|
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: 1099.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 10 DEYGRPFLIIKDQDRKSRLMGLEALKSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAK 89
Cdd:cd03339 1 DEYGRPFIIVREQEKKKRLKGLEAHKSHILAAKSVANILRTSLGPRGMDKILVSPDGEVTVTNDGATILEKMDVDHQIAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 90 LMVELSKSQDDEIGDGTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARIAIQHLDKISDNVLVDINNPEPLIQTA 169
Cdd:cd03339 81 LLVELSKSQDDEIGDGTTGVVVLAGALLEQAEKLLDRGIHPIRIADGYEQACKIAVEHLEEIADKIEFSPDNKEPLIQTA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 170 KTTLGSKVVNSCHRQMAEIAVNAVLTVADMERRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKEVLNAKIA 249
Cdd:cd03339 161 MTSLGSKIVSRCHRQFAEIAVDAVLSVADLERKDVNFELIKVEGKVGGRLEDTKLVKGIVIDKDFSHPQMPKEVKDAKIA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 250 ILTCPFEPPKPKTKHKLDVTSVEDYKALQKYEKEKFEEMIAQIKETGANLAICQWGFDDEANHLLLQNGLPAVRWVGGPE 329
Cdd:cd03339 241 ILTCPFEPPKPKTKHKLDITSVEDYKKLQEYEQKYFREMVEQVKDAGANLVICQWGFDDEANHLLLQNGLPAVRWVGGVE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 330 IELIAIATGGRIVPRFSELTSEKLGFAGVVREISFGTTKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVI 409
Cdd:cd03339 321 IELIAIATGGRIVPRFEDLSPEKLGKAGLVREISFGTTKDKMLVIEGCPNSKAVTIFIRGGNKMIIEEAKRSLHDALCVV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 410 RNLIRDNRVVYGGGAAEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKESNPAL 489
Cdd:cd03339 401 RNLIRDNRIVYGGGAAEISCSLAVEKAADKCSGIEQYAMRAFADALESIPLALAENSGLNPIETLSEVKARQVKEKNPHL 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 51890219 490 GIDCLHKGSNDMQYQHVIETLIGKKQQISLATQMVRMILKIDDIRK 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: 1014.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 6 TLAFDEYGRPFLIIKDQDRKSRLMGLEALKSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDH 85
Cdd:TIGR02343 1 ILAFDEYGRPFIIIKDQDNKKRLKGLEAKKSNIAAAKSVASILRTSLGPKGMDKMLISPDGDITVTNDGATILSQMDVDN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 86 QIAKLMVELSKSQDDEIGDGTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARIAIQHLDKISDNVLVDINNPEPL 165
Cdd:TIGR02343 81 QIAKLMVELSKSQDDEIGDGTTGVVVLAGALLEQAEELLDKGIHPIKIADGFEEAARIAVEHLEEISDEISADNNNREPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 166 IQTAKTTLGSKVVNSCHRQMAEIAVNAVLTVADMERRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKEVLN 245
Cdd:TIGR02343 161 IQAAKTSLGSKIVSKCHRRFAEIAVDAVLNVADMERRDVDFDLIKVEGKVGGSLEDTKLIKGIIIDKDFSHPQMPKEVED 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 246 AKIAILTCPFEPPKPKTKHKLDVTSVEDYKALQKYEKEKFEEMIAQIKETGANLAICQWGFDDEANHLLLQNGLPAVRWV 325
Cdd:TIGR02343 241 AKIAILTCPFEPPKPKTKHKLDISSVEEYKKLQKYEQQKFKEMIDDIKKSGANLVICQWGFDDEANHLLLQNDLPAVRWV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 326 GGPEIELIAIATGGRIVPRFSELTSEKLGFAGVVREISFGTTKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDA 405
Cdd:TIGR02343 321 GGQELELIAIATGGRIVPRFQELSKDKLGKAGLVREISFGTTKDRMLVIEQCKNSKAVTIFIRGGNKMIIEEAKRSIHDA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 406 LCVIRNLIRDNRVVYGGGAAEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKES 485
Cdd:TIGR02343 401 LCVVRNLIKDSRIVYGGGAAEISCSLAVSQEADKYPGVEQYAIRAFADALETIPMALAENSGLDPIGTLSTLKSLQLKEK 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 51890219 486 NPALGIDCLHKGSNDMQYQHVIETLIGKKQQISLATQMVRMILKIDDIRKPG 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: 594.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 25 KSRLMGLEALKSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVELSKSQDDEIGD 104
Cdd:cd00309 1 KEREFGEEARLSNINAAKALADAVKTTLGPKGMDKMLVDSLGDPTITNDGATILKEIEVEHPAAKLLVEVAKSQDDEVGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 105 GTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARIAIQHLDKISdnVLVDINNPEPLIQTAKTTLGSKVVNSCHRQ 184
Cdd:cd00309 81 GTTTVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIA--VPIDVEDREELLKVATTSLNSKLVSGGDDF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 185 MAEIAVNAVLTVADMErRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKEVLNAKIAILTCPFEPpkpktkh 264
Cdd:cd00309 159 LGELVVDAVLKVGKEN-GDVDLGVIRVEKKKGGSLEDSELVVGMVFDKGYLSPYMPKRLENAKILLLDCKLEY------- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 265 kldvtsvedykalqkyekekfeemiaqiketganLAICQWGFDDEANHLLLQNGLPAVRWVGGPEIELIAIATGGRIVPR 344
Cdd:cd00309 231 ----------------------------------VVIAEKGIDDEALHYLAKLGIMAVRRVRKEDLERIAKATGATIVSR 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 345 FSELTSEKLGFAGVVREISFGttKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGA 424
Cdd:cd00309 277 LEDLTPEDLGTAGLVEETKIG--DEKYTFIEGCKGGKVATILLRGATEVELDEAERSLHDALCAVRAAVEDGGIVPGGGA 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 425 AEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKESNPAlGIDCLHKGSNDMQYQ 504
Cdd:cd00309 355 AEIELSKALEELAKTLPGKEQLGIEAFADALEVIPRTLAENAGLDPIEVVTKLRAKHAEGGGNA-GGDVETGEIVDMKEA 433
|
490 500
....*....|....*....|....*....
gi 51890219 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: 555.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 44 VANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVVLAGALLEEAEQL 123
Cdd:pfam00118 1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELEIQHPAAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEEAEKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 124 LDRGIHPIRIADGYEQAARIAIQHLDKIsDNVLVDINNPEPLIQTAKTTLGSKVVNSCHRQMAEIAVNAVLTVADmERRD 203
Cdd:pfam00118 81 LAAGVHPTTIIEGYEKALEKALEILDSI-ISIPVEDVDREDLLKVARTSLSSKIISRESDFLAKLVVDAVLAIPK-NDGS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 204 VDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKEVLNAKIAILTCPFEPPKPKTKHKLDVTSVEDYKALQKYEKE 283
Cdd:pfam00118 159 FDLGNIGVVKILGGSLEDSELVDGVVLDKGPLHPDMPKRLENAKVLLLNCSLEYEKTETKATVVLSDAEQLERFLKAEEE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 284 KFEEMIAQIKETGANLAICQWGFDDEANHLLLQNGLPAVRWVGGPEIELIAIATGGRIVPRFSELTSEKLGFAGVVREIS 363
Cdd:pfam00118 239 QILEIVEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMALRRVKKRDLERLAKATGARAVSSLDDLTPDDLGTAGKVEEEK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 364 FGttKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAEISCALAVSQEADKCPTL 443
Cdd:pfam00118 319 IG--DEKYTFIEGCKSPKAATILLRGATDHVLDEIERSIHDALCVVKNAIEDPRVVPGGGAVEMELARALREYAKSVSGK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 444 EQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQvKESNPALGIDCLHKGSNDMQYQHVIETLIGKKQQISLATQM 523
Cdd:pfam00118 397 EQLAIEAFAEALEVIPKTLAENAGLDPIEVLAELRAAH-ASGEKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKSATEA 475
