|
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: 1100.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 10 DEYGRPFLIIKDQDRKSRLMGLEALKSHIMAAKAVANTMKTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAK 89
Cdd:cd03339 1 DEYGRPFIIVREQEKKKRLKGLEAHKSHILAAKSVANILRTSLGPRGMDKILVSPDGEVTVTNDGATILEKMDVDHQIAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 90 LMVELSKSQDDEIGDGTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARIAIEHLDKISDSVLVDMKNTEPLIQTA 169
Cdd:cd03339 81 LLVELSKSQDDEIGDGTTGVVVLAGALLEQAEKLLDRGIHPIRIADGYEQACKIAVEHLEEIADKIEFSPDNKEPLIQTA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 170 KTTLGSKVVNSCHRQMAEIAVNAVLTVADMQRRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKQVEDAKIA 249
Cdd:cd03339 161 MTSLGSKIVSRCHRQFAEIAVDAVLSVADLERKDVNFELIKVEGKVGGRLEDTKLVKGIVIDKDFSHPQMPKEVKDAKIA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 250 ILTCPFEPPKPKTKHKLDVTSVEDFKALQKYEKEKFEEMIRQIKETGANLAICQWGFDDEANHLLLQNDLPAVRWVGGPE 329
Cdd:cd03339 241 ILTCPFEPPKPKTKHKLDITSVEDYKKLQEYEQKYFREMVEQVKDAGANLVICQWGFDDEANHLLLQNGLPAVRWVGGVE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 330 IELIAIATGGRIVPRFSELTAEKLGFAGLVKEISFGTTKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVI 409
Cdd:cd03339 321 IELIAIATGGRIVPRFEDLSPEKLGKAGLVREISFGTTKDKMLVIEGCPNSKAVTIFIRGGNKMIIEEAKRSLHDALCVV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 410 RNLIRDNRVVYGGGAAEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALAENSGMNPIQTMTEVRARQVKEVNPAL 489
Cdd:cd03339 401 RNLIRDNRIVYGGGAAEISCSLAVEKAADKCSGIEQYAMRAFADALESIPLALAENSGLNPIETLSEVKARQVKEKNPHL 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 296475689 490 GIDCLHKGTNDMKHQHVIETLIGKKQQISLATQMVRMILKIDDIRK 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: 1025.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 6 TLAFDEYGRPFLIIKDQDRKSRLMGLEALKSHIMAAKAVANTMKTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDH 85
Cdd:TIGR02343 1 ILAFDEYGRPFIIIKDQDNKKRLKGLEAKKSNIAAAKSVASILRTSLGPKGMDKMLISPDGDITVTNDGATILSQMDVDN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 86 QIAKLMVELSKSQDDEIGDGTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARIAIEHLDKISDSVLVDMKNTEPL 165
Cdd:TIGR02343 81 QIAKLMVELSKSQDDEIGDGTTGVVVLAGALLEQAEELLDKGIHPIKIADGFEEAARIAVEHLEEISDEISADNNNREPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 166 IQTAKTTLGSKVVNSCHRQMAEIAVNAVLTVADMQRRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKQVED 245
Cdd:TIGR02343 161 IQAAKTSLGSKIVSKCHRRFAEIAVDAVLNVADMERRDVDFDLIKVEGKVGGSLEDTKLIKGIIIDKDFSHPQMPKEVED 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 246 AKIAILTCPFEPPKPKTKHKLDVTSVEDFKALQKYEKEKFEEMIRQIKETGANLAICQWGFDDEANHLLLQNDLPAVRWV 325
Cdd:TIGR02343 241 AKIAILTCPFEPPKPKTKHKLDISSVEEYKKLQKYEQQKFKEMIDDIKKSGANLVICQWGFDDEANHLLLQNDLPAVRWV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 326 GGPEIELIAIATGGRIVPRFSELTAEKLGFAGLVKEISFGTTKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDA 405
Cdd:TIGR02343 321 GGQELELIAIATGGRIVPRFQELSKDKLGKAGLVREISFGTTKDRMLVIEQCKNSKAVTIFIRGGNKMIIEEAKRSIHDA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 406 LCVIRNLIRDNRVVYGGGAAEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALAENSGMNPIQTMTEVRARQVKEV 485
Cdd:TIGR02343 401 LCVVRNLIKDSRIVYGGGAAEISCSLAVSQEADKYPGVEQYAIRAFADALETIPMALAENSGLDPIGTLSTLKSLQLKEK 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 296475689 486 NPALGIDCLHKGTNDMKHQHVIETLIGKKQQISLATQMVRMILKIDDIRKPG 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: 597.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 25 KSRLMGLEALKSHIMAAKAVANTMKTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVELSKSQDDEIGD 104
Cdd:cd00309 1 KEREFGEEARLSNINAAKALADAVKTTLGPKGMDKMLVDSLGDPTITNDGATILKEIEVEHPAAKLLVEVAKSQDDEVGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 105 GTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARIAIEHLDKISDSvlVDMKNTEPLIQTAKTTLGSKVVNSCHRQ 184
Cdd:cd00309 81 GTTTVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVP--IDVEDREELLKVATTSLNSKLVSGGDDF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 185 MAEIAVNAVLTVADMQrRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKQVEDAKIAILTCPFEPpkpktkh 264
Cdd:cd00309 159 LGELVVDAVLKVGKEN-GDVDLGVIRVEKKKGGSLEDSELVVGMVFDKGYLSPYMPKRLENAKILLLDCKLEY------- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 265 kldvtsvedfkalqkyekekfeemirqiketganLAICQWGFDDEANHLLLQNDLPAVRWVGGPEIELIAIATGGRIVPR 344
Cdd:cd00309 231 ----------------------------------VVIAEKGIDDEALHYLAKLGIMAVRRVRKEDLERIAKATGATIVSR 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 345 FSELTAEKLGFAGLVKEISFGttKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGA 424
Cdd:cd00309 277 LEDLTPEDLGTAGLVEETKIG--DEKYTFIEGCKGGKVATILLRGATEVELDEAERSLHDALCAVRAAVEDGGIVPGGGA 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 425 AEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALAENSGMNPIQTMTEVRARQVKEVNPAlGIDCLHKGTNDMKHQ 504
Cdd:cd00309 355 AEIELSKALEELAKTLPGKEQLGIEAFADALEVIPRTLAENAGLDPIEVVTKLRAKHAEGGGNA-GGDVETGEIVDMKEA 433
|
490 500
....*....|....*....|....*....
gi 296475689 505 HVIETLIGKKQQISLATQMVRMILKIDDI 533
Cdd:cd00309 434 GIIDPLKVKRQALKSATEAASLILTIDDI 462
|
|
| Cpn60_TCP1 |
pfam00118 |
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ... |
44-533 |
0e+00 |
|
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family and the TCP-1 (T-complex protein) family.
