|
Name |
Accession |
Description |
Interval |
E-value |
| thermosome_alpha |
NF041082 |
thermosome subunit alpha; |
7-496 |
0e+00 |
|
thermosome subunit alpha;
Pssm-ID: 469009 Cd Length: 518 Bit Score: 799.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 7 VLPENMKRYMGRDAQRMNILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQE 86
Cdd:NF041082 5 ILKEGTQRTSGRDAQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDVVITNDGVTILKEMDIEHPAAKMIVEVAKTQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 87 KEVGDGTTTAVVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQDKEILTKIAMTSITGKGAEKA 166
Cdd:NF041082 85 DEVGDGTTTAVVLAGELLKKAEELLDQDIHPTIIAEGYRLAAEKALEILDEIAIKVDPDDKETLKKIAATAMTGKGAEAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 167 KEKLAEIIVEAVSAVVDDEG--KVDKDLIKIEKKSGASIDDTELIKGVLVDKERVSAQMPKKVTDAKIALLNCAIE---- 240
Cdd:NF041082 165 KDKLADLVVDAVKAVAEKDGgyNVDLDNIKVEKKVGGSIEDSELVEGVVIDKERVHPGMPKRVENAKIALLDAPLEvkkt 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 241 ------------------ETASEMLKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATGAN 302
Cdd:NF041082 245 eidakisitdpdqlqaflDQEEKMLKEMVDKIADSGANVVFCQKGIDDLAQHYLAKEGILAVRRVKKSDMEKLAKATGAR 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 303 VITNIKDLSAQDLGDAGLVEERKISGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIVSGG 382
Cdd:NF041082 325 IVTSIDDLSPEDLGYAGLVEERKVGGDKMIFVEGCKNPKAVTILLRGGTEHVVDEVERALEDALRVVRVVLEDGKVVAGG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 383 GSTEVELSMKLREYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHaSNGNKCAGLNVFTGAVEDMC 462
Cdd:NF041082 405 GAPEVELALRLREYAASVGGREQLAIEAFAEALEIIPRTLAENAGLDPIDALVELRSAH-EKGNKTAGLDVYTGKVVDML 483
|
490 500 510
....*....|....*....|....*....|....
gi 299689058 463 ENGVVEPLRVKTQAIQSAAESTEMLLRIDDVIAA 496
Cdd:NF041082 484 EIGVVEPLRVKTQAIKSATEAAVMILRIDDVIAA 517
|
|
| thermosome_beta |
NF041083 |
thermosome subunit beta; |
7-496 |
0e+00 |
|
thermosome subunit beta;
Pssm-ID: 469010 Cd Length: 519 Bit Score: 776.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 7 VLPENMKRYMGRDAQRMNILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQE 86
Cdd:NF041083 5 ILKEGTQRTKGRDAQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDIVITNDGATILKEMDVQHPAAKMLVEVAKTQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 87 KEVGDGTTTAVVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQDKEILTKIAMTSITGKGAEKA 166
Cdd:NF041083 85 DEVGDGTTTAVVLAGELLKKAEELLDQNIHPTIIANGYRLAAEKAIEILDEIAEKVDPDDRETLKKIAETSLTSKGVEEA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 167 KEKLAEIIVEAVSAVVDDEG---KVDKDLIKIEKKSGASIDDTELIKGVLVDKERVSAQMPKKVTDAKIALLNCAIE--- 240
Cdd:NF041083 165 RDYLAEIAVKAVKQVAEKRDgkyYVDLDNIQIEKKHGGSIEDTQLIYGIVIDKEVVHPGMPKRVENAKIALLDAPLEvkk 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 241 -------------------ETASEMLKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATGA 301
Cdd:NF041083 245 teidaeiritdpdqlqkflDQEEKMLKEMVDKIKATGANVVFCQKGIDDLAQHYLAKAGILAVRRVKKSDMEKLAKATGA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 302 NVITNIKDLSAQDLGDAGLVEERKISGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIVSG 381
Cdd:NF041083 325 RIVTNIDDLTPEDLGYAELVEERKVGDDKMVFVEGCKNPKAVTILIRGGTEHVVDEAERALEDALSVVADAVEDGKIVAG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 382 GGSTEVELSMKLREYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHaSNGNKCAGLNVFTGAVEDM 461
Cdd:NF041083 405 GGAPEVELAKRLREYAATVGGREQLAVEAFAEALEIIPRTLAENAGLDPIDILVKLRSAH-EKGKKWAGINVFTGEVVDM 483
|
490 500 510
....*....|....*....|....*....|....*
gi 299689058 462 CENGVVEPLRVKTQAIQSAAESTEMLLRIDDVIAA 496
