|
Name |
Accession |
Description |
Interval |
E-value |
| thermosome_alpha |
NF041082 |
thermosome subunit alpha; |
1-490 |
0e+00 |
|
thermosome subunit alpha;
Pssm-ID: 469009 Cd Length: 518 Bit Score: 795.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 1 VLPENMKRYMGRDAQRMNILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQE 80
Cdd:NF041082 5 ILKEGTQRTSGRDAQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDVVITNDGVTILKEMDIEHPAAKMIVEVAKTQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 81 KEVGDGTTTAVVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQDKEILTKIAMTSITGKGAEKA 160
Cdd:NF041082 85 DEVGDGTTTAVVLAGELLKKAEELLDQDIHPTIIAEGYRLAAEKALEILDEIAIKVDPDDKETLKKIAATAMTGKGAEAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 161 KEKLAEIIVEAVSAVVDDEG--KVDKDLIKIEKKSGASIDDTELIKGVLVDKERVSAQMPKKVTDAKIALLNCAIE---- 234
Cdd:NF041082 165 KDKLADLVVDAVKAVAEKDGgyNVDLDNIKVEKKVGGSIEDSELVEGVVIDKERVHPGMPKRVENAKIALLDAPLEvkkt 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 235 ------------------ETASEMLKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATGAN 296
Cdd:NF041082 245 eidakisitdpdqlqaflDQEEKMLKEMVDKIADSGANVVFCQKGIDDLAQHYLAKEGILAVRRVKKSDMEKLAKATGAR 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 297 VITNIKDLSAQDLGDAGLVEERKISGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIVSGG 376
Cdd:NF041082 325 IVTSIDDLSPEDLGYAGLVEERKVGGDKMIFVEGCKNPKAVTILLRGGTEHVVDEVERALEDALRVVRVVLEDGKVVAGG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 377 GSTEVELSMKLREYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHaSNGNKCAGLNVFTGAVEDMC 456
Cdd:NF041082 405 GAPEVELALRLREYAASVGGREQLAIEAFAEALEIIPRTLAENAGLDPIDALVELRSAH-EKGNKTAGLDVYTGKVVDML 483
|
490 500 510
....*....|....*....|....*....|....
gi 321159767 457 ENGVVEPLRVKTQAIQSAAESTEMLLRIDDVIAA 490
Cdd:NF041082 484 EIGVVEPLRVKTQAIKSATEAAVMILRIDDVIAA 517
|
|
| thermosome_beta |
NF041083 |
thermosome subunit beta; |
1-490 |
0e+00 |
|
thermosome subunit beta;
Pssm-ID: 469010 Cd Length: 519 Bit Score: 773.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 1 VLPENMKRYMGRDAQRMNILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQE 80
Cdd:NF041083 5 ILKEGTQRTKGRDAQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDIVITNDGATILKEMDVQHPAAKMLVEVAKTQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 81 KEVGDGTTTAVVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQDKEILTKIAMTSITGKGAEKA 160
Cdd:NF041083 85 DEVGDGTTTAVVLAGELLKKAEELLDQNIHPTIIANGYRLAAEKAIEILDEIAEKVDPDDRETLKKIAETSLTSKGVEEA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 161 KEKLAEIIVEAVSAVVDDEG---KVDKDLIKIEKKSGASIDDTELIKGVLVDKERVSAQMPKKVTDAKIALLNCAIE--- 234
Cdd:NF041083 165 RDYLAEIAVKAVKQVAEKRDgkyYVDLDNIQIEKKHGGSIEDTQLIYGIVIDKEVVHPGMPKRVENAKIALLDAPLEvkk 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 235 -------------------ETASEMLKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATGA 295
Cdd:NF041083 245 teidaeiritdpdqlqkflDQEEKMLKEMVDKIKATGANVVFCQKGIDDLAQHYLAKAGILAVRRVKKSDMEKLAKATGA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 296 NVITNIKDLSAQDLGDAGLVEERKISGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIVSG 375
Cdd:NF041083 325 RIVTNIDDLTPEDLGYAELVEERKVGDDKMVFVEGCKNPKAVTILIRGGTEHVVDEAERALEDALSVVADAVEDGKIVAG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 376 GGSTEVELSMKLREYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHaSNGNKCAGLNVFTGAVEDM 455
Cdd:NF041083 405 GGAPEVELAKRLREYAATVGGREQLAVEAFAEALEIIPRTLAENAGLDPIDILVKLRSAH-EKGKKWAGINVFTGEVVDM 483
|
490 500 510
....*....|....*....|....*....|....*
gi 321159767 456 CENGVVEPLRVKTQAIQSAAESTEMLLRIDDVIAA 490
Cdd:NF041083 484 WELGVIEPLRVKTQAIKSATEAATMILRIDDVIAA 518
|
|
| cpn60 |
cd03343 |
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ... |
1-490 |
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: 746.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 1 VLPENMKRYMGRDAQRMNILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQE 80
Cdd:cd03343 3 ILKEGTQRTSGRDAQRMNIAAAKAVAEAVRTTLGPKGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAKTQD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 81 KEVGDGTTTAVVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQDKEILTKIAMTSITGKGAEKA 160
Cdd:cd03343 83 EEVGDGTTTAVVLAGELLEKAEDLLDQNIHPTVIIEGYRLAAEKALELLDEIAIKVDPDDKDTLRKIAKTSLTGKGAEAA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 161 KEKLAEIIVEAVSAVVDDEG---KVDKDLIKIEKKSGASIDDTELIKGVLVDKERVSAQMPKKVTDAKIALLNCAIE--- 234
Cdd:cd03343 163 KDKLADLVVDAVLQVAEKRDgkyVVDLDNIKIEKKTGGSVDDTELIRGIVIDKEVVHPGMPKRVENAKIALLDAPLEvkk 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 235 -------------------ETASEMLKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATGA 295
Cdd:cd03343 243 teidakiritspdqlqaflEQEEAMLKEMVDKIADTGANVVFCQKGIDDLAQHYLAKAGILAVRRVKKSDMEKLARATGA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 296 NVITNIKDLSAQDLGDAGLVEERKISGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIVSG 375
Cdd:cd03343 323 KIVTNIDDLTPEDLGEAELVEERKVGDDKMVFVEGCKNPKAVTILLRGGTEHVVDELERALEDALRVVADALEDGKVVAG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 376 GGSTEVELSMKLREYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHAsNGNKCAGLNVFTGAVEDM 455
Cdd:cd03343 403 GGAVEIELAKRLREYARSVGGREQLAVEAFADALEEIPRTLAENAGLDPIDTLVELRAAHE-KGNKNAGLDVYTGEVVDM 481
|
490 500 510
....*....|....*....|....*....|....*
gi 321159767 456 CENGVVEPLRVKTQAIQSAAESTEMLLRIDDVIAA 490
Cdd:cd03343 482 LEKGVIEPLRVKKQAIKSATEAATMILRIDDVIAA 516
|
|
| thermosome_arch |
TIGR02339 |
thermosome, various subunits, archaeal; Thermosome is the name given to the archaeal rather ... |
1-490 |
0e+00 |
|
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: 664.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 1 VLPENMKRYMGRDAQRMNILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQE 80
Cdd:TIGR02339 4 ILKEGTQRTSGRDAQRNNIAAAKAVAEAVKSTLGPRGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAKTQD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 81 KEVGDGTTTAVVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQDKEILTKIAMTSITGKG-AEK 159
Cdd:TIGR02339 84 EEVGDGTTTAVVLAGELLEKAEDLLEQDIHPTVIIEGYRKAAEKALEIIDEIATKISPEDRDLLKKIAYTSLTSKAsAEV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 160 AKEKLAEIIVEAVSAVV----DDEGKVDKDLIKIEKKSGASIDDTELIKGVLVDKERVSAQMPKKVTDAKIALLNCAIEE 235
Cdd:TIGR02339 164 AKDKLADLVVEAVKQVAelrgDGKYYVDLDNIKIVKKKGGSIEDTELVEGIVVDKEVVHPGMPKRVENAKIALLDAPLEV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 236 TASE----------------------MLKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKAT 293
Cdd:TIGR02339 244 EKTEidakiritdpdqikkfldqeeaMLKEMVDKIASAGANVVICQKGIDDVAQHYLAKAGILAVRRVKKSDIEKLARAT 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 294 GANVITNIKDLSAQDLGDAGLVEERKISGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIV 373
Cdd:TIGR02339 324 GARIVSSIDEITESDLGYAELVEERKVGEDKMVFVEGCKNPKAVTILLRGGTEHVVDELERSIQDALHVVANALEDGKIV 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 374 SGGGSTEVELSMKLREYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHAsNGNKCAGLNVFTGAVE 453
Cdd:TIGR02339 404 AGGGAVEIELALRLRSYARSVGGREQLAIEAFADALEEIPRILAENAGLDPIDALVDLRAKHE-KGNKNAGINVFTGEIE 482
|
490 500 510
....*....|....*....|....*....|....*..
gi 321159767 454 DMCENGVVEPLRVKTQAIQSAAESTEMLLRIDDVIAA 490
Cdd:TIGR02339 483 DMLELGVIEPLRVKEQAIKSATEAATMILRIDDVIAA 519
|
|
| chaperonin_type_I_II |
cd00309 |
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ... |
7-489 |
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: 601.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 7 KRYMGRDAQRMNILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQEKEVGDG 86
Cdd:cd00309 2 EREFGEEARLSNINAAKALADAVKTTLGPKGMDKMLVDSLGDPTITNDGATILKEIEVEHPAAKLLVEVAKSQDDEVGDG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 87 TTTAVVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQDKEILTKIAMTSITGKGAEKAKEKLAE 166
Cdd:cd00309 82 TTTVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVPIDVEDREELLKVATTSLNSKLVSGGDDFLGE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 167 IIVEAVSAVVDDEGKVDKDLIKIEKKSGASIDDTELIKGVLVDKERVSAQMPKKVTDAKIALLNCAIEetasemlkdmva 246
Cdd:cd00309 162 LVVDAVLKVGKENGDVDLGVIRVEKKKGGSLEDSELVVGMVFDKGYLSPYMPKRLENAKILLLDCKLE------------ 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 247 eikasgaNVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATGANVITNIKDLSAQDLGDAGLVEERKISGDSMI 326
Cdd:cd00309 230 -------YVVIAEKGIDDEALHYLAKLGIMAVRRVRKEDLERIAKATGATIVSRLEDLTPEDLGTAGLVEETKIGDEKYT 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 327 FVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIVSGGGSTEVELSMKLREYAEGISGREQLAVRAFA 406
Cdd:cd00309 303 FIEGCKGGKVATILLRGATEVELDEAERSLHDALCAVRAAVEDGGIVPGGGAAEIELSKALEELAKTLPGKEQLGIEAFA 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 407 DALEVIPRTLAENAGLDAIEILVKVRAAHAsNGNKCAGLNVFTGAVEDMCENGVVEPLRVKTQAIQSAAESTEMLLRIDD 486
Cdd:cd00309 383 DALEVIPRTLAENAGLDPIEVVTKLRAKHA-EGGGNAGGDVETGEIVDMKEAGIIDPLKVKRQALKSATEAASLILTIDD 461
|
...
