|
Name |
Accession |
Description |
Interval |
E-value |
| TCP1_epsilon |
cd03339 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ... |
10-535 |
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: 1103.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 10 DEYGRPFLIIKDQDRKSRLMGLEALKSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAK 89
Cdd:cd03339 1 DEYGRPFIIVREQEKKKRLKGLEAHKSHILAAKSVANILRTSLGPRGMDKILVSPDGEVTVTNDGATILEKMDVDHQIAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 90 LMVELSKSQDDEIGDGTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARVAIEHLDKISDSVLVDIKDTEPLIQTA 169
Cdd:cd03339 81 LLVELSKSQDDEIGDGTTGVVVLAGALLEQAEKLLDRGIHPIRIADGYEQACKIAVEHLEEIADKIEFSPDNKEPLIQTA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 170 KTTLGSKVVNSCHRQMAEIAVNAVLTVADMERRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKKVEDAKIA 249
Cdd:cd03339 161 MTSLGSKIVSRCHRQFAEIAVDAVLSVADLERKDVNFELIKVEGKVGGRLEDTKLVKGIVIDKDFSHPQMPKEVKDAKIA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 250 ILTCPFEPPKPKTKHKLDVTSVEDYKALQKYEKEKFEEMIQQIKETGANLAICQWGFDDEANHLLLQNNLPAVRWVGGPE 329
Cdd:cd03339 241 ILTCPFEPPKPKTKHKLDITSVEDYKKLQEYEQKYFREMVEQVKDAGANLVICQWGFDDEANHLLLQNGLPAVRWVGGVE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 330 IELIAIATGGRIVPRFSELTAEKLGFAGLVQEISFGTTKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVI 409
Cdd:cd03339 321 IELIAIATGGRIVPRFEDLSPEKLGKAGLVREISFGTTKDKMLVIEGCPNSKAVTIFIRGGNKMIIEEAKRSLHDALCVV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 410 RNLIRDNRVVYGGGAAEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKEMNPAL 489
Cdd:cd03339 401 RNLIRDNRIVYGGGAAEISCSLAVEKAADKCSGIEQYAMRAFADALESIPLALAENSGLNPIETLSEVKARQVKEKNPHL 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1996390960 490 GIDCLHKGTNDMKQQHVIETLIGKKQQISLATQMVRMILKIDDIRK 535
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 ... |
6-537 |
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: 1014.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 6 TLAFDEYGRPFLIIKDQDRKSRLMGLEALKSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDH 85
Cdd:TIGR02343 1 ILAFDEYGRPFIIIKDQDNKKRLKGLEAKKSNIAAAKSVASILRTSLGPKGMDKMLISPDGDITVTNDGATILSQMDVDN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 86 QIAKLMVELSKSQDDEIGDGTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARVAIEHLDKISDSVLVDIKDTEPL 165
Cdd:TIGR02343 81 QIAKLMVELSKSQDDEIGDGTTGVVVLAGALLEQAEELLDKGIHPIKIADGFEEAARIAVEHLEEISDEISADNNNREPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 166 IQTAKTTLGSKVVNSCHRQMAEIAVNAVLTVADMERRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKKVED 245
Cdd:TIGR02343 161 IQAAKTSLGSKIVSKCHRRFAEIAVDAVLNVADMERRDVDFDLIKVEGKVGGSLEDTKLIKGIIIDKDFSHPQMPKEVED 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 246 AKIAILTCPFEPPKPKTKHKLDVTSVEDYKALQKYEKEKFEEMIQQIKETGANLAICQWGFDDEANHLLLQNNLPAVRWV 325
Cdd:TIGR02343 241 AKIAILTCPFEPPKPKTKHKLDISSVEEYKKLQKYEQQKFKEMIDDIKKSGANLVICQWGFDDEANHLLLQNDLPAVRWV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 326 GGPEIELIAIATGGRIVPRFSELTAEKLGFAGLVQEISFGTTKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDA 405
Cdd:TIGR02343 321 GGQELELIAIATGGRIVPRFQELSKDKLGKAGLVREISFGTTKDRMLVIEQCKNSKAVTIFIRGGNKMIIEEAKRSIHDA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 406 LCVIRNLIRDNRVVYGGGAAEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKEM 485
Cdd:TIGR02343 401 LCVVRNLIKDSRIVYGGGAAEISCSLAVSQEADKYPGVEQYAIRAFADALETIPMALAENSGLDPIGTLSTLKSLQLKEK 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1996390960 486 NPALGIDCLHKGTNDMKQQHVIETLIGKKQQISLATQMVRMILKIDDIRKPG 537
Cdd:TIGR02343 481 NPNLGVDCLGYGTNDMKEQFVFETLIGKKQQILLATQLVRMILKIDDVISPG 532
|
|
| chaperonin_type_I_II |
cd00309 |
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ... |
25-533 |
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: 601.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 25 KSRLMGLEALKSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVELSKSQDDEIGD 104
Cdd:cd00309 1 KEREFGEEARLSNINAAKALADAVKTTLGPKGMDKMLVDSLGDPTITNDGATILKEIEVEHPAAKLLVEVAKSQDDEVGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 105 GTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARVAIEHLDKISDSvlVDIKDTEPLIQTAKTTLGSKVVNSCHRQ 184
Cdd:cd00309 81 GTTTVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVP--IDVEDREELLKVATTSLNSKLVSGGDDF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 185 MAEIAVNAVLTVADMErRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKKVEDAKIAILTCPFEPpkpktkh 264
Cdd:cd00309 159 LGELVVDAVLKVGKEN-GDVDLGVIRVEKKKGGSLEDSELVVGMVFDKGYLSPYMPKRLENAKILLLDCKLEY------- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 265 kldvtsvedykalqkyekekfeemiqqiketganLAICQWGFDDEANHLLLQNNLPAVRWVGGPEIELIAIATGGRIVPR 344
Cdd:cd00309 231 ----------------------------------VVIAEKGIDDEALHYLAKLGIMAVRRVRKEDLERIAKATGATIVSR 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 345 FSELTAEKLGFAGLVQEISFGttKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGA 424
Cdd:cd00309 277 LEDLTPEDLGTAGLVEETKIG--DEKYTFIEGCKGGKVATILLRGATEVELDEAERSLHDALCAVRAAVEDGGIVPGGGA 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 425 AEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKEMNPAlGIDCLHKGTNDMKQQ 504
Cdd:cd00309 355 AEIELSKALEELAKTLPGKEQLGIEAFADALEVIPRTLAENAGLDPIEVVTKLRAKHAEGGGNA-GGDVETGEIVDMKEA 433
|
490 500
....*....|....*....|....*....