Pssm-ID: 395068 [Multi-domain] Cd Length: 489 Bit Score: 561.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 44 VANTMKTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVVLAGALLEEAEQL 123
Cdd:pfam00118 1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELEIQHPAAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEEAEKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 124 LDRGIHPIRIADGYEQAARIAIEHLDKIsDSVLVDMKNTEPLIQTAKTTLGSKVVNSCHRQMAEIAVNAVLTVADMQRrD 203
Cdd:pfam00118 81 LAAGVHPTTIIEGYEKALEKALEILDSI-ISIPVEDVDREDLLKVARTSLSSKIISRESDFLAKLVVDAVLAIPKNDG-S 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 204 VDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKQVEDAKIAILTCPFEPPKPKTKHKLDVTSVEDFKALQKYEKE 283
Cdd:pfam00118 159 FDLGNIGVVKILGGSLEDSELVDGVVLDKGPLHPDMPKRLENAKVLLLNCSLEYEKTETKATVVLSDAEQLERFLKAEEE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 284 KFEEMIRQIKETGANLAICQWGFDDEANHLLLQNDLPAVRWVGGPEIELIAIATGGRIVPRFSELTAEKLGFAGLVKEIS 363
Cdd:pfam00118 239 QILEIVEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMALRRVKKRDLERLAKATGARAVSSLDDLTPDDLGTAGKVEEEK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 364 FGttKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAEISCALAVSQEADKCPTL 443
Cdd:pfam00118 319 IG--DEKYTFIEGCKSPKAATILLRGATDHVLDEIERSIHDALCVVKNAIEDPRVVPGGGAVEMELARALREYAKSVSGK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 444 EQYAMRAFADALEVIPMALAENSGMNPIQTMTEVRARQVKEvNPALGIDCLHKGTNDMKHQHVIETLIGKKQQISLATQM 523
Cdd:pfam00118 397 EQLAIEAFAEALEVIPKTLAENAGLDPIEVLAELRAAHASG-EKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKSATEA 475
|
490
....*....|
gi 296475689 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: 546.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 15 PFLIIKDQdrKSRLMGLEALKSHIMAAKAVANTMKTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVEL 94
Cdd:NF041082 2 PILILKEG--TQRTSGRDAQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDVVITNDGVTILKEMDIEHPAAKMIVEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 95 SKSQDDEIGDGTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARIAIEHLDKIsdSVLVDMKNTEPLIQTAKTTLG 174
Cdd:NF041082 80 AKTQDDEVGDGTTTAVVLAGELLKKAEELLDQDIHPTIIAEGYRLAAEKALEILDEI--AIKVDPDDKETLKKIAATAMT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 175 SKVVNSCHRQMAEIAVNAVLTVADMQ-RRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKQVEDAKIAILTC 253
Cdd:NF041082 158 GKGAEAAKDKLADLVVDAVKAVAEKDgGYNVDLDNIKVEKKVGGSIEDSELVEGVVIDKERVHPGMPKRVENAKIALLDA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 254 PFEPPKPKTKHKLDVTSVEDFKALQKYEKEKFEEMIRQIKETGANLAICQWGFDDEANHLLLQNDLPAVRWVGGPEIELI 333
Cdd:NF041082 238 PLEVKKTEIDAKISITDPDQLQAFLDQEEKMLKEMVDKIADSGANVVFCQKGIDDLAQHYLAKEGILAVRRVKKSDMEKL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 334 AIATGGRIVPRFSELTAEKLGFAGLVKEISFGttKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLI 413
Cdd:NF041082 318 AKATGARIVTSIDDLSPEDLGYAGLVEERKVG--GDKMIFVEGCKNPKAVTILLRGGTEHVVDEVERALEDALRVVRVVL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 414 RDNRVVYGGGAAEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALAENSGMNPIQTMTEVRARQVKEVNPAlGIDC 493
Cdd:NF041082 396 EDGKVVAGGGAPEVELALRLREYAASVGGREQLAIEAFAEALEIIPRTLAENAGLDPIDALVELRSAHEKGNKTA-GLDV 474
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 296475689 494 LHKGTNDMKHQHVIETLIGKKQQISLATQMVRMILKIDDI 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: 531.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 17 LIIKDqdRKSRLMGLEALKSHIMAAKAVANTMKTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVELSK 96
Cdd:cd03343 2 LILKE--GTQRTSGRDAQRMNIAAAKAVAEAVRTTLGPKGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 97 SQDDEIGDGTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARIAIEHLDKISDSvlVDMKNTEPLIQTAKTTLGSK 176
Cdd:cd03343 80 TQDEEVGDGTTTAVVLAGELLEKAEDLLDQNIHPTVIIEGYRLAAEKALELLDEIAIK--VDPDDKDTLRKIAKTSLTGK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 177 VVNSCHRQMAEIAVNAVLTVADMQ--RRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKQVEDAKIAILTCP 254
Cdd:cd03343 158 GAEAAKDKLADLVVDAVLQVAEKRdgKYVVDLDNIKIEKKTGGSVDDTELIRGIVIDKEVVHPGMPKRVENAKIALLDAP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 255 FEPPKPKTKHKLDVTSVEDFKALQKYEKEKFEEMIRQIKETGANLAICQWGFDDEANHLLLQNDLPAVRWVGGPEIELIA 334
Cdd:cd03343 238 LEVKKTEIDAKIRITSPDQLQAFLEQEEAMLKEMVDKIADTGANVVFCQKGIDDLAQHYLAKAGILAVRRVKKSDMEKLA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 335 IATGGRIVPRFSELTAEKLGFAGLVKEISFGttKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIR 414
Cdd:cd03343 318 RATGAKIVTNIDDLTPEDLGEAELVEERKVG--DDKMVFVEGCKNPKAVTILLRGGTEHVVDELERALEDALRVVADALE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 415 DNRVVYGGGAAEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALAENSGMNPIQTMTEVRARQvKEVNPALGIDCL 494
Cdd:cd03343 396 DGKVVAGGGAVEIELAKRLREYARSVGGREQLAVEAFADALEEIPRTLAENAGLDPIDTLVELRAAH-EKGNKNAGLDVY 474
|
490 500 510
....*....|....*....|....*....|....*....
gi 296475689 495 HKGTNDMKHQHVIETLIGKKQQISLATQMVRMILKIDDI 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 296475689 15 PFLIIKDQdrKSRLMGLEALKSHIMAAKAVANTMKTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVEL 94
Cdd:NF041083 2 PVLILKEG--TQRTKGRDAQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDIVITNDGATILKEMDVQHPAAKMLVEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 95 SKSQDDEIGDGTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARIAIEHLDKISDSvlVDMKNTEPLIQTAKTTLG 174
Cdd:NF041083 80 AKTQDDEVGDGTTTAVVLAGELLKKAEELLDQNIHPTIIANGYRLAAEKAIEILDEIAEK--VDPDDRETLKKIAETSLT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 175 SKVVNSCHRQMAEIAVNAVLTVADmqRRD----VDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKQVEDAKIAI 250
Cdd:NF041083 158 SKGVEEARDYLAEIAVKAVKQVAE--KRDgkyyVDLDNIQIEKKHGGSIEDTQLIYGIVIDKEVVHPGMPKRVENAKIAL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 251 LTCPFEPPKPKTKHKLDVTSVEDFKALQKYEKEKFEEMIRQIKETGANLAICQWGFDDEANHLLLQNDLPAVRWVGGPEI 330
Cdd:NF041083 236 LDAPLEVKKTEIDAEIRITDPDQLQKFLDQEEKMLKEMVDKIKATGANVVFCQKGIDDLAQHYLAKAGILAVRRVKKSDM 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 331 ELIAIATGGRIVPRFSELTAEKLGFAGLVKEISFGTtkDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIR 410
Cdd:NF041083 316 EKLAKATGARIVTNIDDLTPEDLGYAELVEERKVGD--DKMVFVEGCKNPKAVTILIRGGTEHVVDEAERALEDALSVVA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 411 NLIRDNRVVYGGGAAEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALAENSGMNPIQTMTEVRARQVKEvNPALG 490
Cdd:NF041083 394 DAVEDGKIVAGGGAPEVELAKRLREYAATVGGREQLAVEAFAEALEIIPRTLAENAGLDPIDILVKLRSAHEKG-KKWAG 472
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 296475689 491 IDCLHKGTNDMKHQHVIETLIGKKQQISLATQMVRMILKIDDI 533
Cdd:NF041083 473 INVFTGEVVDMWELGVIEPLRVKTQAIKSATEAATMILRIDDV 515
|
|
| thermosome_arch |
TIGR02339 |
thermosome, various subunits, archaeal; Thermosome is the name given to the archaeal rather ... |
15-533 |
2.27e-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: 502.29 E-value: 2.27e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 15 PFLIIKDQdrKSRLMGLEALKSHIMAAKAVANTMKTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVEL 94
Cdd:TIGR02339 1 PVFILKEG--TQRTSGRDAQRNNIAAAKAVAEAVKSTLGPRGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 95 SKSQDDEIGDGTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARIAIEHLDKISDSVLVDmkNTEPLIQTAKTTLG 174
Cdd:TIGR02339 79 AKTQDEEVGDGTTTAVVLAGELLEKAEDLLEQDIHPTVIIEGYRKAAEKALEIIDEIATKISPE--DRDLLKKIAYTSLT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 175 SKVVNSCHRQ-MAEIAVNAVLTVADMQ---RRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKQVEDAKIAI 250
Cdd:TIGR02339 157 SKASAEVAKDkLADLVVEAVKQVAELRgdgKYYVDLDNIKIVKKKGGSIEDTELVEGIVVDKEVVHPGMPKRVENAKIAL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 251 LTCPFEPPKPKTKHKLDVTSVEDFKALQKYEKEKFEEMIRQIKETGANLAICQWGFDDEANHLLLQNDLPAVRWVGGPEI 330
Cdd:TIGR02339 237 LDAPLEVEKTEIDAKIRITDPDQIKKFLDQEEAMLKEMVDKIASAGANVVICQKGIDDVAQHYLAKAGILAVRRVKKSDI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 331 ELIAIATGGRIVPRFSELTAEKLGFAGLVKEISFGttKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIR 410
Cdd:TIGR02339 317 EKLARATGARIVSSIDEITESDLGYAELVEERKVG--EDKMVFVEGCKNPKAVTILLRGGTEHVVDELERSIQDALHVVA 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 411 NLIRDNRVVYGGGAAEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALAENSGMNPIQTMTEVRARQVKEvNPALG 490
Cdd:TIGR02339 395 NALEDGKIVAGGGAVEIELALRLRSYARSVGGREQLAIEAFADALEEIPRILAENAGLDPIDALVDLRAKHEKG-NKNAG 473
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 296475689 491 IDCLHKGTNDMKHQHVIETLIGKKQQISLATQMVRMILKIDDI 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 |
1.46e-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: 446.73 E-value: 1.46e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 35 KSHIMAAKAVANTMKTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVVLAG 114
Cdd:cd03338 11 LSNIQAAKAVADAIRTSLGPRGMDKMIQTGKGEVIITNDGATILKQMSVLHPAAKMLVELSKAQDIEAGDGTTSVVVLAG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 115 ALLEEAEQLLDRGIHPIRIADGYEQAARIAIEHLDKIsdSVLVDMKNTEPLIQTAKTTLGSKVVNSCHRQMAEIAVNAVL 194
Cdd:cd03338 91 ALLSACESLLKKGIHPTVISESFQIAAKKAVEILDSM--SIPVDLNDRESLIKSATTSLNSKVVSQYSSLLAPIAVDAVL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 195 TVADMQR-RDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSH-PQMPKQVEDAKIAILTCPFEPPKPKTKHKLDVTSVE 272
Cdd:cd03338 169 KVIDPATaTNVDLKDIRIVKKLGGTIEDTELVDGLVFTQKASKkAGGPTRIEKAKIGLIQFCLSPPKTDMDNNIVVNDYA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 273 DFKALQKYEKEKFEEMIRQIKETGANLAICQW-----GFDDEANHLLLQNDLPAVRWVGGPEIELIAIATGGRIVPRFSE 347
Cdd:cd03338 249 QMDRILREERKYILNMCKKIKKSGCNVLLIQKsilrdAVSDLALHFLAKLKIMVVKDIEREEIEFICKTIGCKPVASIDH 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 348 LTAEKLGFAGLVKEISFGTtkDKMLVIEQCKNS-RAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAE 426
Cdd:cd03338 329 FTEDKLGSADLVEEVSLGD--GKIVKITGVKNPgKTVTILVRGSNKLVLDEAERSLHDALCVIRCLVKKRALIPGGGAPE 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 427 ISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALAENSGMNPIQTMTEVRARQvKEVNPALGIDCLHKGTNDMKHQHV 506
Cdd:cd03338 407 IEIALQLSEWARTLTGVEQYCVRAFADALEVIPYTLAENAGLNPISIVTELRNRH-AQGEKNAGINVRKGAITNILEENV 485
|
490 500
....*....|....*....|....*..
