|
Name |
Accession |
Description |
Interval |
E-value |
| chap_CCT_theta |
TIGR02346 |
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ... |
9-559 |
0e+00 |
|
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: 876.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 9 PNAGLFKQGYNSYSNADGQIIKSIAAIRELHQMCLTSMGPCGRNKIIVNHLGKIIITNDAATMLRELDIVHPAVKVLVMA 88
Cdd:TIGR02346 1 GIASLLKEGYRHFSGLEEAVIKNIEACKELSQITRTSLGPNGMNKMVINHLEKLFVTNDAATILRELEVQHPAAKLLVMA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 89 TEQQKIDMGDGTNLVMILAGELLNVSEKLISMGLSAVEIIQGYNMARKFTLKELDEMVVGEITDKNDKNELLKMIKPVIS 168
Cdd:TIGR02346 81 SEMQENEIGDGTNLVLVLAGELLNKAEELIRMGLHPSEIIKGYEMALKKAMEILEELVVWEVKDLRDKDELIKALKASIS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 169 SKKYGSEDILSELVSEAVSHVLPVAQQAgeipyFNVDSIRVVKIMGGSLSNSTVIKGMVFNREPEGHVKSlseDKKHKVA 248
Cdd:TIGR02346 161 SKQYGNEDFLAQLVAQACSTVLPKNPQN-----FNVDNIRVCKILGGSLSNSEVLKGMVFNREAEGSVKS---VKNAKVA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 249 VFTCPLDIANTETKGTVLLHNAQEMLDFSKGEEKQIDAMMKEIADMGVECIVAGAGVGELALHYLNRYGILVLKVPSKFE 328
Cdd:TIGR02346 233 VFSCPLDTATTETKGTVLIHNAEELLNYSKGEENQIEAMIKAIADSGVNVIVTGGSVGDMALHYLNKYNIMVLKIPSKFE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 329 LRRLCRVCGATPLPRLGAPTPEELGLVETVKTMEIGGDRVTVFKQEQGEiSRTSTIILRGATQNNLDDIERAIDDGVAAV 408
Cdd:TIGR02346 313 LRRLCKTVGATPLPRLGAPTPEEIGYVDSVYVSEIGGDKVTVFKQENGD-SKISTIILRGSTDNLLDDIERAIDDGVNTV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 409 KGLMKPsgGKLLPGAGATEIELISRITKYGERTPGLLQLAIKQFAVAFEVVPRTLAETAGLDVNEVLPNLYAAHnvtepg 488
Cdd:TIGR02346 392 KALVKD--GRLLPGAGATEIELASRLTKYGEKLPGLDQYAIKKFAEAFEIIPRTLAENAGLNANEVIPKLYAAH------ 463
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6322452 489 avKTDHLYKGVDIDGESDeGVKDIREENIYDMLATKKFAINVATEAATTVLSIDQIIMAKKAGGPRAPQGP 559
Cdd:TIGR02346 464 --KKGNKSKGIDIEAESD-GVKDASEAGIYDMLATKKWAIKLATEAAVTVLRVDQIIMAKPAGGPKPPQGK 531
|
|
| TCP1_theta |
cd03341 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ... |
19-548 |
0e+00 |
|
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: 716.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 19 NSYSNADGQIIKSIAAIRELHQMCLTSMGPCGRNKIIVNHLGKIIITNDAATMLRELDIVHPAVKVLVMATEQQKIDMGD 98
Cdd:cd03341 1 RHYSGLEEAVLRNIEACKELSQITRTSYGPNGMNKMVINHLEKLFVTSDAATILRELEVQHPAAKLLVMASQMQEEEIGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 99 GTNLVMILAGELLNVSEKLISMGLSAVEIIQGYNMARKFTLKELDEMVVGEITDKNDKNELLKMIKPVISSKKYGSEDIL 178
Cdd:cd03341 81 GTNLVVVLAGELLEKAEELLRMGLHPSEIIEGYEKALKKALEILEELVVYKIEDLRNKEEVSKALKTAIASKQYGNEDFL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 179 SELVSEAVSHVLPvaqqaGEIPYFNVDSIRVVKIMGGSLSNSTVIKGMVFNREPEGHVKSLsedKKHKVAVFTCPLDIan 258
Cdd:cd03341 161 SPLVAEACISVLP-----ENIGNFNVDNIRVVKILGGSLEDSKVVRGMVFKREPEGSVKRV---KKAKVAVFSCPFDI-- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 259 tetkgtvllhnaqemldfskgeekqidammkeiadmGVECIVAGAGVGELALHYLNRYGILVLKVPSKFELRRLCRVCGA 338
Cdd:cd03341 231 ------------------------------------GVNVIVAGGSVGDLALHYCNKYGIMVIKINSKFELRRLCRTVGA 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 339 TPLPRLGAPTPEELGLVETVKTMEIGGDRVTVFKQEqGEISRTSTIILRGATQNNLDDIERAIDDGVAAVKGLMKPsgGK 418
Cdd:cd03341 275 TPLPRLGAPTPEEIGYCDSVYVEEIGDTKVVVFRQN-KEDSKIATIVLRGATQNILDDVERAIDDGVNVFKSLTKD--GR 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 419 LLPGAGATEIELISRITKYGERTPGLLQLAIKQFAVAFEVVPRTLAETAGLDVNEVLPNLYAAHNVTepgavktdHLYKG 498
Cdd:cd03341 352 FVPGAGATEIELAKKLKEYGEKTPGLEQYAIKKFAEAFEVVPRTLAENAGLDATEVLSELYAAHQKG--------NKSAG 423
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 6322452 499 VDIDGEsDEGVKDIREENIYDMLATKKFAINVATEAATTVLSIDQIIMAK 548
Cdd:cd03341 424 VDIESG-DEGTKDAKEAGIFDHLATKKWAIKLATEAAVTVLRVDQIIMAK 472
|
|
| Cpn60_TCP1 |
pfam00118 |
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ... |
44-548 |
8.89e-164 |
|
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: 475.15 E-value: 8.89e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 44 TSMGPCGRNKIIVNHLGKIIITNDAATMLRELDIVHPAVKVLVMATEQQKIDMGDGTNLVMILAGELLNVSEKLISMGLS 123
Cdd:pfam00118 7 TSLGPKGMDKMLVNSGGDVTVTNDGATILKELEIQHPAAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEEAEKLLAAGVH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 124 AVEIIQGYNMARKFTLKELDEMVVGEITDkNDKNELLKMIKPVISSKKYGSE-DILSELVSEAVSHVLPVAQQageipyF 202
Cdd:pfam00118 87 PTTIIEGYEKALEKALEILDSIISIPVED-VDREDLLKVARTSLSSKIISREsDFLAKLVVDAVLAIPKNDGS------F 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 203 NVDSIRVVKIMGGSLSNSTVIKGMVFNREPEgHVKSLSEDKKHKVAVFTCPLDIANTETKGTVLLHNAQEMLDFSKGEEK 282
Cdd:pfam00118 160 DLGNIGVVKILGGSLEDSELVDGVVLDKGPL-HPDMPKRLENAKVLLLNCSLEYEKTETKATVVLSDAEQLERFLKAEEE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 283 QIDAMMKEIADMGVECIVAGAGVGELALHYLNRYGILVLKVPSKFELRRLCRVCGATPLPRLGAPTPEELGLVETVKTME 362
Cdd:pfam00118 239 QILEIVEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMALRRVKKRDLERLAKATGARAVSSLDDLTPDDLGTAGKVEEEK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 363 IGGDRVTVFkqEQGEISRTSTIILRGATQNNLDDIERAIDDGVAAVKGLMKpsGGKLLPGAGATEIELISRITKYGERTP 442
Cdd:pfam00118 319 IGDEKYTFI--EGCKSPKAATILLRGATDHVLDEIERSIHDALCVVKNAIE--DPRVVPGGGAVEMELARALREYAKSVS 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 443 GLLQLAIKQFAVAFEVVPRTLAETAGLDVNEVLPNLYAAHNVTEPGAvktdhlykGVDIDgesDEGVKDIREENIYDMLA 522
Cdd:pfam00118 395 GKEQLAIEAFAEALEVIPKTLAENAGLDPIEVLAELRAAHASGEKHA--------GIDVE---TGEIIDMKEAGVVDPLK 463
|
490 500
....*....|....*....|....*.
