|
Name |
Accession |
Description |
Interval |
E-value |
| chap_CCT_gamma |
TIGR02344 |
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ... |
7-528 |
0e+00 |
|
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: 984.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 7 PILVLSQNTKRESGRKVQLENIQAGKAIADVIRTCLGPQAMLKMLMDPMGGIVMTNDGNAILREITVQHPAAKSMIEIAR 86
Cdd:TIGR02344 1 PVLVLNQNTKRESGRKAQLSNIQAAKAVADIIRTCLGPRSMLKMLLDPMGGIVMTNDGNAILREIDVAHPAAKSMIELSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 87 TQDEEVGDGTTSVIVLAGEMLAAAEPFLQQQIHPTVIIRAYREALEDIVGHLQsQLSIQLDVKDKAKMADVVKACVGTKF 166
Cdd:TIGR02344 81 TQDEEVGDGTTSVIILAGEMLSVAEPFLEQNIHPTVIIRAYRKALDDALSVLE-EISIPVDVNDDAAMLKLIQSCIGTKF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 167 IGKWSDLAVKIALDAVETVTLSENGRLEVDIKRYAKVEKIPGGAIEESCVLKGVMINKDVTHPKMRRLIENPRIVLLDCS 246
Cdd:TIGR02344 160 VSRWSDLMCDLALDAVRTVQRDENGRKEIDIKRYAKVEKIPGGDIEDSCVLKGVMINKDVTHPKMRRYIENPRIVLLDCP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 247 LEYKKGESQTNVEIIGEQDFTRMLQIEEEFVQRICADIIAVKPDLVFTEKGVSDLAQHYLLKAGITAIRRLRKTDNLRIA 326
Cdd:TIGR02344 240 LEYKKGESQTNIEITKEEDWNRILQMEEEYVQLMCEDIIAVKPDLVITEKGVSDLAQHYLLKANITAIRRVRKTDNNRIA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 327 RACGATIVNRTEELTEKDVGTGAGLFEVKKIGDEYFTFVTECKEPKACTILLRGASKDILNETERNLQDALHVARNLVLE 406
Cdd:TIGR02344 320 RACGATIVNRPEELRESDVGTGCGLFEVKKIGDEYFTFITECKDPKACTILLRGASKDILNEVERNLQDAMAVARNVLLD 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 407 PRLVAGGGAVEMAASQLLTRKQVK------GPYTAVAHALEIIPRTLAQNCGANTIRALTALRAKHAshtGDGVCAWGID 480
Cdd:TIGR02344 400 PKLVPGGGATEMAVSVALTEKSKKlegveqWPYRAVADALEIIPRTLAQNCGANVIRTLTELRAKHA---QENNCTWGID 476
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 24647510 481 GESGEIVDMNVKNIWEPLAVKLQTYKTAVETAILLLRIDDIVSGSKKR 528
Cdd:TIGR02344 477 GETGKIVDMKEKGIWEPLAVKLQTYKTAIESACLLLRIDDIVSGVKKK 524
|
|
| TCP1_gamma |
cd03337 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ... |
7-524 |
0e+00 |
|
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: 908.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 7 PILVLSQNTKRESGRKVQLENIQAGKAIADVIRTCLGPQAMLKMLMDPMGGIVMTNDGNAILREITVQHPAAKSMIEIAR 86
Cdd:cd03337 1 PVLVLNQNTKRESGRKAQLGNIQAAKTVADVIRTCLGPRAMLKMLLDPMGGIVLTNDGNAILREIDVAHPAAKSMIELSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 87 TQDEEVGDGTTSVIVLAGEMLAAAEPFLQQQIHPTVIIRAYREALEDIVGHLQsQLSIQLDVKDKAKMADVVKACVGTKF 166
Cdd:cd03337 81 TQDEEVGDGTTSVIILAGEILAVAEPFLERGIHPTVIIKAYRKALEDALKILE-EISIPVDVNDRAQMLKIIKSCIGTKF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 167 IGKWSDLAVKIALDAVETVTLSENGRL-EVDIKRYAKVEKIPGGAIEESCVLKGVMINKDVTHPKMRRLIENPRIVLLDC 245
Cdd:cd03337 160 VSRWSDLMCNLALDAVKTVAVEENGRKkEIDIKRYAKVEKIPGGEIEDSRVLDGVMLNKDVTHPKMRRRIENPRIVLLDC 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 246 SLEYkkgesqtnveiigeqdftrmlqieeefvqricadiiavkpdLVFTEKGVSDLAQHYLLKAGITAIRRLRKTDNLRI 325
Cdd:cd03337 240 PLEY-----------------------------------------LVITEKGVSDLAQHYLVKAGITALRRVRKTDNNRI 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 326 ARACGATIVNRTEELTEKDVGTGAGLFEVKKIGDEYFTFVTECKEPKACTILLRGASKDILNETERNLQDALHVARNLVL 405
Cdd:cd03337 279 ARACGATIVNRPEELTESDVGTGAGLFEVKKIGDEYFTFITECKDPKACTILLRGASKDVLNEVERNLQDAMAVARNIIL 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 406 EPRLVAGGGAVEMAASQLLTRK------QVKGPYTAVAHALEIIPRTLAQNCGANTIRALTALRAKHAShtgDGVCAWGI 479
Cdd:cd03337 359 NPKLVPGGGATEMAVSHALSEKaksiegVEQWPYKAVASALEVIPRTLAQNCGANVIRTLTELRAKHAQ---GENSTWGI 435
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 24647510 480 DGESGEIVDMNVKNIWEPLAVKLQTYKTAVETAILLLRIDDIVSG 524
Cdd:cd03337 436 DGETGDIVDMKELGIWDPLAVKAQTYKTAIEAACMLLRIDDIVSG 480
|
|
| chaperonin_type_I_II |
cd00309 |
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ... |
15-523 |
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: 564.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 15 TKRESGRKVQLENIQAGKAIADVIRTCLGPQAMLKMLMDPMGGIVMTNDGNAILREITVQHPAAKSMIEIARTQDEEVGD 94
Cdd:cd00309 1 KEREFGEEARLSNINAAKALADAVKTTLGPKGMDKMLVDSLGDPTITNDGATILKEIEVEHPAAKLLVEVAKSQDDEVGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 95 GTTSVIVLAGEMLAAAEPFLQQQIHPTVIIRAYREALEDIVGHLQSqLSIQLDVKDKAKMADVVKACVGTKFIGKWSDLA 174
Cdd:cd00309 81 GTTTVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKE-IAVPIDVEDREELLKVATTSLNSKLVSGGDDFL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 175 VKIALDAVETVTLSENgrleVDIKRYAKVEKIPGGAIEESCVLKGVMINKDVTHPKMRRLIENPRIVLLDCSLEYkkges 254
Cdd:cd00309 160 GELVVDAVLKVGKENG----DVDLGVIRVEKKKGGSLEDSELVVGMVFDKGYLSPYMPKRLENAKILLLDCKLEY----- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 255 qtnveiigeqdftrmlqieeefvqricadiiavkpdLVFTEKGVSDLAQHYLLKAGITAIRRLRKTDNLRIARACGATIV 334
Cdd:cd00309 231 ------------------------------------VVIAEKGIDDEALHYLAKLGIMAVRRVRKEDLERIAKATGATIV 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 335 NRTEELTEKDVGTgAGLFEVKKIGDEYFTFVTECKEPKACTILLRGASKDILNETERNLQDALHVARNLVLEPRLVAGGG 414
Cdd:cd00309 275 SRLEDLTPEDLGT-AGLVEETKIGDEKYTFIEGCKGGKVATILLRGATEVELDEAERSLHDALCAVRAAVEDGGIVPGGG 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 415 AVEMAASQLLTR--KQVKG----PYTAVAHALEIIPRTLAQNCGANTIRALTALRAKHASHTGDgvcaWGIDGESGEIVD 488
Cdd:cd00309 354 AAEIELSKALEElaKTLPGkeqlGIEAFADALEVIPRTLAENAGLDPIEVVTKLRAKHAEGGGN----AGGDVETGEIVD 429
|
490 500 510
....*....|....*....|....*....|....*
gi 24647510 489 MNVKNIWEPLAVKLQTYKTAVETAILLLRIDDIVS 523
Cdd:cd00309 430 MKEAGIIDPLKVKRQALKSATEAASLILTIDDIIV 464
|
|
| Cpn60_TCP1 |
pfam00118 |
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ... |
34-523 |
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: 544.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 34 IADVIRTCLGPQAMLKMLMDPMGGIVMTNDGNAILREITVQHPAAKSMIEIARTQDEEVGDGTTSVIVLAGEMLAAAEPF 113
Cdd:pfam00118 1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELEIQHPAAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEEAEKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 114 LQQQIHPTVIIRAYREALEDIVGHLQSQLSIQLDVKDKAKMADVVKACVGTKFIGKWSDLAVKIALDAVETVtlsENGRL 193
Cdd:pfam00118 81 LAAGVHPTTIIEGYEKALEKALEILDSIISIPVEDVDREDLLKVARTSLSSKIISRESDFLAKLVVDAVLAI---PKNDG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 194 EVDIKRyAKVEKIPGGAIEESCVLKGVMINKDVTHPKMRRLIENPRIVLLDCSLEYKKGESQTNVEIIGEQDFTRMLQIE 273
Cdd:pfam00118 158 SFDLGN-IGVVKILGGSLEDSELVDGVVLDKGPLHPDMPKRLENAKVLLLNCSLEYEKTETKATVVLSDAEQLERFLKAE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 274 EEFVQRICADIIAVKPDLVFTEKGVSDLAQHYLLKAGITAIRRLRKTDNLRIARACGATIVNRTEELTEKDVGTgAGLFE 353
Cdd:pfam00118 237 EEQILEIVEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMALRRVKKRDLERLAKATGARAVSSLDDLTPDDLGT-AGKVE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 354 VKKIGDEYFTFVTECKEPKACTILLRGASKDILNETERNLQDALHVARNLVLEPRLVAGGGAVEMAASQLLTR--KQVKG 431
Cdd:pfam00118 316 EEKIGDEKYTFIEGCKSPKAATILLRGATDHVLDEIERSIHDALCVVKNAIEDPRVVPGGGAVEMELARALREyaKSVSG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 432 P----YTAVAHALEIIPRTLAQNCGANTIRALTALRAKHAShtgdGVCAWGIDGESGEIVDMNVKNIWEPLAVKLQTYKT 507
Cdd:pfam00118 396 KeqlaIEAFAEALEVIPKTLAENAGLDPIEVLAELRAAHAS----GEKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKS 471
|
490
....*....|....*.