gi 321159767 487 VIA 489
Cdd:cd00309 462 IIV 464
|
|
| Cpn60_TCP1 |
pfam00118 |
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ... |
25-490 |
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: 581.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 25 IAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQEKEVGDGTTTAVVVAGELLRKAEEL 104
Cdd:pfam00118 1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELEIQHPAAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEEAEKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 105 LDQNVHPTIVVKGYQAAAQKAQELLKTIAC-EVGAQDKEILTKIAMTSITGKGAEKAKEKLAEIIVEAVSAVVDDEGKVD 183
Cdd:pfam00118 81 LAAGVHPTTIIEGYEKALEKALEILDSIISiPVEDVDREDLLKVARTSLSSKIISRESDFLAKLVVDAVLAIPKNDGSFD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 184 KDLIKIEKKSGASIDDTELIKGVLVDKERVSAQMPKKVTDAKIALLNCAIEETASEM----------------------L 241
Cdd:pfam00118 161 LGNIGVVKILGGSLEDSELVDGVVLDKGPLHPDMPKRLENAKVLLLNCSLEYEKTETkatvvlsdaeqlerflkaeeeqI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 242 KDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATGANVITNIKDLSAQDLGDAGLVEERKIS 321
Cdd:pfam00118 241 LEIVEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMALRRVKKRDLERLAKATGARAVSSLDDLTPDDLGTAGKVEEEKIG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 322 GDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIVSGGGSTEVELSMKLREYAEGISGREQLA 401
Cdd:pfam00118 321 DEKYTFIEGCKSPKAATILLRGATDHVLDEIERSIHDALCVVKNAIEDPRVVPGGGAVEMELARALREYAKSVSGKEQLA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 402 VRAFADALEVIPRTLAENAGLDAIEILVKVRAAHAsNGNKCAGLNVFTGAVEDMCENGVVEPLRVKTQAIQSAAESTEML 481
Cdd:pfam00118 401 IEAFAEALEVIPKTLAENAGLDPIEVLAELRAAHA-SGEKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKSATEAASTI 479
|
....*....
gi 321159767 482 LRIDDVIAA 490
Cdd:pfam00118 480 LRIDDIIKA 488
|
|
| GroEL |
COG0459 |
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ... |
11-490 |
8.30e-179 |
|
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227 Cd Length: 497 Bit Score: 510.78 E-value: 8.30e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 11 GRDAQRMNILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHP----AAKMLIEVAKTQEKEVGDG 86
Cdd:COG0459 8 GEDARRANIRGVKALADAVKVTLGPKGRNVMLVKSFGDPTITNDGVTIAKEIELEDPfenmGAQLVKEVASKTNDEAGDG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 87 TTTAVVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVgaQDKEILTKIAMTSITGkgaekaKEKLAE 166
Cdd:COG0459 88 TTTATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPV--DDKEELAQVATISANG------DEEIGE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 167 IIVEAVSAVVDDegkvdkDLIKIEKKSGASiDDTELIKGVLVDKERVSAQ-------MPKKVTDAKIALLNCAIEetASE 239
Cdd:COG0459 160 LIAEAMEKVGKD------GVITVEEGKGLE-TELEVVEGMQFDKGYLSPYfvtdpekMPAELENAYILLTDKKIS--SIQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 240 MLKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRV-----------KKSDMEKLAKATGANVITN-----IKD 303
Cdd:COG0459 231 DLLPLLEKVAQSGKPLLIIAEDIDGEALATLVVNGIRGVLRVvavkapgfgdrRKAMLEDIAILTGGRVISEdlglkLED 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 304 LSAQDLGDAGLVEERKisgDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGrIVSGGGSTEVEL 383
Cdd:COG0459 311 VTLDDLGRAKRVEVDK---DNTTIVEGAGNPKAIVILVGAATEVEVKERKRRVEDALHATRAAVEEG-IVPGGGAALLRA 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 384 SMKLREYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAhasnGNKCAGLNVFTGAVEDMCENGVVEP 463
Cdd:COG0459 387 ARALRELAAKLEGDEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKVRAA----KDKGFGFDAATGEYVDMLEAGVIDP 462
|
490 500
....*....|....*....|....*..
gi 321159767 464 LRVKTQAIQSAAESTEMLLRIDDVIAA 490
Cdd:COG0459 463 AKVKRSALQNAASVAGLILTTEAVIAD 489
|
|
| TCP1_epsilon |
cd03339 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ... |
4-489 |
5.06e-162 |
|
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: 469.09 E-value: 5.06e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 4 ENMKRYMGRDAQRMNILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQEKEV 83
Cdd:cd03339 14 EKKKRLKGLEAHKSHILAAKSVANILRTSLGPRGMDKILVSPDGEVTVTNDGATILEKMDVDHQIAKLLVELSKSQDDEI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 84 GDGTTTAVVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIA--CEVGAQDKEILTKIAMTSITGKGAEKAK 161
Cdd:cd03339 94 GDGTTGVVVLAGALLEQAEKLLDRGIHPIRIADGYEQACKIAVEHLEEIAdkIEFSPDNKEPLIQTAMTSLGSKIVSRCH 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 162 EKLAEIIVEAVSAVVDDEGK-VDKDLIKIEKKSGASIDDTELIKGVLVDKERVSAQMPKKVTDAKIALLNC--------- 231
Cdd:cd03339 174 RQFAEIAVDAVLSVADLERKdVNFELIKVEGKVGGRLEDTKLVKGIVIDKDFSHPQMPKEVKDAKIAILTCpfeppkpkt 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 232 -------------AIEETASEMLKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATGANVI 298
Cdd:cd03339 254 khklditsvedykKLQEYEQKYFREMVEQVKDAGANLVICQWGFDDEANHLLLQNGLPAVRWVGGVEIELIAIATGGRIV 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 299 TNIKDLSAQDLGDAGLVEERKI--SGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIVSGG 376
Cdd:cd03339 334 PRFEDLSPEKLGKAGLVREISFgtTKDKMLVIEGCPNSKAVTIFIRGGNKMIIEEAKRSLHDALCVVRNLIRDNRIVYGG 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 377 GSTEVELSMKLREYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHASNGNKCAGLNVFTGAVEDMC 456
Cdd:cd03339 414 GAAEISCSLAVEKAADKCSGIEQYAMRAFADALESIPLALAENSGLNPIETLSEVKARQVKEKNPHLGIDCLGRGTNDMK 493
|
490 500 510
....*....|....*....|....*....|...
gi 321159767 457 ENGVVEPLRVKTQAIQSAAESTEMLLRIDDVIA 489
Cdd:cd03339 494 EQKVFETLISKKQQILLATQVVKMILKIDDVIV 526
|
|
| TCP1_gamma |
cd03337 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ... |
1-490 |
1.86e-148 |
|
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: 432.88 E-value: 1.86e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 1 VLPENMKRYMGRDAQRMNILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQE 80
Cdd:cd03337 4 VLNQNTKRESGRKAQLGNIQAAKTVADVIRTCLGPRAMLKMLLDPMGGIVLTNDGNAILREIDVAHPAAKSMIELSRTQD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 81 KEVGDGTTTAVVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQDKEILTKIAMTSITGKGAEKA 160
Cdd:cd03337 84 EEVGDGTTSVIILAGEILAVAEPFLERGIHPTVIIKAYRKALEDALKILEEISIPVDVNDRAQMLKIIKSCIGTKFVSRW 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 161 KEKLAEIIVEAVSAV-VDDEGKVD----KDLIKIEKKSGASIDDTELIKGVLVDKERVSAQMPKKVTDAKIALLNCAIEE 235
Cdd:cd03337 164 SDLMCNLALDAVKTVaVEENGRKKeidiKRYAKVEKIPGGEIEDSRVLDGVMLNKDVTHPKMRRRIENPRIVLLDCPLEY 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 236 tasemlkdmvaeikasganVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATGANVITNIKDLSAQDLGDAGLV 315
Cdd:cd03337 244 -------------------LVITEKGVSDLAQHYLVKAGITALRRVRKTDNNRIARACGATIVNRPEELTESDVGTGAGL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 316 EERKISGDSMI-FVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIVSGGGSTEVELSMKLREYAEGI 394
Cdd:cd03337 305 FEVKKIGDEYFtFITECKDPKACTILLRGASKDVLNEVERNLQDAMAVARNIILNPKLVPGGGATEMAVSHALSEKAKSI 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 395 SGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHASNGNKCAGLNVFTGAVEDMCENGVVEPLRVKTQAIQSA 474
Cdd:cd03337 385 EGVEQWPYKAVASALEVIPRTLAQNCGANVIRTLTELRAKHAQGENSTWGIDGETGDIVDMKELGIWDPLAVKAQTYKTA 464
|
490
....*....|....*.
gi 321159767 475 AESTEMLLRIDDVIAA 490
Cdd:cd03337 465 IEAACMLLRIDDIVSG 480
|
|
| TCP1_delta |
cd03338 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ... |
18-490 |
6.86e-147 |
|
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: 430.17 E-value: 6.86e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 18 NILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQEKEVGDGTTTAVVVAGEL 97
Cdd:cd03338 13 NIQAAKAVADAIRTSLGPRGMDKMIQTGKGEVIITNDGATILKQMSVLHPAAKMLVELSKAQDIEAGDGTTSVVVLAGAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 98 LRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQDKEILTKIAMTSITGKGAEKAKEKLAEIIVEAVSAVVD 177
Cdd:cd03338 93 LSACESLLKKGIHPTVISESFQIAAKKAVEILDSMSIPVDLNDRESLIKSATTSLNSKVVSQYSSLLAPIAVDAVLKVID 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 178 DEGKVDKDL--IKIEKKSGASIDDTELIKGVLVDKERV-SAQMPKKVTDAKIALLNCAIEETASEM-------------- 240
Cdd:cd03338 173 PATATNVDLkdIRIVKKLGGTIEDTELVDGLVFTQKASkKAGGPTRIEKAKIGLIQFCLSPPKTDMdnnivvndyaqmdr 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 241 -LKD-------MVAEIKASGANVLFCQKGI-----DDLAQHYLAKEGIVAARRVKKSDMEKLAKATGANVITNIKDLSAQ 307
Cdd:cd03338 253 iLREerkyilnMCKKIKKSGCNVLLIQKSIlrdavSDLALHFLAKLKIMVVKDIEREEIEFICKTIGCKPVASIDHFTED 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 308 DLGDAGLVEERKISGDSMIFVEECKHP-KAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIVSGGGSTEVELSMK 386
Cdd:cd03338 333 KLGSADLVEEVSLGDGKIVKITGVKNPgKTVTILVRGSNKLVLDEAERSLHDALCVIRCLVKKRALIPGGGAPEIEIALQ 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 387 LREYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHAsNGNKCAGLNVFTGAVEDMCENGVVEPLRV 466
Cdd:cd03338 413 LSEWARTLTGVEQYCVRAFADALEVIPYTLAENAGLNPISIVTELRNRHA-QGEKNAGINVRKGAITNILEENVVQPLLV 491
|
490 500
....*....|....*....|....
