|
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: 1090.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 10 DEYGRPFLIIKDQDRKSRLMGLEALKSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTITNDGATILSMMDVDHQIAK 89
Cdd:cd03339 1 DEYGRPFIIVREQEKKKRLKGLEAHKSHILAAKSVANILRTSLGPRGMDKILVSPDGEVTVTNDGATILEKMDVDHQIAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 90 LMVELSKSQDDEIGDGTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARIAIQHLDKISDKVLVDINNPEPLIQTA 169
Cdd:cd03339 81 LLVELSKSQDDEIGDGTTGVVVLAGALLEQAEKLLDRGIHPIRIADGYEQACKIAVEHLEEIADKIEFSPDNKEPLIQTA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 170 KTTLGSKVINSCHRQMAEIAVNAVLTVADMERRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKKVVDAKIA 249
Cdd:cd03339 161 MTSLGSKIVSRCHRQFAEIAVDAVLSVADLERKDVNFELIKVEGKVGGRLEDTKLVKGIVIDKDFSHPQMPKEVKDAKIA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 250 ILTCPFEPPKPKTKHKLDVMSVEDYKALQKYEKEKFEEMIKQIKETGANLAICQWGFDDEANHLLLQNGLPAVRWVGGPE 329
Cdd:cd03339 241 ILTCPFEPPKPKTKHKLDITSVEDYKKLQEYEQKYFREMVEQVKDAGANLVICQWGFDDEANHLLLQNGLPAVRWVGGVE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 330 IELIAIATGGRIVPRFSELTSEKLGFAGVVQEISFGTTKDKMLVIEKCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVI 409
Cdd:cd03339 321 IELIAIATGGRIVPRFEDLSPEKLGKAGLVREISFGTTKDKMLVIEGCPNSKAVTIFIRGGNKMIIEEAKRSLHDALCVV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 410 RNLIRDNRVVYGGGAAEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKESNPAL 489
Cdd:cd03339 401 RNLIRDNRIVYGGGAAEISCSLAVEKAADKCSGIEQYAMRAFADALESIPLALAENSGLNPIETLSEVKARQVKEKNPHL 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 6671702 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: 1005.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 6 TLAFDEYGRPFLIIKDQDRKSRLMGLEALKSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTITNDGATILSMMDVDH 85
Cdd:TIGR02343 1 ILAFDEYGRPFIIIKDQDNKKRLKGLEAKKSNIAAAKSVASILRTSLGPKGMDKMLISPDGDITVTNDGATILSQMDVDN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 86 QIAKLMVELSKSQDDEIGDGTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARIAIQHLDKISDKVLVDINNPEPL 165
Cdd:TIGR02343 81 QIAKLMVELSKSQDDEIGDGTTGVVVLAGALLEQAEELLDKGIHPIKIADGFEEAARIAVEHLEEISDEISADNNNREPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 166 IQTAKTTLGSKVINSCHRQMAEIAVNAVLTVADMERRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKKVVD 245
Cdd:TIGR02343 161 IQAAKTSLGSKIVSKCHRRFAEIAVDAVLNVADMERRDVDFDLIKVEGKVGGSLEDTKLIKGIIIDKDFSHPQMPKEVED 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 246 AKIAILTCPFEPPKPKTKHKLDVMSVEDYKALQKYEKEKFEEMIKQIKETGANLAICQWGFDDEANHLLLQNGLPAVRWV 325
Cdd:TIGR02343 241 AKIAILTCPFEPPKPKTKHKLDISSVEEYKKLQKYEQQKFKEMIDDIKKSGANLVICQWGFDDEANHLLLQNDLPAVRWV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 326 GGPEIELIAIATGGRIVPRFSELTSEKLGFAGVVQEISFGTTKDKMLVIEKCKNSRAVTIFIRGGNKMIIEEAKRSLHDA 405
Cdd:TIGR02343 321 GGQELELIAIATGGRIVPRFQELSKDKLGKAGLVREISFGTTKDRMLVIEQCKNSKAVTIFIRGGNKMIIEEAKRSIHDA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 406 LCVIRNLIRDNRVVYGGGAAEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKES 485
Cdd:TIGR02343 401 LCVVRNLIKDSRIVYGGGAAEISCSLAVSQEADKYPGVEQYAIRAFADALETIPMALAENSGLDPIGTLSTLKSLQLKEK 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 6671702 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: 590.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 25 KSRLMGLEALKSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTITNDGATILSMMDVDHQIAKLMVELSKSQDDEIGD 104
Cdd:cd00309 1 KEREFGEEARLSNINAAKALADAVKTTLGPKGMDKMLVDSLGDPTITNDGATILKEIEVEHPAAKLLVEVAKSQDDEVGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 105 GTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARIAIQHLDKISDKvlVDINNPEPLIQTAKTTLGSKVINSCHRQ 184
Cdd:cd00309 81 GTTTVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVP--IDVEDREELLKVATTSLNSKLVSGGDDF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 185 MAEIAVNAVLTVADMErRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKKVVDAKIAILTCPFEPpkpktkh 264
Cdd:cd00309 159 LGELVVDAVLKVGKEN-GDVDLGVIRVEKKKGGSLEDSELVVGMVFDKGYLSPYMPKRLENAKILLLDCKLEY------- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 265 kldvmsvedykalqkyekekfeemikqiketganLAICQWGFDDEANHLLLQNGLPAVRWVGGPEIELIAIATGGRIVPR 344
Cdd:cd00309 231 ----------------------------------VVIAEKGIDDEALHYLAKLGIMAVRRVRKEDLERIAKATGATIVSR 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 345 FSELTSEKLGFAGVVQEISFGttKDKMLVIEKCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGA 424
Cdd:cd00309 277 LEDLTPEDLGTAGLVEETKIG--DEKYTFIEGCKGGKVATILLRGATEVELDEAERSLHDALCAVRAAVEDGGIVPGGGA 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 425 AEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKESNPAlGIDCLHKGSNDMQYQ 504
Cdd:cd00309 355 AEIELSKALEELAKTLPGKEQLGIEAFADALEVIPRTLAENAGLDPIEVVTKLRAKHAEGGGNA-GGDVETGEIVDMKEA 433
|
490 500
....*....|....*....|....*....