gi 24647510 508 AVETAILLLRIDDIVS 523
Cdd:pfam00118 472 ATEAASTILRIDDIIK 487
|
|
| thermosome_alpha |
NF041082 |
thermosome subunit alpha; |
6-525 |
1.72e-174 |
|
thermosome subunit alpha;
Pssm-ID: 469009 Cd Length: 518 Bit Score: 502.49 E-value: 1.72e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 6 QPILVLSQNTKRESGRKVQLENIQAGKAIADVIRTCLGPQAMLKMLMDPMGGIVMTNDGNAILREITVQHPAAKSMIEIA 85
Cdd:NF041082 1 QPILILKEGTQRTSGRDAQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDVVITNDGVTILKEMDIEHPAAKMIVEVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 86 RTQDEEVGDGTTSVIVLAGEMLAAAEPFLQQQIHPTVIIRAYREALEDIVGHLQSqLSIQLDVKDKAKMADVVKACVGTK 165
Cdd:NF041082 81 KTQDDEVGDGTTTAVVLAGELLKKAEELLDQDIHPTIIAEGYRLAAEKALEILDE-IAIKVDPDDKETLKKIAATAMTGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 166 FIGKWSDLAVKIALDAVETVTlSENGRLEVDIKrYAKVEKIPGGAIEESCVLKGVMINKDVTHPKMRRLIENPRIVLLDC 245
Cdd:NF041082 160 GAEAAKDKLADLVVDAVKAVA-EKDGGYNVDLD-NIKVEKKVGGSIEDSELVEGVVIDKERVHPGMPKRVENAKIALLDA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 246 SLEYKKGESQTNVEIIGEQDFTRMLQIEEEFVQRICADIIAVKPDLVFTEKGVSDLAQHYLLKAGITAIRRLRKTDNLRI 325
Cdd:NF041082 238 PLEVKKTEIDAKISITDPDQLQAFLDQEEKMLKEMVDKIADSGANVVFCQKGIDDLAQHYLAKEGILAVRRVKKSDMEKL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 326 ARACGATIVNRTEELTEKDVGTgAGLFEVKKIGDEYFTFVTECKEPKACTILLRGASKDILNETERNLQDALHVARNLVL 405
Cdd:NF041082 318 AKATGARIVTSIDDLSPEDLGY-AGLVEERKVGGDKMIFVEGCKNPKAVTILLRGGTEHVVDEVERALEDALRVVRVVLE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 406 EPRLVAGGGAVEMA--------ASQLLTRKQVKgpYTAVAHALEIIPRTLAQNCGANTIRALTALRAKHAshtgDGVCAW 477
Cdd:NF041082 397 DGKVVAGGGAPEVElalrlreyAASVGGREQLA--IEAFAEALEIIPRTLAENAGLDPIDALVELRSAHE----KGNKTA 470
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 24647510 478 GIDGESGEIVDMNVKNIWEPLAVKLQTYKTAVETAILLLRIDDIVSGS 525
Cdd:NF041082 471 GLDVYTGKVVDMLEIGVVEPLRVKTQAIKSATEAAVMILRIDDVIAAA 518
|
|
| cpn60 |
cd03343 |
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ... |
8-523 |
6.39e-173 |
|
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: 498.71 E-value: 6.39e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 8 ILVLSQNTKRESGRKVQLENIQAGKAIADVIRTCLGPQAMLKMLMDPMGGIVMTNDGNAILREITVQHPAAKSMIEIART 87
Cdd:cd03343 1 VLILKEGTQRTSGRDAQRMNIAAAKAVAEAVRTTLGPKGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 88 QDEEVGDGTTSVIVLAGEMLAAAEPFLQQQIHPTVIIRAYREALEDIVGHLQSqLSIQLDVKDKAKMADVVKACVGTKFI 167
Cdd:cd03343 81 QDEEVGDGTTTAVVLAGELLEKAEDLLDQNIHPTVIIEGYRLAAEKALELLDE-IAIKVDPDDKDTLRKIAKTSLTGKGA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 168 GKWSDLAVKIALDAVETVTLSENGRLEVDIKrYAKVEKIPGGAIEESCVLKGVMINKDVTHPKMRRLIENPRIVLLDCSL 247
Cdd:cd03343 160 EAAKDKLADLVVDAVLQVAEKRDGKYVVDLD-NIKIEKKTGGSVDDTELIRGIVIDKEVVHPGMPKRVENAKIALLDAPL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 248 EYKKGESQTNVEIIGEQDFTRMLQIEEEFVQRICADIIAVKPDLVFTEKGVSDLAQHYLLKAGITAIRRLRKTDNLRIAR 327
Cdd:cd03343 239 EVKKTEIDAKIRITSPDQLQAFLEQEEAMLKEMVDKIADTGANVVFCQKGIDDLAQHYLAKAGILAVRRVKKSDMEKLAR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 328 ACGATIVNRTEELTEKDVGTgAGLFEVKKIGDEYFTFVTECKEPKACTILLRGASKDILNETERNLQDALHVARNLVLEP 407
Cdd:cd03343 319 ATGAKIVTNIDDLTPEDLGE-AELVEERKVGDDKMVFVEGCKNPKAVTILLRGGTEHVVDELERALEDALRVVADALEDG 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 408 RLVAGGGAVEMA--------ASQLLTRKQVKgpYTAVAHALEIIPRTLAQNCGANTIRALTALRAKHAshtgDGVCAWGI 479
Cdd:cd03343 398 KVVAGGGAVEIElakrlreyARSVGGREQLA--VEAFADALEEIPRTLAENAGLDPIDTLVELRAAHE----KGNKNAGL 471
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 24647510 480 DGESGEIVDMNVKNIWEPLAVKLQTYKTAVETAILLLRIDDIVS 523
Cdd:cd03343 472 DVYTGEVVDMLEKGVIEPLRVKKQAIKSATEAATMILRIDDVIA 515
|
|
| thermosome_beta |
NF041083 |
thermosome subunit beta; |
6-525 |
1.25e-172 |
|
thermosome subunit beta;
Pssm-ID: 469010 Cd Length: 519 Bit Score: 497.94 E-value: 1.25e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 6 QPILVLSQNTKRESGRKVQLENIQAGKAIADVIRTCLGPQAMLKMLMDPMGGIVMTNDGNAILREITVQHPAAKSMIEIA 85
Cdd:NF041083 1 QPVLILKEGTQRTKGRDAQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDIVITNDGATILKEMDVQHPAAKMLVEVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 86 RTQDEEVGDGTTSVIVLAGEMLAAAEPFLQQQIHPTVIIRAYREALEDIVGHLQSqLSIQLDVKDKAKMADVVKACVGTK 165
Cdd:NF041083 81 KTQDDEVGDGTTTAVVLAGELLKKAEELLDQNIHPTIIANGYRLAAEKAIEILDE-IAEKVDPDDRETLKKIAETSLTSK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 166 FIGKWSDLAVKIALDAVETVTLSENGRLEVDIKrYAKVEKIPGGAIEESCVLKGVMINKDVTHPKMRRLIENPRIVLLDC 245
Cdd:NF041083 160 GVEEARDYLAEIAVKAVKQVAEKRDGKYYVDLD-NIQIEKKHGGSIEDTQLIYGIVIDKEVVHPGMPKRVENAKIALLDA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 246 SLEYKKGESQTNVEIIGEQDFTRMLQIEEEFVQRICADIIAVKPDLVFTEKGVSDLAQHYLLKAGITAIRRLRKTDNLRI 325
Cdd:NF041083 239 PLEVKKTEIDAEIRITDPDQLQKFLDQEEKMLKEMVDKIKATGANVVFCQKGIDDLAQHYLAKAGILAVRRVKKSDMEKL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 326 ARACGATIVNRTEELTEKDVGTgAGLFEVKKIGDEYFTFVTECKEPKACTILLRGASKDILNETERNLQDALHVARNLVL 405
Cdd:NF041083 319 AKATGARIVTNIDDLTPEDLGY-AELVEERKVGDDKMVFVEGCKNPKAVTILIRGGTEHVVDEAERALEDALSVVADAVE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 406 EPRLVAGGGAVEMA--------ASQLLTRKQVKgpYTAVAHALEIIPRTLAQNCGANTIRALTALRAKHAshtgDGVCAW 477
Cdd:NF041083 398 DGKIVAGGGAPEVElakrlreyAATVGGREQLA--VEAFAEALEIIPRTLAENAGLDPIDILVKLRSAHE----KGKKWA 471
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 24647510 478 GIDGESGEIVDMNVKNIWEPLAVKLQTYKTAVETAILLLRIDDIVSGS 525
Cdd:NF041083 472 GINVFTGEVVDMWELGVIEPLRVKTQAIKSATEAATMILRIDDVIAAK 519
|
|
| thermosome_arch |
TIGR02339 |
thermosome, various subunits, archaeal; Thermosome is the name given to the archaeal rather ... |
7-523 |
3.50e-164 |
|
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: 476.48 E-value: 3.50e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 7 PILVLSQNTKRESGRKVQLENIQAGKAIADVIRTCLGPQAMLKMLMDPMGGIVMTNDGNAILREITVQHPAAKSMIEIAR 86
Cdd:TIGR02339 1 PVFILKEGTQRTSGRDAQRNNIAAAKAVAEAVKSTLGPRGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 87 TQDEEVGDGTTSVIVLAGEMLAAAEPFLQQQIHPTVIIRAYREALEDIVGHLQsQLSIQLDVKDKAKMADVVKACVGTKF 166
Cdd:TIGR02339 81 TQDEEVGDGTTTAVVLAGELLEKAEDLLEQDIHPTVIIEGYRKAAEKALEIID-EIATKISPEDRDLLKKIAYTSLTSKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 167 IG-KWSDLAVKIALDAVETVT-LSENGRLEVDIKrYAKVEKIPGGAIEESCVLKGVMINKDVTHPKMRRLIENPRIVLLD 244
Cdd:TIGR02339 160 SAeVAKDKLADLVVEAVKQVAeLRGDGKYYVDLD-NIKIVKKKGGSIEDTELVEGIVVDKEVVHPGMPKRVENAKIALLD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 245 CSLEYKKGESQTNVEIIGEQDFTRMLQIEEEFVQRICADIIAVKPDLVFTEKGVSDLAQHYLLKAGITAIRRLRKTDNLR 324
Cdd:TIGR02339 239 APLEVEKTEIDAKIRITDPDQIKKFLDQEEAMLKEMVDKIASAGANVVICQKGIDDVAQHYLAKAGILAVRRVKKSDIEK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 325 IARACGATIVNRTEELTEKDVGTgAGLFEVKKIGDEYFTFVTECKEPKACTILLRGASKDILNETERNLQDALHVARNLV 404
Cdd:TIGR02339 319 LARATGARIVSSIDEITESDLGY-AELVEERKVGEDKMVFVEGCKNPKAVTILLRGGTEHVVDELERSIQDALHVVANAL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 405 LEPRLVAGGGAVEMA--------ASQLLTRKQVKgpYTAVAHALEIIPRTLAQNCGANTIRALTALRAKHAshtgDGVCA 476
Cdd:TIGR02339 398 EDGKIVAGGGAVEIElalrlrsyARSVGGREQLA--IEAFADALEEIPRILAENAGLDPIDALVDLRAKHE----KGNKN 471