gi 6322452 523 TKKFAINVATEAATTVLSIDQIIMAK 548
Cdd:pfam00118 464 VKRQALKSATEAASTILRIDDIIKAK 489
|
|
| chaperonin_type_I_II |
cd00309 |
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ... |
22-546 |
7.52e-152 |
|
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: 443.79 E-value: 7.52e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 22 SNADGQIIKSIAAIRELHQMCLTSMGPCGRNKIIVNHLGKIIITNDAATMLRELDIVHPAVKVLVMATEQQKIDMGDGTN 101
Cdd:cd00309 4 EFGEEARLSNINAAKALADAVKTTLGPKGMDKMLVDSLGDPTITNDGATILKEIEVEHPAAKLLVEVAKSQDDEVGDGTT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 102 LVMILAGELLNVSEKLISMGLSAVEIIQGYNMARKFTLKELDEMVVgeITDKNDKNELLKMIKPVISSKK-YGSEDILSE 180
Cdd:cd00309 84 TVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAV--PIDVEDREELLKVATTSLNSKLvSGGDDFLGE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 181 LVSEAVSHVLPvaqqagEIPYFNVDSIRVVKIMGGSLSNSTVIKGMVFNREPEgHVKSLSEDKKHKVAVFTCPLDIante 260
Cdd:cd00309 162 LVVDAVLKVGK------ENGDVDLGVIRVEKKKGGSLEDSELVVGMVFDKGYL-SPYMPKRLENAKILLLDCKLEY---- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 261 tkgtvllhnaqemldfskgeekqidammkeiadmgveCIVAGAGVGELALHYLNRYGILVLKVPSKFELRRLCRVCGATP 340
Cdd:cd00309 231 -------------------------------------VVIAEKGIDDEALHYLAKLGIMAVRRVRKEDLERIAKATGATI 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 341 LPRLGAPTPEELGLVETVKTMEIGGDRVTVFkqEQGEISRTSTIILRGATQNNLDDIERAIDDGVAAVKGLMKpsGGKLL 420
Cdd:cd00309 274 VSRLEDLTPEDLGTAGLVEETKIGDEKYTFI--EGCKGGKVATILLRGATEVELDEAERSLHDALCAVRAAVE--DGGIV 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 421 PGAGATEIELISRITKYGERTPGLLQLAIKQFAVAFEVVPRTLAETAGLDVNEVLPNLYAAHNvtepgavkTDHLYKGVD 500
Cdd:cd00309 350 PGGGAAEIELSKALEELAKTLPGKEQLGIEAFADALEVIPRTLAENAGLDPIEVVTKLRAKHA--------EGGGNAGGD 421
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 6322452 501 IDgesDEGVKDIREENIYDMLATKKFAINVATEAATTVLSIDQIIM 546
Cdd:cd00309 422 VE---TGEIVDMKEAGIIDPLKVKRQALKSATEAASLILTIDDIIV 464
|
|
| cpn60 |
cd03343 |
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ... |
13-548 |
8.10e-108 |
|
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: 332.69 E-value: 8.10e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 13 LFKQGYNSYSNADGQIIkSIAAIRELHQMCLTSMGPCGRNKIIVNHLGKIIITNDAATMLRELDIVHPAVKVLVMATEQQ 92
Cdd:cd03343 3 ILKEGTQRTSGRDAQRM-NIAAAKAVAEAVRTTLGPKGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAKTQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 93 KIDMGDGTNLVMILAGELLNVSEKLISMGLSAVEIIQGYNMARKFTLKELDEMVVGeiTDKNDKNELLKMIKPVISSKKY 172
Cdd:cd03343 82 DEEVGDGTTTAVVLAGELLEKAEDLLDQNIHPTVIIEGYRLAAEKALELLDEIAIK--VDPDDKDTLRKIAKTSLTGKGA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 173 GSE-DILSELVSEAvshVLPVAQQAGEIPYFNVDSIRVVKIMGGSLSNSTVIKGMVFNREP--EGHVKSLsedKKHKVAV 249
Cdd:cd03343 160 EAAkDKLADLVVDA---VLQVAEKRDGKYVVDLDNIKIEKKTGGSVDDTELIRGIVIDKEVvhPGMPKRV---ENAKIAL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 250 FTCPLDIANTETKGTVLLHNAQEMLDFSKGEEKQIDAMMKEIADMGVECIVAGAGVGELALHYLNRYGILVLKVPSKFEL 329
Cdd:cd03343 234 LDAPLEVKKTEIDAKIRITSPDQLQAFLEQEEAMLKEMVDKIADTGANVVFCQKGIDDLAQHYLAKAGILAVRRVKKSDM 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 330 RRLCRVCGATPLPRLGAPTPEELGLVETVKTMEIGGDRVTVFkqEQGEISRTSTIILRGATQNNLDDIERAIDDGVAAVK 409
Cdd:cd03343 314 EKLARATGAKIVTNIDDLTPEDLGEAELVEERKVGDDKMVFV--EGCKNPKAVTILLRGGTEHVVDELERALEDALRVVA 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 410 GLMKPsgGKLLPGAGATEIELISRITKYGERTPGLLQLAIKQFAVAFEVVPRTLAETAGLDVNEVLPNLYAAHNVTEPGA 489
Cdd:cd03343 392 DALED--GKVVAGGGAVEIELAKRLREYARSVGGREQLAVEAFADALEEIPRTLAENAGLDPIDTLVELRAAHEKGNKNA 469
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 6322452 490 vktdhlykGVDIDgesDEGVKDIREENIYDMLATKKFAINVATEAATTVLSIDQIIMAK 548
Cdd:cd03343 470 --------GLDVY---TGEVVDMLEKGVIEPLRVKKQAIKSATEAATMILRIDDVIAAK 517
|
|
| thermosome_alpha |
NF041082 |
thermosome subunit alpha; |
13-548 |
3.52e-105 |
|
thermosome subunit alpha;
Pssm-ID: 469009 Cd Length: 518 Bit Score: 326.07 E-value: 3.52e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 13 LFKQGYNSYSNADGQIIkSIAAIRELHQMCLTSMGPCGRNKIIVNHLGKIIITNDAATMLRELDIVHPAVKVLVMATEQQ 92
Cdd:NF041082 5 ILKEGTQRTSGRDAQRN-NIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDVVITNDGVTILKEMDIEHPAAKMIVEVAKTQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 93 KIDMGDGTNLVMILAGELLNVSEKLISMGLSAVEIIQGYNMARKFTLKELDEMVVGeiTDKNDKNELLKMIKPVISSKKY 172
Cdd:NF041082 84 DDEVGDGTTTAVVLAGELLKKAEELLDQDIHPTIIAEGYRLAAEKALEILDEIAIK--VDPDDKETLKKIAATAMTGKGA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 173 GS-EDILSELVSEAvshVLPVAQQAGEIpYFNVDSIRVVKIMGGSLSNSTVIKGMVFNREPEgHVKSLSEDKKHKVAVFT 251
Cdd:NF041082 162 EAaKDKLADLVVDA---VKAVAEKDGGY-NVDLDNIKVEKKVGGSIEDSELVEGVVIDKERV-HPGMPKRVENAKIALLD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 252 CPLDIANTETKGTVLLHNAQEMLDFSKGEEKQIDAMMKEIADMGVECIVAGAGVGELALHYLNRYGILVLKVPSKFELRR 331
Cdd:NF041082 237 APLEVKKTEIDAKISITDPDQLQAFLDQEEKMLKEMVDKIADSGANVVFCQKGIDDLAQHYLAKEGILAVRRVKKSDMEK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 332 LCRVCGATPLPRLGAPTPEELGLVETVKTMEIGGDRVTVFkqEQGEISRTSTIILRGATQNNLDDIERAIDDGVAAVKGL 411
Cdd:NF041082 317 LAKATGARIVTSIDDLSPEDLGYAGLVEERKVGGDKMIFV--EGCKNPKAVTILLRGGTEHVVDEVERALEDALRVVRVV 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 412 MKpsGGKLLPGAGATEIELISRITKYGERTPGLLQLAIKQFAVAFEVVPRTLAETAGLDVNEVLPNLYAAHnvtEPGAVK 491
Cdd:NF041082 395 LE--DGKVVAGGGAPEVELALRLREYAASVGGREQLAIEAFAEALEIIPRTLAENAGLDPIDALVELRSAH---EKGNKT 469
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 6322452 492 TdhlykGVDI-DGEsdegVKDIREENIYDMLATKKFAINVATEAATTVLSIDQIIMAK 548
Cdd:NF041082 470 A-----GLDVyTGK----VVDMLEIGVVEPLRVKTQAIKSATEAAVMILRIDDVIAAA 518
|
|
| thermosome_arch |
TIGR02339 |
thermosome, various subunits, archaeal; Thermosome is the name given to the archaeal rather ... |
13-547 |
6.81e-101 |
|
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: 315.09 E-value: 6.81e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 13 LFKQGYNSYSNADGQIIkSIAAIRELHQMCLTSMGPCGRNKIIVNHLGKIIITNDAATMLRELDIVHPAVKVLVMATEQQ 92
Cdd:TIGR02339 4 ILKEGTQRTSGRDAQRN-NIAAAKAVAEAVKSTLGPRGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAKTQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 93 KIDMGDGTNLVMILAGELLNVSEKLISMGLSAVEIIQGYNMARKFTLKELDEMVVGeiTDKNDKNELLKMIKPVISSKKY 172
Cdd:TIGR02339 83 DEEVGDGTTTAVVLAGELLEKAEDLLEQDIHPTVIIEGYRKAAEKALEIIDEIATK--ISPEDRDLLKKIAYTSLTSKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 173 GSE--DILSELVSEAVSHVlpVAQQAGEIPYFNVDSIRVVKIMGGSLSNSTVIKGMVFNREP--EGHVKSLsedKKHKVA 248
Cdd:TIGR02339 161 AEVakDKLADLVVEAVKQV--AELRGDGKYYVDLDNIKIVKKKGGSIEDTELVEGIVVDKEVvhPGMPKRV---ENAKIA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 249 VFTCPLDIANTETKGTVLLHNAQEMLDFSKGEEKQIDAMMKEIADMGVECIVAGAGVGELALHYLNRYGILVLKVPSKFE 328
