|
Name |
Accession |
Description |
Interval |
E-value |
| TCP1_epsilon |
cd03339 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ... |
10-508 |
0e+00 |
|
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: 1028.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 10 DEYGRPFLIIKDQDRKSRLMGLEALKSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTND---------------- 73
Cdd:cd03339 1 DEYGRPFIIVREQEKKKRLKGLEAHKSHILAAKSVANILRTSLGPRGMDKILVSPDGEVTVTNDgatilekmdvdhqiak 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 74 -----------EIGDGTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARVAIVHLDKISDSVLVDIKDTEPLIQTA 142
Cdd:cd03339 81 llvelsksqddEIGDGTTGVVVLAGALLEQAEKLLDRGIHPIRIADGYEQACKIAVEHLEEIADKIEFSPDNKEPLIQTA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 143 KTTLGSKVVNSCHRQMAEIAVNAVLTVADMERRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKKVEDAKIA 222
Cdd:cd03339 161 MTSLGSKIVSRCHRQFAEIAVDAVLSVADLERKDVNFELIKVEGKVGGRLEDTKLVKGIVIDKDFSHPQMPKEVKDAKIA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 223 ILTCPFEPPKPKTKHKLDVTSVEDYKALQKYEKEKFEEMIQQIKETGANLAICQWGFDDEANHLLLQNNLPAVRWVGGPE 302
Cdd:cd03339 241 ILTCPFEPPKPKTKHKLDITSVEDYKKLQEYEQKYFREMVEQVKDAGANLVICQWGFDDEANHLLLQNGLPAVRWVGGVE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 303 IELIAIATGGRIVPRFSELTAEKLGFAGLVQEISFGTTKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVI 382
Cdd:cd03339 321 IELIAIATGGRIVPRFEDLSPEKLGKAGLVREISFGTTKDKMLVIEGCPNSKAVTIFIRGGNKMIIEEAKRSLHDALCVV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 383 RNLIRDNRVVYGGGAAEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKEMNPAL 462
Cdd:cd03339 401 RNLIRDNRIVYGGGAAEISCSLAVEKAADKCSGIEQYAMRAFADALESIPLALAENSGLNPIETLSEVKARQVKEKNPHL 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 194378060 463 GIDCLHKGTNDMKQQHVIETLIGKKQQISLATQMVRMILKIDDIRK 508
Cdd:cd03339 481 GIDCLGRGTNDMKEQKVFETLISKKQQILLATQVVKMILKIDDVIV 526
|
|
| chap_CCT_epsi |
TIGR02343 |
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ... |
6-510 |
0e+00 |
|
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: 946.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 6 TLAFDEYGRPFLIIKDQDRKSRLMGLEALKSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTND------------ 73
Cdd:TIGR02343 1 ILAFDEYGRPFIIIKDQDNKKRLKGLEAKKSNIAAAKSVASILRTSLGPKGMDKMLISPDGDITVTNDgatilsqmdvdn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 74 ---------------EIGDGTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARVAIVHLDKISDSVLVDIKDTEPL 138
Cdd:TIGR02343 81 qiaklmvelsksqddEIGDGTTGVVVLAGALLEQAEELLDKGIHPIKIADGFEEAARIAVEHLEEISDEISADNNNREPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 139 IQTAKTTLGSKVVNSCHRQMAEIAVNAVLTVADMERRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKKVED 218
Cdd:TIGR02343 161 IQAAKTSLGSKIVSKCHRRFAEIAVDAVLNVADMERRDVDFDLIKVEGKVGGSLEDTKLIKGIIIDKDFSHPQMPKEVED 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 219 AKIAILTCPFEPPKPKTKHKLDVTSVEDYKALQKYEKEKFEEMIQQIKETGANLAICQWGFDDEANHLLLQNNLPAVRWV 298
Cdd:TIGR02343 241 AKIAILTCPFEPPKPKTKHKLDISSVEEYKKLQKYEQQKFKEMIDDIKKSGANLVICQWGFDDEANHLLLQNDLPAVRWV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 299 GGPEIELIAIATGGRIVPRFSELTAEKLGFAGLVQEISFGTTKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDA 378
Cdd:TIGR02343 321 GGQELELIAIATGGRIVPRFQELSKDKLGKAGLVREISFGTTKDRMLVIEQCKNSKAVTIFIRGGNKMIIEEAKRSIHDA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 379 LCVIRNLIRDNRVVYGGGAAEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKEM 458
Cdd:TIGR02343 401 LCVVRNLIKDSRIVYGGGAAEISCSLAVSQEADKYPGVEQYAIRAFADALETIPMALAENSGLDPIGTLSTLKSLQLKEK 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 194378060 459 NPALGIDCLHKGTNDMKQQHVIETLIGKKQQISLATQMVRMILKIDDIRKPG 510
Cdd:TIGR02343 481 NPNLGVDCLGYGTNDMKEQFVFETLIGKKQQILLATQLVRMILKIDDVISPG 532
|
|
| chaperonin_type_I_II |
cd00309 |
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ... |
25-506 |
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: 537.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 25 KSRLMGLEALKSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTND---------------------------EIGD 77
Cdd:cd00309 1 KEREFGEEARLSNINAAKALADAVKTTLGPKGMDKMLVDSLGDPTITNDgatilkeievehpaakllvevaksqddEVGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 78 GTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARVAIVHLDKISDSVlvDIKDTEPLIQTAKTTLGSKVVNSCHRQ 157
Cdd:cd00309 81 GTTTVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVPI--DVEDREELLKVATTSLNSKLVSGGDDF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 158 MAEIAVNAVLTVADMERrDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKKVEDAKIAILTCPFEPpkpktkh 237
Cdd:cd00309 159 LGELVVDAVLKVGKENG-DVDLGVIRVEKKKGGSLEDSELVVGMVFDKGYLSPYMPKRLENAKILLLDCKLEY------- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 238 kldvtsvedykalqkyekekfeemiqqiketganLAICQWGFDDEANHLLLQNNLPAVRWVGGPEIELIAIATGGRIVPR 317
Cdd:cd00309 231 ----------------------------------VVIAEKGIDDEALHYLAKLGIMAVRRVRKEDLERIAKATGATIVSR 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 318 FSELTAEKLGFAGLVQEISFGttKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGA 397
Cdd:cd00309 277 LEDLTPEDLGTAGLVEETKIG--DEKYTFIEGCKGGKVATILLRGATEVELDEAERSLHDALCAVRAAVEDGGIVPGGGA 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 398 AEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKEMNPAlGIDCLHKGTNDMKQQ 477
Cdd:cd00309 355 AEIELSKALEELAKTLPGKEQLGIEAFADALEVIPRTLAENAGLDPIEVVTKLRAKHAEGGGNA-GGDVETGEIVDMKEA 433
|
490 500
....*....|....*....|....*....
