 319 KRTMKACGGAVMT-----TANDIKPNVLGLCEHFEerqVGGERFNLFQGCPNAKTSTLILRGGAEQFLEETERSLHDAIM 393
Cdd:COG0459 289 EDIAILTGGRVISedlglKLEDVTLDDLGRAKRVE---VDKDNTTIVEGAGNPKAIVILVGAATEVEVKERKRRVEDALH 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 394 IVRRTIKhDSVVAGGGAIEMELSKLLRDYSRTIAGKEQLLIAAIAKGLEIIPRQLCDNAGFDATNILNKLRqkhAQGGQW 473
Cdd:COG0459 366 ATRAAVE-EGIVPGGGAALLRAARALRELAAKLEGDEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKVR---AAKDKG 441
|
490 500
....*....|....*....|.
gi 24645179 474 YGVDINKEDISDNYEQCVWEP 494
Cdd:COG0459 442 FGFDAATGEYVDMLEAGVIDP 462
|
|
| TCP1_zeta |
cd03342 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
24-520 |
1.48e-78 |
|
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: 254.88 E-value: 1.48e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 24 NINACQSIVDAVRTTLGPRGMDKLIVDAHGKATISNDGATIMKLLEIIHPAAKTLVDIAKSQDAEVGDGTTSVVLLAGEF 103
Cdd:cd03342 17 NISAAKGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLSEMQIQHPTASMIARAATAQDDITGDGTTSNVLLIGEL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 104 LKQVKPFVEEGVHPRVIIKAIRKALQLCMEKINEMAVQIVEqskDQQRALLEKCAATAMSSKLIHQQKDFFSRIVVDAVL 183
Cdd:cd03342 97 LKQAERYIQEGVHPRIITEGFELAKNKALKFLESFKVPVEI---DTDRELLLSVARTSLRTKLHADLADQLTEIVVDAVL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 184 SL---DELLPLNMIGIKKVTGGSLEESQLVSGVAFKKTFSYAgfEMaPKSYDNCKIALLNIELELkaerDNAEIrvdNVK 260
Cdd:cd03342 174 AIykpDEPIDLHMVEIMQMQHKSDSDTKLIRGLVLDHGARHP--DM-PKRVENAYILTCNVSLEY----EKTEV---NSG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 261 EYQKVVdaewqilynklakIHESGanvvlsklpIGDVATQYFADRDIFCAGRVPEEDLKRTMKACGGAVMTTANDIKPNV 340
Cdd:cd03342 244 FFYSVV-------------INQKG---------IDPPSLDMLAKEGILALRRAKRRNMERLTLACGGVAMNSVDDLSPEC 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 341 LGLCEHFEERQVGGERFNLFQGCPNAKTSTLILRGGAEQFLEETERSLHDAIMIVRRTIKHDSVVAGGGAIEMELSKLLR 420
Cdd:cd03342 302 LGYAGLVYERTLGEEKYTFIEGVKNPKSCTILIKGPNDHTITQIKDAIRDGLRAVKNAIEDKCVVPGAGAFEVALYAHLK 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 421 DYSRTIAGKEQLLIAAIAKGLEIIPRQLCDNAGFDATNILNKLRQKHAQGGQWYGVDINKEDISDNYEQCVWEPSIIKIN 500
Cdd:cd03342 382 EFKKSVKGKAKLGVQAFADALLVIPKTLAENSGLDVQETLVKLQDEYAEGGQVGGVDLDTGEPMDPESEGIWDNYSVKRQ 461
|
490 500
....*....|....*....|
gi 24645179 501 ALTAAAEAACMILSVDETIK 520
Cdd:cd03342 462 ILHSATVIASQLLLVDEIIR 481
|
|
| chap_CCT_zeta |
TIGR02347 |
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ... |
5-524 |
5.18e-77 |
|
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: 252.35 E-value: 5.18e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 5 IVLLKEGTDSSQGKPQLVSNINACQSIVDAVRTTLGPRGMDKLIVDAHGKATISNDGATIMKLLEIIHPAAKTLVDIAKS 84