gi 296475689 507 IETLIGKKQQISLATQMVRMILKIDDI 533
Cdd:cd03338 486 VQPLLVSTSAITLATETVRMILKIDDI 512
|
|
| chap_CCT_delta |
TIGR02342 |
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ... |
35-533 |
2.91e-139 |
|
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: 412.64 E-value: 2.91e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 35 KSHIMAAKAVANTMKTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVVLAG 114
Cdd:TIGR02342 12 TSNIVAAKAVADAIRTSLGPKGMDKMIQDGKGEVIITNDGATILKQMAVLHPAAKMLVELSKAQDIEAGDGTTSVVILAG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 115 ALLEEAEQLLDRGIHPIRIADGYEQAARIAIEHLDKISDSvlVDMKNTEPLIQTAKTTLGSKVVNSCHRQMAEIAVNAVL 194
Cdd:TIGR02342 92 ALLGACERLLNKGIHPTIISESFQSAADEAIKILDEMSIP--VDLSDREQLLKSATTSLSSKVVSQYSSLLAPLAVDAVL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 195 TVADMQR-RDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQ-MPKQVEDAKIAILTCPFEPPKPKTKHKLDVTSVE 272
Cdd:TIGR02342 170 KVIDPENaKNVDLNDIKVVKKLGGTIDDTELIEGLVFTQKASKSAgGPTRIEKAKIGLIQFQISPPKTDMENQIIVNDYA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 273 DFKALQKYEKEKFEEMIRQIKETGANLAICQW-----GFDDEANHLLLQNDLPAVRWVGGPEIELIAIATGGRIVPRFSE 347
Cdd:TIGR02342 250 QMDRVLKEERAYILNIVKKIKKTGCNVLLIQKsilrdAVNDLALHFLAKMKIMVVKDIEREEIEFICKTIGCKPIASIDH 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 348 LTAEKLGFAGLVKEIsfGTTKDKMLVIEQCKN-SRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAE 426
Cdd:TIGR02342 330 FTADKLGSAELVEEV--DSDGGKIIKITGIQNaGKTVTVVVRGSNKLVIDEAERSLHDALCVIRCLVKKRGLIAGGGAPE 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 427 ISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALAENSGMNPIQTMTEVRARQVKEvNPALGIDCLHKGTNDMKHQHV 506
Cdd:TIGR02342 408 IEIARRLSKYARTMKGVESYCVRAFADALEVIPYTLAENAGLNPIKVVTELRNRHANG-EKTAGISVRKGGITNMLEEHV 486
|
490 500
....*....|....*....|....*..
gi 296475689 507 IETLIGKKQQISLATQMVRMILKIDDI 533
Cdd:TIGR02342 487 LQPLLVTTSAITLASETVRSILKIDDI 513
|
|
| GroEL |
COG0459 |
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ... |
25-533 |
2.49e-125 |
|
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227 Cd Length: 497 Bit Score: 376.34 E-value: 2.49e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 25 KSRLMGLEALKSHIMAAKAVANTMKTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQI----AKLMVELSKSQDD 100
Cdd:COG0459 3 KQILFGEDARRANIRGVKALADAVKVTLGPKGRNVMLVKSFGDPTITNDGVTIAKEIELEDPFenmgAQLVKEVASKTND 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 101 EIGDGTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARIAIEHLDKISDSVlvdmKNTEPLIQTAKTTLGSKvvns 180
Cdd:COG0459 83 EAGDGTTTATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPV----DDKEELAQVATISANGD---- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 181 chRQMAEIAVNAVLTVADMQRrdvdfelIKVEgKVGGRLEDTKLIKGVIVDKDFSHPQ-------MPKQVEDAKIAIltc 253
Cdd:COG0459 155 --EEIGELIAEAMEKVGKDGV-------ITVE-EGKGLETELEVVEGMQFDKGYLSPYfvtdpekMPAELENAYILL--- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 254 pfeppkpkTKHKLdvTSVEDFKalqkyekekfeEMIRQIKETGANLAICQWGFDDEANHLLLQNDLPAVR---WVGGP-- 328
Cdd:COG0459 222 --------TDKKI--SSIQDLL-----------PLLEKVAQSGKPLLIIAEDIDGEALATLVVNGIRGVLrvvAVKAPgf 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 329 ------EIELIAIATGGRIV-----PRFSELTAEKLGFAGLVKEisfgtTKDKMLVIEQCKNSRAVTIFIRGGNKMIIEE 397
Cdd:COG0459 281 gdrrkaMLEDIAILTGGRVIsedlgLKLEDVTLDDLGRAKRVEV-----DKDNTTIVEGAGNPKAIVILVGAATEVEVKE 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 398 AKRSLHDALCVIRNLIRDnRVVYGGGAAEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALAENSGMNPIQTMTEV 477
Cdd:COG0459 356 RKRRVEDALHATRAAVEE-GIVPGGGAALLRAARALRELAAKLEGDEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKV 434
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 296475689 478 RARQvkevNPALGIDCLHKGTNDMKHQHVIETLIGKKQQISLATQMVRMILKIDDI 533
Cdd:COG0459 435 RAAK----DKGFGFDAATGEYVDMLEAGVIDPAKVKRSALQNAASVAGLILTTEAV 486
|
|
| TCP1_gamma |
cd03337 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ... |
20-533 |
1.81e-122 |
|
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: 368.16 E-value: 1.81e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 20 KDQDRKSRLmglealkSHIMAAKAVANTMKTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVELSKSQD 99
Cdd:cd03337 11 RESGRKAQL-------GNIQAAKTVADVIRTCLGPRAMLKMLLDPMGGIVLTNDGNAILREIDVAHPAAKSMIELSRTQD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 100 DEIGDGTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARIAIEHLDKISDSvlVDMKNTEPLIQTAKTTLGSKVVN 179
Cdd:cd03337 84 EEVGDGTTSVIILAGEILAVAEPFLERGIHPTVIIKAYRKALEDALKILEEISIP--VDVNDRAQMLKIIKSCIGTKFVS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 180 SCHRQMAEIAVNAVLTVA---DMQRRDVDFE-LIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKQVEDAKIAILTCPF 255
Cdd:cd03337 162 RWSDLMCNLALDAVKTVAveeNGRKKEIDIKrYAKVEKIPGGEIEDSRVLDGVMLNKDVTHPKMRRRIENPRIVLLDCPL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 256 EppkpktkhkldvtsvedfkalqkYekekfeemirqiketganLAICQWGFDDEANHLLLQNDLPAVRWVGGPEIELIAI 335
Cdd:cd03337 242 E-----------------------Y------------------LVITEKGVSDLAQHYLVKAGITALRRVRKTDNNRIAR 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 336 ATGGRIVPRFSELTAEKLGFAGLVKEISFGtTKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRD 415
Cdd:cd03337 281 ACGATIVNRPEELTESDVGTGAGLFEVKKI-GDEYFTFITECKDPKACTILLRGASKDVLNEVERNLQDAMAVARNIILN 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 416 NRVVYGGGAAEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALAENSGMNPIQTMTEVRARQVKEVNPALGIDCLH 495
Cdd:cd03337 360 PKLVPGGGATEMAVSHALSEKAKSIEGVEQWPYKAVASALEVIPRTLAQNCGANVIRTLTELRAKHAQGENSTWGIDGET 439
|
490 500 510
....*....|....*....|....*....|....*...