Cdd:NF041083 484 WELGVIEPLRVKTQAIKSATEAATMILRIDDVIAA 518
|
|
| cpn60 |
cd03343 |
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ... |
7-496 |
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: 749.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 7 VLPENMKRYMGRDAQRMNILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQE 86
Cdd:cd03343 3 ILKEGTQRTSGRDAQRMNIAAAKAVAEAVRTTLGPKGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAKTQD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 87 KEVGDGTTTAVVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQDKEILTKIAMTSITGKGAEKA 166
Cdd:cd03343 83 EEVGDGTTTAVVLAGELLEKAEDLLDQNIHPTVIIEGYRLAAEKALELLDEIAIKVDPDDKDTLRKIAKTSLTGKGAEAA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 167 KEKLAEIIVEAVSAVVDDEG---KVDKDLIKIEKKSGASIDDTELIKGVLVDKERVSAQMPKKVTDAKIALLNCAIE--- 240
Cdd:cd03343 163 KDKLADLVVDAVLQVAEKRDgkyVVDLDNIKIEKKTGGSVDDTELIRGIVIDKEVVHPGMPKRVENAKIALLDAPLEvkk 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 241 -------------------ETASEMLKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATGA 301
Cdd:cd03343 243 teidakiritspdqlqaflEQEEAMLKEMVDKIADTGANVVFCQKGIDDLAQHYLAKAGILAVRRVKKSDMEKLARATGA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 302 NVITNIKDLSAQDLGDAGLVEERKISGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIVSG 381
Cdd:cd03343 323 KIVTNIDDLTPEDLGEAELVEERKVGDDKMVFVEGCKNPKAVTILLRGGTEHVVDELERALEDALRVVADALEDGKVVAG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 382 GGSTEVELSMKLREYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHAsNGNKCAGLNVFTGAVEDM 461
Cdd:cd03343 403 GGAVEIELAKRLREYARSVGGREQLAVEAFADALEEIPRTLAENAGLDPIDTLVELRAAHE-KGNKNAGLDVYTGEVVDM 481
|
490 500 510
....*....|....*....|....*....|....*
gi 299689058 462 CENGVVEPLRVKTQAIQSAAESTEMLLRIDDVIAA 496
Cdd:cd03343 482 LEKGVIEPLRVKKQAIKSATEAATMILRIDDVIAA 516
|
|
| thermosome_arch |
TIGR02339 |
thermosome, various subunits, archaeal; Thermosome is the name given to the archaeal rather ... |
7-496 |
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: 667.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 7 VLPENMKRYMGRDAQRMNILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQE 86
Cdd:TIGR02339 4 ILKEGTQRTSGRDAQRNNIAAAKAVAEAVKSTLGPRGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAKTQD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 87 KEVGDGTTTAVVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQDKEILTKIAMTSITGKG-AEK 165
Cdd:TIGR02339 84 EEVGDGTTTAVVLAGELLEKAEDLLEQDIHPTVIIEGYRKAAEKALEIIDEIATKISPEDRDLLKKIAYTSLTSKAsAEV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 166 AKEKLAEIIVEAVSAVV----DDEGKVDKDLIKIEKKSGASIDDTELIKGVLVDKERVSAQMPKKVTDAKIALLNCAIEE 241
Cdd:TIGR02339 164 AKDKLADLVVEAVKQVAelrgDGKYYVDLDNIKIVKKKGGSIEDTELVEGIVVDKEVVHPGMPKRVENAKIALLDAPLEV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 242 TASE----------------------MLKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKAT 299
Cdd:TIGR02339 244 EKTEidakiritdpdqikkfldqeeaMLKEMVDKIASAGANVVICQKGIDDVAQHYLAKAGILAVRRVKKSDIEKLARAT 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 300 GANVITNIKDLSAQDLGDAGLVEERKISGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIV 379
Cdd:TIGR02339 324 GARIVSSIDEITESDLGYAELVEERKVGEDKMVFVEGCKNPKAVTILLRGGTEHVVDELERSIQDALHVVANALEDGKIV 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 380 SGGGSTEVELSMKLREYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHAsNGNKCAGLNVFTGAVE 459
Cdd:TIGR02339 404 AGGGAVEIELALRLRSYARSVGGREQLAIEAFADALEEIPRILAENAGLDPIDALVDLRAKHE-KGNKNAGINVFTGEIE 482
|
490 500 510
....*....|....*....|....*....|....*..