|
490
....*....|
gi 51890219 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: 542.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 15 PFLIIKDQdrKSRLMGLEALKSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVEL 94
Cdd:NF041082 2 PILILKEG--TQRTSGRDAQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDVVITNDGVTILKEMDIEHPAAKMIVEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 95 SKSQDDEIGDGTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARIAIQHLDKISdnVLVDINNPEPLIQTAKTTLG 174
Cdd:NF041082 80 AKTQDDEVGDGTTTAVVLAGELLKKAEELLDQDIHPTIIAEGYRLAAEKALEILDEIA--IKVDPDDKETLKKIAATAMT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 175 SKVVNSCHRQMAEIAVNAVLTVADME-RRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKEVLNAKIAILTC 253
Cdd:NF041082 158 GKGAEAAKDKLADLVVDAVKAVAEKDgGYNVDLDNIKVEKKVGGSIEDSELVEGVVIDKERVHPGMPKRVENAKIALLDA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 254 PFEPPKPKTKHKLDVTSVEDYKALQKYEKEKFEEMIAQIKETGANLAICQWGFDDEANHLLLQNGLPAVRWVGGPEIELI 333
Cdd:NF041082 238 PLEVKKTEIDAKISITDPDQLQAFLDQEEKMLKEMVDKIADSGANVVFCQKGIDDLAQHYLAKEGILAVRRVKKSDMEKL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 334 AIATGGRIVPRFSELTSEKLGFAGVVREISFGttKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLI 413
Cdd:NF041082 318 AKATGARIVTSIDDLSPEDLGYAGLVEERKVG--GDKMIFVEGCKNPKAVTILLRGGTEHVVDEVERALEDALRVVRVVL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 414 RDNRVVYGGGAAEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKESNPAlGIDC 493
Cdd:NF041082 396 EDGKVVAGGGAPEVELALRLREYAASVGGREQLAIEAFAEALEIIPRTLAENAGLDPIDALVELRSAHEKGNKTA-GLDV 474
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 51890219 494 LHKGSNDMQYQHVIETLIGKKQQISLATQMVRMILKIDDI 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: 530.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 15 PFLIIKDQdrKSRLMGLEALKSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVEL 94
Cdd:NF041083 2 PVLILKEG--TQRTKGRDAQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDIVITNDGATILKEMDVQHPAAKMLVEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 95 SKSQDDEIGDGTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARIAIQHLDKISdnVLVDINNPEPLIQTAKTTLG 174
Cdd:NF041083 80 AKTQDDEVGDGTTTAVVLAGELLKKAEELLDQNIHPTIIANGYRLAAEKAIEILDEIA--EKVDPDDRETLKKIAETSLT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 175 SKVVNSCHRQMAEIAVNAVLTVAdmERRD----VDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKEVLNAKIAI 250
Cdd:NF041083 158 SKGVEEARDYLAEIAVKAVKQVA--EKRDgkyyVDLDNIQIEKKHGGSIEDTQLIYGIVIDKEVVHPGMPKRVENAKIAL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 251 LTCPFEPPKPKTKHKLDVTSVEDYKALQKYEKEKFEEMIAQIKETGANLAICQWGFDDEANHLLLQNGLPAVRWVGGPEI 330
Cdd:NF041083 236 LDAPLEVKKTEIDAEIRITDPDQLQKFLDQEEKMLKEMVDKIKATGANVVFCQKGIDDLAQHYLAKAGILAVRRVKKSDM 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 331 ELIAIATGGRIVPRFSELTSEKLGFAGVVREISFGTtkDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIR 410
Cdd:NF041083 316 EKLAKATGARIVTNIDDLTPEDLGYAELVEERKVGD--DKMVFVEGCKNPKAVTILIRGGTEHVVDEAERALEDALSVVA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 411 NLIRDNRVVYGGGAAEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQvKESNPALG 490
Cdd:NF041083 394 DAVEDGKIVAGGGAPEVELAKRLREYAATVGGREQLAVEAFAEALEIIPRTLAENAGLDPIDILVKLRSAH-EKGKKWAG 472
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 51890219 491 IDCLHKGSNDMQYQHVIETLIGKKQQISLATQMVRMILKIDDI 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: 529.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 17 LIIKDqdRKSRLMGLEALKSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVELSK 96
Cdd:cd03343 2 LILKE--GTQRTSGRDAQRMNIAAAKAVAEAVRTTLGPKGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 97 SQDDEIGDGTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARIAIQHLDKISDNvlVDINNPEPLIQTAKTTLGSK 176
Cdd:cd03343 80 TQDEEVGDGTTTAVVLAGELLEKAEDLLDQNIHPTVIIEGYRLAAEKALELLDEIAIK--VDPDDKDTLRKIAKTSLTGK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 177 VVNSCHRQMAEIAVNAVLTVADME--RRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKEVLNAKIAILTCP 254
Cdd:cd03343 158 GAEAAKDKLADLVVDAVLQVAEKRdgKYVVDLDNIKIEKKTGGSVDDTELIRGIVIDKEVVHPGMPKRVENAKIALLDAP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 255 FEPPKPKTKHKLDVTSVEDYKALQKYEKEKFEEMIAQIKETGANLAICQWGFDDEANHLLLQNGLPAVRWVGGPEIELIA 334
Cdd:cd03343 238 LEVKKTEIDAKIRITSPDQLQAFLEQEEAMLKEMVDKIADTGANVVFCQKGIDDLAQHYLAKAGILAVRRVKKSDMEKLA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 335 IATGGRIVPRFSELTSEKLGFAGVVREISFGttKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIR 414
Cdd:cd03343 318 RATGAKIVTNIDDLTPEDLGEAELVEERKVG--DDKMVFVEGCKNPKAVTILLRGGTEHVVDELERALEDALRVVADALE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 415 DNRVVYGGGAAEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQvKESNPALGIDCL 494
Cdd:cd03343 396 DGKVVAGGGAVEIELAKRLREYARSVGGREQLAVEAFADALEEIPRTLAENAGLDPIDTLVELRAAH-EKGNKNAGLDVY 474
|
490 500 510
....*....|....*....|....*....|....*....
gi 51890219 495 HKGSNDMQYQHVIETLIGKKQQISLATQMVRMILKIDDI 533
Cdd:cd03343 475 TGEVVDMLEKGVIEPLRVKKQAIKSATEAATMILRIDDV 513
|
|
| thermosome_arch |
TIGR02339 |
thermosome, various subunits, archaeal; Thermosome is the name given to the archaeal rather ... |
15-533 |
8.74e-174 |
|
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: 500.75 E-value: 8.74e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 15 PFLIIKDQdrKSRLMGLEALKSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVEL 94
Cdd:TIGR02339 1 PVFILKEG--TQRTSGRDAQRNNIAAAKAVAEAVKSTLGPRGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 95 SKSQDDEIGDGTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARIAIQHLDKISDNvlVDINNPEPLIQTAKTTLG 174
Cdd:TIGR02339 79 AKTQDEEVGDGTTTAVVLAGELLEKAEDLLEQDIHPTVIIEGYRKAAEKALEIIDEIATK--ISPEDRDLLKKIAYTSLT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 175 SKVVNSCHRQ-MAEIAVNAVLTVADME---RRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKEVLNAKIAI 250
Cdd:TIGR02339 157 SKASAEVAKDkLADLVVEAVKQVAELRgdgKYYVDLDNIKIVKKKGGSIEDTELVEGIVVDKEVVHPGMPKRVENAKIAL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 251 LTCPFEPPKPKTKHKLDVTSVEDYKALQKYEKEKFEEMIAQIKETGANLAICQWGFDDEANHLLLQNGLPAVRWVGGPEI 330
Cdd:TIGR02339 237 LDAPLEVEKTEIDAKIRITDPDQIKKFLDQEEAMLKEMVDKIASAGANVVICQKGIDDVAQHYLAKAGILAVRRVKKSDI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 331 ELIAIATGGRIVPRFSELTSEKLGFAGVVREISFGttKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIR 410
