|
Name |
Accession |
Description |
Interval |
E-value |
| chap_CCT_gamma |
TIGR02344 |
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ... |
4-529 |
0e+00 |
|
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: 948.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 4 PVVVMNTQsgGERQTGRKAQLSNIAAAKIVADIIRSCLGPKAMLKMLLDPMGGIVLTNDGHAILREIEVSHPAAKSMIEL 83
Cdd:TIGR02344 1 PVLVLNQN--TKRESGRKAQLSNIQAAKAVADIIRTCLGPRSMLKMLLDPMGGIVMTNDGNAILREIDVAHPAAKSMIEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 84 SRTQDEEVGDGTTSVIILGGEILAQALPQLERNIHPVVIISAFKRALKDALEIIDEISTPIDINDDEAMYQLISSSIGTK 163
Cdd:TIGR02344 79 SRTQDEEVGDGTTSVIILAGEMLSVAEPFLEQNIHPTVIIRAYRKALDDALSVLEEISIPVDVNDDAAMLKLIQSCIGTK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 164 FVSRWSKLMCSLALKAVRTVTWEaGTGKREVDIKRYARIEKVPGGEIEDSRVLDGVMLNKDITHPKMRRRIENPRIILLD 243
Cdd:TIGR02344 159 FVSRWSDLMCDLALDAVRTVQRD-ENGRKEIDIKRYAKVEKIPGGDIEDSCVLKGVMINKDVTHPKMRRYIENPRIVLLD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 244 CPLEYKKGESQTQIEITKEEDWNRILQIEEEQVEAMCKHILELKPDLVITEKGVSDLAQHYFMKANVTALRRVRKTDNNR 323
Cdd:TIGR02344 238 CPLEYKKGESQTNIEITKEEDWNRILQMEEEYVQLMCEDIIAVKPDLVITEKGVSDLAQHYLLKANITAIRRVRKTDNNR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 324 IARATGATIVNRVEDLQESDVGTQCGLFEIEKIGDEYFTFLTKCNTPKACTVLLRGPSKDILNEVERNLQDAMGVARNVM 403
Cdd:TIGR02344 318 IARACGATIVNRPEELRESDVGTGCGLFEVKKIGDEYFTFITECKDPKACTILLRGASKDILNEVERNLQDAMAVARNVL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 404 FHPRLSPGGGATEMAVSVRLGQLAKSIEGVQQWPYRAVAEALEVIPRTLVQNAGASPVRVLTDLRAKHA-EGKSSWGING 482
Cdd:TIGR02344 398 LDPKLVPGGGATEMAVSVALTEKSKKLEGVEQWPYRAVADALEIIPRTLAQNCGANVIRTLTELRAKHAqENNCTWGIDG 477
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 389623377 483 DTGGLADMKEYGVWEPEAIKVQSMKTAIEAACLLLRVDDICSAKKAQ 529
Cdd:TIGR02344 478 ETGKIVDMKEKGIWEPLAVKLQTYKTAIESACLLLRIDDIVSGVKKK 524
|
|
| TCP1_gamma |
cd03337 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ... |
4-525 |
0e+00 |
|
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: 931.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 4 PVVVMNTqsGGERQTGRKAQLSNIAAAKIVADIIRSCLGPKAMLKMLLDPMGGIVLTNDGHAILREIEVSHPAAKSMIEL 83
Cdd:cd03337 1 PVLVLNQ--NTKRESGRKAQLGNIQAAKTVADVIRTCLGPRAMLKMLLDPMGGIVLTNDGNAILREIDVAHPAAKSMIEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 84 SRTQDEEVGDGTTSVIILGGEILAQALPQLERNIHPVVIISAFKRALKDALEIIDEISTPIDINDDEAMYQLISSSIGTK 163
Cdd:cd03337 79 SRTQDEEVGDGTTSVIILAGEILAVAEPFLERGIHPTVIIKAYRKALEDALKILEEISIPVDVNDRAQMLKIIKSCIGTK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 164 FVSRWSKLMCSLALKAVRTVTWEAGTGKREVDIKRYARIEKVPGGEIEDSRVLDGVMLNKDITHPKMRRRIENPRIILLD 243
Cdd:cd03337 159 FVSRWSDLMCNLALDAVKTVAVEENGRKKEIDIKRYAKVEKIPGGEIEDSRVLDGVMLNKDVTHPKMRRRIENPRIVLLD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 244 CPLEYkkgesqtqieitkeedwnrilqieeeqveamckhilelkpdLVITEKGVSDLAQHYFMKANVTALRRVRKTDNNR 323
Cdd:cd03337 239 CPLEY-----------------------------------------LVITEKGVSDLAQHYLVKAGITALRRVRKTDNNR 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 324 IARATGATIVNRVEDLQESDVGTQCGLFEIEKIGDEYFTFLTKCNTPKACTVLLRGPSKDILNEVERNLQDAMGVARNVM 403
Cdd:cd03337 278 IARACGATIVNRPEELTESDVGTGAGLFEVKKIGDEYFTFITECKDPKACTILLRGASKDVLNEVERNLQDAMAVARNII 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 404 FHPRLSPGGGATEMAVSVRLGQLAKSIEGVQQWPYRAVAEALEVIPRTLVQNAGASPVRVLTDLRAKHAE-GKSSWGING 482
Cdd:cd03337 358 LNPKLVPGGGATEMAVSHALSEKAKSIEGVEQWPYKAVASALEVIPRTLAQNCGANVIRTLTELRAKHAQgENSTWGIDG 437
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 389623377 483 DTGGLADMKEYGVWEPEAIKVQSMKTAIEAACLLLRVDDICSA 525
Cdd:cd03337 438 ETGDIVDMKELGIWDPLAVKAQTYKTAIEAACMLLRIDDIVSG 480
|
|
| chaperonin_type_I_II |
cd00309 |
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ... |
14-522 |
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: 604.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 14 GERQTGRKAQLSNIAAAKIVADIIRSCLGPKAMLKMLLDPMGGIVLTNDGHAILREIEVSHPAAKSMIELSRTQDEEVGD 93
Cdd:cd00309 1 KEREFGEEARLSNINAAKALADAVKTTLGPKGMDKMLVDSLGDPTITNDGATILKEIEVEHPAAKLLVEVAKSQDDEVGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 94 GTTSVIILGGEILAQALPQLERNIHPVVIISAFKRALKDALEIIDEISTPIDINDDEAMYQLISSSIGTKFVSRWSKLMC 173
Cdd:cd00309 81 GTTTVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVPIDVEDREELLKVATTSLNSKLVSGGDDFLG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 174 SLALKAVRTVTweagtGKREVDIKRYARIEKVPGGEIEDSRVLDGVMLNKDITHPKMRRRIENPRIILLDCPLEYkkges 253
Cdd:cd00309 161 ELVVDAVLKVG-----KENGDVDLGVIRVEKKKGGSLEDSELVVGMVFDKGYLSPYMPKRLENAKILLLDCKLEY----- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 254 qtqieitkeedwnrilqieeeqveamckhilelkpdLVITEKGVSDLAQHYFMKANVTALRRVRKTDNNRIARATGATIV 333
Cdd:cd00309 231 ------------------------------------VVIAEKGIDDEALHYLAKLGIMAVRRVRKEDLERIAKATGATIV 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 334 NRVEDLQESDVGTqCGLFEIEKIGDEYFTFLTKCNTPKACTVLLRGPSKDILNEVERNLQDAMGVARNVMFHPRLSPGGG 413
Cdd:cd00309 275 SRLEDLTPEDLGT-AGLVEETKIGDEKYTFIEGCKGGKVATILLRGATEVELDEAERSLHDALCAVRAAVEDGGIVPGGG 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 414 ATEMAVSVRLGQLAKSIEGVQQWPYRAVAEALEVIPRTLVQNAGASPVRVLTDLRAKHAEGKSSWGINGDTGGLADMKEY 493
Cdd:cd00309 354 AAEIELSKALEELAKTLPGKEQLGIEAFADALEVIPRTLAENAGLDPIEVVTKLRAKHAEGGGNAGGDVETGEIVDMKEA 433
|
490 500
....*....|....*....|....*....
gi 389623377 494 GVWEPEAIKVQSMKTAIEAACLLLRVDDI 522
Cdd:cd00309 434 GIIDPLKVKRQALKSATEAASLILTIDDI 462
|
|
| Cpn60_TCP1 |
pfam00118 |
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ... |
33-526 |
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: 598.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 33 VADIIRSCLGPKAMLKMLLDPMGGIVLTNDGHAILREIEVSHPAAKSMIELSRTQDEEVGDGTTSVIILGGEILAQALPQ 112
Cdd:pfam00118 1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELEIQHPAAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEEAEKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 113 LERNIHPVVIISAFKRALKDALEIIDEI-STPIDINDDEAMYQLISSSIGTKFVSRWSKLMCSLALKAVRTVTWEAgtgk 191
Cdd:pfam00118 81 LAAGVHPTTIIEGYEKALEKALEILDSIiSIPVEDVDREDLLKVARTSLSSKIISRESDFLAKLVVDAVLAIPKND---- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 192 REVDIKRyARIEKVPGGEIEDSRVLDGVMLNKDITHPKMRRRIENPRIILLDCPLEYKKGESQTQIEITKEEDWNRILQI 271
Cdd:pfam00118 157 GSFDLGN-IGVVKILGGSLEDSELVDGVVLDKGPLHPDMPKRLENAKVLLLNCSLEYEKTETKATVVLSDAEQLERFLKA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 272 EEEQVEAMCKHILELKPDLVITEKGVSDLAQHYFMKANVTALRRVRKTDNNRIARATGATIVNRVEDLQESDVGTqCGLF 351
Cdd:pfam00118 236 EEEQILEIVEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMALRRVKKRDLERLAKATGARAVSSLDDLTPDDLGT-AGKV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 352 EIEKIGDEYFTFLTKCNTPKACTVLLRGPSKDILNEVERNLQDAMGVARNVMFHPRLSPGGGATEMAVSVRLGQLAKSIE 431
Cdd:pfam00118 315 EEEKIGDEKYTFIEGCKSPKAATILLRGATDHVLDEIERSIHDALCVVKNAIEDPRVVPGGGAVEMELARALREYAKSVS 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 432 GVQQWPYRAVAEALEVIPRTLVQNAGASPVRVLTDLRAKHAEGKSSWGINGDTGGLADMKEYGVWEPEAIKVQSMKTAIE 511
Cdd:pfam00118 395 GKEQLAIEAFAEALEVIPKTLAENAGLDPIEVLAELRAAHASGEKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKSATE 474
|
490
....*....|....*
gi 389623377 512 AACLLLRVDDICSAK 526
Cdd:pfam00118 475 AASTILRIDDIIKAK 489
|
|
| cpn60 |
cd03343 |
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ... |
13-526 |
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: 529.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 13 GGERQTGRKAQLSNIAAAKIVADIIRSCLGPKAMLKMLLDPMGGIVLTNDGHAILREIEVSHPAAKSMIELSRTQDEEVG 92
Cdd:cd03343 7 GTQRTSGRDAQRMNIAAAKAVAEAVRTTLGPKGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAKTQDEEVG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 93 DGTTSVIILGGEILAQALPQLERNIHPVVIISAFKRALKDALEIIDEISTPIDINDDEAMYQLISSSIGTKFVSRWSKLM 172
Cdd:cd03343 87 DGTTTAVVLAGELLEKAEDLLDQNIHPTVIIEGYRLAAEKALELLDEIAIKVDPDDKDTLRKIAKTSLTGKGAEAAKDKL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 173 CSLALKAVRTVTwEAGTGKREVDIKrYARIEKVPGGEIEDSRVLDGVMLNKDITHPKMRRRIENPRIILLDCPLEYKKGE 252
Cdd:cd03343 167 ADLVVDAVLQVA-EKRDGKYVVDLD-NIKIEKKTGGSVDDTELIRGIVIDKEVVHPGMPKRVENAKIALLDAPLEVKKTE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 253 SQTQIEITKEEDWNRILQIEEEQVEAMCKHILELKPDLVITEKGVSDLAQHYFMKANVTALRRVRKTDNNRIARATGATI 332
Cdd:cd03343 245 IDAKIRITSPDQLQAFLEQEEAMLKEMVDKIADTGANVVFCQKGIDDLAQHYLAKAGILAVRRVKKSDMEKLARATGAKI 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 333 VNRVEDLQESDVGTqCGLFEIEKIGDEYFTFLTKCNTPKACTVLLRGPSKDILNEVERNLQDAMGVARNVMFHPRLSPGG 412
Cdd:cd03343 325 VTNIDDLTPEDLGE-AELVEERKVGDDKMVFVEGCKNPKAVTILLRGGTEHVVDELERALEDALRVVADALEDGKVVAGG 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 413 GATEMAVSVRLGQLAKSIEGVQQWPYRAVAEALEVIPRTLVQNAGASPVRVLTDLRAKHAEGKSSWGINGDTGGLADMKE 492
Cdd:cd03343 404 GAVEIELAKRLREYARSVGGREQLAVEAFADALEEIPRTLAENAGLDPIDTLVELRAAHEKGNKNAGLDVYTGEVVDMLE 483
|
490 500 510
....*....|....*....|....*....|....