gi 1996390960 505 HVIETLIGKKQQISLATQMVRMILKIDDI 533
Cdd:cd00309 434 GIIDPLKVKRQALKSATEAASLILTIDDI 462
|
|
| Cpn60_TCP1 |
pfam00118 |
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ... |
44-533 |
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: 561.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 44 VANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVVLAGALLEEAEQL 123
Cdd:pfam00118 1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELEIQHPAAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEEAEKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 124 LDRGIHPIRIADGYEQAARVAIEHLDKIsDSVLVDIKDTEPLIQTAKTTLGSKVVNSCHRQMAEIAVNAVLTVADMERrD 203
Cdd:pfam00118 81 LAAGVHPTTIIEGYEKALEKALEILDSI-ISIPVEDVDREDLLKVARTSLSSKIISRESDFLAKLVVDAVLAIPKNDG-S 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 204 VDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKKVEDAKIAILTCPFEPPKPKTKHKLDVTSVEDYKALQKYEKE 283
Cdd:pfam00118 159 FDLGNIGVVKILGGSLEDSELVDGVVLDKGPLHPDMPKRLENAKVLLLNCSLEYEKTETKATVVLSDAEQLERFLKAEEE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 284 KFEEMIQQIKETGANLAICQWGFDDEANHLLLQNNLPAVRWVGGPEIELIAIATGGRIVPRFSELTAEKLGFAGLVQEIS 363
Cdd:pfam00118 239 QILEIVEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMALRRVKKRDLERLAKATGARAVSSLDDLTPDDLGTAGKVEEEK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 364 FGttKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAEISCALAVSQEADKCPTL 443
Cdd:pfam00118 319 IG--DEKYTFIEGCKSPKAATILLRGATDHVLDEIERSIHDALCVVKNAIEDPRVVPGGGAVEMELARALREYAKSVSGK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 444 EQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKEmNPALGIDCLHKGTNDMKQQHVIETLIGKKQQISLATQM 523
Cdd:pfam00118 397 EQLAIEAFAEALEVIPKTLAENAGLDPIEVLAELRAAHASG-EKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKSATEA 475
|
490
....*....|
gi 1996390960 524 VRMILKIDDI 533
Cdd:pfam00118 476 ASTILRIDDI 485
|
|
| thermosome_alpha |
NF041082 |
thermosome subunit alpha; |
15-533 |
0e+00 |
|
thermosome subunit alpha;
Pssm-ID: 469009 Cd Length: 518 Bit Score: 550.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 15 PFLIIKDQdrKSRLMGLEALKSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVEL 94
Cdd:NF041082 2 PILILKEG--TQRTSGRDAQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDVVITNDGVTILKEMDIEHPAAKMIVEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 95 SKSQDDEIGDGTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARVAIEHLDKIsdSVLVDIKDTEPLIQTAKTTLG 174
Cdd:NF041082 80 AKTQDDEVGDGTTTAVVLAGELLKKAEELLDQDIHPTIIAEGYRLAAEKALEILDEI--AIKVDPDDKETLKKIAATAMT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 175 SKVVNSCHRQMAEIAVNAVLTVADME-RRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKKVEDAKIAILTC 253
Cdd:NF041082 158 GKGAEAAKDKLADLVVDAVKAVAEKDgGYNVDLDNIKVEKKVGGSIEDSELVEGVVIDKERVHPGMPKRVENAKIALLDA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 254 PFEPPKPKTKHKLDVTSVEDYKALQKYEKEKFEEMIQQIKETGANLAICQWGFDDEANHLLLQNNLPAVRWVGGPEIELI 333
Cdd:NF041082 238 PLEVKKTEIDAKISITDPDQLQAFLDQEEKMLKEMVDKIADSGANVVFCQKGIDDLAQHYLAKEGILAVRRVKKSDMEKL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 334 AIATGGRIVPRFSELTAEKLGFAGLVQEISFGttKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLI 413
Cdd:NF041082 318 AKATGARIVTSIDDLSPEDLGYAGLVEERKVG--GDKMIFVEGCKNPKAVTILLRGGTEHVVDEVERALEDALRVVRVVL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 414 RDNRVVYGGGAAEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKEMNPAlGIDC 493
Cdd:NF041082 396 EDGKVVAGGGAPEVELALRLREYAASVGGREQLAIEAFAEALEIIPRTLAENAGLDPIDALVELRSAHEKGNKTA-GLDV 474
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1996390960 494 LHKGTNDMKQQHVIETLIGKKQQISLATQMVRMILKIDDI 533
Cdd:NF041082 475 YTGKVVDMLEIGVVEPLRVKTQAIKSATEAAVMILRIDDV 514
|
|
| thermosome_beta |
NF041083 |
thermosome subunit beta; |
15-533 |
0e+00 |
|
thermosome subunit beta;
Pssm-ID: 469010 Cd Length: 519 Bit Score: 536.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 15 PFLIIKDQdrKSRLMGLEALKSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVEL 94
Cdd:NF041083 2 PVLILKEG--TQRTKGRDAQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDIVITNDGATILKEMDVQHPAAKMLVEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 95 SKSQDDEIGDGTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARVAIEHLDKISDSvlVDIKDTEPLIQTAKTTLG 174
Cdd:NF041083 80 AKTQDDEVGDGTTTAVVLAGELLKKAEELLDQNIHPTIIANGYRLAAEKAIEILDEIAEK--VDPDDRETLKKIAETSLT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 175 SKVVNSCHRQMAEIAVNAVLTVAdmERRD----VDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKKVEDAKIAI 250
Cdd:NF041083 158 SKGVEEARDYLAEIAVKAVKQVA--EKRDgkyyVDLDNIQIEKKHGGSIEDTQLIYGIVIDKEVVHPGMPKRVENAKIAL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 251 LTCPFEPPKPKTKHKLDVTSVEDYKALQKYEKEKFEEMIQQIKETGANLAICQWGFDDEANHLLLQNNLPAVRWVGGPEI 330
Cdd:NF041083 236 LDAPLEVKKTEIDAEIRITDPDQLQKFLDQEEKMLKEMVDKIKATGANVVFCQKGIDDLAQHYLAKAGILAVRRVKKSDM 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 331 ELIAIATGGRIVPRFSELTAEKLGFAGLVQEISFGTtkDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIR 410
Cdd:NF041083 316 EKLAKATGARIVTNIDDLTPEDLGYAELVEERKVGD--DKMVFVEGCKNPKAVTILIRGGTEHVVDEAERALEDALSVVA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 411 NLIRDNRVVYGGGAAEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKEmNPALG 490
Cdd:NF041083 394 DAVEDGKIVAGGGAPEVELAKRLREYAATVGGREQLAVEAFAEALEIIPRTLAENAGLDPIDILVKLRSAHEKG-KKWAG 472
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1996390960 491 IDCLHKGTNDMKQQHVIETLIGKKQQISLATQMVRMILKIDDI 533
Cdd:NF041083 473 INVFTGEVVDMWELGVIEPLRVKTQAIKSATEAATMILRIDDV 515
|
|
| cpn60 |
cd03343 |
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ... |
17-533 |
0e+00 |
|
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: 535.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 17 LIIKDqdRKSRLMGLEALKSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVELSK 96
Cdd:cd03343 2 LILKE--GTQRTSGRDAQRMNIAAAKAVAEAVRTTLGPKGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 97 SQDDEIGDGTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARVAIEHLDKISDSvlVDIKDTEPLIQTAKTTLGSK 176
Cdd:cd03343 80 TQDEEVGDGTTTAVVLAGELLEKAEDLLDQNIHPTVIIEGYRLAAEKALELLDEIAIK--VDPDDKDTLRKIAKTSLTGK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 177 VVNSCHRQMAEIAVNAVLTVADME--RRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKKVEDAKIAILTCP 254
Cdd:cd03343 158 GAEAAKDKLADLVVDAVLQVAEKRdgKYVVDLDNIKIEKKTGGSVDDTELIRGIVIDKEVVHPGMPKRVENAKIALLDAP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 255 FEPPKPKTKHKLDVTSVEDYKALQKYEKEKFEEMIQQIKETGANLAICQWGFDDEANHLLLQNNLPAVRWVGGPEIELIA 334
Cdd:cd03343 238 LEVKKTEIDAKIRITSPDQLQAFLEQEEAMLKEMVDKIADTGANVVFCQKGIDDLAQHYLAKAGILAVRRVKKSDMEKLA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 335 IATGGRIVPRFSELTAEKLGFAGLVQEISFGttKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIR 414
Cdd:cd03343 318 RATGAKIVTNIDDLTPEDLGEAELVEERKVG--DDKMVFVEGCKNPKAVTILLRGGTEHVVDELERALEDALRVVADALE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 415 DNRVVYGGGAAEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKEMNPAlGIDCL 494
Cdd:cd03343 396 DGKVVAGGGAVEIELAKRLREYARSVGGREQLAVEAFADALEEIPRTLAENAGLDPIDTLVELRAAHEKGNKNA-GLDVY 474
|
490 500 510
....*....|....*....|....*....|....*....
gi 1996390960 495 HKGTNDMKQQHVIETLIGKKQQISLATQMVRMILKIDDI 533
Cdd:cd03343 475 TGEVVDMLEKGVIEPLRVKKQAIKSATEAATMILRIDDV 513
|
|
| thermosome_arch |
TIGR02339 |
thermosome, various subunits, archaeal; Thermosome is the name given to the archaeal rather ... |
15-533 |
3.95e-176 |
|
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: 506.92 E-value: 3.95e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 15 PFLIIKDQdrKSRLMGLEALKSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVEL 94
Cdd:TIGR02339 1 PVFILKEG--TQRTSGRDAQRNNIAAAKAVAEAVKSTLGPRGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 95 SKSQDDEIGDGTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARVAIEHLDKISDSvlVDIKDTEPLIQTAKTTLG 174
Cdd:TIGR02339 79 AKTQDEEVGDGTTTAVVLAGELLEKAEDLLEQDIHPTVIIEGYRKAAEKALEIIDEIATK--ISPEDRDLLKKIAYTSLT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 175 SKVVNSCHRQ-MAEIAVNAVLTVADME---RRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKKVEDAKIAI 250
Cdd:TIGR02339 157 SKASAEVAKDkLADLVVEAVKQVAELRgdgKYYVDLDNIKIVKKKGGSIEDTELVEGIVVDKEVVHPGMPKRVENAKIAL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 251 LTCPFEPPKPKTKHKLDVTSVEDYKALQKYEKEKFEEMIQQIKETGANLAICQWGFDDEANHLLLQNNLPAVRWVGGPEI 330
Cdd:TIGR02339 237 LDAPLEVEKTEIDAKIRITDPDQIKKFLDQEEAMLKEMVDKIASAGANVVICQKGIDDVAQHYLAKAGILAVRRVKKSDI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 331 ELIAIATGGRIVPRFSELTAEKLGFAGLVQEISFGttKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIR 410
Cdd:TIGR02339 317 EKLARATGARIVSSIDEITESDLGYAELVEERKVG--EDKMVFVEGCKNPKAVTILLRGGTEHVVDELERSIQDALHVVA 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 411 NLIRDNRVVYGGGAAEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKEmNPALG 490
Cdd:TIGR02339 395 NALEDGKIVAGGGAVEIELALRLRSYARSVGGREQLAIEAFADALEEIPRILAENAGLDPIDALVDLRAKHEKG-NKNAG 473
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1996390960 491 IDCLHKGTNDMKQQHVIETLIGKKQQISLATQMVRMILKIDDI 533
Cdd:TIGR02339 474 INVFTGEIEDMLELGVIEPLRVKEQAIKSATEAATMILRIDDV 516
|
|
| TCP1_delta |
cd03338 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ... |
35-533 |
4.53e-154 |
|
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: 450.59 E-value: 4.53e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 35 KSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVVLAG 114
Cdd:cd03338 11 LSNIQAAKAVADAIRTSLGPRGMDKMIQTGKGEVIITNDGATILKQMSVLHPAAKMLVELSKAQDIEAGDGTTSVVVLAG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 115 ALLEEAEQLLDRGIHPIRIADGYEQAARVAIEHLDKIsdSVLVDIKDTEPLIQTAKTTLGSKVVNSCHRQMAEIAVNAVL 194
Cdd:cd03338 91 ALLSACESLLKKGIHPTVISESFQIAAKKAVEILDSM--SIPVDLNDRESLIKSATTSLNSKVVSQYSSLLAPIAVDAVL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 195 TVADMER-RDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSH-PQMPKKVEDAKIAILTCPFEPPKPKTKHKLdvtSVE 272
Cdd:cd03338 169 KVIDPATaTNVDLKDIRIVKKLGGTIEDTELVDGLVFTQKASKkAGGPTRIEKAKIGLIQFCLSPPKTDMDNNI---VVN 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 273 DYKA---LQKYEKEKFEEMIQQIKETGANLAICQW-----GFDDEANHLLLQNNLPAVRWVGGPEIELIAIATGGRIVPR 344
Cdd:cd03338 246 DYAQmdrILREERKYILNMCKKIKKSGCNVLLIQKsilrdAVSDLALHFLAKLKIMVVKDIEREEIEFICKTIGCKPVAS 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 345 FSELTAEKLGFAGLVQEISFGTtkDKMLVIEQCKNS-RAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGG 423
Cdd:cd03338 326 IDHFTEDKLGSADLVEEVSLGD--GKIVKITGVKNPgKTVTILVRGSNKLVLDEAERSLHDALCVIRCLVKKRALIPGGG 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 424 AAEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVK-EMNpaLGIDCLHKGTNDMK 502
Cdd:cd03338 404 APEIEIALQLSEWARTLTGVEQYCVRAFADALEVIPYTLAENAGLNPISIVTELRNRHAQgEKN--AGINVRKGAITNIL 481
|
490 500 510
....*....|....*....|....*....|.