Cdd:TIGR02339 236 LLDAPLEVEKTEIDAKIRITDPDQIKKFLDQEEAMLKEMVDKIASAGANVVICQKGIDDVAQHYLAKAGILAVRRVKKSD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 329 LRRLCRVCGATPLPRLGAPTPEELGLVETVKTMEIGGDRVTVFkqEQGEISRTSTIILRGATQNNLDDIERAIDDGVAAV 408
Cdd:TIGR02339 316 IEKLARATGARIVSSIDEITESDLGYAELVEERKVGEDKMVFV--EGCKNPKAVTILLRGGTEHVVDELERSIQDALHVV 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 409 KGLMKPsgGKLLPGAGATEIELISRITKYGERTPGLLQLAIKQFAVAFEVVPRTLAETAGLDVNEVLPNLYAAHNVTEPG 488
Cdd:TIGR02339 394 ANALED--GKIVAGGGAVEIELALRLRSYARSVGGREQLAIEAFADALEEIPRILAENAGLDPIDALVDLRAKHEKGNKN 471
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 489 AvktdhlykGVDI-DGEsdegVKDIREENIYDMLATKKFAINVATEAATTVLSIDQIIMA 547
Cdd:TIGR02339 472 A--------GINVfTGE----IEDMLELGVIEPLRVKEQAIKSATEAATMILRIDDVIAA 519
|
|
| thermosome_beta |
NF041083 |
thermosome subunit beta; |
15-548 |
7.64e-101 |
|
thermosome subunit beta;
Pssm-ID: 469010 Cd Length: 519 Bit Score: 314.97 E-value: 7.64e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 15 KQGYNSYSNADGQIIkSIAAIRELHQMCLTSMGPCGRNKIIVNHLGKIIITNDAATMLRELDIVHPAVKVLVMATEQQKI 94
Cdd:NF041083 7 KEGTQRTKGRDAQRN-NIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDIVITNDGATILKEMDVQHPAAKMLVEVAKTQDD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 95 DMGDGTNLVMILAGELLNVSEKLISMGLSAVEIIQGYNMARKFTLKELDEmvVGEITDKNDKNELLKMIKPVISSKKYGS 174
Cdd:NF041083 86 EVGDGTTTAVVLAGELLKKAEELLDQNIHPTIIANGYRLAAEKAIEILDE--IAEKVDPDDRETLKKIAETSLTSKGVEE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 175 E-DILSELVSEAvshVLPVAQQAGEIPYFNVDSIRVVKIMGGSLSNSTVIKGMVFNREPEgHVKSLSEDKKHKVAVFTCP 253
Cdd:NF041083 164 ArDYLAEIAVKA---VKQVAEKRDGKYYVDLDNIQIEKKHGGSIEDTQLIYGIVIDKEVV-HPGMPKRVENAKIALLDAP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 254 LDIANTETKGTVLLHNAQEMLDFSKGEEKQIDAMMKEIADMGVECIVAGAGVGELALHYLNRYGILVLKVPSKFELRRLC 333
Cdd:NF041083 240 LEVKKTEIDAEIRITDPDQLQKFLDQEEKMLKEMVDKIKATGANVVFCQKGIDDLAQHYLAKAGILAVRRVKKSDMEKLA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 334 RVCGATPLPRLGAPTPEELGLVETVKTMEIGGDRVTVFkqEQGEISRTSTIILRGATQNNLDDIERAIDDGVAAVKGLMK 413
Cdd:NF041083 320 KATGARIVTNIDDLTPEDLGYAELVEERKVGDDKMVFV--EGCKNPKAVTILIRGGTEHVVDEAERALEDALSVVADAVE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 414 psGGKLLPGAGATEIELISRITKYGERTPGLLQLAIKQFAVAFEVVPRTLAETAGLDVNEVLPNLYAAHnvtEPGAVktd 493
Cdd:NF041083 398 --DGKIVAGGGAPEVELAKRLREYAATVGGREQLAVEAFAEALEIIPRTLAENAGLDPIDILVKLRSAH---EKGKK--- 469
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 6322452 494 hlYKGVDI-DGEsdegVKDIREENIYDMLATKKFAINVATEAATTVLSIDQIIMAK 548
Cdd:NF041083 470 --WAGINVfTGE----VVDMWELGVIEPLRVKTQAIKSATEAATMILRIDDVIAAK 519
|
|
| TCP1_delta |
cd03338 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ... |
30-547 |
1.69e-77 |
|
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: 253.75 E-value: 1.69e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 30 KSIA-AIRelhqmclTSMGPCGRNKIIVNHLGKIIITNDAATMLRELDIVHPAVKVLVMATEQQKIDMGDGTNLVMILAG 108
Cdd:cd03338 18 KAVAdAIR-------TSLGPRGMDKMIQTGKGEVIITNDGATILKQMSVLHPAAKMLVELSKAQDIEAGDGTTSVVVLAG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 109 ELLNVSEKLISMGLSAVEIIQGYNMARKFTLKELDEMVVgEItDKNDKNELLKMIKPVISSK---KYGSedILSELvseA 185
Cdd:cd03338 91 ALLSACESLLKKGIHPTVISESFQIAAKKAVEILDSMSI-PV-DLNDRESLIKSATTSLNSKvvsQYSS--LLAPI---A 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 186 VSHVLPVAQQAGEIpyfNVD--SIRVVKIMGGSLSNSTVIKGMVFNREPEGHVKSLSEDKKHKVAVFTCPLDIANTETKG 263
Cdd:cd03338 164 VDAVLKVIDPATAT---NVDlkDIRIVKKLGGTIEDTELVDGLVFTQKASKKAGGPTRIEKAKIGLIQFCLSPPKTDMDN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 264 TVLLHNAQEMLDFSKGEEKQIDAMMKEIADMGVECIVAGA-----GVGELALHYLNRYGILVLKVPSKFELRRLCRVCGA 338
Cdd:cd03338 241 NIVVNDYAQMDRILREERKYILNMCKKIKKSGCNVLLIQKsilrdAVSDLALHFLAKLKIMVVKDIEREEIEFICKTIGC 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 339 TPLPRLGAPTPEELGLVETVKTMEIGGDRVTVFKQEQGEiSRTSTIILRGATQNNLDDIERAIDDGVAAVKGLMKPSGgk 418
Cdd:cd03338 321 KPVASIDHFTEDKLGSADLVEEVSLGDGKIVKITGVKNP-GKTVTILVRGSNKLVLDEAERSLHDALCVIRCLVKKRA-- 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 419 LLPGAGATEIELISRITKYGERTPGLLQLAIKQFAVAFEVVPRTLAETAGLDVNEVLPNLYAAHnvtepgavKTDHLYKG 498
Cdd:cd03338 398 LIPGGGAPEIEIALQLSEWARTLTGVEQYCVRAFADALEVIPYTLAENAGLNPISIVTELRNRH--------AQGEKNAG 469
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 6322452 499 VDIdgeSDEGVKDIREENIYDMLATKKFAINVATEAATTVLSIDQIIMA 547
Cdd:cd03338 470 INV---RKGAITNILEENVVQPLLVSTSAITLATETVRMILKIDDIVLA 515
|
|
| chap_CCT_eta |
TIGR02345 |
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ... |
8-550 |
7.10e-77 |
|
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: 252.37 E-value: 7.10e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 8 NPNAGLFKQGYNSySNADGQIIKSIAAIRELHQMCLTSMGPCGRNKIIVNHLGKIIITNDAATMLRELDIVHPAVKVLVM 87
Cdd:TIGR02345 1 RPTIVLLKEGTDT-SQGKGQLISNINACVAIAEALKTTLGPRGMDKLIVGSNGKATISNDGATILKLLDIVHPAAKTLVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 88 ATEQQKIDMGDGTNLVMILAGELLNVSEKLISMGLSAVEIIQGYNMARKFTLKELDEMVVGEITDKNDKNELL-KMIKPV 166
Cdd:TIGR02345 80 IAKSQDAEVGDGTTSVTILAGELLKEAKPFIEEGVHPQLIIRCYREALSLAVEKIKEIAVTIDEEKGEQRELLeKCAATA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 167 ISSKKYGSE-DILSELVSEAVSHVLPVAQQAgeipyfnvDSIRVVKIMGGSLSNSTVIKGMVFNR--EPEGHVKSLSEDK 243
Cdd:TIGR02345 160 LSSKLISHNkEFFSKMIVDAVLSLDRDDLDL--------KLIGIKKVQGGALEDSQLVNGVAFKKtfSYAGFEQQPKKFA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 244 KHKVAVFTCPLDIANTETKGTVLLHNAQEMLDFSKGEEKQIDAMMKEIADMGVECIVAGAGVGELALHYLNRYGILVLKV 323
Cdd:TIGR02345 232 NPKILLLNVELELKAEKDNAEIRVEDVEDYQAIVDAEWAIIFRKLEKIVESGANVVLSKLPIGDLATQYFADRDIFCAGR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 324 PSKFELRRLCRVCGATPLPRLGAPTPEELGLVETVKTMEIGGDRVTVFkqEQGEISRTSTIILRGATQNNLDDIERAIDD 403
Cdd:TIGR02345 312 VSAEDLKRVIKACGGSIQSTTSDLEADVLGTCALFEERQIGSERYNYF--TGCPHAKTCTIILRGGAEQFIEEAERSLHD 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 404 GVAAVKGLMKPSggKLLPGAGATEIELISRITKYGERTPGLLQLAIKQFAVAFEVVPRTLAETAGLDVNEVLPNLYAAHn 483
Cdd:TIGR02345 390 AIMIVRRALKNK--KIVAGGGAIEMELSKCLRDYSKTIDGKQQLIINAFAKALEIIPRQLCENAGFDSIEILNKLRSRH- 466
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6322452 484 vtepgavKTDHLYKGVDIDGesdEGVKDIREENIYDMLATKKFAINVATEAATTVLSIDQIIMAKKA 550
Cdd:TIGR02345 467 -------AKGGKWYGVDINT---EDIGDNFEAFVWEPALVKINALKAAFEAACTILSVDETITNPKS 523
|
|
| TCP1_eta |
cd03340 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ... |
13-550 |
1.11e-76 |
|
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: 251.82 E-value: 1.11e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 13 LFKQGYNSySNADGQIIKSIAAIRELHQMCLTSMGPCGRNKIIVNHLGKIIITNDAATMLRELDIVHPAVKVLVMATEQQ 92
Cdd:cd03340 4 LLKEGTDT-SQGKGQLISNINACQAIADAVRTTLGPRGMDKLIVDGRGKVTISNDGATILKLLDIVHPAAKTLVDIAKSQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 93 KIDMGDGTNLVMILAGELLNVSEKLISMGLSAVEIIQGYNMARKFTLKELDEMVVGeiTDKNDKNE----LLKMIKPVIS 168