gi 389623377 493 YGVWEPEAIKVQSMKTAIEAACLLLRVDDICSAK 526
Cdd:cd03343 484 KGVIEPLRVKKQAIKSATEAATMILRIDDVIAAK 517
|
|
| thermosome_beta |
NF041083 |
thermosome subunit beta; |
3-526 |
0e+00 |
|
thermosome subunit beta;
Pssm-ID: 469010 Cd Length: 519 Bit Score: 527.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 3 APVVVMntQSGGERQTGRKAQLSNIAAAKIVADIIRSCLGPKAMLKMLLDPMGGIVLTNDGHAILREIEVSHPAAKSMIE 82
Cdd:NF041083 1 QPVLIL--KEGTQRTKGRDAQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDIVITNDGATILKEMDVQHPAAKMLVE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 83 LSRTQDEEVGDGTTSVIILGGEILAQALPQLERNIHPVVIISAFKRALKDALEIIDEISTPIDINDDEAMYQLISSSIGT 162
Cdd:NF041083 79 VAKTQDDEVGDGTTTAVVLAGELLKKAEELLDQNIHPTIIANGYRLAAEKAIEILDEIAEKVDPDDRETLKKIAETSLTS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 163 KFVSRWSKLMCSLALKAVRTVTWEAGtGKREVDIKrYARIEKVPGGEIEDSRVLDGVMLNKDITHPKMRRRIENPRIILL 242
Cdd:NF041083 159 KGVEEARDYLAEIAVKAVKQVAEKRD-GKYYVDLD-NIQIEKKHGGSIEDTQLIYGIVIDKEVVHPGMPKRVENAKIALL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 243 DCPLEYKKGESQTQIEITKEEDWNRILQIEEEQVEAMCKHILELKPDLVITEKGVSDLAQHYFMKANVTALRRVRKTDNN 322
Cdd:NF041083 237 DAPLEVKKTEIDAEIRITDPDQLQKFLDQEEKMLKEMVDKIKATGANVVFCQKGIDDLAQHYLAKAGILAVRRVKKSDME 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 323 RIARATGATIVNRVEDLQESDVGTqCGLFEIEKIGDEYFTFLTKCNTPKACTVLLRGPSKDILNEVERNLQDAMGVARNV 402
Cdd:NF041083 317 KLAKATGARIVTNIDDLTPEDLGY-AELVEERKVGDDKMVFVEGCKNPKAVTILIRGGTEHVVDEAERALEDALSVVADA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 403 MFHPRLSPGGGATEMAVSVRLGQLAKSIEGVQQWPYRAVAEALEVIPRTLVQNAGASPVRVLTDLRAKHAEGKSSWGING 482
Cdd:NF041083 396 VEDGKIVAGGGAPEVELAKRLREYAATVGGREQLAVEAFAEALEIIPRTLAENAGLDPIDILVKLRSAHEKGKKWAGINV 475
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 389623377 483 DTGGLADMKEYGVWEPEAIKVQSMKTAIEAACLLLRVDDICSAK 526
Cdd:NF041083 476 FTGEVVDMWELGVIEPLRVKTQAIKSATEAATMILRIDDVIAAK 519
|
|
| thermosome_alpha |
NF041082 |
thermosome subunit alpha; |
4-526 |
0e+00 |
|
thermosome subunit alpha;
Pssm-ID: 469009 Cd Length: 518 Bit Score: 520.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 4 PVVVMntQSGGERQTGRKAQLSNIAAAKIVADIIRSCLGPKAMLKMLLDPMGGIVLTNDGHAILREIEVSHPAAKSMIEL 83
Cdd:NF041082 2 PILIL--KEGTQRTSGRDAQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDVVITNDGVTILKEMDIEHPAAKMIVEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 84 SRTQDEEVGDGTTSVIILGGEILAQALPQLERNIHPVVIISAFKRALKDALEIIDEISTPIDINDDEAMYQLISSSIGTK 163
Cdd:NF041082 80 AKTQDDEVGDGTTTAVVLAGELLKKAEELLDQDIHPTIIAEGYRLAAEKALEILDEIAIKVDPDDKETLKKIAATAMTGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 164 FVSRWSKLMCSLALKAVRTVTWEAGTGKREVD-IKryarIEKVPGGEIEDSRVLDGVMLNKDITHPKMRRRIENPRIILL 242
Cdd:NF041082 160 GAEAAKDKLADLVVDAVKAVAEKDGGYNVDLDnIK----VEKKVGGSIEDSELVEGVVIDKERVHPGMPKRVENAKIALL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 243 DCPLEYKKGESQTQIEITKEEDWNRILQIEEEQVEAMCKHILELKPDLVITEKGVSDLAQHYFMKANVTALRRVRKTDNN 322
Cdd:NF041082 236 DAPLEVKKTEIDAKISITDPDQLQAFLDQEEKMLKEMVDKIADSGANVVFCQKGIDDLAQHYLAKEGILAVRRVKKSDME 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 323 RIARATGATIVNRVEDLQESDVGTqCGLFEIEKIGDEYFTFLTKCNTPKACTVLLRGPSKDILNEVERNLQDAMGVARNV 402
Cdd:NF041082 316 KLAKATGARIVTSIDDLSPEDLGY-AGLVEERKVGGDKMIFVEGCKNPKAVTILLRGGTEHVVDEVERALEDALRVVRVV 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 403 MFHPRLSPGGGATEMAVSVRLGQLAKSIEGVQQWPYRAVAEALEVIPRTLVQNAGASPVRVLTDLRAKHAEGKSSWGING 482
Cdd:NF041082 395 LEDGKVVAGGGAPEVELALRLREYAASVGGREQLAIEAFAEALEIIPRTLAENAGLDPIDALVELRSAHEKGNKTAGLDV 474
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 389623377 483 DTGGLADMKEYGVWEPEAIKVQSMKTAIEAACLLLRVDDICSAK 526
Cdd:NF041082 475 YTGKVVDMLEIGVVEPLRVKTQAIKSATEAAVMILRIDDVIAAA 518
|
|
| thermosome_arch |
TIGR02339 |
thermosome, various subunits, archaeal; Thermosome is the name given to the archaeal rather ... |
4-525 |
2.96e-177 |
|
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: 509.61 E-value: 2.96e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 4 PVVVMntQSGGERQTGRKAQLSNIAAAKIVADIIRSCLGPKAMLKMLLDPMGGIVLTNDGHAILREIEVSHPAAKSMIEL 83
Cdd:TIGR02339 1 PVFIL--KEGTQRTSGRDAQRNNIAAAKAVAEAVKSTLGPRGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 84 SRTQDEEVGDGTTSVIILGGEILAQALPQLERNIHPVVIISAFKRALKDALEIIDEISTPIDINDDEAMYQLISSSIGTK 163
Cdd:TIGR02339 79 AKTQDEEVGDGTTTAVVLAGELLEKAEDLLEQDIHPTVIIEGYRKAAEKALEIIDEIATKISPEDRDLLKKIAYTSLTSK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 164 FVSRWSK-LMCSLALKAVRTVTWEAGTGKREVDIKrYARIEKVPGGEIEDSRVLDGVMLNKDITHPKMRRRIENPRIILL 242
Cdd:TIGR02339 159 ASAEVAKdKLADLVVEAVKQVAELRGDGKYYVDLD-NIKIVKKKGGSIEDTELVEGIVVDKEVVHPGMPKRVENAKIALL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 243 DCPLEYKKGESQTQIEITKEEDWNRILQIEEEQVEAMCKHILELKPDLVITEKGVSDLAQHYFMKANVTALRRVRKTDNN 322
Cdd:TIGR02339 238 DAPLEVEKTEIDAKIRITDPDQIKKFLDQEEAMLKEMVDKIASAGANVVICQKGIDDVAQHYLAKAGILAVRRVKKSDIE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 323 RIARATGATIVNRVEDLQESDVGTqCGLFEIEKIGDEYFTFLTKCNTPKACTVLLRGPSKDILNEVERNLQDAMGVARNV 402
Cdd:TIGR02339 318 KLARATGARIVSSIDEITESDLGY-AELVEERKVGEDKMVFVEGCKNPKAVTILLRGGTEHVVDELERSIQDALHVVANA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 403 MFHPRLSPGGGATEMAVSVRLGQLAKSIEGVQQWPYRAVAEALEVIPRTLVQNAGASPVRVLTDLRAKHAEGKSSWGING 482
Cdd:TIGR02339 397 LEDGKIVAGGGAVEIELALRLRSYARSVGGREQLAIEAFADALEEIPRILAENAGLDPIDALVDLRAKHEKGNKNAGINV 476
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 389623377 483 DTGGLADMKEYGVWEPEAIKVQSMKTAIEAACLLLRVDDICSA 525
Cdd:TIGR02339 477 FTGEIEDMLELGVIEPLRVKEQAIKSATEAATMILRIDDVIAA 519
|
|
| TCP1_epsilon |
cd03339 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ... |
4-522 |
3.07e-135 |
|
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: 402.83 E-value: 3.07e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 4 PVVVMNTQSGGERQTGRKAQLSNIAAAKIVADIIRSCLGPKAMLKMLLDPMGGIVLTNDGHAILREIEVSHPAAKSMIEL 83
Cdd:cd03339 6 PFIIVREQEKKKRLKGLEAHKSHILAAKSVANILRTSLGPRGMDKILVSPDGEVTVTNDGATILEKMDVDHQIAKLLVEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 84 SRTQDEEVGDGTTSVIILGGEILAQALPQLERNIHPVVIISAFKRALKDALEIIDEISTPIDINDD--EAMYQLISSSIG 161
Cdd:cd03339 86 SKSQDDEIGDGTTGVVVLAGALLEQAEKLLDRGIHPIRIADGYEQACKIAVEHLEEIADKIEFSPDnkEPLIQTAMTSLG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 162 TKFVSRWSKLMCSLALKAVRTVtweAGTGKREVD---IKryarIEKVPGGEIEDSRVLDGVMLNKDITHPKMRRRIENPR 238