gi 6671702 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: 553.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 44 VANTMRTSLGPNGLDKMMVDKDGDVTITNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVVLAGALLEEAEQL 123
Cdd:pfam00118 1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELEIQHPAAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEEAEKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 124 LDRGIHPIRIADGYEQAARIAIQHLDKIsDKVLVDINNPEPLIQTAKTTLGSKVINSCHRQMAEIAVNAVLTVADmERRD 203
Cdd:pfam00118 81 LAAGVHPTTIIEGYEKALEKALEILDSI-ISIPVEDVDREDLLKVARTSLSSKIISRESDFLAKLVVDAVLAIPK-NDGS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 204 VDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKKVVDAKIAILTCPFEPPKPKTKHKLDVMSVEDYKALQKYEKE 283
Cdd:pfam00118 159 FDLGNIGVVKILGGSLEDSELVDGVVLDKGPLHPDMPKRLENAKVLLLNCSLEYEKTETKATVVLSDAEQLERFLKAEEE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 284 KFEEMIKQIKETGANLAICQWGFDDEANHLLLQNGLPAVRWVGGPEIELIAIATGGRIVPRFSELTSEKLGFAGVVQEIS 363
Cdd:pfam00118 239 QILEIVEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMALRRVKKRDLERLAKATGARAVSSLDDLTPDDLGTAGKVEEEK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 364 FGttKDKMLVIEKCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAEISCALAVSQEADKCPTL 443
Cdd:pfam00118 319 IG--DEKYTFIEGCKSPKAATILLRGATDHVLDEIERSIHDALCVVKNAIEDPRVVPGGGAVEMELARALREYAKSVSGK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 444 EQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQvKESNPALGIDCLHKGSNDMQYQHVIETLIGKKQQISLATQM 523
Cdd:pfam00118 397 EQLAIEAFAEALEVIPKTLAENAGLDPIEVLAELRAAH-ASGEKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKSATEA 475
|
490
....*....|
gi 6671702 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: 539.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 15 PFLIIKDQdrKSRLMGLEALKSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTITNDGATILSMMDVDHQIAKLMVEL 94
Cdd:NF041082 2 PILILKEG--TQRTSGRDAQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDVVITNDGVTILKEMDIEHPAAKMIVEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 95 SKSQDDEIGDGTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARIAIQHLDKISDKvlVDINNPEPLIQTAKTTLG 174
Cdd:NF041082 80 AKTQDDEVGDGTTTAVVLAGELLKKAEELLDQDIHPTIIAEGYRLAAEKALEILDEIAIK--VDPDDKETLKKIAATAMT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 175 SKVINSCHRQMAEIAVNAVLTVADME-RRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKKVVDAKIAILTC 253
Cdd:NF041082 158 GKGAEAAKDKLADLVVDAVKAVAEKDgGYNVDLDNIKVEKKVGGSIEDSELVEGVVIDKERVHPGMPKRVENAKIALLDA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 254 PFEPPKPKTKHKLDVMSVEDYKALQKYEKEKFEEMIKQIKETGANLAICQWGFDDEANHLLLQNGLPAVRWVGGPEIELI 333
Cdd:NF041082 238 PLEVKKTEIDAKISITDPDQLQAFLDQEEKMLKEMVDKIADSGANVVFCQKGIDDLAQHYLAKEGILAVRRVKKSDMEKL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 334 AIATGGRIVPRFSELTSEKLGFAGVVQEISFGttKDKMLVIEKCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLI 413
Cdd:NF041082 318 AKATGARIVTSIDDLSPEDLGYAGLVEERKVG--GDKMIFVEGCKNPKAVTILLRGGTEHVVDEVERALEDALRVVRVVL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 414 RDNRVVYGGGAAEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKESNPAlGIDC 493
Cdd:NF041082 396 EDGKVVAGGGAPEVELALRLREYAASVGGREQLAIEAFAEALEIIPRTLAENAGLDPIDALVELRSAHEKGNKTA-GLDV 474
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 6671702 494 LHKGSNDMQYQHVIETLIGKKQQISLATQMVRMILKIDDI 533
Cdd:NF041082 475 YTGKVVDMLEIGVVEPLRVKTQAIKSATEAAVMILRIDDV 514
|
|
| 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 6671702 17 LIIKDqdRKSRLMGLEALKSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTITNDGATILSMMDVDHQIAKLMVELSK 96
Cdd:cd03343 2 LILKE--GTQRTSGRDAQRMNIAAAKAVAEAVRTTLGPKGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 97 SQDDEIGDGTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARIAIQHLDKISDKvlVDINNPEPLIQTAKTTLGSK 176
Cdd:cd03343 80 TQDEEVGDGTTTAVVLAGELLEKAEDLLDQNIHPTVIIEGYRLAAEKALELLDEIAIK--VDPDDKDTLRKIAKTSLTGK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 177 VINSCHRQMAEIAVNAVLTVADME--RRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKKVVDAKIAILTCP 254
Cdd:cd03343 158 GAEAAKDKLADLVVDAVLQVAEKRdgKYVVDLDNIKIEKKTGGSVDDTELIRGIVIDKEVVHPGMPKRVENAKIALLDAP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 255 FEPPKPKTKHKLDVMSVEDYKALQKYEKEKFEEMIKQIKETGANLAICQWGFDDEANHLLLQNGLPAVRWVGGPEIELIA 334
Cdd:cd03343 238 LEVKKTEIDAKIRITSPDQLQAFLEQEEAMLKEMVDKIADTGANVVFCQKGIDDLAQHYLAKAGILAVRRVKKSDMEKLA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 335 IATGGRIVPRFSELTSEKLGFAGVVQEISFGttKDKMLVIEKCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIR 414
Cdd:cd03343 318 RATGAKIVTNIDDLTPEDLGEAELVEERKVG--DDKMVFVEGCKNPKAVTILLRGGTEHVVDELERALEDALRVVADALE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 415 DNRVVYGGGAAEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQvKESNPALGIDCL 494
Cdd:cd03343 396 DGKVVAGGGAVEIELAKRLREYARSVGGREQLAVEAFADALEEIPRTLAENAGLDPIDTLVELRAAH-EKGNKNAGLDVY 474
|
490 500 510
....*....|....*....|....*....|....*....
gi 6671702 495 HKGSNDMQYQHVIETLIGKKQQISLATQMVRMILKIDDI 533
Cdd:cd03343 475 TGEVVDMLEKGVIEPLRVKKQAIKSATEAATMILRIDDV 513
|
|
| thermosome_beta |
NF041083 |
thermosome subunit beta; |
15-533 |
0e+00 |
|
thermosome subunit beta;
Pssm-ID: 469010 Cd Length: 519 Bit Score: 528.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 15 PFLIIKDQdrKSRLMGLEALKSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTITNDGATILSMMDVDHQIAKLMVEL 94
Cdd:NF041083 2 PVLILKEG--TQRTKGRDAQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDIVITNDGATILKEMDVQHPAAKMLVEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 95 SKSQDDEIGDGTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARIAIQHLDKISDKvlVDINNPEPLIQTAKTTLG 174
Cdd:NF041083 80 AKTQDDEVGDGTTTAVVLAGELLKKAEELLDQNIHPTIIANGYRLAAEKAIEILDEIAEK--VDPDDRETLKKIAETSLT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 175 SKVINSCHRQMAEIAVNAVLTVAdmERRD----VDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKKVVDAKIAI 250
Cdd:NF041083 158 SKGVEEARDYLAEIAVKAVKQVA--EKRDgkyyVDLDNIQIEKKHGGSIEDTQLIYGIVIDKEVVHPGMPKRVENAKIAL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 251 LTCPFEPPKPKTKHKLDVMSVEDYKALQKYEKEKFEEMIKQIKETGANLAICQWGFDDEANHLLLQNGLPAVRWVGGPEI 330
Cdd:NF041083 236 LDAPLEVKKTEIDAEIRITDPDQLQKFLDQEEKMLKEMVDKIKATGANVVFCQKGIDDLAQHYLAKAGILAVRRVKKSDM 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 331 ELIAIATGGRIVPRFSELTSEKLGFAGVVQEISFGTtkDKMLVIEKCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIR 410
Cdd:NF041083 316 EKLAKATGARIVTNIDDLTPEDLGYAELVEERKVGD--DKMVFVEGCKNPKAVTILIRGGTEHVVDEAERALEDALSVVA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 411 NLIRDNRVVYGGGAAEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQvKESNPALG 490
Cdd:NF041083 394 DAVEDGKIVAGGGAPEVELAKRLREYAATVGGREQLAVEAFAEALEIIPRTLAENAGLDPIDILVKLRSAH-EKGKKWAG 472
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 6671702 491 IDCLHKGSNDMQYQHVIETLIGKKQQISLATQMVRMILKIDDI 533
Cdd:NF041083 473 INVFTGEVVDMWELGVIEPLRVKTQAIKSATEAATMILRIDDV 515
|
|
| thermosome_arch |
TIGR02339 |
thermosome, various subunits, archaeal; Thermosome is the name given to the archaeal rather ... |
15-533 |
1.80e-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: 502.68 E-value: 1.80e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 15 PFLIIKDQdrKSRLMGLEALKSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTITNDGATILSMMDVDHQIAKLMVEL 94
Cdd:TIGR02339 1 PVFILKEG--TQRTSGRDAQRNNIAAAKAVAEAVKSTLGPRGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 95 SKSQDDEIGDGTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARIAIQHLDKISDKvlVDINNPEPLIQTAKTTLG 174
Cdd:TIGR02339 79 AKTQDEEVGDGTTTAVVLAGELLEKAEDLLEQDIHPTVIIEGYRKAAEKALEIIDEIATK--ISPEDRDLLKKIAYTSLT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 175 SKVINSCHRQ-MAEIAVNAVLTVADME---RRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKKVVDAKIAI 250
Cdd:TIGR02339 157 SKASAEVAKDkLADLVVEAVKQVAELRgdgKYYVDLDNIKIVKKKGGSIEDTELVEGIVVDKEVVHPGMPKRVENAKIAL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 251 LTCPFEPPKPKTKHKLDVMSVEDYKALQKYEKEKFEEMIKQIKETGANLAICQWGFDDEANHLLLQNGLPAVRWVGGPEI 330