Cdd:TIGR02347 2 VKLLNPKAESLRRDAALMMNINAARGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEMQIQHPTASMIARAATA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 85 QDAEVGDGTTSVVLLAGEFLKQVKPFVEEGVHPRVIIKAIRKALQLCMEKINEMAVQIvEQSKDqqRALLEKCAATAMSS 164
Cdd:TIGR02347 82 QDDITGDGTTSTVLLIGELLKQAERYILEGVHPRIITEGFEIARKEALQFLDKFKVKK-EDEVD--REFLLNVARTSLRT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 165 KLIHQQKDFFSRIVVDAVLSL---DELLPLNMIGIKKVTGGSLEESQLVSGVAFKKTFSYAGFemaPKSYDNCKIALLNI 241
Cdd:TIGR02347 159 KLPADLADQLTEIVVDAVLAIkkdGEDIDLFMVEIMEMKHKSATDTTLIRGLVLDHGARHPDM---PRRVKNAYILTCNV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 242 ELELKAERDNAEIRVDNVKEYQKVVDAEWQILYNKLAKIHE-------SGAN---VVLSKLPIGDVATQYFADRDIFCAG 311
Cdd:TIGR02347 236 SLEYEKTEVNSGFFYSSAEQREKLVKAERKFVDDRVKKIIElkkkvcgKSPDkgfVVINQKGIDPPSLDLLAKEGIMALR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 312 RVPEEDLKRTMKACGGAVMTTANDIKPNVLGLCEHFEERQVGGERFNLFQGCPNAKTSTLILRGGAEQFLEETERSLHDA 391
Cdd:TIGR02347 316 RAKRRNMERLTLACGGEALNSVEDLTPECLGWAGLVYETTIGEEKYTFIEECKNPKSCTILIKGPNDHTIAQIKDAVRDG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 392 IMIVRRTIKHDSVVAGGGAIEMELSKLLRDYSRTIAGKEQLLIAAIAKGLEIIPRQLCDNAGFDATNILNKLRQKHAQGG 471
Cdd:TIGR02347 396 LRAVKNAIEDKCVVPGAGAFEIAAYRHLKEYKKSVKGKAKLGVEAFANALLVIPKTLAENSGFDAQDTLVKLEDEHDEGG 475
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 24645179 472 QWYGVDINKEDISDNYEQCVWEPSIIKINALTAAAEAACMILSVDETIKSPKA 524
Cdd:TIGR02347 476 EVVGVDLNTGEPIDPEIKGIWDNYRVKKQLIQSATVIASQLLLVDEVMRAGRS 528
|
|
| chaperonin_like |
cd03333 |
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ... |
151-401 |
1.46e-63 |
|
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: 206.55 E-value: 1.46e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 151 RALLEKCAATAMSSKlIHQQKDFFSRIVVDAVLSL---DELLPLNMIGIKKVTGGSLEESQLVSGVAFKKTFSYAGFema 227
Cdd:cd03333 1 RELLLQVATTSLNSK-LSSWDDFLGKLVVDAVLKVgpdNRMDDLGVIKVEKIPGGSLEDSELVVGVVFDKGYASPYM--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 228 PKSYDNCKIALLNIELElkaerdnaeirvdnvkeyqkvvdaewqilynklakihesgaNVVLSKLPIGDVATQYFADRDI 307
Cdd:cd03333 77 PKRLENAKILLLDCPLE-----------------------------------------YVVIAEKGIDDLALHYLAKAGI 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 308 FCAGRVPEEDLKRTMKACGGAVMTTANDIKPNVLGLCEHFEERQVGGERFNLFQGCPNAKTSTLILRGGAEQFLEETERS 387
Cdd:cd03333 116 MAVRRVKKEDLERIARATGATIVSSLEDLTPEDLGTAELVEETKIGEEKLTFIEGCKGGKAATILLRGATEVELDEVKRS 195
|
250
....*....|....