Cdd:cd03340 83 DAEVGDGTTSVVVLAGEFLKEAKPFIEDGVHPQIIIRGYRKALQLAIEKIKEIAVN--IDKEDKEEqrelLEKCAATALN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 169 SKKYGSE-DILSELVSEAVSHVlpvaqqageIPYFNVDSIRVVKIMGGSLSNSTVIKGMVFNR--EPEGHVKSLSEDKKH 245
Cdd:cd03340 161 SKLIASEkEFFAKMVVDAVLSL---------DDDLDLDMIGIKKVPGGSLEDSQLVNGVAFKKtfSYAGFEQQPKKFKNP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 246 KVAVFTCPLDIANTETKGTVLLHNAQEMLDFSKGEEKQIDAMMKEIADMGVECIVAGAGVGELALHYLNRYGILVLKVPS 325
Cdd:cd03340 232 KILLLNVELELKAEKDNAEVRVEDPEEYQAIVDAEWKIIYDKLEKIVKSGANVVLSKLPIGDLATQYFADRDIFCAGRVP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 326 KFELRRLCRVCGATPLPRLGAPTPEELGLVETVKTMEIGGDRVTVFkqEQGEISRTSTIILRGATQNNLDDIERAIDDGV 405
Cdd:cd03340 312 EEDLKRVAQATGGSIQTTVSNITDDVLGTCGLFEERQVGGERYNIF--TGCPKAKTCTIILRGGAEQFIEEAERSLHDAI 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 406 AAVKGLMKPSggKLLPGAGATEIELISRITKYGERTPGLLQLAIKQFAVAFEVVPRTLAETAGLDVNEVLPNLYAAHNvt 485
Cdd:cd03340 390 MIVRRAIKND--SVVAGGGAIEMELSKYLRDYSRTIAGKQQLVINAFAKALEIIPRQLCDNAGFDATDILNKLRQKHA-- 465
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6322452 486 epgavKTDHLYKGVDIDGesdEGVKDIREENIYDMLATKKFAINVATEAATTVLSIDQIIMAKKA 550
Cdd:cd03340 466 -----QGGGKWYGVDINN---EGIADNFEAFVWEPSLVKINALTAATEAACLILSVDETIKNPKS 522
|
|
| chap_CCT_delta |
TIGR02342 |
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ... |
30-548 |
1.44e-73 |
|
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: 243.54 E-value: 1.44e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 30 KSIA-AIRelhqmclTSMGPCGRNKIIVNHLGKIIITNDAATMLRELDIVHPAVKVLVMATEQQKIDMGDGTNLVMILAG 108
Cdd:TIGR02342 19 KAVAdAIR-------TSLGPKGMDKMIQDGKGEVIITNDGATILKQMAVLHPAAKMLVELSKAQDIEAGDGTTSVVILAG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 109 ELLNVSEKLISMGLSAVEIIQGYNMARKFTLKELDEMVVGeiTDKNDKNELLKMIKPVISSKKYGS-EDILSELvseAVS 187
Cdd:TIGR02342 92 ALLGACERLLNKGIHPTIISESFQSAADEAIKILDEMSIP--VDLSDREQLLKSATTSLSSKVVSQySSLLAPL---AVD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 188 HVLPVAQQAGEIpyfNVD--SIRVVKIMGGSLSNSTVIKGMVFNREPEGHVKSLSEDKKHKVAVFTCPLDIANTETKGTV 265
Cdd:TIGR02342 167 AVLKVIDPENAK---NVDlnDIKVVKKLGGTIDDTELIEGLVFTQKASKSAGGPTRIEKAKIGLIQFQISPPKTDMENQI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 266 LLHNAQEMLDFSKGEEKQIDAMMKEIADMGVECI-----VAGAGVGELALHYLNRYGILVLKVPSKFELRRLCRVCGATP 340
Cdd:TIGR02342 244 IVNDYAQMDRVLKEERAYILNIVKKIKKTGCNVLliqksILRDAVNDLALHFLAKMKIMVVKDIEREEIEFICKTIGCKP 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 341 LPRLGAPTPEELGLVETVKTMEIGGDRVTVFKQEQgEISRTSTIILRGATQNNLDDIERAIDDGVAAVKGLMKPSGgkLL 420
Cdd:TIGR02342 324 IASIDHFTADKLGSAELVEEVDSDGGKIIKITGIQ-NAGKTVTVVVRGSNKLVIDEAERSLHDALCVIRCLVKKRG--LI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 421 PGAGATEIELISRITKYGERTPGLLQLAIKQFAVAFEVVPRTLAETAGLDVNEVLPNLYAAHnvtepgavKTDHLYKGVD 500
Cdd:TIGR02342 401 AGGGAPEIEIARRLSKYARTMKGVESYCVRAFADALEVIPYTLAENAGLNPIKVVTELRNRH--------ANGEKTAGIS 472
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 6322452 501 IdgeSDEGVKDIREENIYDMLATKKFAINVATEAATTVLSIDQIIMAK 548
Cdd:TIGR02342 473 V---RKGGITNMLEEHVLQPLLVTTSAITLASETVRSILKIDDIVFTR 517
|
|
| chap_CCT_gamma |
TIGR02344 |
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ... |
29-545 |
2.41e-72 |
|
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: 240.41 E-value: 2.41e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 29 IKSIAAIRELHQMCLTSMGPCGRNKIIVNHLGKIIITNDAATMLRELDIVHPAVKVLVMATEQQKIDMGDGTNLVMILAG 108
Cdd:TIGR02344 19 LSNIQAAKAVADIIRTCLGPRSMLKMLLDPMGGIVMTNDGNAILREIDVAHPAAKSMIELSRTQDEEVGDGTTSVIILAG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 109 ELLNVSEKLISMGLSAVEIIQGYNMARKFTLKELDEMVVgeITDKNDKNELLKMIKPVISSK---KYGseDILSELVSEA 185
Cdd:TIGR02344 99 EMLSVAEPFLEQNIHPTVIIRAYRKALDDALSVLEEISI--PVDVNDDAAMLKLIQSCIGTKfvsRWS--DLMCDLALDA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 186 VSHVlpvaqQAGEIPYFNVD---SIRVVKIMGGSLSNSTVIKGMVFNREPEgHVKSLSEDKKHKVAVFTCPLDIANTETK 262
Cdd:TIGR02344 175 VRTV-----QRDENGRKEIDikrYAKVEKIPGGDIEDSCVLKGVMINKDVT-HPKMRRYIENPRIVLLDCPLEYKKGESQ 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 263 GTVLLHNAQEMLDFSKGEEKQIDAMMKEIADMGVECIVAGAGVGELALHYLNRYGILVLKVPSKFELRRLCRVCGATPLP 342
Cdd:TIGR02344 249 TNIEITKEEDWNRILQMEEEYVQLMCEDIIAVKPDLVITEKGVSDLAQHYLLKANITAIRRVRKTDNNRIARACGATIVN 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 343 RlgaptPEEL---------GLVETVKtmeIGGDRVTVFkqEQGEISRTSTIILRGATQNNLDDIERAIDDGVAAVKGLMK 413
Cdd:TIGR02344 329 R-----PEELresdvgtgcGLFEVKK---IGDEYFTFI--TECKDPKACTILLRGASKDILNEVERNLQDAMAVARNVLL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 414 psGGKLLPGAGATEIELISRITKYGERTPGLLQLAIKQFAVAFEVVPRTLAETAGLDVNEVLPNLYAAHNvTEPGavktd 493
Cdd:TIGR02344 399 --DPKLVPGGGATEMAVSVALTEKSKKLEGVEQWPYRAVADALEIIPRTLAQNCGANVIRTLTELRAKHA-QENN----- 470
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 6322452 494 hlyKGVDIDGESDEGVkDIREENIYDMLATKKFAINVATEAATTVLSIDQII 545
Cdd:TIGR02344 471 ---CTWGIDGETGKIV-DMKEKGIWEPLAVKLQTYKTAIESACLLLRIDDIV 518
|
|
| TCP1_gamma |
cd03337 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ... |
29-545 |
8.54e-72 |
|
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: 237.96 E-value: 8.54e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 29 IKSIAAIRELHQMCLTSMGPCGRNKIIVNHLGKIIITNDAATMLRELDIVHPAVKVLVMATEQQKIDMGDGTNLVMILAG 108
Cdd:cd03337 19 LGNIQAAKTVADVIRTCLGPRAMLKMLLDPMGGIVLTNDGNAILREIDVAHPAAKSMIELSRTQDEEVGDGTTSVIILAG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 109 ELLNVSEKLISMGLSAVEIIQGYNMARKFTLKELDEMVVGeiTDKNDKNELLKMIKPVISSKKYGSE-DILSELVSEAVS 187
Cdd:cd03337 99 EILAVAEPFLERGIHPTVIIKAYRKALEDALKILEEISIP--VDVNDRAQMLKIIKSCIGTKFVSRWsDLMCNLALDAVK 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 188 HV-LPVAQQAGEIPYFNVdsIRVVKIMGGSLSNSTVIKGMVFNREPEgHVKSLSEDKKHKVAVFTCPLdiantetkgtvl 266
Cdd:cd03337 177 TVaVEENGRKKEIDIKRY--AKVEKIPGGEIEDSRVLDGVMLNKDVT-HPKMRRRIENPRIVLLDCPL------------ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 267 lhnaqEMLDFSkgeEKqidammkeiadmgvecivagaGVGELALHYLNRYGILVLKVPSKFELRRLCRVCGATPLPRLGA 346
Cdd:cd03337 242 -----EYLVIT---EK---------------------GVSDLAQHYLVKAGITALRRVRKTDNNRIARACGATIVNRPEE 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 347 PTPEELGLVETVKTMEIGGDRVTVFKQEQGEiSRTSTIILRGATQNNLDDIERAIDDGVAAVKGLMKpsGGKLLPGAGAT 426
Cdd:cd03337 293 LTESDVGTGAGLFEVKKIGDEYFTFITECKD-PKACTILLRGASKDVLNEVERNLQDAMAVARNIIL--NPKLVPGGGAT 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 427 EIELISRITKYGERTPGLLQLAIKQFAVAFEVVPRTLAETAGLDVNEVLPNLYAAHnvTEPGAVKTdhlykgvDIDGESD 506
Cdd:cd03337 370 EMAVSHALSEKAKSIEGVEQWPYKAVASALEVIPRTLAQNCGANVIRTLTELRAKH--AQGENSTW-------GIDGETG 440
|
490 500 510
....*....|....*....|....*....|....*....