gi 194378060 478 HVIETLIGKKQQISLATQMVRMILKIDDI 506
Cdd:cd00309 434 GIIDPLKVKRQALKSATEAASLILTIDDI 462
|
|
| Cpn60_TCP1 |
pfam00118 |
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ... |
44-506 |
6.29e-176 |
|
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: 504.04 E-value: 6.29e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 44 VANTMRTSLGPNGLDKMMVDKDGDVTVTND---------------------------EIGDGTTGVVVLAGALLEEAEQL 96
Cdd:pfam00118 1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDgatilkeleiqhpaakllveaakaqdeEVGDGTTTVVVLAGELLEEAEKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 97 LDRGIHPIRIADGYEQAARVAIVHLDKIsDSVLVDIKDTEPLIQTAKTTLGSKVVNSCHRQMAEIAVNAVLTVADmERRD 176
Cdd:pfam00118 81 LAAGVHPTTIIEGYEKALEKALEILDSI-ISIPVEDVDREDLLKVARTSLSSKIISRESDFLAKLVVDAVLAIPK-NDGS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 177 VDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKKVEDAKIAILTCPFEPPKPKTKHKLDVTSVEDYKALQKYEKE 256
Cdd:pfam00118 159 FDLGNIGVVKILGGSLEDSELVDGVVLDKGPLHPDMPKRLENAKVLLLNCSLEYEKTETKATVVLSDAEQLERFLKAEEE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 257 KFEEMIQQIKETGANLAICQWGFDDEANHLLLQNNLPAVRWVGGPEIELIAIATGGRIVPRFSELTAEKLGFAGLVQEIS 336
Cdd:pfam00118 239 QILEIVEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMALRRVKKRDLERLAKATGARAVSSLDDLTPDDLGTAGKVEEEK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 337 FGttKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAEISCALAVSQEADKCPTL 416
Cdd:pfam00118 319 IG--DEKYTFIEGCKSPKAATILLRGATDHVLDEIERSIHDALCVVKNAIEDPRVVPGGGAVEMELARALREYAKSVSGK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 417 EQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKEmNPALGIDCLHKGTNDMKQQHVIETLIGKKQQISLATQM 496
Cdd:pfam00118 397 EQLAIEAFAEALEVIPKTLAENAGLDPIEVLAELRAAHASG-EKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKSATEA 475
|
490
....*....|
gi 194378060 497 VRMILKIDDI 506
Cdd:pfam00118 476 ASTILRIDDI 485
|
|
| thermosome_alpha |
NF041082 |
thermosome subunit alpha; |
15-506 |
8.54e-171 |
|
thermosome subunit alpha;
Pssm-ID: 469009 Cd Length: 518 Bit Score: 492.09 E-value: 8.54e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 15 PFLIIKDQdrKSRLMGLEALKSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTND--------------------- 73
Cdd:NF041082 2 PILILKEG--TQRTSGRDAQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDVVITNDgvtilkemdiehpaakmivev 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 74 ------EIGDGTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARVAIVHLDKIsdSVLVDIKDTEPLIQTAKTTLG 147
Cdd:NF041082 80 aktqddEVGDGTTTAVVLAGELLKKAEELLDQDIHPTIIAEGYRLAAEKALEILDEI--AIKVDPDDKETLKKIAATAMT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 148 SKVVNSCHRQMAEIAVNAVLTVADME-RRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKKVEDAKIAILTC 226
Cdd:NF041082 158 GKGAEAAKDKLADLVVDAVKAVAEKDgGYNVDLDNIKVEKKVGGSIEDSELVEGVVIDKERVHPGMPKRVENAKIALLDA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 227 PFEPPKPKTKHKLDVTSVEDYKALQKYEKEKFEEMIQQIKETGANLAICQWGFDDEANHLLLQNNLPAVRWVGGPEIELI 306
Cdd:NF041082 238 PLEVKKTEIDAKISITDPDQLQAFLDQEEKMLKEMVDKIADSGANVVFCQKGIDDLAQHYLAKEGILAVRRVKKSDMEKL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 307 AIATGGRIVPRFSELTAEKLGFAGLVQEISFGttKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLI 386
Cdd:NF041082 318 AKATGARIVTSIDDLSPEDLGYAGLVEERKVG--GDKMIFVEGCKNPKAVTILLRGGTEHVVDEVERALEDALRVVRVVL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 387 RDNRVVYGGGAAEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKEMNPAlGIDC 466
Cdd:NF041082 396 EDGKVVAGGGAPEVELALRLREYAASVGGREQLAIEAFAEALEIIPRTLAENAGLDPIDALVELRSAHEKGNKTA-GLDV 474
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 194378060 467 LHKGTNDMKQQHVIETLIGKKQQISLATQMVRMILKIDDI 506
Cdd:NF041082 475 YTGKVVDMLEIGVVEPLRVKTQAIKSATEAAVMILRIDDV 514
|
|
| cpn60 |
cd03343 |
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ... |
17-506 |
2.49e-165 |
|
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: 478.30 E-value: 2.49e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 17 LIIKDqdRKSRLMGLEALKSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTND----------------------- 73
Cdd:cd03343 2 LILKE--GTQRTSGRDAQRMNIAAAKAVAEAVRTTLGPKGMDKMLVDSLGDVTITNDgatilkemdiehpaakmlvevak 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 74 ----EIGDGTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARVAIVHLDKISDSvlVDIKDTEPLIQTAKTTLGSK 149
Cdd:cd03343 80 tqdeEVGDGTTTAVVLAGELLEKAEDLLDQNIHPTVIIEGYRLAAEKALELLDEIAIK--VDPDDKDTLRKIAKTSLTGK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 150 VVNSCHRQMAEIAVNAVLTVADME--RRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKKVEDAKIAILTCP 227
Cdd:cd03343 158 GAEAAKDKLADLVVDAVLQVAEKRdgKYVVDLDNIKIEKKTGGSVDDTELIRGIVIDKEVVHPGMPKRVENAKIALLDAP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 228 FEPPKPKTKHKLDVTSVEDYKALQKYEKEKFEEMIQQIKETGANLAICQWGFDDEANHLLLQNNLPAVRWVGGPEIELIA 307
Cdd:cd03343 238 LEVKKTEIDAKIRITSPDQLQAFLEQEEAMLKEMVDKIADTGANVVFCQKGIDDLAQHYLAKAGILAVRRVKKSDMEKLA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 308 IATGGRIVPRFSELTAEKLGFAGLVQEISFGttKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIR 387
Cdd:cd03343 318 RATGAKIVTNIDDLTPEDLGEAELVEERKVG--DDKMVFVEGCKNPKAVTILLRGGTEHVVDELERALEDALRVVADALE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 388 DNRVVYGGGAAEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKEMNPAlGIDCL 467
Cdd:cd03343 396 DGKVVAGGGAVEIELAKRLREYARSVGGREQLAVEAFADALEEIPRTLAENAGLDPIDTLVELRAAHEKGNKNA-GLDVY 474
|
490 500 510
....*....|....*....|....*....|....*....
gi 194378060 468 HKGTNDMKQQHVIETLIGKKQQISLATQMVRMILKIDDI 506
Cdd:cd03343 475 TGEVVDMLEKGVIEPLRVKKQAIKSATEAATMILRIDDV 513
|
|
| thermosome_beta |
NF041083 |
thermosome subunit beta; |
15-506 |
3.57e-164 |
|
thermosome subunit beta;
Pssm-ID: 469010 Cd Length: 519 Bit Score: 475.21 E-value: 3.57e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 15 PFLIIKDQdrKSRLMGLEALKSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTND--------------------- 73
Cdd:NF041083 2 PVLILKEG--TQRTKGRDAQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDIVITNDgatilkemdvqhpaakmlvev 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 74 ------EIGDGTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARVAIVHLDKISDSvlVDIKDTEPLIQTAKTTLG 147
Cdd:NF041083 80 aktqddEVGDGTTTAVVLAGELLKKAEELLDQNIHPTIIANGYRLAAEKAIEILDEIAEK--VDPDDRETLKKIAETSLT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 148 SKVVNSCHRQMAEIAVNAVLTVAdmERRD----VDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKKVEDAKIAI 223
Cdd:NF041083 158 SKGVEEARDYLAEIAVKAVKQVA--EKRDgkyyVDLDNIQIEKKHGGSIEDTQLIYGIVIDKEVVHPGMPKRVENAKIAL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 224 LTCPFEPPKPKTKHKLDVTSVEDYKALQKYEKEKFEEMIQQIKETGANLAICQWGFDDEANHLLLQNNLPAVRWVGGPEI 303
Cdd:NF041083 236 LDAPLEVKKTEIDAEIRITDPDQLQKFLDQEEKMLKEMVDKIKATGANVVFCQKGIDDLAQHYLAKAGILAVRRVKKSDM 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 304 ELIAIATGGRIVPRFSELTAEKLGFAGLVQEISFGTtkDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIR 383
Cdd:NF041083 316 EKLAKATGARIVTNIDDLTPEDLGYAELVEERKVGD--DKMVFVEGCKNPKAVTILIRGGTEHVVDEAERALEDALSVVA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 384 NLIRDNRVVYGGGAAEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKEmNPALG 463
Cdd:NF041083 394 DAVEDGKIVAGGGAPEVELAKRLREYAATVGGREQLAVEAFAEALEIIPRTLAENAGLDPIDILVKLRSAHEKG-KKWAG 472
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 194378060 464 IDCLHKGTNDMKQQHVIETLIGKKQQISLATQMVRMILKIDDI 506
Cdd:NF041083 473 INVFTGEVVDMWELGVIEPLRVKTQAIKSATEAATMILRIDDV 515
|
|
| thermosome_arch |
TIGR02339 |
thermosome, various subunits, archaeal; Thermosome is the name given to the archaeal rather ... |
15-506 |
5.40e-155 |
|
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: 451.83 E-value: 5.40e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 15 PFLIIKDQdrKSRLMGLEALKSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTND--------------------- 73
Cdd:TIGR02339 1 PVFILKEG--TQRTSGRDAQRNNIAAAKAVAEAVKSTLGPRGMDKMLVDSLGDVTITNDgatilkemdiehpaakmlvev 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 74 ------EIGDGTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARVAIVHLDKISDSvlVDIKDTEPLIQTAKTTLG 147
Cdd:TIGR02339 79 aktqdeEVGDGTTTAVVLAGELLEKAEDLLEQDIHPTVIIEGYRKAAEKALEIIDEIATK--ISPEDRDLLKKIAYTSLT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 148 SKVVNSCHRQ-MAEIAVNAVLTVADME---RRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKKVEDAKIAI 223
Cdd:TIGR02339 157 SKASAEVAKDkLADLVVEAVKQVAELRgdgKYYVDLDNIKIVKKKGGSIEDTELVEGIVVDKEVVHPGMPKRVENAKIAL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 224 LTCPFEPPKPKTKHKLDVTSVEDYKALQKYEKEKFEEMIQQIKETGANLAICQWGFDDEANHLLLQNNLPAVRWVGGPEI 303
Cdd:TIGR02339 237 LDAPLEVEKTEIDAKIRITDPDQIKKFLDQEEAMLKEMVDKIASAGANVVICQKGIDDVAQHYLAKAGILAVRRVKKSDI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 304 ELIAIATGGRIVPRFSELTAEKLGFAGLVQEISFGttKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIR 383
Cdd:TIGR02339 317 EKLARATGARIVSSIDEITESDLGYAELVEERKVG--EDKMVFVEGCKNPKAVTILLRGGTEHVVDELERSIQDALHVVA 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 384 NLIRDNRVVYGGGAAEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKEmNPALG 463
Cdd:TIGR02339 395 NALEDGKIVAGGGAVEIELALRLRSYARSVGGREQLAIEAFADALEEIPRILAENAGLDPIDALVDLRAKHEKG-NKNAG 473
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 194378060 464 IDCLHKGTNDMKQQHVIETLIGKKQQISLATQMVRMILKIDDI 506
Cdd:TIGR02339 474 INVFTGEIEDMLELGVIEPLRVKEQAIKSATEAATMILRIDDV 516
|
|
| TCP1_delta |
cd03338 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ... |
35-506 |
2.10e-131 |
|
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.