Cdd:TIGR02339 317 EKLARATGARIVSSIDEITESDLGYAELVEERKVG--EDKMVFVEGCKNPKAVTILLRGGTEHVVDELERSIQDALHVVA 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 411 NLIRDNRVVYGGGAAEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKEsNPALG 490
Cdd:TIGR02339 395 NALEDGKIVAGGGAVEIELALRLRSYARSVGGREQLAIEAFADALEEIPRILAENAGLDPIDALVDLRAKHEKG-NKNAG 473
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 51890219 491 IDCLHKGSNDMQYQHVIETLIGKKQQISLATQMVRMILKIDDI 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 |
7.66e-150 |
|
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: 439.80 E-value: 7.66e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 35 KSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVVLAG 114
Cdd:cd03338 11 LSNIQAAKAVADAIRTSLGPRGMDKMIQTGKGEVIITNDGATILKQMSVLHPAAKMLVELSKAQDIEAGDGTTSVVVLAG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 115 ALLEEAEQLLDRGIHPIRIADGYEQAARIAIQHLDKISDNvlVDINNPEPLIQTAKTTLGSKVVNSCHRQMAEIAVNAVL 194
Cdd:cd03338 91 ALLSACESLLKKGIHPTVISESFQIAAKKAVEILDSMSIP--VDLNDRESLIKSATTSLNSKVVSQYSSLLAPIAVDAVL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 195 TVADMER-RDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSH-PQMPKEVLNAKIAILTCPFEPPKPKTKHKLdvtSVE 272
Cdd:cd03338 169 KVIDPATaTNVDLKDIRIVKKLGGTIEDTELVDGLVFTQKASKkAGGPTRIEKAKIGLIQFCLSPPKTDMDNNI---VVN 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 273 DYKA---LQKYEKEKFEEMIAQIKETGANLAICQW-----GFDDEANHLLLQNGLPAVRWVGGPEIELIAIATGGRIVPR 344
Cdd:cd03338 246 DYAQmdrILREERKYILNMCKKIKKSGCNVLLIQKsilrdAVSDLALHFLAKLKIMVVKDIEREEIEFICKTIGCKPVAS 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 345 FSELTSEKLGFAGVVREISFGTtkDKMLVIEQCKNS-RAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGG 423
Cdd:cd03338 326 IDHFTEDKLGSADLVEEVSLGD--GKIVKITGVKNPgKTVTILVRGSNKLVLDEAERSLHDALCVIRCLVKKRALIPGGG 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 424 AAEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQvKESNPALGIDCLHKGSNDMQY 503
Cdd:cd03338 404 APEIEIALQLSEWARTLTGVEQYCVRAFADALEVIPYTLAENAGLNPISIVTELRNRH-AQGEKNAGINVRKGAITNILE 482
|
490 500 510
....*....|....*....|....*....|
gi 51890219 504 QHVIETLIGKKQQISLATQMVRMILKIDDI 533
Cdd:cd03338 483 ENVVQPLLVSTSAITLATETVRMILKIDDI 512
|
|
| chap_CCT_delta |
TIGR02342 |
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ... |
35-533 |
1.54e-136 |
|
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: 405.71 E-value: 1.54e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 35 KSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVVLAG 114
Cdd:TIGR02342 12 TSNIVAAKAVADAIRTSLGPKGMDKMIQDGKGEVIITNDGATILKQMAVLHPAAKMLVELSKAQDIEAGDGTTSVVILAG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 115 ALLEEAEQLLDRGIHPIRIADGYEQAARIAIQHLDKISdnVLVDINNPEPLIQTAKTTLGSKVVNSCHRQMAEIAVNAVL 194
Cdd:TIGR02342 92 ALLGACERLLNKGIHPTIISESFQSAADEAIKILDEMS--IPVDLSDREQLLKSATTSLSSKVVSQYSSLLAPLAVDAVL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 195 TVADMER-RDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQ-MPKEVLNAKIAILTCPFEPPKPKTKHKLDVTSVE 272
Cdd:TIGR02342 170 KVIDPENaKNVDLNDIKVVKKLGGTIDDTELIEGLVFTQKASKSAgGPTRIEKAKIGLIQFQISPPKTDMENQIIVNDYA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 273 DYKALQKYEKEKFEEMIAQIKETGANLAICQW-----GFDDEANHLLLQNGLPAVRWVGGPEIELIAIATGGRIVPRFSE 347
Cdd:TIGR02342 250 QMDRVLKEERAYILNIVKKIKKTGCNVLLIQKsilrdAVNDLALHFLAKMKIMVVKDIEREEIEFICKTIGCKPIASIDH 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 348 LTSEKLGFAGVVREIsfGTTKDKMLVIEQCKN-SRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAE 426
Cdd:TIGR02342 330 FTADKLGSAELVEEV--DSDGGKIIKITGIQNaGKTVTVVVRGSNKLVIDEAERSLHDALCVIRCLVKKRGLIAGGGAPE 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 427 ISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQvKESNPALGIDCLHKGSNDMQYQHV 506
Cdd:TIGR02342 408 IEIARRLSKYARTMKGVESYCVRAFADALEVIPYTLAENAGLNPIKVVTELRNRH-ANGEKTAGISVRKGGITNMLEEHV 486
|
490 500
....*....|....*....|....*..
gi 51890219 507 IETLIGKKQQISLATQMVRMILKIDDI 533
Cdd:TIGR02342 487 LQPLLVTTSAITLASETVRSILKIDDI 513
|
|
| TCP1_gamma |
cd03337 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ... |
20-533 |
4.44e-123 |
|
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: 369.70 E-value: 4.44e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 20 KDQDRKSRLmglealkSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVELSKSQD 99
Cdd:cd03337 11 RESGRKAQL-------GNIQAAKTVADVIRTCLGPRAMLKMLLDPMGGIVLTNDGNAILREIDVAHPAAKSMIELSRTQD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 100 DEIGDGTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARIAIQHLDKISdnVLVDINNPEPLIQTAKTTLGSKVVN 179
Cdd:cd03337 84 EEVGDGTTSVIILAGEILAVAEPFLERGIHPTVIIKAYRKALEDALKILEEIS--IPVDVNDRAQMLKIIKSCIGTKFVS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 180 SCHRQMAEIAVNAVLTVA---DMERRDVDFE-LIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKEVLNAKIAILTCPF 255
Cdd:cd03337 162 RWSDLMCNLALDAVKTVAveeNGRKKEIDIKrYAKVEKIPGGEIEDSRVLDGVMLNKDVTHPKMRRRIENPRIVLLDCPL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 256 EppkpktkhkldvtsvedYkalqkyekekfeemiaqiketganLAICQWGFDDEANHLLLQNGLPAVRWVGGPEIELIAI 335
Cdd:cd03337 242 E-----------------Y------------------------LVITEKGVSDLAQHYLVKAGITALRRVRKTDNNRIAR 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 336 ATGGRIVPRFSELTSEKLGFAGVVREISFGtTKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRD 415
Cdd:cd03337 281 ACGATIVNRPEELTESDVGTGAGLFEVKKI-GDEYFTFITECKDPKACTILLRGASKDVLNEVERNLQDAMAVARNIILN 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 416 NRVVYGGGAAEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKESNPALGIDCLH 495
Cdd:cd03337 360 PKLVPGGGATEMAVSHALSEKAKSIEGVEQWPYKAVASALEVIPRTLAQNCGANVIRTLTELRAKHAQGENSTWGIDGET 439
|
490 500 510
....*....|....*....|....*....|....*...
gi 51890219 496 KGSNDMQYQHVIETLIGKKQQISLATQMVRMILKIDDI 533
Cdd:cd03337 440 GDIVDMKELGIWDPLAVKAQTYKTAIEAACMLLRIDDI 477
|
|
| GroEL |
COG0459 |
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ... |
25-533 |
4.54e-123 |
|
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227 Cd Length: 497 Bit Score: 370.56 E-value: 4.54e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 25 KSRLMGLEALKSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQI----AKLMVELSKSQDD 100
Cdd:COG0459 3 KQILFGEDARRANIRGVKALADAVKVTLGPKGRNVMLVKSFGDPTITNDGVTIAKEIELEDPFenmgAQLVKEVASKTND 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 101 EIGDGTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARIAIQHLDKISdnvlVDINNPEPLIQTAKTTLGSKvvns 180