gi 1996390960 503 QQHVIETLIGKKQQISLATQMVRMILKIDDI 533
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 ... |
35-533 |
1.66e-141 |
|
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: 418.42 E-value: 1.66e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 35 KSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVVLAG 114
Cdd:TIGR02342 12 TSNIVAAKAVADAIRTSLGPKGMDKMIQDGKGEVIITNDGATILKQMAVLHPAAKMLVELSKAQDIEAGDGTTSVVILAG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 115 ALLEEAEQLLDRGIHPIRIADGYEQAARVAIEHLDKISDSvlVDIKDTEPLIQTAKTTLGSKVVNSCHRQMAEIAVNAVL 194
Cdd:TIGR02342 92 ALLGACERLLNKGIHPTIISESFQSAADEAIKILDEMSIP--VDLSDREQLLKSATTSLSSKVVSQYSSLLAPLAVDAVL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 195 TVADMER-RDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQ-MPKKVEDAKIAILTCPFEPPKPKTKHKLDVTSVE 272
Cdd:TIGR02342 170 KVIDPENaKNVDLNDIKVVKKLGGTIDDTELIEGLVFTQKASKSAgGPTRIEKAKIGLIQFQISPPKTDMENQIIVNDYA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 273 DYKALQKYEKEKFEEMIQQIKETGANLAICQW-----GFDDEANHLLLQNNLPAVRWVGGPEIELIAIATGGRIVPRFSE 347
Cdd:TIGR02342 250 QMDRVLKEERAYILNIVKKIKKTGCNVLLIQKsilrdAVNDLALHFLAKMKIMVVKDIEREEIEFICKTIGCKPIASIDH 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 348 LTAEKLGFAGLVQEIsfGTTKDKMLVIEQCKN-SRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAE 426
Cdd:TIGR02342 330 FTADKLGSAELVEEV--DSDGGKIIKITGIQNaGKTVTVVVRGSNKLVIDEAERSLHDALCVIRCLVKKRGLIAGGGAPE 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 427 ISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVK-EMNpaLGIDCLHKGTNDMKQQH 505
Cdd:TIGR02342 408 IEIARRLSKYARTMKGVESYCVRAFADALEVIPYTLAENAGLNPIKVVTELRNRHANgEKT--AGISVRKGGITNMLEEH 485
|
490 500
....*....|....*....|....*...
gi 1996390960 506 VIETLIGKKQQISLATQMVRMILKIDDI 533
Cdd:TIGR02342 486 VLQPLLVTTSAITLASETVRSILKIDDI 513
|
|
| GroEL |
COG0459 |
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ... |
25-533 |
1.74e-127 |
|
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227 Cd Length: 497 Bit Score: 381.73 E-value: 1.74e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 25 KSRLMGLEALKSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQI----AKLMVELSKSQDD 100
Cdd:COG0459 3 KQILFGEDARRANIRGVKALADAVKVTLGPKGRNVMLVKSFGDPTITNDGVTIAKEIELEDPFenmgAQLVKEVASKTND 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 101 EIGDGTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARVAIEHLDKISdsvlVDIKDTEPLIQTAKTTLGSKvvns 180
Cdd:COG0459 83 EAGDGTTTATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIA----KPVDDKEELAQVATISANGD---- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 181 chRQMAEIAVNAVLTVADMERrdvdfelIKVEgKVGGRLEDTKLIKGVIVDKDFSHPQ-------MPKKVEDAKIAILTC 253
Cdd:COG0459 155 --EEIGELIAEAMEKVGKDGV-------ITVE-EGKGLETELEVVEGMQFDKGYLSPYfvtdpekMPAELENAYILLTDK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 254 PFEPPKPktkhkldvtsvedykalqkyekekFEEMIQQIKETGANLAICQWGFDDEANHLLLQNNLPAVR---WVGGP-- 328
Cdd:COG0459 225 KISSIQD------------------------LLPLLEKVAQSGKPLLIIAEDIDGEALATLVVNGIRGVLrvvAVKAPgf 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 329 ------EIELIAIATGGRIV-----PRFSELTAEKLGFAGLVQEisfgtTKDKMLVIEQCKNSRAVTIFIRGGNKMIIEE 397
Cdd:COG0459 281 gdrrkaMLEDIAILTGGRVIsedlgLKLEDVTLDDLGRAKRVEV-----DKDNTTIVEGAGNPKAIVILVGAATEVEVKE 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 398 AKRSLHDALCVIRNLIRDnRVVYGGGAAEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEV 477
Cdd:COG0459 356 RKRRVEDALHATRAAVEE-GIVPGGGAALLRAARALRELAAKLEGDEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKV 434
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1996390960 478 RARQvkemNPALGIDCLHKGTNDMKQQHVIETLIGKKQQISLATQMVRMILKIDDI 533
Cdd:COG0459 435 RAAK----DKGFGFDAATGEYVDMLEAGVIDPAKVKRSALQNAASVAGLILTTEAV 486
|
|
| TCP1_gamma |
cd03337 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ... |
20-533 |
6.91e-125 |
|
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: 374.32 E-value: 6.91e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 20 KDQDRKSRLmglealkSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVELSKSQD 99
Cdd:cd03337 11 RESGRKAQL-------GNIQAAKTVADVIRTCLGPRAMLKMLLDPMGGIVLTNDGNAILREIDVAHPAAKSMIELSRTQD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 100 DEIGDGTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARVAIEHLDKISDSvlVDIKDTEPLIQTAKTTLGSKVVN 179
Cdd:cd03337 84 EEVGDGTTSVIILAGEILAVAEPFLERGIHPTVIIKAYRKALEDALKILEEISIP--VDVNDRAQMLKIIKSCIGTKFVS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 180 SCHRQMAEIAVNAVLTVA---DMERRDVDFE-LIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKKVEDAKIAILTCPF 255
Cdd:cd03337 162 RWSDLMCNLALDAVKTVAveeNGRKKEIDIKrYAKVEKIPGGEIEDSRVLDGVMLNKDVTHPKMRRRIENPRIVLLDCPL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 256 EppkpktkhkldvtsvedYkalqkyekekfeemiqqiketganLAICQWGFDDEANHLLLQNNLPAVRWVGGPEIELIAI 335
Cdd:cd03337 242 E-----------------Y------------------------LVITEKGVSDLAQHYLVKAGITALRRVRKTDNNRIAR 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 336 ATGGRIVPRFSELTAEKLGFAGLVQEISFGtTKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRD 415
Cdd:cd03337 281 ACGATIVNRPEELTESDVGTGAGLFEVKKI-GDEYFTFITECKDPKACTILLRGASKDVLNEVERNLQDAMAVARNIILN 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 416 NRVVYGGGAAEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKEMNPALGIDCLH 495
Cdd:cd03337 360 PKLVPGGGATEMAVSHALSEKAKSIEGVEQWPYKAVASALEVIPRTLAQNCGANVIRTLTELRAKHAQGENSTWGIDGET 439
|
490 500 510
....*....|....*....|....*....|....*...