gi 321159767 467 KTQAIQSAAESTEMLLRIDDVIAA 490
Cdd:cd03338 492 STSAITLATETVRMILKIDDIVLA 515
|
|
| chap_CCT_epsi |
TIGR02343 |
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ... |
4-491 |
1.60e-146 |
|
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: 429.99 E-value: 1.60e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 4 ENMKRYMGRDAQRMNILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQEKEV 83
Cdd:TIGR02343 18 DNKKRLKGLEAKKSNIAAAKSVASILRTSLGPKGMDKMLISPDGDITVTNDGATILSQMDVDNQIAKLMVELSKSQDDEI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 84 GDGTTTAVVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQD--KEILTKIAMTSITGKGAEKAK 161
Cdd:TIGR02343 98 GDGTTGVVVLAGALLEQAEELLDKGIHPIKIADGFEEAARIAVEHLEEISDEISADNnnREPLIQAAKTSLGSKIVSKCH 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 162 EKLAEIIVEAVSAVVDDEGK-VDKDLIKIEKKSGASIDDTELIKGVLVDKERVSAQMPKKVTDAKIALLNC--------- 231
Cdd:TIGR02343 178 RRFAEIAVDAVLNVADMERRdVDFDLIKVEGKVGGSLEDTKLIKGIIIDKDFSHPQMPKEVEDAKIAILTCpfeppkpkt 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 232 -------------AIEETASEMLKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATGANVI 298
Cdd:TIGR02343 258 khkldissveeykKLQKYEQQKFKEMIDDIKKSGANLVICQWGFDDEANHLLLQNDLPAVRWVGGQELELIAIATGGRIV 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 299 TNIKDLSAQDLGDAGLVEERKI--SGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIVSGG 376
Cdd:TIGR02343 338 PRFQELSKDKLGKAGLVREISFgtTKDRMLVIEQCKNSKAVTIFIRGGNKMIIEEAKRSIHDALCVVRNLIKDSRIVYGG 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 377 GSTEVELSMKLREYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHASNGNKCAGLNVFTGAVEDMC 456
Cdd:TIGR02343 418 GAAEISCSLAVSQEADKYPGVEQYAIRAFADALETIPMALAENSGLDPIGTLSTLKSLQLKEKNPNLGVDCLGYGTNDMK 497
|
490 500 510
....*....|....*....|....*....|....*
gi 321159767 457 ENGVVEPLRVKTQAIQSAAESTEMLLRIDDVIAAE 491
Cdd:TIGR02343 498 EQFVFETLIGKKQQILLATQLVRMILKIDDVISPG 532
|
|
| TCP1_eta |
cd03340 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ... |
18-491 |
3.37e-140 |
|
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: 413.22 E-value: 3.37e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 18 NILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQEKEVGDGTTTAVVVAGEL 97
Cdd:cd03340 21 NINACQAIADAVRTTLGPRGMDKLIVDGRGKVTISNDGATILKLLDIVHPAAKTLVDIAKSQDAEVGDGTTSVVVLAGEF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 98 LRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQDK----EILTKIAMTSITGKGAEKAKEKLAEIIVEAVS 173
Cdd:cd03340 101 LKEAKPFIEDGVHPQIIIRGYRKALQLAIEKIKEIAVNIDKEDKeeqrELLEKCAATALNSKLIASEKEFFAKMVVDAVL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 174 AVVDDegkVDKDLIKIEKKSGASIDDTELIKGVLVDKERVSA---QMPKKVTDAKIALLNCAIE------------ETAS 238
Cdd:cd03340 181 SLDDD---LDLDMIGIKKVPGGSLEDSQLVNGVAFKKTFSYAgfeQQPKKFKNPKILLLNVELElkaekdnaevrvEDPE 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 239 E----------MLKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATGANVITNIKDLSAQD 308
Cdd:cd03340 258 EyqaivdaewkIIYDKLEKIVKSGANVVLSKLPIGDLATQYFADRDIFCAGRVPEEDLKRVAQATGGSIQTTVSNITDDV 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 309 LGDAGLVEERKISGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIVSGGGSTEVELSMKLR 388
Cdd:cd03340 338 LGTCGLFEERQVGGERYNIFTGCPKAKTCTIILRGGAEQFIEEAERSLHDAIMIVRRAIKNDSVVAGGGAIEMELSKYLR 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 389 EYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHASNGNKCAGLNVFTGAVEDMCENGVVEPLRVKT 468
Cdd:cd03340 418 DYSRTIAGKQQLVINAFAKALEIIPRQLCDNAGFDATDILNKLRQKHAQGGGKWYGVDINNEGIADNFEAFVWEPSLVKI 497
|
490 500
....*....|....*....|...
gi 321159767 469 QAIQSAAESTEMLLRIDDVIAAE 491
Cdd:cd03340 498 NALTAATEAACLILSVDETIKNP 520
|
|
| TCP1_alpha |
cd03335 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ... |
7-488 |
1.35e-139 |
|
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: 412.06 E-value: 1.35e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 7 KRYMGRDAQRMNILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQEKEVGDG 86
Cdd:cd03335 2 ERTSGQDVRTQNVTAAMAIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDKEVGDG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 87 TTTAVVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKA-QELLKTIACEVGAQDKEILTKIAMTSITGKGAEKAKEKLA 165
Cdd:cd03335 82 TTSVVIIAAELLKRANELVKQKIHPTTIISGYRLACKEAvKYIKEHLSISVDNLGKESLINVAKTSMSSKIIGADSDFFA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 166 EIIVEAVSAV--VDDEGKVDKDL--IKIEKKSGASIDDTELIKGVLVDKERVSAQMPKKVTDAKIALLNC---------- 231
Cdd:cd03335 162 NMVVDAILAVktTNEKGKTKYPIkaVNILKAHGKSAKESYLVNGYALNCTRASQGMPTRVKNAKIACLDFnlqktkmklg 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 232 ------------AIEETASEMLKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATGANVIT 299
Cdd:cd03335 242 vqvvvtdpekleKIRQRESDITKERIKKILAAGANVVLTTGGIDDMCLKYFVEAGAMAVRRVKKEDLRRIAKATGATLVS 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 300 NIKDL------SAQDLGDAGLVEERKISGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIV 373
Cdd:cd03335 322 TLANLegeetfDPSYLGEAEEVVQERIGDDELILIKGTKKRSSASIILRGANDFMLDEMERSLHDALCVVKRTLESNSVV 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 374 SGGGSTEVELSMKLREYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHAS-------NGNKCAGLN 446
Cdd:cd03335 402 PGGGAVETALSIYLENFATTLGSREQLAIAEFAEALLVIPKTLAVNAAKDATELVAKLRAYHAAaqvkpdkKHLKWYGLD 481
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 321159767 447 VFTGAVEDMCENGVVEPLRVKTQAIQSAAESTEMLLRIDDVI 488
Cdd:cd03335 482 LINGKVRDNLEAGVLEPTVSKIKSLKFATEAAITILRIDDLI 523
|
|
| chap_CCT_gamma |
TIGR02344 |
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ... |
1-489 |
1.57e-137 |
|
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: 406.43 E-value: 1.57e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 1 VLPENMKRYMGRDAQRMNILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQE 80
Cdd:TIGR02344 4 VLNQNTKRESGRKAQLSNIQAAKAVADIIRTCLGPRSMLKMLLDPMGGIVMTNDGNAILREIDVAHPAAKSMIELSRTQD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 81 KEVGDGTTTAVVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQDKEILTKIAMTSITGKGAEKA 160
Cdd:TIGR02344 84 EEVGDGTTSVIILAGEMLSVAEPFLEQNIHPTVIIRAYRKALDDALSVLEEISIPVDVNDDAAMLKLIQSCIGTKFVSRW 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 161 KEKLAEIIVEAVSAVVDDEG---KVD-KDLIKIEKKSGASIDDTELIKGVLVDKERVSAQMPKKVTDAKIALLNCAIE-- 234
Cdd:TIGR02344 164 SDLMCDLALDAVRTVQRDENgrkEIDiKRYAKVEKIPGGDIEDSCVLKGVMINKDVTHPKMRRYIENPRIVLLDCPLEyk 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 235 ----ETASEMLKD----------------MVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATG 294
Cdd:TIGR02344 244 kgesQTNIEITKEedwnrilqmeeeyvqlMCEDIIAVKPDLVITEKGVSDLAQHYLLKANITAIRRVRKTDNNRIARACG 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 295 ANVITNIKDLSAQDLG-DAGLVEERKISGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIV 373
Cdd:TIGR02344 324 ATIVNRPEELRESDVGtGCGLFEVKKIGDEYFTFITECKDPKACTILLRGASKDILNEVERNLQDAMAVARNVLLDPKLV 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 374 SGGGSTEVELSMKLREYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHASNGNKCAGLNVFTGAVE 453
Cdd:TIGR02344 404 PGGGATEMAVSVALTEKSKKLEGVEQWPYRAVADALEIIPRTLAQNCGANVIRTLTELRAKHAQENNCTWGIDGETGKIV 483
|
490 500 510
....*....|....*....|....*....|....*.