Cdd:COG0459 83 EAGDGTTTATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIA----KPVDDKEELAQVATISANGD---- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 181 chRQMAEIAVNAVLTVADMERrdvdfelIKVEgKVGGRLEDTKLIKGVIVDKDFSHPQ-------MPKEVLNAKIAILTC 253
Cdd:COG0459 155 --EEIGELIAEAMEKVGKDGV-------ITVE-EGKGLETELEVVEGMQFDKGYLSPYfvtdpekMPAELENAYILLTDK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 254 PFEPPKPktkhkldvtsvedykalqkyekekFEEMIAQIKETGANLAICQWGFDDEANHLLLQNGLPAVR---WVGGP-- 328
Cdd:COG0459 225 KISSIQD------------------------LLPLLEKVAQSGKPLLIIAEDIDGEALATLVVNGIRGVLrvvAVKAPgf 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 329 ------EIELIAIATGGRIV-----PRFSELTSEKLGFAGVVREisfgtTKDKMLVIEQCKNSRAVTIFIRGGNKMIIEE 397
Cdd:COG0459 281 gdrrkaMLEDIAILTGGRVIsedlgLKLEDVTLDDLGRAKRVEV-----DKDNTTIVEGAGNPKAIVILVGAATEVEVKE 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 398 AKRSLHDALCVIRNLIRDnRVVYGGGAAEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEV 477
Cdd:COG0459 356 RKRRVEDALHATRAAVEE-GIVPGGGAALLRAARALRELAAKLEGDEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKV 434
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 51890219 478 RArqvkESNPALGIDCLHKGSNDMQYQHVIETLIGKKQQISLATQMVRMILKIDDI 533
Cdd:COG0459 435 RA----AKDKGFGFDAATGEYVDMLEAGVIDPAKVKRSALQNAASVAGLILTTEAV 486
|
|
| chap_CCT_gamma |
TIGR02344 |
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ... |
15-533 |
2.47e-117 |
|
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: 356.74 E-value: 2.47e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 15 PFLIIKDQDRksRLMGLEALKSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVEL 94
Cdd:TIGR02344 1 PVLVLNQNTK--RESGRKAQLSNIQAAKAVADIIRTCLGPRSMLKMLLDPMGGIVMTNDGNAILREIDVAHPAAKSMIEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 95 SKSQDDEIGDGTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARIAIQHLDKISdnVLVDINNPEPLIQTAKTTLG 174
Cdd:TIGR02344 79 SRTQDEEVGDGTTSVIILAGEMLSVAEPFLEQNIHPTVIIRAYRKALDDALSVLEEIS--IPVDVNDDAAMLKLIQSCIG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 175 SKVVNSCHRQMAEIAVNAVLTVA--DMERRDVDFE-LIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKEVLNAKIAIL 251
Cdd:TIGR02344 157 TKFVSRWSDLMCDLALDAVRTVQrdENGRKEIDIKrYAKVEKIPGGDIEDSCVLKGVMINKDVTHPKMRRYIENPRIVLL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 252 TCPFEPPKPKTKHKLDVTSVEDYKALQKYEKEKFEEMIAQIKETGANLAICQWGFDDEANHLLLQNGLPAVRWVGGPEIE 331
Cdd:TIGR02344 237 DCPLEYKKGESQTNIEITKEEDWNRILQMEEEYVQLMCEDIIAVKPDLVITEKGVSDLAQHYLLKANITAIRRVRKTDNN 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 332 LIAIATGGRIVPRFSELTSEKLGF-AGVVREISFGttKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIR 410
Cdd:TIGR02344 317 RIARACGATIVNRPEELRESDVGTgCGLFEVKKIG--DEYFTFITECKDPKACTILLRGASKDILNEVERNLQDAMAVAR 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 411 NLIRDNRVVYGGGAAEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKESNPALG 490
Cdd:TIGR02344 395 NVLLDPKLVPGGGATEMAVSVALTEKSKKLEGVEQWPYRAVADALEIIPRTLAQNCGANVIRTLTELRAKHAQENNCTWG 474
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 51890219 491 IDCLHKGSNDMQYQHVIETLIGKKQQISLATQMVRMILKIDDI 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 |
3.36e-110 |
|
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: 338.15 E-value: 3.36e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 18 IIKDQDRKSRlmGLEALKSHIMAAKAVANTMRTSLGPNGLDKMM--VDKDGDVTVTNDGATILSMMDVDHQIAKLMVELS 95
Cdd:cd03336 1 ILKDGAQEEK--GETARLSSFVGAIAIGDLVKTTLGPKGMDKILqsVGRSGGVTVTNDGATILKSIGVDNPAAKVLVDIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 96 KSQDDEIGDGTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARIAIQHLDKISDNVLVDINN-PEPLIQTAKTTLG 174
Cdd:cd03336 79 KVQDDEVGDGTTSVTVLAAELLREAEKLVAQKIHPQTIIEGYRMATAAAREALLSSAVDHSSDEEAfREDLLNIARTTLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 175 SKVVNSCHRQMAEIAVNAVLTVADmerrDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQmPKEVLNAKIAILTCP 254
Cdd:cd03336 159 SKILTQDKEHFAELAVDAVLRLKG----SGNLDAIQIIKKLGGSLKDSYLDEGFLLDKKIGVNQ-PKRIENAKILIANTP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 255 FEPPKPKT-KHKLDVTSVEDYKALQKYEKEKFEEMIAQIKETGANLAICQWGFDDEANHLLLQNGLPAVRWVGGPEIELI 333
Cdd:cd03336 234 MDTDKIKIfGAKVRVDSTAKVAEIEEAEKEKMKNKVEKILKHGINCFINRQLIYNYPEQLFADAGIMAIEHADFDGVERL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 334 AIATGGRIVPRFSELTSEKLGFAGVVREISFGttKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLI 413
Cdd:cd03336 314 ALVTGGEIASTFDHPELVKLGTCKLIEEIMIG--EDKLIRFSGVAAGEACTIVLRGASQQILDEAERSLHDALCVLAQTV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 414 RDNRVVYGGGAAEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKESNPAlGIDC 493
Cdd:cd03336 392 KDTRVVLGGGCSEMLMAKAVEELAKKTPGKKSLAIEAFAKALRQLPTIIADNAGYDSAELVAQLRAAHYNGNTTA-GLDM 470
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 51890219 494 LHKGSNDMQYQHVIETLIGKKQQISLATQMVRMILKIDDIRK 535
Cdd:cd03336 471 RKGTVGDMKELGITESFKVKRQVLLSASEAAEMILRVDDIIK 512
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
36-535 |
1.90e-107 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 331.61 E-value: 1.90e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 36 SHIMAAKAVANTMRTSLGPNGLDKMMV-----DKDGDVTVTNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVV 110
Cdd:PTZ00212 26 QSFVGAIAVADLVKTTLGPKGMDKILQpmsegPRSGNVTVTNDGATILKSVWLDNPAAKILVDISKTQDEEVGDGTTSVV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 111 VLAGALLEEAEQLLDRGIHPIRIADGYEQAARIAIQHLDKISDNVLVDINN-PEPLIQTAKTTLGSKVVNSCHRQMAEIA 189
Cdd:PTZ00212 106 VLAGELLREAEKLLDQKIHPQTIIEGWRMALDVARKALEEIAFDHGSDEEKfKEDLLNIARTTLSSKLLTVEKDHFAKLA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 190 VNAVLTVadmeRRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQmPKEVLNAKIAILTCPFEPPKPKT-KHKLDV 268
Cdd:PTZ00212 186 VDAVLRL----KGSGNLDYIQIIKKPGGTLRDSYLEDGFILEKKIGVGQ-PKRLENCKILVANTPMDTDKIKIyGAKVKV 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 269 TSVEDYKALQKYEKEKFEEMIAQIKETGANLAICQWGFDDEANHLLLQNGLPAVRWVGGPEIELIAIATGGRIVPRFSEL 348
Cdd:PTZ00212 261 DSMEKVAEIEAAEKEKMKNKVDKILAHGCNVFINRQLIYNYPEQLFAEAGIMAIEHADFDGMERLAAALGAEIVSTFDTP 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 349 TSEKLGFAGVVREISFGttKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAEIS 428
Cdd:PTZ00212 341 EKVKLGHCDLIEEIMIG--EDKLIRFSGCAKGEACTIVLRGASTHILDEAERSLHDALCVLSQTVKDTRVVLGGGCSEML 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 429 CALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKESNPAlGIDCLHKGSNDMQYQHVIE 508
Cdd:PTZ00212 419 MANAVEELAKKVEGKKSLAIEAFAKALRQIPTIIADNGGYDSAELVSKLRAEHYKGNKTA-GIDMEKGTVGDMKELGITE 497
|
490 500
....*....|....*....|....*..