gi 24645179 388 LHDAIMIVRRTIKH 401
Cdd:cd03333 196 LHDALCAVRAAVEE 209
|
|
| groEL |
CHL00093 |
chaperonin GroEL |
31-495 |
4.57e-18 |
|
chaperonin GroEL
Pssm-ID: 177025 Cd Length: 529 Bit Score: 87.08 E-value: 4.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 31 IVDAVRTTLGPRGMDKLIVDAHGKATISNDGATIMKLLEIIHPAAKT---LVDIAKSQDAEV-GDGTTSVVLLAGEFLKQ 106
Cdd:CHL00093 22 LAEAVSVTLGPKGRNVVLEKKYGSPQIVNDGVTIAKEIELEDHIENTgvaLIRQAASKTNDVaGDGTTTATVLAYAIVKQ 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 107 VKPFVEEGVHPRVIIKAIRKALQLCMEKINEMAvQIVEQSKDQQRALLEKCAATAMSSKLIhqqKDFFSRIVVDAVLSLD 186
Cdd:CHL00093 102 GMKNVAAGANPISLKRGIEKATQYVVSQIAEYA-RPVEDIQAITQVASISAGNDEEVGSMI---ADAIEKVGREGVISLE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 187 EllplnmigiKKVTGGSLEESQlvsGVAFKKTFSYAGFEMAPK----SYDNC-------KIALLNIE----LEL--KAER 249
Cdd:CHL00093 178 E---------GKSTVTELEITE---GMRFEKGFISPYFVTDTErmevVQENPyilltdkKITLVQQDllpiLEQvtKTKR 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 250 DNAEIRVDNVKEyqkvvdAEWQILYNKLAKIhesgANVVLSKLP-IGDVATQYFADRDIFCAGRVPEEDLKRTMKACGGA 328
Cdd:CHL00093 246 PLLIIAEDVEKE------ALATLVLNKLRGI----VNVVAVRAPgFGDRRKAMLEDIAILTGGQVITEDAGLSLETIQLD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 329 VMTTANDI--------------KPNVLGLCEHFE----------ERQVGGERFnlfqgcpnAKTS---TLILRGGA-EQF 380
Cdd:CHL00093 316 LLGQARRIivtkdsttiiadgnEEQVKARCEQLRkqieiadssyEKEKLQERL--------AKLSggvAVIKVGAAtETE 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 381 LEETERSLHDAIMIVRRTIKhDSVVAGGGAIEMELSKLLRDYSRTIAGKEQLLIAAI-AKGLEIIPRQLCDNAGFDATNI 459
Cdd:CHL00093 388 MKDKKLRLEDAINATKAAVE-EGIVPGGGATLVHLSENLKTWAKNNLKEDELIGALIvARAILAPLKRIAENAGKNGSVI 466
|
490 500 510
....*....|....*....|....*....|....*.
gi 24645179 460 LNKLRQKHAQggqwYGVDINKEDISDNYEQCVWEPS 495
Cdd:CHL00093 467 IEKVQEQDFE----IGYNAANNKFVNMYEAGIIDPA 498
|
|
| Fab1_TCP |
cd03334 |
TCP-1 like domain of the eukaryotic phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinase Fab1. ... |
186-395 |
4.15e-14 |
|
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: 72.25 E-value: 4.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 186 DELLPLNMIGIKKVTGGSLEESQLVSGVAFKKTFSYAGfeMaPKSYDNCKIALLNIELELkAERDNAEIRVDNVKEYQKV 265
Cdd:cd03334 42 DDMDIRQYVKIKKIPGGSPSDSEVVDGVVFTKNVAHKR--M-PSKIKNPRILLLQGPLEY-QRVENKLLSLDPVILQEKE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 266 vdaewqILYNKLAKIHESGANVVLSKLPIGDVATQYFADRDIFCAGRVPEEDLKRTMKACGGAVMTTAND-IKPNVLGLC 344
Cdd:cd03334 118 ------YLKNLVSRIVALRPDVILVEKSVSRIAQDLLLEAGITLVLNVKPSVLERISRCTGADIISSMDDlLTSPKLGTC 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 24645179 345 EHFEERQV---GGERFNL--FQGCPNAKTSTLILRGGAEQFLEETERSLHDAIMIV 395