gi 1996390960 496 KGTNDMKQQHVIETLIGKKQQISLATQMVRMILKIDDI 533
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 ... |
15-533 |
3.50e-119 |
|
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: 361.36 E-value: 3.50e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 15 PFLIIKDQDRksRLMGLEALKSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVEL 94
Cdd:TIGR02344 1 PVLVLNQNTK--RESGRKAQLSNIQAAKAVADIIRTCLGPRSMLKMLLDPMGGIVMTNDGNAILREIDVAHPAAKSMIEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 95 SKSQDDEIGDGTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARVAIEHLDKIsdSVLVDIKDTEPLIQTAKTTLG 174
Cdd:TIGR02344 79 SRTQDEEVGDGTTSVIILAGEMLSVAEPFLEQNIHPTVIIRAYRKALDDALSVLEEI--SIPVDVNDDAAMLKLIQSCIG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 175 SKVVNSCHRQMAEIAVNAVLTVA--DMERRDVDFE-LIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKKVEDAKIAIL 251
Cdd:TIGR02344 157 TKFVSRWSDLMCDLALDAVRTVQrdENGRKEIDIKrYAKVEKIPGGDIEDSCVLKGVMINKDVTHPKMRRYIENPRIVLL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 252 TCPFEPPKPKTKHKLDVTSVEDYKALQKYEKEKFEEMIQQIKETGANLAICQWGFDDEANHLLLQNNLPAVRWVGGPEIE 331
Cdd:TIGR02344 237 DCPLEYKKGESQTNIEITKEEDWNRILQMEEEYVQLMCEDIIAVKPDLVITEKGVSDLAQHYLLKANITAIRRVRKTDNN 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 332 LIAIATGGRIVPRFSELTAEKLGF-AGLVQEISFGttKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIR 410
Cdd:TIGR02344 317 RIARACGATIVNRPEELRESDVGTgCGLFEVKKIG--DEYFTFITECKDPKACTILLRGASKDILNEVERNLQDAMAVAR 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 411 NLIRDNRVVYGGGAAEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKEMNPALG 490
Cdd:TIGR02344 395 NVLLDPKLVPGGGATEMAVSVALTEKSKKLEGVEQWPYRAVADALEIIPRTLAQNCGANVIRTLTELRAKHAQENNCTWG 474
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1996390960 491 IDCLHKGTNDMKQQHVIETLIGKKQQISLATQMVRMILKIDDI 533
Cdd:TIGR02344 475 IDGETGKIVDMKEKGIWEPLAVKLQTYKTAIESACLLLRIDDI 517
|
|
| TCP1_beta |
cd03336 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ... |
18-535 |
6.28e-112 |
|
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: 342.39 E-value: 6.28e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 18 IIKDQDRKSRlmGLEALKSHIMAAKAVANTMRTSLGPNGLDKMM--VDKDGDVTVTNDGATILSMMDVDHQIAKLMVELS 95
Cdd:cd03336 1 ILKDGAQEEK--GETARLSSFVGAIAIGDLVKTTLGPKGMDKILqsVGRSGGVTVTNDGATILKSIGVDNPAAKVLVDIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 96 KSQDDEIGDGTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARVAIEHLDKISDSVLVDIKDT-EPLIQTAKTTLG 174
Cdd:cd03336 79 KVQDDEVGDGTTSVTVLAAELLREAEKLVAQKIHPQTIIEGYRMATAAAREALLSSAVDHSSDEEAFrEDLLNIARTTLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 175 SKVVNSCHRQMAEIAVNAVLTVADmerrDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQmPKKVEDAKIAILTCP 254
Cdd:cd03336 159 SKILTQDKEHFAELAVDAVLRLKG----SGNLDAIQIIKKLGGSLKDSYLDEGFLLDKKIGVNQ-PKRIENAKILIANTP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 255 FEPPKPKT-KHKLDVTSVEDYKALQKYEKEKFEEMIQQIKETGANLAICQWGFDDEANHLLLQNNLPAVRWVGGPEIELI 333
Cdd:cd03336 234 MDTDKIKIfGAKVRVDSTAKVAEIEEAEKEKMKNKVEKILKHGINCFINRQLIYNYPEQLFADAGIMAIEHADFDGVERL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 334 AIATGGRIVPRFSELTAEKLGFAGLVQEISFGttKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLI 413
Cdd:cd03336 314 ALVTGGEIASTFDHPELVKLGTCKLIEEIMIG--EDKLIRFSGVAAGEACTIVLRGASQQILDEAERSLHDALCVLAQTV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 414 RDNRVVYGGGAAEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKEMNPAlGIDC 493
Cdd:cd03336 392 KDTRVVLGGGCSEMLMAKAVEELAKKTPGKKSLAIEAFAKALRQLPTIIADNAGYDSAELVAQLRAAHYNGNTTA-GLDM 470
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1996390960 494 LHKGTNDMKQQHVIETLIGKKQQISLATQMVRMILKIDDIRK 535
Cdd:cd03336 471 RKGTVGDMKELGITESFKVKRQVLLSASEAAEMILRVDDIIK 512
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
36-533 |
1.38e-110 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 339.70 E-value: 1.38e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 36 SHIMAAKAVANTMRTSLGPNGLDKMMV-----DKDGDVTVTNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVV 110
Cdd:PTZ00212 26 QSFVGAIAVADLVKTTLGPKGMDKILQpmsegPRSGNVTVTNDGATILKSVWLDNPAAKILVDISKTQDEEVGDGTTSVV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 111 VLAGALLEEAEQLLDRGIHPIRIADGYEQAARVAIEHLDKISDSVLVDIKD-TEPLIQTAKTTLGSKVVNSCHRQMAEIA 189
Cdd:PTZ00212 106 VLAGELLREAEKLLDQKIHPQTIIEGWRMALDVARKALEEIAFDHGSDEEKfKEDLLNIARTTLSSKLLTVEKDHFAKLA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 190 VNAVLTVadmeRRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQmPKKVEDAKIAILTCPFEPPKPKT-KHKLDV 268
Cdd:PTZ00212 186 VDAVLRL----KGSGNLDYIQIIKKPGGTLRDSYLEDGFILEKKIGVGQ-PKRLENCKILVANTPMDTDKIKIyGAKVKV 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 269 TSVEDYKALQKYEKEKFEEMIQQIKETGANLAICQWGFDDEANHLLLQNNLPAVRWVGGPEIELIAIATGGRIVPRFSEL 348
Cdd:PTZ00212 261 DSMEKVAEIEAAEKEKMKNKVDKILAHGCNVFINRQLIYNYPEQLFAEAGIMAIEHADFDGMERLAAALGAEIVSTFDTP 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 349 TAEKLGFAGLVQEISFGttKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAEIS 428
Cdd:PTZ00212 341 EKVKLGHCDLIEEIMIG--EDKLIRFSGCAKGEACTIVLRGASTHILDEAERSLHDALCVLSQTVKDTRVVLGGGCSEML 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 429 CALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKEMNPAlGIDCLHKGTNDMKQQHVIE 508
Cdd:PTZ00212 419 MANAVEELAKKVEGKKSLAIEAFAKALRQIPTIIADNGGYDSAELVSKLRAEHYKGNKTA-GIDMEKGTVGDMKELGITE 497
|
490 500
....*....|....*....|....*
gi 1996390960 509 TLIGKKQQISLATQMVRMILKIDDI 533
Cdd:PTZ00212 498 SYKVKLSQLCSATEAAEMILRVDDI 522
|
|
| TCP1_eta |
cd03340 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ... |
15-531 |
1.15e-108 |
|
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: 334.26 E-value: 1.15e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 15 PFLIIKDQDRKSRlmGLEALKSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVEL 94
Cdd:cd03340 1 PIILLKEGTDTSQ--GKGQLISNINACQAIADAVRTTLGPRGMDKLIVDGRGKVTISNDGATILKLLDIVHPAAKTLVDI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 95 SKSQDDEIGDGTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARVAIEHLDKIsdSVLVDIKDTEP----LIQTAK 170
Cdd:cd03340 79 AKSQDAEVGDGTTSVVVLAGEFLKEAKPFIEDGVHPQIIIRGYRKALQLAIEKIKEI--AVNIDKEDKEEqrelLEKCAA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 171 TTLGSKVVNSCHRQMAEIAVNAVLTVADmerrDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFS---HPQMPKKVEDAK 247
Cdd:cd03340 157 TALNSKLIASEKEFFAKMVVDAVLSLDD----DLDLDMIGIKKVPGGSLEDSQLVNGVAFKKTFSyagFEQQPKKFKNPK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 248 IAILTCPFEPPKPKTKHKLDVTSVEDYKALQKYEKEKFEEMIQQIKETGANLAICQWGFDDEANHLLLQNNLPAVRWVGG 327
Cdd:cd03340 233 ILLLNVELELKAEKDNAEVRVEDPEEYQAIVDAEWKIIYDKLEKIVKSGANVVLSKLPIGDLATQYFADRDIFCAGRVPE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 328 PEIELIAIATGGRIVPRFSELTAEKLGFAGLVQEISFGttKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALC 407
Cdd:cd03340 313 EDLKRVAQATGGSIQTTVSNITDDVLGTCGLFEERQVG--GERYNIFTGCPKAKTCTIILRGGAEQFIEEAERSLHDAIM 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 408 VIRNLIRDNRVVYGGGAAEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKEMNP 487
Cdd:cd03340 391 IVRRAIKNDSVVAGGGAIEMELSKYLRDYSRTIAGKQQLVINAFAKALEIIPRQLCDNAGFDATDILNKLRQKHAQGGGK 470