gi 321159767 454 DMCENGVVEPLRVKTQAIQSAAESTEMLLRIDDVIA 489
Cdd:TIGR02344 484 DMKEKGIWEPLAVKLQTYKTAIESACLLLRIDDIVS 519
|
|
| chap_CCT_alpha |
TIGR02340 |
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ... |
7-488 |
9.94e-132 |
|
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: 392.16 E-value: 9.94e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 7 KRYMGRDAQRMNILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQEKEVGDG 86
Cdd:TIGR02340 6 ERTSGQDVRTQNVTAAMAIANIVKTSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDREVGDG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 87 TTTAVVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKA-QELLKTIACEVGAQDKEILTKIAMTSITGKGAEKAKEKLA 165
Cdd:TIGR02340 86 TTSVVIIAAELLKRADELVKNKIHPTSVISGYRLACKEAvKYIKENLSVSVDELGREALINVAKTSMSSKIIGLDSDFFS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 166 EIIVEAVSAV--VDDEGKVDKDL--IKIEKKSGASIDDTELIKGVLVDKERVSAQMPKKVTDAKIALLNC---------- 231
Cdd:TIGR02340 166 NIVVDAVLAVktTNENGETKYPIkaINILKAHGKSARESMLVKGYALNCTVASQQMPKRIKNAKIACLDFnlqkakmalg 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 232 ------------AIEETASEMLKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATGANVIT 299
Cdd:TIGR02340 246 vqivvddpekleQIRQREADITKERIKKILDAGANVVLTTGGIDDMCLKYFVEAGAMGVRRCKKEDLKRIAKATGATLVS 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 300 NIKDLSAQD------LGDAGLVEERKISGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIV 373
Cdd:TIGR02340 326 TLADLEGEEtfeasyLGFADEVVQERIADDECILIKGTKKRKSASIILRGANDFMLDEMERSLHDALCVVKRTLESNSVV 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 374 SGGGSTEVELSMKLREYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHAS-------NGNKCAGLN 446
Cdd:TIGR02340 406 PGGGAVEAALSIYLENFATTLGSREQLAIAEFARALLIIPKTLAVNAAKDSTELVAKLRAYHAAaqlkpekKHLKWYGLD 485
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 321159767 447 VFTGAVEDMCENGVVEPLRVKTQAIQSAAESTEMLLRIDDVI 488
Cdd:TIGR02340 486 LVNGKIRDNKEAGVLEPTVSKVKSLKFATEAAITILRIDDLI 527
|
|
| chap_CCT_delta |
TIGR02342 |
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ... |
13-490 |
3.30e-129 |
|
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: 384.91 E-value: 3.30e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 13 DAQRMNILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQEKEVGDGTTTAVV 92
Cdd:TIGR02342 9 DVRTSNIVAAKAVADAIRTSLGPKGMDKMIQDGKGEVIITNDGATILKQMAVLHPAAKMLVELSKAQDIEAGDGTTSVVI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 93 VAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQDKEILTKIAMTSITGKGAEKAKEKLAEIIVEAV 172
Cdd:TIGR02342 89 LAGALLGACERLLNKGIHPTIISESFQSAADEAIKILDEMSIPVDLSDREQLLKSATTSLSSKVVSQYSSLLAPLAVDAV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 173 SAVVDDEGKVDKDL--IKIEKKSGASIDDTELIKGVLVD-KERVSAQMPKKVTDAKIALLNCAIEETASEM--------- 240
Cdd:TIGR02342 169 LKVIDPENAKNVDLndIKVVKKLGGTIDDTELIEGLVFTqKASKSAGGPTRIEKAKIGLIQFQISPPKTDMenqiivndy 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 241 -------------LKDMVAEIKASGANVLFCQKGI-----DDLAQHYLAKEGIVAARRVKKSDMEKLAKATGANVITNIK 302
Cdd:TIGR02342 249 aqmdrvlkeerayILNIVKKIKKTGCNVLLIQKSIlrdavNDLALHFLAKMKIMVVKDIEREEIEFICKTIGCKPIASID 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 303 DLSAQDLGDAGLVEERKISGDSMIFVEECKHP-KAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIVSGGGSTEV 381
Cdd:TIGR02342 329 HFTADKLGSAELVEEVDSDGGKIIKITGIQNAgKTVTVVVRGSNKLVIDEAERSLHDALCVIRCLVKKRGLIAGGGAPEI 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 382 ELSMKLREYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHAsNGNKCAGLNVFTGAVEDMCENGVV 461
Cdd:TIGR02342 409 EIARRLSKYARTMKGVESYCVRAFADALEVIPYTLAENAGLNPIKVVTELRNRHA-NGEKTAGISVRKGGITNMLEEHVL 487
|
490 500
....*....|....*....|....*....
gi 321159767 462 EPLRVKTQAIQSAAESTEMLLRIDDVIAA 490
Cdd:TIGR02342 488 QPLLVTTSAITLASETVRSILKIDDIVFT 516
|
|
| chap_CCT_eta |
TIGR02345 |
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ... |
18-491 |
4.78e-128 |
|
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: 382.18 E-value: 4.78e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 18 NILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQEKEVGDGTTTAVVVAGEL 97
Cdd:TIGR02345 23 NINACVAIAEALKTTLGPRGMDKLIVGSNGKATISNDGATILKLLDIVHPAAKTLVDIAKSQDAEVGDGTTSVTILAGEL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 98 LRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQD---KEILTKIAMTSITGKGAEKAKEKLAEIIVEAVSA 174
Cdd:TIGR02345 103 LKEAKPFIEEGVHPQLIIRCYREALSLAVEKIKEIAVTIDEEKgeqRELLEKCAATALSSKLISHNKEFFSKMIVDAVLS 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 175 VVDDEgkVDKDLIKIEKKSGASIDDTELIKGVLVDKERVSA---QMPKKVTDAKIALLNCAIEETAS------------- 238
Cdd:TIGR02345 183 LDRDD--LDLKLIGIKKVQGGALEDSQLVNGVAFKKTFSYAgfeQQPKKFANPKILLLNVELELKAEkdnaeirvedved 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 239 ---------EMLKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATGANVITNIKDLSAQDL 309
Cdd:TIGR02345 261 yqaivdaewAIIFRKLEKIVESGANVVLSKLPIGDLATQYFADRDIFCAGRVSAEDLKRVIKACGGSIQSTTSDLEADVL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 310 GDAGLVEERKISGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIVSGGGSTEVELSMKLRE 389
Cdd:TIGR02345 341 GTCALFEERQIGSERYNYFTGCPHAKTCTIILRGGAEQFIEEAERSLHDAIMIVRRALKNKKIVAGGGAIEMELSKCLRD 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 390 YAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHAsNGNKCAGLNVFTGAVEDMCENGVVEPLRVKTQ 469
Cdd:TIGR02345 421 YSKTIDGKQQLIINAFAKALEIIPRQLCENAGFDSIEILNKLRSRHA-KGGKWYGVDINTEDIGDNFEAFVWEPALVKIN 499
|
490 500
....*....|....*....|..
gi 321159767 470 AIQSAAESTEMLLRIDDVIAAE 491
Cdd:TIGR02345 500 ALKAAFEAACTILSVDETITNP 521
|
|
| TCP1_zeta |
cd03342 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
14-490 |
4.22e-121 |
|
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: 363.12 E-value: 4.22e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 14 AQRMNILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQEKEVGDGTTTAVVV 93
Cdd:cd03342 13 ALAVNISAAKGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLSEMQIQHPTASMIARAATAQDDITGDGTTSNVLL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 94 AGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVG-AQDKEILTKIAMTSITGKGAEKAKEKLAEIIVEAV 172
Cdd:cd03342 93 IGELLKQAERYIQEGVHPRIITEGFELAKNKALKFLESFKVPVEiDTDRELLLSVARTSLRTKLHADLADQLTEIVVDAV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 173 SAVVDDEGKVDKDLIKIEKKSGASIDDTELIKGVLVDKERVSAQMPKKVTDAKIALLNCAIEETASEmlkdmvaeIKASG 252
Cdd:cd03342 173 LAIYKPDEPIDLHMVEIMQMQHKSDSDTKLIRGLVLDHGARHPDMPKRVENAYILTCNVSLEYEKTE--------VNSGF 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 253 A-NVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATGANVITNIKDLSAQDLGDAGLVEERKISGDSMIFVEEC 331
Cdd:cd03342 245 FySVVINQKGIDPPSLDMLAKEGILALRRAKRRNMERLTLACGGVAMNSVDDLSPECLGYAGLVYERTLGEEKYTFIEGV 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 332 KHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIVSGGGSTEVELSMKLREYAEGISGREQLAVRAFADALEV 411
Cdd:cd03342 325 KNPKSCTILIKGPNDHTITQIKDAIRDGLRAVKNAIEDKCVVPGAGAFEVALYAHLKEFKKSVKGKAKLGVQAFADALLV 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 321159767 412 IPRTLAENAGLDAIEILVKVRAAHASnGNKCAGLNVFTGAVEDMCENGVVEPLRVKTQAIQSAAESTEMLLRIDDVIAA 490
Cdd:cd03342 405 IPKTLAENSGLDVQETLVKLQDEYAE-GGQVGGVDLDTGEPMDPESEGIWDNYSVKRQILHSATVIASQLLLVDEIIRA 482
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
1-490 |
1.70e-120 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 363.19 E-value: 1.70e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 1 VLPENMKRYMGRDAQRMNILAGRIIAETVRSTLGPKGMDKMLV-----DDLGDVVVTNDGVTILREMSVEHPAAKMLIEV 75
Cdd:PTZ00212 10 VLKQGAQEEKGETARLQSFVGAIAVADLVKTTLGPKGMDKILQpmsegPRSGNVTVTNDGATILKSVWLDNPAAKILVDI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 76 AKTQEKEVGDGTTTAVVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQD---KEILTKIAMTSI 152
Cdd:PTZ00212 90 SKTQDEEVGDGTTSVVVLAGELLREAEKLLDQKIHPQTIIEGWRMALDVARKALEEIAFDHGSDEekfKEDLLNIARTTL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 153 TGKGAEKAKEKLAEIiveAVSAVVDDEGKVDKDLIKIEKKSGASIDDTELIKGVLVDKeRVSAQMPKKVTDAKIALLNCA 232
Cdd:PTZ00212 170 SSKLLTVEKDHFAKL---AVDAVLRLKGSGNLDYIQIIKKPGGTLRDSYLEDGFILEK-KIGVGQPKRLENCKILVANTP 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 233 -----------------------IEETASEMLKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKL 289
Cdd:PTZ00212 246 mdtdkikiygakvkvdsmekvaeIEAAEKEKMKNKVDKILAHGCNVFINRQLIYNYPEQLFAEAGIMAIEHADFDGMERL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 290 AKATGANVITNIKDLSAQDLGDAGLVEERKISGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIED 369
Cdd:PTZ00212 326 AAALGAEIVSTFDTPEKVKLGHCDLIEEIMIGEDKLIRFSGCAKGEACTIVLRGASTHILDEAERSLHDALCVLSQTVKD 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 370 GRIVSGGGSTEVELSMKLREYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHAsNGNKCAGLNVFT 449
Cdd:PTZ00212 406 TRVVLGGGCSEMLMANAVEELAKKVEGKKSLAIEAFAKALRQIPTIIADNGGYDSAELVSKLRAEHY-KGNKTAGIDMEK 484
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 321159767 450 GAVEDMCENGVVEPLRVKTQAIQSAAESTEMLLRIDDVIAA 490
Cdd:PTZ00212 485 GTVGDMKELGITESYKVKLSQLCSATEAAEMILRVDDIIRC 525
|
|
| TCP1_theta |
cd03341 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ... |
18-490 |
1.05e-117 |
|
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: 353.83 E-value: 1.05e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 18 NILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQEKEVGDGTTTAVVVAGEL 97