gi 296475689 496 KGTNDMKHQHVIETLIGKKQQISLATQMVRMILKIDDI 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 |
9.46e-118 |
|
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: 357.90 E-value: 9.46e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 15 PFLIIKDQDRksRLMGLEALKSHIMAAKAVANTMKTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVEL 94
Cdd:TIGR02344 1 PVLVLNQNTK--RESGRKAQLSNIQAAKAVADIIRTCLGPRSMLKMLLDPMGGIVMTNDGNAILREIDVAHPAAKSMIEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 95 SKSQDDEIGDGTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARIAIEHLDKIsdSVLVDMKNTEPLIQTAKTTLG 174
Cdd:TIGR02344 79 SRTQDEEVGDGTTSVIILAGEMLSVAEPFLEQNIHPTVIIRAYRKALDDALSVLEEI--SIPVDVNDDAAMLKLIQSCIG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 175 SKVVNSCHRQMAEIAVNAVLTVA--DMQRRDVDFE-LIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKQVEDAKIAIL 251
Cdd:TIGR02344 157 TKFVSRWSDLMCDLALDAVRTVQrdENGRKEIDIKrYAKVEKIPGGDIEDSCVLKGVMINKDVTHPKMRRYIENPRIVLL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 252 TCPFEPPKPKTKHKLDVTSVEDFKALQKYEKEKFEEMIRQIKETGANLAICQWGFDDEANHLLLQNDLPAVRWVGGPEIE 331
Cdd:TIGR02344 237 DCPLEYKKGESQTNIEITKEEDWNRILQMEEEYVQLMCEDIIAVKPDLVITEKGVSDLAQHYLLKANITAIRRVRKTDNN 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 332 LIAIATGGRIVPRFSELTAEKLGF-AGLVKEISFGttKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIR 410
Cdd:TIGR02344 317 RIARACGATIVNRPEELRESDVGTgCGLFEVKKIG--DEYFTFITECKDPKACTILLRGASKDILNEVERNLQDAMAVAR 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 411 NLIRDNRVVYGGGAAEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALAENSGMNPIQTMTEVRARQVKEVNPALG 490
Cdd:TIGR02344 395 NVLLDPKLVPGGGATEMAVSVALTEKSKKLEGVEQWPYRAVADALEIIPRTLAQNCGANVIRTLTELRAKHAQENNCTWG 474
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 296475689 491 IDCLHKGTNDMKHQHVIETLIGKKQQISLATQMVRMILKIDDI 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 |
1.07e-111 |
|
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.
Pssm-ID: 239452 [Multi-domain] Cd Length: 517 Bit Score: 342.00 E-value: 1.07e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 18 IIKDQDRKSRlmGLEALKSHIMAAKAVANTMKTSLGPNGLDKMM--VDKDGDVTVTNDGATILSMMDVDHQIAKLMVELS 95
Cdd:cd03336 1 ILKDGAQEEK--GETARLSSFVGAIAIGDLVKTTLGPKGMDKILqsVGRSGGVTVTNDGATILKSIGVDNPAAKVLVDIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 96 KSQDDEIGDGTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARIAIEHLDKISDSVLVDMKNT-EPLIQTAKTTLG 174
Cdd:cd03336 79 KVQDDEVGDGTTSVTVLAAELLREAEKLVAQKIHPQTIIEGYRMATAAAREALLSSAVDHSSDEEAFrEDLLNIARTTLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 175 SKVVNSCHRQMAEIAVNAVLTVADmqrrDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQmPKQVEDAKIAILTCP 254
Cdd:cd03336 159 SKILTQDKEHFAELAVDAVLRLKG----SGNLDAIQIIKKLGGSLKDSYLDEGFLLDKKIGVNQ-PKRIENAKILIANTP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 255 FEPPKPKT-KHKLDVTSVEDFKALQKYEKEKFEEMIRQIKETGANLAICQWGFDDEANHLLLQNDLPAVRWVGGPEIELI 333
Cdd:cd03336 234 MDTDKIKIfGAKVRVDSTAKVAEIEEAEKEKMKNKVEKILKHGINCFINRQLIYNYPEQLFADAGIMAIEHADFDGVERL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 334 AIATGGRIVPRFSELTAEKLGFAGLVKEISFGttKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLI 413
Cdd:cd03336 314 ALVTGGEIASTFDHPELVKLGTCKLIEEIMIG--EDKLIRFSGVAAGEACTIVLRGASQQILDEAERSLHDALCVLAQTV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 414 RDNRVVYGGGAAEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALAENSGMNPIQTMTEVRARQVKEVNPAlGIDC 493
Cdd:cd03336 392 KDTRVVLGGGCSEMLMAKAVEELAKKTPGKKSLAIEAFAKALRQLPTIIADNAGYDSAELVAQLRAAHYNGNTTA-GLDM 470
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 296475689 494 LHKGTNDMKHQHVIETLIGKKQQISLATQMVRMILKIDDIRK 535
Cdd:cd03336 471 RKGTVGDMKELGITESFKVKRQVLLSASEAAEMILRVDDIIK 512
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
36-533 |
8.34e-111 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 340.08 E-value: 8.34e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 36 SHIMAAKAVANTMKTSLGPNGLDKMMV-----DKDGDVTVTNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVV 110
Cdd:PTZ00212 26 QSFVGAIAVADLVKTTLGPKGMDKILQpmsegPRSGNVTVTNDGATILKSVWLDNPAAKILVDISKTQDEEVGDGTTSVV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 111 VLAGALLEEAEQLLDRGIHPIRIADGYEQAARIAIEHLDKISDSVLVDMKN-TEPLIQTAKTTLGSKVVNSCHRQMAEIA 189
Cdd:PTZ00212 106 VLAGELLREAEKLLDQKIHPQTIIEGWRMALDVARKALEEIAFDHGSDEEKfKEDLLNIARTTLSSKLLTVEKDHFAKLA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 190 VNAVLTVadmqRRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQmPKQVEDAKIAILTCPFEPPKPKT-KHKLDV 268
Cdd:PTZ00212 186 VDAVLRL----KGSGNLDYIQIIKKPGGTLRDSYLEDGFILEKKIGVGQ-PKRLENCKILVANTPMDTDKIKIyGAKVKV 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 269 TSVEDFKALQKYEKEKFEEMIRQIKETGANLAICQWGFDDEANHLLLQNDLPAVRWVGGPEIELIAIATGGRIVPRFSEL 348
Cdd:PTZ00212 261 DSMEKVAEIEAAEKEKMKNKVDKILAHGCNVFINRQLIYNYPEQLFAEAGIMAIEHADFDGMERLAAALGAEIVSTFDTP 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 349 TAEKLGFAGLVKEISFGttKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAEIS 428
Cdd:PTZ00212 341 EKVKLGHCDLIEEIMIG--EDKLIRFSGCAKGEACTIVLRGASTHILDEAERSLHDALCVLSQTVKDTRVVLGGGCSEML 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 429 CALAVSQEADKCPTLEQYAMRAFADALEVIPMALAENSGMNPIQTMTEVRARQVKEVNPAlGIDCLHKGTNDMKHQHVIE 508
Cdd:PTZ00212 419 MANAVEELAKKVEGKKSLAIEAFAKALRQIPTIIADNGGYDSAELVSKLRAEHYKGNKTA-GIDMEKGTVGDMKELGITE 497
|
490 500
....*....|....*....|....*
gi 296475689 509 TLIGKKQQISLATQMVRMILKIDDI 533
Cdd:PTZ00212 498 SYKVKLSQLCSATEAAEMILRVDDI 522
|
|
| TCP1_eta |
cd03340 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ... |
15-531 |
5.97e-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: 5.97e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 15 PFLIIKDQDRKSRlmGLEALKSHIMAAKAVANTMKTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVEL 94
Cdd:cd03340 1 PIILLKEGTDTSQ--GKGQLISNINACQAIADAVRTTLGPRGMDKLIVDGRGKVTISNDGATILKLLDIVHPAAKTLVDI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 95 SKSQDDEIGDGTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARIAIEHLDKISdsvlVDMKNTEP------LIQT 168
Cdd:cd03340 79 AKSQDAEVGDGTTSVVVLAGEFLKEAKPFIEDGVHPQIIIRGYRKALQLAIEKIKEIA----VNIDKEDKeeqrelLEKC 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 169 AKTTLGSKVVNSCHRQMAEIAVNAVLTVADmqrrDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFS---HPQMPKQVED 245
Cdd:cd03340 155 AATALNSKLIASEKEFFAKMVVDAVLSLDD----DLDLDMIGIKKVPGGSLEDSQLVNGVAFKKTFSyagFEQQPKKFKN 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 246 AKIAILTCPFEPPKPKTKHKLDVTSVEDFKALQKYEKEKFEEMIRQIKETGANLAICQWGFDDEANHLLLQNDLPAVRWV 325
Cdd:cd03340 231 PKILLLNVELELKAEKDNAEVRVEDPEEYQAIVDAEWKIIYDKLEKIVKSGANVVLSKLPIGDLATQYFADRDIFCAGRV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 326 GGPEIELIAIATGGRIVPRFSELTAEKLGFAGLVKEISFGttKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDA 405
Cdd:cd03340 311 PEEDLKRVAQATGGSIQTTVSNITDDVLGTCGLFEERQVG--GERYNIFTGCPKAKTCTIILRGGAEQFIEEAERSLHDA 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 406 LCVIRNLIRDNRVVYGGGAAEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALAENSGMNPIQTMTEVRARQVKEV 485
Cdd:cd03340 389 IMIVRRAIKNDSVVAGGGAIEMELSKYLRDYSRTIAGKQQLVINAFAKALEIIPRQLCDNAGFDATDILNKLRQKHAQGG 468
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 296475689 486 NPALGIDCLHKGTNDMKHQHVIETLIGKKQQISLATQMVRMILKID 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 |
3.89e-106 |
|
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.