gi 51890219 509 TLIGKKQQISLATQMVRMILKIDDIRK 535
Cdd:PTZ00212 498 SYKVKLSQLCSATEAAEMILRVDDIIR 524
|
|
| TCP1_eta |
cd03340 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ... |
15-531 |
2.20e-107 |
|
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: 330.79 E-value: 2.20e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 15 PFLIIKDQDRKSRlmGLEALKSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVEL 94
Cdd:cd03340 1 PIILLKEGTDTSQ--GKGQLISNINACQAIADAVRTTLGPRGMDKLIVDGRGKVTISNDGATILKLLDIVHPAAKTLVDI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 95 SKSQDDEIGDGTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARIAIQHLDKISdnvlVDINNPEP------LIQT 168
Cdd:cd03340 79 AKSQDAEVGDGTTSVVVLAGEFLKEAKPFIEDGVHPQIIIRGYRKALQLAIEKIKEIA----VNIDKEDKeeqrelLEKC 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 169 AKTTLGSKVVNSCHRQMAEIAVNAVLTVADmerrDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFS---HPQMPKEVLN 245
Cdd:cd03340 155 AATALNSKLIASEKEFFAKMVVDAVLSLDD----DLDLDMIGIKKVPGGSLEDSQLVNGVAFKKTFSyagFEQQPKKFKN 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 246 AKIAILTCPFEPPKPKTKHKLDVTSVEDYKALQKYEKEKFEEMIAQIKETGANLAICQWGFDDEANHLLLQNGLPAVRWV 325
Cdd:cd03340 231 PKILLLNVELELKAEKDNAEVRVEDPEEYQAIVDAEWKIIYDKLEKIVKSGANVVLSKLPIGDLATQYFADRDIFCAGRV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 326 GGPEIELIAIATGGRIVPRFSELTSEKLGFAGVVREISFGttKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDA 405
Cdd:cd03340 311 PEEDLKRVAQATGGSIQTTVSNITDDVLGTCGLFEERQVG--GERYNIFTGCPKAKTCTIILRGGAEQFIEEAERSLHDA 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 406 LCVIRNLIRDNRVVYGGGAAEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKES 485
Cdd:cd03340 389 IMIVRRAIKNDSVVAGGGAIEMELSKYLRDYSRTIAGKQQLVINAFAKALEIIPRQLCDNAGFDATDILNKLRQKHAQGG 468
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 51890219 486 NPALGIDCLHKGSNDMQYQHVIETLIGKKQQISLATQMVRMILKID 531
Cdd:cd03340 469 GKWYGVDINNEGIADNFEAFVWEPSLVKINALTAATEAACLILSVD 514
|
|
| TCP1_alpha |
cd03335 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ... |
27-535 |
5.28e-105 |
|
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: 325.01 E-value: 5.28e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 27 RLMGLEALKSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGT 106
Cdd:cd03335 3 RTSGQDVRTQNVTAAMAIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDKEVGDGT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 107 TGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARIAIQHldkISDNVLVDINN--PEPLIQTAKTTLGSKVVNSCHRQ 184
Cdd:cd03335 83 TSVVIIAAELLKRANELVKQKIHPTTIISGYRLACKEAVKY---IKEHLSISVDNlgKESLINVAKTSMSSKIIGADSDF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 185 MAEIAVNAVLTVADM-ERRDV-----DFELIKVEGKvggRLEDTKLIKGVIVDKDFSHPQMPKEVLNAKIAILTCPFEpp 258
Cdd:cd03335 160 FANMVVDAILAVKTTnEKGKTkypikAVNILKAHGK---SAKESYLVNGYALNCTRASQGMPTRVKNAKIACLDFNLQ-- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 259 kpKTKHKLDV----TSVEDYKALQKYEKEKFEEMIAQIKETGANLAICQWGFDDEANHLLLQNGLPAVRWVGGPEIELIA 334
Cdd:cd03335 235 --KTKMKLGVqvvvTDPEKLEKIRQRESDITKERIKKILAAGANVVLTTGGIDDMCLKYFVEAGAMAVRRVKKEDLRRIA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 335 IATGGRIVPRFSELTSE------KLGFAGVVREISFGttKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCV 408
Cdd:cd03335 313 KATGATLVSTLANLEGEetfdpsYLGEAEEVVQERIG--DDELILIKGTKKRSSASIILRGANDFMLDEMERSLHDALCV 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 409 IRNLIRDNRVVYGGGAAEisCALAVSQE--ADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRAR----QV 482
Cdd:cd03335 391 VKRTLESNSVVPGGGAVE--TALSIYLEnfATTLGSREQLAIAEFAEALLVIPKTLAVNAAKDATELVAKLRAYhaaaQV 468
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 51890219 483 KESNPAL---GIDcLHKGS--NDMQYQhVIETLIGKKQQISLATQMVRMILKIDDIRK 535
Cdd:cd03335 469 KPDKKHLkwyGLD-LINGKvrDNLEAG-VLEPTVSKIKSLKFATEAAITILRIDDLIK 524
|
|
| chap_CCT_eta |
TIGR02345 |
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ... |
15-537 |
3.29e-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: 322.86 E-value: 3.29e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 15 PFLIIKDQDRKSRlmGLEALKSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVEL 94
Cdd:TIGR02345 3 TIVLLKEGTDTSQ--GKGQLISNINACVAIAEALKTTLGPRGMDKLIVGSNGKATISNDGATILKLLDIVHPAAKTLVDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 95 SKSQDDEIGDGTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARIAIQHLDKISDNV-LVDINNPEPLIQTAKTTL 173
Cdd:TIGR02345 81 AKSQDAEVGDGTTSVTILAGELLKEAKPFIEEGVHPQLIIRCYREALSLAVEKIKEIAVTIdEEKGEQRELLEKCAATAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 174 GSKVVNSCHRQMAEIAVNAVLTvadMERRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFS---HPQMPKEVLNAKIAI 250
Cdd:TIGR02345 161 SSKLISHNKEFFSKMIVDAVLS---LDRDDLDLKLIGIKKVQGGALEDSQLVNGVAFKKTFSyagFEQQPKKFANPKILL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 251 LTCPFEPPKPKTKHKLDVTSVEDYKALQKYEKEKFEEMIAQIKETGANLAICQWGFDDEANHLLLQNGLPAVRWVGGPEI 330
Cdd:TIGR02345 238 LNVELELKAEKDNAEIRVEDVEDYQAIVDAEWAIIFRKLEKIVESGANVVLSKLPIGDLATQYFADRDIFCAGRVSAEDL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 331 ELIAIATGGRIVPRFSELTSEKLGFAGVVREISFGttKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIR 410
Cdd:TIGR02345 318 KRVIKACGGSIQSTTSDLEADVLGTCALFEERQIG--SERYNYFTGCPHAKTCTIILRGGAEQFIEEAERSLHDAIMIVR 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 411 NLIRDNRVVYGGGAAEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKESNPAlG 490
Cdd:TIGR02345 396 RALKNKKIVAGGGAIEMELSKCLRDYSKTIDGKQQLIINAFAKALEIIPRQLCENAGFDSIEILNKLRSRHAKGGKWY-G 474
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 51890219 491 IDCLHKGSNDMQYQHVIETLIGKKQQISLATQMVRMILKIDD-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 |
3.60e-102 |
|
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: 317.82 E-value: 3.60e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 27 RLMGLEALKSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGT 106
Cdd:TIGR02340 7 RTSGQDVRTQNVTAAMAIANIVKTSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDREVGDGT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 107 TGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARIAIQHldkISDNVLVDINN--PEPLIQTAKTTLGSKVVNSCHRQ 184
Cdd:TIGR02340 87 TSVVIIAAELLKRADELVKNKIHPTSVISGYRLACKEAVKY---IKENLSVSVDElgREALINVAKTSMSSKIIGLDSDF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 185 MAEIAVNAVLTVADM-ERRDVDF--ELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKEVLNAKIAILTCPFEppkpK 261
Cdd:TIGR02340 164 FSNIVVDAVLAVKTTnENGETKYpiKAINILKAHGKSARESMLVKGYALNCTVASQQMPKRIKNAKIACLDFNLQ----K 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 262 TKHKLDVT-SVEDYKALQKYEKEKFE---EMIAQIKETGANLAICQWGFDDEANHLLLQNGLPAVRWVGGPEIELIAIAT 337
Cdd:TIGR02340 240 AKMALGVQiVVDDPEKLEQIRQREADitkERIKKILDAGANVVLTTGGIDDMCLKYFVEAGAMGVRRCKKEDLKRIAKAT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 338 GGRIVPRFSELTSE------KLGFAGVVREISFGttKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRN 411
Cdd:TIGR02340 320 GATLVSTLADLEGEetfeasYLGFADEVVQERIA--DDECILIKGTKKRKSASIILRGANDFMLDEMERSLHDALCVVKR 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 412 LIRDNRVVYGGGAAEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQ-------VKE 484
Cdd:TIGR02340 398 TLESNSVVPGGGAVEAALSIYLENFATTLGSREQLAIAEFARALLIIPKTLAVNAAKDSTELVAKLRAYHaaaqlkpEKK 477
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 51890219 485 SNPALGIDCLHKGSNDMQYQHVIETLIGKKQQISLATQMVRMILKIDD-IRKPGESEE 541
Cdd:TIGR02340 478 HLKWYGLDLVNGKIRDNKEAGVLEPTVSKVKSLKFATEAAITILRIDDlIKLNPEQSK 535
|
|
| TCP1_theta |
cd03341 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ... |
32-533 |
2.66e-99 |
|
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: 308.38 E-value: 2.66e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 32 EALKSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVV 111
Cdd:cd03341 8 EAVLRNIEACKELSQITRTSYGPNGMNKMVINHLEKLFVTSDAATILRELEVQHPAAKLLVMASQMQEEEIGDGTNLVVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 112 LAGALLEEAEQLLDRGIHPIRIADGYEQAARIAIQHLDKISDNVLVDINNPEPLIQTAKTTLGSKVV-NSCHrqMAEIAV 190