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 24647510 477 WGIDGESGEIVDMNVKNIWEPLAVKLQTYKTAVETAILLLRIDDIVS 523
Cdd:TIGR02339 472 AGINVFTGEIEDMLELGVIEPLRVKEQAIKSATEAATMILRIDDVIA 518
|
|
| TCP1_eta |
cd03340 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ... |
7-522 |
3.28e-117 |
|
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: 356.21 E-value: 3.28e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 7 PILVLSQNTKRESGRKVQLENIQAGKAIADVIRTCLGPQAMLKMLMDPMGGIVMTNDGNAILREITVQHPAAKSMIEIAR 86
Cdd:cd03340 1 PIILLKEGTDTSQGKGQLISNINACQAIADAVRTTLGPRGMDKLIVDGRGKVTISNDGATILKLLDIVHPAAKTLVDIAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 87 TQDEEVGDGTTSVIVLAGEMLAAAEPFLQQQIHPTVIIRAYREALEDIVGHLQsQLSIQLDVKDKAKMADVVKACVGT-- 164
Cdd:cd03340 81 SQDAEVGDGTTSVVVLAGEFLKEAKPFIEDGVHPQIIIRGYRKALQLAIEKIK-EIAVNIDKEDKEEQRELLEKCAATal 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 165 --KFIGKWSDLAVKIALDAVEtvTLSENGRLE-VDIKryakveKIPGGAIEESCVLKGVMINKDVTH------PKmrrLI 235
Cdd:cd03340 160 nsKLIASEKEFFAKMVVDAVL--SLDDDLDLDmIGIK------KVPGGSLEDSQLVNGVAFKKTFSYagfeqqPK---KF 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 236 ENPRIVLLDCSLEYKKGESQTNVEIIGEQDFTRMLQIEEEFVQRICADIIAVKPDLVFTEKGVSDLAQHYLLKAGITAIR 315
Cdd:cd03340 229 KNPKILLLNVELELKAEKDNAEVRVEDPEEYQAIVDAEWKIIYDKLEKIVKSGANVVLSKLPIGDLATQYFADRDIFCAG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 316 RLRKTDNLRIARACGATIVNRTEELTEKDVGTgAGLFEVKKIGDEYFTFVTECKEPKACTILLRGASKDILNETERNLQD 395
Cdd:cd03340 309 RVPEEDLKRVAQATGGSIQTTVSNITDDVLGT-CGLFEERQVGGERYNIFTGCPKAKTCTIILRGGAEQFIEEAERSLHD 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 396 ALHVARNLVLEPRLVAGGGAVEMAASQLLTRKQVKGP------YTAVAHALEIIPRTLAQNCGANTIRALTALRAKHASh 469
Cdd:cd03340 388 AIMIVRRAIKNDSVVAGGGAIEMELSKYLRDYSRTIAgkqqlvINAFAKALEIIPRQLCDNAGFDATDILNKLRQKHAQ- 466
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 24647510 470 tgdGVCAW-GIDGESGEIVDMNVKNIWEPLAVKLQTYKTAVETAILLLRIDDIV 522
Cdd:cd03340 467 ---GGGKWyGVDINNEGIADNFEAFVWEPSLVKINALTAATEAACLILSVDETI 517
|
|
| TCP1_delta |
cd03338 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ... |
15-522 |
1.50e-111 |
|
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: 341.57 E-value: 1.50e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 15 TKRESGRKVQLENIQAGKAIADVIRTCLGPQAMLKMLMDPMGGIVMTNDGNAILREITVQHPAAKSMIEIARTQDEEVGD 94
Cdd:cd03338 1 TDKEKPADVRLSNIQAAKAVADAIRTSLGPRGMDKMIQTGKGEVIITNDGATILKQMSVLHPAAKMLVELSKAQDIEAGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 95 GTTSVIVLAGEMLAAAEPFLQQQIHPTVIIRAYREALEDIVGHLQSqLSIQLDVKDKAKMADVVKACVGTKFIGKWSDLA 174
Cdd:cd03338 81 GTTSVVVLAGALLSACESLLKKGIHPTVISESFQIAAKKAVEILDS-MSIPVDLNDRESLIKSATTSLNSKVVSQYSSLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 175 VKIALDAVETVTLSENGRlEVDIKRYAKVEKIpGGAIEESCVLKGVMINKDVTH-PKMRRLIENPRIVLLDCSLEYKKGE 253
Cdd:cd03338 160 APIAVDAVLKVIDPATAT-NVDLKDIRIVKKL-GGTIEDTELVDGLVFTQKASKkAGGPTRIEKAKIGLIQFCLSPPKTD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 254 SQTNVEIIGEQDFTRMLQIEEEFVQRICADIIAVKPDLVFTEK-----GVSDLAQHYLLKAGITAIRRLRKTDNLRIARA 328
Cdd:cd03338 238 MDNNIVVNDYAQMDRILREERKYILNMCKKIKKSGCNVLLIQKsilrdAVSDLALHFLAKLKIMVVKDIEREEIEFICKT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 329 CGATIVNRTEELTEKDVGTgAGLFEVKKIGDEYFTFVTECKEP-KACTILLRGASKDILNETERNLQDALHVARNLVLEP 407
Cdd:cd03338 318 IGCKPVASIDHFTEDKLGS-ADLVEEVSLGDGKIVKITGVKNPgKTVTILVRGSNKLVLDEAERSLHDALCVIRCLVKKR 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 408 RLVAGGGAVEMAASQLLTR--KQVKGPYT----AVAHALEIIPRTLAQNCGANTIRALTALRAKHAShtgdGVCAWGIDG 481
Cdd:cd03338 397 ALIPGGGAPEIEIALQLSEwaRTLTGVEQycvrAFADALEVIPYTLAENAGLNPISIVTELRNRHAQ----GEKNAGINV 472
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 24647510 482 ESGEIVDMNVKNIWEPLAVKLQTYKTAVETAILLLRIDDIV 522
Cdd:cd03338 473 RKGAITNILEENVVQPLLVSTSAITLATETVRMILKIDDIV 513
|
|
| TCP1_epsilon |
cd03339 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ... |
6-523 |
8.69e-111 |
|
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: 340.05 E-value: 8.69e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 6 QPILVL--SQNTKRESGRKVQLENIQAGKAIADVIRTCLGPQAMLKMLMDPMGGIVMTNDGNAILREITVQHPAAKSMIE 83
Cdd:cd03339 5 RPFIIVreQEKKKRLKGLEAHKSHILAAKSVANILRTSLGPRGMDKILVSPDGEVTVTNDGATILEKMDVDHQIAKLLVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 84 IARTQDEEVGDGTTSVIVLAGEMLAAAEPFLQQQIHPTVIIRAYREALEDIVGHLQS-QLSIQLDVKDKAKMADVVKACV 162
Cdd:cd03339 85 LSKSQDDEIGDGTTGVVVLAGALLEQAEKLLDRGIHPIRIADGYEQACKIAVEHLEEiADKIEFSPDNKEPLIQTAMTSL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 163 GTKFIGKWSDLAVKIALDAVETVTLSEngRLEVDIKrYAKVEKIPGGAIEESCVLKGVMINKDVTHPKMRRLIENPRIVL 242
Cdd:cd03339 165 GSKIVSRCHRQFAEIAVDAVLSVADLE--RKDVNFE-LIKVEGKVGGRLEDTKLVKGIVIDKDFSHPQMPKEVKDAKIAI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 243 LDCSLEYKKGESQTNVEIIGEQDFTRMLQIEEEFVQRICADIIAVKPDLVFTEKGVSDLAQHYLLKAGITAIRRLRKTDN 322
Cdd:cd03339 242 LTCPFEPPKPKTKHKLDITSVEDYKKLQEYEQKYFREMVEQVKDAGANLVICQWGFDDEANHLLLQNGLPAVRWVGGVEI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 323 LRIARACGATIVNRTEELTEKDVGTgAGLfeVKKIG----DEYFTFVTECKEPKACTILLRGASKDILNETERNLQDALH 398
Cdd:cd03339 322 ELIAIATGGRIVPRFEDLSPEKLGK-AGL--VREISfgttKDKMLVIEGCPNSKAVTIFIRGGNKMIIEEAKRSLHDALC 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 399 VARNLVLEPRLVAGGGAVEMAASQLLTRKQVKGP------YTAVAHALEIIPRTLAQNCGANTIRALTALRAKHAShtgD 472
Cdd:cd03339 399 VVRNLIRDNRIVYGGGAAEISCSLAVEKAADKCSgieqyaMRAFADALESIPLALAENSGLNPIETLSEVKARQVK---E 475
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 24647510 473 GVCAWGIDGESGEIVDMNVKNIWEPLAVKLQTYKTAVETAILLLRIDDIVS 523
Cdd:cd03339 476 KNPHLGIDCLGRGTNDMKEQKVFETLISKKQQILLATQVVKMILKIDDVIV 526
|
|
| chap_CCT_eta |
TIGR02345 |
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ... |
5-522 |
6.28e-110 |
|
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: 337.50 E-value: 6.28e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 5 QQPILVLSQNTKRESGRKVQLENIQAGKAIADVIRTCLGPQAMLKMLMDPMGGIVMTNDGNAILREITVQHPAAKSMIEI 84
Cdd:TIGR02345 1 RPTIVLLKEGTDTSQGKGQLISNINACVAIAEALKTTLGPRGMDKLIVGSNGKATISNDGATILKLLDIVHPAAKTLVDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 85 ARTQDEEVGDGTTSVIVLAGEMLAAAEPFLQQQIHPTVIIRAYREALEDIVGHLQsQLSIQLDvKDKAKMADVVKACVGT 164
Cdd:TIGR02345 81 AKSQDAEVGDGTTSVTILAGELLKEAKPFIEEGVHPQLIIRCYREALSLAVEKIK-EIAVTID-EEKGEQRELLEKCAAT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 165 ----KFIGKWSDLAVKIALDAVETVTLSENGRLEVDIKryakveKIPGGAIEESCVLKGVMINKDVT---HPKMRRLIEN 237
Cdd:TIGR02345 159 alssKLISHNKEFFSKMIVDAVLSLDRDDLDLKLIGIK------KVQGGALEDSQLVNGVAFKKTFSyagFEQQPKKFAN 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 238 PRIVLLDCSLEYKKGESQTNVEIIGEQDFTRMLQIEEEFVQRICADIIAVKPDLVFTEKGVSDLAQHYLLKAGITAIRRL 317
Cdd:TIGR02345 233 PKILLLNVELELKAEKDNAEIRVEDVEDYQAIVDAEWAIIFRKLEKIVESGANVVLSKLPIGDLATQYFADRDIFCAGRV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 318 RKTDNLRIARACGATIVNRTEELTEKDVGTgAGLFEVKKIGDEYFTFVTECKEPKACTILLRGASKDILNETERNLQDAL 397
Cdd:TIGR02345 313 SAEDLKRVIKACGGSIQSTTSDLEADVLGT-CALFEERQIGSERYNYFTGCPHAKTCTIILRGGAEQFIEEAERSLHDAI 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 398 HVARNLVLEPRLVAGGGAVEMAASQLLTRKQVKGP------YTAVAHALEIIPRTLAQNCGANTIRALTALRAKHAShtg 471