Cdd:cd03341 13 NIEACKELSQITRTSYGPNGMNKMVINHLEKLFVTSDAATILRELEVQHPAAKLLVMASQMQEEEIGDGTNLVVVLAGEL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 98 LRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACE--VGAQDKEILTKIAMTSITGKGAEKAkEKLAEIIVEAVSAV 175
Cdd:cd03341 93 LEKAEELLRMGLHPSEIIEGYEKALKKALEILEELVVYkiEDLRNKEEVSKALKTAIASKQYGNE-DFLSPLVAEACISV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 176 V-DDEGKVDKDLIKIEKKSGASIDDTELIKGVLVDKErVSAQMpKKVTDAKIALLNCAIEEtasemlkdmvaeikasGAN 254
Cdd:cd03341 172 LpENIGNFNVDNIRVVKILGGSLEDSKVVRGMVFKRE-PEGSV-KRVKKAKVAVFSCPFDI----------------GVN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 255 VLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATGANVITNIKDLSAQDLGDAGLVEERKISGDSMIFVEECKHP 334
Cdd:cd03341 234 VIVAGGSVGDLALHYCNKYGIMVIKINSKFELRRLCRTVGATPLPRLGAPTPEEIGYCDSVYVEEIGDTKVVVFRQNKED 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 335 KAV-TMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIVSGGGSTEVELSMKLREYAEGISGREQLAVRAFADALEVIP 413
Cdd:cd03341 314 SKIaTIVLRGATQNILDDVERAIDDGVNVFKSLTKDGRFVPGAGATEIELAKKLKEYGEKTPGLEQYAIKKFAEAFEVVP 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 321159767 414 RTLAENAGLDAIEILVKVRAAHaSNGNKCAGLNVFTG--AVEDMCENGVVEPLRVKTQAIQSAAESTEMLLRIDDVIAA 490
Cdd:cd03341 394 RTLAENAGLDATEVLSELYAAH-QKGNKSAGVDIESGdeGTKDAKEAGIFDHLATKKWAIKLATEAAVTVLRVDQIIMA 471
|
|
| TCP1_beta |
cd03336 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ... |
1-490 |
3.24e-116 |
|
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: 351.63 E-value: 3.24e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 1 VLPENMKRYMGRDAQRMNILAGRIIAETVRSTLGPKGMDKML--VDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKT 78
Cdd:cd03336 1 ILKDGAQEEKGETARLSSFVGAIAIGDLVKTTLGPKGMDKILqsVGRSGGVTVTNDGATILKSIGVDNPAAKVLVDISKV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 79 QEKEVGDGTTTAVVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQD---KEILTKIAMTSITGK 155
Cdd:cd03336 81 QDDEVGDGTTSVTVLAAELLREAEKLVAQKIHPQTIIEGYRMATAAAREALLSSAVDHSSDEeafREDLLNIARTTLSSK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 156 GAEKAKEKLAEIiveAVSAVVDDEGKVDKDLIKIEKKSGASIDDTELIKGVLVDKeRVSAQMPKKVTDAKIALLNCA--- 232
Cdd:cd03336 161 ILTQDKEHFAEL---AVDAVLRLKGSGNLDAIQIIKKLGGSLKDSYLDEGFLLDK-KIGVNQPKRIENAKILIANTPmdt 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 233 --------------------IEETASEMLKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKA 292
Cdd:cd03336 237 dkikifgakvrvdstakvaeIEEAEKEKMKNKVEKILKHGINCFINRQLIYNYPEQLFADAGIMAIEHADFDGVERLALV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 293 TGANVITNIKDLSAQDLGDAGLVEERKISGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRI 372
Cdd:cd03336 317 TGGEIASTFDHPELVKLGTCKLIEEIMIGEDKLIRFSGVAAGEACTIVLRGASQQILDEAERSLHDALCVLAQTVKDTRV 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 373 VSGGGSTEVELSMKLREYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHAsNGNKCAGLNVFTGAV 452
Cdd:cd03336 397 VLGGGCSEMLMAKAVEELAKKTPGKKSLAIEAFAKALRQLPTIIADNAGYDSAELVAQLRAAHY-NGNTTAGLDMRKGTV 475
|
490 500 510
....*....|....*....|....*....|....*...
gi 321159767 453 EDMCENGVVEPLRVKTQAIQSAAESTEMLLRIDDVIAA 490
Cdd:cd03336 476 GDMKELGITESFKVKRQVLLSASEAAEMILRVDDIIKC 513
|
|
| chap_CCT_zeta |
TIGR02347 |
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ... |
14-490 |
4.38e-113 |
|
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: 344.03 E-value: 4.38e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 14 AQRMNILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQEKEVGDGTTTAVVV 93
Cdd:TIGR02347 17 ALMMNINAARGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEMQIQHPTASMIARAATAQDDITGDGTTSTVLL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 94 AGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQ-DKEILTKIAMTSITGKGAEKAKEKLAEIIVEAV 172
Cdd:TIGR02347 97 IGELLKQAERYILEGVHPRIITEGFEIARKEALQFLDKFKVKKEDEvDREFLLNVARTSLRTKLPADLADQLTEIVVDAV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 173 SAVVDDEGKVDKDLIKIEKKSGASIDDTELIKGVLVDKERVSAQMPKKVTDAKIALLNCAIEETASEM------------ 240
Cdd:TIGR02347 177 LAIKKDGEDIDLFMVEIMEMKHKSATDTTLIRGLVLDHGARHPDMPRRVKNAYILTCNVSLEYEKTEVnsgffyssaeqr 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 241 --------------------LKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATGANVITN 300
Cdd:TIGR02347 257 eklvkaerkfvddrvkkiieLKKKVCGKSPDKGFVVINQKGIDPPSLDLLAKEGIMALRRAKRRNMERLTLACGGEALNS 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 301 IKDLSAQDLGDAGLVEERKISGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIVSGGGSTE 380
Cdd:TIGR02347 337 VEDLTPECLGWAGLVYETTIGEEKYTFIEECKNPKSCTILIKGPNDHTIAQIKDAVRDGLRAVKNAIEDKCVVPGAGAFE 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 381 VELSMKLREYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHaSNGNKCAGLNVFTGAVEDMCENGV 460
Cdd:TIGR02347 417 IAAYRHLKEYKKSVKGKAKLGVEAFANALLVIPKTLAENSGFDAQDTLVKLEDEH-DEGGEVVGVDLNTGEPIDPEIKGI 495
|
490 500 510
....*....|....*....|....*....|
gi 321159767 461 VEPLRVKTQAIQSAAESTEMLLRIDDVIAA 490
Cdd:TIGR02347 496 WDNYRVKKQLIQSATVIASQLLLVDEVMRA 525
|
|
| chap_CCT_theta |
TIGR02346 |
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ... |
18-490 |
1.38e-104 |
|
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: 322.44 E-value: 1.38e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 18 NILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQEKEVGDGTTTAVVVAGEL 97
Cdd:TIGR02346 23 NIEACKELSQITRTSLGPNGMNKMVINHLEKLFVTNDAATILRELEVQHPAAKLLVMASEMQENEIGDGTNLVLVLAGEL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 98 LRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKT-IACEV-GAQDKEILTKIAMTSITGKGAEKAkEKLAEIIVEAVSAV 175
Cdd:TIGR02346 103 LNKAEELIRMGLHPSEIIKGYEMALKKAMEILEElVVWEVkDLRDKDELIKALKASISSKQYGNE-DFLAQLVAQACSTV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 176 V-DDEGKVDKDLIKIEKKSGASIDDTELIKGVLVDKERVSAQmpKKVTDAKIALLNCAIEETASE--------------- 239
Cdd:TIGR02346 182 LpKNPQNFNVDNIRVCKILGGSLSNSEVLKGMVFNREAEGSV--KSVKNAKVAVFSCPLDTATTEtkgtvlihnaeelln 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 240 -------MLKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATGANVITNIKDLSAQDLGDA 312
Cdd:TIGR02346 260 yskgeenQIEAMIKAIADSGVNVIVTGGSVGDMALHYLNKYNIMVLKIPSKFELRRLCKTVGATPLPRLGAPTPEEIGYV 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 313 GLVEERKISGDSM-IFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIVSGGGSTEVELSMKLREYA 391
Cdd:TIGR02346 340 DSVYVSEIGGDKVtVFKQENGDSKISTIILRGSTDNLLDDIERAIDDGVNTVKALVKDGRLLPGAGATEIELASRLTKYG 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 392 EGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHASnGNKCAGLNVFTG--AVEDMCENGVVEPLRVKTQ 469
Cdd:TIGR02346 420 EKLPGLDQYAIKKFAEAFEIIPRTLAENAGLNANEVIPKLYAAHKK-GNKSKGIDIEAEsdGVKDASEAGIYDMLATKKW 498
|
490 500
....*....|....*....|.
gi 321159767 470 AIQSAAESTEMLLRIDDVIAA 490
Cdd:TIGR02346 499 AIKLATEAAVTVLRVDQIIMA 519
|
|
| chap_CCT_beta |
TIGR02341 |
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ... |
16-490 |
1.04e-89 |
|
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: 283.29 E-value: 1.04e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 16 RMNILAGRI-IAETVRSTLGPKGMDKMLVDD--LGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQEKEVGDGTTTAVV 92
Cdd:TIGR02341 16 RLSSFVGAIaIGDLVKSTLGPKGMDKILQSSssDASIMVTNDGATILKSIGVDNPAAKVLVDMSKVQDDEVGDGTTSVTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 93 VAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQDKEI---LTKIAMTSITGKGAEKAKEKLAEIiv 169
Cdd:TIGR02341 96 LAAELLREAEKLINQKIHPQTIIAGYREATKAARDALLKSAVDNGSDEVKFrqdLMNIARTTLSSKILSQHKDHFAQL-- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 170 eAVSAVVDDEGKVDKDLIKIEKKSGASIDDTELIKGVLVDKeRVSAQMPKKVTDAKIALLNCA----------------- 232
Cdd:TIGR02341 174 -AVDAVLRLKGSGNLEAIQIIKKLGGSLADSYLDEGFLLDK-KIGVNQPKRIENAKILIANTGmdtdkvkifgsrvrvds 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 233 ------IEETASEMLKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATGANVITNIKDLSA 306
Cdd:TIGR02341 252 takvaeLEHAEKEKMKEKVEKILKHGINCFINRQLIYNYPEQLFADAGVMAIEHADFEGVERLALVTGGEIVSTFDHPEL 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 307 QDLGDAGLVEERKISGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIVSGGGSTEVELSMK 386
Cdd:TIGR02341 332 VKLGSCDLIEEIMIGEDKLLKFSGVKLGEACTIVLRGATQQILDEAERSLHDALCVLSQTVKESRTVLGGGCSEMLMSKA 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 387 LREYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHAsNGNKCAGLNVFTGAVEDMCENGVVEPLRV 466
Cdd:TIGR02341 412 VTQEAQRTPGKEALAVEAFARALRQLPTIIADNAGFDSAELVAQLRAAHY-NGNTTMGLDMNEGTIADMRQLGITESYKV 490
|
490 500
....*....|....*....|....
gi 321159767 467 KTQAIQSAAESTEMLLRIDDVIAA 490
Cdd:TIGR02341 491 KRAVVSSAAEAAEVILRVDNIIKA 514
|
|
| chaperonin_like |
cd03333 |
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ... |
141-369 |
1.69e-75 |
|
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings, each composed of 7-9 subunits. There are 2 main chaperonin groups. The symmetry of type I is seven-fold and they are found in eubacteria (GroEL) and in organelles of eubacterial descent (hsp60 and RBP). The symmetry of type II is eight- or nine-fold and they are found in archea (thermosome), thermophilic bacteria (TF55) and in the eukaryotic cytosol (CTT). Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. This superfamily also contains related domains from Fab1-like phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinases that only contain the intermediate and apical domains.