Cdd:cd03339 166 SKIVSRCHRQFAEIAVDAVLSV---ADLERKDVNfelIK----VEGKVGGRLEDTKLVKGIVIDKDFSHPQMPKEVKDAK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 239 IILLDCPLEYKKGESQTQIEITKEEDWNRILQIEEEQVEAMCKHILELKPDLVITEKGVSDLAQHYFMKANVTALRRVRK 318
Cdd:cd03339 239 IAILTCPFEPPKPKTKHKLDITSVEDYKKLQEYEQKYFREMVEQVKDAGANLVICQWGFDDEANHLLLQNGLPAVRWVGG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 319 TDNNRIARATGATIVNRVEDLQESDVGTqCGLfeIEKIG----DEYFTFLTKCNTPKACTVLLRGPSKDILNEVERNLQD 394
Cdd:cd03339 319 VEIELIAIATGGRIVPRFEDLSPEKLGK-AGL--VREISfgttKDKMLVIEGCPNSKAVTIFIRGGNKMIIEEAKRSLHD 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 395 AMGVARNVMFHPRLSPGGGATEMAVSVRLGQLAKSIEGVQQWPYRAVAEALEVIPRTLVQNAGASPVRVLTDLRAKH-AE 473
Cdd:cd03339 396 ALCVVRNLIRDNRIVYGGGAAEISCSLAVEKAADKCSGIEQYAMRAFADALESIPLALAENSGLNPIETLSEVKARQvKE 475
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 389623377 474 GKSSWGINGDTGGLADMKEYGVWEPEAIKVQSMKTAIEAACLLLRVDDI 522
Cdd:cd03339 476 KNPHLGIDCLGRGTNDMKEQKVFETLISKKQQILLATQVVKMILKIDDV 524
|
|
| TCP1_eta |
cd03340 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ... |
21-528 |
9.83e-131 |
|
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: 390.88 E-value: 9.83e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 21 KAQL-SNIAAAKIVADIIRSCLGPKAMLKMLLDPMGGIVLTNDGHAILREIEVSHPAAKSMIELSRTQDEEVGDGTTSVI 99
Cdd:cd03340 15 KGQLiSNINACQAIADAVRTTLGPRGMDKLIVDGRGKVTISNDGATILKLLDIVHPAAKTLVDIAKSQDAEVGDGTTSVV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 100 ILGGEILAQALPQLERNIHPVVIISAFKRALKDALEIIDEISTPIDINDDEAMYQLI----SSSIGTKFVSRWSKLMCSL 175
Cdd:cd03340 95 VLAGEFLKEAKPFIEDGVHPQIIIRGYRKALQLAIEKIKEIAVNIDKEDKEEQRELLekcaATALNSKLIASEKEFFAKM 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 176 ALKAVRTVtweagtgKREVDIKRYArIEKVPGGEIEDSRVLDGVMLNKDITH------PKmrrRIENPRIILLDCPLEYK 249
Cdd:cd03340 175 VVDAVLSL-------DDDLDLDMIG-IKKVPGGSLEDSQLVNGVAFKKTFSYagfeqqPK---KFKNPKILLLNVELELK 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 250 KGESQTQIEITKEEDWNRILQIEEEQVEAMCKHILELKPDLVITEKGVSDLAQHYFMKANVTALRRVRKTDNNRIARATG 329
Cdd:cd03340 244 AEKDNAEVRVEDPEEYQAIVDAEWKIIYDKLEKIVKSGANVVLSKLPIGDLATQYFADRDIFCAGRVPEEDLKRVAQATG 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 330 ATIVNRVEDLQESDVGTqCGLFEIEKIGDEYFTFLTKCNTPKACTVLLRGPSKDILNEVERNLQDAMGVARNVMFHPRLS 409
Cdd:cd03340 324 GSIQTTVSNITDDVLGT-CGLFEERQVGGERYNIFTGCPKAKTCTIILRGGAEQFIEEAERSLHDAIMIVRRAIKNDSVV 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 410 PGGGATEMAVSVRLGQLAKSIEGVQQWPYRAVAEALEVIPRTLVQNAGASPVRVLTDLRAKHAEGKSSW-GINGDTGGLA 488
Cdd:cd03340 403 AGGGAIEMELSKYLRDYSRTIAGKQQLVINAFAKALEIIPRQLCDNAGFDATDILNKLRQKHAQGGGKWyGVDINNEGIA 482
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 389623377 489 DMKEYGVWEPEAIKVQSMKTAIEAACLLLRVDDICSAKKA 528
Cdd:cd03340 483 DNFEAFVWEPSLVKINALTAATEAACLILSVDETIKNPKS 522
|
|
| chap_CCT_epsi |
TIGR02343 |
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ... |
4-524 |
8.64e-127 |
|
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: 381.07 E-value: 8.64e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 4 PVVVMNTQSGGERQTGRKAQLSNIAAAKIVADIIRSCLGPKAMLKMLLDPMGGIVLTNDGHAILREIEVSHPAAKSMIEL 83
Cdd:TIGR02343 10 PFIIIKDQDNKKRLKGLEAKKSNIAAAKSVASILRTSLGPKGMDKMLISPDGDITVTNDGATILSQMDVDNQIAKLMVEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 84 SRTQDEEVGDGTTSVIILGGEILAQALPQLERNIHPVVIISAFKRALKDALEIIDEISTPIDINDD--EAMYQLISSSIG 161
Cdd:TIGR02343 90 SKSQDDEIGDGTTGVVVLAGALLEQAEELLDKGIHPIKIADGFEEAARIAVEHLEEISDEISADNNnrEPLIQAAKTSLG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 162 TKFVSRWSKLMCSLALKAVRTVtweAGTGKREVDIKRYARIEKVpGGEIEDSRVLDGVMLNKDITHPKMRRRIENPRIIL 241
Cdd:TIGR02343 170 SKIVSKCHRRFAEIAVDAVLNV---ADMERRDVDFDLIKVEGKV-GGSLEDTKLIKGIIIDKDFSHPQMPKEVEDAKIAI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 242 LDCPLEYKKGESQTQIEITKEEDWNRILQIEEEQVEAMCKHILELKPDLVITEKGVSDLAQHYFMKANVTALRRVRKTDN 321
Cdd:TIGR02343 246 LTCPFEPPKPKTKHKLDISSVEEYKKLQKYEQQKFKEMIDDIKKSGANLVICQWGFDDEANHLLLQNDLPAVRWVGGQEL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 322 NRIARATGATIVNRVEDLQESDVGTqCGLFEIEKIG--DEYFTFLTKCNTPKACTVLLRGPSKDILNEVERNLQDAMGVA 399
Cdd:TIGR02343 326 ELIAIATGGRIVPRFQELSKDKLGK-AGLVREISFGttKDRMLVIEQCKNSKAVTIFIRGGNKMIIEEAKRSIHDALCVV 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 400 RNVMFHPRLSPGGGATEMAVSVRLGQLAKSIEGVQQWPYRAVAEALEVIPRTLVQNAGASPVRVLTDLRAKHAEGK-SSW 478
Cdd:TIGR02343 405 RNLIKDSRIVYGGGAAEISCSLAVSQEADKYPGVEQYAIRAFADALETIPMALAENSGLDPIGTLSTLKSLQLKEKnPNL 484
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 389623377 479 GINGDTGGLADMKEYGVWEPEAIKVQSMKTAIEAACLLLRVDDICS 524
Cdd:TIGR02343 485 GVDCLGYGTNDMKEQFVFETLIGKKQQILLATQLVRMILKIDDVIS 530
|
|
| TCP1_delta |
cd03338 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ... |
24-522 |
2.97e-124 |
|
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: 373.93 E-value: 2.97e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 24 LSNIAAAKIVADIIRSCLGPKAMLKMLLDPMGGIVLTNDGHAILREIEVSHPAAKSMIELSRTQDEEVGDGTTSVIILGG 103
Cdd:cd03338 11 LSNIQAAKAVADAIRTSLGPRGMDKMIQTGKGEVIITNDGATILKQMSVLHPAAKMLVELSKAQDIEAGDGTTSVVVLAG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 104 EILAQALPQLERNIHPVVIISAFKRALKDALEIIDEISTPIDINDDEAMYQLISSSIGTKFVSRWSKLMCSLALKAVRTV 183
Cdd:cd03338 91 ALLSACESLLKKGIHPTVISESFQIAAKKAVEILDSMSIPVDLNDRESLIKSATTSLNSKVVSQYSSLLAPIAVDAVLKV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 184 TWEAgtGKREVDIKRyARIEKVPGGEIEDSRVLDGVMLNKDITH-PKMRRRIENPRIILLDCPLEYKKGESQTQIEITKE 262
Cdd:cd03338 171 IDPA--TATNVDLKD-IRIVKKLGGTIEDTELVDGLVFTQKASKkAGGPTRIEKAKIGLIQFCLSPPKTDMDNNIVVNDY 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 263 EDWNRILQIEEEQVEAMCKHILELKPDLVITEK-----GVSDLAQHYFMKANVTALRRVRKTDNNRIARATGATIVNRVE 337
Cdd:cd03338 248 AQMDRILREERKYILNMCKKIKKSGCNVLLIQKsilrdAVSDLALHFLAKLKIMVVKDIEREEIEFICKTIGCKPVASID 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 338 DLQESDVGTqCGLFEIEKIGDEYFTFLTKCNTP-KACTVLLRGPSKDILNEVERNLQDAMGVARNVMFHPRLSPGGGATE 416
Cdd:cd03338 328 HFTEDKLGS-ADLVEEVSLGDGKIVKITGVKNPgKTVTILVRGSNKLVLDEAERSLHDALCVIRCLVKKRALIPGGGAPE 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 417 MAVSVRLGQLAKSIEGVQQWPYRAVAEALEVIPRTLVQNAGASPVRVLTDLRAKHAEGKSSWGINGDTGGLADMKEYGVW 496
Cdd:cd03338 407 IEIALQLSEWARTLTGVEQYCVRAFADALEVIPYTLAENAGLNPISIVTELRNRHAQGEKNAGINVRKGAITNILEENVV 486
|
490 500
....*....|....*....|....*.