Cdd:TIGR02339 237 LDAPLEVEKTEIDAKIRITDPDQIKKFLDQEEAMLKEMVDKIASAGANVVICQKGIDDVAQHYLAKAGILAVRRVKKSDI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 331 ELIAIATGGRIVPRFSELTSEKLGFAGVVQEISFGttKDKMLVIEKCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIR 410
Cdd:TIGR02339 317 EKLARATGARIVSSIDEITESDLGYAELVEERKVG--EDKMVFVEGCKNPKAVTILLRGGTEHVVDELERSIQDALHVVA 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 411 NLIRDNRVVYGGGAAEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKEsNPALG 490
Cdd:TIGR02339 395 NALEDGKIVAGGGAVEIELALRLRSYARSVGGREQLAIEAFADALEEIPRILAENAGLDPIDALVDLRAKHEKG-NKNAG 473
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 6671702 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 |
5.26e-152 |
|
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: 445.19 E-value: 5.26e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 35 KSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTITNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVVLAG 114
Cdd:cd03338 11 LSNIQAAKAVADAIRTSLGPRGMDKMIQTGKGEVIITNDGATILKQMSVLHPAAKMLVELSKAQDIEAGDGTTSVVVLAG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 115 ALLEEAEQLLDRGIHPIRIADGYEQAARIAIQHLDKISDKvlVDINNPEPLIQTAKTTLGSKVINSCHRQMAEIAVNAVL 194
Cdd:cd03338 91 ALLSACESLLKKGIHPTVISESFQIAAKKAVEILDSMSIP--VDLNDRESLIKSATTSLNSKVVSQYSSLLAPIAVDAVL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 195 TVADMER-RDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSH-PQMPKKVVDAKIAILTCPFEPPKPKTKHKLdvmSVE 272
Cdd:cd03338 169 KVIDPATaTNVDLKDIRIVKKLGGTIEDTELVDGLVFTQKASKkAGGPTRIEKAKIGLIQFCLSPPKTDMDNNI---VVN 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 273 DYKA---LQKYEKEKFEEMIKQIKETGANLAICQW-----GFDDEANHLLLQNGLPAVRWVGGPEIELIAIATGGRIVPR 344
Cdd:cd03338 246 DYAQmdrILREERKYILNMCKKIKKSGCNVLLIQKsilrdAVSDLALHFLAKLKIMVVKDIEREEIEFICKTIGCKPVAS 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 345 FSELTSEKLGFAGVVQEISFGTtkDKMLVIEKCKNS-RAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGG 423
Cdd:cd03338 326 IDHFTEDKLGSADLVEEVSLGD--GKIVKITGVKNPgKTVTILVRGSNKLVLDEAERSLHDALCVIRCLVKKRALIPGGG 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 424 AAEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQvKESNPALGIDCLHKGSNDMQY 503
Cdd:cd03338 404 APEIEIALQLSEWARTLTGVEQYCVRAFADALEVIPYTLAENAGLNPISIVTELRNRH-AQGEKNAGINVRKGAITNILE 482
|
490 500 510
....*....|....*....|....*....|
gi 6671702 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 |
6.73e-138 |
|
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: 409.17 E-value: 6.73e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 35 KSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTITNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVVLAG 114
Cdd:TIGR02342 12 TSNIVAAKAVADAIRTSLGPKGMDKMIQDGKGEVIITNDGATILKQMAVLHPAAKMLVELSKAQDIEAGDGTTSVVILAG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 115 ALLEEAEQLLDRGIHPIRIADGYEQAARIAIQHLDKISDKvlVDINNPEPLIQTAKTTLGSKVINSCHRQMAEIAVNAVL 194
Cdd:TIGR02342 92 ALLGACERLLNKGIHPTIISESFQSAADEAIKILDEMSIP--VDLSDREQLLKSATTSLSSKVVSQYSSLLAPLAVDAVL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 195 TVADMER-RDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQ-MPKKVVDAKIAILTCPFEPPKPKTKHKLdvmSVE 272
Cdd:TIGR02342 170 KVIDPENaKNVDLNDIKVVKKLGGTIDDTELIEGLVFTQKASKSAgGPTRIEKAKIGLIQFQISPPKTDMENQI---IVN 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 273 DYKALQKYEKEK---FEEMIKQIKETGANLAICQW-----GFDDEANHLLLQNGLPAVRWVGGPEIELIAIATGGRIVPR 344
Cdd:TIGR02342 247 DYAQMDRVLKEErayILNIVKKIKKTGCNVLLIQKsilrdAVNDLALHFLAKMKIMVVKDIEREEIEFICKTIGCKPIAS 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 345 FSELTSEKLGFAGVVQEIsfGTTKDKMLVIEKCKN-SRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGG 423
Cdd:TIGR02342 327 IDHFTADKLGSAELVEEV--DSDGGKIIKITGIQNaGKTVTVVVRGSNKLVIDEAERSLHDALCVIRCLVKKRGLIAGGG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 424 AAEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQvKESNPALGIDCLHKGSNDMQY 503
Cdd:TIGR02342 405 APEIEIARRLSKYARTMKGVESYCVRAFADALEVIPYTLAENAGLNPIKVVTELRNRH-ANGEKTAGISVRKGGITNMLE 483
|
490 500 510
....*....|....*....|....*....|
gi 6671702 504 QHVIETLIGKKQQISLATQMVRMILKIDDI 533
Cdd:TIGR02342 484 EHVLQPLLVTTSAITLASETVRSILKIDDI 513
|
|
| GroEL |
COG0459 |
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ... |
25-533 |
2.65e-123 |
|
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227 Cd Length: 497 Bit Score: 370.95 E-value: 2.65e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 25 KSRLMGLEALKSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTITNDGATILSMMDVDHQI----AKLMVELSKSQDD 100
Cdd:COG0459 3 KQILFGEDARRANIRGVKALADAVKVTLGPKGRNVMLVKSFGDPTITNDGVTIAKEIELEDPFenmgAQLVKEVASKTND 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 101 EIGDGTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARIAIQHLDKISdkvlVDINNPEPLIQTAKTTLGSKvins 180
Cdd:COG0459 83 EAGDGTTTATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIA----KPVDDKEELAQVATISANGD---- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 181 chRQMAEIAVNAVLTVADMERrdvdfelIKVEgKVGGRLEDTKLIKGVIVDKDFSHPQ-------MPKKVVDAKIAIltc 253
Cdd:COG0459 155 --EEIGELIAEAMEKVGKDGV-------ITVE-EGKGLETELEVVEGMQFDKGYLSPYfvtdpekMPAELENAYILL--- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 254 pfeppkpkTKHKLDVMsvedykalqkyekEKFEEMIKQIKETGANLAICQWGFDDEANHLLLQNGLPAVR---WVGGP-- 328
Cdd:COG0459 222 --------TDKKISSI-------------QDLLPLLEKVAQSGKPLLIIAEDIDGEALATLVVNGIRGVLrvvAVKAPgf 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 329 ------EIELIAIATGGRIV-----PRFSELTSEKLGFAGVVQEisfgtTKDKMLVIEKCKNSRAVTIFIRGGNKMIIEE 397
Cdd:COG0459 281 gdrrkaMLEDIAILTGGRVIsedlgLKLEDVTLDDLGRAKRVEV-----DKDNTTIVEGAGNPKAIVILVGAATEVEVKE 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 398 AKRSLHDALCVIRNLIRDnRVVYGGGAAEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEV 477
Cdd:COG0459 356 RKRRVEDALHATRAAVEE-GIVPGGGAALLRAARALRELAAKLEGDEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKV 434
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 6671702 478 RArqvkESNPALGIDCLHKGSNDMQYQHVIETLIGKKQQISLATQMVRMILKIDDI 533
Cdd:COG0459 435 RA----AKDKGFGFDAATGEYVDMLEAGVIDPAKVKRSALQNAASVAGLILTTEAV 486
|
|
| TCP1_gamma |
cd03337 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ... |
20-533 |
7.45e-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: 369.32 E-value: 7.45e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 20 KDQDRKSRLmglealkSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTITNDGATILSMMDVDHQIAKLMVELSKSQD 99
Cdd:cd03337 11 RESGRKAQL-------GNIQAAKTVADVIRTCLGPRAMLKMLLDPMGGIVLTNDGNAILREIDVAHPAAKSMIELSRTQD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 100 DEIGDGTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARIAIQHLDKISDKvlVDINNPEPLIQTAKTTLGSKVIN 179
Cdd:cd03337 84 EEVGDGTTSVIILAGEILAVAEPFLERGIHPTVIIKAYRKALEDALKILEEISIP--VDVNDRAQMLKIIKSCIGTKFVS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 180 SCHRQMAEIAVNAVLTVA---DMERRDVDFE-LIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKKVVDAKIAILTCPF 255
Cdd:cd03337 162 RWSDLMCNLALDAVKTVAveeNGRKKEIDIKrYAKVEKIPGGEIEDSRVLDGVMLNKDVTHPKMRRRIENPRIVLLDCPL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 256 EppkpktkhkldvmsvedYkalqkyekekfeemikqiketganLAICQWGFDDEANHLLLQNGLPAVRWVGGPEIELIAI 335
Cdd:cd03337 242 E-----------------Y------------------------LVITEKGVSDLAQHYLVKAGITALRRVRKTDNNRIAR 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 336 ATGGRIVPRFSELTSEKLGFAGVVQEISFGtTKDKMLVIEKCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRD 415
Cdd:cd03337 281 ACGATIVNRPEELTESDVGTGAGLFEVKKI-GDEYFTFITECKDPKACTILLRGASKDVLNEVERNLQDAMAVARNIILN 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 416 NRVVYGGGAAEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKESNPALGIDCLH 495
Cdd:cd03337 360 PKLVPGGGATEMAVSHALSEKAKSIEGVEQWPYKAVASALEVIPRTLAQNCGANVIRTLTELRAKHAQGENSTWGIDGET 439
|
490 500 510
....*....|....*....|....*....|....*...