Pssm-ID: 239449 [Multi-domain] Cd Length: 209 Bit Score: 236.21 E-value: 1.69e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 141 KEILTKIAMTSITGKGaEKAKEKLAEIIVEAVSAVVDDEGKVDKDLIKIEKKSGASIDDTELIKGVLVDKERVSAQMPKK 220
Cdd:cd03333 1 RELLLQVATTSLNSKL-SSWDDFLGKLVVDAVLKVGPDNRMDDLGVIKVEKIPGGSLEDSELVVGVVFDKGYASPYMPKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 221 VTDAKIALLNCAIEetasemlkdmvaeikasgaNVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATGANVITN 300
Cdd:cd03333 80 LENAKILLLDCPLE-------------------YVVIAEKGIDDLALHYLAKAGIMAVRRVKKEDLERIARATGATIVSS 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 321159767 301 IKDLSAQDLGDAGLVEERKISGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIED 369
Cdd:cd03333 141 LEDLTPEDLGTAELVEETKIGEEKLTFIEGCKGGKAATILLRGATEVELDEVKRSLHDALCAVRAAVEE 209
|
|
| GroEL |
cd03344 |
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ... |
16-475 |
1.71e-33 |
|
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: 132.58 E-value: 1.71e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 16 RMNILAG-RIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHP----AAKMLIEVAKTQEKEVGDGTTTA 90
Cdd:cd03344 10 RKALLRGvNKLADAVKVTLGPKGRNVVIEKSFGSPKITKDGVTVAKEIELEDPfenmGAQLVKEVASKTNDVAGDGTTTA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 91 VVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVgaQDKEILTKIAMTSITGkgaekaKEKLAEIIVE 170
Cdd:cd03344 90 TVLARAIIKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKPV--KTKEEIAQVATISANG------DEEIGELIAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 171 AVSavvddegKVDKD-LIKIEkkSGASIDDT-ELIKGVLVDKERVSaqmPKKVTDAkiallncaieetasemlKDMVAEI 248
Cdd:cd03344 162 AME-------KVGKDgVITVE--EGKTLETElEVVEGMQFDRGYLS---PYFVTDP-----------------EKMEVEL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 249 kaSGANVLFCQKGIDDLAQHYLAKEGIVAARR------------------------------VK--------KSDMEKLA 290
Cdd:cd03344 213 --ENPYILLTDKKISSIQELLPILELVAKAGRplliiaedvegealatlvvnklrgglkvcaVKapgfgdrrKAMLEDIA 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 291 KATGANVITN-----IKDLSAQDLGDAGLVEerkISGDSMIFVEECKHPKAV---------------------------- 337
Cdd:cd03344 291 ILTGGTVISEelglkLEDVTLEDLGRAKKVV---VTKDDTTIIGGAGDKAAIkariaqirkqieettsdydkeklqerla 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 338 -----TMLIR--GTTEHVIEEVARAVDDAVGVVGCTIEDGrIVSGGGSTEVELSMKLrEYAEGISGREQLAVRAFADALE 410
Cdd:cd03344 368 klsggVAVIKvgGATEVELKEKKDRVEDALNATRAAVEEG-IVPGGGVALLRASPAL-DKLKALNGDEKLGIEIVRRALE 445
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 321159767 411 VIPRTLAENAGLDAIEILVKVRaahasNGNKCAGLNVFTGAVEDMCENGVVEPLRVKTQAIQSAA 475
Cdd:cd03344 446 APLRQIAENAGVDGSVVVEKVL-----ESPDGFGYDAATGEYVDMIEAGIIDPTKVVRSALQNAA 505
|
|
| groEL |
PRK12849 |
chaperonin GroEL; Reviewed |
12-489 |
2.69e-31 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237230 Cd Length: 542 Bit Score: 126.85 E-value: 2.69e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 12 RDAQRMNILAG-RIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHP----AAKMLIEVAKTQEKEVGDG 86
Cdd:PRK12849 8 DEEARRALERGvNKLADAVKVTLGPKGRNVVIDKSFGAPTITKDGVSIAKEIELEDPfenlGAQLVKEVASKTNDVAGDG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 87 TTTAVVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVgaQDKEILTKIAMTSITGkgaekaKEKLAE 166
Cdd:PRK12849 88 TTTATVLAQALVQEGLKNVAAGANPMDLKRGIDKAVEAVVEELKALARPV--SGSEEIAQVATISANG------DEEIGE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 167 IIVEAVSavvddegKVDKD-LIKIEKKSGASiDDTELIKGVLVDKERVSAQMpkkVTDAkiallncaieETasemlkdMV 245
Cdd:PRK12849 160 LIAEAME-------KVGKDgVITVEESKTLE-TELEVTEGMQFDRGYLSPYF---VTDP----------ER-------ME 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 246 AEIKasGANVLFCQKGIDDLAQ--HYLAK---------------EG------IVAARR-------VK--------KSDME 287
Cdd:PRK12849 212 AVLE--DPLILLTDKKISSLQDllPLLEKvaqsgkplliiaedvEGealatlVVNKLRgglkvaaVKapgfgdrrKAMLE 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 288 KLAKATGANVIT-----NIKDLSAQDLGDAGLVEerkISGDSMIFVEECKHPKAV------------------------- 337
Cdd:PRK12849 290 DIAILTGGTVISedlglKLEEVTLDDLGRAKRVT---ITKDNTTIVDGAGDKEAIearvaqirrqieettsdydreklqe 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 338 --------TMLIR--GTTEHVIEEVARAVDDAVGVVGCTIEDGrIVSGGGSTEVELSMKLREYAeGISGREQLAVRAFAD 407
Cdd:PRK12849 367 rlaklaggVAVIKvgAATEVELKERKDRVEDALNATRAAVEEG-IVPGGGVALLRAAKALDELA-GLNGDQAAGVEIVRR 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 408 ALEVIPRTLAENAGLDAIEILVKVRAahasnGNKCAGLNVFTGAVEDMCENGVVEPLRVKTQAIQSAAESTEMLLRIDDV 487
Cdd:PRK12849 445 ALEAPLRQIAENAGLDGSVVVAKVLE-----LEDGFGFNAATGEYGDLIAAGIIDPVKVTRSALQNAASVAGLLLTTEAL 519
|
..