Cdd:cd03334 192 ESFRVRTYveeHGRSKTLmfFEGCPKELGCTILLRGGDLEELKKVKRVVEFMVFAA 247
|
|
| PTZ00114 |
PTZ00114 |
Heat shock protein 60; Provisional |
25-463 |
1.14e-13 |
|
Heat shock protein 60; Provisional
Pssm-ID: 185455 Cd Length: 555 Bit Score: 73.41 E-value: 1.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 25 INACQSIVDAVRTTLGPRGMDKLIVDAHGKATISNDGATIMKLLEIIHPA----AKTLVDIAKSQDAEVGDGTTSVVLLA 100
Cdd:PTZ00114 28 LKGIERLADAVAVTLGPKGRNVIIEQEYGSPKITKDGVTVAKAIEFSDRFenvgAQLIRQVASKTNDKAGDGTTTATILA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 101 GEFLKQVKPFVEEGVHPRVIIKAIRKALQLCMEKINEMAvQIVEQSKDqqralLEKCAATAMS-----SKLIHQQkdfFS 175
Cdd:PTZ00114 108 RAIFREGCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQS-RPVKTKED-----ILNVATISANgdveiGSLIADA---MD 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 176 RIVVDAVLSLDEllplnmigikkvtGGSLE-ESQLVSGVAFKKTFSYAGFEMAPKS----YDN-----CKIALLNIE--- 242
Cdd:PTZ00114 179 KVGKDGTITVED-------------GKTLEdELEVVEGMSFDRGYISPYFVTNEKTqkveLENplilvTDKKISSIQsil 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 243 --LEL-KAERDNAEIRVDNVKEyqkvvDAEWQILYNKLakihESGANVVLSKLP-IGDVATQYFADRDIFCAGRVPEEDl 318
Cdd:PTZ00114 246 piLEHaVKNKRPLLIIAEDVEG-----EALQTLIINKL----RGGLKVCAVKAPgFGDNRKDILQDIAVLTGATVVSED- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 319 krtmkacggAVMTTANDIKPNVLGLCEHFEERQ-----VGG--------ERFNLFQGCPNAKTS---------------- 369
Cdd:PTZ00114 316 ---------NVGLKLDDFDPSMLGSAKKVTVTKdetviLTGggdkaeikERVELLRSQIERTTSeydkeklkerlaklsg 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 370 --TLILRGGAEQF-LEETERSLHDAIMIVRRTIKhDSVVAGGGAIEMELSKLLrDY---SRTIAGKEQLLIAAIAKGLEI 443
Cdd:PTZ00114 387 gvAVIKVGGASEVeVNEKKDRIEDALNATRAAVE-EGIVPGGGVALLRASKLL-DKleeDNELTPDQRTGVKIVRNALRL 464
|
490 500
....*....|....*....|
gi 24645179 444 IPRQLCDNAGFDATNILNKL 463
Cdd:PTZ00114 465 PTKQIAENAGVEGAVVVEKI 484
|
|
| GroEL |
cd03344 |
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ... |
28-142 |
1.03e-12 |
|
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: 70.56 E-value: 1.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 28 CQSIVDAVRTTLGPRGMDKLIVDAHGKATISNDGATIMKllEIIHP------AAKTLVDIAKSQDAEVGDGTTSVVLLAG 101
Cdd:cd03344 17 VNKLADAVKVTLGPKGRNVVIEKSFGSPKITKDGVTVAK--EIELEdpfenmGAQLVKEVASKTNDVAGDGTTTATVLAR 94
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 24645179 102 EFLKQVKPFVEEGVHPRVIIKAIRKALQLCMEKINEMAVQI 142
Cdd:cd03344 95 AIIKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKPV 135
|
|
| PLN03167 |
PLN03167 |
Chaperonin-60 beta subunit; Provisional |
31-463 |
5.53e-12 |
|
Chaperonin-60 beta subunit; Provisional