gi 6671702 496 KGSNDMQYQHVIETLIGKKQQISLATQMVRMILKIDDI 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 |
7.17e-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: 355.58 E-value: 7.17e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 15 PFLIIKDQDRksRLMGLEALKSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTITNDGATILSMMDVDHQIAKLMVEL 94
Cdd:TIGR02344 1 PVLVLNQNTK--RESGRKAQLSNIQAAKAVADIIRTCLGPRSMLKMLLDPMGGIVMTNDGNAILREIDVAHPAAKSMIEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 95 SKSQDDEIGDGTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARIAIQHLDKISdkVLVDINNPEPLIQTAKTTLG 174
Cdd:TIGR02344 79 SRTQDEEVGDGTTSVIILAGEMLSVAEPFLEQNIHPTVIIRAYRKALDDALSVLEEIS--IPVDVNDDAAMLKLIQSCIG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 175 SKVINSCHRQMAEIAVNAVLTVA--DMERRDVDFE-LIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKKVVDAKIAIL 251
Cdd:TIGR02344 157 TKFVSRWSDLMCDLALDAVRTVQrdENGRKEIDIKrYAKVEKIPGGDIEDSCVLKGVMINKDVTHPKMRRYIENPRIVLL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 252 TCPFEPPKPKTKHKLDVMSVEDYKALQKYEKEKFEEMIKQIKETGANLAICQWGFDDEANHLLLQNGLPAVRWVGGPEIE 331
Cdd:TIGR02344 237 DCPLEYKKGESQTNIEITKEEDWNRILQMEEEYVQLMCEDIIAVKPDLVITEKGVSDLAQHYLLKANITAIRRVRKTDNN 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 332 LIAIATGGRIVPRFSELTSEKLGF-AGVVQEISFGttKDKMLVIEKCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIR 410
Cdd:TIGR02344 317 RIARACGATIVNRPEELRESDVGTgCGLFEVKKIG--DEYFTFITECKDPKACTILLRGASKDILNEVERNLQDAMAVAR 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 411 NLIRDNRVVYGGGAAEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKESNPALG 490
Cdd:TIGR02344 395 NVLLDPKLVPGGGATEMAVSVALTEKSKKLEGVEQWPYRAVADALEIIPRTLAQNCGANVIRTLTELRAKHAQENNCTWG 474
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 6671702 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 |
5.67e-109 |
|
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: 334.68 E-value: 5.67e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 18 IIKDQDRKSRlmGLEALKSHIMAAKAVANTMRTSLGPNGLDKMM--VDKDGDVTITNDGATILSMMDVDHQIAKLMVELS 95
Cdd:cd03336 1 ILKDGAQEEK--GETARLSSFVGAIAIGDLVKTTLGPKGMDKILqsVGRSGGVTVTNDGATILKSIGVDNPAAKVLVDIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 96 KSQDDEIGDGTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARIAIQHLDKISDKVLVDINN-PEPLIQTAKTTLG 174
Cdd:cd03336 79 KVQDDEVGDGTTSVTVLAAELLREAEKLVAQKIHPQTIIEGYRMATAAAREALLSSAVDHSSDEEAfREDLLNIARTTLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 175 SKVINSCHRQMAEIAVNAVLTVADmerrDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQmPKKVVDAKIAILTCP 254
Cdd:cd03336 159 SKILTQDKEHFAELAVDAVLRLKG----SGNLDAIQIIKKLGGSLKDSYLDEGFLLDKKIGVNQ-PKRIENAKILIANTP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 255 FEPPKPKT-KHKLDVMSVEDYKALQKYEKEKFEEMIKQIKETGANLAICQWGFDDEANHLLLQNGLPAVRWVGGPEIELI 333
Cdd:cd03336 234 MDTDKIKIfGAKVRVDSTAKVAEIEEAEKEKMKNKVEKILKHGINCFINRQLIYNYPEQLFADAGIMAIEHADFDGVERL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 334 AIATGGRIVPRFSELTSEKLGFAGVVQEISFGttKDKMLVIEKCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLI 413
Cdd:cd03336 314 ALVTGGEIASTFDHPELVKLGTCKLIEEIMIG--EDKLIRFSGVAAGEACTIVLRGASQQILDEAERSLHDALCVLAQTV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 414 RDNRVVYGGGAAEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKESNPAlGIDC 493
Cdd:cd03336 392 KDTRVVLGGGCSEMLMAKAVEELAKKTPGKKSLAIEAFAKALRQLPTIIADNAGYDSAELVAQLRAAHYNGNTTA-GLDM 470
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 6671702 494 LHKGSNDMQYQHVIETLIGKKQQISLATQMVRMILKIDDIRK 535
Cdd:cd03336 471 RKGTVGDMKELGITESFKVKRQVLLSASEAAEMILRVDDIIK 512
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
36-533 |
2.57e-107 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 331.22 E-value: 2.57e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 36 SHIMAAKAVANTMRTSLGPNGLDKMMV-----DKDGDVTITNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVV 110
Cdd:PTZ00212 26 QSFVGAIAVADLVKTTLGPKGMDKILQpmsegPRSGNVTVTNDGATILKSVWLDNPAAKILVDISKTQDEEVGDGTTSVV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 111 VLAGALLEEAEQLLDRGIHPIRIADGYEQAARIAIQHLDKISDKVLVDINN-PEPLIQTAKTTLGSKVINSCHRQMAEIA 189
Cdd:PTZ00212 106 VLAGELLREAEKLLDQKIHPQTIIEGWRMALDVARKALEEIAFDHGSDEEKfKEDLLNIARTTLSSKLLTVEKDHFAKLA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 190 VNAVLTVadmeRRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQmPKKVVDAKIAILTCPFEPPKPK---TKHKL 266
Cdd:PTZ00212 186 VDAVLRL----KGSGNLDYIQIIKKPGGTLRDSYLEDGFILEKKIGVGQ-PKRLENCKILVANTPMDTDKIKiygAKVKV 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 267 DvmSVEDYKALQKYEKEKFEEMIKQIKETGANLAICQWGFDDEANHLLLQNGLPAVRWVGGPEIELIAIATGGRIVPRFS 346
Cdd:PTZ00212 261 D--SMEKVAEIEAAEKEKMKNKVDKILAHGCNVFINRQLIYNYPEQLFAEAGIMAIEHADFDGMERLAAALGAEIVSTFD 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 347 ELTSEKLGFAGVVQEISFGttKDKMLVIEKCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAE 426
Cdd:PTZ00212 339 TPEKVKLGHCDLIEEIMIG--EDKLIRFSGCAKGEACTIVLRGASTHILDEAERSLHDALCVLSQTVKDTRVVLGGGCSE 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 427 ISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKESNPAlGIDCLHKGSNDMQYQHV 506
Cdd:PTZ00212 417 MLMANAVEELAKKVEGKKSLAIEAFAKALRQIPTIIADNGGYDSAELVSKLRAEHYKGNKTA-GIDMEKGTVGDMKELGI 495
|
490 500
....*....|....*....|....*..