gi 321159767 488 IA 489
Cdd:PRK12849 520 VA 521
|
|
| GroEL |
TIGR02348 |
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ... |
16-489 |
1.72e-27 |
|
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: 115.47 E-value: 1.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 16 RMNILAG-RIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHP----AAKMLIEVAKTQEKEVGDGTTTA 90
Cdd:TIGR02348 11 RKALLRGvDKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDKfenmGAQLVKEVASKTNDVAGDGTTTA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 91 VVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGaqDKEILTKIAMTSITGkgaekaKEKLAEIIVE 170
Cdd:TIGR02348 91 TVLAQAIVKEGLKNVAAGANPIELKRGIEKAVEAVVEELKKLSKPVK--GKKEIAQVATISANN------DEEIGSLIAE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 171 AVSavvddegKVDKD-LIKIEKKSGAsIDDTELIKGVLVDKERVSaqmPKKVTDAK--IALLNCA---IEETASEMLKDM 244
Cdd:TIGR02348 163 AME-------KVGKDgVITVEESKSL-ETELEVVEGMQFDRGYIS---PYFVTDAEkmEVELENPyilITDKKISNIKDL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 245 V---AEIKASGANVLFCQKGIDDLAQHYLA---KEGIVAARRVK--------KSDMEKLAKATGANVIT-----NIKDLS 305
Cdd:TIGR02348 232 LpllEKVAQSGKPLLIIAEDVEGEALATLVvnkLRGTLNVCAVKapgfgdrrKAMLEDIAILTGGQVISeelglKLEEVT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 306 AQDLGDAGLVeerKISGDSMIFVEECKHPKAVTMLIR-----------------------------------GTTEHVIE 350
Cdd:TIGR02348 312 LDDLGKAKKV---TVDKDNTTIVEGAGDKAAIKARVAqikaqieettsdydreklqerlaklaggvavikvgAATETEMK 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 351 EVARAVDDAVGVVGCTIEDGrIVSGGGSTEVELSMKLrEYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVK 430
Cdd:TIGR02348 389 EKKLRIEDALNATRAAVEEG-IVPGGGVALLRAAAAL-EGLKGDGEDEAIGIDIVKRALEAPLRQIAENAGLDGAVVAEK 466
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 321159767 431 VRaahASNGNKcaGLNVFTGAVEDMCENGVVEPLRVKTQAIQSAAESTEMLLRIDDVIA 489
Cdd:TIGR02348 467 VK---ELKGNF--GFNAATGEYEDLVEAGIIDPTKVTRSALQNAASIAGLLLTTEAVVA 520
|
|
| Fab1_TCP |
cd03334 |
TCP-1 like domain of the eukaryotic phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinase Fab1. ... |
154-363 |
9.33e-25 |
|
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: 103.07 E-value: 9.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 154 GKGAEKAKEKLAEIIVEAVSAVVDDEGKVDKDLI----KIEKKSGASIDDTELIKGVLVDKERVSAQMPKKVTDAKIALL 229
Cdd:cd03334 13 ISNDESWLDILLPLVWKAASNVKPDVRAGDDMDIrqyvKIKKIPGGSPSDSEVVDGVVFTKNVAHKRMPSKIKNPRILLL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 230 NCAIE---------------ETASEMLKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATG 294
Cdd:cd03334 93 QGPLEyqrvenkllsldpviLQEKEYLKNLVSRIVALRPDVILVEKSVSRIAQDLLLEAGITLVLNVKPSVLERISRCTG 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 321159767 295 ANVITNIKDLSA-QDLGDAGLVEERKI-----SGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVV 363
Cdd:cd03334 173 ADIISSMDDLLTsPKLGTCESFRVRTYveehgRSKTLMFFEGCPKELGCTILLRGGDLEELKKVKRVVEFMVFAA 247
|
|
| groEL |
PRK12850 |
chaperonin GroEL; Reviewed |
24-491 |
2.86e-24 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237231 Cd Length: 544 Bit Score: 105.96 E-value: 2.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 24 IIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHP----AAKMLIEVAKTQEKEVGDGTTTAVVVAGELLR 99
Cdd:PRK12850 22 ILANAVKVTLGPKGRNVVLEKSFGAPRITKDGVTVAKEIELEDKfenmGAQMVKEVASKTNDLAGDGTTTATVLAQAIVR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 100 KAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQDKeiLTKIAMTSITGkgaekaKEKLAEIIVEAVSavvdde 179
Cdd:PRK12850 102 EGAKLVAAGMNPMDLKRGIDLAVAAVVDELKKIAKKVTSSKE--IAQVATISANG------DESIGEMIAEAMD------ 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 180 gKVDKD-LIKIEKKSGASiDDTELIKGVLVDKERVSaqmPKKVTDAK--IALLN---CAIEETASEMLKDMVAEIKA--- 250
Cdd:PRK12850 168 -KVGKEgVITVEEAKTLG-TELDVVEGMQFDRGYLS---PYFVTNPEkmRAELEdpyILLHEKKISNLQDLLPILEAvvq 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 251 SGANVLFCQKGIDDLAQHYLAKEGI-----VAARRV------KKSDMEKLAKATGANVI---TNIK--DLSAQDLGDAGL 314
Cdd:PRK12850 243 SGRPLLIIAEDVEGEALATLVVNKLrgglkSVAVKApgfgdrRKAMLEDIAVLTGGQVIsedLGIKleNVTLDMLGRAKR 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 315 VEerkISGDSMIFVEECKHPKAV---------------------------------TMLIR--GTTEHVIEEVARAVDDA 359
Cdd:PRK12850 323 VL---ITKENTTIIDGAGDKKNIearvkqiraqieettsdydreklqerlaklaggVAVIRvgGATEVEVKEKKDRVDDA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 360 VGVVGCTIEDGrIVSGGGSTEVELSMKLREyAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRaahasNG 439
Cdd:PRK12850 400 LHATRAAVEEG-IVPGGGVALLRARSALRG-LKGANADETAGIDIVRRALEEPLRQIATNAGFEGSVVVGKVA-----EL 472
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 321159767 440 NKCAGLNVFTGAVEDMCENGVVEPLRVKTQAIQSAAESTEMLLRIDDVIAAE 491
Cdd:PRK12850 473 PGNFGFNAQTGEYGDMVEAGIIDPAKVTRTALQDAASIAALLITTEAMVAEA 524
|
|
| groEL |
PRK12851 |
chaperonin GroEL; Reviewed |
7-489 |
9.14e-22 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 171770 Cd Length: 541 Bit Score: 98.28 E-value: 9.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 7 KRYMGRDAQRMNILAG-RIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHP----AAKMLIEVAKTQEK 81
Cdd:PRK12851 4 KEVKFHVEAREKMLRGvNILADAVKVTLGPKGRNVVIDKSFGAPTITNDGVTIAKEIELEDKfenmGAQMVREVASKTND 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 82 EVGDGTTTAVVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQDKeiltKIAMTSITGKGaekaK 161
Cdd:PRK12851 84 VAGDGTTTATVLAQAIVREGAKAVAAGANPMDLKRGIDRAVAAVVEELKANARPVTTNAE----IAQVATISANG----D 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 162 EKLAEIIVEAVsavvddeGKVDKDLIKIEKKSGASIDDTELIKGVLVDKERVSA-------QMPKKVTDAKIALLNCAIE 234
Cdd:PRK12851 156 AEIGRLVAEAM-------EKVGNEGVITVEESKTAETELEVVEGMQFDRGYLSPyfvtdadKMEAELEDPYILIHEKKIS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 235 EtasemLKDMVA---EIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRV-----------KKSDMEKLAKATGANVIT- 299
Cdd:PRK12851 229 N-----LQDLLPvleAVVQSGKPLLIIAEDVEGEALATLVVNKLRGGLKVaavkapgfgdrRKAMLEDIAILTGGTVISe 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 300 ----NIKDLSAQDLGDAGLVEERKI-------SGDSMIFVEECKHPKAV-----------------------TMLIR--G 343
Cdd:PRK12851 304 dlgiKLENVTLEQLGRAKKVVVEKEnttiidgAGSKTEIEGRVAQIRAQieettsdydreklqerlaklaggVAVIRvgA 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 344 TTEHVIEEVARAVDDAVGVVGCTIEDGrIVSGGGSTEVELSMKLREyAEGISGREQLAVRAFADALEVIPRTLAENAGLD 423
Cdd:PRK12851 384 STEVEVKEKKDRVDDALHATRAAVEEG-IVPGGGVALLRAVKALDK-LETANGDQRTGVEIVRRALEAPVRQIAENAGAE 461
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 321159767 424 AIEILVKVRaahasNGNKCAGLNVFTGAVEDMCENGVVEPLRVKTQAIQSAAESTEMLLRIDDVIA 489
Cdd:PRK12851 462 GSVVVGKLR-----EKPGGYGFNAATNEYGDLYAQGVIDPVKVVRTALQNAASVAGLLLTTEAMVA 522
|
|
| PTZ00114 |
PTZ00114 |
Heat shock protein 60; Provisional |
16-482 |
1.41e-21 |
|
Heat shock protein 60; Provisional
Pssm-ID: 185455 Cd Length: 555 Bit Score: 97.68 E-value: 1.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 16 RMNILAG-RIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILR--EMS--VEHPAAKMLIEVAKTQEKEVGDGTTTA 90
Cdd:PTZ00114 24 RQSLLKGiERLADAVAVTLGPKGRNVIIEQEYGSPKITKDGVTVAKaiEFSdrFENVGAQLIRQVASKTNDKAGDGTTTA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 91 VVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVgaQDKEILTKIAMTSITGkgaekaKEKLAEIIVE 170
Cdd:PTZ00114 104 TILARAIFREGCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQSRPV--KTKEDILNVATISANG------DVEIGSLIAD 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 171 AVsavvddeGKVDKD-LIKIEkkSGASIDDT-ELIKGVLVDKERVSaqmPKKVTDA---KIALLNCAIEETASEMLKdmV 245
Cdd:PTZ00114 176 AM-------DKVGKDgTITVE--DGKTLEDElEVVEGMSFDRGYIS---PYFVTNEktqKVELENPLILVTDKKISS--I 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 246 AEI-------KASGANVLFCQKGIDDLAQHYLA----KEGI-VAARRV------KKSDMEKLAKATGANVITN------I 301
Cdd:PTZ00114 242 QSIlpilehaVKNKRPLLIIAEDVEGEALQTLIinklRGGLkVCAVKApgfgdnRKDILQDIAVLTGATVVSEdnvglkL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 302 KDLSAQDLGDAGLVEerkISGDSMIFVEECKHPKAV-----------------------------------TMLIRGTTE 346
Cdd:PTZ00114 322 DDFDPSMLGSAKKVT---VTKDETVILTGGGDKAEIkervellrsqierttseydkeklkerlaklsggvaVIKVGGASE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 347 HVIEEVARAVDDAVGVVGCTIEDGrIVSGGGSTEVELSMKLREYAEG--ISGREQLAVRAFADALEVIPRTLAENAGLDA 424
Cdd:PTZ00114 399 VEVNEKKDRIEDALNATRAAVEEG-IVPGGGVALLRASKLLDKLEEDneLTPDQRTGVKIVRNALRLPTKQIAENAGVEG 477
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 321159767 425 IEILVKVraahASNGNKCAGLNVFTGAVEDMCENGVVEPLRVKTQAIQSAAESTEMLL 482
Cdd:PTZ00114 478 AVVVEKI----LEKKDPSFGYDAQTGEYVNMFEAGIIDPTKVVRSALVDAASVASLML 531
|
|
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
11-489 |
1.13e-19 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 91.72 E-value: 1.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 11 GRDAQRmNILAG-RIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHP----AAKMLIEVA-KTQEKeVG 84