gi 389623377 497 EPEAIKVQSMKTAIEAACLLLRVDDI 522
Cdd:cd03338 487 QPLLVSTSAITLATETVRMILKIDDI 512
|
|
| chap_CCT_eta |
TIGR02345 |
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ... |
21-528 |
1.52e-123 |
|
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: 372.55 E-value: 1.52e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 21 KAQL-SNIAAAKIVADIIRSCLGPKAMLKMLLDPMGGIVLTNDGHAILREIEVSHPAAKSMIELSRTQDEEVGDGTTSVI 99
Cdd:TIGR02345 17 KGQLiSNINACVAIAEALKTTLGPRGMDKLIVGSNGKATISNDGATILKLLDIVHPAAKTLVDIAKSQDAEVGDGTTSVT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 100 ILGGEILAQALPQLERNIHPVVIISAFKRALKDALEIIDEISTPIDINDD---EAMYQLISSSIGTKFVSRWSKLMCSLA 176
Cdd:TIGR02345 97 ILAGELLKEAKPFIEEGVHPQLIIRCYREALSLAVEKIKEIAVTIDEEKGeqrELLEKCAATALSSKLISHNKEFFSKMI 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 177 LKAVRTVtweagtgKREVDIKRYARIEKVPGGEIEDSRVLDGVMLNKDIT---HPKMRRRIENPRIILLDCPLEYKKGES 253
Cdd:TIGR02345 177 VDAVLSL-------DRDDLDLKLIGIKKVQGGALEDSQLVNGVAFKKTFSyagFEQQPKKFANPKILLLNVELELKAEKD 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 254 QTQIEITKEEDWNRILQIEEEQVEAMCKHILELKPDLVITEKGVSDLAQHYFMKANVTALRRVRKTDNNRIARATGATIV 333
Cdd:TIGR02345 250 NAEIRVEDVEDYQAIVDAEWAIIFRKLEKIVESGANVVLSKLPIGDLATQYFADRDIFCAGRVSAEDLKRVIKACGGSIQ 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 334 NRVEDLQESDVGTqCGLFEIEKIGDEYFTFLTKCNTPKACTVLLRGPSKDILNEVERNLQDAMGVARNVMFHPRLSPGGG 413
Cdd:TIGR02345 330 STTSDLEADVLGT-CALFEERQIGSERYNYFTGCPHAKTCTIILRGGAEQFIEEAERSLHDAIMIVRRALKNKKIVAGGG 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 414 ATEMAVSVRLGQLAKSIEGVQQWPYRAVAEALEVIPRTLVQNAGASPVRVLTDLRAKHAEGKSSWGINGDTGGLADMKEY 493
Cdd:TIGR02345 409 AIEMELSKCLRDYSKTIDGKQQLIINAFAKALEIIPRQLCENAGFDSIEILNKLRSRHAKGGKWYGVDINTEDIGDNFEA 488
|
490 500 510
....*....|....*....|....*....|....*
gi 389623377 494 GVWEPEAIKVQSMKTAIEAACLLLRVDDICSAKKA 528
Cdd:TIGR02345 489 FVWEPALVKINALKAAFEAACTILSVDETITNPKS 523
|
|
| TCP1_alpha |
cd03335 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ... |
14-521 |
3.20e-115 |
|
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: 351.20 E-value: 3.20e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 14 GERQTGRKAQLSNIAAAKIVADIIRSCLGPKAMLKMLLDPMGGIVLTNDGHAILREIEVSHPAAKSMIELSRTQDEEVGD 93
Cdd:cd03335 1 GERTSGQDVRTQNVTAAMAIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDKEVGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 94 GTTSVIILGGEILAQALPQLERNIHPVVIISAFKRALKDALEIIDE-ISTPIDINDDEAMYQLISSSIGTKFVSRWSKLM 172
Cdd:cd03335 81 GTTSVVIIAAELLKRANELVKQKIHPTTIISGYRLACKEAVKYIKEhLSISVDNLGKESLINVAKTSMSSKIIGADSDFF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 173 CSLALKAVRTVTWEAGTGKREVDIKRyARIEKVPGGEIEDSRVLDGVMLNKDITHPKMRRRIENPRIILLDCPLEYKKGE 252
Cdd:cd03335 161 ANMVVDAILAVKTTNEKGKTKYPIKA-VNILKAHGKSAKESYLVNGYALNCTRASQGMPTRVKNAKIACLDFNLQKTKMK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 253 SQTQIEITKEEDWNRILQIEEEQVEAMCKHILELKPDLVITEKGVSDLAQHYFMKANVTALRRVRKTDNNRIARATGATI 332
Cdd:cd03335 240 LGVQVVVTDPEKLEKIRQRESDITKERIKKILAAGANVVLTTGGIDDMCLKYFVEAGAMAVRRVKKEDLRRIAKATGATL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 333 VNRVEDLQ-----ESDVGTQCGLFEIEKIGDEYFTFLTKCNTPKACTVLLRGPSKDILNEVERNLQDAMGVARNVMFHPR 407
Cdd:cd03335 320 VSTLANLEgeetfDPSYLGEAEEVVQERIGDDELILIKGTKKRSSASIILRGANDFMLDEMERSLHDALCVVKRTLESNS 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 408 LSPGGGATEMAVSVRLGQLAKSIEGVQQWPYRAVAEALEVIPRTLVQNAGASPVRVLTDLRAKHAEGKSS--------WG 479
Cdd:cd03335 400 VVPGGGAVETALSIYLENFATTLGSREQLAIAEFAEALLVIPKTLAVNAAKDATELVAKLRAYHAAAQVKpdkkhlkwYG 479
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 389623377 480 INGDTGGLADMKEYGVWEPEAIKVQSMKTAIEAACLLLRVDD 521
Cdd:cd03335 480 LDLINGKVRDNLEAGVLEPTVSKIKSLKFATEAAITILRIDD 521
|
|
| chap_CCT_alpha |
TIGR02340 |
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ... |
12-530 |
5.34e-114 |
|
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: 348.63 E-value: 5.34e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 12 SGGERQTGRKAQLSNIAAAKIVADIIRSCLGPKAMLKMLLDPMGGIVLTNDGHAILREIEVSHPAAKSMIELSRTQDEEV 91
Cdd:TIGR02340 3 LGGERTSGQDVRTQNVTAAMAIANIVKTSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDREV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 92 GDGTTSVIILGGEILAQALPQLERNIHPVVIISAFKRALKDALEIIDE-ISTPIDINDDEAMYQLISSSIGTKFVSRWSK 170
Cdd:TIGR02340 83 GDGTTSVVIIAAELLKRADELVKNKIHPTSVISGYRLACKEAVKYIKEnLSVSVDELGREALINVAKTSMSSKIIGLDSD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 171 LMCSLALKAVRTVTWEAGTGKREVDIKRyARIEKVPGGEIEDSRVLDGVMLNKDITHPKMRRRIENPRIILLDCPLEYKK 250
Cdd:TIGR02340 163 FFSNIVVDAVLAVKTTNENGETKYPIKA-INILKAHGKSARESMLVKGYALNCTVASQQMPKRIKNAKIACLDFNLQKAK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 251 GESQTQIEITKEEDWNRILQIEEEQVEAMCKHILELKPDLVITEKGVSDLAQHYFMKANVTALRRVRKTDNNRIARATGA 330
Cdd:TIGR02340 242 MALGVQIVVDDPEKLEQIRQREADITKERIKKILDAGANVVLTTGGIDDMCLKYFVEAGAMGVRRCKKEDLKRIAKATGA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 331 TIVNRVEDLQ-----ESDVGTQCGLFEIEKIGDEYFTFLTKCNTPKACTVLLRGPSKDILNEVERNLQDAMGVARNVMFH 405
Cdd:TIGR02340 322 TLVSTLADLEgeetfEASYLGFADEVVQERIADDECILIKGTKKRKSASIILRGANDFMLDEMERSLHDALCVVKRTLES 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 406 PRLSPGGGATEMAVSVRLGQLAKSIEGVQQWPYRAVAEALEVIPRTLVQNAGASPVRVLTDLRAKHAEGKSS-------- 477
Cdd:TIGR02340 402 NSVVPGGGAVEAALSIYLENFATTLGSREQLAIAEFARALLIIPKTLAVNAAKDSTELVAKLRAYHAAAQLKpekkhlkw 481
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 389623377 478 WGINGDTGGLADMKEYGVWEPEAIKVQSMKTAIEAACLLLRVDDICSAKKAQP 530
Cdd:TIGR02340 482 YGLDLVNGKIRDNKEAGVLEPTVSKVKSLKFATEAAITILRIDDLIKLNPEQS 534
|
|
| chap_CCT_delta |
TIGR02342 |
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ... |
25-522 |
5.92e-113 |
|
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: 345.23 E-value: 5.92e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 25 SNIAAAKIVADIIRSCLGPKAMLKMLLDPMGGIVLTNDGHAILREIEVSHPAAKSMIELSRTQDEEVGDGTTSVIILGGE 104
Cdd:TIGR02342 13 SNIVAAKAVADAIRTSLGPKGMDKMIQDGKGEVIITNDGATILKQMAVLHPAAKMLVELSKAQDIEAGDGTTSVVILAGA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 105 ILAQALPQLERNIHPVVIISAFKRALKDALEIIDEISTPIDINDDEAMYQLISSSIGTKFVSRWSKLMCSLALKAVRTVT 184
Cdd:TIGR02342 93 LLGACERLLNKGIHPTIISESFQSAADEAIKILDEMSIPVDLSDREQLLKSATTSLSSKVVSQYSSLLAPLAVDAVLKVI 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 185 weAGTGKREVDIKRYARIEKVpGGEIEDSRVLDGVMLNKDITHPK-MRRRIENPRIILLDCPLEYKKGESQTQIEITKEE 263
Cdd:TIGR02342 173 --DPENAKNVDLNDIKVVKKL-GGTIDDTELIEGLVFTQKASKSAgGPTRIEKAKIGLIQFQISPPKTDMENQIIVNDYA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 264 DWNRILQIEEEQVEAMCKHILELKPDLVITEK-----GVSDLAQHYFMKANVTALRRVRKTDNNRIARATGATIVNRVED 338
Cdd:TIGR02342 250 QMDRVLKEERAYILNIVKKIKKTGCNVLLIQKsilrdAVNDLALHFLAKMKIMVVKDIEREEIEFICKTIGCKPIASIDH 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 339 LQESDVGtQCGLFEIEKIGDEYFTFLTKCNTP-KACTVLLRGPSKDILNEVERNLQDAMGVARNVMFHPRLSPGGGATEM 417
Cdd:TIGR02342 330 FTADKLG-SAELVEEVDSDGGKIIKITGIQNAgKTVTVVVRGSNKLVIDEAERSLHDALCVIRCLVKKRGLIAGGGAPEI 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 418 AVSVRLGQLAKSIEGVQQWPYRAVAEALEVIPRTLVQNAGASPVRVLTDLRAKHAEGKSSWGINGDTGGLADMKEYGVWE 497
Cdd:TIGR02342 409 EIARRLSKYARTMKGVESYCVRAFADALEVIPYTLAENAGLNPIKVVTELRNRHANGEKTAGISVRKGGITNMLEEHVLQ 488
|
490 500
....*....|....*....|....*
gi 389623377 498 PEAIKVQSMKTAIEAACLLLRVDDI 522
Cdd:TIGR02342 489 PLLVTTSAITLASETVRSILKIDDI 513
|
|
| TCP1_theta |
cd03341 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ... |
22-526 |
5.42e-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: 315.31 E-value: 5.42e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 22 AQLSNIAAAKIVADIIRSCLGPKAMLKMLLDPMGGIVLTNDGHAILREIEVSHPAAKSMIELSRTQDEEVGDGTTSVIIL 101
Cdd:cd03341 9 AVLRNIEACKELSQITRTSYGPNGMNKMVINHLEKLFVTSDAATILRELEVQHPAAKLLVMASQMQEEEIGDGTNLVVVL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 102 GGEILAQALPQLERNIHPVVIISAFKRALKDALEIIDE--ISTPIDINDDEAMYQLISSSIGTKFVSRwSKLMCSLALKA 179
Cdd:cd03341 89 AGELLEKAEELLRMGLHPSEIIEGYEKALKKALEILEElvVYKIEDLRNKEEVSKALKTAIASKQYGN-EDFLSPLVAEA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 180 VRTVTWEAgTGKREVDikrYARIEKVPGGEIEDSRVLDGVMLNKD----IThpkmrrRIENPRIILLDCPLEykkgesqt 255
Cdd:cd03341 168 CISVLPEN-IGNFNVD---NIRVVKILGGSLEDSKVVRGMVFKREpegsVK------RVKKAKVAVFSCPFD-------- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 256 qieitkeedwnrilqieeeqveamckhileLKPDLVITEKGVSDLAQHYFMKANVTALRRVRKTDNNRIARATGATIVNR 335
Cdd:cd03341 230 ------------------------------IGVNVIVAGGSVGDLALHYCNKYGIMVIKINSKFELRRLCRTVGATPLPR 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 336 VEDLQESDVGTqCGLFEIEKIGDEYFTFLTKCNTP-KACTVLLRGPSKDILNEVERNLQDAMGVARNVMFHPRLSPGGGA 414
Cdd:cd03341 280 LGAPTPEEIGY-CDSVYVEEIGDTKVVVFRQNKEDsKIATIVLRGATQNILDDVERAIDDGVNVFKSLTKDGRFVPGAGA 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 415 TEMAVSVRLGQLAKSIEGVQQWPYRAVAEALEVIPRTLVQNAGASPVRVLTDLRAKHAEGKSSWGINGDTG--GLADMKE 492
Cdd:cd03341 359 TEIELAKKLKEYGEKTPGLEQYAIKKFAEAFEVVPRTLAENAGLDATEVLSELYAAHQKGNKSAGVDIESGdeGTKDAKE 438
|
490 500 510
....*....|....*....|....*....|....