gi 6671702 507 IETLIGKKQQISLATQMVRMILKIDDI 533
Cdd:PTZ00212 496 TESYKVKLSQLCSATEAAEMILRVDDI 522
|
|
| TCP1_eta |
cd03340 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ... |
15-531 |
6.86e-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: 329.63 E-value: 6.86e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 15 PFLIIKDQDRKSRlmGLEALKSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTITNDGATILSMMDVDHQIAKLMVEL 94
Cdd:cd03340 1 PIILLKEGTDTSQ--GKGQLISNINACQAIADAVRTTLGPRGMDKLIVDGRGKVTISNDGATILKLLDIVHPAAKTLVDI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 95 SKSQDDEIGDGTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARIAIQHLDKISdkvlVDINNPEP------LIQT 168
Cdd:cd03340 79 AKSQDAEVGDGTTSVVVLAGEFLKEAKPFIEDGVHPQIIIRGYRKALQLAIEKIKEIA----VNIDKEDKeeqrelLEKC 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 169 AKTTLGSKVINSCHRQMAEIAVNAVLTVADmerrDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFS---HPQMPKKVVD 245
Cdd:cd03340 155 AATALNSKLIASEKEFFAKMVVDAVLSLDD----DLDLDMIGIKKVPGGSLEDSQLVNGVAFKKTFSyagFEQQPKKFKN 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 246 AKIAILTCPFEPPKPKTKHKLDVMSVEDYKALQKYEKEKFEEMIKQIKETGANLAICQWGFDDEANHLLLQNGLPAVRWV 325
Cdd:cd03340 231 PKILLLNVELELKAEKDNAEVRVEDPEEYQAIVDAEWKIIYDKLEKIVKSGANVVLSKLPIGDLATQYFADRDIFCAGRV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 326 GGPEIELIAIATGGRIVPRFSELTSEKLGFAGVVQEISFGttKDKMLVIEKCKNSRAVTIFIRGGNKMIIEEAKRSLHDA 405
Cdd:cd03340 311 PEEDLKRVAQATGGSIQTTVSNITDDVLGTCGLFEERQVG--GERYNIFTGCPKAKTCTIILRGGAEQFIEEAERSLHDA 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 406 LCVIRNLIRDNRVVYGGGAAEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKES 485
Cdd:cd03340 389 IMIVRRAIKNDSVVAGGGAIEMELSKYLRDYSRTIAGKQQLVINAFAKALEIIPRQLCDNAGFDATDILNKLRQKHAQGG 468
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 6671702 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 |
1.19e-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: 326.55 E-value: 1.19e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 27 RLMGLEALKSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTITNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGT 106
Cdd:cd03335 3 RTSGQDVRTQNVTAAMAIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDKEVGDGT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 107 TGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARIAIQHldkISDKVLVDINN--PEPLIQTAKTTLGSKVINSCHRQ 184
Cdd:cd03335 83 TSVVIIAAELLKRANELVKQKIHPTTIISGYRLACKEAVKY---IKEHLSISVDNlgKESLINVAKTSMSSKIIGADSDF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 185 MAEIAVNAVLTVADM-ERRDV-----DFELIKVEGKvggRLEDTKLIKGVIVDKDFSHPQMPKKVVDAKIAILTCPFEpp 258
Cdd:cd03335 160 FANMVVDAILAVKTTnEKGKTkypikAVNILKAHGK---SAKESYLVNGYALNCTRASQGMPTRVKNAKIACLDFNLQ-- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 259 kpKTKHKLDV-MSVEDYKALQKYEKEKFE---EMIKQIKETGANLAICQWGFDDEANHLLLQNGLPAVRWVGGPEIELIA 334
Cdd:cd03335 235 --KTKMKLGVqVVVTDPEKLEKIRQRESDitkERIKKILAAGANVVLTTGGIDDMCLKYFVEAGAMAVRRVKKEDLRRIA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 335 IATGGRIVPRFSELTSE------KLGFAGVVQEISFGttKDKMLVIEKCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCV 408
Cdd:cd03335 313 KATGATLVSTLANLEGEetfdpsYLGEAEEVVQERIG--DDELILIKGTKKRSSASIILRGANDFMLDEMERSLHDALCV 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 409 IRNLIRDNRVVYGGGAAEisCALAVSQE--ADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRAR----QV 482
Cdd:cd03335 391 VKRTLESNSVVPGGGAVE--TALSIYLEnfATTLGSREQLAIAEFAEALLVIPKTLAVNAAKDATELVAKLRAYhaaaQV 468
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 6671702 483 KESNPAL---GIDcLHKGS--NDMQYQhVIETLIGKKQQISLATQMVRMILKIDDIRK 535
Cdd:cd03335 469 KPDKKHLkwyGLD-LINGKvrDNLEAG-VLEPTVSKIKSLKFATEAAITILRIDDLIK 524
|
|
| chap_CCT_alpha |
TIGR02340 |
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ... |
27-541 |
3.37e-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: 320.51 E-value: 3.37e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 27 RLMGLEALKSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTITNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGT 106
Cdd:TIGR02340 7 RTSGQDVRTQNVTAAMAIANIVKTSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDREVGDGT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 107 TGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARIAIQHldkISDKVLVDINN--PEPLIQTAKTTLGSKVINSCHRQ 184
Cdd:TIGR02340 87 TSVVIIAAELLKRADELVKNKIHPTSVISGYRLACKEAVKY---IKENLSVSVDElgREALINVAKTSMSSKIIGLDSDF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 185 MAEIAVNAVLTVADM-ERRDVDF--ELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKKVVDAKIAILTCPFEppkpK 261
Cdd:TIGR02340 164 FSNIVVDAVLAVKTTnENGETKYpiKAINILKAHGKSARESMLVKGYALNCTVASQQMPKRIKNAKIACLDFNLQ----K 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 262 TKHKLDV-MSVEDYKALQKYEKEKFE---EMIKQIKETGANLAICQWGFDDEANHLLLQNGLPAVRWVGGPEIELIAIAT 337
Cdd:TIGR02340 240 AKMALGVqIVVDDPEKLEQIRQREADitkERIKKILDAGANVVLTTGGIDDMCLKYFVEAGAMGVRRCKKEDLKRIAKAT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 338 GGRIVPRFSELTSE------KLGFAGVVQEISFGttKDKMLVIEKCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRN 411
Cdd:TIGR02340 320 GATLVSTLADLEGEetfeasYLGFADEVVQERIA--DDECILIKGTKKRKSASIILRGANDFMLDEMERSLHDALCVVKR 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 412 LIRDNRVVYGGGAAEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQ-------VKE 484
Cdd:TIGR02340 398 TLESNSVVPGGGAVEAALSIYLENFATTLGSREQLAIAEFARALLIIPKTLAVNAAKDSTELVAKLRAYHaaaqlkpEKK 477
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 6671702 485 SNPALGIDCLHKGSNDMQYQHVIETLIGKKQQISLATQMVRMILKIDD-IRKPGESEE 541
Cdd:TIGR02340 478 HLKWYGLDLVNGKIRDNKEAGVLEPTVSKVKSLKFATEAAITILRIDDlIKLNPEQSK 535
|
|
| chap_CCT_eta |
TIGR02345 |
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ... |
15-537 |
4.40e-103 |
|
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: 319.78 E-value: 4.40e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 15 PFLIIKDQDRKSRlmGLEALKSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTITNDGATILSMMDVDHQIAKLMVEL 94
Cdd:TIGR02345 3 TIVLLKEGTDTSQ--GKGQLISNINACVAIAEALKTTLGPRGMDKLIVGSNGKATISNDGATILKLLDIVHPAAKTLVDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 95 SKSQDDEIGDGTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARIAIQHLDKISDKV-LVDINNPEPLIQTAKTTL 173
Cdd:TIGR02345 81 AKSQDAEVGDGTTSVTILAGELLKEAKPFIEEGVHPQLIIRCYREALSLAVEKIKEIAVTIdEEKGEQRELLEKCAATAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 174 GSKVINSCHRQMAEIAVNAVLTvadMERRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFS---HPQMPKKVVDAKIAI 250
Cdd:TIGR02345 161 SSKLISHNKEFFSKMIVDAVLS---LDRDDLDLKLIGIKKVQGGALEDSQLVNGVAFKKTFSyagFEQQPKKFANPKILL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 251 LTCPFEPPKPKTKHKLDVMSVEDYKALQKYEKEKFEEMIKQIKETGANLAICQWGFDDEANHLLLQNGLPAVRWVGGPEI 330
Cdd:TIGR02345 238 LNVELELKAEKDNAEIRVEDVEDYQAIVDAEWAIIFRKLEKIVESGANVVLSKLPIGDLATQYFADRDIFCAGRVSAEDL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 331 ELIAIATGGRIVPRFSELTSEKLGFAGVVQEISFGttKDKMLVIEKCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIR 410
Cdd:TIGR02345 318 KRVIKACGGSIQSTTSDLEADVLGTCALFEERQIG--SERYNYFTGCPHAKTCTIILRGGAEQFIEEAERSLHDAIMIVR 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 411 NLIRDNRVVYGGGAAEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKESNPAlG 490