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1996390960 488 ALGIDCLHKGTNDMKQQHVIETLIGKKQQISLATQMVRMILKID 531
Cdd:cd03340 471 WYGVDINNEGIADNFEAFVWEPSLVKINALTAATEAACLILSVD 514
|
|
| TCP1_alpha |
cd03335 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ... |
27-535 |
4.24e-106 |
|
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: 327.70 E-value: 4.24e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 27 RLMGLEALKSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGT 106
Cdd:cd03335 3 RTSGQDVRTQNVTAAMAIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDKEVGDGT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 107 TGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARVAIEHLDKiSDSVLVDIKDTEPLIQTAKTTLGSKVVNSCHRQMA 186
Cdd:cd03335 83 TSVVIIAAELLKRANELVKQKIHPTTIISGYRLACKEAVKYIKE-HLSISVDNLGKESLINVAKTSMSSKIIGADSDFFA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 187 EIAVNAVLTVADM-ERRDV-----DFELIKVEGKvggRLEDTKLIKGVIVDKDFSHPQMPKKVEDAKIAILTCPFEppkp 260
Cdd:cd03335 162 NMVVDAILAVKTTnEKGKTkypikAVNILKAHGK---SAKESYLVNGYALNCTRASQGMPTRVKNAKIACLDFNLQ---- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 261 KTKHKLDV----TSVEDYKALQKYEKEKFEEMIQQIKETGANLAICQWGFDDEANHLLLQNNLPAVRWVGGPEIELIAIA 336
Cdd:cd03335 235 KTKMKLGVqvvvTDPEKLEKIRQRESDITKERIKKILAAGANVVLTTGGIDDMCLKYFVEAGAMAVRRVKKEDLRRIAKA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 337 TGGRIVPRFSELTAE------KLGFAGLVQEISFGttKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIR 410
Cdd:cd03335 315 TGATLVSTLANLEGEetfdpsYLGEAEEVVQERIG--DDELILIKGTKKRSSASIILRGANDFMLDEMERSLHDALCVVK 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 411 NLIRDNRVVYGGGAAEisCALAVSQE--ADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKEMNPA 488
Cdd:cd03335 393 RTLESNSVVPGGGAVE--TALSIYLEnfATTLGSREQLAIAEFAEALLVIPKTLAVNAAKDATELVAKLRAYHAAAQVKP 470
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1996390960 489 -------LGIDcLHKGT-NDMKQQHVIETLIGKKQQISLATQMVRMILKIDDIRK 535
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 ... |
15-537 |
2.49e-104 |
|
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: 323.25 E-value: 2.49e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 15 PFLIIKDQDRKSRlmGLEALKSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVEL 94
Cdd:TIGR02345 3 TIVLLKEGTDTSQ--GKGQLISNINACVAIAEALKTTLGPRGMDKLIVGSNGKATISNDGATILKLLDIVHPAAKTLVDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 95 SKSQDDEIGDGTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARVAIEHLDKISDSV-LVDIKDTEPLIQTAKTTL 173
Cdd:TIGR02345 81 AKSQDAEVGDGTTSVTILAGELLKEAKPFIEEGVHPQLIIRCYREALSLAVEKIKEIAVTIdEEKGEQRELLEKCAATAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 174 GSKVVNSCHRQMAEIAVNAVLTvadMERRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFS---HPQMPKKVEDAKIAI 250
Cdd:TIGR02345 161 SSKLISHNKEFFSKMIVDAVLS---LDRDDLDLKLIGIKKVQGGALEDSQLVNGVAFKKTFSyagFEQQPKKFANPKILL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 251 LTCPFEPPKPKTKHKLDVTSVEDYKALQKYEKEKFEEMIQQIKETGANLAICQWGFDDEANHLLLQNNLPAVRWVGGPEI 330
Cdd:TIGR02345 238 LNVELELKAEKDNAEIRVEDVEDYQAIVDAEWAIIFRKLEKIVESGANVVLSKLPIGDLATQYFADRDIFCAGRVSAEDL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 331 ELIAIATGGRIVPRFSELTAEKLGFAGLVQEISFGttKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIR 410
Cdd:TIGR02345 318 KRVIKACGGSIQSTTSDLEADVLGTCALFEERQIG--SERYNYFTGCPHAKTCTIILRGGAEQFIEEAERSLHDAIMIVR 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 411 NLIRDNRVVYGGGAAEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKEmNPALG 490
Cdd:TIGR02345 396 RALKNKKIVAGGGAIEMELSKCLRDYSKTIDGKQQLIINAFAKALEIIPRQLCENAGFDSIEILNKLRSRHAKG-GKWYG 474
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1996390960 491 IDCLHKGTNDMKQQHVIETLIGKKQQISLATQMVRMILKIDD-IRKPG 537
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 ... |
27-541 |
1.75e-103 |
|
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: 321.28 E-value: 1.75e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 27 RLMGLEALKSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGT 106
Cdd:TIGR02340 7 RTSGQDVRTQNVTAAMAIANIVKTSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDREVGDGT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 107 TGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARVAIEHLDKiSDSVLVDIKDTEPLIQTAKTTLGSKVVNSCHRQMA 186
Cdd:TIGR02340 87 TSVVIIAAELLKRADELVKNKIHPTSVISGYRLACKEAVKYIKE-NLSVSVDELGREALINVAKTSMSSKIIGLDSDFFS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 187 EIAVNAVLTVADM-ERRDVDF--ELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKKVEDAKIAILTCPFEppkpKTK 263
Cdd:TIGR02340 166 NIVVDAVLAVKTTnENGETKYpiKAINILKAHGKSARESMLVKGYALNCTVASQQMPKRIKNAKIACLDFNLQ----KAK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 264 HKLDVT-SVEDYKALQKYEKEKFE---EMIQQIKETGANLAICQWGFDDEANHLLLQNNLPAVRWVGGPEIELIAIATGG 339
Cdd:TIGR02340 242 MALGVQiVVDDPEKLEQIRQREADitkERIKKILDAGANVVLTTGGIDDMCLKYFVEAGAMGVRRCKKEDLKRIAKATGA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 340 RIVPRFSELTAE------KLGFAGLVQEISFGttKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLI 413
Cdd:TIGR02340 322 TLVSTLADLEGEetfeasYLGFADEVVQERIA--DDECILIKGTKKRKSASIILRGANDFMLDEMERSLHDALCVVKRTL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 414 RDNRVVYGGGAAEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKEM-NPA---- 488
Cdd:TIGR02340 400 ESNSVVPGGGAVEAALSIYLENFATTLGSREQLAIAEFARALLIIPKTLAVNAAKDSTELVAKLRAYHAAAQlKPEkkhl 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1996390960 489 --LGIDCLHKGTNDMKQQHVIETLIGKKQQISLATQMVRMILKIDD-IRKPGESEE 541
Cdd:TIGR02340 480 kwYGLDLVNGKIRDNKEAGVLEPTVSKVKSLKFATEAAITILRIDDlIKLNPEQSK 535
|
|
| TCP1_theta |
cd03341 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ... |
32-533 |
9.83e-103 |
|
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: 317.24 E-value: 9.83e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 32 EALKSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVV 111
Cdd:cd03341 8 EAVLRNIEACKELSQITRTSYGPNGMNKMVINHLEKLFVTSDAATILRELEVQHPAAKLLVMASQMQEEEIGDGTNLVVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 112 LAGALLEEAEQLLDRGIHPIRIADGYEQAARVAIEHLDKISDSVLVDIKDTEPLIQTAKTTLGSKVV-NSCHrqMAEIAV 190
Cdd:cd03341 88 LAGELLEKAEELLRMGLHPSEIIEGYEKALKKALEILEELVVYKIEDLRNKEEVSKALKTAIASKQYgNEDF--LSPLVA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 191 NAVLTVADMERRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDfSHPQMpKKVEDAKIAILTCPFeppkpktkhkldvts 270
Cdd:cd03341 166 EACISVLPENIGNFNVDNIRVVKILGGSLEDSKVVRGMVFKRE-PEGSV-KRVKKAKVAVFSCPF--------------- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 271 vedykalqkyekekfeemiqqikETGANLAICQWGFDDEANHLLLQNNLPAVRWVGGPEIELIAIATGGRIVPRFSELTA 350
Cdd:cd03341 229 -----------------------DIGVNVIVAGGSVGDLALHYCNKYGIMVIKINSKFELRRLCRTVGATPLPRLGAPTP 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 351 EKLGFAGLVQEISFGTTkdKMLVIEQCKNSRAV-TIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAEISC 429
Cdd:cd03341 286 EEIGYCDSVYVEEIGDT--KVVVFRQNKEDSKIaTIVLRGATQNILDDVERAIDDGVNVFKSLTKDGRFVPGAGATEIEL 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 430 ALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKE-MNPALGIDCLHKGTNDMKQQHVIE 508
Cdd:cd03341 364 AKKLKEYGEKTPGLEQYAIKKFAEAFEVVPRTLAENAGLDATEVLSELYAAHQKGnKSAGVDIESGDEGTKDAKEAGIFD 443