Cdd:PRK00013 8 GEDARR-KLLRGvNKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDPfenmGAQLVKEVAsKTNDV-AG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 85 DGTTTAVVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGaqDKEILTKIAmtSITGKGaekaKEKL 164
Cdd:PRK00013 86 DGTTTATVLAQAIVREGLKNVAAGANPMDLKRGIDKAVEAAVEELKKISKPVE--DKEEIAQVA--TISANG----DEEI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 165 AEIIVEAVSavvddegKVDKD-LIKIEKKSGASiDDTELIKGVLVDKERVSAQMpkkVTDAK--IALLNCA---IEETAS 238
Cdd:PRK00013 158 GKLIAEAME-------KVGKEgVITVEESKGFE-TELEVVEGMQFDRGYLSPYF---VTDPEkmEAELENPyilITDKKI 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 239 EMLKDMVA---EIKASGANVLFCQKGIDDLAQHYLAKEGI-----VAA--------RRvkKSDMEKLAKATGANVIT--- 299
Cdd:PRK00013 227 SNIQDLLPvleQVAQSGKPLLIIAEDVEGEALATLVVNKLrgtlkVVAvkapgfgdRR--KAMLEDIAILTGGTVISeel 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 300 --NIKDLSAQDLGDAGLVeerKISGDSMIFVEECKHPKAVT---MLIRGTTEH----------------------VI--- 349
Cdd:PRK00013 305 glKLEDATLEDLGQAKKV---VVTKDNTTIVDGAGDKEAIKarvAQIKAQIEEttsdydreklqerlaklaggvaVIkvg 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 350 --------EEVARaVDDAVGVVGCTIEDGrIVSGGGSTEVELSMKLrEYAEGISGREQLAVRAFADALEVIPRTLAENAG 421
Cdd:PRK00013 382 aatevemkEKKDR-VEDALHATRAAVEEG-IVPGGGVALLRAAPAL-EALKGLNGDEATGINIVLRALEAPLRQIAENAG 458
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 321159767 422 LDAIEILVKVRAAHASNgnkcAGLNVFTGAVEDMCENGVVEPLRVKTQAIQSAAESTEMLLRIDDVIA 489
Cdd:PRK00013 459 LEGSVVVEKVKNGKGKG----YGYNAATGEYVDMIEAGIIDPTKVTRSALQNAASVAGLLLTTEAVVA 522
|
|
| groEL |
CHL00093 |
chaperonin GroEL |
24-482 |
6.82e-19 |
|
chaperonin GroEL
Pssm-ID: 177025 Cd Length: 529 Bit Score: 89.39 E-value: 6.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 24 IIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKM---LIEVAKTQEKEV-GDGTTTAVVVAGELLR 99
Cdd:CHL00093 21 ILAEAVSVTLGPKGRNVVLEKKYGSPQIVNDGVTIAKEIELEDHIENTgvaLIRQAASKTNDVaGDGTTTATVLAYAIVK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 100 KAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVgaQDKEILTKIAMTSiTGKGAEkakekLAEIIVEAVSavvdde 179
Cdd:CHL00093 101 QGMKNVAAGANPISLKRGIEKATQYVVSQIAEYARPV--EDIQAITQVASIS-AGNDEE-----VGSMIADAIE------ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 180 gKVDKD-LIKIEKKSGASIdDTELIKGVLVDKERVSaqmPKKVTDA---KIALLNCAIEETASEM------LKDMVAEIK 249
Cdd:CHL00093 167 -KVGREgVISLEEGKSTVT-ELEITEGMRFEKGFIS---PYFVTDTermEVVQENPYILLTDKKItlvqqdLLPILEQVT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 250 ASGANVLFCQKGIDD--LAQHYLAK-EGI--VAARRV------KKSDMEKLAKATGANVITNIKDLSAQDLGDAGLVEER 318
Cdd:CHL00093 242 KTKRPLLIIAEDVEKeaLATLVLNKlRGIvnVVAVRApgfgdrRKAMLEDIAILTGGQVITEDAGLSLETIQLDLLGQAR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 319 KI--SGDSMIFVEEcKHPKAVTM---------------------------------LIR--GTTEHVIEEVARAVDDAVG 361
Cdd:CHL00093 322 RIivTKDSTTIIAD-GNEEQVKArceqlrkqieiadssyekeklqerlaklsggvaVIKvgAATETEMKDKKLRLEDAIN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 362 VVGCTIEDGrIVSGGGSTEVELSMKLREYAE-GISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRaahasNGN 440
Cdd:CHL00093 401 ATKAAVEEG-IVPGGGATLVHLSENLKTWAKnNLKEDELIGALIVARAILAPLKRIAENAGKNGSVIIEKVQ-----EQD 474
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 321159767 441 KCAGLNVFTGAVEDMCENGVVEPLRVKTQAIQSAAESTEMLL 482
Cdd:CHL00093 475 FEIGYNAANNKFVNMYEAGIIDPAKVTRSALQNAASIASMIL 516
|
|
| groEL |
PRK12852 |
chaperonin GroEL; Reviewed |
24-489 |
3.07e-16 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237232 Cd Length: 545 Bit Score: 81.43 E-value: 3.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 24 IIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSV----EHPAAKMLIEVAKTQEKEVGDGTTTAVVVAGELLR 99
Cdd:PRK12852 22 ILANAVKVTLGPKGRNVVIEKSFGAPRITKDGVTVAKEIELedkfENMGAQMVREVASKTNDLAGDGTTTATVLAQAIVR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 100 KAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQ-------------DKEILTKI--AMTSITGKGAEKAKE-K 163
Cdd:PRK12852 102 EGAKAVAAGMNPMDLKRGIDIAVAAVVKDIEKRAKPVASSaeiaqvgtisangDAAIGKMIaqAMQKVGNEGVITVEEnK 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 164 LAEIIVEAVSAVVDDEGKVDKDLIKIEKKSGASIDDTElikgVLVDKERVS---AQMP--KKVTDAKIALLNCAiEETAS 238
Cdd:PRK12852 182 SLETEVDIVEGMKFDRGYLSPYFVTNAEKMTVELDDAY----ILLHEKKLSglqAMLPvlEAVVQSGKPLLIIA-EDVEG 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 239 EMLKDMV----------AEIKASGAN-----------VLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKlAKATGANV 297
Cdd:PRK12852 257 EALATLVvnrlrgglkvAAVKAPGFGdrrkamlediaILTGGQLISEDLGIKLENVTLKMLGRAKKVVIDK-ENTTIVNG 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 298 ITNIKDLSAQDLGDAGLVEERKISGDSMIFVEECKHPKAVTMLIR--GTTEHVIEEVARAVDDAVGVVGCTIEDGrIVSG 375
Cdd:PRK12852 336 AGKKADIEARVGQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRvgGATEVEVKEKKDRVEDALNATRAAVQEG-IVPG 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 376 GGsteVELsMKLREYAEGISGR---EQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRaahaSNGNKCAGLNVFTGAV 452
Cdd:PRK12852 415 GG---VAL-LRAKKAVGRINNDnadVQAGINIVLKALEAPIRQIAENAGVEGSIVVGKIL----ENKSETFGFDAQTEEY 486
|
490 500 510
....*....|....*....|....*....|....*..
gi 321159767 453 EDMCENGVVEPLRVKTQAIQSAAESTEMLLRIDDVIA 489
Cdd:PRK12852 487 VDMVAKGIIDPAKVVRTALQDAASVAGLLVTTEAMVA 523
|
|
| PLN03167 |
PLN03167 |
Chaperonin-60 beta subunit; Provisional |
25-488 |
7.64e-16 |
|
Chaperonin-60 beta subunit; Provisional
Pssm-ID: 215611 [Multi-domain] Cd Length: 600 Bit Score: 79.97 E-value: 7.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 25 IAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHP----AAKMLIEVAKTQEKEVGDGTTTAVVVAGELLRK 100
Cdd:PLN03167 78 LADLVGVTLGPKGRNVVLESKYGSPKIVNDGVTVAKEVELEDPveniGAKLVRQAAAKTNDLAGDGTTTSVVLAQGLIAE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 101 AEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEV------------GAQDKEILTKI--AMTSITGKGAEKAKE-KLA 165
Cdd:PLN03167 158 GVKVVAAGANPVQITRGIEKTAKALVKELKKMSKEVedseladvaavsAGNNYEVGNMIaeAMSKVGRKGVVTLEEgKSA 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 166 EIIVEAVSAVVDDEGKVDKDLIKIEKKSGASIDDTELIkgvLVDkervsaqmpKKVTDAK--IALLNCAI---------- 233
Cdd:PLN03167 238 ENNLYVVEGMQFDRGYISPYFVTDSEKMSVEYDNCKLL---LVD---------KKITNARdlIGILEDAIrggyplliia 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 234 EETASEMLKDMVA-EIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSD----MEKLAK---ATGANVI------T 299
Cdd:PLN03167 306 EDIEQEALATLVVnKLRGSLKIAALKAPGFGERKSQYLDDIAILTGGTVIREEvglsLDKVGKevlGTAAKVVltkdttT 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 300 NIKDLSAQDlgdagLVEERKISGDSMIFVEECKHPK-------------AVTMLIRGTTEHVIEEVARAVDDAVGVVGCT 366
Cdd:PLN03167 386 IVGDGSTQE-----AVNKRVAQIKNLIEAAEQDYEKeklneriaklsggVAVIQVGAQTETELKEKKLRVEDALNATKAA 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 367 IEDGrIVSGGGSTEVELSMKLREYAEGISGREQ-LAVRAFADALEVIPRTLAENAGLDAIEILVKVraahASNGNKCAGL 445
Cdd:PLN03167 461 VEEG-IVVGGGCTLLRLASKVDAIKDTLENDEQkVGADIVKRALSYPLKLIAKNAGVNGSVVSEKV----LSNDNPKFGY 535
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 321159767 446 NVFTGAVEDMCENGVVEPLRVKTQAIQSAAESTEMLLRIDDVI 488
Cdd:PLN03167 536 NAATGKYEDLMAAGIIDPTKVVRCCLEHAASVAKTFLTSDCVV 578
|
|
| PRK14104 |
PRK14104 |
chaperonin GroEL; Provisional |
11-489 |
2.06e-13 |
|
chaperonin GroEL; Provisional
Pssm-ID: 172594 Cd Length: 546 Bit Score: 72.37 E-value: 2.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 11 GRDAQRMNILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSV----EHPAAKMLIEVAKTQEKEVGDG 86
Cdd:PRK14104 9 GVDARDRMLRGVDILANAVKVTLGPKGRNVVLDKSFGAPRITKDGVTVAKEIELedkfENMGAQMVREVASKSADAAGDG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 87 TTTAVVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELL-----KTIACEVGAQ--------DKEI--LTKIAMTS 151
Cdd:PRK14104 89 TTTATVLAQAIVREGAKSVAAGMNPMDLKRGIDLAVEAVVADLvknskKVTSNDEIAQvgtisangDAEIgkFLADAMKK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 152 ITGKGAEKAKE-KLAEIIVEAVSAVVDDEGKVDKDLIKIEKKSGASIDDTElikgVLVDKERVSA-----QMPKKVTDAK 225
Cdd:PRK14104 169 VGNEGVITVEEaKSLETELDVVEGMQFDRGYISPYFVTNADKMRVEMDDAY----ILINEKKLSSlnellPLLEAVVQTG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 226 IALLNCAiEETASEMLKDM----------VAEIKASGAN-----------VLFCQKGIDDLAQHYLAKEGIVAARRVKKS 284
Cdd:PRK14104 245 KPLVIVA-EDVEGEALATLvvnrlrgglkVAAVKAPGFGdrrkamlqdiaILTGGQAISEDLGIKLENVTLQMLGRAKKV 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 285 DMEKlAKATGANVITNIKDLSAQDLGDAGLVEERKISGDSMIFVEECKHPKAVTMLIR--GTTEHVIEEVARAVDDAVGV 362
Cdd:PRK14104 324 MIDK-ENTTIVNGAGKKADIEARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRvgGATEVEVKERKDRVDDAMHA 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321159767 363 VGCTIEDGrIVSGGGSTEVELSMKLREYAEGiSGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVraahASNGNKC 442
Cdd:PRK14104 403 TRAAVEEG-IVPGGGVALLRASEQLKGIKTK-NDDQKTGVEIVRKALSAPARQIAINAGEDGSVIVGKI----LEKEQYS 476
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 321159767 443 AGLNVFTGAVEDMCENGVVEPLRVKTQAIQSAAESTEMLLRIDDVIA 489
Cdd:PRK14104 477 YGFDSQTGEYGNLVSKGIIDPTKVVRTAIQNAASVAALLITTEAMVA 523
|
|
| |