Cdd:TIGR02345 392 MIVRRALKNKKIVAGGGAIEMELSKCLRDYSKTIDgkqqliINAFAKALEIIPRQLCENAGFDSIEILNKLRSRHAK--- 468
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 24647510 472 DGVCAwGIDGESGEIVDMNVKNIWEPLAVKLQTYKTAVETAILLLRIDDIV 522
Cdd:TIGR02345 469 GGKWY-GVDINTEDIGDNFEAFVWEPALVKINALKAAFEAACTILSVDETI 518
|
|
| TCP1_alpha |
cd03335 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ... |
16-522 |
2.50e-109 |
|
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: 336.18 E-value: 2.50e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 16 KRESGRKVQLENIQAGKAIADVIRTCLGPQAMLKMLMDPMGGIVMTNDGNAILREITVQHPAAKSMIEIARTQDEEVGDG 95
Cdd:cd03335 2 ERTSGQDVRTQNVTAAMAIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDKEVGDG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 96 TTSVIVLAGEMLAAAEPFLQQQIHPTVIIRAYREALEDIVGHLQSQLSIQLDVKDKAKMADVVKACVGTKFIGKWSDLAV 175
Cdd:cd03335 82 TTSVVIIAAELLKRANELVKQKIHPTTIISGYRLACKEAVKYIKEHLSISVDNLGKESLINVAKTSMSSKIIGADSDFFA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 176 KIALDAVETV-TLSENGRLEVDIKRyAKVEKIPGGAIEESCVLKGVMINKDVTHPKMRRLIENPRIVLLDCSLEYKKGES 254
Cdd:cd03335 162 NMVVDAILAVkTTNEKGKTKYPIKA-VNILKAHGKSAKESYLVNGYALNCTRASQGMPTRVKNAKIACLDFNLQKTKMKL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 255 QTNVEIIGEQDFTRMLQIEEEFVQRICADIIAVKPDLVFTEKGVSDLAQHYLLKAGITAIRRLRKTDNLRIARACGATIV 334
Cdd:cd03335 241 GVQVVVTDPEKLEKIRQRESDITKERIKKILAAGANVVLTTGGIDDMCLKYFVEAGAMAVRRVKKEDLRRIAKATGATLV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 335 N-----RTEELTEKDVGTGAGLFEVKKIGDEYFTFVTECKEPKACTILLRGASKDILNETERNLQDALHVARNLVLEPRL 409
Cdd:cd03335 321 StlanlEGEETFDPSYLGEAEEVVQERIGDDELILIKGTKKRSSASIILRGANDFMLDEMERSLHDALCVVKRTLESNSV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 410 VAGGGAVEMAASQLL--------TRKQVKgpYTAVAHALEIIPRTLAQNCGANTIRALTALRAKHASH----TGDGVCAW 477
Cdd:cd03335 401 VPGGGAVETALSIYLenfattlgSREQLA--IAEFAEALLVIPKTLAVNAAKDATELVAKLRAYHAAAqvkpDKKHLKWY 478
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 24647510 478 GIDGESGEIVDmNVKN-IWEPLAVKLQTYKTAVETAILLLRIDDIV 522
Cdd:cd03335 479 GLDLINGKVRD-NLEAgVLEPTVSKIKSLKFATEAAITILRIDDLI 523
|
|
| chap_CCT_epsi |
TIGR02343 |
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ... |
4-523 |
3.09e-108 |
|
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: 333.69 E-value: 3.09e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 4 GQQPILVLSQNTK-RESGRKVQLENIQAGKAIADVIRTCLGPQAMLKMLMDPMGGIVMTNDGNAILREITVQHPAAKSMI 82
Cdd:TIGR02343 8 GRPFIIIKDQDNKkRLKGLEAKKSNIAAAKSVASILRTSLGPKGMDKMLISPDGDITVTNDGATILSQMDVDNQIAKLMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 83 EIARTQDEEVGDGTTSVIVLAGEMLAAAEPFLQQQIHPTVIIRAYREALEDIVGHLQS-QLSIQLDVKDKAKMADVVKAC 161
Cdd:TIGR02343 88 ELSKSQDDEIGDGTTGVVVLAGALLEQAEELLDKGIHPIKIADGFEEAARIAVEHLEEiSDEISADNNNREPLIQAAKTS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 162 VGTKFIGKWSDLAVKIALDAVETVTLSENGRLEVDIkryAKVEKIPGGAIEESCVLKGVMINKDVTHPKMRRLIENPRIV 241
Cdd:TIGR02343 168 LGSKIVSKCHRRFAEIAVDAVLNVADMERRDVDFDL---IKVEGKVGGSLEDTKLIKGIIIDKDFSHPQMPKEVEDAKIA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 242 LLDCSLEYKKGESQTNVEIIGEQDFTRMLQIEEEFVQRICADIIAVKPDLVFTEKGVSDLAQHYLLKAGITAIRRLRKTD 321
Cdd:TIGR02343 245 ILTCPFEPPKPKTKHKLDISSVEEYKKLQKYEQQKFKEMIDDIKKSGANLVICQWGFDDEANHLLLQNDLPAVRWVGGQE 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 322 NLRIARACGATIVNRTEELTEKDVGTgAGLFEVKKIG--DEYFTFVTECKEPKACTILLRGASKDILNETERNLQDALHV 399
Cdd:TIGR02343 325 LELIAIATGGRIVPRFQELSKDKLGK-AGLVREISFGttKDRMLVIEQCKNSKAVTIFIRGGNKMIIEEAKRSIHDALCV 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 400 ARNLVLEPRLVAGGGAVEMAASQLLTRKQVKGP------YTAVAHALEIIPRTLAQNCGANTIRALTALRAKHASHTgdg 473
Cdd:TIGR02343 404 VRNLIKDSRIVYGGGAAEISCSLAVSQEADKYPgveqyaIRAFADALETIPMALAENSGLDPIGTLSTLKSLQLKEK--- 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 24647510 474 VCAWGIDGESGEIVDMNVKNIWEPLAVKLQTYKTAVETAILLLRIDDIVS 523
Cdd:TIGR02343 481 NPNLGVDCLGYGTNDMKEQFVFETLIGKKQQILLATQLVRMILKIDDVIS 530
|
|
| chap_CCT_alpha |
TIGR02340 |
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ... |
16-522 |
8.13e-105 |
|
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: 324.75 E-value: 8.13e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 16 KRESGRKVQLENIQAGKAIADVIRTCLGPQAMLKMLMDPMGGIVMTNDGNAILREITVQHPAAKSMIEIARTQDEEVGDG 95
Cdd:TIGR02340 6 ERTSGQDVRTQNVTAAMAIANIVKTSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDREVGDG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 96 TTSVIVLAGEMLAAAEPFLQQQIHPTVIIRAYREALEDIVGHLQSQLSIQLDVKDKAKMADVVKACVGTKFIGKWSDLAV 175
Cdd:TIGR02340 86 TTSVVIIAAELLKRADELVKNKIHPTSVISGYRLACKEAVKYIKENLSVSVDELGREALINVAKTSMSSKIIGLDSDFFS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 176 KIALDAVETV-TLSENGRLEVDIKRyAKVEKIPGGAIEESCVLKGVMINKDVTHPKMRRLIENPRIVLLDCSLEYKKGES 254
Cdd:TIGR02340 166 NIVVDAVLAVkTTNENGETKYPIKA-INILKAHGKSARESMLVKGYALNCTVASQQMPKRIKNAKIACLDFNLQKAKMAL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 255 QTNVEIIGEQDFTRMLQIEEEFVQRICADIIAVKPDLVFTEKGVSDLAQHYLLKAGITAIRRLRKTDNLRIARACGATIV 334
Cdd:TIGR02340 245 GVQIVVDDPEKLEQIRQREADITKERIKKILDAGANVVLTTGGIDDMCLKYFVEAGAMGVRRCKKEDLKRIAKATGATLV 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 335 NRTEELTEKDVGTGAGL-----FEVKKIGDEYFTFVTECKEPKACTILLRGASKDILNETERNLQDALHVARNLVLEPRL 409
Cdd:TIGR02340 325 STLADLEGEETFEASYLgfadeVVQERIADDECILIKGTKKRKSASIILRGANDFMLDEMERSLHDALCVVKRTLESNSV 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 410 VAGGGAVEMAASQLL--------TRKQVKgpYTAVAHALEIIPRTLAQNCGANTIRALTALRAKHASH----TGDGVCAW 477
Cdd:TIGR02340 405 VPGGGAVEAALSIYLenfattlgSREQLA--IAEFARALLIIPKTLAVNAAKDSTELVAKLRAYHAAAqlkpEKKHLKWY 482
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 24647510 478 GIDGESGEIVDMNVKNIWEPLAVKLQTYKTAVETAILLLRIDDIV 522
Cdd:TIGR02340 483 GLDLVNGKIRDNKEAGVLEPTVSKVKSLKFATEAAITILRIDDLI 527
|
|
| GroEL |
COG0459 |
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ... |
20-522 |
8.40e-97 |
|
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227 Cd Length: 497 Bit Score: 302.77 E-value: 8.40e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 20 GRKVQLENIQAGKAIADVIRTCLGPQAMLKMLMDPMGGIVMTNDGNAILREITVQHP----AAKSMIEIARTQDEEVGDG 95
Cdd:COG0459 8 GEDARRANIRGVKALADAVKVTLGPKGRNVMLVKSFGDPTITNDGVTIAKEIELEDPfenmGAQLVKEVASKTNDEAGDG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 96 TTSVIVLAGEMLAAAEPFLQQQIHPTVIIRAYREALEDIVGHLQSQlSIqlDVKDKAKMADVVK-ACVGTKFIGkwsdla 174
Cdd:COG0459 88 TTTATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKI-AK--PVDDKEELAQVATiSANGDEEIG------ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 175 vKIALDAVETVTlsENGRLevdikryaKVEKiPGGAIEESCVLKGVMINKDVTHP-------KMRRLIENPRIVLLDCSL 247
Cdd:COG0459 159 -ELIAEAMEKVG--KDGVI--------TVEE-GKGLETELEVVEGMQFDKGYLSPyfvtdpeKMPAELENAYILLTDKKI 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 248 EykkgesqtnveiiGEQDFTRMLQIeeefvqricadIIAVKPDLVFTEKGVSDLAQHYLLKAGITAIRRL---------- 317
Cdd:COG0459 227 S-------------SIQDLLPLLEK-----------VAQSGKPLLIIAEDIDGEALATLVVNGIRGVLRVvavkapgfgd 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 318 -RKTDNLRIARACGATIVNR-----TEELTEKDVGTgAGLFEVkkiGDEYFTFVTECKEPKACTILLRGASKDILNETER 391