Pssm-ID: 239454 [Multi-domain] Cd Length: 515 Bit Score: 391.26 E-value: 2.10e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 35 KSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTND---------------------------EIGDGTTGVVVLAG 87
Cdd:cd03338 11 LSNIQAAKAVADAIRTSLGPRGMDKMIQTGKGEVIITNDgatilkqmsvlhpaakmlvelskaqdiEAGDGTTSVVVLAG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 88 ALLEEAEQLLDRGIHPIRIADGYEQAARVAIVHLDKIsdSVLVDIKDTEPLIQTAKTTLGSKVVNSCHRQMAEIAVNAVL 167
Cdd:cd03338 91 ALLSACESLLKKGIHPTVISESFQIAAKKAVEILDSM--SIPVDLNDRESLIKSATTSLNSKVVSQYSSLLAPIAVDAVL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 168 TVADMER-RDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSH-PQMPKKVEDAKIAILTCPFEPPKPKTKHKLdvtSVE 245
Cdd:cd03338 169 KVIDPATaTNVDLKDIRIVKKLGGTIEDTELVDGLVFTQKASKkAGGPTRIEKAKIGLIQFCLSPPKTDMDNNI---VVN 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 246 DYKA---LQKYEKEKFEEMIQQIKETGANLAICQW-----GFDDEANHLLLQNNLPAVRWVGGPEIELIAIATGGRIVPR 317
Cdd:cd03338 246 DYAQmdrILREERKYILNMCKKIKKSGCNVLLIQKsilrdAVSDLALHFLAKLKIMVVKDIEREEIEFICKTIGCKPVAS 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 318 FSELTAEKLGFAGLVQEISFGTtkDKMLVIEQCKNS-RAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGG 396
Cdd:cd03338 326 IDHFTEDKLGSADLVEEVSLGD--GKIVKITGVKNPgKTVTILVRGSNKLVLDEAERSLHDALCVIRCLVKKRALIPGGG 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 397 AAEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVK-EMNpaLGIDCLHKGTNDMK 475
Cdd:cd03338 404 APEIEIALQLSEWARTLTGVEQYCVRAFADALEVIPYTLAENAGLNPISIVTELRNRHAQgEKN--AGINVRKGAITNIL 481
|
490 500 510
....*....|....*....|....*....|.
gi 194378060 476 QQHVIETLIGKKQQISLATQMVRMILKIDDI 506
Cdd:cd03338 482 EENVVQPLLVSTSAITLATETVRMILKIDDI 512
|
|
| chap_CCT_delta |
TIGR02342 |
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ... |
35-506 |
3.06e-121 |
|
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: 365.65 E-value: 3.06e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 35 KSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTND---------------------------EIGDGTTGVVVLAG 87
Cdd:TIGR02342 12 TSNIVAAKAVADAIRTSLGPKGMDKMIQDGKGEVIITNDgatilkqmavlhpaakmlvelskaqdiEAGDGTTSVVILAG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 88 ALLEEAEQLLDRGIHPIRIADGYEQAARVAIVHLDKISDSvlVDIKDTEPLIQTAKTTLGSKVVNSCHRQMAEIAVNAVL 167
Cdd:TIGR02342 92 ALLGACERLLNKGIHPTIISESFQSAADEAIKILDEMSIP--VDLSDREQLLKSATTSLSSKVVSQYSSLLAPLAVDAVL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 168 TVADMER-RDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQ-MPKKVEDAKIAILTCPFEPPKPKTKHKLDVTSVE 245
Cdd:TIGR02342 170 KVIDPENaKNVDLNDIKVVKKLGGTIDDTELIEGLVFTQKASKSAgGPTRIEKAKIGLIQFQISPPKTDMENQIIVNDYA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 246 DYKALQKYEKEKFEEMIQQIKETGANLAICQW-----GFDDEANHLLLQNNLPAVRWVGGPEIELIAIATGGRIVPRFSE 320
Cdd:TIGR02342 250 QMDRVLKEERAYILNIVKKIKKTGCNVLLIQKsilrdAVNDLALHFLAKMKIMVVKDIEREEIEFICKTIGCKPIASIDH 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 321 LTAEKLGFAGLVQEIsfGTTKDKMLVIEQCKN-SRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAE 399
Cdd:TIGR02342 330 FTADKLGSAELVEEV--DSDGGKIIKITGIQNaGKTVTVVVRGSNKLVIDEAERSLHDALCVIRCLVKKRGLIAGGGAPE 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 400 ISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVK-EMNpaLGIDCLHKGTNDMKQQH 478
Cdd:TIGR02342 408 IEIARRLSKYARTMKGVESYCVRAFADALEVIPYTLAENAGLNPIKVVTELRNRHANgEKT--AGISVRKGGITNMLEEH 485
|
490 500
....*....|....*....|....*...
gi 194378060 479 VIETLIGKKQQISLATQMVRMILKIDDI 506
Cdd:TIGR02342 486 VLQPLLVTTSAITLASETVRSILKIDDI 513
|
|
| GroEL |
COG0459 |
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ... |
25-506 |
4.78e-109 |
|
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227 Cd Length: 497 Bit Score: 333.20 E-value: 4.78e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 25 KSRLMGLEALKSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTND------------------------------- 73
Cdd:COG0459 3 KQILFGEDARRANIRGVKALADAVKVTLGPKGRNVMLVKSFGDPTITNDgvtiakeieledpfenmgaqlvkevasktnd 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 74 EIGDGTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARVAIVHLDKISdsvlVDIKDTEPLIQTAKTTLGSKvvns 153
Cdd:COG0459 83 EAGDGTTTATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIA----KPVDDKEELAQVATISANGD---- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 154 chRQMAEIAVNAVLTVADMERrdvdfelIKVEgKVGGRLEDTKLIKGVIVDKDFSHPQ-------MPKKVEDAKIAILTC 226
Cdd:COG0459 155 --EEIGELIAEAMEKVGKDGV-------ITVE-EGKGLETELEVVEGMQFDKGYLSPYfvtdpekMPAELENAYILLTDK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 227 PFEPPKPktkhkldvtsvedykalqkyekekFEEMIQQIKETGANLAICQWGFDDEANHLLLQNNLPAVR---WVGGP-- 301
Cdd:COG0459 225 KISSIQD------------------------LLPLLEKVAQSGKPLLIIAEDIDGEALATLVVNGIRGVLrvvAVKAPgf 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 302 ------EIELIAIATGGRIV-----PRFSELTAEKLGFAGLVQEisfgtTKDKMLVIEQCKNSRAVTIFIRGGNKMIIEE 370
Cdd:COG0459 281 gdrrkaMLEDIAILTGGRVIsedlgLKLEDVTLDDLGRAKRVEV-----DKDNTTIVEGAGNPKAIVILVGAATEVEVKE 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 371 AKRSLHDALCVIRNLIRDnRVVYGGGAAEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEV 450
Cdd:COG0459 356 RKRRVEDALHATRAAVEE-GIVPGGGAALLRAARALRELAAKLEGDEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKV 434
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 194378060 451 RARQvkemNPALGIDCLHKGTNDMKQQHVIETLIGKKQQISLATQMVRMILKIDDI 506
Cdd:COG0459 435 RAAK----DKGFGFDAATGEYVDMLEAGVIDPAKVKRSALQNAASVAGLILTTEAV 486
|
|
| TCP1_gamma |
cd03337 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ... |
20-506 |
4.34e-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: 327.72 E-value: 4.34e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 20 KDQDRKSRLmglealkSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTND-------------------------- 73
Cdd:cd03337 11 RESGRKAQL-------GNIQAAKTVADVIRTCLGPRAMLKMLLDPMGGIVLTNDgnailreidvahpaaksmielsrtqd 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 74 -EIGDGTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARVAIVHLDKISDSVlvDIKDTEPLIQTAKTTLGSKVVN 152
Cdd:cd03337 84 eEVGDGTTSVIILAGEILAVAEPFLERGIHPTVIIKAYRKALEDALKILEEISIPV--DVNDRAQMLKIIKSCIGTKFVS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 153 SCHRQMAEIAVNAVLTVA---DMERRDVDFE-LIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKKVEDAKIAILTCPF 228
Cdd:cd03337 162 RWSDLMCNLALDAVKTVAveeNGRKKEIDIKrYAKVEKIPGGEIEDSRVLDGVMLNKDVTHPKMRRRIENPRIVLLDCPL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 229 EppkpktkhkldvtsvedykalqkYekekfeemiqqiketganLAICQWGFDDEANHLLLQNNLPAVRWVGGPEIELIAI 308
Cdd:cd03337 242 E-----------------------Y------------------LVITEKGVSDLAQHYLVKAGITALRRVRKTDNNRIAR 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 309 ATGGRIVPRFSELTAEKLGFAGLVQEISFGTtKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRD 388
Cdd:cd03337 281 ACGATIVNRPEELTESDVGTGAGLFEVKKIG-DEYFTFITECKDPKACTILLRGASKDVLNEVERNLQDAMAVARNIILN 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 389 NRVVYGGGAAEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKEMNPALGIDCLH 468
Cdd:cd03337 360 PKLVPGGGATEMAVSHALSEKAKSIEGVEQWPYKAVASALEVIPRTLAQNCGANVIRTLTELRAKHAQGENSTWGIDGET 439
|
490 500 510
....*....|....*....|....*....|....*...