gi 299689058 460 DMCENGVVEPLRVKTQAIQSAAESTEMLLRIDDVIAA 496
Cdd:TIGR02339 483 DMLELGVIEPLRVKEQAIKSATEAATMILRIDDVIAA 519
|
|
| chaperonin_type_I_II |
cd00309 |
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ... |
13-495 |
0e+00 |
|
chaperonin families, type I and type II. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings, each composed of 7-9 subunits. There are 2 main chaperonin groups. The symmetry of type I is seven-fold and they are found in eubacteria (GroEL) and in organelles of eubacterial descent (hsp60 and RBP). The symmetry of type II is eight- or nine-fold and they are found in archea (thermosome), thermophilic bacteria (TF55) and in the eukaryotic cytosol (CTT). Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis.
Pssm-ID: 238189 Cd Length: 464 Bit Score: 604.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 13 KRYMGRDAQRMNILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQEKEVGDG 92
Cdd:cd00309 2 EREFGEEARLSNINAAKALADAVKTTLGPKGMDKMLVDSLGDPTITNDGATILKEIEVEHPAAKLLVEVAKSQDDEVGDG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 93 TTTAVVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQDKEILTKIAMTSITGKGAEKAKEKLAE 172
Cdd:cd00309 82 TTTVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVPIDVEDREELLKVATTSLNSKLVSGGDDFLGE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 173 IIVEAVSAVVDDEGKVDKDLIKIEKKSGASIDDTELIKGVLVDKERVSAQMPKKVTDAKIALLNCAIEetasemlkdmva 252
Cdd:cd00309 162 LVVDAVLKVGKENGDVDLGVIRVEKKKGGSLEDSELVVGMVFDKGYLSPYMPKRLENAKILLLDCKLE------------ 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 253 eikasgaNVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATGANVITNIKDLSAQDLGDAGLVEERKISGDSMI 332
Cdd:cd00309 230 -------YVVIAEKGIDDEALHYLAKLGIMAVRRVRKEDLERIAKATGATIVSRLEDLTPEDLGTAGLVEETKIGDEKYT 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 333 FVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIVSGGGSTEVELSMKLREYAEGISGREQLAVRAFA 412
Cdd:cd00309 303 FIEGCKGGKVATILLRGATEVELDEAERSLHDALCAVRAAVEDGGIVPGGGAAEIELSKALEELAKTLPGKEQLGIEAFA 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 413 DALEVIPRTLAENAGLDAIEILVKVRAAHAsNGNKCAGLNVFTGAVEDMCENGVVEPLRVKTQAIQSAAESTEMLLRIDD 492
Cdd:cd00309 383 DALEVIPRTLAENAGLDPIEVVTKLRAKHA-EGGGNAGGDVETGEIVDMKEAGIIDPLKVKRQALKSATEAASLILTIDD 461
|
...