gi 6322452 507 EGVkDIREENIYDMLATKKFAINVATEAATTVLSIDQII 545
Cdd:cd03337 441 DIV-DMKELGIWDPLAVKAQTYKTAIEAACMLLRIDDIV 478
|
|
| chap_CCT_epsi |
TIGR02343 |
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ... |
27-545 |
2.30e-69 |
|
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: 232.77 E-value: 2.30e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 27 QIIKS-IAAIRELHQMCLTSMGPCGRNKIIVNHLGKIIITNDAATMLRELDIVHPAVKVLVMATEQQKIDMGDGTNLVMI 105
Cdd:TIGR02343 27 EAKKSnIAAAKSVASILRTSLGPKGMDKMLISPDGDITVTNDGATILSQMDVDNQIAKLMVELSKSQDDEIGDGTTGVVV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 106 LAGELLNVSEKLISMGLSAVEIIQGYNMARKFTLKELDEmVVGEITDKNDKNE-LLKMIKPVISSK-KYGSEDILSELvs 183
Cdd:TIGR02343 107 LAGALLEQAEELLDKGIHPIKIADGFEEAARIAVEHLEE-ISDEISADNNNREpLIQAAKTSLGSKiVSKCHRRFAEI-- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 184 eAVSHVLPVAQQagEIPYFNVDSIRVVKIMGGSLSNSTVIKGMVFNREpEGHVKSLSEDKKHKVAVFTCPLDIANTETKG 263
Cdd:TIGR02343 184 -AVDAVLNVADM--ERRDVDFDLIKVEGKVGGSLEDTKLIKGIIIDKD-FSHPQMPKEVEDAKIAILTCPFEPPKPKTKH 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 264 TVLLHNAQEMLDFSKGEEKQIDAMMKEIADMGVECIVAGAGVGELALHYLNRYGILVLKVPSKFELRRLCRVCGATPLPR 343
Cdd:TIGR02343 260 KLDISSVEEYKKLQKYEQQKFKEMIDDIKKSGANLVICQWGFDDEANHLLLQNDLPAVRWVGGQELELIAIATGGRIVPR 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 344 LGAPTPEELGLVETVKTMEIGGDRVTVFKQEQGEISRTSTIILRGATQNNLDDIERAIDDGVAAVKGLMKPSggKLLPGA 423
Cdd:TIGR02343 340 FQELSKDKLGKAGLVREISFGTTKDRMLVIEQCKNSKAVTIFIRGGNKMIIEEAKRSIHDALCVVRNLIKDS--RIVYGG 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 424 GATEIELISRITKYGERTPGLLQLAIKQFAVAFEVVPRTLAETAGLDVNEVLPNLYAAHNvtepgavKTDHLYKGVDIDG 503
Cdd:TIGR02343 418 GAAEISCSLAVSQEADKYPGVEQYAIRAFADALETIPMALAENSGLDPIGTLSTLKSLQL-------KEKNPNLGVDCLG 490
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 6322452 504 esdEGVKDIREENIYDMLATKKFAINVATEAATTVLSIDQII 545
Cdd:TIGR02343 491 ---YGTNDMKEQFVFETLIGKKQQILLATQLVRMILKIDDVI 529
|
|
| TCP1_alpha |
cd03335 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ... |
44-545 |
1.26e-68 |
|
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: 230.63 E-value: 1.26e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 44 TSMGPCGRNKIIVNHLGKIIITNDAATMLRELDIVHPAVKVLVMATEQQKIDMGDGTNLVMILAGELLNVSEKLISMGLS 123
Cdd:cd03335 26 SSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDKEVGDGTTSVVIIAAELLKRANELVKQKIH 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 124 AVEIIQGYNMARKFTLKELDEMVVgEITDKNDKNELLKMIKPVISSKKYGSE-DILSELVSEAVSHVlPVAQQAGEIPYf 202
Cdd:cd03335 106 PTTIISGYRLACKEAVKYIKEHLS-ISVDNLGKESLINVAKTSMSSKIIGADsDFFANMVVDAILAV-KTTNEKGKTKY- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 203 NVDSIRVVKIMGGSLSNSTVIKGMVFN--REPEGHVKSLsedKKHKVAVftcpLDIANTETK---GT-VLLHNAQEMLDF 276
Cdd:cd03335 183 PIKAVNILKAHGKSAKESYLVNGYALNctRASQGMPTRV---KNAKIAC----LDFNLQKTKmklGVqVVVTDPEKLEKI 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 277 SKGEEKQIDAMMKEIADMGVECIVAGAGVGELALHYLNRYGILVLKVPSKFELRRLCRVCGATPLPRLGAPTPEE----- 351
Cdd:cd03335 256 RQRESDITKERIKKILAAGANVVLTTGGIDDMCLKYFVEAGAMAVRRVKKEDLRRIAKATGATLVSTLANLEGEEtfdps 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 352 -LGLVETVKTMEIGGDRVTVFKQEQGeiSRTSTIILRGATQNNLDDIERAIDDGVAAVKGLMKpsGGKLLPGAGATEIEL 430
Cdd:cd03335 336 yLGEAEEVVQERIGDDELILIKGTKK--RSSASIILRGANDFMLDEMERSLHDALCVVKRTLE--SNSVVPGGGAVETAL 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 431 ISRITKYGERTPGLLQLAIKQFAVAFEVVPRTLAETAGLDVNEVLPNLYAAHNVTEPGAVKTDHLYKGVD-IDGEsdegV 509
Cdd:cd03335 412 SIYLENFATTLGSREQLAIAEFAEALLVIPKTLAVNAAKDATELVAKLRAYHAAAQVKPDKKHLKWYGLDlINGK----V 487
|
490 500 510
....*....|....*....|....*....|....*.
gi 6322452 510 KDIREENIYDMLATKKFAINVATEAATTVLSIDQII 545
Cdd:cd03335 488 RDNLEAGVLEPTVSKIKSLKFATEAAITILRIDDLI 523
|
|
| TCP1_epsilon |
cd03339 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ... |
29-545 |
4.40e-68 |
|
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: 229.11 E-value: 4.40e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 29 IKS-IAAIRELHQMCLTSMGPCGRNKIIVNHLGKIIITNDAATMLRELDIVHPAVKVLVMATEQQKIDMGDGTNLVMILA 107
Cdd:cd03339 25 HKShILAAKSVANILRTSLGPRGMDKILVSPDGEVTVTNDGATILEKMDVDHQIAKLLVELSKSQDDEIGDGTTGVVVLA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 108 GELLNVSEKLISMGLSAVEIIQGYNMARKFTLKELDEMVVGEITDKNDKNELLKMIKPVISSK-KYGSEDILSELvseAV 186
Cdd:cd03339 105 GALLEQAEKLLDRGIHPIRIADGYEQACKIAVEHLEEIADKIEFSPDNKEPLIQTAMTSLGSKiVSRCHRQFAEI---AV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 187 SHVLPVAQQagEIPYFNVDSIRVVKIMGGSLSNSTVIKGMVFNREpEGHVKSLSEDKKHKVAVFTCPLDIANTETKGTVL 266
Cdd:cd03339 182 DAVLSVADL--ERKDVNFELIKVEGKVGGRLEDTKLVKGIVIDKD-FSHPQMPKEVKDAKIAILTCPFEPPKPKTKHKLD 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 267 LHNAQEMLDFSKGEEKQIDAMMKEIADMGVECIVAGAGVGELALHYLNRYGILVLKVPSKFELRRLCRVCGATPLPRLGA 346
Cdd:cd03339 259 ITSVEDYKKLQEYEQKYFREMVEQVKDAGANLVICQWGFDDEANHLLLQNGLPAVRWVGGVEIELIAIATGGRIVPRFED 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 347 PTPEELGLVETVKTMEIGGDRVTVFKQEQGEISRTSTIILRGATQNNLDDIERAIDDGVAAVKGLMKPSggKLLPGAGAT 426
Cdd:cd03339 339 LSPEKLGKAGLVREISFGTTKDKMLVIEGCPNSKAVTIFIRGGNKMIIEEAKRSLHDALCVVRNLIRDN--RIVYGGGAA 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 427 EIELISRITKYGERTPGLLQLAIKQFAVAFEVVPRTLAETAGLDVNEVLPNLYAAHnvtepgaVKTDHLYKGVDIDGesd 506
Cdd:cd03339 417 EISCSLAVEKAADKCSGIEQYAMRAFADALESIPLALAENSGLNPIETLSEVKARQ-------VKEKNPHLGIDCLG--- 486
|
490 500 510
....*....|....*....|....*....|....*....
gi 6322452 507 EGVKDIREENIYDMLATKKFAINVATEAATTVLSIDQII 545
Cdd:cd03339 487 RGTNDMKEQKVFETLISKKQQILLATQVVKMILKIDDVI 525
|
|
| chap_CCT_alpha |
TIGR02340 |
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ... |
44-545 |
6.81e-66 |
|
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: 223.83 E-value: 6.81e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 44 TSMGPCGRNKIIVNHLGKIIITNDAATMLRELDIVHPAVKVLVMATEQQKIDMGDGTNLVMILAGELLNVSEKLISMGLS 123
Cdd:TIGR02340 30 TSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDREVGDGTTSVVIIAAELLKRADELVKNKIH 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 124 AVEIIQGYNMARKFTLKELDEMVVGEiTDKNDKNELLKMIKPVISSKKYGSE-DILSELVSEAVSHVlPVAQQAGEIPYf 202
Cdd:TIGR02340 110 PTSVISGYRLACKEAVKYIKENLSVS-VDELGREALINVAKTSMSSKIIGLDsDFFSNIVVDAVLAV-KTTNENGETKY- 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 203 NVDSIRVVKIMGGSLSNSTVIKGMVFN--REPEGHVKSLsedKKHKVAVFTCPLDIANTETKGTVLLHNAQEMLDFSKGE 280
Cdd:TIGR02340 187 PIKAINILKAHGKSARESMLVKGYALNctVASQQMPKRI---KNAKIACLDFNLQKAKMALGVQIVVDDPEKLEQIRQRE 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 281 EKQIDAMMKEIADMGVECIVAGAGVGELALHYLNRYGILVLKVPSKFELRRLCRVCGATPLPRLGAPTPEE------LGL 354
Cdd:TIGR02340 264 ADITKERIKKILDAGANVVLTTGGIDDMCLKYFVEAGAMGVRRCKKEDLKRIAKATGATLVSTLADLEGEEtfeasyLGF 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 355 VETVKTMEIGGDRVTVFKQEQGeiSRTSTIILRGATQNNLDDIERAIDDGVAAVKGLMKpsGGKLLPGAGATEIELISRI 434
Cdd:TIGR02340 344 ADEVVQERIADDECILIKGTKK--RKSASIILRGANDFMLDEMERSLHDALCVVKRTLE--SNSVVPGGGAVEAALSIYL 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 435 TKYGERTPGLLQLAIKQFAVAFEVVPRTLAETAGLDVNEVLPNLYAAHNVTEPGAVKTDHLYKGVDIdgeSDEGVKDIRE 514
Cdd:TIGR02340 420 ENFATTLGSREQLAIAEFARALLIIPKTLAVNAAKDSTELVAKLRAYHAAAQLKPEKKHLKWYGLDL---VNGKIRDNKE 496
|
490 500 510
....*....|....*....|....*....|.