Cdd:TIGR02345 396 RALKNKKIVAGGGAIEMELSKCLRDYSKTIDGKQQLIINAFAKALEIIPRQLCENAGFDSIEILNKLRSRHAKGGKWY-G 474
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 6671702 491 IDCLHKGSNDMQYQHVIETLIGKKQQISLATQMVRMILKIDD-IRKPG 537
Cdd:TIGR02345 475 VDINTEDIGDNFEAFVWEPALVKINALKAAFEAACTILSVDEtITNPK 522
|
|
| TCP1_theta |
cd03341 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ... |
32-533 |
1.19e-98 |
|
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: 306.84 E-value: 1.19e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 32 EALKSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTITNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVV 111
Cdd:cd03341 8 EAVLRNIEACKELSQITRTSYGPNGMNKMVINHLEKLFVTSDAATILRELEVQHPAAKLLVMASQMQEEEIGDGTNLVVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 112 LAGALLEEAEQLLDRGIHPIRIADGYEQAARIAIQHLDKISDKVLVDINNPEPLIQTAKTTLGSKVI-NSCHrqMAEIAV 190
Cdd:cd03341 88 LAGELLEKAEELLRMGLHPSEIIEGYEKALKKALEILEELVVYKIEDLRNKEEVSKALKTAIASKQYgNEDF--LSPLVA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 191 NAVLTVADMERRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDfSHPQMpKKVVDAKIAILTCPFeppkpktkhkldvms 270
Cdd:cd03341 166 EACISVLPENIGNFNVDNIRVVKILGGSLEDSKVVRGMVFKRE-PEGSV-KRVKKAKVAVFSCPF--------------- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 271 vedykalqkyekekfeemikqikETGANLAICQWGFDDEANHLLLQNGLPAVRWVGGPEIELIAIATGGRIVPRFSELTS 350
Cdd:cd03341 229 -----------------------DIGVNVIVAGGSVGDLALHYCNKYGIMVIKINSKFELRRLCRTVGATPLPRLGAPTP 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 351 EKLGFAGVVQEISFGTTkdKMLVIEKCKNSRAV-TIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAEISC 429
Cdd:cd03341 286 EEIGYCDSVYVEEIGDT--KVVVFRQNKEDSKIaTIVLRGATQNILDDVERAIDDGVNVFKSLTKDGRFVPGAGATEIEL 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 430 ALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKESNPA-LGIDCLHKGSNDMQYQHVIE 508
Cdd:cd03341 364 AKKLKEYGEKTPGLEQYAIKKFAEAFEVVPRTLAENAGLDATEVLSELYAAHQKGNKSAgVDIESGDEGTKDAKEAGIFD 443
|
490 500
....*....|....*....|....*
gi 6671702 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 |
1.47e-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: 305.87 E-value: 1.47e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 32 EALKSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTITNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVV 111
Cdd:TIGR02346 18 EAVIKNIEACKELSQITRTSLGPNGMNKMVINHLEKLFVTNDAATILRELEVQHPAAKLLVMASEMQENEIGDGTNLVLV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 112 LAGALLEEAEQLLDRGIHPIRIADGYEQAARIAIQHLDKISDKVLVDINNPEPLIQTAKTTLGSKVINScHRQMAEIAVN 191
Cdd:TIGR02346 98 LAGELLNKAEELIRMGLHPSEIIKGYEMALKKAMEILEELVVWEVKDLRDKDELIKALKASISSKQYGN-EDFLAQLVAQ 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 192 AVLTVADMERRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFShpQMPKKVVDAKIAILTCPFEPPKPKTKHKLDVMSV 271
Cdd:TIGR02346 177 ACSTVLPKNPQNFNVDNIRVCKILGGSLSNSEVLKGMVFNREAE--GSVKSVKNAKVAVFSCPLDTATTETKGTVLIHNA 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 272 EDYKALQKYEKEKFEEMIKQIKETGANLAICQWGFDDEANHLLLQNGLPAVRWVGGPEIELIAIATGGRIVPRFSELTSE 351
Cdd:TIGR02346 255 EELLNYSKGEENQIEAMIKAIADSGVNVIVTGGSVGDMALHYLNKYNIMVLKIPSKFELRRLCKTVGATPLPRLGAPTPE 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 352 KLGFAGVVQEISFGTtkDKMLVIE-KCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAEISCA 430
Cdd:TIGR02346 335 EIGYVDSVYVSEIGG--DKVTVFKqENGDSKISTIILRGSTDNLLDDIERAIDDGVNTVKALVKDGRLLPGAGATEIELA 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 431 LAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQvKESNPALGID--CLHKGSNDMQYQHVIE 508
Cdd:TIGR02346 413 SRLTKYGEKLPGLDQYAIKKFAEAFEIIPRTLAENAGLNANEVIPKLYAAH-KKGNKSKGIDieAESDGVKDASEAGIYD 491
|
490 500
....*....|....*....|....*
gi 6671702 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 |
2.32e-91 |
|
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: 289.45 E-value: 2.32e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 18 IIKDQDRKSRlmGLEALKSHIMAAKAVANTMRTSLGPNGLDKMMV--DKDGDVTITNDGATILSMMDVDHQIAKLMVELS 95
Cdd:TIGR02341 2 IFKDGADEER--AENARLSSFVGAIAIGDLVKSTLGPKGMDKILQssSSDASIMVTNDGATILKSIGVDNPAAKVLVDMS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 96 KSQDDEIGDGTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARIAIQHL-----DKISDKVLVDinnpEPLIQTAK 170
Cdd:TIGR02341 80 KVQDDEVGDGTTSVTVLAAELLREAEKLINQKIHPQTIIAGYREATKAARDALlksavDNGSDEVKFR----QDLMNIAR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 171 TTLGSKVINSCHRQMAEIAVNAVLTVadmeRRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQmPKKVVDAKIAI 250
Cdd:TIGR02341 156 TTLSSKILSQHKDHFAQLAVDAVLRL----KGSGNLEAIQIIKKLGGSLADSYLDEGFLLDKKIGVNQ-PKRIENAKILI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 251 LTCPFEPPKPKT-KHKLDVMSVEDYKALQKYEKEKFEEMIKQIKETGANLAICQWGFDDEANHLLLQNGLPAVRWVGGPE 329
Cdd:TIGR02341 231 ANTGMDTDKVKIfGSRVRVDSTAKVAELEHAEKEKMKEKVEKILKHGINCFINRQLIYNYPEQLFADAGVMAIEHADFEG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 330 IELIAIATGGRIVPRFSELTSEKLGFAGVVQEISFGttKDKMLVIEKCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVI 409
Cdd:TIGR02341 311 VERLALVTGGEIVSTFDHPELVKLGSCDLIEEIMIG--EDKLLKFSGVKLGEACTIVLRGATQQILDEAERSLHDALCVL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 410 RNLIRDNRVVYGGGAAEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRArQVKESNPAL 489
Cdd:TIGR02341 389 SQTVKESRTVLGGGCSEMLMSKAVTQEAQRTPGKEALAVEAFARALRQLPTIIADNAGFDSAELVAQLRA-AHYNGNTTM 467
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 6671702 490 GIDCLHKGSNDMQYQHVIETLIGKKQQISLATQMVRMILKIDDIRK 535
Cdd:TIGR02341 468 GLDMNEGTIADMRQLGITESYKVKRAVVSSAAEAAEVILRVDNIIK 513
|
|
| chap_CCT_zeta |
TIGR02347 |
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ... |
33-539 |
5.24e-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: 275.84 E-value: 5.24e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 33 ALKSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTITNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVVL 112
Cdd:TIGR02347 17 ALMMNINAARGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEMQIQHPTASMIARAATAQDDITGDGTTSTVLL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 113 AGALLEEAEQLLDRGIHPIRIADGYEQAARIAIQHLDKISDKVlVDINNPEPLIQTAKTTLGSKVINSCHRQMAEIAVNA 192
Cdd:TIGR02347 97 IGELLKQAERYILEGVHPRIITEGFEIARKEALQFLDKFKVKK-EDEVDREFLLNVARTSLRTKLPADLADQLTEIVVDA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 193 VLTVADMErRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKKVVDAKIAILTCPFEPPKPKTKHKLDVMSVE 272
Cdd:TIGR02347 176 VLAIKKDG-EDIDLFMVEIMEMKHKSATDTTLIRGLVLDHGARHPDMPRRVKNAYILTCNVSLEYEKTEVNSGFFYSSAE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 273 DYKALQKYEKEKFEEMIKQIKE-------TGAN---LAICQWGFDDEANHLLLQNGLPAVRWVGGPEIELIAIATGGRIV 342
Cdd:TIGR02347 255 QREKLVKAERKFVDDRVKKIIElkkkvcgKSPDkgfVVINQKGIDPPSLDLLAKEGIMALRRAKRRNMERLTLACGGEAL 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 343 PRFSELTSEKLGFAGVVQEISFGttKDKMLVIEKCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGG 422
Cdd:TIGR02347 335 NSVEDLTPECLGWAGLVYETTIG--EEKYTFIEECKNPKSCTILIKGPNDHTIAQIKDAVRDGLRAVKNAIEDKCVVPGA 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 423 GAAEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRArQVKESNPALGIDCLHKGSNDMQ 502
Cdd:TIGR02347 413 GAFEIAAYRHLKEYKKSVKGKAKLGVEAFANALLVIPKTLAENSGFDAQDTLVKLED-EHDEGGEVVGVDLNTGEPIDPE 491
|
490 500 510
....*....|....*....|....*....|....*..