gi 299689058 493 VIA 495
Cdd:cd00309 462 IIV 464
|
|
| Cpn60_TCP1 |
pfam00118 |
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ... |
31-496 |
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: 584.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 31 IAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQEKEVGDGTTTAVVVAGELLRKAEEL 110
Cdd:pfam00118 1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELEIQHPAAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEEAEKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 111 LDQNVHPTIVVKGYQAAAQKAQELLKTIAC-EVGAQDKEILTKIAMTSITGKGAEKAKEKLAEIIVEAVSAVVDDEGKVD 189
Cdd:pfam00118 81 LAAGVHPTTIIEGYEKALEKALEILDSIISiPVEDVDREDLLKVARTSLSSKIISRESDFLAKLVVDAVLAIPKNDGSFD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 190 KDLIKIEKKSGASIDDTELIKGVLVDKERVSAQMPKKVTDAKIALLNCAIEETASEM----------------------L 247
Cdd:pfam00118 161 LGNIGVVKILGGSLEDSELVDGVVLDKGPLHPDMPKRLENAKVLLLNCSLEYEKTETkatvvlsdaeqlerflkaeeeqI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 248 KDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATGANVITNIKDLSAQDLGDAGLVEERKIS 327
Cdd:pfam00118 241 LEIVEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMALRRVKKRDLERLAKATGARAVSSLDDLTPDDLGTAGKVEEEKIG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 328 GDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIVSGGGSTEVELSMKLREYAEGISGREQLA 407
Cdd:pfam00118 321 DEKYTFIEGCKSPKAATILLRGATDHVLDEIERSIHDALCVVKNAIEDPRVVPGGGAVEMELARALREYAKSVSGKEQLA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 408 VRAFADALEVIPRTLAENAGLDAIEILVKVRAAHAsNGNKCAGLNVFTGAVEDMCENGVVEPLRVKTQAIQSAAESTEML 487
Cdd:pfam00118 401 IEAFAEALEVIPKTLAENAGLDPIEVLAELRAAHA-SGEKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKSATEAASTI 479
|
....*....
gi 299689058 488 LRIDDVIAA 496
Cdd:pfam00118 480 LRIDDIIKA 488
|
|
| GroEL |
COG0459 |
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ... |
17-498 |
1.41e-179 |
|
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227 Cd Length: 497 Bit Score: 513.86 E-value: 1.41e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 17 GRDAQRMNILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHP----AAKMLIEVAKTQEKEVGDG 92
Cdd:COG0459 8 GEDARRANIRGVKALADAVKVTLGPKGRNVMLVKSFGDPTITNDGVTIAKEIELEDPfenmGAQLVKEVASKTNDEAGDG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 93 TTTAVVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVgaQDKEILTKIAMTSITGkgaekaKEKLAE 172
Cdd:COG0459 88 TTTATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPV--DDKEELAQVATISANG------DEEIGE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 173 IIVEAVSAVVDDegkvdkDLIKIEKKSGASiDDTELIKGVLVDKERVSAQ-------MPKKVTDAKIALLNCAIEetASE 245
Cdd:COG0459 160 LIAEAMEKVGKD------GVITVEEGKGLE-TELEVVEGMQFDKGYLSPYfvtdpekMPAELENAYILLTDKKIS--SIQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 246 MLKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRV-----------KKSDMEKLAKATGANVITN-----IKD 309
Cdd:COG0459 231 DLLPLLEKVAQSGKPLLIIAEDIDGEALATLVVNGIRGVLRVvavkapgfgdrRKAMLEDIAILTGGRVISEdlglkLED 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 310 LSAQDLGDAGLVEERKisgDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGrIVSGGGSTEVEL 389
Cdd:COG0459 311 VTLDDLGRAKRVEVDK---DNTTIVEGAGNPKAIVILVGAATEVEVKERKRRVEDALHATRAAVEEG-IVPGGGAALLRA 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 390 SMKLREYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAhasnGNKCAGLNVFTGAVEDMCENGVVEP 469
Cdd:COG0459 387 ARALRELAAKLEGDEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKVRAA----KDKGFGFDAATGEYVDMLEAGVIDP 462
|
490 500
....*....|....*....|....*....