Pssm-ID: 215611 [Multi-domain] Cd Length: 600 Bit Score: 68.41 E-value: 5.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 31 IVDAVRTTLGPRGMDKLIVDAHGKATISNDGATIMKLLEIIHP----AAKTLVDIAKSQDAEVGDGTTSVVLLAGEFLKQ 106
Cdd:PLN03167 78 LADLVGVTLGPKGRNVVLESKYGSPKIVNDGVTVAKEVELEDPveniGAKLVRQAAAKTNDLAGDGTTTSVVLAQGLIAE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 107 VKPFVEEGVHPRVIIKAIRKALQLCMEKINEMAVQiVEQSKdqqraLLEKCAATAMSSKLIHQQ-KDFFSRIVVDAVLSL 185
Cdd:PLN03167 158 GVKVVAAGANPVQITRGIEKTAKALVKELKKMSKE-VEDSE-----LADVAAVSAGNNYEVGNMiAEAMSKVGRKGVVTL 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 186 DEllplnmigikkvtGGSLEES-QLVSGVAFKKTFSYAGF----EMAPKSYDNCKiaLLNIELELKAERDNAEIRVDNVK 260
Cdd:PLN03167 232 EE-------------GKSAENNlYVVEGMQFDRGYISPYFvtdsEKMSVEYDNCK--LLLVDKKITNARDLIGILEDAIR 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 261 EYQKVV----DAEWQILYNKLAKIHESGANVVLSKLP-IGDVATQYFADRDIFCAGRVPEEDLKRTMKACGGAVMTTA-- 333
Cdd:PLN03167 297 GGYPLLiiaeDIEQEALATLVVNKLRGSLKIAALKAPgFGERKSQYLDDIAILTGGTVIREEVGLSLDKVGKEVLGTAak 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 334 ------------------------NDIKpNVLGLCEHFEERQVGGERFNLFQGcpnaktSTLILRGGAEQFLEETERSL- 388
Cdd:PLN03167 377 vvltkdtttivgdgstqeavnkrvAQIK-NLIEAAEQDYEKEKLNERIAKLSG------GVAVIQVGAQTETELKEKKLr 449
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24645179 389 -HDAIMIVRRTIKhDSVVAGGGAIEMELSKLLRDYSRTIAGKEQLLIAAIAKGLEIIPRQL-CDNAGFDATNILNKL 463
Cdd:PLN03167 450 vEDALNATKAAVE-EGIVVGGGCTLLRLASKVDAIKDTLENDEQKVGADIVKRALSYPLKLiAKNAGVNGSVVSEKV 525
|
|
| groEL |
PRK12852 |
chaperonin GroEL; Reviewed |
31-495 |
6.21e-11 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237232 Cd Length: 545 Bit Score: 64.87 E-value: 6.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 31 IVDAVRTTLGPRGMDKLIVDAHGKATISNDGATIMKLLEII----HPAAKTLVDIAKSQDAEVGDGTTSVVLLAGEFLKQ 106
Cdd:PRK12852 23 LANAVKVTLGPKGRNVVIEKSFGAPRITKDGVTVAKEIELEdkfeNMGAQMVREVASKTNDLAGDGTTTATVLAQAIVRE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 107 VKPFVEEGVHPRVIIKAIRKALQLCMEKINEMAVQIVEQSKDQQRALLEKCAATAMsSKLIHQQKDffsRIVVDAVLSLD 186
Cdd:PRK12852 103 GAKAVAAGMNPMDLKRGIDIAVAAVVKDIEKRAKPVASSAEIAQVGTISANGDAAI-GKMIAQAMQ---KVGNEGVITVE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 187 EllplnmigikkvtGGSLE-ESQLVSGVAFKKTFsyagfeMAPKSYDNCKiallnielELKAERDNAEI-----RVDNVK 260
Cdd:PRK12852 179 E-------------NKSLEtEVDIVEGMKFDRGY------LSPYFVTNAE--------KMTVELDDAYIllhekKLSGLQ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 261 EYQKVVDAEWQ-------------------ILYNKLakihESGANVVLSKLP-IGDVATQYFADRDIFCAGRVPEEDL-- 318
Cdd:PRK12852 232 AMLPVLEAVVQsgkplliiaedvegealatLVVNRL----RGGLKVAAVKAPgFGDRRKAMLEDIAILTGGQLISEDLgi 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 319 ---KRTMKACGGA--VMT------------TANDIKPNVLGLCEHFEERQVGGERFNLFQGCPNAKTSTLILR-GGA-EQ 379