gi 6322452 515 ENIYDMLATKKFAINVATEAATTVLSIDQII 545
Cdd:TIGR02340 497 AGVLEPTVSKVKSLKFATEAAITILRIDDLI 527
|
|
| chap_CCT_zeta |
TIGR02347 |
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ... |
8-550 |
1.01e-60 |
|
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: 209.59 E-value: 1.01e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 8 NPNAGLfkqgynsySNADGQIIKSIAAIRELHQMCLTSMGPCGRNKIIVNHLGKIIITNDAATMLRELDIVHPAVKVLVM 87
Cdd:TIGR02347 6 NPKAES--------LRRDAALMMNINAARGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEMQIQHPTASMIAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 88 ATEQQKIDMGDGTNLVMILAGELLNVSEKLISMGLSAVEIIQGYNMARKFTLKELDEMVVgEITDKNDKNELLKMIKPVI 167
Cdd:TIGR02347 78 AATAQDDITGDGTTSTVLLIGELLKQAERYILEGVHPRIITEGFEIARKEALQFLDKFKV-KKEDEVDREFLLNVARTSL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 168 SSKKY-GSEDILSELVSEAvshVLPVAQQAGEIPYFNVDsirVVKIMGGSLSNSTVIKGMVFN---REPEghvkslSEDK 243
Cdd:TIGR02347 157 RTKLPaDLADQLTEIVVDA---VLAIKKDGEDIDLFMVE---IMEMKHKSATDTTLIRGLVLDhgaRHPD------MPRR 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 244 KHKVAVFTC--PLDIANTETKGTVLLHNAQEMLDFSKGEEKQIDAMMKEIADMGVE----------CIVAGAGVGELALH 311
Cdd:TIGR02347 225 VKNAYILTCnvSLEYEKTEVNSGFFYSSAEQREKLVKAERKFVDDRVKKIIELKKKvcgkspdkgfVVINQKGIDPPSLD 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 312 YLNRYGILVLKVPSKFELRRLCRVCGATPLPRLGAPTPEELGLVETVKTMEIGGDRVTVFkqEQGEISRTSTIILRGATQ 391
Cdd:TIGR02347 305 LLAKEGIMALRRAKRRNMERLTLACGGEALNSVEDLTPECLGWAGLVYETTIGEEKYTFI--EECKNPKSCTILIKGPND 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 392 NNLDDIERAIDDGVAAVKGLMKPSGgkLLPGAGATEIELISRITKYGERTPGLLQLAIKQFAVAFEVVPRTLAETAGLDV 471
Cdd:TIGR02347 383 HTIAQIKDAVRDGLRAVKNAIEDKC--VVPGAGAFEIAAYRHLKEYKKSVKGKAKLGVEAFANALLVIPKTLAENSGFDA 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 472 NEVLPNLYAAHNVTEPgavktdhlYKGVDID-GESdegvKDIREENIYDMLATKKFAINVATEAATTVLSIDQIIMAKKA 550
Cdd:TIGR02347 461 QDTLVKLEDEHDEGGE--------VVGVDLNtGEP----IDPEIKGIWDNYRVKKQLIQSATVIASQLLLVDEVMRAGRS 528
|
|
| chaperonin_like |
cd03333 |
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ... |
156-413 |
3.49e-54 |
|
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: 182.67 E-value: 3.49e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 156 KNELLKMIKPVISSKKYGSEDILSELVSEAVSHVLPvaqqagEIPYFNVDSIRVVKIMGGSLSNSTVIKGMVFNREPEgH 235
Cdd:cd03333 1 RELLLQVATTSLNSKLSSWDDFLGKLVVDAVLKVGP------DNRMDDLGVIKVEKIPGGSLEDSELVVGVVFDKGYA-S 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 236 VKSLSEDKKHKVAVFTCPLDIantetkgtvllhnaqemldfskgeekqidammkeiadmgveCIVAGAGVGELALHYLNR 315
Cdd:cd03333 74 PYMPKRLENAKILLLDCPLEY-----------------------------------------VVIAEKGIDDLALHYLAK 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 316 YGILVLKVPSKFELRRLCRVCGATPLPRLGAPTPEELGLVETVKTMEIGGDRVTVFkqEQGEISRTSTIILRGATQNNLD 395
Cdd:cd03333 113 AGIMAVRRVKKEDLERIARATGATIVSSLEDLTPEDLGTAELVEETKIGEEKLTFI--EGCKGGKAATILLRGATEVELD 190
|
250
....*....|....*...
gi 6322452 396 DIERAIDDGVAAVKGLMK 413
Cdd:cd03333 191 EVKRSLHDALCAVRAAVE 208
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
44-545 |
6.74e-54 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 191.40 E-value: 6.74e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 44 TSMGPCGRNKIIV-----NHLGKIIITNDAATMLRELDIVHPAVKVLVMATEQQKIDMGDGTNLVMILAGELLNVSEKLI 118
Cdd:PTZ00212 40 TTLGPKGMDKILQpmsegPRSGNVTVTNDGATILKSVWLDNPAAKILVDISKTQDEEVGDGTTSVVVLAGELLREAEKLL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 119 SMGLSAVEIIQGYNMARKFTLKELDEMVVGEITDKND-KNELLKMIKPVISSKKYGSE-DILSELvseAVSHVLPVAQQA 196
Cdd:PTZ00212 120 DQKIHPQTIIEGWRMALDVARKALEEIAFDHGSDEEKfKEDLLNIARTTLSSKLLTVEkDHFAKL---AVDAVLRLKGSG 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 197 geipyfNVDSIRVVKIMGGSLSNSTVIKGMVFNRE-PEGHVKSLSEdkkHKVAVFTCPLDIANTETKGT-VLLHNAQEML 274
Cdd:PTZ00212 197 ------NLDYIQIIKKPGGTLRDSYLEDGFILEKKiGVGQPKRLEN---CKILVANTPMDTDKIKIYGAkVKVDSMEKVA 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 275 DFSKGEEKQIDAMMKEIADMGVECIVAGAGVGELALHYLNRYGILVLKvPSKFE-LRRLCRVCGATPLPRLGAPTPEELG 353
Cdd:PTZ00212 268 EIEAAEKEKMKNKVDKILAHGCNVFINRQLIYNYPEQLFAEAGIMAIE-HADFDgMERLAAALGAEIVSTFDTPEKVKLG 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 354 LVETVKTMEIGGDRVTVFKQ-EQGEisrTSTIILRGATQNNLDDIERAIDDGVAAVKGLMKpsGGKLLPGAGATEIELIS 432
Cdd:PTZ00212 347 HCDLIEEIMIGEDKLIRFSGcAKGE---ACTIVLRGASTHILDEAERSLHDALCVLSQTVK--DTRVVLGGGCSEMLMAN 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 433 RITKYGERTPGLLQLAIKQFAVAFEVVPRTLAETAGLDVNEVLPNLYAAHNvtepgavkTDHLYKGVDIDgesDEGVKDI 512
Cdd:PTZ00212 422 AVEELAKKVEGKKSLAIEAFAKALRQIPTIIADNGGYDSAELVSKLRAEHY--------KGNKTAGIDME---KGTVGDM 490
|
490 500 510
....*....|....*....|....*....|...