Cdd:cd03341 88 LAGELLEKAEELLRMGLHPSEIIEGYEKALKKALEILEELVVYKIEDLRNKEEVSKALKTAIASKQYgNEDF--LSPLVA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 191 NAVLTVADMERRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDfSHPQMpKEVLNAKIAILTCPFeppkpktkhkldvts 270
Cdd:cd03341 166 EACISVLPENIGNFNVDNIRVVKILGGSLEDSKVVRGMVFKRE-PEGSV-KRVKKAKVAVFSCPF--------------- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 271 vedykalqkyekekfeemiaqikETGANLAICQWGFDDEANHLLLQNGLPAVRWVGGPEIELIAIATGGRIVPRFSELTS 350
Cdd:cd03341 229 -----------------------DIGVNVIVAGGSVGDLALHYCNKYGIMVIKINSKFELRRLCRTVGATPLPRLGAPTP 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 351 EKLGFAGVVREISFGTTkdKMLVIEQCKNSRAV-TIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAEISC 429
Cdd:cd03341 286 EEIGYCDSVYVEEIGDT--KVVVFRQNKEDSKIaTIVLRGATQNILDDVERAIDDGVNVFKSLTKDGRFVPGAGATEIEL 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 430 ALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKESNPA-LGIDCLHKGSNDMQYQHVIE 508
Cdd:cd03341 364 AKKLKEYGEKTPGLEQYAIKKFAEAFEVVPRTLAENAGLDATEVLSELYAAHQKGNKSAgVDIESGDEGTKDAKEAGIFD 443
|
490 500
....*....|....*....|....*
gi 51890219 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 |
2.62e-97 |
|
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: 305.10 E-value: 2.62e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 32 EALKSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVV 111
Cdd:TIGR02346 18 EAVIKNIEACKELSQITRTSLGPNGMNKMVINHLEKLFVTNDAATILRELEVQHPAAKLLVMASEMQENEIGDGTNLVLV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 112 LAGALLEEAEQLLDRGIHPIRIADGYEQAARIAIQHLDKISDNVLVDINNPEPLIQTAKTTLGSKVVNScHRQMAEIAVN 191
Cdd:TIGR02346 98 LAGELLNKAEELIRMGLHPSEIIKGYEMALKKAMEILEELVVWEVKDLRDKDELIKALKASISSKQYGN-EDFLAQLVAQ 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 192 AVLTVADMERRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFShpQMPKEVLNAKIAILTCPFEPPKPKTKHKLDVTSV 271
Cdd:TIGR02346 177 ACSTVLPKNPQNFNVDNIRVCKILGGSLSNSEVLKGMVFNREAE--GSVKSVKNAKVAVFSCPLDTATTETKGTVLIHNA 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 272 EDYKALQKYEKEKFEEMIAQIKETGANLAICQWGFDDEANHLLLQNGLPAVRWVGGPEIELIAIATGGRIVPRFSELTSE 351
Cdd:TIGR02346 255 EELLNYSKGEENQIEAMIKAIADSGVNVIVTGGSVGDMALHYLNKYNIMVLKIPSKFELRRLCKTVGATPLPRLGAPTPE 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 352 KLGFAGVVREISFGTtkDKMLVIEQCK-NSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAEISCA 430
Cdd:TIGR02346 335 EIGYVDSVYVSEIGG--DKVTVFKQENgDSKISTIILRGSTDNLLDDIERAIDDGVNTVKALVKDGRLLPGAGATEIELA 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 431 LAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQvKESNPALGID--CLHKGSNDMQYQHVIE 508
Cdd:TIGR02346 413 SRLTKYGEKLPGLDQYAIKKFAEAFEIIPRTLAENAGLNANEVIPKLYAAH-KKGNKSKGIDieAESDGVKDASEAGIYD 491
|
490 500
....*....|....*....|....*
gi 51890219 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 |
5.43e-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: 293.69 E-value: 5.43e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 18 IIKDQDRKSRlmGLEALKSHIMAAKAVANTMRTSLGPNGLDKMMV--DKDGDVTVTNDGATILSMMDVDHQIAKLMVELS 95
Cdd:TIGR02341 2 IFKDGADEER--AENARLSSFVGAIAIGDLVKSTLGPKGMDKILQssSSDASIMVTNDGATILKSIGVDNPAAKVLVDMS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 96 KSQDDEIGDGTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARIAIQHLDKIS-DNVLVDINNPEPLIQTAKTTLG 174
Cdd:TIGR02341 80 KVQDDEVGDGTTSVTVLAAELLREAEKLINQKIHPQTIIAGYREATKAARDALLKSAvDNGSDEVKFRQDLMNIARTTLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 175 SKVVNSCHRQMAEIAVNAVLTVadmeRRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQmPKEVLNAKIAILTCP 254
Cdd:TIGR02341 160 SKILSQHKDHFAQLAVDAVLRL----KGSGNLEAIQIIKKLGGSLADSYLDEGFLLDKKIGVNQ-PKRIENAKILIANTG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 255 FEPPKPKT-KHKLDVTSVEDYKALQKYEKEKFEEMIAQIKETGANLAICQWGFDDEANHLLLQNGLPAVRWVGGPEIELI 333
Cdd:TIGR02341 235 MDTDKVKIfGSRVRVDSTAKVAELEHAEKEKMKEKVEKILKHGINCFINRQLIYNYPEQLFADAGVMAIEHADFEGVERL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 334 AIATGGRIVPRFSELTSEKLGFAGVVREISFGttKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLI 413
Cdd:TIGR02341 315 ALVTGGEIVSTFDHPELVKLGSCDLIEEIMIG--EDKLLKFSGVKLGEACTIVLRGATQQILDEAERSLHDALCVLSQTV 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 414 RDNRVVYGGGAAEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRArQVKESNPALGIDC 493
Cdd:TIGR02341 393 KESRTVLGGGCSEMLMSKAVTQEAQRTPGKEALAVEAFARALRQLPTIIADNAGFDSAELVAQLRA-AHYNGNTTMGLDM 471
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 51890219 494 LHKGSNDMQYQHVIETLIGKKQQISLATQMVRMILKIDDIRK 535
Cdd:TIGR02341 472 NEGTIADMRQLGITESYKVKRAVVSSAAEAAEVILRVDNIIK 513
|
|
| chap_CCT_zeta |
TIGR02347 |
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ... |
33-539 |
1.47e-85 |
|
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT zeta chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.
Pssm-ID: 274088 [Multi-domain] Cd Length: 531 Bit Score: 274.69 E-value: 1.47e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 33 ALKSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVVL 112
Cdd:TIGR02347 17 ALMMNINAARGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEMQIQHPTASMIARAATAQDDITGDGTTSTVLL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 113 AGALLEEAEQLLDRGIHPIRIADGYEQAARIAIQHLDKISDNVlVDINNPEPLIQTAKTTLGSKVVNSCHRQMAEIAVNA 192
Cdd:TIGR02347 97 IGELLKQAERYILEGVHPRIITEGFEIARKEALQFLDKFKVKK-EDEVDREFLLNVARTSLRTKLPADLADQLTEIVVDA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 193 VLTVADMErRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKEVLNAKIAILTCPFEPPKPKTKHKLDVTSVE 272
Cdd:TIGR02347 176 VLAIKKDG-EDIDLFMVEIMEMKHKSATDTTLIRGLVLDHGARHPDMPRRVKNAYILTCNVSLEYEKTEVNSGFFYSSAE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 273 DYKALQKYEKEKFEEMIAQIKE-------TGAN---LAICQWGFDDEANHLLLQNGLPAVRWVGGPEIELIAIATGGRIV 342
Cdd:TIGR02347 255 QREKLVKAERKFVDDRVKKIIElkkkvcgKSPDkgfVVINQKGIDPPSLDLLAKEGIMALRRAKRRNMERLTLACGGEAL 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 343 PRFSELTSEKLGFAGVVREISFGttKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGG 422
Cdd:TIGR02347 335 NSVEDLTPECLGWAGLVYETTIG--EEKYTFIEECKNPKSCTILIKGPNDHTIAQIKDAVRDGLRAVKNAIEDKCVVPGA 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 423 GAAEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRArQVKESNPALGIDCLHKGSNDMQ 502
Cdd:TIGR02347 413 GAFEIAAYRHLKEYKKSVKGKAKLGVEAFANALLVIPKTLAENSGFDAQDTLVKLED-EHDEGGEVVGVDLNTGEPIDPE 491
|
490 500 510
....*....|....*....|....*....|....*..
gi 51890219 503 YQHVIETLIGKKQQISLATQMVRMILKIDDIRKPGES 539
Cdd:TIGR02347 492 IKGIWDNYRVKKQLIQSATVIASQLLLVDEVMRAGRS 528
|
|
| TCP1_zeta |
cd03342 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
32-537 |
1.83e-83 |
|
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: 267.59 E-value: 1.83e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 32 EALKSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVV 111
Cdd:cd03342 12 QALAVNISAAKGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLSEMQIQHPTASMIARAATAQDDITGDGTTSNVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 112 LAGALLEEAEQLLDRGIHPIRIADGYEQAARIAIQHLDKISDNVLVDiNNPEPLIQTAKTTLGSKVVNSCHRQMAEIAVN 191
Cdd:cd03342 92 LIGELLKQAERYIQEGVHPRIITEGFELAKNKALKFLESFKVPVEID-TDRELLLSVARTSLRTKLHADLADQLTEIVVD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 192 AVLTVadmERRDVDFELIKVE-GKVGGRLE-DTKLIKGVIVDKDFSHPQMPKEVLNAkiAILTCPFeppkpktkhkldvt 269
Cdd:cd03342 171 AVLAI---YKPDEPIDLHMVEiMQMQHKSDsDTKLIRGLVLDHGARHPDMPKRVENA--YILTCNV-------------- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 270 SVEdykalqkYEK-EKFEEMIaqiketgANLAICQWGFDDEANHLLLQNGLPAVRWVGGPEIELIAIATGGRIVPRFSEL 348
Cdd:cd03342 232 SLE-------YEKtEVNSGFF-------YSVVINQKGIDPPSLDMLAKEGILALRRAKRRNMERLTLACGGVAMNSVDDL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 349 TSEKLGFAGVVREISFGttKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAEIS 428
Cdd:cd03342 298 SPECLGYAGLVYERTLG--EEKYTFIEGVKNPKSCTILIKGPNDHTITQIKDAIRDGLRAVKNAIEDKCVVPGAGAFEVA 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 429 CALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRaRQVKESNPALGIDCLHKGSNDMQYQHVIE 508
Cdd:cd03342 376 LYAHLKEFKKSVKGKAKLGVQAFADALLVIPKTLAENSGLDVQETLVKLQ-DEYAEGGQVGGVDLDTGEPMDPESEGIWD 454
|
490 500
....*....|....*....|....*....