|
490 500
....*....|....*....|....*
gi 1996390960 509 TLIGKKQQISLATQMVRMILKIDDI 533
Cdd:cd03341 444 HLATKKWAIKLATEAAVTVLRVDQI 468
|
|
| chap_CCT_theta |
TIGR02346 |
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ... |
32-533 |
7.12e-99 |
|
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: 309.34 E-value: 7.12e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 32 EALKSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVV 111
Cdd:TIGR02346 18 EAVIKNIEACKELSQITRTSLGPNGMNKMVINHLEKLFVTNDAATILRELEVQHPAAKLLVMASEMQENEIGDGTNLVLV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 112 LAGALLEEAEQLLDRGIHPIRIADGYEQAARVAIEHLDKISDSVLVDIKDTEPLIQTAKTTLGSKVVNScHRQMAEIAVN 191
Cdd:TIGR02346 98 LAGELLNKAEELIRMGLHPSEIIKGYEMALKKAMEILEELVVWEVKDLRDKDELIKALKASISSKQYGN-EDFLAQLVAQ 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 192 AVLTVADMERRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFShpQMPKKVEDAKIAILTCPFEPPKPKTKHKLDVTSV 271
Cdd:TIGR02346 177 ACSTVLPKNPQNFNVDNIRVCKILGGSLSNSEVLKGMVFNREAE--GSVKSVKNAKVAVFSCPLDTATTETKGTVLIHNA 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 272 EDYKALQKYEKEKFEEMIQQIKETGANLAICQWGFDDEANHLLLQNNLPAVRWVGGPEIELIAIATGGRIVPRFSELTAE 351
Cdd:TIGR02346 255 EELLNYSKGEENQIEAMIKAIADSGVNVIVTGGSVGDMALHYLNKYNIMVLKIPSKFELRRLCKTVGATPLPRLGAPTPE 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 352 KLGFAGLVQEISFGTtkDKMLVIEQCK-NSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAEISCA 430
Cdd:TIGR02346 335 EIGYVDSVYVSEIGG--DKVTVFKQENgDSKISTIILRGSTDNLLDDIERAIDDGVNTVKALVKDGRLLPGAGATEIELA 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 431 LAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQvKEMNPALGID--CLHKGTNDMKQQHVIE 508
Cdd:TIGR02346 413 SRLTKYGEKLPGLDQYAIKKFAEAFEIIPRTLAENAGLNANEVIPKLYAAH-KKGNKSKGIDieAESDGVKDASEAGIYD 491
|
490 500
....*....|....*....|....*
gi 1996390960 509 TLIGKKQQISLATQMVRMILKIDDI 533
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 ... |
18-535 |
1.13e-93 |
|
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: 295.23 E-value: 1.13e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 18 IIKDQDRKSRlmGLEALKSHIMAAKAVANTMRTSLGPNGLDKMMV--DKDGDVTVTNDGATILSMMDVDHQIAKLMVELS 95
Cdd:TIGR02341 2 IFKDGADEER--AENARLSSFVGAIAIGDLVKSTLGPKGMDKILQssSSDASIMVTNDGATILKSIGVDNPAAKVLVDMS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 96 KSQDDEIGDGTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARVAIEHLDKIS-DSVLVDIKDTEPLIQTAKTTLG 174
Cdd:TIGR02341 80 KVQDDEVGDGTTSVTVLAAELLREAEKLINQKIHPQTIIAGYREATKAARDALLKSAvDNGSDEVKFRQDLMNIARTTLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 175 SKVVNSCHRQMAEIAVNAVLTVadmeRRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQmPKKVEDAKIAILTCP 254
Cdd:TIGR02341 160 SKILSQHKDHFAQLAVDAVLRL----KGSGNLEAIQIIKKLGGSLADSYLDEGFLLDKKIGVNQ-PKRIENAKILIANTG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 255 FEPPKPKT-KHKLDVTSVEDYKALQKYEKEKFEEMIQQIKETGANLAICQWGFDDEANHLLLQNNLPAVRWVGGPEIELI 333
Cdd:TIGR02341 235 MDTDKVKIfGSRVRVDSTAKVAELEHAEKEKMKEKVEKILKHGINCFINRQLIYNYPEQLFADAGVMAIEHADFEGVERL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 334 AIATGGRIVPRFSELTAEKLGFAGLVQEISFGttKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLI 413
Cdd:TIGR02341 315 ALVTGGEIVSTFDHPELVKLGSCDLIEEIMIG--EDKLLKFSGVKLGEACTIVLRGATQQILDEAERSLHDALCVLSQTV 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 414 RDNRVVYGGGAAEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRArQVKEMNPALGIDc 493
Cdd:TIGR02341 393 KESRTVLGGGCSEMLMSKAVTQEAQRTPGKEALAVEAFARALRQLPTIIADNAGFDSAELVAQLRA-AHYNGNTTMGLD- 470
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1996390960 494 LHKGT-NDMKQQHVIETLIGKKQQISLATQMVRMILKIDDIRK 535
Cdd:TIGR02341 471 MNEGTiADMRQLGITESYKVKRAVVSSAAEAAEVILRVDNIIK 513
|
|
| chap_CCT_zeta |
TIGR02347 |
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ... |
33-539 |
6.76e-86 |
|
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: 275.46 E-value: 6.76e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 33 ALKSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVVL 112
Cdd:TIGR02347 17 ALMMNINAARGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEMQIQHPTASMIARAATAQDDITGDGTTSTVLL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 113 AGALLEEAEQLLDRGIHPIRIADGYEQAARVAIEHLDKISdSVLVDIKDTEPLIQTAKTTLGSKVVNSCHRQMAEIAVNA 192
Cdd:TIGR02347 97 IGELLKQAERYILEGVHPRIITEGFEIARKEALQFLDKFK-VKKEDEVDREFLLNVARTSLRTKLPADLADQLTEIVVDA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 193 VLTVADMErRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKKVEDAKIAILTCPFEPPKPKTKHKLDVTSVE 272
Cdd:TIGR02347 176 VLAIKKDG-EDIDLFMVEIMEMKHKSATDTTLIRGLVLDHGARHPDMPRRVKNAYILTCNVSLEYEKTEVNSGFFYSSAE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 273 DYKALQKYEKEKFEEMIQQIKE-------TGAN---LAICQWGFDDEANHLLLQNNLPAVRWVGGPEIELIAIATGGRIV 342
Cdd:TIGR02347 255 QREKLVKAERKFVDDRVKKIIElkkkvcgKSPDkgfVVINQKGIDPPSLDLLAKEGIMALRRAKRRNMERLTLACGGEAL 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 343 PRFSELTAEKLGFAGLVQEISFGttKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGG 422
Cdd:TIGR02347 335 NSVEDLTPECLGWAGLVYETTIG--EEKYTFIEECKNPKSCTILIKGPNDHTIAQIKDAVRDGLRAVKNAIEDKCVVPGA 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 423 GAAEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKEMNPaLGIDcLHKGTN-DM 501
Cdd:TIGR02347 413 GAFEIAAYRHLKEYKKSVKGKAKLGVEAFANALLVIPKTLAENSGFDAQDTLVKLEDEHDEGGEV-VGVD-LNTGEPiDP 490
|
490 500 510
....*....|....*....|....*....|....*...
gi 1996390960 502 KQQHVIETLIGKKQQISLATQMVRMILKIDDIRKPGES 539
Cdd:TIGR02347 491 EIKGIWDNYRVKKQLIQSATVIASQLLLVDEVMRAGRS 528
|
|
| TCP1_zeta |
cd03342 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
32-537 |
4.10e-85 |
|
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: 271.82 E-value: 4.10e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 32 EALKSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVV 111
Cdd:cd03342 12 QALAVNISAAKGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLSEMQIQHPTASMIARAATAQDDITGDGTTSNVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 112 LAGALLEEAEQLLDRGIHPIRIADGYEQAARVAIEHLDKISDSVLVDIkDTEPLIQTAKTTLGSKVVNSCHRQMAEIAVN 191
Cdd:cd03342 92 LIGELLKQAERYIQEGVHPRIITEGFELAKNKALKFLESFKVPVEIDT-DRELLLSVARTSLRTKLHADLADQLTEIVVD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 192 AVLTVadmERRDVDFELIKVE-GKVGGRLE-DTKLIKGVIVDKDFSHPQMPKKVEDAkiAILTCPFeppkpktkhkldvt 269
Cdd:cd03342 171 AVLAI---YKPDEPIDLHMVEiMQMQHKSDsDTKLIRGLVLDHGARHPDMPKRVENA--YILTCNV-------------- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 270 SVEdykalqkYEK-EKFEEMIQqiketgaNLAICQWGFDDEANHLLLQNNLPAVRWVGGPEIELIAIATGGRIVPRFSEL 348
Cdd:cd03342 232 SLE-------YEKtEVNSGFFY-------SVVINQKGIDPPSLDMLAKEGILALRRAKRRNMERLTLACGGVAMNSVDDL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 349 TAEKLGFAGLVQEISFGttKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAEIS 428
Cdd:cd03342 298 SPECLGYAGLVYERTLG--EEKYTFIEGVKNPKSCTILIKGPNDHTITQIKDAIRDGLRAVKNAIEDKCVVPGAGAFEVA 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 429 CALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRaRQVKEMNPALGIDCLHKGTNDMKQQHVIE 508
Cdd:cd03342 376 LYAHLKEFKKSVKGKAKLGVQAFADALLVIPKTLAENSGLDVQETLVKLQ-DEYAEGGQVGGVDLDTGEPMDPESEGIWD 454
|
490 500
....*....|....*....|....*....