gi 6322452 513 REENIYDMLATKKFAINVATEAATTVLSIDQII 545
Cdd:PTZ00212 491 KELGITESYKVKLSQLCSATEAAEMILRVDDII 523
|
|
| GroEL |
COG0459 |
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ... |
32-553 |
9.98e-54 |
|
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227 Cd Length: 497 Bit Score: 189.90 E-value: 9.98e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 32 IAAIRELHQMCLTSMGPCGRNKIIVNHLGKIIITNDAATMLRELDIVHP----AVKVLVMATEQQKIDMGDGTNLVMILA 107
Cdd:COG0459 16 IRGVKALADAVKVTLGPKGRNVMLVKSFGDPTITNDGVTIAKEIELEDPfenmGAQLVKEVASKTNDEAGDGTTTATVLA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 108 GELLNVSEKLISMGLSAVEIIQGYNMARKFTLKELDEMVVgEITDKndknellKMIKPV--ISSkkyGSEDILSELVSEA 185
Cdd:COG0459 96 GALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAK-PVDDK-------EELAQVatISA---NGDEEIGELIAEA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 186 VSHVlpvaqqaGEIPYFNVDSirvvkimGGSLSNST-VIKGMVFNREPeghvksLSE----DKKHKVAVFTCPLdIANTE 260
Cdd:COG0459 165 MEKV-------GKDGVITVEE-------GKGLETELeVVEGMQFDKGY------LSPyfvtDPEKMPAELENAY-ILLTD 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 261 TKgtvlLHNAQEMLDfskgeekqidaMMKEIADMGVECIVAGAGVGELALHYLNRYGIL-VLKVPS----------KFEL 329
Cdd:COG0459 224 KK----ISSIQDLLP-----------LLEKVAQSGKPLLIIAEDIDGEALATLVVNGIRgVLRVVAvkapgfgdrrKAML 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 330 RRLCRVCGATPL-----PRLGAPTPEELGLVETVktmEIGGDRVTVFkqEQGEISRTSTIILRGATQNNLDDIERAIDDG 404
Cdd:COG0459 289 EDIAILTGGRVIsedlgLKLEDVTLDDLGRAKRV---EVDKDNTTIV--EGAGNPKAIVILVGAATEVEVKERKRRVEDA 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 405 VAAVKGLMKpsgGKLLPGAGATEIELISRITKYGERTPGLLQLAIKQFAVAFEVVPRTLAETAGLDVNEVLPNLYAAHNv 484
Cdd:COG0459 364 LHATRAAVE---EGIVPGGGAALLRAARALRELAAKLEGDEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKVRAAKD- 439
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6322452 485 tepgavktdhlyKGVDIDGESDEgVKDIREENIYDMLATKKFAINVATEAATTVLSIDQIIMAKKAGGP 553
Cdd:COG0459 440 ------------KGFGFDAATGE-YVDMLEAGVIDPAKVKRSALQNAASVAGLILTTEAVIADKPEKEE 495
|
|
| TCP1_beta |
cd03336 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ... |
44-554 |
3.28e-53 |
|
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: 189.08 E-value: 3.28e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 44 TSMGPCGRNKII--VNHLGKIIITNDAATMLRELDIVHPAVKVLVMATEQQKIDMGDGTNLVMILAGELLNVSEKLISMG 121
Cdd:cd03336 31 TTLGPKGMDKILqsVGRSGGVTVTNDGATILKSIGVDNPAAKVLVDISKVQDDEVGDGTTSVTVLAAELLREAEKLVAQK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 122 LSAVEIIQGYNMARKFTLKELDEMVVGEITDKND-KNELLKMIKPVISSKKYGSE-DILSELvseAVSHVLPVAQQAgei 199
Cdd:cd03336 111 IHPQTIIEGYRMATAAAREALLSSAVDHSSDEEAfREDLLNIARTTLSSKILTQDkEHFAEL---AVDAVLRLKGSG--- 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 200 pyfNVDSIRVVKIMGGSLSNSTVIKGMVFNREPE-GHVKSLSedkKHKVAVFTCPLDIANTETKGT-VLLHNAQEMLDFS 277
Cdd:cd03336 185 ---NLDAIQIIKKLGGSLKDSYLDEGFLLDKKIGvNQPKRIE---NAKILIANTPMDTDKIKIFGAkVRVDSTAKVAEIE 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 278 KGEEKQIDAMMKEIADMGVECIVAGAGVGELALHYLNRYGILVLKVPSkFE-LRRLCRVCGATPLPRLGAPTPEELGLVE 356
Cdd:cd03336 259 EAEKEKMKNKVEKILKHGINCFINRQLIYNYPEQLFADAGIMAIEHAD-FDgVERLALVTGGEIASTFDHPELVKLGTCK 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 357 TVKTMEIGGDRVTVFKQ-EQGEisrTSTIILRGATQNNLDDIERAIDDGVAAVKGLMKPSggKLLPGAGATEIELISRIT 435
Cdd:cd03336 338 LIEEIMIGEDKLIRFSGvAAGE---ACTIVLRGASQQILDEAERSLHDALCVLAQTVKDT--RVVLGGGCSEMLMAKAVE 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 436 KYGERTPGLLQLAIKQFAVAFEVVPRTLAETAGLDVNEVLPNLYAAHNvtepgavKTDHLYkGVDIDGESdegVKDIREE 515
Cdd:cd03336 413 ELAKKTPGKKSLAIEAFAKALRQLPTIIADNAGYDSAELVAQLRAAHY-------NGNTTA-GLDMRKGT---VGDMKEL 481
|
490 500 510
....*....|....*....|....*....|....*....
gi 6322452 516 NIYDMLATKKFAINVATEAATTVLSIDQIIMAKkaggPR 554
Cdd:cd03336 482 GITESFKVKRQVLLSASEAAEMILRVDDIIKCA----PR 516
|
|
| TCP1_zeta |
cd03342 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
32-549 |
3.46e-49 |
|
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: 177.45 E-value: 3.46e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 32 IAAIRELHQMCLTSMGPCGRNKIIVNHLGKIIITNDAATMLRELDIVHP-AVKVLVMATEQQKIdMGDGTNLVMILAGEL 110
Cdd:cd03342 18 ISAAKGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLSEMQIQHPtASMIARAATAQDDI-TGDGTTSNVLLIGEL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 111 LNVSEKLISMGLSAVEIIQGYNMARKFTLKELDEMVVgEITDKNDKNELLKMIKPVISSKKYGS-EDILSELVSEAVshv 189
Cdd:cd03342 97 LKQAERYIQEGVHPRIITEGFELAKNKALKFLESFKV-PVEIDTDRELLLSVARTSLRTKLHADlADQLTEIVVDAV--- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 190 LPVAQQAGEIPYFNVDsirVVKIMGGSLSNSTVIKGMVFN---REPeghvkslseDKKHKVavftcpldianteTKGTVL 266
Cdd:cd03342 173 LAIYKPDEPIDLHMVE---IMQMQHKSDSDTKLIRGLVLDhgaRHP---------DMPKRV-------------ENAYIL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 267 LHNAQemLDFSKGE------------EKQIDAMmkeiadmgvecivagagvgelALHYLNRYGILVLKVPSKFELRRLCR 334
Cdd:cd03342 228 TCNVS--LEYEKTEvnsgffysvvinQKGIDPP---------------------SLDMLAKEGILALRRAKRRNMERLTL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 335 VCGATPLPRLGAPTPEELGLVETVKTMEIGGDRVTVfkQEQGEISRTSTIILRGATQNNLDDIERAIDDGVAAVKGLMKp 414
Cdd:cd03342 285 ACGGVAMNSVDDLSPECLGYAGLVYERTLGEEKYTF--IEGVKNPKSCTILIKGPNDHTITQIKDAIRDGLRAVKNAIE- 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 415 sGGKLLPGAGATEIELISRITKYGERTPGLLQLAIKQFAVAFEVVPRTLAETAGLDVNEVLPNLYAAHnvtepgavktDH 494
Cdd:cd03342 362 -DKCVVPGAGAFEVALYAHLKEFKKSVKGKAKLGVQAFADALLVIPKTLAENSGLDVQETLVKLQDEY----------AE 430
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 6322452 495 LYKGVDIDGESDEGVkDIREENIYDMLATKKFAINVATEAATTVLSIDQIIMAKK 549
Cdd:cd03342 431 GGQVGGVDLDTGEPM-DPESEGIWDNYSVKRQILHSATVIASQLLLVDEIIRAGR 484
|
|
| chap_CCT_beta |
TIGR02341 |
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ... |
44-555 |
1.30e-44 |
|
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: 165.42 E-value: 1.30e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 44 TSMGPCGRNKIIV--NHLGKIIITNDAATMLRELDIVHPAVKVLVMATEQQKIDMGDGTNLVMILAGELLNVSEKLISMG 121
Cdd:TIGR02341 32 STLGPKGMDKILQssSSDASIMVTNDGATILKSIGVDNPAAKVLVDMSKVQDDEVGDGTTSVTVLAAELLREAEKLINQK 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 122 LSAVEIIQGYNMARKFTLKELDEMVVGEITDKND-KNELLKMIKPVISSKKYGS-EDILSELVSEAVSHVlpvaQQAGei 199
Cdd:TIGR02341 112 IHPQTIIAGYREATKAARDALLKSAVDNGSDEVKfRQDLMNIARTTLSSKILSQhKDHFAQLAVDAVLRL----KGSG-- 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 200 pyfNVDSIRVVKIMGGSLSNSTVIKGMVFNREPEGHVKSLSEdkKHKVAVFTCPLDIANTETKGT-VLLHNAQEMLDFSK 278
Cdd:TIGR02341 186 ---NLEAIQIIKKLGGSLADSYLDEGFLLDKKIGVNQPKRIE--NAKILIANTGMDTDKVKIFGSrVRVDSTAKVAELEH 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 279 GEEKQIDAMMKEIADMGVECIVAGAGVGELALHYLNRYGILVLKVPSKFELRRLCRVCGATPLPRLGAPTPEELGLVETV 358
Cdd:TIGR02341 261 AEKEKMKEKVEKILKHGINCFINRQLIYNYPEQLFADAGVMAIEHADFEGVERLALVTGGEIVSTFDHPELVKLGSCDLI 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 359 KTMEIGGDRVTVFKQ-EQGEisrTSTIILRGATQNNLDDIERAIDDGVAAVKGLMKPSggKLLPGAGATEIELISRITKY 437
Cdd:TIGR02341 341 EEIMIGEDKLLKFSGvKLGE---ACTIVLRGATQQILDEAERSLHDALCVLSQTVKES--RTVLGGGCSEMLMSKAVTQE 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 438 GERTPGLLQLAIKQFAVAFEVVPRTLAETAGLDVNEVLPNLYAAHnvtepgavktdhlYKGVDIDG-ESDEG-VKDIREE 515
Cdd:TIGR02341 416 AQRTPGKEALAVEAFARALRQLPTIIADNAGFDSAELVAQLRAAH-------------YNGNTTMGlDMNEGtIADMRQL 482
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 6322452 516 NIYDMLATKKFAINVATEAATTVLSIDQIIMAKkaggPRA 555
Cdd:TIGR02341 483 GITESYKVKRAVVSSAAEAAEVILRVDNIIKAA----PRK 518
|
|
| Fab1_TCP |
cd03334 |
TCP-1 like domain of the eukaryotic phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinase Fab1. ... |
176-408 |
2.78e-10 |
|
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: 61.08 E-value: 2.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 176 DILSELVSEAVSHVLPVAQQAGEIpyFNVDSIRVVKIMGGSLSNSTVIKGMVFNRepegHV--KSLSEDKKH-KVAVFTC 252
Cdd:cd03334 21 DILLPLVWKAASNVKPDVRAGDDM--DIRQYVKIKKIPGGSPSDSEVVDGVVFTK----NVahKRMPSKIKNpRILLLQG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 253 PLDIANTETK----GTVLLHnaqemldfskgEEKQIDAMMKEIADMGVECIVAGAGVGELALHYLNRYGI-LVLKVPSKF 327
Cdd:cd03334 95 PLEYQRVENKllslDPVILQ-----------EKEYLKNLVSRIVALRPDVILVEKSVSRIAQDLLLEAGItLVLNVKPSV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 328 eLRRLCRVCGATPL---------PRLGaptpeELGLVETVKTMEIGGDRVTVFKQEQGEISRTSTIILRGATQNNLDDIE 398
Cdd:cd03334 164 -LERISRCTGADIIssmddlltsPKLG-----TCESFRVRTYVEEHGRSKTLMFFEGCPKELGCTILLRGGDLEELKKVK 237
|
250
....*....|
gi 6322452 399 RAIDDGVAAV 408
Cdd:cd03334 238 RVVEFMVFAA 247
|
|
| PLN03167 |
PLN03167 |
Chaperonin-60 beta subunit; Provisional |
21-145 |
5.01e-08 |
|
Chaperonin-60 beta subunit; Provisional
Pssm-ID: 215611 [Multi-domain] Cd Length: 600 Bit Score: 55.70 E-value: 5.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 21 YSNADGQIIKSI-AAIRELHQMCLTSMGPCGRNKIIVNHLGKIIITNDAATMLRELDIVHP----AVKVLVMATEQQKID 95
Cdd:PLN03167 60 HFNKDGSAIKKLqAGVNKLADLVGVTLGPKGRNVVLESKYGSPKIVNDGVTVAKEVELEDPveniGAKLVRQAAAKTNDL 139
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 6322452 96 MGDGTNLVMILAGELLNVSEKLISMGLSAVEIIQGYNMARKFTLKELDEM 145
Cdd:PLN03167 140 AGDGTTTSVVLAQGLIAEGVKVVAAGANPVQITRGIEKTAKALVKELKKM 189
|
|
| GroEL |
cd03344 |
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ... |
46-189 |
2.70e-05 |
|
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: 47.07 E-value: 2.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 46 MGPCGRNKIIVNHLGKIIITNDAATMLRELDIVHP----AVKVLVMATEQQKIDMGDGTNLVMILAGELLNVSEKLISMG 121
Cdd:cd03344 28 LGPKGRNVVIEKSFGSPKITKDGVTVAKEIELEDPfenmGAQLVKEVASKTNDVAGDGTTTATVLARAIIKEGLKAVAAG 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 122 LSAVEIIQGYNMARKFTLKELDEMVVgEITDKNDknellkmIKPV--ISSkkyGSEDILSELVSEAVSHV 189
Cdd:cd03344 108 ANPMDLKRGIEKAVEAVVEELKKLSK-PVKTKEE-------IAQVatISA---NGDEEIGELIAEAMEKV 166
|
|
| PTZ00114 |
PTZ00114 |
Heat shock protein 60; Provisional |
44-155 |
1.66e-04 |
|
Heat shock protein 60; Provisional
Pssm-ID: 185455 Cd Length: 555 Bit Score: 44.52 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 44 TSMGPCGRNKIIVNHLGKIIITNDAATMLRELDIVHPAVKV---LVMATEQQKIDM-GDGTNLVMILAGELLNVSEKLIS 119
Cdd:PTZ00114 40 VTLGPKGRNVIIEQEYGSPKITKDGVTVAKAIEFSDRFENVgaqLIRQVASKTNDKaGDGTTTATILARAIFREGCKAVA 119
|
90 100 110
....*....|....*....|....*....|....*.