Pssm-ID: 239451 Cd Length: 527 Bit Score: 327.70 E-value: 3.89e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 27 RLMGLEALKSHIMAAKAVANTMKTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGT 106
Cdd:cd03335 3 RTSGQDVRTQNVTAAMAIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDKEVGDGT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 107 TGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARIAIEHLDKiSDSVLVDMKNTEPLIQTAKTTLGSKVVNSCHRQMA 186
Cdd:cd03335 83 TSVVIIAAELLKRANELVKQKIHPTTIISGYRLACKEAVKYIKE-HLSISVDNLGKESLINVAKTSMSSKIIGADSDFFA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 187 EIAVNAVLTVADM-QRRDV-----DFELIKVEGKvggRLEDTKLIKGVIVDKDFSHPQMPKQVEDAKIAILTCPFEppkp 260
Cdd:cd03335 162 NMVVDAILAVKTTnEKGKTkypikAVNILKAHGK---SAKESYLVNGYALNCTRASQGMPTRVKNAKIACLDFNLQ---- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 261 KTKHKLDV----TSVEDFKALQKYEKEKFEEMIRQIKETGANLAICQWGFDDEANHLLLQNDLPAVRWVGGPEIELIAIA 336
Cdd:cd03335 235 KTKMKLGVqvvvTDPEKLEKIRQRESDITKERIKKILAAGANVVLTTGGIDDMCLKYFVEAGAMAVRRVKKEDLRRIAKA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 337 TGGRIVPRFSELTAE------KLGFAGLVKEISFGttKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIR 410
Cdd:cd03335 315 TGATLVSTLANLEGEetfdpsYLGEAEEVVQERIG--DDELILIKGTKKRSSASIILRGANDFMLDEMERSLHDALCVVK 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 411 NLIRDNRVVYGGGAAEisCALAVSQE--ADKCPTLEQYAMRAFADALEVIPMALAENSGMNPIQTMTEVRAR----QVKE 484
Cdd:cd03335 393 RTLESNSVVPGGGAVE--TALSIYLEnfATTLGSREQLAIAEFAEALLVIPKTLAVNAAKDATELVAKLRAYhaaaQVKP 470
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 296475689 485 VNPAL---GIDcLHKGT-NDMKHQHVIETLIGKKQQISLATQMVRMILKIDDIRK 535
Cdd:cd03335 471 DKKHLkwyGLD-LINGKvRDNLEAGVLEPTVSKIKSLKFATEAAITILRIDDLIK 524
|
|
| chap_CCT_eta |
TIGR02345 |
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ... |
15-537 |
5.32e-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: 322.09 E-value: 5.32e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 15 PFLIIKDQDRKSRlmGLEALKSHIMAAKAVANTMKTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVEL 94
Cdd:TIGR02345 3 TIVLLKEGTDTSQ--GKGQLISNINACVAIAEALKTTLGPRGMDKLIVGSNGKATISNDGATILKLLDIVHPAAKTLVDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 95 SKSQDDEIGDGTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARIAIEHLDKISDSV-LVDMKNTEPLIQTAKTTL 173
Cdd:TIGR02345 81 AKSQDAEVGDGTTSVTILAGELLKEAKPFIEEGVHPQLIIRCYREALSLAVEKIKEIAVTIdEEKGEQRELLEKCAATAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 174 GSKVVNSCHRQMAEIAVNAVLTvadMQRRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFS---HPQMPKQVEDAKIAI 250
Cdd:TIGR02345 161 SSKLISHNKEFFSKMIVDAVLS---LDRDDLDLKLIGIKKVQGGALEDSQLVNGVAFKKTFSyagFEQQPKKFANPKILL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 251 LTCPFEPPKPKTKHKLDVTSVEDFKALQKYEKEKFEEMIRQIKETGANLAICQWGFDDEANHLLLQNDLPAVRWVGGPEI 330
Cdd:TIGR02345 238 LNVELELKAEKDNAEIRVEDVEDYQAIVDAEWAIIFRKLEKIVESGANVVLSKLPIGDLATQYFADRDIFCAGRVSAEDL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 331 ELIAIATGGRIVPRFSELTAEKLGFAGLVKEISFGttKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIR 410
Cdd:TIGR02345 318 KRVIKACGGSIQSTTSDLEADVLGTCALFEERQIG--SERYNYFTGCPHAKTCTIILRGGAEQFIEEAERSLHDAIMIVR 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 411 NLIRDNRVVYGGGAAEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALAENSGMNPIQTMTEVRARQVKEvNPALG 490
Cdd:TIGR02345 396 RALKNKKIVAGGGAIEMELSKCLRDYSKTIDGKQQLIINAFAKALEIIPRQLCENAGFDSIEILNKLRSRHAKG-GKWYG 474
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 296475689 491 IDCLHKGTNDMKHQHVIETLIGKKQQISLATQMVRMILKIDD-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 |
2.08e-103 |
|
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT alpha chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.
Pssm-ID: 274081 [Multi-domain] Cd Length: 536 Bit Score: 321.28 E-value: 2.08e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 27 RLMGLEALKSHIMAAKAVANTMKTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGT 106
Cdd:TIGR02340 7 RTSGQDVRTQNVTAAMAIANIVKTSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDREVGDGT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 107 TGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARIAIEHLDKiSDSVLVDMKNTEPLIQTAKTTLGSKVVNSCHRQMA 186
Cdd:TIGR02340 87 TSVVIIAAELLKRADELVKNKIHPTSVISGYRLACKEAVKYIKE-NLSVSVDELGREALINVAKTSMSSKIIGLDSDFFS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 187 EIAVNAVLTVADM-QRRDVDF--ELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKQVEDAKIAILTCPFEppkpKTK 263
Cdd:TIGR02340 166 NIVVDAVLAVKTTnENGETKYpiKAINILKAHGKSARESMLVKGYALNCTVASQQMPKRIKNAKIACLDFNLQ----KAK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 264 HKLDVT-SVEDFKALQKYEKEKFE---EMIRQIKETGANLAICQWGFDDEANHLLLQNDLPAVRWVGGPEIELIAIATGG 339
Cdd:TIGR02340 242 MALGVQiVVDDPEKLEQIRQREADitkERIKKILDAGANVVLTTGGIDDMCLKYFVEAGAMGVRRCKKEDLKRIAKATGA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 340 RIVPRFSELTAE------KLGFAGLVKEISFGttKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLI 413
Cdd:TIGR02340 322 TLVSTLADLEGEetfeasYLGFADEVVQERIA--DDECILIKGTKKRKSASIILRGANDFMLDEMERSLHDALCVVKRTL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 414 RDNRVVYGGGAAEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALAENSGMNPIQTMTEVRARQVKE-VNPA---- 488
Cdd:TIGR02340 400 ESNSVVPGGGAVEAALSIYLENFATTLGSREQLAIAEFARALLIIPKTLAVNAAKDSTELVAKLRAYHAAAqLKPEkkhl 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 296475689 489 --LGIDCLHKGTNDMKHQHVIETLIGKKQQISLATQMVRMILKIDD-IRKPGESEE 541
Cdd:TIGR02340 480 kwYGLDLVNGKIRDNKEAGVLEPTVSKVKSLKFATEAAITILRIDDlIKLNPEQSK 535
|
|
| TCP1_theta |
cd03341 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ... |
32-533 |
1.98e-102 |
|
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: 316.47 E-value: 1.98e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 32 EALKSHIMAAKAVANTMKTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVV 111
Cdd:cd03341 8 EAVLRNIEACKELSQITRTSYGPNGMNKMVINHLEKLFVTSDAATILRELEVQHPAAKLLVMASQMQEEEIGDGTNLVVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 112 LAGALLEEAEQLLDRGIHPIRIADGYEQAARIAIEHLDKISDSVLVDMKNTEPLIQTAKTTLGSKVV-NSCHrqMAEIAV 190
Cdd:cd03341 88 LAGELLEKAEELLRMGLHPSEIIEGYEKALKKALEILEELVVYKIEDLRNKEEVSKALKTAIASKQYgNEDF--LSPLVA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 191 NAVLTVADMQRRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDfSHPQMpKQVEDAKIAILTCPFeppkpktkhkldvts 270