Cdd:COG0459 283 rRKAMLEDIAILTGGRVISEdlglkLEDVTLDDLGR-AKRVEV---DKDNTTIVEGAGNPKAIVILVGAATEVEVKERKR 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 392 NLQDALHVARNlVLEPRLVAGGGAVEMAASQLLTRKQVKGP------YTAVAHALEIIPRTLAQNCGANTIRALTALRAK 465
Cdd:COG0459 359 RVEDALHATRA-AVEEGIVPGGGAALLRAARALRELAAKLEgdeqlgIEIVARALEAPLRQIAENAGLDGSVVVEKVRAA 437
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 24647510 466 hashtgdGVCAWGIDGESGEIVDMNVKNIWEPLAVKLQTYKTAVETAILLLRIDDIV 522
Cdd:COG0459 438 -------KDKGFGFDAATGEYVDMLEAGVIDPAKVKRSALQNAASVAGLILTTEAVI 487
|
|
| chap_CCT_delta |
TIGR02342 |
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ... |
17-522 |
9.27e-95 |
|
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: 298.24 E-value: 9.27e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 17 RESGRKVQLENIQAGKAIADVIRTCLGPQAMLKMLMDPMGGIVMTNDGNAILREITVQHPAAKSMIEIARTQDEEVGDGT 96
Cdd:TIGR02342 4 KDKPQDVRTSNIVAAKAVADAIRTSLGPKGMDKMIQDGKGEVIITNDGATILKQMAVLHPAAKMLVELSKAQDIEAGDGT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 97 TSVIVLAGEMLAAAEPFLQQQIHPTVIIRAYREALEDIVGHLqSQLSIQLDVKDKAKMADVVKACVGTKFIGKWSDLAVK 176
Cdd:TIGR02342 84 TSVVILAGALLGACERLLNKGIHPTIISESFQSAADEAIKIL-DEMSIPVDLSDREQLLKSATTSLSSKVVSQYSSLLAP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 177 IALDAVETVTLSENGRlEVDIKRYAKVEKIpGGAIEESCVLKGVMINKDVTHPK-MRRLIENPRIVLLDCSLEYKKGESQ 255
Cdd:TIGR02342 163 LAVDAVLKVIDPENAK-NVDLNDIKVVKKL-GGTIDDTELIEGLVFTQKASKSAgGPTRIEKAKIGLIQFQISPPKTDME 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 256 TNVEIIGEQDFTRMLQIEEEFVQRICADIIAVKPDLVFTEK-----GVSDLAQHYLLKAGITAIRRLRKTDNLRIARACG 330
Cdd:TIGR02342 241 NQIIVNDYAQMDRVLKEERAYILNIVKKIKKTGCNVLLIQKsilrdAVNDLALHFLAKMKIMVVKDIEREEIEFICKTIG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 331 ATIVNRTEELTEKDVGTgAGLFEVKKIGDEYFTFVTECKEP-KACTILLRGASKDILNETERNLQDALHVARNLVLEPRL 409
Cdd:TIGR02342 321 CKPIASIDHFTADKLGS-AELVEEVDSDGGKIIKITGIQNAgKTVTVVVRGSNKLVIDEAERSLHDALCVIRCLVKKRGL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 410 VAGGGAVEMAASQLLTR--KQVKGP----YTAVAHALEIIPRTLAQNCGANTIRALTALRAKHAShtgdGVCAWGIDGES 483
Cdd:TIGR02342 400 IAGGGAPEIEIARRLSKyaRTMKGVesycVRAFADALEVIPYTLAENAGLNPIKVVTELRNRHAN----GEKTAGISVRK 475
|
490 500 510
....*....|....*....|....*....|....*....
gi 24647510 484 GEIVDMNVKNIWEPLAVKLQTYKTAVETAILLLRIDDIV 522
Cdd:TIGR02342 476 GGITNMLEEHVLQPLLVTTSAITLASETVRSILKIDDIV 514
|
|
| TCP1_theta |
cd03341 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ... |
25-522 |
5.37e-94 |
|
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: 294.90 E-value: 5.37e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 25 LENIQAGKAIADVIRTCLGPQAMLKMLMDPMGGIVMTNDGNAILREITVQHPAAKSMIEIARTQDEEVGDGTTSVIVLAG 104
Cdd:cd03341 11 LRNIEACKELSQITRTSYGPNGMNKMVINHLEKLFVTSDAATILRELEVQHPAAKLLVMASQMQEEEIGDGTNLVVVLAG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 105 EMLAAAEPFLQQQIHPTVIIRAYREALEDIVGHLQsQLSIQ--LDVKDKAKMADVVKACVGTKFIGKwSDLAVKIALDAV 182
Cdd:cd03341 91 ELLEKAEELLRMGLHPSEIIEGYEKALKKALEILE-ELVVYkiEDLRNKEEVSKALKTAIASKQYGN-EDFLSPLVAEAC 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 183 ETVTLSENGRLEVDIKRyakVEKIPGGAIEESCVLKGVMINKD----VTHpkmrrlIENPRIVLLDCSLEykkgesqtnv 258
Cdd:cd03341 169 ISVLPENIGNFNVDNIR---VVKILGGSLEDSKVVRGMVFKREpegsVKR------VKKAKVAVFSCPFD---------- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 259 eiigeqdftrmlqieeefvqricadiIAVKpdLVFTEKGVSDLAQHYLLKAGITAIRRLRKTDNLRIARACGATIVNRTE 338
Cdd:cd03341 230 --------------------------IGVN--VIVAGGSVGDLALHYCNKYGIMVIKINSKFELRRLCRTVGATPLPRLG 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 339 ELTEKDVGTgAGLFEVKKIGDEYFTFVTECKEP-KACTILLRGASKDILNETERNLQDALHVARNLVLEPRLVAGGGAVE 417
Cdd:cd03341 282 APTPEEIGY-CDSVYVEEIGDTKVVVFRQNKEDsKIATIVLRGATQNILDDVERAIDDGVNVFKSLTKDGRFVPGAGATE 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 418 MAASQLLTR--KQVKGPY----TAVAHALEIIPRTLAQNCGANTIRALTALRAKHAS-HTGDGVcawGIDGESGEIVDMN 490
Cdd:cd03341 361 IELAKKLKEygEKTPGLEqyaiKKFAEAFEVVPRTLAENAGLDATEVLSELYAAHQKgNKSAGV---DIESGDEGTKDAK 437
|
490 500 510
....*....|....*....|....*....|..
gi 24647510 491 VKNIWEPLAVKLQTYKTAVETAILLLRIDDIV 522
Cdd:cd03341 438 EAGIFDHLATKKWAIKLATEAAVTVLRVDQII 469
|
|
| TCP1_zeta |
cd03342 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
14-526 |
4.62e-86 |
|
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: 274.52 E-value: 4.62e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 14 NTKRESGRKVQ-LE-NIQAGKAIADVIRTCLGPQAMLKMLMDPMGGIVMTNDGNAILREITVQHPAAkSMIEIART-QDE 90
Cdd:cd03342 2 NPKAEVLRRGQaLAvNISAAKGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLSEMQIQHPTA-SMIARAATaQDD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 91 EVGDGTTSVIVLAGEMLAAAEPFLQQQIHPTVIIRAYREALEDIVGHLqSQLSIQLDVK-DKAKMADVVKACVGTKFIGK 169
Cdd:cd03342 81 ITGDGTTSNVLLIGELLKQAERYIQEGVHPRIITEGFELAKNKALKFL-ESFKVPVEIDtDRELLLSVARTSLRTKLHAD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 170 WSDLAVKIALDAVETVTLSENgrlEVDIKRyakVE--KIPGGAIEESCVLKGVMINKDVTHPKMRRLIENPRIVLLDCSL 247
Cdd:cd03342 160 LADQLTEIVVDAVLAIYKPDE---PIDLHM---VEimQMQHKSDSDTKLIRGLVLDHGARHPDMPKRVENAYILTCNVSL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 248 EYKKGEsqtnveiigeqdftrmlqIEEEFVQRIcadiiavkpdlVFTEKGVSDLAQHYLLKAGITAIRRLRKTDNLRIAR 327
Cdd:cd03342 234 EYEKTE------------------VNSGFFYSV-----------VINQKGIDPPSLDMLAKEGILALRRAKRRNMERLTL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 328 ACGATIVNRTEELTEKDVGTgAGLFEVKKIGDEYFTFVTECKEPKACTILLRGASKDILNETERNLQDALHVARNLVLEP 407
Cdd:cd03342 285 ACGGVAMNSVDDLSPECLGY-AGLVYERTLGEEKYTFIEGVKNPKSCTILIKGPNDHTITQIKDAIRDGLRAVKNAIEDK 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 408 RLVAGGGAVEMAASQLLTR--KQVKGP----YTAVAHALEIIPRTLAQNCGANTIRALTALRAKHASHTGDGvcawGIDG 481
Cdd:cd03342 364 CVVPGAGAFEVALYAHLKEfkKSVKGKaklgVQAFADALLVIPKTLAENSGLDVQETLVKLQDEYAEGGQVG----GVDL 439
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 24647510 482 ESGEIVDMNVKNIWEPLAVKLQTYKTAVETAILLLRIDDIVSGSK 526
Cdd:cd03342 440 DTGEPMDPESEGIWDNYSVKRQILHSATVIASQLLLVDEIIRAGR 484
|
|
| chap_CCT_zeta |
TIGR02347 |
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ... |
14-522 |
1.04e-85 |
|
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: 275.07 E-value: 1.04e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 14 NTKRESGRKVQ--LENIQAGKAIADVIRTCLGPQAMLKMLMDPMGGIVMTNDGNAILREITVQHPAAKSMIEIARTQDEE 91
Cdd:TIGR02347 6 NPKAESLRRDAalMMNINAARGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEMQIQHPTASMIARAATAQDDI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 92 VGDGTTSVIVLAGEMLAAAEPFLQQQIHPTVIIRAYREALEDIVGHLQSQLSIQLDVKDKAKMADVVKACVGTKFIGKWS 171
Cdd:TIGR02347 86 TGDGTTSTVLLIGELLKQAERYILEGVHPRIITEGFEIARKEALQFLDKFKVKKEDEVDREFLLNVARTSLRTKLPADLA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 172 DLAVKIALDAVETVTLSENgrlEVDIKRYAKVEKIPGGAIEESCVlKGVMINKDVTHPKMRRLIENPRIVLLDCSLEYKK 251
Cdd:TIGR02347 166 DQLTEIVVDAVLAIKKDGE---DIDLFMVEIMEMKHKSATDTTLI-RGLVLDHGARHPDMPRRVKNAYILTCNVSLEYEK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 252 GESQTNVEIIGEQDFTRMLQIEEEFVQRICADIIAVK-------PD---LVFTEKGVSDLAQHYLLKAGITAIRRLRKTD 321