gi 6322452 120 MGLSAVEIIQGYNMARKFTLKELDEMVVgEITDKND 155
Cdd:PTZ00114 120 AGLNPMDLKRGIDLAVKVVLESLKEQSR-PVKTKED 154
|
|
| groEL |
PRK12849 |
chaperonin GroEL; Reviewed |
46-189 |
2.79e-04 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237230 Cd Length: 542 Bit Score: 43.64 E-value: 2.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 46 MGPCGRNKIIVNHLGKIIITNDAATMLRELDIVHP----AVKVLVMATEQQKIDMGDGTNLVMILAGELLNVSEKLISMG 121
Cdd:PRK12849 30 LGPKGRNVVIDKSFGAPTITKDGVSIAKEIELEDPfenlGAQLVKEVASKTNDVAGDGTTTATVLAQALVQEGLKNVAAG 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 122 LSAVEIIQGYNMARKFTLKELDEMVVgEITDKndknellKMIKPV--ISSkkyGSEDILSELVSEAVSHV 189
Cdd:PRK12849 110 ANPMDLKRGIDKAVEAVVEELKALAR-PVSGS-------EEIAQVatISA---NGDEEIGELIAEAMEKV 168
|
|
| groEL |
PRK12851 |
chaperonin GroEL; Reviewed |
45-230 |
4.98e-04 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 171770 Cd Length: 541 Bit Score: 42.81 E-value: 4.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 45 SMGPCGRNKIIVNHLGKIIITNDAATMLRELDIVHP----AVKVLVMATEQQKIDMGDGTNLVMILAGELLNVSEKLISM 120
Cdd:PRK12851 30 TLGPKGRNVVIDKSFGAPTITNDGVTIAKEIELEDKfenmGAQMVREVASKTNDVAGDGTTTATVLAQAIVREGAKAVAA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 121 GLSAVEIIQGYNMARKFTLKELDEMvVGEITDKNDKNEllkmikpVISSKKYGSEDIlSELVSEAVSHVlpvaqqAGEip 200
Cdd:PRK12851 110 GANPMDLKRGIDRAVAAVVEELKAN-ARPVTTNAEIAQ-------VATISANGDAEI-GRLVAEAMEKV------GNE-- 172
|
170 180 190
....*....|....*....|....*....|
gi 6322452 201 yfNVDSIRVVKIMGGSLSnstVIKGMVFNR 230
Cdd:PRK12851 173 --GVITVEESKTAETELE---VVEGMQFDR 197
|
|
| PRK14104 |
PRK14104 |
chaperonin GroEL; Provisional |
45-209 |
1.08e-03 |
|
chaperonin GroEL; Provisional
Pssm-ID: 172594 Cd Length: 546 Bit Score: 41.94 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 45 SMGPCGRNKIIVNHLGKIIITNDAATMLRELDIVHPAVKV---LVMATEQQKIDM-GDGTNLVMILAGELLNVSEKLISM 120
Cdd:PRK14104 30 TLGPKGRNVVLDKSFGAPRITKDGVTVAKEIELEDKFENMgaqMVREVASKSADAaGDGTTTATVLAQAIVREGAKSVAA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 121 GLSAVEIIQGYNMARKFTLKEL----------DEMV-VGEITDKNDKnELLKMIKPVIssKKYGSEDILSELVSEAVSHV 189
Cdd:PRK14104 110 GMNPMDLKRGIDLAVEAVVADLvknskkvtsnDEIAqVGTISANGDA-EIGKFLADAM--KKVGNEGVITVEEAKSLETE 186
|
170 180
....*....|....*....|....*..
gi 6322452 190 LPVAQ----QAGEI-PYF--NVDSIRV 209
Cdd:PRK14104 187 LDVVEgmqfDRGYIsPYFvtNADKMRV 213
|
|
| groEL |
PRK12850 |
chaperonin GroEL; Reviewed |
45-189 |
1.29e-03 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237231 Cd Length: 544 Bit Score: 41.63 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 45 SMGPCGRNKIIVNHLGKIIITNDAATMLRELDIVHPAVKV---LVMATEQQKIDM-GDGTNLVMILAGELLNVSEKLISM 120
Cdd:PRK12850 30 TLGPKGRNVVLEKSFGAPRITKDGVTVAKEIELEDKFENMgaqMVKEVASKTNDLaGDGTTTATVLAQAIVREGAKLVAA 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6322452 121 GLSAVEIIQGYNMARkftlkeldEMVVGEITDKNDKNELLKMIKPVISSKKYGSEDIlSELVSEAVSHV 189
Cdd:PRK12850 110 GMNPMDLKRGIDLAV--------AAVVDELKKIAKKVTSSKEIAQVATISANGDESI-GEMIAEAMDKV 169
|
|
| MTH1175 |
cd00851 |
This uncharacterized conserved protein belongs to a family of iron-molybdenum cluster-binding ... |
286-325 |
6.10e-03 |
|
This uncharacterized conserved protein belongs to a family of iron-molybdenum cluster-binding proteins that includes NifX, NifB, and NifY, all of which are involved in the synthesis of an iron-molybdenum cofactor (FeMo-co) that binds the active site of the dinitrogenase enzyme. This domain is a predicted small-molecule-binding domain (SMBD) with an alpha/beta fold that is present either as a stand-alone domain (e.g. NifX and NifY) or fused to another conserved domain (e.g. NifB) however, its function is still undetermined.The SCOP database suggests that this domain is most similar to structures within the ribonuclease H superfamily. This conserved domain is represented in two of the three major divisions of life (bacteria and archaea).
Pssm-ID: 238431 Cd Length: 103 Bit Score: 36.48 E-value: 6.10e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 6322452 286 AMMKEIADMGVECIVAGaGVGELALHYLNRYGILVLKVPS 325
Cdd:cd00851 54 KAAEFLADEGVDVVIVG-GIGPRALNKLRNAGIKVYKGAE 92
|
|
| groEL |
CHL00093 |
chaperonin GroEL |
45-208 |
7.54e-03 |
|
chaperonin GroEL
Pssm-ID: 177025 Cd Length: 529 Bit Score: 38.93 E-value: 7.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 45 SMGPCGRNKIIVNHLGKIIITNDAATMLRELDIVHPA----VKVLVMATEQQKIDMGDGTNLVMILAGELLNVSEKLISM 120
Cdd:CHL00093 29 TLGPKGRNVVLEKKYGSPQIVNDGVTIAKEIELEDHIentgVALIRQAASKTNDVAGDGTTTATVLAYAIVKQGMKNVAA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322452 121 GLSAVEIIQGYNMARKFTLKELDEMV-----------VGEITDKNDkNELLKMIKPVIssKKYGSEDILSELVSEAVSHV 189
Cdd:CHL00093 109 GANPISLKRGIEKATQYVVSQIAEYArpvediqaitqVASISAGND-EEVGSMIADAI--EKVGREGVISLEEGKSTVTE 185
|
170 180
....*....|....*....|....
gi 6322452 190 LPVAQ----QAGEI-PYFNVDSIR 208
Cdd:CHL00093 186 LEITEgmrfEKGFIsPYFVTDTER 209
|
|
| |