gi 51890219 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 |
3.98e-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: 239.29 E-value: 3.98e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 163 EPLIQTAKTTLGSKVvNSCHRQMAEIAVNAVLTVADMERrDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKE 242
Cdd:cd03333 2 ELLLQVATTSLNSKL-SSWDDFLGKLVVDAVLKVGPDNR-MDDLGVIKVEKIPGGSLEDSELVVGVVFDKGYASPYMPKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 243 VLNAKIAILTCPFEPpkpktkhkldvtsvedykalqkyekekfeemiaqiketganLAICQWGFDDEANHLLLQNGLPAV 322
Cdd:cd03333 80 LENAKILLLDCPLEY-----------------------------------------VVIAEKGIDDLALHYLAKAGIMAV 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 323 RWVGGPEIELIAIATGGRIVPRFSELTSEKLGFAGVVREISFGTtkDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSL 402
Cdd:cd03333 119 RRVKKEDLERIARATGATIVSSLEDLTPEDLGTAELVEETKIGE--EKLTFIEGCKGGKAATILLRGATEVELDEVKRSL 196
|
250
....*....|...
gi 51890219 403 HDALCVIRNLIRD 415
Cdd:cd03333 197 HDALCAVRAAVEE 209
|
|
| Fab1_TCP |
cd03334 |
TCP-1 like domain of the eukaryotic phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinase Fab1. ... |
187-413 |
1.27e-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: 76.88 E-value: 1.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 187 EIAVNAVLTVADMERRDVDF-------ELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKEVLNAKIAILTCPFEPPK 259
Cdd:cd03334 21 DILLPLVWKAASNVKPDVRAgddmdirQYVKIKKIPGGSPSDSEVVDGVVFTKNVAHKRMPSKIKNPRILLLQGPLEYQR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 260 PKTKhkldVTSVEDYKAlqkYEKEKFEEMIAQIKETGANLAICQWGFDDEANHLLLQNGLPAVRWVGGPEIELIAIATGG 339
Cdd:cd03334 101 VENK----LLSLDPVIL---QEKEYLKNLVSRIVALRPDVILVEKSVSRIAQDLLLEAGITLVLNVKPSVLERISRCTGA 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 51890219 340 RIVPRFSEL-TSEKLGFAGVVREISF----GTTKDKMLvIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLI 413
Cdd:cd03334 174 DIISSMDDLlTSPKLGTCESFRVRTYveehGRSKTLMF-FEGCPKELGCTILLRGGDLEELKKVKRVVEFMVFAAYHLK 251
|
|
| GroEL |
cd03344 |
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ... |
30-501 |
1.81e-14 |
|
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings, each composed of 7-9 subunits. The symmetry of type I is seven-fold and they are found in eubacteria (GroEL) and in organelles of eubacterial descent (hsp60 and RBP). With the aid of cochaperonin GroES, GroEL encapsulates non-native substrate proteins inside the cavity of the GroEL-ES complex and promotes folding by using energy derived from ATP hydrolysis.
Pssm-ID: 239460 Cd Length: 520 Bit Score: 75.96 E-value: 1.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 30 GLEALKSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATI---LSMMD-VDHQIAKLMVELSKSQDDEIGDG 105
Cdd:cd03344 6 GEEARKALLRGVNKLADAVKVTLGPKGRNVVIEKSFGSPKITKDGVTVakeIELEDpFENMGAQLVKEVASKTNDVAGDG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 106 TTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARIAIQHLDKISdnvlVDINNPEPLIQTAKT------TLGSKVVN 179
Cdd:cd03344 86 TTTATVLARAIIKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLS----KPVKTKEEIAQVATIsangdeEIGELIAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 180 SchrqMAEIAVNAVLTVADmerrdvdfelikvegkvGGRLEDT-KLIKGVIVDKDFSHPQMpkeVLNAKIAIltCPFEpp 258
Cdd:cd03344 162 A----MEKVGKDGVITVEE-----------------GKTLETElEVVEGMQFDRGYLSPYF---VTDPEKME--VELE-- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 259 KPK---TKHKLDvtsvedykalqkyekeKFEEMIA---QIKETGANLAICQWGFDDEANHLL----LQNGLPAVRwVGGP 328
Cdd:cd03344 214 NPYillTDKKIS----------------SIQELLPileLVAKAGRPLLIIAEDVEGEALATLvvnkLRGGLKVCA-VKAP 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 329 E--------IELIAIATGGRIVP-----RFSELTSEKLGFAGVVReisfgTTKDKMLV-------------IEQCKNSRA 382
Cdd:cd03344 277 GfgdrrkamLEDIAILTGGTVISeelglKLEDVTLEDLGRAKKVV-----VTKDDTTIiggagdkaaikarIAQIRKQIE 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 383 VT----------------------IFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNrVVYGGGAAEISCALAVSQEADKC 440
Cdd:cd03344 352 ETtsdydkeklqerlaklsggvavIKVGGATEVELKEKKDRVEDALNATRAAVEEG-IVPGGGVALLRASPALDKLKALN 430
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 51890219 441 PtLEQYAMRAFADALEVIPMALSENSGMNPiqtmtEVRARQVKESNPALGIDCLHKGSNDM 501
Cdd:cd03344 431 G-DEKLGIEIVRRALEAPLRQIAENAGVDG-----SVVVEKVLESPDGFGYDAATGEYVDM 485
|
|
| GroEL |
TIGR02348 |
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ... |
32-213 |
1.49e-12 |
|
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: 70.01 E-value: 1.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 32 EALKSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQI----AKLMVELSKSQDDEIGDGTT 107
Cdd:TIGR02348 9 EARKALLRGVDKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDKFenmgAQLVKEVASKTNDVAGDGTT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 108 GVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARIAIQHLDKISdnvlVDINNPEPLIQTAKTTLGS--KVVNSCHRQM 185
Cdd:TIGR02348 89 TATVLAQAIVKEGLKNVAAGANPIELKRGIEKAVEAVVEELKKLS----KPVKGKKEIAQVATISANNdeEIGSLIAEAM 164
|
170 180
....*....|....*....|....*...
gi 51890219 186 AEIAVNAVLTVAdmERRDVDFELIKVEG 213
Cdd:TIGR02348 165 EKVGKDGVITVE--ESKSLETELEVVEG 190
|
|
| PLN03167 |
PLN03167 |
Chaperonin-60 beta subunit; Provisional |
33-254 |
1.85e-10 |
|
Chaperonin-60 beta subunit; Provisional
Pssm-ID: 215611 [Multi-domain] Cd Length: 600 Bit Score: 63.40 E-value: 1.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 33 ALKSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQI----AKLMVELSKSQDDEIGDGTTG 108
Cdd:PLN03167 67 AIKKLQAGVNKLADLVGVTLGPKGRNVVLESKYGSPKIVNDGVTVAKEVELEDPVenigAKLVRQAAAKTNDLAGDGTTT 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 109 VVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARIAIQHLDKIS----DNVLVDI------NNPE--PLIQTAKTTLGSK 176
Cdd:PLN03167 147 SVVLAQGLIAEGVKVVAAGANPVQITRGIEKTAKALVKELKKMSkeveDSELADVaavsagNNYEvgNMIAEAMSKVGRK 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 177 -VVNSCHRQMAEIAVNAV------------LTVADMERRDVDFE---LIKVEGKVG------GRLEDTklIKG----VIV 230
Cdd:PLN03167 227 gVVTLEEGKSAENNLYVVegmqfdrgyispYFVTDSEKMSVEYDnckLLLVDKKITnardliGILEDA--IRGgyplLII 304
|
250 260
....*....|....*....|....*....