Cdd:TIGR02347 242 TEVNSGFFYSSAEQREKLVKAERKFVDDRVKKIIELKkkvcgksPDkgfVVINQKGIDPPSLDLLAKEGIMALRRAKRRN 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 322 NLRIARACGATIVNRTEELTEKDVGTgAGLFEVKKIGDEYFTFVTECKEPKACTILLRGASKDILNETERNLQDALHVAR 401
Cdd:TIGR02347 322 MERLTLACGGEALNSVEDLTPECLGW-AGLVYETTIGEEKYTFIEECKNPKSCTILIKGPNDHTIAQIKDAVRDGLRAVK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 402 NLVLEPRLVAGGGAVEMAASQLLT--RKQVKGP----YTAVAHALEIIPRTLAQNCGANTIRALTALRAKHASHTGDGvc 475
Cdd:TIGR02347 401 NAIEDKCVVPGAGAFEIAAYRHLKeyKKSVKGKaklgVEAFANALLVIPKTLAENSGFDAQDTLVKLEDEHDEGGEVV-- 478
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 24647510 476 awGIDGESGEIVDMNVKNIWEPLAVKLQTYKTAVETAILLLRIDDIV 522
Cdd:TIGR02347 479 --GVDLNTGEPIDPEIKGIWDNYRVKKQLIQSATVIASQLLLVDEVM 523
|
|
| chap_CCT_theta |
TIGR02346 |
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ... |
25-533 |
1.11e-85 |
|
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: 275.06 E-value: 1.11e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 25 LENIQAGKAIADVIRTCLGPQAMLKMLMDPMGGIVMTNDGNAILREITVQHPAAKSMIEIARTQDEEVGDGTTSVIVLAG 104
Cdd:TIGR02346 21 IKNIEACKELSQITRTSLGPNGMNKMVINHLEKLFVTNDAATILRELEVQHPAAKLLVMASEMQENEIGDGTNLVLVLAG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 105 EMLAAAEPFLQQQIHPTVIIRAYREALEDIVGHLQSQLSIQL-DVKDKAKMADVVKACVGTKFIGKWSDLAVKIAlDAVE 183
Cdd:TIGR02346 101 ELLNKAEELIRMGLHPSEIIKGYEMALKKAMEILEELVVWEVkDLRDKDELIKALKASISSKQYGNEDFLAQLVA-QACS 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 184 TVTLSENGRLEVDIKRyakVEKIPGGAIEESCVLKGVMINKD-VTHPKMrrlIENPRIVLLDCSLEYKKGESQTNVEIIG 262
Cdd:TIGR02346 180 TVLPKNPQNFNVDNIR---VCKILGGSLSNSEVLKGMVFNREaEGSVKS---VKNAKVAVFSCPLDTATTETKGTVLIHN 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 263 EQDFTRMLQIEEEFVQRICADIIAVKPDLVFTEKGVSDLAQHYLLKAGITAIRRLRKTDNLRIARACGATIVNRTEELTE 342
Cdd:TIGR02346 254 AEELLNYSKGEENQIEAMIKAIADSGVNVIVTGGSVGDMALHYLNKYNIMVLKIPSKFELRRLCKTVGATPLPRLGAPTP 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 343 KDVGTGAGLfEVKKIGDEYFT-FVTECKEPKACTILLRGASKDILNETERNLQDALHVARNLVLEPRLVAGGGAVEMAAS 421
Cdd:TIGR02346 334 EEIGYVDSV-YVSEIGGDKVTvFKQENGDSKISTIILRGSTDNLLDDIERAIDDGVNTVKALVKDGRLLPGAGATEIELA 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 422 QLLTR--KQVKGPY----TAVAHALEIIPRTLAQNCGANTIRALTALRAKHAS-HTGDGVcawGIDGESGEIVDMNVKNI 494
Cdd:TIGR02346 413 SRLTKygEKLPGLDqyaiKKFAEAFEIIPRTLAENAGLNANEVIPKLYAAHKKgNKSKGI---DIEAESDGVKDASEAGI 489
|
490 500 510
....*....|....*....|....*....|....*....
gi 24647510 495 WEPLAVKLQTYKTAVETAILLLRIDDIVSgSKKRGGNEP 533
Cdd:TIGR02346 490 YDMLATKKWAIKLATEAAVTVLRVDQIIM-AKPAGGPKP 527
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
1-523 |
9.46e-85 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 272.67 E-value: 9.46e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 1 MFGGQQPILVLSQNTKRESGRKVQLENIQAGKAIADVIRTCLGPQAMLKML--MDP---MGGIVMTNDGNAILREITVQH 75
Cdd:PTZ00212 1 MIMANVPPQVLKQGAQEEKGETARLQSFVGAIAVADLVKTTLGPKGMDKILqpMSEgprSGNVTVTNDGATILKSVWLDN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 76 PAAKSMIEIARTQDEEVGDGTTSVIVLAGEMLAAAEPFLQQQIHPTVIIRAYREALEdiVGHLQSQLSIQLDVKDKAK-- 153
Cdd:PTZ00212 81 PAAKILVDISKTQDEEVGDGTTSVVVLAGELLREAEKLLDQKIHPQTIIEGWRMALD--VARKALEEIAFDHGSDEEKfk 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 154 --MADVVKACVGTKFIGKWSDLAVKIALDAVEtvTLSENGRLEvdikrYAKVEKIPGGAIEESCVLKGVMINKDVTHPKM 231
Cdd:PTZ00212 159 edLLNIARTTLSSKLLTVEKDHFAKLAVDAVL--RLKGSGNLD-----YIQIIKKPGGTLRDSYLEDGFILEKKIGVGQP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 232 RRlIENPRIVLLDCSLEYKKgesqtnVEIIGEQ----DFTRMLQIEEEFVQRI---CADIIAVKPDLVFTEKGVSDLAQH 304
Cdd:PTZ00212 232 KR-LENCKILVANTPMDTDK------IKIYGAKvkvdSMEKVAEIEAAEKEKMknkVDKILAHGCNVFINRQLIYNYPEQ 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 305 YLLKAGITAIRRLRKTDNLRIARACGATIVNRTEELTEKDVGTGAGLFEVkKIGDEYFTFVTECKEPKACTILLRGASKD 384
Cdd:PTZ00212 305 LFAEAGIMAIEHADFDGMERLAAALGAEIVSTFDTPEKVKLGHCDLIEEI-MIGEDKLIRFSGCAKGEACTIVLRGASTH 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 385 ILNETERNLQDALHVARNLVLEPRLVAGGGAVE--MAASQLLTRKQVKGPYT----AVAHALEIIPRTLAQNCGANTIRA 458
Cdd:PTZ00212 384 ILDEAERSLHDALCVLSQTVKDTRVVLGGGCSEmlMANAVEELAKKVEGKKSlaieAFAKALRQIPTIIADNGGYDSAEL 463
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24647510 459 LTALRAKHAShtgdGVCAWGIDGESGEIVDMNVKNIWEPLAVKLQTYKTAVETAILLLRIDDIVS 523
Cdd:PTZ00212 464 VSKLRAEHYK----GNKTAGIDMEKGTVGDMKELGITESYKVKLSQLCSATEAAEMILRVDDIIR 524
|
|
| TCP1_beta |
cd03336 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ... |
10-523 |
8.11e-81 |
|
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: 261.88 E-value: 8.11e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 10 VLSQNTKRESGRKVQLENIQAGKAIADVIRTCLGPQAMLKML--MDPMGGIVMTNDGNAILREITVQHPAAKSMIEIART 87
Cdd:cd03336 1 ILKDGAQEEKGETARLSSFVGAIAIGDLVKTTLGPKGMDKILqsVGRSGGVTVTNDGATILKSIGVDNPAAKVLVDISKV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 88 QDEEVGDGTTSVIVLAGEMLAAAEPFLQQQIHPTVIIRAYREALEDIvghLQSQLSIQLDVK-DKAK----MADVVKACV 162
Cdd:cd03336 81 QDDEVGDGTTSVTVLAAELLREAEKLVAQKIHPQTIIEGYRMATAAA---REALLSSAVDHSsDEEAfredLLNIARTTL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 163 GTKFIGKWSDLAVKIALDAVEtvTLSENGRLEvdikrYAKVEKIPGGAIEESCVLKGVMINKD--VTHPKMrrlIENPRI 240
Cdd:cd03336 158 SSKILTQDKEHFAELAVDAVL--RLKGSGNLD-----AIQIIKKLGGSLKDSYLDEGFLLDKKigVNQPKR---IENAKI 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 241 VLLDCSLEYKKgesqtnVEIIGEQ----DFTRMLQIEEEFVQRI---CADIIAVKPDLVFTEKGVSDLAQHYLLKAGITA 313
Cdd:cd03336 228 LIANTPMDTDK------IKIFGAKvrvdSTAKVAEIEEAEKEKMknkVEKILKHGINCFINRQLIYNYPEQLFADAGIMA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 314 IRRLRKTDNLRIARACGATIVNRTEELTEKDVGTgAGLFEVKKIGDEYFTFVTECKEPKACTILLRGASKDILNETERNL 393
Cdd:cd03336 302 IEHADFDGVERLALVTGGEIASTFDHPELVKLGT-CKLIEEIMIGEDKLIRFSGVAAGEACTIVLRGASQQILDEAERSL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 394 QDALHVARNLVLEPRLVAGGGAVEMAASQLLTRKQVKGP------YTAVAHALEIIPRTLAQNCGANTIRALTALRAKHA 467
Cdd:cd03336 381 HDALCVLAQTVKDTRVVLGGGCSEMLMAKAVEELAKKTPgkkslaIEAFAKALRQLPTIIADNAGYDSAELVAQLRAAHY 460
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 24647510 468 shtgDGVCAWGIDGESGEIVDMNVKNIWEPLAVKLQTYKTAVETAILLLRIDDIVS 523
Cdd:cd03336 461 ----NGNTTAGLDMRKGTVGDMKELGITESFKVKRQVLLSASEAAEMILRVDDIIK 512
|
|
| chaperonin_like |
cd03333 |
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ... |
151-406 |
3.18e-77 |
|
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: 241.99 E-value: 3.18e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 151 KAKMADVVKACVGTKfIGKWSDLAVKIALDAVETVTLSENgrleVDIKRYAKVEKIPGGAIEESCVLKGVMINKDVTHPK 230
Cdd:cd03333 1 RELLLQVATTSLNSK-LSSWDDFLGKLVVDAVLKVGPDNR----MDDLGVIKVEKIPGGSLEDSELVVGVVFDKGYASPY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 231 MRRLIENPRIVLLDCSLEYkkgesqtnveiigeqdftrmlqieeefvqricadiiavkpdLVFTEKGVSDLAQHYLLKAG 310
Cdd:cd03333 76 MPKRLENAKILLLDCPLEY-----------------------------------------VVIAEKGIDDLALHYLAKAG 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 311 ITAIRRLRKTDNLRIARACGATIVNRTEELTEKDVGTgAGLFEVKKIGDEYFTFVTECKEPKACTILLRGASKDILNETE 390
Cdd:cd03333 115 IMAVRRVKKEDLERIARATGATIVSSLEDLTPEDLGT-AELVEETKIGEEKLTFIEGCKGGKAATILLRGATEVELDEVK 193
|
250
....*....|....*.