gi 194378060 469 KGTNDMKQQHVIETLIGKKQQISLATQMVRMILKIDDI 506
Cdd:cd03337 440 GDIVDMKELGIWDPLAVKAQTYKTAIEAACMLLRIDDI 477
|
|
| chap_CCT_gamma |
TIGR02344 |
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ... |
15-506 |
2.68e-102 |
|
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: 317.06 E-value: 2.68e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 15 PFLIIKDQDRksRLMGLEALKSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTND--------------------- 73
Cdd:TIGR02344 1 PVLVLNQNTK--RESGRKAQLSNIQAAKAVADIIRTCLGPRSMLKMLLDPMGGIVMTNDgnailreidvahpaaksmiel 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 74 ------EIGDGTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARVAIVHLDKISdsVLVDIKDTEPLIQTAKTTLG 147
Cdd:TIGR02344 79 srtqdeEVGDGTTSVIILAGEMLSVAEPFLEQNIHPTVIIRAYRKALDDALSVLEEIS--IPVDVNDDAAMLKLIQSCIG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 148 SKVVNSCHRQMAEIAVNAVLTVA--DMERRDVDFE-LIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKKVEDAKIAIL 224
Cdd:TIGR02344 157 TKFVSRWSDLMCDLALDAVRTVQrdENGRKEIDIKrYAKVEKIPGGDIEDSCVLKGVMINKDVTHPKMRRYIENPRIVLL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 225 TCPFEPPKPKTKHKLDVTSVEDYKALQKYEKEKFEEMIQQIKETGANLAICQWGFDDEANHLLLQNNLPAVRWVGGPEIE 304
Cdd:TIGR02344 237 DCPLEYKKGESQTNIEITKEEDWNRILQMEEEYVQLMCEDIIAVKPDLVITEKGVSDLAQHYLLKANITAIRRVRKTDNN 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 305 LIAIATGGRIVPRFSELTAEKLGF-AGLVQEISFGttKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIR 383
Cdd:TIGR02344 317 RIARACGATIVNRPEELRESDVGTgCGLFEVKKIG--DEYFTFITECKDPKACTILLRGASKDILNEVERNLQDAMAVAR 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 384 NLIRDNRVVYGGGAAEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKEMNPALG 463
Cdd:TIGR02344 395 NVLLDPKLVPGGGATEMAVSVALTEKSKKLEGVEQWPYRAVADALEIIPRTLAQNCGANVIRTLTELRAKHAQENNCTWG 474
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 194378060 464 IDCLHKGTNDMKQQHVIETLIGKKQQISLATQMVRMILKIDDI 506
Cdd:TIGR02344 475 IDGETGKIVDMKEKGIWEPLAVKLQTYKTAIESACLLLRIDDI 517
|
|
| TCP1_beta |
cd03336 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ... |
18-508 |
3.28e-94 |
|
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: 295.78 E-value: 3.28e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 18 IIKDQDRKSRlmGLEALKSHIMAAKAVANTMRTSLGPNGLDKMM--VDKDGDVTVTND---------------------- 73
Cdd:cd03336 1 ILKDGAQEEK--GETARLSSFVGAIAIGDLVKTTLGPKGMDKILqsVGRSGGVTVTNDgatilksigvdnpaakvlvdis 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 74 -----EIGDGTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARVAIVHLDKISDSVLVDIKDT-EPLIQTAKTTLG 147
Cdd:cd03336 79 kvqddEVGDGTTSVTVLAAELLREAEKLVAQKIHPQTIIEGYRMATAAAREALLSSAVDHSSDEEAFrEDLLNIARTTLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 148 SKVVNSCHRQMAEIAVNAVLTVADmerrDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQmPKKVEDAKIAILTCP 227
Cdd:cd03336 159 SKILTQDKEHFAELAVDAVLRLKG----SGNLDAIQIIKKLGGSLKDSYLDEGFLLDKKIGVNQ-PKRIENAKILIANTP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 228 FEPPKPKT-KHKLDVTSVEDYKALQKYEKEKFEEMIQQIKETGANLAICQWGFDDEANHLLLQNNLPAVRWVGGPEIELI 306
Cdd:cd03336 234 MDTDKIKIfGAKVRVDSTAKVAEIEEAEKEKMKNKVEKILKHGINCFINRQLIYNYPEQLFADAGIMAIEHADFDGVERL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 307 AIATGGRIVPRFSELTAEKLGFAGLVQEISFGttKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLI 386
Cdd:cd03336 314 ALVTGGEIASTFDHPELVKLGTCKLIEEIMIG--EDKLIRFSGVAAGEACTIVLRGASQQILDEAERSLHDALCVLAQTV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 387 RDNRVVYGGGAAEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKEMNPAlGIDC 466
Cdd:cd03336 392 KDTRVVLGGGCSEMLMAKAVEELAKKTPGKKSLAIEAFAKALRQLPTIIADNAGYDSAELVAQLRAAHYNGNTTA-GLDM 470
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 194378060 467 LHKGTNDMKQQHVIETLIGKKQQISLATQMVRMILKIDDIRK 508
Cdd:cd03336 471 RKGTVGDMKELGITESFKVKRQVLLSASEAAEMILRVDDIIK 512
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
36-508 |
7.17e-93 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 292.70 E-value: 7.17e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 36 SHIMAAKAVANTMRTSLGPNGLDKMMV-----DKDGDVTVTND---------------------------EIGDGTTGVV 83
Cdd:PTZ00212 26 QSFVGAIAVADLVKTTLGPKGMDKILQpmsegPRSGNVTVTNDgatilksvwldnpaakilvdisktqdeEVGDGTTSVV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 84 VLAGALLEEAEQLLDRGIHPIRIADGYEQAARVAIVHLDKISDSVLVDIKD-TEPLIQTAKTTLGSKVVNSCHRQMAEIA 162
Cdd:PTZ00212 106 VLAGELLREAEKLLDQKIHPQTIIEGWRMALDVARKALEEIAFDHGSDEEKfKEDLLNIARTTLSSKLLTVEKDHFAKLA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 163 VNAVLTVadmeRRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQmPKKVEDAKIAILTCPFEPPKPKT-KHKLDV 241
Cdd:PTZ00212 186 VDAVLRL----KGSGNLDYIQIIKKPGGTLRDSYLEDGFILEKKIGVGQ-PKRLENCKILVANTPMDTDKIKIyGAKVKV 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 242 TSVEDYKALQKYEKEKFEEMIQQIKETGANLAICQWGFDDEANHLLLQNNLPAVRWVGGPEIELIAIATGGRIVPRFSEL 321
Cdd:PTZ00212 261 DSMEKVAEIEAAEKEKMKNKVDKILAHGCNVFINRQLIYNYPEQLFAEAGIMAIEHADFDGMERLAAALGAEIVSTFDTP 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 322 TAEKLGFAGLVQEISFGttKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAEIS 401
Cdd:PTZ00212 341 EKVKLGHCDLIEEIMIG--EDKLIRFSGCAKGEACTIVLRGASTHILDEAERSLHDALCVLSQTVKDTRVVLGGGCSEML 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 402 CALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKEMNPAlGIDCLHKGTNDMKQQHVIE 481
Cdd:PTZ00212 419 MANAVEELAKKVEGKKSLAIEAFAKALRQIPTIIADNGGYDSAELVSKLRAEHYKGNKTA-GIDMEKGTVGDMKELGITE 497
|
490 500
....*....|....*....|....*..