gi 299689058 470 LRVKTQAIQSAAESTEMLLRIDDVIAAEK 498
Cdd:COG0459 463 AKVKRSALQNAASVAGLILTTEAVIADKP 491
|
|
| TCP1_epsilon |
cd03339 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ... |
10-495 |
6.28e-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: 470.24 E-value: 6.28e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 10 ENMKRYMGRDAQRMNILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQEKEV 89
Cdd:cd03339 14 EKKKRLKGLEAHKSHILAAKSVANILRTSLGPRGMDKILVSPDGEVTVTNDGATILEKMDVDHQIAKLLVELSKSQDDEI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 90 GDGTTTAVVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIA--CEVGAQDKEILTKIAMTSITGKGAEKAK 167
Cdd:cd03339 94 GDGTTGVVVLAGALLEQAEKLLDRGIHPIRIADGYEQACKIAVEHLEEIAdkIEFSPDNKEPLIQTAMTSLGSKIVSRCH 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 168 EKLAEIIVEAVSAVVDDEGK-VDKDLIKIEKKSGASIDDTELIKGVLVDKERVSAQMPKKVTDAKIALLNC--------- 237
Cdd:cd03339 174 RQFAEIAVDAVLSVADLERKdVNFELIKVEGKVGGRLEDTKLVKGIVIDKDFSHPQMPKEVKDAKIAILTCpfeppkpkt 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 238 -------------AIEETASEMLKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATGANVI 304
Cdd:cd03339 254 khklditsvedykKLQEYEQKYFREMVEQVKDAGANLVICQWGFDDEANHLLLQNGLPAVRWVGGVEIELIAIATGGRIV 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 305 TNIKDLSAQDLGDAGLVEERKI--SGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIVSGG 382
Cdd:cd03339 334 PRFEDLSPEKLGKAGLVREISFgtTKDKMLVIEGCPNSKAVTIFIRGGNKMIIEEAKRSLHDALCVVRNLIRDNRIVYGG 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 383 GSTEVELSMKLREYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHASNGNKCAGLNVFTGAVEDMC 462
Cdd:cd03339 414 GAAEISCSLAVEKAADKCSGIEQYAMRAFADALESIPLALAENSGLNPIETLSEVKARQVKEKNPHLGIDCLGRGTNDMK 493
|
490 500 510
....*....|....*....|....*....|...
gi 299689058 463 ENGVVEPLRVKTQAIQSAAESTEMLLRIDDVIA 495
Cdd:cd03339 494 EQKVFETLISKKQQILLATQVVKMILKIDDVIV 526
|
|
| TCP1_gamma |
cd03337 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ... |
7-496 |
1.79e-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: 434.03 E-value: 1.79e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 7 VLPENMKRYMGRDAQRMNILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQE 86
Cdd:cd03337 4 VLNQNTKRESGRKAQLGNIQAAKTVADVIRTCLGPRAMLKMLLDPMGGIVLTNDGNAILREIDVAHPAAKSMIELSRTQD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 87 KEVGDGTTTAVVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQDKEILTKIAMTSITGKGAEKA 166
Cdd:cd03337 84 EEVGDGTTSVIILAGEILAVAEPFLERGIHPTVIIKAYRKALEDALKILEEISIPVDVNDRAQMLKIIKSCIGTKFVSRW 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 167 KEKLAEIIVEAVSAV-VDDEGKVD----KDLIKIEKKSGASIDDTELIKGVLVDKERVSAQMPKKVTDAKIALLNCAIEE 241
Cdd:cd03337 164 SDLMCNLALDAVKTVaVEENGRKKeidiKRYAKVEKIPGGEIEDSRVLDGVMLNKDVTHPKMRRRIENPRIVLLDCPLEY 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 242 tasemlkdmvaeikasganVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATGANVITNIKDLSAQDLGDAGLV 321
Cdd:cd03337 244 -------------------LVITEKGVSDLAQHYLVKAGITALRRVRKTDNNRIARACGATIVNRPEELTESDVGTGAGL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 322 EERKISGDSMI-FVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIVSGGGSTEVELSMKLREYAEGI 400
Cdd:cd03337 305 FEVKKIGDEYFtFITECKDPKACTILLRGASKDVLNEVERNLQDAMAVARNIILNPKLVPGGGATEMAVSHALSEKAKSI 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 401 SGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHASNGNKCAGLNVFTGAVEDMCENGVVEPLRVKTQAIQSA 480
Cdd:cd03337 385 EGVEQWPYKAVASALEVIPRTLAQNCGANVIRTLTELRAKHAQGENSTWGIDGETGDIVDMKELGIWDPLAVKAQTYKTA 464
|
490
....*....|....*.