gi 1996390960 509 TLIGKKQQISLATQMVRMILKIDDIRKPG 537
Cdd:cd03342 455 NYSVKRQILHSATVIASQLLLVDEIIRAG 483
|
|
| chaperonin_like |
cd03333 |
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ... |
163-415 |
1.82e-76 |
|
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: 240.06 E-value: 1.82e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 163 EPLIQTAKTTLGSKVvNSCHRQMAEIAVNAVLTVADMERrDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKK 242
Cdd:cd03333 2 ELLLQVATTSLNSKL-SSWDDFLGKLVVDAVLKVGPDNR-MDDLGVIKVEKIPGGSLEDSELVVGVVFDKGYASPYMPKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 243 VEDAKIAILTCPFEPpkpktkhkldvtsvedykalqkyekekfeemiqqiketganLAICQWGFDDEANHLLLQNNLPAV 322
Cdd:cd03333 80 LENAKILLLDCPLEY-----------------------------------------VVIAEKGIDDLALHYLAKAGIMAV 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 323 RWVGGPEIELIAIATGGRIVPRFSELTAEKLGFAGLVQEISFGTtkDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSL 402
Cdd:cd03333 119 RRVKKEDLERIARATGATIVSSLEDLTPEDLGTAELVEETKIGE--EKLTFIEGCKGGKAATILLRGATEVELDEVKRSL 196
|
250
....*....|...
gi 1996390960 403 HDALCVIRNLIRD 415
Cdd:cd03333 197 HDALCAVRAAVEE 209
|
|
| GroEL |
cd03344 |
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ... |
30-507 |
7.84e-16 |
|
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: 80.19 E-value: 7.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 30 GLEALKSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATI---LSMMD-VDHQIAKLMVELSKSQDDEIGDG 105
Cdd:cd03344 6 GEEARKALLRGVNKLADAVKVTLGPKGRNVVIEKSFGSPKITKDGVTVakeIELEDpFENMGAQLVKEVASKTNDVAGDG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 106 TTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARVAIEHLDKISdsvlVDIKDTEPLIQTAKT------TLGSKVVN 179
Cdd:cd03344 86 TTTATVLARAIIKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLS----KPVKTKEEIAQVATIsangdeEIGELIAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 180 SchrqMAEIAVNAVLTVADmerrdvdfelikvegkvGGRLEDT-KLIKGVIVDKDFSHPQM---PKK----VEDAKIAIl 251
Cdd:cd03344 162 A----MEKVGKDGVITVEE-----------------GKTLETElEVVEGMQFDRGYLSPYFvtdPEKmeveLENPYILL- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 252 tcpfeppkpkTKHKLDvtSVEDYKALqkyekekfeemIQQIKETGANLAICQWGFDDEANHLLLQNNLP------AVRwv 325
Cdd:cd03344 220 ----------TDKKIS--SIQELLPI-----------LELVAKAGRPLLIIAEDVEGEALATLVVNKLRgglkvcAVK-- 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 326 gGPE--------IELIAIATGGRIVP-----RFSELTAEKLGFAGLVQeisfgTTKDKMLV-------------IEQCKN 379
Cdd:cd03344 275 -APGfgdrrkamLEDIAILTGGTVISeelglKLEDVTLEDLGRAKKVV-----VTKDDTTIiggagdkaaikarIAQIRK 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 380 SRAVT----------------------IFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNrVVYGGGAAEISCALAVSQEA 437
Cdd:cd03344 349 QIEETtsdydkeklqerlaklsggvavIKVGGATEVELKEKKDRVEDALNATRAAVEEG-IVPGGGVALLRASPALDKLK 427
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 438 DKCPtLEQYAMRAFADALEVIPMALSENSGMNPiqtmtEVRARQVKEMNPALGIDCLHKGTNDMKQQHVI 507
Cdd:cd03344 428 ALNG-DEKLGIEIVRRALEAPLRQIAENAGVDG-----SVVVEKVLESPDGFGYDAATGEYVDMIEAGII 491
|
|
| Fab1_TCP |
cd03334 |
TCP-1 like domain of the eukaryotic phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinase Fab1. ... |
187-413 |
1.04e-15 |
|
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: 1.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 187 EIAVNAVLTVADMERRDVDF-------ELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKKVEDAKIAILTCPFEPPK 259
Cdd:cd03334 21 DILLPLVWKAASNVKPDVRAgddmdirQYVKIKKIPGGSPSDSEVVDGVVFTKNVAHKRMPSKIKNPRILLLQGPLEYQR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 260 PKTKhkldVTSVEDYKAlqkYEKEKFEEMIQQIKETGANLAICQWGFDDEANHLLLQNNLPAVRWVGGPEIELIAIATGG 339
Cdd:cd03334 101 VENK----LLSLDPVIL---QEKEYLKNLVSRIVALRPDVILVEKSVSRIAQDLLLEAGITLVLNVKPSVLERISRCTGA 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1996390960 340 RIVPRFSELTAE-KLGFAGLVQEISF----GTTKDKMLvIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLI 413
Cdd:cd03334 174 DIISSMDDLLTSpKLGTCESFRVRTYveehGRSKTLMF-FEGCPKELGCTILLRGGDLEELKKVKRVVEFMVFAAYHLK 251
|
|
| GroEL |
TIGR02348 |
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ... |
32-213 |
2.78e-13 |
|
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: 72.33 E-value: 2.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 32 EALKSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQI----AKLMVELSKSQDDEIGDGTT 107
Cdd:TIGR02348 9 EARKALLRGVDKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDKFenmgAQLVKEVASKTNDVAGDGTT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 108 GVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARVAIEHLDKISdsvlVDIKDTEPLIQTAKTTLGS--KVVNSCHRQM 185
Cdd:TIGR02348 89 TATVLAQAIVKEGLKNVAAGANPIELKRGIEKAVEAVVEELKKLS----KPVKGKKEIAQVATISANNdeEIGSLIAEAM 164
|
170 180
....*....|....*....|....*...
gi 1996390960 186 AEIAVNAVLTVAdmERRDVDFELIKVEG 213
Cdd:TIGR02348 165 EKVGKDGVITVE--ESKSLETELEVVEG 190
|
|
| groEL |
PRK12850 |
chaperonin GroEL; Reviewed |
18-356 |
8.98e-12 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237231 Cd Length: 544 Bit Score: 67.44 E-value: 8.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 18 IIKDQDRKSRLM-GLEALkshimaakavANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKL---MV- 92
Cdd:PRK12850 6 IRFSTDARDRLLrGVNIL----------ANAVKVTLGPKGRNVVLEKSFGAPRITKDGVTVAKEIELEDKFENMgaqMVk 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 93 ELSKSQDDEIGDGTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARVAIEHLDKISdsvlVDIKDTEPLIQTA--- 169
Cdd:PRK12850 76 EVASKTNDLAGDGTTTATVLAQAIVREGAKLVAAGMNPMDLKRGIDLAVAAVVDELKKIA----KKVTSSKEIAQVAtis 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 170 ---KTTLGSKVVnschRQMAEIAVNAVLTVAdmERRDVDFELIKVEGKvggRLEDTKLIKGVIVDKDfshpQMPKKVEDA 246
Cdd:PRK12850 152 angDESIGEMIA----EAMDKVGKEGVITVE--EAKTLGTELDVVEGM---QFDRGYLSPYFVTNPE----KMRAELEDP 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 247 KIAIltcpfeppkpktkHKLDVTSVEDYKALqkyekekfeemIQQIKETGANLAICQWGFDDEANHLLLQNNL------P 320
Cdd:PRK12850 219 YILL-------------HEKKISNLQDLLPI-----------LEAVVQSGRPLLIIAEDVEGEALATLVVNKLrgglksV 274
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1996390960 321 AVRWVG-----GPEIELIAIATGGRIVP-----RFSELTAEKLGFA 356
Cdd:PRK12850 275 AVKAPGfgdrrKAMLEDIAVLTGGQVISedlgiKLENVTLDMLGRA 320
|
|
| PTZ00114 |
PTZ00114 |
Heat shock protein 60; Provisional |
25-469 |
1.28e-11 |
|
Heat shock protein 60; Provisional
Pssm-ID: 185455 Cd Length: 555 Bit Score: 66.86 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 25 KSRLMGLEALKSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATIL-------SMMDVDhqiAKLMVELSKS 97
Cdd:PTZ00114 15 KEIRFGDEARQSLLKGIERLADAVAVTLGPKGRNVIIEQEYGSPKITKDGVTVAkaiefsdRFENVG---AQLIRQVASK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 98 QDDEIGDGTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARVAIEHLDKISDsvlvDIKDTEPLIQTAKTT----- 172
Cdd:PTZ00114 92 TNDKAGDGTTTATILARAIFREGCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQSR----PVKTKEDILNVATISangdv 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 173 -LGSKVVNSchrqMAEIAVNAVLTVADmerrdvdfelikvegkvGGRLEDT-KLIKGVIVDKDFSHPQMPKKVEDAKIaI 250
Cdd:PTZ00114 168 eIGSLIADA----MDKVGKDGTITVED-----------------GKTLEDElEVVEGMSFDRGYISPYFVTNEKTQKV-E 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 251 LTCPFeppkpktkhkldvTSVEDYKALQkyekekfeemIQQI-------KETGANLAICQWGFDDEANHLLLQNNLP--- 320
Cdd:PTZ00114 226 LENPL-------------ILVTDKKISS----------IQSIlpilehaVKNKRPLLIIAEDVEGEALQTLIINKLRggl 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 321 ---AVRWVGGPE-----IELIAIATGGRIVPR------FSELTAEKLGFAGLVQ-----EISFGTTKDKMLVIEQCKNSR 381
Cdd:PTZ00114 283 kvcAVKAPGFGDnrkdiLQDIAVLTGATVVSEdnvglkLDDFDPSMLGSAKKVTvtkdeTVILTGGGDKAEIKERVELLR 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 382 A-------------------------VTIFIRGGNKMIIEEAKRSLHDALCVIRNLIrDNRVVYGGGAAEI--SCALAVS 434
Cdd:PTZ00114 363 SqierttseydkeklkerlaklsggvAVIKVGGASEVEVNEKKDRIEDALNATRAAV-EEGIVPGGGVALLraSKLLDKL 441
|
490 500 510
....*....|....*....|....*....|....*
gi 1996390960 435 QEADKCPTLEQYAMRAFADALEVIPMALSENSGMN 469
Cdd:PTZ00114 442 EEDNELTPDQRTGVKIVRNALRLPTKQIAENAGVE 476
|
|
| PLN03167 |
PLN03167 |
Chaperonin-60 beta subunit; Provisional |
33-213 |
3.58e-10 |
|
Chaperonin-60 beta subunit; Provisional
Pssm-ID: 215611 [Multi-domain] Cd Length: 600 Bit Score: 62.63 E-value: 3.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 33 ALKSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQI----AKLMVELSKSQDDEIGDGTTG 108
Cdd:PLN03167 67 AIKKLQAGVNKLADLVGVTLGPKGRNVVLESKYGSPKIVNDGVTVAKEVELEDPVenigAKLVRQAAAKTNDLAGDGTTT 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 109 VVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARVAIEHLDKISDSVlvdiKDTEpLIQTAKTTLGS--KVVNSCHRQMA 186
Cdd:PLN03167 147 SVVLAQGLIAEGVKVVAAGANPVQITRGIEKTAKALVKELKKMSKEV----EDSE-LADVAAVSAGNnyEVGNMIAEAMS 221
|
170 180
....*....|....*....|....*..