gi 194378060 482 TLIGKKQQISLATQMVRMILKIDDIRK 508
Cdd:PTZ00212 498 SYKVKLSQLCSATEAAEMILRVDDIIR 524
|
|
| TCP1_eta |
cd03340 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ... |
15-504 |
1.10e-87 |
|
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: 279.17 E-value: 1.10e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 15 PFLIIKDQDRKSRlmGLEALKSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTND--------------------- 73
Cdd:cd03340 1 PIILLKEGTDTSQ--GKGQLISNINACQAIADAVRTTLGPRGMDKLIVDGRGKVTISNDgatilklldivhpaaktlvdi 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 74 ------EIGDGTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARVAIVHLDKISdsVLVDIKDTEP----LIQTAK 143
Cdd:cd03340 79 aksqdaEVGDGTTSVVVLAGEFLKEAKPFIEDGVHPQIIIRGYRKALQLAIEKIKEIA--VNIDKEDKEEqrelLEKCAA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 144 TTLGSKVVNSCHRQMAEIAVNAVLTVADmerrDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFS---HPQMPKKVEDAK 220
Cdd:cd03340 157 TALNSKLIASEKEFFAKMVVDAVLSLDD----DLDLDMIGIKKVPGGSLEDSQLVNGVAFKKTFSyagFEQQPKKFKNPK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 221 IAILTCPFEPPKPKTKHKLDVTSVEDYKALQKYEKEKFEEMIQQIKETGANLAICQWGFDDEANHLLLQNNLPAVRWVGG 300
Cdd:cd03340 233 ILLLNVELELKAEKDNAEVRVEDPEEYQAIVDAEWKIIYDKLEKIVKSGANVVLSKLPIGDLATQYFADRDIFCAGRVPE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 301 PEIELIAIATGGRIVPRFSELTAEKLGFAGLVQEISFGttKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALC 380
Cdd:cd03340 313 EDLKRVAQATGGSIQTTVSNITDDVLGTCGLFEERQVG--GERYNIFTGCPKAKTCTIILRGGAEQFIEEAERSLHDAIM 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 381 VIRNLIRDNRVVYGGGAAEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKEMNP 460
Cdd:cd03340 391 IVRRAIKNDSVVAGGGAIEMELSKYLRDYSRTIAGKQQLVINAFAKALEIIPRQLCDNAGFDATDILNKLRQKHAQGGGK 470
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 194378060 461 ALGIDCLHKGTNDMKQQHVIETLIGKKQQISLATQMVRMILKID 504
Cdd:cd03340 471 WYGVDINNEGIADNFEAFVWEPSLVKINALTAATEAACLILSVD 514
|
|
| TCP1_theta |
cd03341 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ... |
32-506 |
1.17e-86 |
|
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: 274.87 E-value: 1.17e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 32 EALKSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTND---------------------------EIGDGTTGVVV 84
Cdd:cd03341 8 EAVLRNIEACKELSQITRTSYGPNGMNKMVINHLEKLFVTSDaatilrelevqhpaakllvmasqmqeeEIGDGTNLVVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 85 LAGALLEEAEQLLDRGIHPIRIADGYEQAARVAIVHLDKISDSVLVDIKDTEPLIQTAKTTLGSKVV-NSCHrqMAEIAV 163
Cdd:cd03341 88 LAGELLEKAEELLRMGLHPSEIIEGYEKALKKALEILEELVVYKIEDLRNKEEVSKALKTAIASKQYgNEDF--LSPLVA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 164 NAVLTVADMERRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDfSHPQMpKKVEDAKIAILTCPFEppkpktkhkldvts 243
Cdd:cd03341 166 EACISVLPENIGNFNVDNIRVVKILGGSLEDSKVVRGMVFKRE-PEGSV-KRVKKAKVAVFSCPFD-------------- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 244 vedykalqkyekekfeemiqqikeTGANLAICQWGFDDEANHLLLQNNLPAVRWVGGPEIELIAIATGGRIVPRFSELTA 323
Cdd:cd03341 230 ------------------------IGVNVIVAGGSVGDLALHYCNKYGIMVIKINSKFELRRLCRTVGATPLPRLGAPTP 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 324 EKLGFAGLVQEISFGTTKdkMLVIEQCKNSRAV-TIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAEISC 402
Cdd:cd03341 286 EEIGYCDSVYVEEIGDTK--VVVFRQNKEDSKIaTIVLRGATQNILDDVERAIDDGVNVFKSLTKDGRFVPGAGATEIEL 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 403 ALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKE-MNPALGIDCLHKGTNDMKQQHVIE 481
Cdd:cd03341 364 AKKLKEYGEKTPGLEQYAIKKFAEAFEVVPRTLAENAGLDATEVLSELYAAHQKGnKSAGVDIESGDEGTKDAKEAGIFD 443
|
490 500
....*....|....*....|....*
gi 194378060 482 TLIGKKQQISLATQMVRMILKIDDI 506
Cdd:cd03341 444 HLATKKWAIKLATEAAVTVLRVDQI 468
|
|
| TCP1_alpha |
cd03335 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ... |
27-508 |
4.65e-86 |
|
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: 274.93 E-value: 4.65e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 27 RLMGLEALKSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTND---------------------------EIGDGT 79
Cdd:cd03335 3 RTSGQDVRTQNVTAAMAIANIVKSSLGPVGLDKMLVDDIGDVTITNDgatilkllevehpaakilvelaqlqdkEVGDGT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 80 TGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARVAIVHLDKiSDSVLVDIKDTEPLIQTAKTTLGSKVVNSCHRQMA 159
Cdd:cd03335 83 TSVVIIAAELLKRANELVKQKIHPTTIISGYRLACKEAVKYIKE-HLSISVDNLGKESLINVAKTSMSSKIIGADSDFFA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 160 EIAVNAVLTVADM-ERRDV-----DFELIKVEGKvggRLEDTKLIKGVIVDKDFSHPQMPKKVEDAKIAILTCPFEppkp 233
Cdd:cd03335 162 NMVVDAILAVKTTnEKGKTkypikAVNILKAHGK---SAKESYLVNGYALNCTRASQGMPTRVKNAKIACLDFNLQ---- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 234 KTKHKLDV----TSVEDYKALQKYEKEKFEEMIQQIKETGANLAICQWGFDDEANHLLLQNNLPAVRWVGGPEIELIAIA 309
Cdd:cd03335 235 KTKMKLGVqvvvTDPEKLEKIRQRESDITKERIKKILAAGANVVLTTGGIDDMCLKYFVEAGAMAVRRVKKEDLRRIAKA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 310 TGGRIVPRFSELTAE------KLGFAGLVQEISFGttKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIR 383
Cdd:cd03335 315 TGATLVSTLANLEGEetfdpsYLGEAEEVVQERIG--DDELILIKGTKKRSSASIILRGANDFMLDEMERSLHDALCVVK 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 384 NLIRDNRVVYGGGAAEisCALAVSQE--ADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKEMNPA 461
Cdd:cd03335 393 RTLESNSVVPGGGAVE--TALSIYLEnfATTLGSREQLAIAEFAEALLVIPKTLAVNAAKDATELVAKLRAYHAAAQVKP 470
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 194378060 462 -------LGIDcLHKGT-NDMKQQHVIETLIGKKQQISLATQMVRMILKIDDIRK 508
Cdd:cd03335 471 dkkhlkwYGLD-LINGKvRDNLEAGVLEPTVSKIKSLKFATEAAITILRIDDLIK 524
|
|
| chap_CCT_eta |
TIGR02345 |
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ... |
15-510 |
5.30e-84 |
|
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: 269.32 E-value: 5.30e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 15 PFLIIKDQDRKSRlmGLEALKSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTND--------------------- 73
Cdd:TIGR02345 3 TIVLLKEGTDTSQ--GKGQLISNINACVAIAEALKTTLGPRGMDKLIVGSNGKATISNDgatilklldivhpaaktlvdi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 74 ------EIGDGTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARVAIVHLDKISDSV-LVDIKDTEPLIQTAKTTL 146
Cdd:TIGR02345 81 aksqdaEVGDGTTSVTILAGELLKEAKPFIEEGVHPQLIIRCYREALSLAVEKIKEIAVTIdEEKGEQRELLEKCAATAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 147 GSKVVNSCHRQMAEIAVNAVLTvadMERRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFS---HPQMPKKVEDAKIAI 223
Cdd:TIGR02345 161 SSKLISHNKEFFSKMIVDAVLS---LDRDDLDLKLIGIKKVQGGALEDSQLVNGVAFKKTFSyagFEQQPKKFANPKILL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 224 LTCPFEPPKPKTKHKLDVTSVEDYKALQKYEKEKFEEMIQQIKETGANLAICQWGFDDEANHLLLQNNLPAVRWVGGPEI 303
Cdd:TIGR02345 238 LNVELELKAEKDNAEIRVEDVEDYQAIVDAEWAIIFRKLEKIVESGANVVLSKLPIGDLATQYFADRDIFCAGRVSAEDL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 304 ELIAIATGGRIVPRFSELTAEKLGFAGLVQEISFGttKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIR 383
Cdd:TIGR02345 318 KRVIKACGGSIQSTTSDLEADVLGTCALFEERQIG--SERYNYFTGCPHAKTCTIILRGGAEQFIEEAERSLHDAIMIVR 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 384 NLIRDNRVVYGGGAAEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKEmNPALG 463
Cdd:TIGR02345 396 RALKNKKIVAGGGAIEMELSKCLRDYSKTIDGKQQLIINAFAKALEIIPRQLCENAGFDSIEILNKLRSRHAKG-GKWYG 474
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 194378060 464 IDCLHKGTNDMKQQHVIETLIGKKQQISLATQMVRMILKIDD-IRKPG 510
Cdd:TIGR02345 475 VDINTEDIGDNFEAFVWEPALVKINALKAAFEAACTILSVDEtITNPK 522
|
|
| chap_CCT_alpha |
TIGR02340 |
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ... |
27-514 |
6.10e-84 |
|
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: 269.67 E-value: 6.10e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 27 RLMGLEALKSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTND---------------------------EIGDGT 79