gi 24647510 391 RNLQDALHVARNLVLE 406
Cdd:cd03333 194 RSLHDALCAVRAAVEE 209
|
|
| chap_CCT_beta |
TIGR02341 |
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ... |
10-522 |
5.86e-66 |
|
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: 222.81 E-value: 5.86e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 10 VLSQNTKRESGRKVQLENIQAGKAIADVIRTCLGPQAMLKMLM--DPMGGIVMTNDGNAILREITVQHPAAKSMIEIART 87
Cdd:TIGR02341 2 IFKDGADEERAENARLSSFVGAIAIGDLVKSTLGPKGMDKILQssSSDASIMVTNDGATILKSIGVDNPAAKVLVDMSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 88 QDEEVGDGTTSVIVLAGEMLAAAEPFLQQQIHPTVIIRAYREALEdivGHLQSQLSIQLD-----VKDKAKMADVVKACV 162
Cdd:TIGR02341 82 QDDEVGDGTTSVTVLAAELLREAEKLINQKIHPQTIIAGYREATK---AARDALLKSAVDngsdeVKFRQDLMNIARTTL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 163 GTKFIGKWSDLAVKIALDAVetVTLSENGRLEvdikrYAKVEKIPGGAIEESCVLKGVMINKDVTHPKMRRlIENPRIVL 242
Cdd:TIGR02341 159 SSKILSQHKDHFAQLAVDAV--LRLKGSGNLE-----AIQIIKKLGGSLADSYLDEGFLLDKKIGVNQPKR-IENAKILI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 243 LDCSLEYKKGES-QTNVEIIGEQDFTRMLQIEEEFVQRICADIIAVKPDLVFTEKGVSDLAQHYLLKAGITAIRRLRKTD 321
Cdd:TIGR02341 231 ANTGMDTDKVKIfGSRVRVDSTAKVAELEHAEKEKMKEKVEKILKHGINCFINRQLIYNYPEQLFADAGVMAIEHADFEG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 322 NLRIARACGATIVNRTEELTEKDVGTgAGLFEVKKIGDEYFTFVTECKEPKACTILLRGASKDILNETERNLQDALHVAR 401
Cdd:TIGR02341 311 VERLALVTGGEIVSTFDHPELVKLGS-CDLIEEIMIGEDKLLKFSGVKLGEACTIVLRGATQQILDEAERSLHDALCVLS 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 402 NLVLEPRLVAGGGAVEMAASQLLTRKQVKGP------YTAVAHALEIIPRTLAQNCGANTIRALTALRAKHAshtgDGVC 475
Cdd:TIGR02341 390 QTVKESRTVLGGGCSEMLMSKAVTQEAQRTPgkealaVEAFARALRQLPTIIADNAGFDSAELVAQLRAAHY----NGNT 465
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 24647510 476 AWGIDGESGEIVDMNVKNIWEPLAVKLQTYKTAVETAILLLRIDDIV 522
Cdd:TIGR02341 466 TMGLDMNEGTIADMRQLGITESYKVKRAVVSSAAEAAEVILRVDNII 512
|
|
| Fab1_TCP |
cd03334 |
TCP-1 like domain of the eukaryotic phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinase Fab1. ... |
168-406 |
1.13e-50 |
|
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: 174.72 E-value: 1.13e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 168 GKWSDLAVKIALDAVETVTLSENGRLEVDIKRYAKVEKIPGGAIEESCVLKGVMINKDVTHPKMRRLIENPRIVLLDCSL 247
Cdd:cd03334 17 ESWLDILLPLVWKAASNVKPDVRAGDDMDIRQYVKIKKIPGGSPSDSEVVDGVVFTKNVAHKRMPSKIKNPRILLLQGPL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 248 EYKKGESQTnveiigeQDFTRMLQIEEEFVQRICADIIAVKPDLVFTEKGVSDLAQHYLLKAGITAIRRLRKTDNLRIAR 327
Cdd:cd03334 97 EYQRVENKL-------LSLDPVILQEKEYLKNLVSRIVALRPDVILVEKSVSRIAQDLLLEAGITLVLNVKPSVLERISR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 328 ACGATIVNRTEEL-TEKDVGTgAGLFEVKKIGDEY-----FTFVTECKEPKACTILLRGASKDILNETERNLQDALHVAR 401
Cdd:cd03334 170 CTGADIISSMDDLlTSPKLGT-CESFRVRTYVEEHgrsktLMFFEGCPKELGCTILLRGGDLEELKKVKRVVEFMVFAAY 248
|
....*
gi 24647510 402 NLVLE 406
Cdd:cd03334 249 HLKLE 253
|
|
| PRK14104 |
PRK14104 |
chaperonin GroEL; Provisional |
34-542 |
4.96e-08 |
|
chaperonin GroEL; Provisional
Pssm-ID: 172594 Cd Length: 546 Bit Score: 55.81 E-value: 4.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 34 IADVIRTCLGPQAMLKMLMDPMGGIVMTNDGNAILREITV----QHPAAKSMIEIARTQDEEVGDGTTSVIVLAGEMLAA 109
Cdd:PRK14104 23 LANAVKVTLGPKGRNVVLDKSFGAPRITKDGVTVAKEIELedkfENMGAQMVREVASKSADAAGDGTTTATVLAQAIVRE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 110 AEPFLQQQIHPTVIIRAYREALEDIVGHLQSQlSIQLDVKDKAKMADVVKACvGTKFIGKW-SDLAVKIALDAVETVTLS 188
Cdd:PRK14104 103 GAKSVAAGMNPMDLKRGIDLAVEAVVADLVKN-SKKVTSNDEIAQVGTISAN-GDAEIGKFlADAMKKVGNEGVITVEEA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 189 ENGRLEVDIkryakvekIPGGAIEESCVLKGVMINKDVTHPKMRR---LIENPRIVLLDCSLEYKKGESQTNVEIIGEQD 265
Cdd:PRK14104 181 KSLETELDV--------VEGMQFDRGYISPYFVTNADKMRVEMDDayiLINEKKLSSLNELLPLLEAVVQTGKPLVIVAE 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 266 FTRMLQIEEEFVQRICA--DIIAVKPDlVFTEKGVSDLAQHYLLKAGITAIRRLR-KTDNLRIARACGATIVNRTEELTE 342
Cdd:PRK14104 253 DVEGEALATLVVNRLRGglKVAAVKAP-GFGDRRKAMLQDIAILTGGQAISEDLGiKLENVTLQMLGRAKKVMIDKENTT 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 343 KDVGTG------AGLFEVK-KIGDEYFTFVTECKEPK-------ACTILLRGASKDILNETERNLQDALHVARNLVlEPR 408
Cdd:PRK14104 332 IVNGAGkkadieARVAQIKaQIEETTSDYDREKLQERlaklaggVAVIRVGGATEVEVKERKDRVDDAMHATRAAV-EEG 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 409 LVAGGGAVEMAASQLLTRKQV-----KGPYTAVAHALEIIPRTLAQNCGANTIRALTALRAKHAShtgdgvcAWGIDGES 483
Cdd:PRK14104 411 IVPGGGVALLRASEQLKGIKTknddqKTGVEIVRKALSAPARQIAINAGEDGSVIVGKILEKEQY-------SYGFDSQT 483
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 24647510 484 GEIVDMNVKNIWEPLAVKLQTYKTAVETAILLLRIDDIVSGSKKRGGNEPTNPAAMAQG 542
Cdd:PRK14104 484 GEYGNLVSKGIIDPTKVVRTAIQNAASVAALLITTEAMVAELPKKGGAGPAMPPGGGMG 542
|
|
| GroEL |
cd03344 |
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ... |
17-185 |
5.67e-08 |
|
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: 55.54 E-value: 5.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 17 RESGRKVQLENIQAgkaIADVIRTCLGPQAMLKMLMDPMGGIVMTNDGNAILREITVQHP----AAKSMIEIARTQDEEV 92
Cdd:cd03344 6 GEEARKALLRGVNK---LADAVKVTLGPKGRNVVIEKSFGSPKITKDGVTVAKEIELEDPfenmGAQLVKEVASKTNDVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 93 GDGTTSVIVLAGEMLAAAEPFLQQQIHPTVIIRAYREALEDIVGHLQSQlSIqlDVKDKAKMADVvkACV---GTKFIGK 169
Cdd:cd03344 83 GDGTTTATVLARAIIKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKL-SK--PVKTKEEIAQV--ATIsanGDEEIGE 157
|
170
....*....|....*.
gi 24647510 170 wsdlavKIAlDAVETV 185
Cdd:cd03344 158 ------LIA-EAMEKV 166
|
|
| groEL |
PRK12850 |
chaperonin GroEL; Reviewed |
33-537 |
4.90e-07 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237231 Cd Length: 544 Bit Score: 52.41 E-value: 4.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 33 AIADVIRTCLGPQAMLKMLMDPMGGIVMTNDGNAILREITVQHP----AAKSMIEIARTQDEEVGDGTTSVIVLAGEMLA 108
Cdd:PRK12850 22 ILANAVKVTLGPKGRNVVLEKSFGAPRITKDGVTVAKEIELEDKfenmGAQMVKEVASKTNDLAGDGTTTATVLAQAIVR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 109 AAEPFLQQQIHPTVIIRAYREALEDIVGHLQSQLSiqlDVKDKAKMADVVK-ACVGTKFIGKWSDLAV-KIALDAVETVT 186
Cdd:PRK12850 102 EGAKLVAAGMNPMDLKRGIDLAVAAVVDELKKIAK---KVTSSKEIAQVATiSANGDESIGEMIAEAMdKVGKEGVITVE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 187 LSENGRLEVDIkryakVEKIPGGaieescvlKGVMINKDVTHP-KMRRLIENPRIVLldcsleykkgesqTNVEIIGEQD 265
Cdd:PRK12850 179 EAKTLGTELDV-----VEGMQFD--------RGYLSPYFVTNPeKMRAELEDPYILL-------------HEKKISNLQD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 266 ftrMLQIEEEFVQricadiiAVKPDLVFTEkgvsDLAQHYLLKAGITAIRRLRKTDNLR--------------IARACGA 331
Cdd:PRK12850 233 ---LLPILEAVVQ-------SGRPLLIIAE----DVEGEALATLVVNKLRGGLKSVAVKapgfgdrrkamledIAVLTGG 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 332 TIVN-----RTEELTEKDVGTGAGLFevkkIGDEYFTFVTECKEPKA--------------------------------- 373
Cdd:PRK12850 299 QVISedlgiKLENVTLDMLGRAKRVL----ITKENTTIIDGAGDKKNiearvkqiraqieettsdydreklqerlaklag 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 374 --CTILLRGASKDILNETERNLQDALHVARNLVlEPRLVAGGG-AVEMAASQLLTRKQVKGPYTA----VAHALEIIPRT 446
Cdd:PRK12850 375 gvAVIRVGGATEVEVKEKKDRVDDALHATRAAV-EEGIVPGGGvALLRARSALRGLKGANADETAgidiVRRALEEPLRQ 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 447 LAQNCGANTIRALTALRakhashtgDGVCAWGIDGESGEIVDMNVKNIWEPLAVKLQTYKTAVETAILLLRIDDIVSGSK 526
Cdd:PRK12850 454 IATNAGFEGSVVVGKVA--------ELPGNFGFNAQTGEYGDMVEAGIIDPAKVTRTALQDAASIAALLITTEAMVAEAP 525
|
570
....*....|.