Cdd:cd03341 166 EACISVLPENIGNFNVDNIRVVKILGGSLEDSKVVRGMVFKRE-PEGSV-KRVKKAKVAVFSCPF--------------- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 271 vedfkalqkyekekfeemirqikETGANLAICQWGFDDEANHLLLQNDLPAVRWVGGPEIELIAIATGGRIVPRFSELTA 350
Cdd:cd03341 229 -----------------------DIGVNVIVAGGSVGDLALHYCNKYGIMVIKINSKFELRRLCRTVGATPLPRLGAPTP 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 351 EKLGFAGLVKEISFGTTkdKMLVIEQCKNSRAV-TIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAEISC 429
Cdd:cd03341 286 EEIGYCDSVYVEEIGDT--KVVVFRQNKEDSKIaTIVLRGATQNILDDVERAIDDGVNVFKSLTKDGRFVPGAGATEIEL 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 430 ALAVSQEADKCPTLEQYAMRAFADALEVIPMALAENSGMNPIQTMTEVRARQVKE-VNPALGIDCLHKGTNDMKHQHVIE 508
Cdd:cd03341 364 AKKLKEYGEKTPGLEQYAIKKFAEAFEVVPRTLAENAGLDATEVLSELYAAHQKGnKSAGVDIESGDEGTKDAKEAGIFD 443
|
490 500
....*....|....*....|....*
gi 296475689 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 |
1.78e-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: 305.49 E-value: 1.78e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 32 EALKSHIMAAKAVANTMKTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVV 111
Cdd:TIGR02346 18 EAVIKNIEACKELSQITRTSLGPNGMNKMVINHLEKLFVTNDAATILRELEVQHPAAKLLVMASEMQENEIGDGTNLVLV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 112 LAGALLEEAEQLLDRGIHPIRIADGYEQAARIAIEHLDKISDSVLVDMKNTEPLIQTAKTTLGSKVVNScHRQMAEIAVN 191
Cdd:TIGR02346 98 LAGELLNKAEELIRMGLHPSEIIKGYEMALKKAMEILEELVVWEVKDLRDKDELIKALKASISSKQYGN-EDFLAQLVAQ 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 192 AVLTVADMQRRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFShpQMPKQVEDAKIAILTCPFEPPKPKTKHKLDVTSV 271
Cdd:TIGR02346 177 ACSTVLPKNPQNFNVDNIRVCKILGGSLSNSEVLKGMVFNREAE--GSVKSVKNAKVAVFSCPLDTATTETKGTVLIHNA 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 272 EDFKALQKYEKEKFEEMIRQIKETGANLAICQWGFDDEANHLLLQNDLPAVRWVGGPEIELIAIATGGRIVPRFSELTAE 351
Cdd:TIGR02346 255 EELLNYSKGEENQIEAMIKAIADSGVNVIVTGGSVGDMALHYLNKYNIMVLKIPSKFELRRLCKTVGATPLPRLGAPTPE 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 352 KLGFAGLVKEISFGTtkDKMLVIEQCK-NSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAEISCA 430
Cdd:TIGR02346 335 EIGYVDSVYVSEIGG--DKVTVFKQENgDSKISTIILRGSTDNLLDDIERAIDDGVNTVKALVKDGRLLPGAGATEIELA 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 431 LAVSQEADKCPTLEQYAMRAFADALEVIPMALAENSGMNPIQTMTEVRARQvKEVNPALGID--CLHKGTNDMKHQHVIE 508
Cdd:TIGR02346 413 SRLTKYGEKLPGLDQYAIKKFAEAFEIIPRTLAENAGLNANEVIPKLYAAH-KKGNKSKGIDieAESDGVKDASEAGIYD 491
|
490 500
....*....|....*....|....*
gi 296475689 509 TLIGKKQQISLATQMVRMILKIDDI 533
Cdd:TIGR02346 492 MLATKKWAIKLATEAAVTVLRVDQI 516
|
|
| chap_CCT_beta |
TIGR02341 |
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ... |
18-535 |
1.06e-93 |
|
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT beta chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.
Pssm-ID: 274082 Cd Length: 519 Bit Score: 295.62 E-value: 1.06e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 18 IIKDQDRKSRlmGLEALKSHIMAAKAVANTMKTSLGPNGLDKMMV--DKDGDVTVTNDGATILSMMDVDHQIAKLMVELS 95
Cdd:TIGR02341 2 IFKDGADEER--AENARLSSFVGAIAIGDLVKSTLGPKGMDKILQssSSDASIMVTNDGATILKSIGVDNPAAKVLVDMS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 96 KSQDDEIGDGTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARIAIEHLDKIS-DSVLVDMKNTEPLIQTAKTTLG 174
Cdd:TIGR02341 80 KVQDDEVGDGTTSVTVLAAELLREAEKLINQKIHPQTIIAGYREATKAARDALLKSAvDNGSDEVKFRQDLMNIARTTLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 175 SKVVNSCHRQMAEIAVNAVLTVadmqRRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQmPKQVEDAKIAILTCP 254
Cdd:TIGR02341 160 SKILSQHKDHFAQLAVDAVLRL----KGSGNLEAIQIIKKLGGSLADSYLDEGFLLDKKIGVNQ-PKRIENAKILIANTG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 255 FEPPKPKT-KHKLDVTSVEDFKALQKYEKEKFEEMIRQIKETGANLAICQWGFDDEANHLLLQNDLPAVRWVGGPEIELI 333
Cdd:TIGR02341 235 MDTDKVKIfGSRVRVDSTAKVAELEHAEKEKMKEKVEKILKHGINCFINRQLIYNYPEQLFADAGVMAIEHADFEGVERL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 334 AIATGGRIVPRFSELTAEKLGFAGLVKEISFGttKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLI 413
Cdd:TIGR02341 315 ALVTGGEIVSTFDHPELVKLGSCDLIEEIMIG--EDKLLKFSGVKLGEACTIVLRGATQQILDEAERSLHDALCVLSQTV 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 414 RDNRVVYGGGAAEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALAENSGMNPIQTMTEVRArQVKEVNPALGIDc 493
Cdd:TIGR02341 393 KESRTVLGGGCSEMLMSKAVTQEAQRTPGKEALAVEAFARALRQLPTIIADNAGFDSAELVAQLRA-AHYNGNTTMGLD- 470
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 296475689 494 LHKGT-NDMKHQHVIETLIGKKQQISLATQMVRMILKIDDIRK 535
Cdd:TIGR02341 471 MNEGTiADMRQLGITESYKVKRAVVSSAAEAAEVILRVDNIIK 513
|
|
| chap_CCT_zeta |
TIGR02347 |
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ... |
33-539 |
1.16e-84 |
|
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: 272.38 E-value: 1.16e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 33 ALKSHIMAAKAVANTMKTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVVL 112
Cdd:TIGR02347 17 ALMMNINAARGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEMQIQHPTASMIARAATAQDDITGDGTTSTVLL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 113 AGALLEEAEQLLDRGIHPIRIADGYEQAARIAIEHLDKISdSVLVDMKNTEPLIQTAKTTLGSKVVNSCHRQMAEIAVNA 192
Cdd:TIGR02347 97 IGELLKQAERYILEGVHPRIITEGFEIARKEALQFLDKFK-VKKEDEVDREFLLNVARTSLRTKLPADLADQLTEIVVDA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 193 VLTVADmQRRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKQVEDAKIAILTCPFEPPKPKTKHKLDVTSVE 272
Cdd:TIGR02347 176 VLAIKK-DGEDIDLFMVEIMEMKHKSATDTTLIRGLVLDHGARHPDMPRRVKNAYILTCNVSLEYEKTEVNSGFFYSSAE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 273 DFKALQKYEKE-------KFEEMIRQIKETGAN---LAICQWGFDDEANHLLLQNDLPAVRWVGGPEIELIAIATGGRIV 342
Cdd:TIGR02347 255 QREKLVKAERKfvddrvkKIIELKKKVCGKSPDkgfVVINQKGIDPPSLDLLAKEGIMALRRAKRRNMERLTLACGGEAL 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 343 PRFSELTAEKLGFAGLVKEISFGttKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGG 422
Cdd:TIGR02347 335 NSVEDLTPECLGWAGLVYETTIG--EEKYTFIEECKNPKSCTILIKGPNDHTIAQIKDAVRDGLRAVKNAIEDKCVVPGA 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 423 GAAEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALAENSGMNPIQTMTEVRARQVKEVNPaLGIDcLHKGTN-DM 501
Cdd:TIGR02347 413 GAFEIAAYRHLKEYKKSVKGKAKLGVEAFANALLVIPKTLAENSGFDAQDTLVKLEDEHDEGGEV-VGVD-LNTGEPiDP 490
|
490 500 510
....*....|....*....|....*....|....*...