gi 299689058 481 AESTEMLLRIDDVIAA 496
Cdd:cd03337 465 IEAACMLLRIDDIVSG 480
|
|
| TCP1_delta |
cd03338 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ... |
24-496 |
4.28e-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: 431.71 E-value: 4.28e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 24 NILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQEKEVGDGTTTAVVVAGEL 103
Cdd:cd03338 13 NIQAAKAVADAIRTSLGPRGMDKMIQTGKGEVIITNDGATILKQMSVLHPAAKMLVELSKAQDIEAGDGTTSVVVLAGAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 104 LRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQDKEILTKIAMTSITGKGAEKAKEKLAEIIVEAVSAVVD 183
Cdd:cd03338 93 LSACESLLKKGIHPTVISESFQIAAKKAVEILDSMSIPVDLNDRESLIKSATTSLNSKVVSQYSSLLAPIAVDAVLKVID 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 184 DEGKVDKDL--IKIEKKSGASIDDTELIKGVLVDKERV-SAQMPKKVTDAKIALLNCAIEETASEM-------------- 246
Cdd:cd03338 173 PATATNVDLkdIRIVKKLGGTIEDTELVDGLVFTQKASkKAGGPTRIEKAKIGLIQFCLSPPKTDMdnnivvndyaqmdr 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 247 -LKD-------MVAEIKASGANVLFCQKGI-----DDLAQHYLAKEGIVAARRVKKSDMEKLAKATGANVITNIKDLSAQ 313
Cdd:cd03338 253 iLREerkyilnMCKKIKKSGCNVLLIQKSIlrdavSDLALHFLAKLKIMVVKDIEREEIEFICKTIGCKPVASIDHFTED 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 314 DLGDAGLVEERKISGDSMIFVEECKHP-KAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIVSGGGSTEVELSMK 392
Cdd:cd03338 333 KLGSADLVEEVSLGDGKIVKITGVKNPgKTVTILVRGSNKLVLDEAERSLHDALCVIRCLVKKRALIPGGGAPEIEIALQ 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 393 LREYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHAsNGNKCAGLNVFTGAVEDMCENGVVEPLRV 472
Cdd:cd03338 413 LSEWARTLTGVEQYCVRAFADALEVIPYTLAENAGLNPISIVTELRNRHA-QGEKNAGINVRKGAITNILEENVVQPLLV 491
|
490 500
....*....|....*....|....
gi 299689058 473 KTQAIQSAAESTEMLLRIDDVIAA 496
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 ... |
10-497 |
3.41e-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: 430.38 E-value: 3.41e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 10 ENMKRYMGRDAQRMNILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQEKEV 89
Cdd:TIGR02343 18 DNKKRLKGLEAKKSNIAAAKSVASILRTSLGPKGMDKMLISPDGDITVTNDGATILSQMDVDNQIAKLMVELSKSQDDEI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 90 GDGTTTAVVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQD--KEILTKIAMTSITGKGAEKAK 167
Cdd:TIGR02343 98 GDGTTGVVVLAGALLEQAEELLDKGIHPIKIADGFEEAARIAVEHLEEISDEISADNnnREPLIQAAKTSLGSKIVSKCH 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 168 EKLAEIIVEAVSAVVDDEGK-VDKDLIKIEKKSGASIDDTELIKGVLVDKERVSAQMPKKVTDAKIALLNC--------- 237
Cdd:TIGR02343 178 RRFAEIAVDAVLNVADMERRdVDFDLIKVEGKVGGSLEDTKLIKGIIIDKDFSHPQMPKEVEDAKIAILTCpfeppkpkt 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 238 -------------AIEETASEMLKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATGANVI 304
Cdd:TIGR02343 258 khkldissveeykKLQKYEQQKFKEMIDDIKKSGANLVICQWGFDDEANHLLLQNDLPAVRWVGGQELELIAIATGGRIV 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 305 TNIKDLSAQDLGDAGLVEERKI--SGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIVSGG 382
Cdd:TIGR02343 338 PRFQELSKDKLGKAGLVREISFgtTKDRMLVIEQCKNSKAVTIFIRGGNKMIIEEAKRSIHDALCVVRNLIKDSRIVYGG 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 383 GSTEVELSMKLREYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHASNGNKCAGLNVFTGAVEDMC 462