gi 389623377 493 YGVWEPEAIKVQSMKTAIEAACLLLRVDDICSAK 526
Cdd:cd03341 439 AGIFDHLATKKWAIKLATEAAVTVLRVDQIIMAK 472
|
|
| GroEL |
COG0459 |
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ... |
19-531 |
2.08e-100 |
|
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227 Cd Length: 497 Bit Score: 312.01 E-value: 2.08e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 19 GRKAQLSNIAAAKIVADIIRSCLGPKAMLKMLLDPMGGIVLTNDGHAILREIEVSHP----AAKSMIELSRTQDEEVGDG 94
Cdd:COG0459 8 GEDARRANIRGVKALADAVKVTLGPKGRNVMLVKSFGDPTITNDGVTIAKEIELEDPfenmGAQLVKEVASKTNDEAGDG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 95 TTSVIILGGEILAQALPQLERNIHPVVIISAFKRALKDALEIIDEISTPIDinDDEAMYQLISSSIGTKfvsrwsKLMCS 174
Cdd:COG0459 88 TTTATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPVD--DKEELAQVATISANGD------EEIGE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 175 LALKAVRTVTweagtgkREVDIKryarIEKvpGGEIE-DSRVLDGVMLNKDITHP-------KMRRRIENPRIILLDCPL 246
Cdd:COG0459 160 LIAEAMEKVG-------KDGVIT----VEE--GKGLEtELEVVEGMQFDKGYLSPyfvtdpeKMPAELENAYILLTDKKI 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 247 EykkgesqtqieitkeedwnrILQIEEEQVEAmckhILELKPDLVITEKGVSDLAQHYFMKANVTALRRV---------- 316
Cdd:COG0459 227 S--------------------SIQDLLPLLEK----VAQSGKPLLIIAEDIDGEALATLVVNGIRGVLRVvavkapgfgd 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 317 -RKTDNNRIARATGATIVNR-----VEDLQESDVGTqCGLFEIEKigdEYFTFLTKCNTPKACTVLLRGPSKDILNEVER 390
Cdd:COG0459 283 rRKAMLEDIAILTGGRVISEdlglkLEDVTLDDLGR-AKRVEVDK---DNTTIVEGAGNPKAIVILVGAATEVEVKERKR 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 391 NLQDAMGVARNVMfHPRLSPGGGATEMAVSVRLGQLAKSIEGVQQWPYRAVAEALEVIPRTLVQNAGASPVRVLTDLRAK 470
Cdd:COG0459 359 RVEDALHATRAAV-EEGIVPGGGAALLRAARALRELAAKLEGDEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKVRAA 437
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 389623377 471 haeGKSSWGINGDTGGLADMKEYGVWEPEAIKVQSMKTAIEAACLLLRVDDICSAKKAQPG 531
Cdd:COG0459 438 ---KDKGFGFDAATGEYVDMLEAGVIDPAKVKRSALQNAASVAGLILTTEAVIADKPEKEE 495
|
|
| chap_CCT_theta |
TIGR02346 |
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ... |
22-528 |
4.17e-99 |
|
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT alpha chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.
Pssm-ID: 274087 [Multi-domain] Cd Length: 531 Bit Score: 309.72 E-value: 4.17e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 22 AQLSNIAAAKIVADIIRSCLGPKAMLKMLLDPMGGIVLTNDGHAILREIEVSHPAAKSMIELSRTQDEEVGDGTTSVIIL 101
Cdd:TIGR02346 19 AVIKNIEACKELSQITRTSLGPNGMNKMVINHLEKLFVTNDAATILRELEVQHPAAKLLVMASEMQENEIGDGTNLVLVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 102 GGEILAQALPQLERNIHPVVIISAFKRALKDALEIIDEIS--TPIDINDDEAMYQLISSSIGTKFVSRwSKLMCSLALKA 179
Cdd:TIGR02346 99 AGELLNKAEELIRMGLHPSEIIKGYEMALKKAMEILEELVvwEVKDLRDKDELIKALKASISSKQYGN-EDFLAQLVAQA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 180 VRTVTWEAgTGKREVDikrYARIEKVPGGEIEDSRVLDGVMLNKD-ITHPKmrrRIENPRIILLDCPLEYKKGESQTQIE 258
Cdd:TIGR02346 178 CSTVLPKN-PQNFNVD---NIRVCKILGGSLSNSEVLKGMVFNREaEGSVK---SVKNAKVAVFSCPLDTATTETKGTVL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 259 ITKEEDWNRILQIEEEQVEAMCKHILELKPDLVITEKGVSDLAQHYFMKANVTALRRVRKTDNNRIARATGATIVNRVED 338
Cdd:TIGR02346 251 IHNAEELLNYSKGEENQIEAMIKAIADSGVNVIVTGGSVGDMALHYLNKYNIMVLKIPSKFELRRLCKTVGATPLPRLGA 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 339 LQESDVGtQCGLFEIEKIGDEYFTFLTKCNT-PKACTVLLRGPSKDILNEVERNLQDAMGVARNVMFHPRLSPGGGATEM 417
Cdd:TIGR02346 331 PTPEEIG-YVDSVYVSEIGGDKVTVFKQENGdSKISTIILRGSTDNLLDDIERAIDDGVNTVKALVKDGRLLPGAGATEI 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 418 AVSVRLGQLAKSIEGVQQWPYRAVAEALEVIPRTLVQNAGASPVRVLTDLRAKHAEGKSSWGIN--GDTGGLADMKEYGV 495
Cdd:TIGR02346 410 ELASRLTKYGEKLPGLDQYAIKKFAEAFEIIPRTLAENAGLNANEVIPKLYAAHKKGNKSKGIDieAESDGVKDASEAGI 489
|
490 500 510
....*....|....*....|....*....|...
gi 389623377 496 WEPEAIKVQSMKTAIEAACLLLRVDDICSAKKA 528
Cdd:TIGR02346 490 YDMLATKKWAIKLATEAAVTVLRVDQIIMAKPA 522
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
1-525 |
6.05e-96 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 301.56 E-value: 6.05e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 1 MQAPVVVMntQSGGERQTGRKAQLSNIAAAKIVADIIRSCLGPKAMLKmLLDPM------GGIVLTNDGHAILREIEVSH 74
Cdd:PTZ00212 4 ANVPPQVL--KQGAQEEKGETARLQSFVGAIAVADLVKTTLGPKGMDK-ILQPMsegprsGNVTVTNDGATILKSVWLDN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 75 PAAKSMIELSRTQDEEVGDGTTSVIILGGEILAQALPQLERNIHPVVIISAFKRALKDALEIIDEISTPIDINDD---EA 151
Cdd:PTZ00212 81 PAAKILVDISKTQDEEVGDGTTSVVVLAGELLREAEKLLDQKIHPQTIIEGWRMALDVARKALEEIAFDHGSDEEkfkED 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 152 MYQLISSSIGTKFVSRWSKLMCSLALKAVRTVtweagtgKREVDIKrYARIEKVPGGEIEDSRVLDGVMLNKDIThPKMR 231
Cdd:PTZ00212 161 LLNIARTTLSSKLLTVEKDHFAKLAVDAVLRL-------KGSGNLD-YIQIIKKPGGTLRDSYLEDGFILEKKIG-VGQP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 232 RRIENPRIILLDCPLEYKKgesqtqIEI----TKEEDWNRILQIEEEQVEAM---CKHILELKPDLVITEKGVSDLAQHY 304
Cdd:PTZ00212 232 KRLENCKILVANTPMDTDK------IKIygakVKVDSMEKVAEIEAAEKEKMknkVDKILAHGCNVFINRQLIYNYPEQL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 305 FMKANVTALRRVRKTDNNRIARATGATIVNRVEDLQESDVGTqCGLFEIEKIGDEYFTFLTKCNTPKACTVLLRGPSKDI 384
Cdd:PTZ00212 306 FAEAGIMAIEHADFDGMERLAAALGAEIVSTFDTPEKVKLGH-CDLIEEIMIGEDKLIRFSGCAKGEACTIVLRGASTHI 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 385 LNEVERNLQDAMGVARNVMFHPRLSPGGGATEMAVSVRLGQLAKSIEGVQQWPYRAVAEALEVIPRTLVQNAGASPVRVL 464
Cdd:PTZ00212 385 LDEAERSLHDALCVLSQTVKDTRVVLGGGCSEMLMANAVEELAKKVEGKKSLAIEAFAKALRQIPTIIADNGGYDSAELV 464
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 389623377 465 TDLRAKHAEGKSSWGINGDTGGLADMKEYGVWEPEAIKVQSMKTAIEAACLLLRVDDICSA 525
Cdd:PTZ00212 465 SKLRAEHYKGNKTAGIDMEKGTVGDMKELGITESYKVKLSQLCSATEAAEMILRVDDIIRC 525
|
|
| TCP1_beta |
cd03336 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ... |
12-526 |
3.87e-93 |
|
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: 293.85 E-value: 3.87e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 12 SGGERQTGRKAQLSNIAAAKIVADIIRSCLGPKAMLKMLL--DPMGGIVLTNDGHAILREIEVSHPAAKSMIELSRTQDE 89
Cdd:cd03336 4 DGAQEEKGETARLSSFVGAIAIGDLVKTTLGPKGMDKILQsvGRSGGVTVTNDGATILKSIGVDNPAAKVLVDISKVQDD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 90 EVGDGTTSVIILGGEILAQALPQLERNIHPVVIISAFKRALKDALEIIDEIStpIDINDDEAMYQ-----LISSSIGTKF 164
Cdd:cd03336 84 EVGDGTTSVTVLAAELLREAEKLVAQKIHPQTIIEGYRMATAAAREALLSSA--VDHSSDEEAFRedllnIARTTLSSKI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 165 VSRWSKLMCSLALKAVRTVtweAGTGKREvdikrYARIEKVPGGEIEDSRVLDGVMLNKDI--THPKmrrRIENPRIILL 242
Cdd:cd03336 162 LTQDKEHFAELAVDAVLRL---KGSGNLD-----AIQIIKKLGGSLKDSYLDEGFLLDKKIgvNQPK---RIENAKILIA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 243 DCPLEYKKgesqtqIEI----TKEEDWNRILQIEEEQVEAM---CKHILELKPDLVITEKGVSDLAQHYFMKANVTALRR 315
Cdd:cd03336 231 NTPMDTDK------IKIfgakVRVDSTAKVAEIEEAEKEKMknkVEKILKHGINCFINRQLIYNYPEQLFADAGIMAIEH 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 316 VRKTDNNRIARATGATIVNRVEDLQESDVGTqCGLFEIEKIGDEYFTFLTKCNTPKACTVLLRGPSKDILNEVERNLQDA 395
Cdd:cd03336 305 ADFDGVERLALVTGGEIASTFDHPELVKLGT-CKLIEEIMIGEDKLIRFSGVAAGEACTIVLRGASQQILDEAERSLHDA 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 396 MGVARNVMFHPRLSPGGGATEMAVSVRLGQLAKSIEGVQQWPYRAVAEALEVIPRTLVQNAGASPVRVLTDLRAKHAEGK 475
Cdd:cd03336 384 LCVLAQTVKDTRVVLGGGCSEMLMAKAVEELAKKTPGKKSLAIEAFAKALRQLPTIIADNAGYDSAELVAQLRAAHYNGN 463
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 389623377 476 SSWGINGDTGGLADMKEYGVWEPEAIKVQSMKTAIEAACLLLRVDDICSAK 526
Cdd:cd03336 464 TTAGLDMRKGTVGDMKELGITESFKVKRQVLLSASEAAEMILRVDDIIKCA 514
|
|
| chap_CCT_zeta |
TIGR02347 |
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ... |
26-528 |
1.21e-91 |
|
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: 290.48 E-value: 1.21e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 26 NIAAAKIVADIIRSCLGPKAMLKMLLDPMGGIVLTNDGHAILREIEVSHPAAKSMIELSRTQDEEVGDGTTSVIILGGEI 105
Cdd:TIGR02347 21 NINAARGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEMQIQHPTASMIARAATAQDDITGDGTTSTVLLIGEL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 106 LAQALPQLERNIHPVVIISAFKRALKDALEIIDEISTPI-DINDDEAMYQLISSSIGTK----FVSRWSKLMCSlALKAV 180
Cdd:TIGR02347 101 LKQAERYILEGVHPRIITEGFEIARKEALQFLDKFKVKKeDEVDREFLLNVARTSLRTKlpadLADQLTEIVVD-AVLAI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 181 RTVTWEAGTGKREV-DIKRYARIekvpggeieDSRVLDGVMLNKDITHPKMRRRIENPRIILLDCPLEYKKGESQTQIEI 259
Cdd:TIGR02347 180 KKDGEDIDLFMVEImEMKHKSAT---------DTTLIRGLVLDHGARHPDMPRRVKNAYILTCNVSLEYEKTEVNSGFFY 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 260 TKEEDWNRILQIEEEQVEAMCKHILELK-------PD---LVITEKGVSDLAQHYFMKANVTALRRVRKTDNNRIARATG 329
Cdd:TIGR02347 251 SSAEQREKLVKAERKFVDDRVKKIIELKkkvcgksPDkgfVVINQKGIDPPSLDLLAKEGIMALRRAKRRNMERLTLACG 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 330 ATIVNRVEDLQESDVGtQCGLFEIEKIGDEYFTFLTKCNTPKACTVLLRGPSKDILNEVERNLQDAMGVARNVMFHPRLS 409
Cdd:TIGR02347 331 GEALNSVEDLTPECLG-WAGLVYETTIGEEKYTFIEECKNPKSCTILIKGPNDHTIAQIKDAVRDGLRAVKNAIEDKCVV 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 410 PGGGATEMAVSVRLGQLAKSIEGVQQWPYRAVAEALEVIPRTLVQNAGASPVRVLTDLRAKHAEGKSSWGINGDTGGLAD 489
Cdd:TIGR02347 410 PGAGAFEIAAYRHLKEYKKSVKGKAKLGVEAFANALLVIPKTLAENSGFDAQDTLVKLEDEHDEGGEVVGVDLNTGEPID 489
|
490 500 510
....*....|....*....|....*....|....*....