gi 296475689 502 KHQHVIETLIGKKQQISLATQMVRMILKIDDIRKPGES 539
Cdd:TIGR02347 491 EIKGIWDNYRVKKQLIQSATVIASQLLLVDEVMRAGRS 528
|
|
| TCP1_zeta |
cd03342 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
32-537 |
2.05e-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: 2.05e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 32 EALKSHIMAAKAVANTMKTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVV 111
Cdd:cd03342 12 QALAVNISAAKGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLSEMQIQHPTASMIARAATAQDDITGDGTTSNVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 112 LAGALLEEAEQLLDRGIHPIRIADGYEQAARIAIEHLDKISDSVLVDMkNTEPLIQTAKTTLGSKVVNSCHRQMAEIAVN 191
Cdd:cd03342 92 LIGELLKQAERYIQEGVHPRIITEGFELAKNKALKFLESFKVPVEIDT-DRELLLSVARTSLRTKLHADLADQLTEIVVD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 192 AVLTVadmQRRDVDFELIKVE-GKVGGRLE-DTKLIKGVIVDKDFSHPQMPKQVEDAkiAILTCPFeppkpktkhkldvt 269
Cdd:cd03342 171 AVLAI---YKPDEPIDLHMVEiMQMQHKSDsDTKLIRGLVLDHGARHPDMPKRVENA--YILTCNV-------------- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 270 SVEdfkalqkYEK-EKFEEMIrqiketgANLAICQWGFDDEANHLLLQNDLPAVRWVGGPEIELIAIATGGRIVPRFSEL 348
Cdd:cd03342 232 SLE-------YEKtEVNSGFF-------YSVVINQKGIDPPSLDMLAKEGILALRRAKRRNMERLTLACGGVAMNSVDDL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 349 TAEKLGFAGLVKEISFGttKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAEIS 428
Cdd:cd03342 298 SPECLGYAGLVYERTLG--EEKYTFIEGVKNPKSCTILIKGPNDHTITQIKDAIRDGLRAVKNAIEDKCVVPGAGAFEVA 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 429 CALAVSQEADKCPTLEQYAMRAFADALEVIPMALAENSGMNPIQTMTEVRaRQVKEVNPALGIDCLHKGTNDMKHQHVIE 508
Cdd:cd03342 376 LYAHLKEFKKSVKGKAKLGVQAFADALLVIPKTLAENSGLDVQETLVKLQ-DEYAEGGQVGGVDLDTGEPMDPESEGIWD 454
|
490 500
....*....|....*....|....*....
gi 296475689 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 |
6.30e-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: 236.21 E-value: 6.30e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 163 EPLIQTAKTTLGSKVvNSCHRQMAEIAVNAVLTVADMQRrDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKQ 242
Cdd:cd03333 2 ELLLQVATTSLNSKL-SSWDDFLGKLVVDAVLKVGPDNR-MDDLGVIKVEKIPGGSLEDSELVVGVVFDKGYASPYMPKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 243 VEDAKIAILTCPFEPpkpktkhkldvtsvedfkalqkyekekfeemirqiketganLAICQWGFDDEANHLLLQNDLPAV 322
Cdd:cd03333 80 LENAKILLLDCPLEY-----------------------------------------VVIAEKGIDDLALHYLAKAGIMAV 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 323 RWVGGPEIELIAIATGGRIVPRFSELTAEKLGFAGLVKEISFGTtkDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSL 402
Cdd:cd03333 119 RRVKKEDLERIARATGATIVSSLEDLTPEDLGTAELVEETKIGE--EKLTFIEGCKGGKAATILLRGATEVELDEVKRSL 196
|
250
....*....|...
gi 296475689 403 HDALCVIRNLIRD 415
Cdd:cd03333 197 HDALCAVRAAVEE 209
|
|
| GroEL |
cd03344 |
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ... |
30-494 |
2.37e-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: 75.57 E-value: 2.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 30 GLEALKSHIMAAKAVANTMKTSLGPNGLDKMMVDKDGDVTVTNDGATI---LSMMD-VDHQIAKLMVELSKSQDDEIGDG 105
Cdd:cd03344 6 GEEARKALLRGVNKLADAVKVTLGPKGRNVVIEKSFGSPKITKDGVTVakeIELEDpFENMGAQLVKEVASKTNDVAGDG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 106 TTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARIAIEHLDKISDSVlvdmKNTEPLIQTAKT------TLGSKVVN 179
Cdd:cd03344 86 TTTATVLARAIIKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKPV----KTKEEIAQVATIsangdeEIGELIAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 180 SchrqMAEIAVNAVLTVADmqrrdvdfelikvegkvGGRLEDT-KLIKGVIVDKDFSHPQMPKQV-------EDAKIAIl 251
Cdd:cd03344 162 A----MEKVGKDGVITVEE-----------------GKTLETElEVVEGMQFDRGYLSPYFVTDPekmevelENPYILL- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 252 tcpfeppkpkTKHKLDvtSVEDFKALqkyekekfeemIRQIKETGANLAICQWGFDDEANHLLLQNDLP------AVRwv 325
Cdd:cd03344 220 ----------TDKKIS--SIQELLPI-----------LELVAKAGRPLLIIAEDVEGEALATLVVNKLRgglkvcAVK-- 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 326 gGPE--------IELIAIATGGRIVP-----RFSELTAEKLGFAGLVKeisfgTTKDKMLV-------------IEQCKN 379
Cdd:cd03344 275 -APGfgdrrkamLEDIAILTGGTVISeelglKLEDVTLEDLGRAKKVV-----VTKDDTTIiggagdkaaikarIAQIRK 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 380 SRAVT----------------------IFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNrVVYGGGAAEISCALAVSQEA 437
Cdd:cd03344 349 QIEETtsdydkeklqerlaklsggvavIKVGGATEVELKEKKDRVEDALNATRAAVEEG-IVPGGGVALLRASPALDKLK 427
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 296475689 438 DKCPtLEQYAMRAFADALEVIPMALAENSGMNPiqtmtEVRARQVKEVNPALGIDCL 494
Cdd:cd03344 428 ALNG-DEKLGIEIVRRALEAPLRQIAENAGVDG-----SVVVEKVLESPDGFGYDAA 478
|
|
| Fab1_TCP |
cd03334 |
TCP-1 like domain of the eukaryotic phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinase Fab1. ... |
187-413 |
1.86e-13 |
|
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: 70.33 E-value: 1.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 187 EIAVNAVLTVADMQRRDVDF-------ELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKQVEDAKIAILTCPFEPPK 259
Cdd:cd03334 21 DILLPLVWKAASNVKPDVRAgddmdirQYVKIKKIPGGSPSDSEVVDGVVFTKNVAHKRMPSKIKNPRILLLQGPLEYQR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 260 PKTKhkldVTSVEDFKAlqkYEKEKFEEMIRQIKETGANLAICQWGFDDEANHLLLQNDLPAVRWVGGPEIELIAIATGG 339
Cdd:cd03334 101 VENK----LLSLDPVIL---QEKEYLKNLVSRIVALRPDVILVEKSVSRIAQDLLLEAGITLVLNVKPSVLERISRCTGA 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 296475689 340 RIVPRFSELTAE-KLGFAGLVKEISF----GTTKDKMLvIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLI 413
Cdd:cd03334 174 DIISSMDDLLTSpKLGTCESFRVRTYveehGRSKTLMF-FEGCPKELGCTILLRGGDLEELKKVKRVVEFMVFAAYHLK 251
|
|
| GroEL |
TIGR02348 |
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ... |
32-213 |
7.58e-13 |
|
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES cytosolic chaperonin. It is found in bacteria, organelles derived from bacteria, and occasionally in the Archaea. The bacterial GroEL/GroES group I chaperonin is replaced a group II chaperonin, usually called the thermosome in the Archaeota and CCT (chaperone-containing TCP) in the Eukaryota. GroEL, thermosome subunits, and CCT subunits all fall under the scope of pfam00118. [Protein fate, Protein folding and stabilization]
Pssm-ID: 274089 Cd Length: 524 Bit Score: 70.78 E-value: 7.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 32 EALKSHIMAAKAVANTMKTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQI----AKLMVELSKSQDDEIGDGTT 107
Cdd:TIGR02348 9 EARKALLRGVDKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDKFenmgAQLVKEVASKTNDVAGDGTT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 108 GVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARIAIEHLDKISdsvlVDMKNTEPLIQTAKTTLGS--KVVNSCHRQM 185
Cdd:TIGR02348 89 TATVLAQAIVKEGLKNVAAGANPIELKRGIEKAVEAVVEELKKLS----KPVKGKKEIAQVATISANNdeEIGSLIAEAM 164
|
170 180
....*....|....*....|....*...