gi 24647510 527 KRGGNEPTNPA 537
Cdd:PRK12850 526 KKAAAAAAGPG 536
|
|
| PTZ00114 |
PTZ00114 |
Heat shock protein 60; Provisional |
26-513 |
5.37e-07 |
|
Heat shock protein 60; Provisional
Pssm-ID: 185455 Cd Length: 555 Bit Score: 52.22 E-value: 5.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 26 ENIQAG-KAIADVIRTCLGPQAMLKMLMDPMGGIVMTNDGNAILREITVQHPA----AKSMIEIARTQDEEVGDGTTSVI 100
Cdd:PTZ00114 25 QSLLKGiERLADAVAVTLGPKGRNVIIEQEYGSPKITKDGVTVAKAIEFSDRFenvgAQLIRQVASKTNDKAGDGTTTAT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 101 VLAGEMLAAAEPFLQQQIHPTVIIRAYREALEDIVGHLQSQlsiQLDVKDKAKMADVVK-ACVGTKFIGKW-SDLAVKIA 178
Cdd:PTZ00114 105 ILARAIFREGCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQ---SRPVKTKEDILNVATiSANGDVEIGSLiADAMDKVG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 179 LDAveTVTLSENGRLEVDIKRYakvekipggaiEESCVLKGVMINKDVTHPKMRRLI-ENPRIVLLDcsleyKKGESQTN 257
Cdd:PTZ00114 182 KDG--TITVEDGKTLEDELEVV-----------EGMSFDRGYISPYFVTNEKTQKVElENPLILVTD-----KKISSIQS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 258 VeiigeqdftrmLQIEEEFVQR---ICadIIAvkPDlvFTEKGVSDLA-QHYLLKAGITAIRR----LRKTDNLR-IARA 328
Cdd:PTZ00114 244 I-----------LPILEHAVKNkrpLL--IIA--ED--VEGEALQTLIiNKLRGGLKVCAVKApgfgDNRKDILQdIAVL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 329 CGATIVNRT------EELTEKDVGTgAGLFEVKKigDEyfTFVTECKEPKA----------------------------- 373
Cdd:PTZ00114 307 TGATVVSEDnvglklDDFDPSMLGS-AKKVTVTK--DE--TVILTGGGDKAeikervellrsqierttseydkeklkerl 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 374 -------CTILLRGASKDILNETERNLQDALHVARNlVLEPRLVAGGGAVEMAASQLLTRKQVKGPYTA--------VAH 438
Cdd:PTZ00114 382 aklsggvAVIKVGGASEVEVNEKKDRIEDALNATRA-AVEEGIVPGGGVALLRASKLLDKLEEDNELTPdqrtgvkiVRN 460
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24647510 439 ALEIIPRTLAQNCGAN---TIRALtaLRAKHASHtgdgvcawGIDGESGEIVDMNVKNIWEPLAVklqtYKTAVETAI 513
Cdd:PTZ00114 461 ALRLPTKQIAENAGVEgavVVEKI--LEKKDPSF--------GYDAQTGEYVNMFEAGIIDPTKV----VRSALVDAA 524
|
|
| groEL |
PRK12849 |
chaperonin GroEL; Reviewed |
33-103 |
3.77e-06 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237230 Cd Length: 542 Bit Score: 49.42 E-value: 3.77e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24647510 33 AIADVIRTCLGPQAMLKMLMDPMGGIVMTNDGNAILREITVQHP----AAKSMIEIARTQDEEVGDGTTSVIVLA 103
Cdd:PRK12849 21 KLADAVKVTLGPKGRNVVIDKSFGAPTITKDGVSIAKEIELEDPfenlGAQLVKEVASKTNDVAGDGTTTATVLA 95
|
|
| PLN03167 |
PLN03167 |
Chaperonin-60 beta subunit; Provisional |
25-166 |
3.61e-05 |
|
Chaperonin-60 beta subunit; Provisional
Pssm-ID: 215611 [Multi-domain] Cd Length: 600 Bit Score: 46.46 E-value: 3.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 25 LENIQAG-KAIADVIRTCLGPQAMLKMLMDPMGGIVMTNDGNAILREITVQHP----AAKSMIEIARTQDEEVGDGTTSV 99
Cdd:PLN03167 68 IKKLQAGvNKLADLVGVTLGPKGRNVVLESKYGSPKIVNDGVTVAKEVELEDPveniGAKLVRQAAAKTNDLAGDGTTTS 147
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24647510 100 IVLAGEMLAAAEPFLQQQIHPTVIIRAYREALEDIVGHLQsqlSIQLDVKDkAKMADVVKACVGTKF 166
Cdd:PLN03167 148 VVLAQGLIAEGVKVVAAGANPVQITRGIEKTAKALVKELK---KMSKEVED-SELADVAAVSAGNNY 210
|
|
| groEL |
PRK12851 |
chaperonin GroEL; Reviewed |
33-538 |
1.52e-04 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 171770 Cd Length: 541 Bit Score: 44.35 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 33 AIADVIRTCLGPQAMLKMLMDPMGGIVMTNDGNAILREITVQHP----AAKSMIEIARTQDEEVGDGTTSVIVLAGEMLA 108
Cdd:PRK12851 22 ILADAVKVTLGPKGRNVVIDKSFGAPTITNDGVTIAKEIELEDKfenmGAQMVREVASKTNDVAGDGTTTATVLAQAIVR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 109 AAEPFLQQQIHPTVIIRAYREALEDIVGHLQSQLSIQLDVKDKAKMADVvkACVGTKFIGKWSDLAV-KIALDAVETVTL 187
Cdd:PRK12851 102 EGAKAVAAGANPMDLKRGIDRAVAAVVEELKANARPVTTNAEIAQVATI--SANGDAEIGRLVAEAMeKVGNEGVITVEE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 188 SENGRLEVDIKRYAKVEkipggaieescvlKGVMINKDVTHP-KMRRLIENPRIVLLDcsleYKKGESQTNVEIIGE--Q 264
Cdd:PRK12851 180 SKTAETELEVVEGMQFD-------------RGYLSPYFVTDAdKMEAELEDPYILIHE----KKISNLQDLLPVLEAvvQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 265 DFTRMLQIEEEFVQRICADIIAVKPDLVFTEKGV-------------SDLAqhyLLKAGITAIRRL-RKTDNLRIARACG 330
Cdd:PRK12851 243 SGKPLLIIAEDVEGEALATLVVNKLRGGLKVAAVkapgfgdrrkamlEDIA---ILTGGTVISEDLgIKLENVTLEQLGR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 331 ATIVNRTEELTEkdVGTGAGLFE-----VKKIGDEYFTFVTECKEPKACTILLR----------GASKDI-LNETERNLQ 394
Cdd:PRK12851 320 AKKVVVEKENTT--IIDGAGSKTeiegrVAQIRAQIEETTSDYDREKLQERLAKlaggvavirvGASTEVeVKEKKDRVD 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 395 DALHVARNLVLEPRLVAGGGAVEMAASQLLTRKQVKGPYTA----VAHALEIIPRTLAQNCGANTIRALTALRAKHASHt 470
Cdd:PRK12851 398 DALHATRAAVEEGIVPGGGVALLRAVKALDKLETANGDQRTgveiVRRALEAPVRQIAENAGAEGSVVVGKLREKPGGY- 476
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24647510 471 gdgvcawGIDGESGEIVDMNVKNIWEPLAVKLQTYKTAVETAILLLRIDDIVSGSKKRGGNEPTNPAA 538
Cdd:PRK12851 477 -------GFNAATNEYGDLYAQGVIDPVKVVRTALQNAASVAGLLLTTEAMVAEKPKKEPAPPAPPGG 537
|
|
| groEL |
PRK12852 |
chaperonin GroEL; Reviewed |
34-542 |
2.14e-04 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237232 Cd Length: 545 Bit Score: 44.07 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 34 IADVIRTCLGPQAMLKMLMDPMGGIVMTNDGNAILREITV----QHPAAKSMIEIARTQDEEVGDGTTSVIVLAGEMLAA 109
Cdd:PRK12852 23 LANAVKVTLGPKGRNVVIEKSFGAPRITKDGVTVAKEIELedkfENMGAQMVREVASKTNDLAGDGTTTATVLAQAIVRE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 110 AEPFLQQQIHPTVIIRAYREALEDIVGHLQSQLSiqlDVKDKAKMADV-VKACVGTKFIGKWSDLAV-KIALDAVETVTL 187
Cdd:PRK12852 103 GAKAVAAGMNPMDLKRGIDIAVAAVVKDIEKRAK---PVASSAEIAQVgTISANGDAAIGKMIAQAMqKVGNEGVITVEE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 188 SENGRLEVDIKRYAKVEkipggaieescvlKGVMINKDVTHP-KMRRLIENPRIVLLDcsleyKKgesqtnveIIGEQDf 266
Cdd:PRK12852 180 NKSLETEVDIVEGMKFD-------------RGYLSPYFVTNAeKMTVELDDAYILLHE-----KK--------LSGLQA- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 267 trMLQIEEEFVQricadiiAVKPDLVFTEKgVSDLAQHYL----LKAG--ITAIRR-----LRKTDNLRIARACGATIVN 335
Cdd:PRK12852 233 --MLPVLEAVVQ-------SGKPLLIIAED-VEGEALATLvvnrLRGGlkVAAVKApgfgdRRKAMLEDIAILTGGQLIS 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 336 -----RTEELTEKDVG---------------TGAGLFE-----VKKIGDEYFTFVTECKEPK-----------ACTILLR 379
Cdd:PRK12852 303 edlgiKLENVTLKMLGrakkvvidkenttivNGAGKKAdiearVGQIKAQIEETTSDYDREKlqerlaklaggVAVIRVG 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 380 GASKDILNETERNLQDALHVARNLVLEPrLVAGGGAVEMAASQLLTR-----KQVKGPYTAVAHALEIIPRTLAQNCGAN 454
Cdd:PRK12852 383 GATEVEVKEKKDRVEDALNATRAAVQEG-IVPGGGVALLRAKKAVGRinndnADVQAGINIVLKALEAPIRQIAENAGVE 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647510 455 TIRALTALRAKHAShtgdgvcAWGIDGESGEIVDMNVKNIWEPLAVKLQTYKTAVETAILLLRIDDIVSGSKKRGGnEPT 534
Cdd:PRK12852 462 GSIVVGKILENKSE-------TFGFDAQTEEYVDMVAKGIIDPAKVVRTALQDAASVAGLLVTTEAMVAELPKKDA-APA 533
|
....*...
gi 24647510 535 NPAAMAQG 542
Cdd:PRK12852 534 MPAGGGMG 541
|
|
| |