gi 389623377 490 MKEYGVWEPEAIKVQSMKTAIEAACLLLRVDDICSAKKA 528
Cdd:TIGR02347 490 PEIKGIWDNYRVKKQLIQSATVIASQLLLVDEVMRAGRS 528
|
|
| TCP1_zeta |
cd03342 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
26-527 |
9.23e-90 |
|
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: 284.15 E-value: 9.23e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 26 NIAAAKIVADIIRSCLGPKAMLKMLLDPMGGIVLTNDGHAILREIEVSHPAAkSMIELSRT-QDEEVGDGTTSVIILGGE 104
Cdd:cd03342 17 NISAAKGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLSEMQIQHPTA-SMIARAATaQDDITGDGTTSNVLLIGE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 105 ILAQALPQLERNIHPVVIISAFKRALKDALEIIDEISTPIDINDD-EAMYQLISSSIGTKFVSRWSKLMCSLALKAVRTV 183
Cdd:cd03342 96 LLKQAERYIQEGVHPRIITEGFELAKNKALKFLESFKVPVEIDTDrELLLSVARTSLRTKLHADLADQLTEIVVDAVLAI 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 184 TWEAGtgkrEVDIkRYARIEKVPGGEIEDSRVLDGVMLNKDITHPKMRRRIENPRIILLDCPLEYKKGESQTqieitkee 263
Cdd:cd03342 176 YKPDE----PIDL-HMVEIMQMQHKSDSDTKLIRGLVLDHGARHPDMPKRVENAYILTCNVSLEYEKTEVNS-------- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 264 dwnrilqieeeqveamckhilELKPDLVITEKGVSDLAQHYFMKANVTALRRVRKTDNNRIARATGATIVNRVEDLQESD 343
Cdd:cd03342 243 ---------------------GFFYSVVINQKGIDPPSLDMLAKEGILALRRAKRRNMERLTLACGGVAMNSVDDLSPEC 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 344 VGtQCGLFEIEKIGDEYFTFLTKCNTPKACTVLLRGPSKDILNEVERNLQDAMGVARNVMFHPRLSPGGGATEMAVSVRL 423
Cdd:cd03342 302 LG-YAGLVYERTLGEEKYTFIEGVKNPKSCTILIKGPNDHTITQIKDAIRDGLRAVKNAIEDKCVVPGAGAFEVALYAHL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 424 GQLAKSIEGVQQWPYRAVAEALEVIPRTLVQNAGASPVRVLTDLRAKHAEGKSSWGINGDTGGLADMKEYGVWEPEAIKV 503
Cdd:cd03342 381 KEFKKSVKGKAKLGVQAFADALLVIPKTLAENSGLDVQETLVKLQDEYAEGGQVGGVDLDTGEPMDPESEGIWDNYSVKR 460
|
490 500
....*....|....*....|....
gi 389623377 504 QSMKTAIEAACLLLRVDDICSAKK 527
Cdd:cd03342 461 QILHSATVIASQLLLVDEIIRAGR 484
|
|
| chaperonin_like |
cd03333 |
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ... |
149-403 |
4.51e-78 |
|
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: 244.30 E-value: 4.51e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 149 DEAMYQLISSSIGTKfVSRWSKLMCSLALKAVRTVTweagtGKREVDIKRYARIEKVPGGEIEDSRVLDGVMLNKDITHP 228
Cdd:cd03333 1 RELLLQVATTSLNSK-LSSWDDFLGKLVVDAVLKVG-----PDNRMDDLGVIKVEKIPGGSLEDSELVVGVVFDKGYASP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 229 KMRRRIENPRIILLDCPLEYkkgesqtqieitkeedwnrilqieeeqveamckhilelkpdLVITEKGVSDLAQHYFMKA 308
Cdd:cd03333 75 YMPKRLENAKILLLDCPLEY-----------------------------------------VVIAEKGIDDLALHYLAKA 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 309 NVTALRRVRKTDNNRIARATGATIVNRVEDLQESDVGTqCGLFEIEKIGDEYFTFLTKCNTPKACTVLLRGPSKDILNEV 388
Cdd:cd03333 114 GIMAVRRVKKEDLERIARATGATIVSSLEDLTPEDLGT-AELVEETKIGEEKLTFIEGCKGGKAATILLRGATEVELDEV 192
|
250
....*....|....*
gi 389623377 389 ERNLQDAMGVARNVM 403
Cdd:cd03333 193 KRSLHDALCAVRAAV 207
|
|
| chap_CCT_beta |
TIGR02341 |
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ... |
13-525 |
1.99e-75 |
|
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: 247.85 E-value: 1.99e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 13 GGERQTGRKAQLSNIAAAKIVADIIRSCLGPKAMLKMLL--DPMGGIVLTNDGHAILREIEVSHPAAKSMIELSRTQDEE 90
Cdd:TIGR02341 6 GADEERAENARLSSFVGAIAIGDLVKSTLGPKGMDKILQssSSDASIMVTNDGATILKSIGVDNPAAKVLVDMSKVQDDE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 91 VGDGTTSVIILGGEILAQALPQLERNIHPVVIISAFKRALKDALEIIDEIStpIDINDDEAMYQ-----LISSSIGTKFV 165
Cdd:TIGR02341 86 VGDGTTSVTVLAAELLREAEKLINQKIHPQTIIAGYREATKAARDALLKSA--VDNGSDEVKFRqdlmnIARTTLSSKIL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 166 SRWSKLMCSLALKAVRTVTweaGTGKREvdikrYARIEKVPGGEIEDSRVLDGVMLNKDI--THPKmrrRIENPRIILLD 243
Cdd:TIGR02341 164 SQHKDHFAQLAVDAVLRLK---GSGNLE-----AIQIIKKLGGSLADSYLDEGFLLDKKIgvNQPK---RIENAKILIAN 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 244 CPLEYKKGES-QTQIEITKEEDWNRILQIEEEQVEAMCKHILELKPDLVITEKGVSDLAQHYFMKANVTALRRVRKTDNN 322
Cdd:TIGR02341 233 TGMDTDKVKIfGSRVRVDSTAKVAELEHAEKEKMKEKVEKILKHGINCFINRQLIYNYPEQLFADAGVMAIEHADFEGVE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 323 RIARATGATIVNRVEDLQESDVGtQCGLFEIEKIGDEYFTFLTKCNTPKACTVLLRGPSKDILNEVERNLQDAMGVARNV 402
Cdd:TIGR02341 313 RLALVTGGEIVSTFDHPELVKLG-SCDLIEEIMIGEDKLLKFSGVKLGEACTIVLRGATQQILDEAERSLHDALCVLSQT 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 403 MFHPRLSPGGGATEMAVSVRLGQLAKSIEGVQQWPYRAVAEALEVIPRTLVQNAGASPVRVLTDLRAKHAEGKSSWGING 482
Cdd:TIGR02341 392 VKESRTVLGGGCSEMLMSKAVTQEAQRTPGKEALAVEAFARALRQLPTIIADNAGFDSAELVAQLRAAHYNGNTTMGLDM 471
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 389623377 483 DTGGLADMKEYGVWEPEAIKVQSMKTAIEAACLLLRVDDICSA 525
Cdd:TIGR02341 472 NEGTIADMRQLGITESYKVKRAVVSSAAEAAEVILRVDNIIKA 514
|
|
| Fab1_TCP |
cd03334 |
TCP-1 like domain of the eukaryotic phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinase Fab1. ... |
154-393 |
3.79e-51 |
|
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: 175.87 E-value: 3.79e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 154 QLISSSiGTKFVSRWSKLMCSLALKAVRTVTWEAGTGKrEVDIKRYARIEKVPGGEIEDSRVLDGVMLNKDITHPKMRRR 233
Cdd:cd03334 6 QLLKDE-GISNDESWLDILLPLVWKAASNVKPDVRAGD-DMDIRQYVKIKKIPGGSPSDSEVVDGVVFTKNVAHKRMPSK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 234 IENPRIILLDCPLEYKKGESQ-TQIEItkeedwnrILQIEEEQVEAMCKHILELKPDLVITEKGVSDLAQHYFMKANVTA 312
Cdd:cd03334 84 IKNPRILLLQGPLEYQRVENKlLSLDP--------VILQEKEYLKNLVSRIVALRPDVILVEKSVSRIAQDLLLEAGITL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 313 LRRVRKTDNNRIARATGATIVNRVEDL-QESDVGTqCGLFEIEKIGDEY-----FTFLTKCNTPKACTVLLRGPSKDILN 386
Cdd:cd03334 156 VLNVKPSVLERISRCTGADIISSMDDLlTSPKLGT-CESFRVRTYVEEHgrsktLMFFEGCPKELGCTILLRGGDLEELK 234
|
....*..
gi 389623377 387 EVERNLQ 393
Cdd:cd03334 235 KVKRVVE 241
|
|
| GroEL |
cd03344 |
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ... |
16-149 |
3.77e-11 |
|
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings, each composed of 7-9 subunits. The symmetry of type I is seven-fold and they are found in eubacteria (GroEL) and in organelles of eubacterial descent (hsp60 and RBP). With the aid of cochaperonin GroES, GroEL encapsulates non-native substrate proteins inside the cavity of the GroEL-ES complex and promotes folding by using energy derived from ATP hydrolysis.