Cdd:PRK12852 308 kleNVTLKMLGRAkkVVIdkenttivngagKKADIEARVGQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRvGGAtEV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 380 FLEETERSLHDAIMIVRRTIKhDSVVAGGGA----IEMELSKLLRDYSRTIAGkeqllIAAIAKGLEIIPRQLCDNAGFD 455
Cdd:PRK12852 388 EVKEKKDRVEDALNATRAAVQ-EGIVPGGGVallrAKKAVGRINNDNADVQAG-----INIVLKALEAPIRQIAENAGVE 461
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 24645179 456 ATNILNKLRQKHaqgGQWYGVDINKEDISDNYEQCVWEPS 495
Cdd:PRK12852 462 GSIVVGKILENK---SETFGFDAQTEEYVDMVAKGIIDPA 498
|
|
| groEL |
PRK12850 |
chaperonin GroEL; Reviewed |
33-152 |
8.57e-11 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237231 Cd Length: 544 Bit Score: 64.35 E-value: 8.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 33 DAVRTTLGPRGMDKLIVDAHGKATISNDGATIMKLLEIIHP----AAKTLVDIAKSQDAEVGDGTTSVVLLAGEFLKQVK 108
Cdd:PRK12850 25 NAVKVTLGPKGRNVVLEKSFGAPRITKDGVTVAKEIELEDKfenmGAQMVKEVASKTNDLAGDGTTTATVLAQAIVREGA 104
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 24645179 109 PFVEEGVHPRVIIKAIRKALQLCMEKINEMAVQIVEQSKDQQRA 152
Cdd:PRK12850 105 KLVAAGMNPMDLKRGIDLAVAAVVDELKKIAKKVTSSKEIAQVA 148
|
|
| groEL |
PRK12849 |
chaperonin GroEL; Reviewed |
33-142 |
3.82e-10 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237230 Cd Length: 542 Bit Score: 62.13 E-value: 3.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 33 DAVRTTLGPRGMDKLIVDAHGKATISNDGATIMKLLEIIHP----AAKTLVDIAKSQDAEVGDGTTSVVLLAGEFLKQVK 108
Cdd:PRK12849 24 DAVKVTLGPKGRNVVIDKSFGAPTITKDGVSIAKEIELEDPfenlGAQLVKEVASKTNDVAGDGTTTATVLAQALVQEGL 103
|
90 100 110
....*....|....*....|....*....|....
gi 24645179 109 PFVEEGVHPRVIIKAIRKALQLCMEKINEMAVQI 142
Cdd:PRK12849 104 KNVAAGANPMDLKRGIDKAVEAVVEELKALARPV 137
|
|
| PRK14104 |
PRK14104 |
chaperonin GroEL; Provisional |
31-495 |
5.52e-10 |
|
chaperonin GroEL; Provisional
Pssm-ID: 172594 Cd Length: 546 Bit Score: 61.97 E-value: 5.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 31 IVDAVRTTLGPRGMDKLIVDAHGKATISNDGATIMKLLEII----HPAAKTLVDIA-KSQDAeVGDGTTSVVLLAGEFLK 105
Cdd:PRK14104 23 LANAVKVTLGPKGRNVVLDKSFGAPRITKDGVTVAKEIELEdkfeNMGAQMVREVAsKSADA-AGDGTTTATVLAQAIVR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 106 QVKPFVEEGVHPRVIIKAIRKALQLCMEKINEMAVQIVEQSKDQQRALLEKCAATAMSSKLihqqKDFFSRIVVDAVLSL 185
Cdd:PRK14104 102 EGAKSVAAGMNPMDLKRGIDLAVEAVVADLVKNSKKVTSNDEIAQVGTISANGDAEIGKFL----ADAMKKVGNEGVITV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 186 DEllplnmigikkvtGGSLE-ESQLVSGVAFKKTFsyagfeMAPKSYDNCKiallnielELKAERDNA-----EIRVDNV 259