gi 1996390960 187 EIAVNAVLTVAdmERRDVDFELIKVEG 213
Cdd:PLN03167 222 KVGRKGVVTLE--EGKSAENNLYVVEG 246
|
|
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
43-169 |
1.24e-09 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 60.52 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 43 AVANTMRTSLGPNG----LDKmmvdKDGDVTVTNDGATILSMMDVDHQI----AKLMVELSKSQDDEIGDGTTGVVVLAG 114
Cdd:PRK00013 21 KLADAVKVTLGPKGrnvvLEK----SFGAPTITKDGVTVAKEIELEDPFenmgAQLVKEVASKTNDVAGDGTTTATVLAQ 96
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1996390960 115 ALLEEAEQLLDRGIHPIRIADGYEQAARVAIEHLDKISdsvlVDIKDTEPLIQTA 169
Cdd:PRK00013 97 AIVREGLKNVAAGANPMDLKRGIDKAVEAAVEELKKIS----KPVEDKEEIAQVA 147
|
|
| groEL |
PRK12851 |
chaperonin GroEL; Reviewed |
41-213 |
2.15e-09 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 171770 Cd Length: 541 Bit Score: 59.76 E-value: 2.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 41 AKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQI----AKLMVELSKSQDDEIGDGTTGVVVLAGAL 116
Cdd:PRK12851 20 VNILADAVKVTLGPKGRNVVIDKSFGAPTITNDGVTIAKEIELEDKFenmgAQMVREVASKTNDVAGDGTTTATVLAQAI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 117 LEEAEQLLDRGIHPIRIADGYEQAARVAIEHLDKISDSVLV--DIKDTEPLIQTAKTTLGSKVVNSchrqMAEIAVNAVL 194
Cdd:PRK12851 100 VREGAKAVAAGANPMDLKRGIDRAVAAVVEELKANARPVTTnaEIAQVATISANGDAEIGRLVAEA----MEKVGNEGVI 175
|
170
....*....|....*....
gi 1996390960 195 TVAdmERRDVDFELIKVEG 213
Cdd:PRK12851 176 TVE--ESKTAETELEVVEG 192
|
|
| PRK14104 |
PRK14104 |
chaperonin GroEL; Provisional |
30-213 |
2.45e-09 |
|
chaperonin GroEL; Provisional
Pssm-ID: 172594 Cd Length: 546 Bit Score: 59.66 E-value: 2.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 30 GLEALKSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQI----AKLMVELSKSQDDEIGDG 105
Cdd:PRK14104 9 GVDARDRMLRGVDILANAVKVTLGPKGRNVVLDKSFGAPRITKDGVTVAKEIELEDKFenmgAQMVREVASKSADAAGDG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 106 TTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARVAIEHLDKISDSVLV--DIKDTEPLIQTAKTTLGSKVVNSchr 183
Cdd:PRK14104 89 TTTATVLAQAIVREGAKSVAAGMNPMDLKRGIDLAVEAVVADLVKNSKKVTSndEIAQVGTISANGDAEIGKFLADA--- 165
|
170 180 190
....*....|....*....|....*....|
gi 1996390960 184 qMAEIAVNAVLTVAdmERRDVDFELIKVEG 213
Cdd:PRK14104 166 -MKKVGNEGVITVE--EAKSLETELDVVEG 192
|
|
| groEL |
PRK12849 |
chaperonin GroEL; Reviewed |
43-367 |
2.60e-09 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237230 Cd Length: 542 Bit Score: 59.82 E-value: 2.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 43 AVANTMRTSLGPNGLDkMMVDKD-GDVTVTNDGATILSMMDVDHQI----AKLMVELSKSQDDEIGDGTTGVVVLAGALL 117
Cdd:PRK12849 21 KLADAVKVTLGPKGRN-VVIDKSfGAPTITKDGVSIAKEIELEDPFenlgAQLVKEVASKTNDVAGDGTTTATVLAQALV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 118 EEAEQLLDRGIHPIRIADGYEQAARVAIEHLDKISdsvlVDIKDTEPLIQTAKT------TLGSKVVnschRQMAEIAVN 191
Cdd:PRK12849 100 QEGLKNVAAGANPMDLKRGIDKAVEAVVEELKALA----RPVSGSEEIAQVATIsangdeEIGELIA----EAMEKVGKD 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 192 AVLTVAdmERRDVDFELIKVEGkvggrledtklikgVIVDKDFSHPQM---PKK----VEDAKIAIltcpfeppkpkTKH 264
Cdd:PRK12849 172 GVITVE--ESKTLETELEVTEG--------------MQFDRGYLSPYFvtdPERmeavLEDPLILL-----------TDK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 265 KLdvTSVEDYKALqkyekekfeemIQQIKETGANLAICQWGFDDEANHLLLQN----NLPAVRwVGGPE--------IEL 332
Cdd:PRK12849 225 KI--SSLQDLLPL-----------LEKVAQSGKPLLIIAEDVEGEALATLVVNklrgGLKVAA-VKAPGfgdrrkamLED 290
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1996390960 333 IAIATGGRIVPR-----FSELTAEKLGFAGLVqEISFGTT 367
Cdd:PRK12849 291 IAILTGGTVISEdlglkLEEVTLDDLGRAKRV-TITKDNT 329
|
|
| groEL |
PRK12852 |
chaperonin GroEL; Reviewed |
44-213 |
9.17e-08 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237232 Cd Length: 545 Bit Score: 54.85 E-value: 9.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 44 VANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQI----AKLMVELSKSQDDEIGDGTTGVVVLAGALLEE 119
Cdd:PRK12852 23 LANAVKVTLGPKGRNVVIEKSFGAPRITKDGVTVAKEIELEDKFenmgAQMVREVASKTNDLAGDGTTTATVLAQAIVRE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 120 AEQLLDRGIHPIRIADGYEQAARVAIEHLDKISDSVL--VDIKDTEPLIQTAKTTLGSKVVNSchrqMAEIAVNAVLTVA 197
Cdd:PRK12852 103 GAKAVAAGMNPMDLKRGIDIAVAAVVKDIEKRAKPVAssAEIAQVGTISANGDAAIGKMIAQA----MQKVGNEGVITVE 178
|
170
....*....|....*.
gi 1996390960 198 DMERRDVDFELikVEG 213
Cdd:PRK12852 179 ENKSLETEVDI--VEG 192
|
|
| groEL |
CHL00093 |
chaperonin GroEL |
20-174 |
1.52e-07 |
|
chaperonin GroEL
Pssm-ID: 177025 Cd Length: 529 Bit Score: 53.95 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 20 KDQDRKSRLMGLEALkshimaAKAVANTmrtsLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVEL----- 94
Cdd:CHL00093 8 QDNARRALERGMDIL------AEAVSVT----LGPKGRNVVLEKKYGSPQIVNDGVTIAKEIELEDHIENTGVALirqaa 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390960 95 SKSqDDEIGDGTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARVAIEHLDKISDSvlvdIKDTEPLIQTAKTTLG 174
Cdd:CHL00093 78 SKT-NDVAGDGTTTATVLAYAIVKQGMKNVAAGANPISLKRGIEKATQYVVSQIAEYARP----VEDIQAITQVASISAG 152
|
|
| |