Pssm-ID: 239460 Cd Length: 520 Bit Score: 65.56 E-value: 3.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 16 RQTGRKAQLsniAAAKIVADIIRSCLGPKAMLKMLLDPMGGIVLTNDGHAILREIEVSHP----AAKSMIELSRTQDEEV 91
Cdd:cd03344 6 GEEARKALL---RGVNKLADAVKVTLGPKGRNVVIEKSFGSPKITKDGVTVAKEIELEDPfenmGAQLVKEVASKTNDVA 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 389623377 92 GDGTTSVIILGGEILAQALPQLERNIHPVVIISAFKRALKDALEIIDEISTPIDINDD 149
Cdd:cd03344 83 GDGTTTATVLARAIIKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKPVKTKEE 140
|
|
| groEL |
PRK12850 |
chaperonin GroEL; Reviewed |
32-541 |
5.94e-10 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237231 Cd Length: 544 Bit Score: 61.66 E-value: 5.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 32 IVADIIRSCLGPKAMLKMLLDPMGGIVLTNDGHAILREIEVSHPAAKSMIEL-----SRTQDEeVGDGTTSVIILGGEIL 106
Cdd:PRK12850 22 ILANAVKVTLGPKGRNVVLEKSFGAPRITKDGVTVAKEIELEDKFENMGAQMvkevaSKTNDL-AGDGTTTATVLAQAIV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 107 AQALPQLERNIHPVVIISAFKRALKDALEIIDEISTPIDINDDEAMYQLISSSIGTKFVSRWSKLMCSLALKAVRTVTwE 186
Cdd:PRK12850 101 REGAKLVAAGMNPMDLKRGIDLAVAAVVDELKKIAKKVTSSKEIAQVATISANGDESIGEMIAEAMDKVGKEGVITVE-E 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 187 AGTGKREVDIkryariekVPGGEIeDSRVLDGVMlnkdITHP-KMRRRIENPRIILldcpleYKKGESQTQ-----IEIT 260
Cdd:PRK12850 180 AKTLGTELDV--------VEGMQF-DRGYLSPYF----VTNPeKMRAELEDPYILL------HEKKISNLQdllpiLEAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 261 KEEDwnRILQIEEEQVEAmckhilELKPDLVITE--KGVSDLAqhyfMKANVTALRRVRKTDNnrIARATGATIVNRved 338
Cdd:PRK12850 241 VQSG--RPLLIIAEDVEG------EALATLVVNKlrGGLKSVA----VKAPGFGDRRKAMLED--IAVLTGGQVISE--- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 339 lqesDVGTQCGLFEIEKIGDEYFTFLTKCNT----PKACTVLLRGPSKDILNEVERNLQD-------------AMGVArn 401
Cdd:PRK12850 304 ----DLGIKLENVTLDMLGRAKRVLITKENTtiidGAGDKKNIEARVKQIRAQIEETTSDydreklqerlaklAGGVA-- 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 402 VMfhpRLspgGGATEMAVS--------------------------VRLGQLAKSIEGV------QQWPYRAVAEALEVIP 449
Cdd:PRK12850 378 VI---RV---GGATEVEVKekkdrvddalhatraaveegivpgggVALLRARSALRGLkganadETAGIDIVRRALEEPL 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 450 RTLVQNAGASPVRVLtdlrAKHAEGKSSWGINGDTGGLADMKEYGVWEPEAIKVQSMKTAIEAACLLLRVDDICSAKKAQ 529
Cdd:PRK12850 452 RQIATNAGFEGSVVV----GKVAELPGNFGFNAQTGEYGDMVEAGIIDPAKVTRTALQDAASIAALLITTEAMVAEAPKK 527
|
570
....*....|..
gi 389623377 530 PGVGTGMTGGDD 541
Cdd:PRK12850 528 AAAAAAGPGPGM 539
|
|
| PTZ00114 |
PTZ00114 |
Heat shock protein 60; Provisional |
33-514 |
1.79e-09 |
|
Heat shock protein 60; Provisional
Pssm-ID: 185455 Cd Length: 555 Bit Score: 60.31 E-value: 1.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 33 VADIIRSCLGPKAMLKMLLDPMGGIVLTNDGHAILREIEVSHPA----AKSMIELSRTQDEEVGDGTTSVIILGGEILAQ 108
Cdd:PTZ00114 34 LADAVAVTLGPKGRNVIIEQEYGSPKITKDGVTVAKAIEFSDRFenvgAQLIRQVASKTNDKAGDGTTTATILARAIFRE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 109 ALPQLERNIHPVVIISAFKRALKDALEIIDEISTPI----DI--------NDDEAMYQLISSsigtkfvsrwsklmcslA 176
Cdd:PTZ00114 114 GCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQSRPVktkeDIlnvatisaNGDVEIGSLIAD-----------------A 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 177 LKAVrtvtweagtGKREVdikryarIEKVPGGEIEDS-RVLDGVMLNKDITHP-------KMRRRIENPRIILLDCPLEy 248
Cdd:PTZ00114 177 MDKV---------GKDGT-------ITVEDGKTLEDElEVVEGMSFDRGYISPyfvtnekTQKVELENPLILVTDKKIS- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 249 kkgESQTqieitkeedwnrILQIEEeqveamckHILELKPDLVITEKGVSD--LAQHYFMKAN-------VTA--LRRVR 317
Cdd:PTZ00114 240 ---SIQS------------ILPILE--------HAVKNKRPLLIIAEDVEGeaLQTLIINKLRgglkvcaVKApgFGDNR 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 318 KTDNNRIARATGATIVNRVEDLQESDVGTQCGLFEIEKIgdeyftfltkcNTPKACTVLLRGP----------------- 380
Cdd:PTZ00114 297 KDILQDIAVLTGATVVSEDNVGLKLDDFDPSMLGSAKKV-----------TVTKDETVILTGGgdkaeikervellrsqi 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 381 -------SKDILN-------------------EVERN-----LQDAMGVARNVMfHPRLSPGGGATEMAVSVRLGQLA-- 427
Cdd:PTZ00114 366 erttseyDKEKLKerlaklsggvavikvggasEVEVNekkdrIEDALNATRAAV-EEGIVPGGGVALLRASKLLDKLEed 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 428 KSIEGVQQWPYRAVAEALEVIPRTLVQNAGASPVRVLTDLRakhAEGKSSWGINGDTGGLADMKEYGVWEPeaIKVqsMK 507
Cdd:PTZ00114 445 NELTPDQRTGVKIVRNALRLPTKQIAENAGVEGAVVVEKIL---EKKDPSFGYDAQTGEYVNMFEAGIIDP--TKV--VR 517
|
....*..
gi 389623377 508 TAIEAAC 514
Cdd:PTZ00114 518 SALVDAA 524
|
|
| groEL |
PRK12851 |
chaperonin GroEL; Reviewed |
27-517 |
1.66e-08 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 171770 Cd Length: 541 Bit Score: 57.06 E-value: 1.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 27 IAAAKIVADIIRSCLGPKAMLKMLLDPMGGIVLTNDGHAILREIEVSHP----AAKSMIELSRTQDEEVGDGTTSVIILG 102
Cdd:PRK12851 17 LRGVNILADAVKVTLGPKGRNVVIDKSFGAPTITNDGVTIAKEIELEDKfenmGAQMVREVASKTNDVAGDGTTTATVLA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 103 GEILAQALPQLERNIHPVVIISAFKRALKDALEIIDEISTPIDINDDEAMYQLIS----SSIGtKFVsrwSKLMCSLALK 178
Cdd:PRK12851 97 QAIVREGAKAVAAGANPMDLKRGIDRAVAAVVEELKANARPVTTNAEIAQVATISangdAEIG-RLV---AEAMEKVGNE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 179 AVRTVTwEAGTGKREVDikryariekvpggeiedsrVLDGVMLNKDITHP-------KMRRRIENPRIILLDcpleYKKG 251
Cdd:PRK12851 173 GVITVE-ESKTAETELE-------------------VVEGMQFDRGYLSPyfvtdadKMEAELEDPYILIHE----KKIS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 252 ESQTQIEITKE-EDWNRILQIEEEQVE-------------------------------AMCKHILELKPDLVITEKGVSD 299
Cdd:PRK12851 229 NLQDLLPVLEAvVQSGKPLLIIAEDVEgealatlvvnklrgglkvaavkapgfgdrrkAMLEDIAILTGGTVISEDLGIK 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 300 LAqhyfmKANVTALRRVRKTdnnrIARATGATIVNRVEDLQESDVGTQCGLFEIEKIGDEY-----FTFLTKCNTPKAcT 374
Cdd:PRK12851 309 LE-----NVTLEQLGRAKKV----VVEKENTTIIDGAGSKTEIEGRVAQIRAQIEETTSDYdreklQERLAKLAGGVA-V 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 375 VLLRGPSKDILNEVERNLQDAMGVARNVMFHPRLSPGGGATEMAVSVRLGQLAKsiEGVQQWPYRAVAEALEVIPRTLVQ 454
Cdd:PRK12851 379 IRVGASTEVEVKEKKDRVDDALHATRAAVEEGIVPGGGVALLRAVKALDKLETA--NGDQRTGVEIVRRALEAPVRQIAE 456
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 389623377 455 NAGASPVRVLtdlrAKHAEGKSSWGINGDTGGLADMKEYGVWEPEAIKVQSMKTAIEAACLLL 517
Cdd:PRK12851 457 NAGAEGSVVV----GKLREKPGGYGFNAATNEYGDLYAQGVIDPVKVVRTALQNAASVAGLLL 515
|
|
| groEL |
PRK12849 |
chaperonin GroEL; Reviewed |
16-158 |
2.19e-07 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237230 Cd Length: 542 Bit Score: 53.66 E-value: 2.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 16 RQTGRKAQLSNIAAakiVADIIRSCLGPKAMLKMLLDPMGGIVLTNDGHAILREIEVSHP----AAKSMIELSRTQDEEV 91
Cdd:PRK12849 8 DEEARRALERGVNK---LADAVKVTLGPKGRNVVIDKSFGAPTITKDGVSIAKEIELEDPfenlGAQLVKEVASKTNDVA 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 389623377 92 GDGTTSVIILGGEILAQALPQLERNIHPVVIISAFKRALKDALEIIDEISTPIDINDDEAMYQLISS 158
Cdd:PRK12849 85 GDGTTTATVLAQALVQEGLKNVAAGANPMDLKRGIDKAVEAVVEELKALARPVSGSEEIAQVATISA 151
|
|
| PRK14104 |
PRK14104 |
chaperonin GroEL; Provisional |
12-539 |
2.25e-07 |
|
chaperonin GroEL; Provisional
Pssm-ID: 172594 Cd Length: 546 Bit Score: 53.50 E-value: 2.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 12 SGGERQTGRKAQLSNIAAAKIVADIIRSCLGPKAMLKMLLDPMGGIVLTNDGHAILREIEV----SHPAAKSMIELSRTQ 87
Cdd:PRK14104 2 SAKEVKFGVDARDRMLRGVDILANAVKVTLGPKGRNVVLDKSFGAPRITKDGVTVAKEIELedkfENMGAQMVREVASKS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 88 DEEVGDGTTSVIILGGEILAQALPQLERNIHPVVIISAFKRALKDALEIIDEISTPIDINDDEAMYQLISSSIGTKFVSR 167
Cdd:PRK14104 82 ADAAGDGTTTATVLAQAIVREGAKSVAAGMNPMDLKRGIDLAVEAVVADLVKNSKKVTSNDEIAQVGTISANGDAEIGKF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 168 WSKLMCSLALKAVRTVTwEAGTGKREVDIkryariekVPGGEIEDSRVLDGVMLNKDithpKMRRRIENPRII------- 240
Cdd:PRK14104 162 LADAMKKVGNEGVITVE-EAKSLETELDV--------VEGMQFDRGYISPYFVTNAD----KMRVEMDDAYILinekkls 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 241 -------LLDCPLEYKK----------GESQTQIEITKEEDWNRILQIEE----EQVEAMCKHILELKPDLVITEkgvsD 299
Cdd:PRK14104 229 slnellpLLEAVVQTGKplvivaedveGEALATLVVNRLRGGLKVAAVKApgfgDRRKAMLQDIAILTGGQAISE----D 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 300 LAQHyFMKANVTALRRVRKT----DNNRIARATG--ATIVNRVEDLQeSDVGTQCGLFEIEKIGDEyftfLTKCNTPKAc 373
Cdd:PRK14104 305 LGIK-LENVTLQMLGRAKKVmidkENTTIVNGAGkkADIEARVAQIK-AQIEETTSDYDREKLQER----LAKLAGGVA- 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 374 TVLLRGPSKDILNEVERNLQDAMGVARNVMfHPRLSPGGGATEMAVSVRLGQLaKSIEGVQQWPYRAVAEALEVIPRTLV 453
Cdd:PRK14104 378 VIRVGGATEVEVKERKDRVDDAMHATRAAV-EEGIVPGGGVALLRASEQLKGI-KTKNDDQKTGVEIVRKALSAPARQIA 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 454 QNAGASPVRVLTDLRAKHaegKSSWGINGDTGGLADMKEYGVWEPEAIKVQSMKTAIEAACLLLRVDDICSAKKAQPGVG 533
Cdd:PRK14104 456 INAGEDGSVIVGKILEKE---QYSYGFDSQTGEYGNLVSKGIIDPTKVVRTAIQNAASVAALLITTEAMVAELPKKGGAG 532
|
....*.