gi 296475689 186 AEIAVNAVLTVADMQRRDVDFELikVEG 213
Cdd:TIGR02348 165 EKVGKDGVITVEESKSLETELEV--VEG 190
|
|
| groEL |
PRK12850 |
chaperonin GroEL; Reviewed |
18-356 |
1.45e-10 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237231 Cd Length: 544 Bit Score: 63.58 E-value: 1.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 18 IIKDQDRKSRLM-GLEALkshimaakavANTMKTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKL---MV- 92
Cdd:PRK12850 6 IRFSTDARDRLLrGVNIL----------ANAVKVTLGPKGRNVVLEKSFGAPRITKDGVTVAKEIELEDKFENMgaqMVk 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 93 ELSKSQDDEIGDGTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARIAIEHLDKIsdsvlvdmkntepliqtAKTT 172
Cdd:PRK12850 76 EVASKTNDLAGDGTTTATVLAQAIVREGAKLVAAGMNPMDLKRGIDLAVAAVVDELKKI-----------------AKKV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 173 LGSKVVnschRQMAEIAVNAVLTVADMQRRDVDfeliKVeGKVG------GRLEDTKL--IKGVIVDKDFSHP------- 237
Cdd:PRK12850 139 TSSKEI----AQVATISANGDESIGEMIAEAMD----KV-GKEGvitveeAKTLGTELdvVEGMQFDRGYLSPyfvtnpe 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 238 QMPKQVEDAKIAIltcpfeppkpktkHKLDVTSVEDFKALqkyekekfeemIRQIKETGANLAICQWGFDDEANHLLLQN 317
Cdd:PRK12850 210 KMRAELEDPYILL-------------HEKKISNLQDLLPI-----------LEAVVQSGRPLLIIAEDVEGEALATLVVN 265
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 296475689 318 DL------PAVRWVG-----GPEIELIAIATGGRIVP-----RFSELTAEKLGFA 356
Cdd:PRK12850 266 KLrgglksVAVKAPGfgdrrKAMLEDIAVLTGGQVISedlgiKLENVTLDMLGRA 320
|
|
| PTZ00114 |
PTZ00114 |
Heat shock protein 60; Provisional |
24-213 |
2.32e-10 |
|
Heat shock protein 60; Provisional
Pssm-ID: 185455 Cd Length: 555 Bit Score: 63.01 E-value: 2.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 24 RKSRLMGLEALkshimaAKAVAntmkTSLGPNGLDKMMVDKDGDVTVTNDGATIL-------SMMDVDhqiAKLMVELSK 96
Cdd:PTZ00114 24 RQSLLKGIERL------ADAVA----VTLGPKGRNVIIEQEYGSPKITKDGVTVAkaiefsdRFENVG---AQLIRQVAS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 97 SQDDEIGDGTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARIAIEHLDKISDSVlvdmKNTEPLIQTAKTT---- 172
Cdd:PTZ00114 91 KTNDKAGDGTTTATILARAIFREGCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQSRPV----KTKEDILNVATISangd 166
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 296475689 173 --LGSKVVNSchrqMAEIAVNAVLTVADmqRRDVDFELIKVEG 213
Cdd:PTZ00114 167 veIGSLIADA----MDKVGKDGTITVED--GKTLEDELEVVEG 203
|
|
| groEL |
PRK12849 |
chaperonin GroEL; Reviewed |
43-367 |
8.01e-10 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237230 Cd Length: 542 Bit Score: 61.36 E-value: 8.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 43 AVANTMKTSLGPNGLDkMMVDKD-GDVTVTNDGATILSMMDVDHQI----AKLMVELSKSQDDEIGDGTTGVVVLAGALL 117
Cdd:PRK12849 21 KLADAVKVTLGPKGRN-VVIDKSfGAPTITKDGVSIAKEIELEDPFenlgAQLVKEVASKTNDVAGDGTTTATVLAQALV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 118 EEAEQLLDRGIHPIRIADGYEQAARIAIEHLDKISDSVlvdmKNTEPLIQTAKT------TLGSKVVnschRQMAEIAVN 191
Cdd:PRK12849 100 QEGLKNVAAGANPMDLKRGIDKAVEAVVEELKALARPV----SGSEEIAQVATIsangdeEIGELIA----EAMEKVGKD 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 192 AVLTVADMQrrDVDFELIKVEgkvggrledtklikGVIVDKDFSHPQM----PKQV---EDAKIAIltcpfeppkpkTKH 264
Cdd:PRK12849 172 GVITVEESK--TLETELEVTE--------------GMQFDRGYLSPYFvtdpERMEavlEDPLILL-----------TDK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 265 KLdvTSVEDFKALqkyekekfeemIRQIKETGANLAICQWGFDDEANHLLLQNDLPA---VRWVGGPE--------IELI 333
Cdd:PRK12849 225 KI--SSLQDLLPL-----------LEKVAQSGKPLLIIAEDVEGEALATLVVNKLRGglkVAAVKAPGfgdrrkamLEDI 291
|
330 340 350
....*....|....*....|....*....|....*....
gi 296475689 334 AIATGGRIVPR-----FSELTAEKLGFAGLVkEISFGTT 367
Cdd:PRK12849 292 AILTGGTVISEdlglkLEEVTLDDLGRAKRV-TITKDNT 329
|
|
| PLN03167 |
PLN03167 |
Chaperonin-60 beta subunit; Provisional |
33-159 |
1.26e-09 |
|
Chaperonin-60 beta subunit; Provisional
Pssm-ID: 215611 [Multi-domain] Cd Length: 600 Bit Score: 60.71 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 33 ALKSHIMAAKAVANTMKTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQI----AKLMVELSKSQDDEIGDGTTG 108
Cdd:PLN03167 67 AIKKLQAGVNKLADLVGVTLGPKGRNVVLESKYGSPKIVNDGVTVAKEVELEDPVenigAKLVRQAAAKTNDLAGDGTTT 146
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 296475689 109 VVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARIAIEHLDKIS----DSVLVDM 159
Cdd:PLN03167 147 SVVLAQGLIAEGVKVVAAGANPVQITRGIEKTAKALVKELKKMSkeveDSELADV 201
|
|
| groEL |
PRK12851 |
chaperonin GroEL; Reviewed |
41-155 |
3.44e-09 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 171770 Cd Length: 541 Bit Score: 59.37 E-value: 3.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 41 AKAVANTMKTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQI----AKLMVELSKSQDDEIGDGTTGVVVLAGAL 116
Cdd:PRK12851 20 VNILADAVKVTLGPKGRNVVIDKSFGAPTITNDGVTIAKEIELEDKFenmgAQMVREVASKTNDVAGDGTTTATVLAQAI 99
|
90 100 110
....*....|....*....|....*....|....*....
gi 296475689 117 LEEAEQLLDRGIHPIRIADGYEQAARIAIEHLDKISDSV 155
Cdd:PRK12851 100 VREGAKAVAAGANPMDLKRGIDRAVAAVVEELKANARPV 138
|
|
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
43-152 |
4.03e-09 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 58.98 E-value: 4.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 43 AVANTMKTSLGPNG----LDKmmvdKDGDVTVTNDGATILSMMDVDHQI----AKLMVELSKSQDDEIGDGTTGVVVLAG 114
Cdd:PRK00013 21 KLADAVKVTLGPKGrnvvLEK----SFGAPTITKDGVTVAKEIELEDPFenmgAQLVKEVASKTNDVAGDGTTTATVLAQ 96
|
90 100 110
....*....|....*....|....*....|....*...
gi 296475689 115 ALLEEAEQLLDRGIHPIRIADGYEQAARIAIEHLDKIS 152
Cdd:PRK00013 97 AIVREGLKNVAAGANPMDLKRGIDKAVEAAVEELKKIS 134
|
|
| PRK14104 |
PRK14104 |
chaperonin GroEL; Provisional |
30-210 |
7.59e-09 |
|
chaperonin GroEL; Provisional
Pssm-ID: 172594 Cd Length: 546 Bit Score: 58.12 E-value: 7.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 30 GLEALKSHIMAAKAVANTMKTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQI----AKLMVELSKSQDDEIGDG 105
Cdd:PRK14104 9 GVDARDRMLRGVDILANAVKVTLGPKGRNVVLDKSFGAPRITKDGVTVAKEIELEDKFenmgAQMVREVASKSADAAGDG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 106 TTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARIAIEHLDKISDSVLVDMKNTEplIQTAKTTLGSKVVNSCHRQM 185
Cdd:PRK14104 89 TTTATVLAQAIVREGAKSVAAGMNPMDLKRGIDLAVEAVVADLVKNSKKVTSNDEIAQ--VGTISANGDAEIGKFLADAM 166
|
170 180
....*....|....*....|....*
gi 296475689 186 AEIAVNAVLTVADMQRRDVDFELIK 210
Cdd:PRK14104 167 KKVGNEGVITVEEAKSLETELDVVE 191
|
|
| groEL |
PRK12852 |
chaperonin GroEL; Reviewed |
44-213 |
1.71e-07 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237232 Cd Length: 545 Bit Score: 53.70 E-value: 1.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 44 VANTMKTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQI----AKLMVELSKSQDDEIGDGTTGVVVLAGALLEE 119
Cdd:PRK12852 23 LANAVKVTLGPKGRNVVIEKSFGAPRITKDGVTVAKEIELEDKFenmgAQMVREVASKTNDLAGDGTTTATVLAQAIVRE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 120 AEQLLDRGIHPIRIADGYEQAARIAIEHLDKISDSVlvdmKNTEPLIQTA------KTTLGSKVVNSchrqMAEIAVNAV 193
Cdd:PRK12852 103 GAKAVAAGMNPMDLKRGIDIAVAAVVKDIEKRAKPV----ASSAEIAQVGtisangDAAIGKMIAQA----MQKVGNEGV 174
|
170 180
....*....|....*....|
gi 296475689 194 LTVADMQRRDVDFELikVEG 213
Cdd:PRK12852 175 ITVEENKSLETEVDI--VEG 192
|
|
| groEL |
CHL00093 |
chaperonin GroEL |
20-174 |
3.12e-07 |
|
chaperonin GroEL
Pssm-ID: 177025 Cd Length: 529 Bit Score: 53.18 E-value: 3.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 20 KDQDRKSRLMGLEALkshimaAKAVANTmktsLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVEL----- 94
Cdd:CHL00093 8 QDNARRALERGMDIL------AEAVSVT----LGPKGRNVVLEKKYGSPQIVNDGVTIAKEIELEDHIENTGVALirqaa 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296475689 95 SKSqDDEIGDGTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARIAIEHLDKISDSVlvdmKNTEPLIQTAKTTLG 174
Cdd:CHL00093 78 SKT-NDVAGDGTTTATVLAYAIVKQGMKNVAAGANPISLKRGIEKATQYVVSQIAEYARPV----EDIQAITQVASISAG 152
|
|
| |