gi 51890219 231 DKDFSHPQMPKEVLNA-----KIAILTCP 254
Cdd:PLN03167 305 AEDIEQEALATLVVNKlrgslKIAALKAP 333
|
|
| groEL |
PRK12850 |
chaperonin GroEL; Reviewed |
18-213 |
2.14e-10 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237231 Cd Length: 544 Bit Score: 63.20 E-value: 2.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 18 IIKDQDRKSRLM-GLEALkshimaakavANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKL---MV- 92
Cdd:PRK12850 6 IRFSTDARDRLLrGVNIL----------ANAVKVTLGPKGRNVVLEKSFGAPRITKDGVTVAKEIELEDKFENMgaqMVk 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 93 ELSKSQDDEIGDGTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARIAIQHLDKISdnvlVDINNPEPLIQTA--- 169
Cdd:PRK12850 76 EVASKTNDLAGDGTTTATVLAQAIVREGAKLVAAGMNPMDLKRGIDLAVAAVVDELKKIA----KKVTSSKEIAQVAtis 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 51890219 170 ---KTTLGSKVVnschRQMAEIAVNAVLTVAdmERRDVDFELIKVEG 213
Cdd:PRK12850 152 angDESIGEMIA----EAMDKVGKEGVITVE--EAKTLGTELDVVEG 192
|
|
| PTZ00114 |
PTZ00114 |
Heat shock protein 60; Provisional |
25-469 |
1.41e-09 |
|
Heat shock protein 60; Provisional
Pssm-ID: 185455 Cd Length: 555 Bit Score: 60.70 E-value: 1.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 25 KSRLMGLEALKSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATIL-------SMMDVDhqiAKLMVELSKS 97
Cdd:PTZ00114 15 KEIRFGDEARQSLLKGIERLADAVAVTLGPKGRNVIIEQEYGSPKITKDGVTVAkaiefsdRFENVG---AQLIRQVASK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 98 QDDEIGDGTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARIAIQHLDKISDNVlvdiNNPEPLIQTAKTT----- 172
Cdd:PTZ00114 92 TNDKAGDGTTTATILARAIFREGCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQSRPV----KTKEDILNVATISangdv 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 173 -LGSKVVNSchrqMAEIAVNAVLTVADmerrdvdfelikvegkvGGRLEDT-KLIKGVIVDKDFSHPQMpkeVLNAK--I 248
Cdd:PTZ00114 168 eIGSLIADA----MDKVGKDGTITVED-----------------GKTLEDElEVVEGMSFDRGYISPYF---VTNEKtqK 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 249 AILTCPFeppkpktkhkldvTSVEDYKALQkyekekfeemIAQI-------KETGANLAICQWGFDDEA------NHllL 315
Cdd:PTZ00114 224 VELENPL-------------ILVTDKKISS----------IQSIlpilehaVKNKRPLLIIAEDVEGEAlqtliiNK--L 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 316 QNGLP--AVRWVGGPE-----IELIAIATGGRIVPR------FSELTSEKLGFAGVV-----REISFGTTKDKMLVIEQC 377
Cdd:PTZ00114 279 RGGLKvcAVKAPGFGDnrkdiLQDIAVLTGATVVSEdnvglkLDDFDPSMLGSAKKVtvtkdETVILTGGGDKAEIKERV 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 378 KNSRA-------------------------VTIFIRGGNKMIIEEAKRSLHDALCVIRNLIrDNRVVYGGGAAEI--SCA 430
Cdd:PTZ00114 359 ELLRSqierttseydkeklkerlaklsggvAVIKVGGASEVEVNEKKDRIEDALNATRAAV-EEGIVPGGGVALLraSKL 437
|
490 500 510
....*....|....*....|....*....|....*....
gi 51890219 431 LAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMN 469
Cdd:PTZ00114 438 LDKLEEDNELTPDQRTGVKIVRNALRLPTKQIAENAGVE 476
|
|
| PRK14104 |
PRK14104 |
chaperonin GroEL; Provisional |
30-213 |
3.41e-09 |
|
chaperonin GroEL; Provisional
Pssm-ID: 172594 Cd Length: 546 Bit Score: 59.27 E-value: 3.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 30 GLEALKSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQI----AKLMVELSKSQDDEIGDG 105
Cdd:PRK14104 9 GVDARDRMLRGVDILANAVKVTLGPKGRNVVLDKSFGAPRITKDGVTVAKEIELEDKFenmgAQMVREVASKSADAAGDG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 106 TTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARIAIQHLDKISDNVLVdiNNPEPLIQTAKTTLGSKVVNSCHRQM 185
Cdd:PRK14104 89 TTTATVLAQAIVREGAKSVAAGMNPMDLKRGIDLAVEAVVADLVKNSKKVTS--NDEIAQVGTISANGDAEIGKFLADAM 166
|
170 180
....*....|....*....|....*...
gi 51890219 186 AEIAVNAVLTVAdmERRDVDFELIKVEG 213
Cdd:PRK14104 167 KKVGNEGVITVE--EAKSLETELDVVEG 192
|
|
| groEL |
PRK12851 |
chaperonin GroEL; Reviewed |
41-155 |
7.94e-09 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 171770 Cd Length: 541 Bit Score: 58.21 E-value: 7.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 41 AKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQI----AKLMVELSKSQDDEIGDGTTGVVVLAGAL 116
Cdd:PRK12851 20 VNILADAVKVTLGPKGRNVVIDKSFGAPTITNDGVTIAKEIELEDKFenmgAQMVREVASKTNDVAGDGTTTATVLAQAI 99
|
90 100 110
....*....|....*....|....*....|....*....
gi 51890219 117 LEEAEQLLDRGIHPIRIADGYEQAARIAIQHLDKISDNV 155
Cdd:PRK12851 100 VREGAKAVAAGANPMDLKRGIDRAVAAVVEELKANARPV 138
|
|
| groEL |
PRK12849 |
chaperonin GroEL; Reviewed |
43-213 |
1.01e-08 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237230 Cd Length: 542 Bit Score: 57.89 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 43 AVANTMRTSLGPNGLDkMMVDKD-GDVTVTNDGATILSMMDVDHQI----AKLMVELSKSQDDEIGDGTTGVVVLAGALL 117
Cdd:PRK12849 21 KLADAVKVTLGPKGRN-VVIDKSfGAPTITKDGVSIAKEIELEDPFenlgAQLVKEVASKTNDVAGDGTTTATVLAQALV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 118 EEAEQLLDRGIHPIRIADGYEQAARIAIQHLDKISdnvlVDINNPEPLIQTAKT------TLGSKVVnschRQMAEIAVN 191
Cdd:PRK12849 100 QEGLKNVAAGANPMDLKRGIDKAVEAVVEELKALA----RPVSGSEEIAQVATIsangdeEIGELIA----EAMEKVGKD 171
|
170 180
....*....|....*....|..
gi 51890219 192 AVLTVAdmERRDVDFELIKVEG 213
Cdd:PRK12849 172 GVITVE--ESKTLETELEVTEG 191
|
|
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
43-169 |
2.81e-08 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 56.29 E-value: 2.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 43 AVANTMRTSLGPNG----LDKmmvdKDGDVTVTNDGATILSMMDVDHQI----AKLMVELSKSQDDEIGDGTTGVVVLAG 114
Cdd:PRK00013 21 KLADAVKVTLGPKGrnvvLEK----SFGAPTITKDGVTVAKEIELEDPFenmgAQLVKEVASKTNDVAGDGTTTATVLAQ 96
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 51890219 115 ALLEEAEQLLDRGIHPIRIADGYEQAARIAIQHLDKISdnvlVDINNPEPLIQTA 169
Cdd:PRK00013 97 AIVREGLKNVAAGANPMDLKRGIDKAVEAAVEELKKIS----KPVEDKEEIAQVA 147
|
|
| groEL |
PRK12852 |
chaperonin GroEL; Reviewed |
44-213 |
2.71e-07 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237232 Cd Length: 545 Bit Score: 53.31 E-value: 2.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 44 VANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQI----AKLMVELSKSQDDEIGDGTTGVVVLAGALLEE 119
Cdd:PRK12852 23 LANAVKVTLGPKGRNVVIEKSFGAPRITKDGVTVAKEIELEDKFenmgAQMVREVASKTNDLAGDGTTTATVLAQAIVRE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 120 AEQLLDRGIHPIRIADGYEQAARIAIQHLDKISDNVL--VDINNPEPLIQTAKTTLGSKVVNSchrqMAEIAVNAVLTVA 197
Cdd:PRK12852 103 GAKAVAAGMNPMDLKRGIDIAVAAVVKDIEKRAKPVAssAEIAQVGTISANGDAAIGKMIAQA----MQKVGNEGVITVE 178
|
170
....*....|....*.
gi 51890219 198 DMERRDVDFELikVEG 213
Cdd:PRK12852 179 ENKSLETEVDI--VEG 192
|
|
| groEL |
CHL00093 |
chaperonin GroEL |
20-154 |
1.36e-06 |
|
chaperonin GroEL
Pssm-ID: 177025 Cd Length: 529 Bit Score: 50.87 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 20 KDQDRKSRLMGLEALkshimaAKAVANTmrtsLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVEL----- 94
Cdd:CHL00093 8 QDNARRALERGMDIL------AEAVSVT----LGPKGRNVVLEKKYGSPQIVNDGVTIAKEIELEDHIENTGVALirqaa 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 51890219 95 SKSqDDEIGDGTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARIAIQhldKISDN 154
Cdd:CHL00093 78 SKT-NDVAGDGTTTATVLAYAIVKQGMKNVAAGANPISLKRGIEKATQYVVS---QIAEY 133
|
|
| |