gi 389623377 534 TGMTGG 539
Cdd:PRK14104 533 PAMPPG 538
|
|
| GroEL |
TIGR02348 |
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ... |
20-161 |
3.73e-07 |
|
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: 52.68 E-value: 3.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 20 RKAQLSNIaaaKIVADIIRSCLGPKAMLKMLLDPMGGIVLTNDGHAILREIEVSHP----AAKSMIEL-SRTQDeEVGDG 94
Cdd:TIGR02348 11 RKALLRGV---DKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDKfenmGAQLVKEVaSKTND-VAGDG 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 389623377 95 TTSVIILGGEILAQALPQLERNIHPVVIISAFKRALKDALEIIDEISTPidINDDEAMYQLISSSIG 161
Cdd:TIGR02348 87 TTTATVLAQAIVKEGLKNVAAGANPIELKRGIEKAVEAVVEELKKLSKP--VKGKKEIAQVATISAN 151
|
|
| groEL |
CHL00093 |
chaperonin GroEL |
31-517 |
2.09e-06 |
|
chaperonin GroEL
Pssm-ID: 177025 Cd Length: 529 Bit Score: 50.49 E-value: 2.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 31 KIVADIIRSCLGPKAMLKMLLDPMGGIVLTNDGHAILREIEVSHPAAKSMIEL-----SRTQDeEVGDGTTSVIILGGEI 105
Cdd:CHL00093 20 DILAEAVSVTLGPKGRNVVLEKKYGSPQIVNDGVTIAKEIELEDHIENTGVALirqaaSKTND-VAGDGTTTATVLAYAI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 106 LAQALPQLERNIHPVVIISAFKRALKDALEIIDEISTPIDinDDEAMYQLISSSIGTKFVsrwSKLMCSLALKAV---RT 182
Cdd:CHL00093 99 VKQGMKNVAAGANPISLKRGIEKATQYVVSQIAEYARPVE--DIQAITQVASISAGNDEE---VGSMIADAIEKVgreGV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 183 VTWEAGTG-KREVDIKRYARIEKvpggeiedsrvldGVMLNKDITHP-KMRRRIENPRIILLDCPLEYKKGESQTQIE-I 259
Cdd:CHL00093 174 ISLEEGKStVTELEITEGMRFEK-------------GFISPYFVTDTeRMEVVQENPYILLTDKKITLVQQDLLPILEqV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 260 TKEedwNRILQIEEEQVEAmckhilELKPDLVITE-KGVsdlaqhyfmkANVTALR-----RVRKTDNNRIARATGATIV 333
Cdd:CHL00093 241 TKT---KRPLLIIAEDVEK------EALATLVLNKlRGI----------VNVVAVRapgfgDRRKAMLEDIAILTGGQVI 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 334 NRvedlqesDVGTQCGLFEIEKIGDEYFTFLTKCNTpkacTVLLRGPSKDILNEVER---------------NLQD---- 394
Cdd:CHL00093 302 TE-------DAGLSLETIQLDLLGQARRIIVTKDST----TIIADGNEEQVKARCEQlrkqieiadssyekeKLQErlak 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 395 -AMGVA--------RNVMFHPRLS-----------------PGGGATEMAVSVRLGQLAKS-IEGVQQWPYRAVAEALEV 447
Cdd:CHL00093 371 lSGGVAvikvgaatETEMKDKKLRledainatkaaveegivPGGGATLVHLSENLKTWAKNnLKEDELIGALIVARAILA 450
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 448 IPRTLVQNAGASPVRVLTDLRAKHAEgkssWGINGDTGGLADMKEYGVWEPEAIKVQSMKTAIEAACLLL 517
Cdd:CHL00093 451 PLKRIAENAGKNGSVIIEKVQEQDFE----IGYNAANNKFVNMYEAGIIDPAKVTRSALQNAASIASMIL 516
|
|
| groEL |
PRK12852 |
chaperonin GroEL; Reviewed |
32-538 |
2.35e-06 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237232 Cd Length: 545 Bit Score: 50.23 E-value: 2.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 32 IVADIIRSCLGPKAMLKMLLDPMGGIVLTNDGHAILREIEVS----HPAAKSMIELSRTQDEEVGDGTTSVIILGGEILA 107
Cdd:PRK12852 22 ILANAVKVTLGPKGRNVVIEKSFGAPRITKDGVTVAKEIELEdkfeNMGAQMVREVASKTNDLAGDGTTTATVLAQAIVR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 108 QALPQLERNIHPVVIISAFKRALKDALEIIDEISTPIDINDDEAMYQLISSSIGTKFVSRWSKLMCSLALKAVRTVTwEA 187
Cdd:PRK12852 102 EGAKAVAAGMNPMDLKRGIDIAVAAVVKDIEKRAKPVASSAEIAQVGTISANGDAAIGKMIAQAMQKVGNEGVITVE-EN 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 188 GTGKREVDIkryariekvpggeIEDSRVLDGVMLNKDITHP-KMRRRIENPRIILLDCPL-------------------- 246
Cdd:PRK12852 181 KSLETEVDI-------------VEGMKFDRGYLSPYFVTNAeKMTVELDDAYILLHEKKLsglqamlpvleavvqsgkpl 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 247 ----EYKKGESQTQIEITKEEDWNRILQIEEEQVEAMCKHILElkpDLVITEKG--VSDLAQHYFMKANVTALRRVRKT- 319
Cdd:PRK12852 248 liiaEDVEGEALATLVVNRLRGGLKVAAVKAPGFGDRRKAMLE---DIAILTGGqlISEDLGIKLENVTLKMLGRAKKVv 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 320 ---DNNRIARATG--ATIVNRVEDLQeSDVGTQCGLFEIEKIGDEyftfLTKCNTPKActVLLRGPSKDI-LNEVERNLQ 393
Cdd:PRK12852 325 idkENTTIVNGAGkkADIEARVGQIK-AQIEETTSDYDREKLQER----LAKLAGGVA--VIRVGGATEVeVKEKKDRVE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 394 DAMGVARNVMfHPRLSPGGGATEMAVSVRLGQLAKSIEGVQQwPYRAVAEALEVIPRTLVQNAGASPVRVLTDLRAKHAE 473
Cdd:PRK12852 398 DALNATRAAV-QEGIVPGGGVALLRAKKAVGRINNDNADVQA-GINIVLKALEAPIRQIAENAGVEGSIVVGKILENKSE 475
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 474 gksSWGINGDTGGLADMKEYGVWEPEAIKVQSMKTAIEAACLLLRVDDICS---AKKAQP--GVGTGMTG 538
Cdd:PRK12852 476 ---TFGFDAQTEEYVDMVAKGIIDPAKVVRTALQDAASVAGLLVTTEAMVAelpKKDAAPamPAGGGMGG 542
|
|
| PLN03167 |
PLN03167 |
Chaperonin-60 beta subunit; Provisional |
33-150 |
1.98e-04 |
|
Chaperonin-60 beta subunit; Provisional
Pssm-ID: 215611 [Multi-domain] Cd Length: 600 Bit Score: 44.14 E-value: 1.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 33 VADIIRSCLGPKAMLKMLLDPMGGIVLTNDGHAILREIEVSHP----AAKSMIELSRTQDEEVGDGTTSVIILGGEILAQ 108
Cdd:PLN03167 78 LADLVGVTLGPKGRNVVLESKYGSPKIVNDGVTVAKEVELEDPveniGAKLVRQAAAKTNDLAGDGTTTSVVLAQGLIAE 157
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 389623377 109 ALPQLERNIHPVVIISAFKRALKDALEIIDEISTpiDINDDE 150
Cdd:PLN03167 158 GVKVVAAGANPVQITRGIEKTAKALVKELKKMSK--EVEDSE 197
|
|
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
32-158 |
2.84e-03 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 40.49 E-value: 2.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 32 IVADIIRSCLGPKAMLKMLLDPMGGIVLTNDGHAILREIEVSHP----AAKSMIEL-SRTQDeEVGDGTTSVIILGGEIL 106
Cdd:PRK00013 21 KLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDPfenmGAQLVKEVaSKTND-VAGDGTTTATVLAQAIV 99
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 389623377 107 AQALpqleRNI----HPVVIISAFKRALKDALEIIDEISTPidINDDEAMYQL--ISS 158
Cdd:PRK00013 100 REGL----KNVaagaNPMDLKRGIDKAVEAAVEELKKISKP--VEDKEEIAQVatISA 151
|
|
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
410-539 |
4.15e-03 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 39.72 E-value: 4.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389623377 410 PGGGATEMAVSVRLGQLaKSIEGVQQWPYRAVAEALEVIPRTLVQNAGASPVRVLTDLRAKHAEGkssWGINGDTGGLAD 489
Cdd:PRK00013 412 PGGGVALLRAAPALEAL-KGLNGDEATGINIVLRALEAPLRQIAENAGLEGSVVVEKVKNGKGKG---YGYNAATGEYVD 487
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 389623377 490 MKEYGVWEPeaIKVqsMKTAIEAAC----LLLR----VDDICSAKKAQPGVGTGMTGG 539
Cdd:PRK00013 488 MIEAGIIDP--TKV--TRSALQNAAsvagLLLTteavVADKPEKKAAAPPMGGGGMGG 541
|
|
| |