gi 6671702 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 |
2.03e-84 |
|
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: 270.28 E-value: 2.03e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 32 EALKSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTITNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVV 111
Cdd:cd03342 12 QALAVNISAAKGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLSEMQIQHPTASMIARAATAQDDITGDGTTSNVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 112 LAGALLEEAEQLLDRGIHPIRIADGYEQAARIAIQHLDKISDKVLVDiNNPEPLIQTAKTTLGSKVINSCHRQMAEIAVN 191
Cdd:cd03342 92 LIGELLKQAERYIQEGVHPRIITEGFELAKNKALKFLESFKVPVEID-TDRELLLSVARTSLRTKLHADLADQLTEIVVD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 192 AVLTVadmERRDVDFELIKVE-GKVGGRLE-DTKLIKGVIVDKDFSHPQMPKKVVDAkiAILTCPfeppkpktkhkldvM 269
Cdd:cd03342 171 AVLAI---YKPDEPIDLHMVEiMQMQHKSDsDTKLIRGLVLDHGARHPDMPKRVENA--YILTCN--------------V 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 270 SVEdykalqkYEK-EKFEEMIkqiketgANLAICQWGFDDEANHLLLQNGLPAVRWVGGPEIELIAIATGGRIVPRFSEL 348
Cdd:cd03342 232 SLE-------YEKtEVNSGFF-------YSVVINQKGIDPPSLDMLAKEGILALRRAKRRNMERLTLACGGVAMNSVDDL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 349 TSEKLGFAGVVQEISFGttKDKMLVIEKCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAEIS 428
Cdd:cd03342 298 SPECLGYAGLVYERTLG--EEKYTFIEGVKNPKSCTILIKGPNDHTITQIKDAIRDGLRAVKNAIEDKCVVPGAGAFEVA 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 429 CALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRaRQVKESNPALGIDCLHKGSNDMQYQHVIE 508
Cdd:cd03342 376 LYAHLKEFKKSVKGKAKLGVQAFADALLVIPKTLAENSGLDVQETLVKLQ-DEYAEGGQVGGVDLDTGEPMDPESEGIWD 454
|
490 500
....*....|....*....|....*....
gi 6671702 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 |
3.14e-75 |
|
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: 236.98 E-value: 3.14e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 163 EPLIQTAKTTLGSKvINSCHRQMAEIAVNAVLTVADMERrDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKK 242
Cdd:cd03333 2 ELLLQVATTSLNSK-LSSWDDFLGKLVVDAVLKVGPDNR-MDDLGVIKVEKIPGGSLEDSELVVGVVFDKGYASPYMPKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 243 VVDAKIAILTCPFEPpkpktkhkldvmsvedykalqkyekekfeemikqiketganLAICQWGFDDEANHLLLQNGLPAV 322
Cdd:cd03333 80 LENAKILLLDCPLEY-----------------------------------------VVIAEKGIDDLALHYLAKAGIMAV 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 323 RWVGGPEIELIAIATGGRIVPRFSELTSEKLGFAGVVQEISFGTtkDKMLVIEKCKNSRAVTIFIRGGNKMIIEEAKRSL 402
Cdd:cd03333 119 RRVKKEDLERIARATGATIVSSLEDLTPEDLGTAELVEETKIGE--EKLTFIEGCKGGKAATILLRGATEVELDEVKRSL 196
|
250
....*....|...
gi 6671702 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 |
3.99e-16 |
|
TCP-1 like domain of the eukaryotic phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinase Fab1. Fab1p is important for vacuole size regulation, presumably by modulating PtdIns(3,5)P2 effector activity. In the human homolog p235/PIKfyve deletion of this domain leads to loss of catalytic activity. However no exact function this domain has been defined. In general, chaperonins are involved in productive folding of proteins.
Pssm-ID: 239450 [Multi-domain] Cd Length: 261 Bit Score: 78.42 E-value: 3.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 187 EIAVNAVLTVADMERRDVDF-------ELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKKVVDAKIAILTCPFEPPK 259
Cdd:cd03334 21 DILLPLVWKAASNVKPDVRAgddmdirQYVKIKKIPGGSPSDSEVVDGVVFTKNVAHKRMPSKIKNPRILLLQGPLEYQR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 260 PKTKhkldVMSVEDYKAlqkYEKEKFEEMIKQIKETGANLAICQWGFDDEANHLLLQNGLPAVRWVGGPEIELIAIATGG 339
Cdd:cd03334 101 VENK----LLSLDPVIL---QEKEYLKNLVSRIVALRPDVILVEKSVSRIAQDLLLEAGITLVLNVKPSVLERISRCTGA 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6671702 340 RIVPRFSEL-TSEKLGFAGVVQEISF----GTTKDKMLvIEKCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLI 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 |
3.32e-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: 75.19 E-value: 3.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 30 GLEALKSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTITNDGATI---LSMMD-VDHQIAKLMVELSKSQDDEIGDG 105
Cdd:cd03344 6 GEEARKALLRGVNKLADAVKVTLGPKGRNVVIEKSFGSPKITKDGVTVakeIELEDpFENMGAQLVKEVASKTNDVAGDG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 106 TTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARIAIQHLDKISdkvlVDINNPEPLIQTAKT------TLGSKVIN 179
Cdd:cd03344 86 TTTATVLARAIIKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLS----KPVKTKEEIAQVATIsangdeEIGELIAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 180 SchrqMAEIAVNAVLTVADmerrdvdfelikvegkvGGRLEDT-KLIKGVIVDKDFSHPQM-----PKKVV--DAKIAIl 251
Cdd:cd03344 162 A----MEKVGKDGVITVEE-----------------GKTLETElEVVEGMQFDRGYLSPYFvtdpeKMEVEleNPYILL- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 252 tcpfeppkpkTKHKLDvmSVED-YKALQkyekekfeemikQIKETGANLAICQWGFDDEANHLL----LQNGLPAVRwVG 326
Cdd:cd03344 220 ----------TDKKIS--SIQElLPILE------------LVAKAGRPLLIIAEDVEGEALATLvvnkLRGGLKVCA-VK 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 327 GPE--------IELIAIATGGRIVP-----RFSELTSEKLGFAGVVQeisfgTTKDKMLVIEKCKNSRAV---------- 383
Cdd:cd03344 275 APGfgdrrkamLEDIAILTGGTVISeelglKLEDVTLEDLGRAKKVV-----VTKDDTTIIGGAGDKAAIkariaqirkq 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 384 -------------------------TIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNrVVYGGGAAEISCALAVSQEAD 438
Cdd:cd03344 350 ieettsdydkeklqerlaklsggvaVIKVGGATEVELKEKKDRVEDALNATRAAVEEG-IVPGGGVALLRASPALDKLKA 428
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6671702 439 KCPtLEQYAMRAFADALEVIPMALSENSGMNPiqtmtEVRARQVKESNPALGIDCLHKGSNDM 501
Cdd:cd03344 429 LNG-DEKLGIEIVRRALEAPLRQIAENAGVDG-----SVVVEKVLESPDGFGYDAATGEYVDM 485
|
|
| GroEL |
TIGR02348 |
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ... |
32-213 |
1.10e-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: 70.40 E-value: 1.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 32 EALKSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTITNDGATILSMMDVDHQI----AKLMVELSKSQDDEIGDGTT 107
Cdd:TIGR02348 9 EARKALLRGVDKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDKFenmgAQLVKEVASKTNDVAGDGTT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 108 GVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARIAIQHLDKISdkvlVDINNPEPLIQTAKTTLGS--KVINSCHRQM 185
Cdd:TIGR02348 89 TATVLAQAIVKEGLKNVAAGANPIELKRGIEKAVEAVVEELKKLS----KPVKGKKEIAQVATISANNdeEIGSLIAEAM 164
|
170 180
....*....|....*....|....*...