Cdd:PRK14104 178 EE-------------AKSLEtELDVVEGMQFDRGY------ISPYFVTNAD--------KMRVEMDDAyilinEKKLSSL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 260 KE----YQKVV-----------DAEWQILYNKLAKIHESGANVVLSKLP-IGDVATQYFADRDIFCAGRVPEEDL----- 318
Cdd:PRK14104 231 NEllplLEAVVqtgkplvivaeDVEGEALATLVVNRLRGGLKVAAVKAPgFGDRRKAMLQDIAILTGGQAISEDLgikle 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 319 KRTMKACGGA--VM------TTAN------DIKPNVLGLCEHFEERQVGGERFNLFQGCPNAKTSTLILRGGAEQFLEET 384
Cdd:PRK14104 311 NVTLQMLGRAkkVMidkentTIVNgagkkaDIEARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVK 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 385 ERS--LHDAIMIVRRTIKhDSVVAGGGAIEMELSKLLRDYsRTIAGKEQLLIAAIAKGLEIIPRQLCDNAGFDATNILNK 462
Cdd:PRK14104 391 ERKdrVDDAMHATRAAVE-EGIVPGGGVALLRASEQLKGI-KTKNDDQKTGVEIVRKALSAPARQIAINAGEDGSVIVGK 468
|
490 500 510
....*....|....*....|....*....|...
gi 24645179 463 LRQKHAQGgqwYGVDINKEDISDNYEQCVWEPS 495
Cdd:PRK14104 469 ILEKEQYS---YGFDSQTGEYGNLVSKGIIDPT 498
|
|
| groEL |
PRK12851 |
chaperonin GroEL; Reviewed |
33-152 |
8.33e-10 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 171770 Cd Length: 541 Bit Score: 61.30 E-value: 8.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 33 DAVRTTLGPRGMDKLIVDAHGKATISNDGATIMKLLEIIHP----AAKTLVDIAKSQDAEVGDGTTSVVLLAGEFLKQVK 108
Cdd:PRK12851 25 DAVKVTLGPKGRNVVIDKSFGAPTITNDGVTIAKEIELEDKfenmGAQMVREVASKTNDVAGDGTTTATVLAQAIVREGA 104
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 24645179 109 PFVEEGVHPRVIIKAIRKALQLCMEKINEMAVQIVEQSKDQQRA 152
Cdd:PRK12851 105 KAVAAGANPMDLKRGIDRAVAAVVEELKANARPVTTNAEIAQVA 148
|
|
| GroEL |
TIGR02348 |
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ... |
33-142 |
1.42e-09 |
|
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: 60.38 E-value: 1.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 33 DAVRTTLGPRGMDKLIVDAHGKATISNDGATIMKLLEIIHP----AAKTLVDIAKSQDAEVGDGTTSVVLLAGEFLKQVK 108
Cdd:TIGR02348 23 DAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDKfenmGAQLVKEVASKTNDVAGDGTTTATVLAQAIVKEGL 102
|
90 100 110
....*....|....*....|....*....|....
gi 24645179 109 PFVEEGVHPRVIIKAIRKALQLCMEKINEMAVQI 142
Cdd:TIGR02348 103 KNVAAGANPIELKRGIEKAVEAVVEELKKLSKPV 136
|
|
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
33-142 |
4.37e-07 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 52.43 E-value: 4.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645179 33 DAVRTTLGPRGMDKLIVDAHGKATISNDGATIMKLLEIIHP----AAKTLVDIAKSQDAEVGDGTTSVVLLAGEFLKQVK 108
Cdd:PRK00013 24 DAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDPfenmGAQLVKEVASKTNDVAGDGTTTATVLAQAIVREGL 103
|
90 100 110
....*....|....*....|....*....|....
gi 24645179 109 PFVEEGVHPRVIIKAIRKALQLCMEKINEMAVQI 142
Cdd:PRK00013 104 KNVAAGANPMDLKRGIDKAVEAAVEELKKISKPV 137
|
|
| |