Cdd:TIGR02340 7 RTSGQDVRTQNVTAAMAIANIVKTSLGPVGLDKMLVDDIGDVTITNDgatilkllevehpaakilvelaqlqdrEVGDGT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 80 TGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARVAIVHLDKiSDSVLVDIKDTEPLIQTAKTTLGSKVVNSCHRQMA 159
Cdd:TIGR02340 87 TSVVIIAAELLKRADELVKNKIHPTSVISGYRLACKEAVKYIKE-NLSVSVDELGREALINVAKTSMSSKIIGLDSDFFS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 160 EIAVNAVLTVADM-ERRDVDF--ELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKKVEDAKIAILTCPFEppkpKTK 236
Cdd:TIGR02340 166 NIVVDAVLAVKTTnENGETKYpiKAINILKAHGKSARESMLVKGYALNCTVASQQMPKRIKNAKIACLDFNLQ----KAK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 237 HKLDVT-SVEDYKALQKYEKEKFE---EMIQQIKETGANLAICQWGFDDEANHLLLQNNLPAVRWVGGPEIELIAIATGG 312
Cdd:TIGR02340 242 MALGVQiVVDDPEKLEQIRQREADitkERIKKILDAGANVVLTTGGIDDMCLKYFVEAGAMGVRRCKKEDLKRIAKATGA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 313 RIVPRFSELTAE------KLGFAGLVQEISFGttKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLI 386
Cdd:TIGR02340 322 TLVSTLADLEGEetfeasYLGFADEVVQERIA--DDECILIKGTKKRKSASIILRGANDFMLDEMERSLHDALCVVKRTL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 387 RDNRVVYGGGAAEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKEM-NPA---- 461
Cdd:TIGR02340 400 ESNSVVPGGGAVEAALSIYLENFATTLGSREQLAIAEFARALLIIPKTLAVNAAKDSTELVAKLRAYHAAAQlKPEkkhl 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 194378060 462 --LGIDCLHKGTNDMKQQHVIETLIGKKQQISLATQMVRMILKIDD-IRKPGESEE 514
Cdd:TIGR02340 480 kwYGLDLVNGKIRDNKEAGVLEPTVSKVKSLKFATEAAITILRIDDlIKLNPEQSK 535
|
|
| chap_CCT_theta |
TIGR02346 |
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ... |
32-506 |
7.10e-83 |
|
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: 266.58 E-value: 7.10e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 32 EALKSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTND---------------------------EIGDGTTGVVV 84
Cdd:TIGR02346 18 EAVIKNIEACKELSQITRTSLGPNGMNKMVINHLEKLFVTNDaatilrelevqhpaakllvmasemqenEIGDGTNLVLV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 85 LAGALLEEAEQLLDRGIHPIRIADGYEQAARVAIVHLDKISDSVLVDIKDTEPLIQTAKTTLGSKVVNScHRQMAEIAVN 164
Cdd:TIGR02346 98 LAGELLNKAEELIRMGLHPSEIIKGYEMALKKAMEILEELVVWEVKDLRDKDELIKALKASISSKQYGN-EDFLAQLVAQ 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 165 AVLTVADMERRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFShpQMPKKVEDAKIAILTCPFEPPKPKTKHKLDVTSV 244
Cdd:TIGR02346 177 ACSTVLPKNPQNFNVDNIRVCKILGGSLSNSEVLKGMVFNREAE--GSVKSVKNAKVAVFSCPLDTATTETKGTVLIHNA 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 245 EDYKALQKYEKEKFEEMIQQIKETGANLAICQWGFDDEANHLLLQNNLPAVRWVGGPEIELIAIATGGRIVPRFSELTAE 324
Cdd:TIGR02346 255 EELLNYSKGEENQIEAMIKAIADSGVNVIVTGGSVGDMALHYLNKYNIMVLKIPSKFELRRLCKTVGATPLPRLGAPTPE 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 325 KLGFAGLVQEISFGTtkDKMLVIEQCK-NSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAEISCA 403
Cdd:TIGR02346 335 EIGYVDSVYVSEIGG--DKVTVFKQENgDSKISTIILRGSTDNLLDDIERAIDDGVNTVKALVKDGRLLPGAGATEIELA 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 404 LAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQvKEMNPALGID--CLHKGTNDMKQQHVIE 481
Cdd:TIGR02346 413 SRLTKYGEKLPGLDQYAIKKFAEAFEIIPRTLAENAGLNANEVIPKLYAAH-KKGNKSKGIDieAESDGVKDASEAGIYD 491
|
490 500
....*....|....*....|....*
gi 194378060 482 TLIGKKQQISLATQMVRMILKIDDI 506
Cdd:TIGR02346 492 MLATKKWAIKLATEAAVTVLRVDQI 516
|
|
| chap_CCT_beta |
TIGR02341 |
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ... |
18-508 |
5.47e-77 |
|
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: 250.93 E-value: 5.47e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 18 IIKDQDRKSRlmGLEALKSHIMAAKAVANTMRTSLGPNGLDKMMV--DKDGDVTVTND---------------------- 73
Cdd:TIGR02341 2 IFKDGADEER--AENARLSSFVGAIAIGDLVKSTLGPKGMDKILQssSSDASIMVTNDgatilksigvdnpaakvlvdms 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 74 -----EIGDGTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARVAIVHLDKIS-DSVLVDIKDTEPLIQTAKTTLG 147
Cdd:TIGR02341 80 kvqddEVGDGTTSVTVLAAELLREAEKLINQKIHPQTIIAGYREATKAARDALLKSAvDNGSDEVKFRQDLMNIARTTLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 148 SKVVNSCHRQMAEIAVNAVLTVadmeRRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQmPKKVEDAKIAILTCP 227
Cdd:TIGR02341 160 SKILSQHKDHFAQLAVDAVLRL----KGSGNLEAIQIIKKLGGSLADSYLDEGFLLDKKIGVNQ-PKRIENAKILIANTG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 228 FEPPKPKT-KHKLDVTSVEDYKALQKYEKEKFEEMIQQIKETGANLAICQWGFDDEANHLLLQNNLPAVRWVGGPEIELI 306
Cdd:TIGR02341 235 MDTDKVKIfGSRVRVDSTAKVAELEHAEKEKMKEKVEKILKHGINCFINRQLIYNYPEQLFADAGVMAIEHADFEGVERL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 307 AIATGGRIVPRFSELTAEKLGFAGLVQEISFGttKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLI 386
Cdd:TIGR02341 315 ALVTGGEIVSTFDHPELVKLGSCDLIEEIMIG--EDKLLKFSGVKLGEACTIVLRGATQQILDEAERSLHDALCVLSQTV 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 387 RDNRVVYGGGAAEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRArQVKEMNPALGIDc 466
Cdd:TIGR02341 393 KESRTVLGGGCSEMLMSKAVTQEAQRTPGKEALAVEAFARALRQLPTIIADNAGFDSAELVAQLRA-AHYNGNTTMGLD- 470
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 194378060 467 LHKGT-NDMKQQHVIETLIGKKQQISLATQMVRMILKIDDIRK 508
Cdd:TIGR02341 471 MNEGTiADMRQLGITESYKVKRAVVSSAAEAAEVILRVDNIIK 513
|
|
| chaperonin_like |
cd03333 |
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ... |
136-388 |
7.32e-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: 240.45 E-value: 7.32e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 136 EPLIQTAKTTLGSKVvNSCHRQMAEIAVNAVLTVADMERrDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKK 215
Cdd:cd03333 2 ELLLQVATTSLNSKL-SSWDDFLGKLVVDAVLKVGPDNR-MDDLGVIKVEKIPGGSLEDSELVVGVVFDKGYASPYMPKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 216 VEDAKIAILTCPFEPpkpktkhkldvtsvedykalqkyekekfeemiqqiketganLAICQWGFDDEANHLLLQNNLPAV 295
Cdd:cd03333 80 LENAKILLLDCPLEY-----------------------------------------VVIAEKGIDDLALHYLAKAGIMAV 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 296 RWVGGPEIELIAIATGGRIVPRFSELTAEKLGFAGLVQEISFGTtkDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSL 375
Cdd:cd03333 119 RRVKKEDLERIARATGATIVSSLEDLTPEDLGTAELVEETKIGE--EKLTFIEGCKGGKAATILLRGATEVELDEVKRSL 196
|
250
....*....|...
gi 194378060 376 HDALCVIRNLIRD 388
Cdd:cd03333 197 HDALCAVRAAVEE 209
|
|
| chap_CCT_zeta |
TIGR02347 |
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ... |
33-512 |
9.95e-74 |
|
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: 242.72 E-value: 9.95e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 33 ALKSHIMAAKAVANTMRTSLGPNGLDKMMVD--------KDGDVTVTN------------------DEI-GDGTTGVVVL 85
Cdd:TIGR02347 17 ALMMNINAARGLQDVLKTNLGPKGTLKMLVSgagdikltKDGNVLLNEmqiqhptasmiaraataqDDItGDGTTSTVLL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 86 AGALLEEAEQLLDRGIHPIRIADGYEQAARVAIVHLDKISdSVLVDIKDTEPLIQTAKTTLGSKVVNSCHRQMAEIAVNA 165
Cdd:TIGR02347 97 IGELLKQAERYILEGVHPRIITEGFEIARKEALQFLDKFK-VKKEDEVDREFLLNVARTSLRTKLPADLADQLTEIVVDA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 166 VLTVADMERrDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKKVEDAKIAILTCPFEPPKPKTKHKLDVTSVE 245
Cdd:TIGR02347 176 VLAIKKDGE-DIDLFMVEIMEMKHKSATDTTLIRGLVLDHGARHPDMPRRVKNAYILTCNVSLEYEKTEVNSGFFYSSAE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 246 DYKALQKYEKEKFEEMIQQIKE-------TGAN---LAICQWGFDDEANHLLLQNNLPAVRWVGGPEIELIAIATGGRIV 315
Cdd:TIGR02347 255 QREKLVKAERKFVDDRVKKIIElkkkvcgKSPDkgfVVINQKGIDPPSLDLLAKEGIMALRRAKRRNMERLTLACGGEAL 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 316 PRFSELTAEKLGFAGLVQEISFGttKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGG 395
Cdd:TIGR02347 335 NSVEDLTPECLGWAGLVYETTIG--EEKYTFIEECKNPKSCTILIKGPNDHTIAQIKDAVRDGLRAVKNAIEDKCVVPGA 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 396 GAAEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKEMNPaLGIDcLHKGTN-DM 474
Cdd:TIGR02347 413 GAFEIAAYRHLKEYKKSVKGKAKLGVEAFANALLVIPKTLAENSGFDAQDTLVKLEDEHDEGGEV-VGVD-LNTGEPiDP 490
|
490 500 510
....*....|....*....|....*....|....*...