gi 6671702 186 AEIAVNAVLTVAdmERRDVDFELIKVEG 213
Cdd:TIGR02348 165 EKVGKDGVITVE--ESKSLETELEVVEG 190
|
|
| groEL |
PRK12850 |
chaperonin GroEL; Reviewed |
18-155 |
8.56e-11 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237231 Cd Length: 544 Bit Score: 64.35 E-value: 8.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 18 IIKDQDRKSRLM-GLEALkshimaakavANTMRTSLGPNGLDKMMVDKDGDVTITNDGATILSMMDVDHQIAKL---MV- 92
Cdd:PRK12850 6 IRFSTDARDRLLrGVNIL----------ANAVKVTLGPKGRNVVLEKSFGAPRITKDGVTVAKEIELEDKFENMgaqMVk 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6671702 93 ELSKSQDDEIGDGTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARIAIQHLDKISDKV 155
Cdd:PRK12850 76 EVASKTNDLAGDGTTTATVLAQAIVREGAKLVAAGMNPMDLKRGIDLAVAAVVDELKKIAKKV 138
|
|
| PTZ00114 |
PTZ00114 |
Heat shock protein 60; Provisional |
25-469 |
1.81e-10 |
|
Heat shock protein 60; Provisional
Pssm-ID: 185455 Cd Length: 555 Bit Score: 63.39 E-value: 1.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 25 KSRLMGLEALKSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTITNDGATIL-------SMMDVDhqiAKLMVELSKS 97
Cdd:PTZ00114 15 KEIRFGDEARQSLLKGIERLADAVAVTLGPKGRNVIIEQEYGSPKITKDGVTVAkaiefsdRFENVG---AQLIRQVASK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 98 QDDEIGDGTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARIAIQHLDKISDKVlvdiNNPEPLIQTAK-TTLGSK 176
Cdd:PTZ00114 92 TNDKAGDGTTTATILARAIFREGCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQSRPV----KTKEDILNVATiSANGDV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 177 VINSCHRQ-MAEIAVNAVLTVADmerrdvdfelikvegkvGGRLEDT-KLIKGVIVDKDFSHPQMpkkVVDAK--IAILT 252
Cdd:PTZ00114 168 EIGSLIADaMDKVGKDGTITVED-----------------GKTLEDElEVVEGMSFDRGYISPYF---VTNEKtqKVELE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 253 CPFeppkpktkhkldvMSVEDYKALQkyekekfeemIKQI-------KETGANLAICQWGFDDEA------NHllLQNGL 319
Cdd:PTZ00114 228 NPL-------------ILVTDKKISS----------IQSIlpilehaVKNKRPLLIIAEDVEGEAlqtliiNK--LRGGL 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 320 P--AVRWVGGPE-----IELIAIATGGRIVPR------FSELTSEKLGFAGVVQ----EISF-GTTKDKMLVIEKCKNSR 381
Cdd:PTZ00114 283 KvcAVKAPGFGDnrkdiLQDIAVLTGATVVSEdnvglkLDDFDPSMLGSAKKVTvtkdETVIlTGGGDKAEIKERVELLR 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 382 A-------------------------VTIFIRGGNKMIIEEAKRSLHDALCVIRNLIrDNRVVYGGGAAEI--SCALAVS 434
Cdd:PTZ00114 363 SqierttseydkeklkerlaklsggvAVIKVGGASEVEVNEKKDRIEDALNATRAAV-EEGIVPGGGVALLraSKLLDKL 441
|
490 500 510
....*....|....*....|....*....|....*
gi 6671702 435 QEADKCPTLEQYAMRAFADALEVIPMALSENSGMN 469
Cdd:PTZ00114 442 EEDNELTPDQRTGVKIVRNALRLPTKQIAENAGVE 476
|
|
| PLN03167 |
PLN03167 |
Chaperonin-60 beta subunit; Provisional |
33-176 |
1.86e-10 |
|
Chaperonin-60 beta subunit; Provisional
Pssm-ID: 215611 [Multi-domain] Cd Length: 600 Bit Score: 63.40 E-value: 1.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 33 ALKSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTITNDGATILSMMDVDHQI----AKLMVELSKSQDDEIGDGTTG 108
Cdd:PLN03167 67 AIKKLQAGVNKLADLVGVTLGPKGRNVVLESKYGSPKIVNDGVTVAKEVELEDPVenigAKLVRQAAAKTNDLAGDGTTT 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 109 VVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARIAIQHLDKISDKV----LVDI------NNPE--PLIQTAKTTLGSK 176
Cdd:PLN03167 147 SVVLAQGLIAEGVKVVAAGANPVQITRGIEKTAKALVKELKKMSKEVedseLADVaavsagNNYEvgNMIAEAMSKVGRK 226
|
|
| PRK14104 |
PRK14104 |
chaperonin GroEL; Provisional |
30-213 |
5.19e-10 |
|
chaperonin GroEL; Provisional
Pssm-ID: 172594 Cd Length: 546 Bit Score: 61.97 E-value: 5.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 30 GLEALKSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTITNDGATILSMMDVDHQI----AKLMVELSKSQDDEIGDG 105
Cdd:PRK14104 9 GVDARDRMLRGVDILANAVKVTLGPKGRNVVLDKSFGAPRITKDGVTVAKEIELEDKFenmgAQMVREVASKSADAAGDG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 106 TTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARIAIQHLDKISDKVLVdiNNPEPLIQTAKTTLGSKVINSCHRQM 185
Cdd:PRK14104 89 TTTATVLAQAIVREGAKSVAAGMNPMDLKRGIDLAVEAVVADLVKNSKKVTS--NDEIAQVGTISANGDAEIGKFLADAM 166
|
170 180
....*....|....*....|....*...
gi 6671702 186 AEIAVNAVLTVAdmERRDVDFELIKVEG 213
Cdd:PRK14104 167 KKVGNEGVITVE--EAKSLETELDVVEG 192
|
|
| groEL |
PRK12851 |
chaperonin GroEL; Reviewed |
41-155 |
1.28e-09 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 171770 Cd Length: 541 Bit Score: 60.53 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 41 AKAVANTMRTSLGPNGLDKMMVDKDGDVTITNDGATILSMMDVDHQI----AKLMVELSKSQDDEIGDGTTGVVVLAGAL 116
Cdd:PRK12851 20 VNILADAVKVTLGPKGRNVVIDKSFGAPTITNDGVTIAKEIELEDKFenmgAQMVREVASKTNDVAGDGTTTATVLAQAI 99
|
90 100 110
....*....|....*....|....*....|....*....
gi 6671702 117 LEEAEQLLDRGIHPIRIADGYEQAARIAIQHLDKISDKV 155
Cdd:PRK12851 100 VREGAKAVAAGANPMDLKRGIDRAVAAVVEELKANARPV 138
|
|
| groEL |
PRK12849 |
chaperonin GroEL; Reviewed |
43-213 |
4.65e-09 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237230 Cd Length: 542 Bit Score: 58.66 E-value: 4.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 43 AVANTMRTSLGPNGLDkMMVDKD-GDVTITNDGATILSMMDVDHQI----AKLMVELSKSQDDEIGDGTTGVVVLAGALL 117
Cdd:PRK12849 21 KLADAVKVTLGPKGRN-VVIDKSfGAPTITKDGVSIAKEIELEDPFenlgAQLVKEVASKTNDVAGDGTTTATVLAQALV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 118 EEAEQLLDRGIHPIRIADGYEQAARIAIQHLDKISDKVlvdiNNPEPLIQTAKT------TLGSKVinscHRQMAEIAVN 191
Cdd:PRK12849 100 QEGLKNVAAGANPMDLKRGIDKAVEAVVEELKALARPV----SGSEEIAQVATIsangdeEIGELI----AEAMEKVGKD 171
|
170 180
....*....|....*....|..
gi 6671702 192 AVLTVAdmERRDVDFELIKVEG 213
Cdd:PRK12849 172 GVITVE--ESKTLETELEVTEG 191
|
|
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
43-155 |
5.76e-09 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 58.60 E-value: 5.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 43 AVANTMRTSLGPNG----LDKmmvdKDGDVTITNDGATILSMMDVDHQI----AKLMVELSKSQDDEIGDGTTGVVVLAG 114
Cdd:PRK00013 21 KLADAVKVTLGPKGrnvvLEK----SFGAPTITKDGVTVAKEIELEDPFenmgAQLVKEVASKTNDVAGDGTTTATVLAQ 96
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 6671702 115 ALLEEAEQLLDRGIHPIRIADGYEQAARIAIQHLDKISDKV 155
Cdd:PRK00013 97 AIVREGLKNVAAGANPMDLKRGIDKAVEAAVEELKKISKPV 137
|
|
| groEL |
PRK12852 |
chaperonin GroEL; Reviewed |
44-155 |
6.15e-08 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237232 Cd Length: 545 Bit Score: 55.24 E-value: 6.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 44 VANTMRTSLGPNGLDKMMVDKDGDVTITNDGATILSMMDVDHQI----AKLMVELSKSQDDEIGDGTTGVVVLAGALLEE 119
Cdd:PRK12852 23 LANAVKVTLGPKGRNVVIEKSFGAPRITKDGVTVAKEIELEDKFenmgAQMVREVASKTNDLAGDGTTTATVLAQAIVRE 102
|
90 100 110
....*....|....*....|....*....|....*.
gi 6671702 120 AEQLLDRGIHPIRIADGYEQAARIAIQHLDKISDKV 155
Cdd:PRK12852 103 GAKAVAAGMNPMDLKRGIDIAVAAVVKDIEKRAKPV 138
|
|
| groEL |
CHL00093 |
chaperonin GroEL |
20-153 |
4.01e-07 |
|
chaperonin GroEL
Pssm-ID: 177025 Cd Length: 529 Bit Score: 52.80 E-value: 4.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671702 20 KDQDRKSRLMGLEALkshimaAKAVANTmrtsLGPNGLDKMMVDKDGDVTITNDGATILSMMDVDHQIAKLMVEL----- 94
Cdd:CHL00093 8 QDNARRALERGMDIL------AEAVSVT----LGPKGRNVVLEKKYGSPQIVNDGVTIAKEIELEDHIENTGVALirqaa 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 6671702 95 SKSqDDEIGDGTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARIAIQhldKISD 153
Cdd:CHL00093 78 SKT-NDVAGDGTTTATVLAYAIVKQGMKNVAAGANPISLKRGIEKATQYVVS---QIAE 132
|
|
| |