gi 194378060 475 KQQHVIETLIGKKQQISLATQMVRMILKIDDIRKPGES 512
Cdd:TIGR02347 491 EIKGIWDNYRVKKQLIQSATVIASQLLLVDEVMRAGRS 528
|
|
| TCP1_zeta |
cd03342 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
32-510 |
1.96e-72 |
|
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: 237.93 E-value: 1.96e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 32 EALKSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTND------EI---------------------GDGTTGVVV 84
Cdd:cd03342 12 QALAVNISAAKGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDgnvllsEMqiqhptasmiaraataqdditGDGTTSNVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 85 LAGALLEEAEQLLDRGIHPIRIADGYEQAARVAIVHLDKISDSVLVDIkDTEPLIQTAKTTLGSKVVNSCHRQMAEIAVN 164
Cdd:cd03342 92 LIGELLKQAERYIQEGVHPRIITEGFELAKNKALKFLESFKVPVEIDT-DRELLLSVARTSLRTKLHADLADQLTEIVVD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 165 AVLTVadmERRDVDFELIKVE-GKVGGRLE-DTKLIKGVIVDKDFSHPQMPKKVEDAkiAILTCPFeppkpktkhkldvt 242
Cdd:cd03342 171 AVLAI---YKPDEPIDLHMVEiMQMQHKSDsDTKLIRGLVLDHGARHPDMPKRVENA--YILTCNV-------------- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 243 SVEdykalqkYEK-EKFEEMIQqiketgaNLAICQWGFDDEANHLLLQNNLPAVRWVGGPEIELIAIATGGRIVPRFSEL 321
Cdd:cd03342 232 SLE-------YEKtEVNSGFFY-------SVVINQKGIDPPSLDMLAKEGILALRRAKRRNMERLTLACGGVAMNSVDDL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 322 TAEKLGFAGLVQEISFGttKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAEIS 401
Cdd:cd03342 298 SPECLGYAGLVYERTLG--EEKYTFIEGVKNPKSCTILIKGPNDHTITQIKDAIRDGLRAVKNAIEDKCVVPGAGAFEVA 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 402 CALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRaRQVKEMNPALGIDCLHKGTNDMKQQHVIE 481
Cdd:cd03342 376 LYAHLKEFKKSVKGKAKLGVQAFADALLVIPKTLAENSGLDVQETLVKLQ-DEYAEGGQVGGVDLDTGEPMDPESEGIWD 454
|
490 500
....*....|....*....|....*....
gi 194378060 482 TLIGKKQQISLATQMVRMILKIDDIRKPG 510
Cdd:cd03342 455 NYSVKRQILHSATVIASQLLLVDEIIRAG 483
|
|
| Fab1_TCP |
cd03334 |
TCP-1 like domain of the eukaryotic phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinase Fab1. ... |
160-386 |
9.08e-16 |
|
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: 77.26 E-value: 9.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 160 EIAVNAVLTVADMERRDVDF-------ELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKKVEDAKIAILTCPFEPPK 232
Cdd:cd03334 21 DILLPLVWKAASNVKPDVRAgddmdirQYVKIKKIPGGSPSDSEVVDGVVFTKNVAHKRMPSKIKNPRILLLQGPLEYQR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 233 PKTKhkldVTSVEDYKAlqkYEKEKFEEMIQQIKETGANLAICQWGFDDEANHLLLQNNLPAVRWVGGPEIELIAIATGG 312
Cdd:cd03334 101 VENK----LLSLDPVIL---QEKEYLKNLVSRIVALRPDVILVEKSVSRIAQDLLLEAGITLVLNVKPSVLERISRCTGA 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 194378060 313 RIVPRFSELTAE-KLGFAGLVQEISF----GTTKDKMLvIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLI 386
Cdd:cd03334 174 DIISSMDDLLTSpKLGTCESFRVRTYveehGRSKTLMF-FEGCPKELGCTILLRGGDLEELKKVKRVVEFMVFAAYHLK 251
|
|
| GroEL |
cd03344 |
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ... |
30-480 |
3.93e-11 |
|
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: 65.17 E-value: 3.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 30 GLEALKSHIMAAKAVANTMRTSLGPNG----LDKMM----VDKDGdVTV------------------------TNDEIGD 77
Cdd:cd03344 6 GEEARKALLRGVNKLADAVKVTLGPKGrnvvIEKSFgspkITKDG-VTVakeieledpfenmgaqlvkevaskTNDVAGD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 78 GTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARVAIVHLDKISdsvlVDIKDTEPLIQTAKT------TLGSKVV 151
Cdd:cd03344 85 GTTTATVLARAIIKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLS----KPVKTKEEIAQVATIsangdeEIGELIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 152 NSchrqMAEIAVNAVLTVADmerrdvdfelikvegkvGGRLEDT-KLIKGVIVDKDFSHPQM---PKK----VEDAKIAI 223
Cdd:cd03344 161 EA----MEKVGKDGVITVEE-----------------GKTLETElEVVEGMQFDRGYLSPYFvtdPEKmeveLENPYILL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 224 ltcpfeppkpkTKHKLDvtSVEDYKALqkyekekfeemIQQIKETGANLAICQWGFDDEANHLLLQNNLP------AVRw 297
Cdd:cd03344 220 -----------TDKKIS--SIQELLPI-----------LELVAKAGRPLLIIAEDVEGEALATLVVNKLRgglkvcAVK- 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 298 vgGPE--------IELIAIATGGRIVP-----RFSELTAEKLGFAGLVQeisfgTTKDKMLV-------------IEQCK 351
Cdd:cd03344 275 --APGfgdrrkamLEDIAILTGGTVISeelglKLEDVTLEDLGRAKKVV-----VTKDDTTIiggagdkaaikarIAQIR 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 352 NSRAVT----------------------IFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNrVVYGGGAAEISCALAVSQE 409
Cdd:cd03344 348 KQIEETtsdydkeklqerlaklsggvavIKVGGATEVELKEKKDRVEDALNATRAAVEEG-IVPGGGVALLRASPALDKL 426
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 194378060 410 ADKCPtLEQYAMRAFADALEVIPMALSENSGMNPiqtmtEVRARQVKEMNPALGIDCLHKGTNDMKQQHVI 480
Cdd:cd03344 427 KALNG-DEKLGIEIVRRALEAPLRQIAENAGVDG-----SVVVEKVLESPDGFGYDAATGEYVDMIEAGII 491
|
|
| GroEL |
TIGR02348 |
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ... |
32-186 |
5.29e-08 |
|
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: 55.38 E-value: 5.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 32 EALKSHIMAAKAVANTMRTSLGPNG----LDKM----MVDKDGdVTV------------------------TNDEIGDGT 79
Cdd:TIGR02348 9 EARKALLRGVDKLADAVKVTLGPKGrnvvLEKSfgapTITKDG-VTVakeieledkfenmgaqlvkevaskTNDVAGDGT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 80 TGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARVAIVHLDKISdsvlVDIKDTEPLIQTAKTTLGS--KVVNSCHRQ 157
Cdd:TIGR02348 88 TTATVLAQAIVKEGLKNVAAGANPIELKRGIEKAVEAVVEELKKLS----KPVKGKKEIAQVATISANNdeEIGSLIAEA 163
|
170 180
....*....|....*....|....*....
gi 194378060 158 MAEIAVNAVLTVAdmERRDVDFELIKVEG 186
Cdd:TIGR02348 164 MEKVGKDGVITVE--ESKSLETELEVVEG 190
|
|
| PTZ00114 |
PTZ00114 |
Heat shock protein 60; Provisional |
25-442 |
1.21e-07 |
|
Heat shock protein 60; Provisional
Pssm-ID: 185455 Cd Length: 555 Bit Score: 54.15 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 25 KSRLMGLEALKSHIMAAKAVANTMRTSLGPNG----LDKM----MVDKDGdVTV------------------------TN 72
Cdd:PTZ00114 15 KEIRFGDEARQSLLKGIERLADAVAVTLGPKGrnviIEQEygspKITKDG-VTVakaiefsdrfenvgaqlirqvaskTN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 73 DEIGDGTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARVAIVHLDKISDsvlvDIKDTEPLIQTAKTT------L 146
Cdd:PTZ00114 94 DKAGDGTTTATILARAIFREGCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQSR----PVKTKEDILNVATISangdveI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 147 GSKVVNSchrqMAEIAVNAVLTVADmerrdvdfelikvegkvGGRLEDT-KLIKGVIVDKDFSHPQMPKKVEDAKIaILT 225
Cdd:PTZ00114 170 GSLIADA----MDKVGKDGTITVED-----------------GKTLEDElEVVEGMSFDRGYISPYFVTNEKTQKV-ELE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 226 CPFeppkpktkhkldvTSVEDYKALQkyekekfeemIQQI-------KETGANLAICQWGFDDEANHLLLQNNLP----- 293
Cdd:PTZ00114 228 NPL-------------ILVTDKKISS----------IQSIlpilehaVKNKRPLLIIAEDVEGEALQTLIINKLRgglkv 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 294 -AVRWVGGPE-----IELIAIATGGRIVPR------FSELTAEKLGFAGLVQ----EISF-GTTKDKMLVIEQCKNSRA- 355
Cdd:PTZ00114 285 cAVKAPGFGDnrkdiLQDIAVLTGATVVSEdnvglkLDDFDPSMLGSAKKVTvtkdETVIlTGGGDKAEIKERVELLRSq 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 356 ------------------------VTIFIRGGNKMIIEEAKRSLHDALCVIRNLIrDNRVVYGGGAAEI--SCALAVSQE 409
Cdd:PTZ00114 365 ierttseydkeklkerlaklsggvAVIKVGGASEVEVNEKKDRIEDALNATRAAV-EEGIVPGGGVALLraSKLLDKLEE 443
|
490 500 510
....*....|....*....|....*....|...
gi 194378060 410 ADKCPTLEQYAMRAFADALEVIPMALSENSGMN 442
Cdd:PTZ00114 444 DNELTPDQRTGVKIVRNALRLPTKQIAENAGVE 476
|
|
| groEL |
PRK12850 |
chaperonin GroEL; Reviewed |
18-329 |
3.41e-07 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237231 Cd Length: 544 Bit Score: 52.80 E-value: 3.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 18 IIKDQDRKSRLM-GLEALkshimaakavANTMRTSLGPNG----LDKMM----VDKDGdVTV------------------ 70
Cdd:PRK12850 6 IRFSTDARDRLLrGVNIL----------ANAVKVTLGPKGrnvvLEKSFgaprITKDG-VTVakeieledkfenmgaqmv 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 71 ------TNDEIGDGTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARVAIVHLDKISdsvlVDIKDTEPLIQTA-- 142
Cdd:PRK12850 75 kevaskTNDLAGDGTTTATVLAQAIVREGAKLVAAGMNPMDLKRGIDLAVAAVVDELKKIA----KKVTSSKEIAQVAti 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 143 ----KTTLGSKVVnschRQMAEIAVNAVLTVAdmERRDVDFELIKVEGKvggRLEDTKLIKGVIVDKDfshpQMPKKVED 218
Cdd:PRK12850 151 sangDESIGEMIA----EAMDKVGKEGVITVE--EAKTLGTELDVVEGM---QFDRGYLSPYFVTNPE----KMRAELED 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 219 AKIAIltcpfeppkpktkHKLDVTSVEDYKALqkyekekfeemIQQIKETGANLAICQWGFDDEANHLLLQNNL------ 292
Cdd:PRK12850 218 PYILL-------------HEKKISNLQDLLPI-----------LEAVVQSGRPLLIIAEDVEGEALATLVVNKLrgglks 273
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 194378060 293 PAVRWVG-----GPEIELIAIATGGRIVP-----RFSELTAEKLGFA 329
Cdd:PRK12850 274 VAVKAPGfgdrrKAMLEDIAVLTGGQVISedlgiKLENVTLDMLGRA 320
|
|
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
43-142 |
1.07e-05 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 48.20 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 43 AVANTMRTSLGPNG----LDKM----MVDKDGdVTV------------------------TNDEIGDGTTGVVVLAGALL 90
Cdd:PRK00013 21 KLADAVKVTLGPKGrnvvLEKSfgapTITKDG-VTVakeieledpfenmgaqlvkevaskTNDVAGDGTTTATVLAQAIV 99
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 194378060 91 EEAEQLLDRGIHPIRIADGYEQAARVAIVHLDKISdsvlVDIKDTEPLIQTA 142
Cdd:PRK00013 100 REGLKNVAAGANPMDLKRGIDKAVEAAVEELKKIS----KPVEDKEEIAQVA 147
|
|
| PLN03167 |
PLN03167 |
Chaperonin-60 beta subunit; Provisional |
71-186 |
1.69e-05 |
|
Chaperonin-60 beta subunit; Provisional
Pssm-ID: 215611 [Multi-domain] Cd Length: 600 Bit Score: 47.61 E-value: 1.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 71 TNDEIGDGTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARVAIVHLDKISDSVlvdiKDTEpLIQTAKTTLGS-- 148
Cdd:PLN03167 136 TNDLAGDGTTTSVVLAQGLIAEGVKVVAAGANPVQITRGIEKTAKALVKELKKMSKEV----EDSE-LADVAAVSAGNny 210
|
90 100 110
....*....|....*....|....*....|....*...
gi 194378060 149 KVVNSCHRQMAEIAVNAVLTVAdmERRDVDFELIKVEG 186
Cdd:PLN03167 211 EVGNMIAEAMSKVGRKGVVTLE--EGKSAENNLYVVEG 246
|
|
| groEL |
PRK12849 |
chaperonin GroEL; Reviewed |
43-340 |
2.68e-04 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237230 Cd Length: 542 Bit Score: 43.64 E-value: 2.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 43 AVANTMRTSLGPNG----LDKM----MVDKDGdVTV------------------------TNDEIGDGTTGVVVLAGALL 90
Cdd:PRK12849 21 KLADAVKVTLGPKGrnvvIDKSfgapTITKDG-VSIakeieledpfenlgaqlvkevaskTNDVAGDGTTTATVLAQALV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 91 EEAEQLLDRGIHPIRIADGYEQAARVAIVHLDKISdsvlVDIKDTEPLIQTAKT------TLGSKVVnschRQMAEIAVN 164
Cdd:PRK12849 100 QEGLKNVAAGANPMDLKRGIDKAVEAVVEELKALA----RPVSGSEEIAQVATIsangdeEIGELIA----EAMEKVGKD 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 165 AVLTVAdmERRDVDFELIKVEGkvggrledtklikgVIVDKDFSHPQM---PKK----VEDAKIAIltcpfeppkpkTKH 237
Cdd:PRK12849 172 GVITVE--ESKTLETELEVTEG--------------MQFDRGYLSPYFvtdPERmeavLEDPLILL-----------TDK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 238 KLdvTSVEDYKALqkyekekfeemIQQIKETGANLAICQWGFDDEANHLLLQN----NLPAVRwVGGPE--------IEL 305
Cdd:PRK12849 225 KI--SSLQDLLPL-----------LEKVAQSGKPLLIIAEDVEGEALATLVVNklrgGLKVAA-VKAPGfgdrrkamLED 290
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 194378060 306 IAIATGGRIVPR-----FSELTAEKLGFAGLVqEISFGTT 340
Cdd:PRK12849 291 IAILTGGTVISEdlglkLEEVTLDDLGRAKRV-TITKDNT 329
|
|
| groEL |
PRK12852 |
chaperonin GroEL; Reviewed |
44-186 |
3.97e-04 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237232 Cd Length: 545 Bit Score: 42.91 E-value: 3.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 44 VANTMRTSLGPNGLDKMM--------VDKDGdVTV------------------------TNDEIGDGTTGVVVLAGALLE 91
Cdd:PRK12852 23 LANAVKVTLGPKGRNVVIeksfgaprITKDG-VTVakeieledkfenmgaqmvrevaskTNDLAGDGTTTATVLAQAIVR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 92 EAEQLLDRGIHPIRIADGYEQAARVAIVHLDKISDSVL--VDIKDTEPLIQTAKTTLGSKVVNSchrqMAEIAVNAVLTV 169
Cdd:PRK12852 102 EGAKAVAAGMNPMDLKRGIDIAVAAVVKDIEKRAKPVAssAEIAQVGTISANGDAAIGKMIAQA----MQKVGNEGVITV 177
|
170
....*....|....*..
gi 194378060 170 ADMERRDVDFELikVEG 186
Cdd:PRK12852 178 EENKSLETEVDI--VEG 192
|
|
| PRK14104 |
PRK14104 |
chaperonin GroEL; Provisional |
30-186 |
6.74e-04 |
|
chaperonin GroEL; Provisional
Pssm-ID: 172594 Cd Length: 546 Bit Score: 42.32 E-value: 6.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 30 GLEALKSHIMAAKAVANTMRTSLGPNG----LDKMM----VDKDGdVTVTN------------------------DEIGD 77
Cdd:PRK14104 9 GVDARDRMLRGVDILANAVKVTLGPKGrnvvLDKSFgaprITKDG-VTVAKeieledkfenmgaqmvrevasksaDAAGD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 78 GTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARVAIVHLDKISDSVLV--DIKDTEPLIQTAKTTLGSKVVNSch 155
Cdd:PRK14104 88 GTTTATVLAQAIVREGAKSVAAGMNPMDLKRGIDLAVEAVVADLVKNSKKVTSndEIAQVGTISANGDAEIGKFLADA-- 165
|
170 180 190
....*....|....*....|....*....|.
gi 194378060 156 rqMAEIAVNAVLTVAdmERRDVDFELIKVEG 186
Cdd:PRK14104 166 --MKKVGNEGVITVE--EAKSLETELDVVEG 192
|
|
| groEL |
PRK12851 |
chaperonin GroEL; Reviewed |
41-186 |
2.55e-03 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 171770 Cd Length: 541 Bit Score: 40.50 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 41 AKAVANTMRTSLGPNG----LDKM----MVDKDGdVTV------------------------TNDEIGDGTTGVVVLAGA 88
Cdd:PRK12851 20 VNILADAVKVTLGPKGrnvvIDKSfgapTITNDG-VTIakeieledkfenmgaqmvrevaskTNDVAGDGTTTATVLAQA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194378060 89 LLEEAEQLLDRGIHPIRIADGYEQAARVAIVHLDKISDSVLV--DIKDTEPLIQTAKTTLGSKVVNSchrqMAEIAVNAV 166
Cdd:PRK12851 99 IVREGAKAVAAGANPMDLKRGIDRAVAAVVEELKANARPVTTnaEIAQVATISANGDAEIGRLVAEA----MEKVGNEGV 174
|
170 180
....*....|....*....|
gi 194378060 167 LTVAdmERRDVDFELIKVEG 186
Cdd:PRK12851 175 ITVE--ESKTAETELEVVEG 192
|
|
| groEL |
CHL00093 |
chaperonin GroEL |
71-147 |
4.39e-03 |
|
chaperonin GroEL
Pssm-ID: 177025 Cd Length: 529 Bit Score: 39.70 E-value: 4.39e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 194378060 71 TNDEIGDGTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARVAIVHLDKISDSvlvdIKDTEPLIQTAKTTLG 147
Cdd:CHL00093 80 TNDVAGDGTTTATVLAYAIVKQGMKNVAAGANPISLKRGIEKATQYVVSQIAEYARP----VEDIQAITQVASISAG 152
|
|
| |