Cdd:TIGR02343 418 GAAEISCSLAVSQEADKYPGVEQYAIRAFADALETIPMALAENSGLDPIGTLSTLKSLQLKEKNPNLGVDCLGYGTNDMK 497
|
490 500 510
....*....|....*....|....*....|....*
gi 299689058 463 ENGVVEPLRVKTQAIQSAAESTEMLLRIDDVIAAE 497
Cdd:TIGR02343 498 EQFVFETLIGKKQQILLATQLVRMILKIDDVISPG 532
|
|
| TCP1_eta |
cd03340 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ... |
24-498 |
1.17e-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: 415.53 E-value: 1.17e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 24 NILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQEKEVGDGTTTAVVVAGEL 103
Cdd:cd03340 21 NINACQAIADAVRTTLGPRGMDKLIVDGRGKVTISNDGATILKLLDIVHPAAKTLVDIAKSQDAEVGDGTTSVVVLAGEF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 104 LRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQDK----EILTKIAMTSITGKGAEKAKEKLAEIIVEAVS 179
Cdd:cd03340 101 LKEAKPFIEDGVHPQIIIRGYRKALQLAIEKIKEIAVNIDKEDKeeqrELLEKCAATALNSKLIASEKEFFAKMVVDAVL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 180 AVVDDegkVDKDLIKIEKKSGASIDDTELIKGVLVDKERVSA---QMPKKVTDAKIALLNCAIE------------ETAS 244
Cdd:cd03340 181 SLDDD---LDLDMIGIKKVPGGSLEDSQLVNGVAFKKTFSYAgfeQQPKKFKNPKILLLNVELElkaekdnaevrvEDPE 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 245 E----------MLKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATGANVITNIKDLSAQD 314
Cdd:cd03340 258 EyqaivdaewkIIYDKLEKIVKSGANVVLSKLPIGDLATQYFADRDIFCAGRVPEEDLKRVAQATGGSIQTTVSNITDDV 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 315 LGDAGLVEERKISGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIVSGGGSTEVELSMKLR 394
Cdd:cd03340 338 LGTCGLFEERQVGGERYNIFTGCPKAKTCTIILRGGAEQFIEEAERSLHDAIMIVRRAIKNDSVVAGGGAIEMELSKYLR 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 395 EYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHASNGNKCAGLNVFTGAVEDMCENGVVEPLRVKT 474
Cdd:cd03340 418 DYSRTIAGKQQLVINAFAKALEIIPRQLCDNAGFDATDILNKLRQKHAQGGGKWYGVDINNEGIADNFEAFVWEPSLVKI 497
|
490 500
....*....|....*....|....
gi 299689058 475 QAIQSAAESTEMLLRIDDVIAAEK 498
Cdd:cd03340 498 NALTAATEAACLILSVDETIKNPK 521
|
|
| TCP1_alpha |
cd03335 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ... |
13-494 |
1.33e-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: 413.22 E-value: 1.33e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 13 KRYMGRDAQRMNILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQEKEVGDG 92
Cdd:cd03335 2 ERTSGQDVRTQNVTAAMAIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDKEVGDG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 93 TTTAVVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKA-QELLKTIACEVGAQDKEILTKIAMTSITGKGAEKAKEKLA 171
Cdd:cd03335 82 TTSVVIIAAELLKRANELVKQKIHPTTIISGYRLACKEAvKYIKEHLSISVDNLGKESLINVAKTSMSSKIIGADSDFFA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 172 EIIVEAVSAV--VDDEGKVDKDL--IKIEKKSGASIDDTELIKGVLVDKERVSAQMPKKVTDAKIALLNC---------- 237
Cdd:cd03335 162 NMVVDAILAVktTNEKGKTKYPIkaVNILKAHGKSAKESYLVNGYALNCTRASQGMPTRVKNAKIACLDFnlqktkmklg 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 238 ------------AIEETASEMLKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATGANVIT 305
Cdd:cd03335 242 vqvvvtdpekleKIRQRESDITKERIKKILAAGANVVLTTGGIDDMCLKYFVEAGAMAVRRVKKEDLRRIAKATGATLVS 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 306 NIKDL------SAQDLGDAGLVEERKISGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIV 379
Cdd:cd03335 322 TLANLegeetfDPSYLGEAEEVVQERIGDDELILIKGTKKRSSASIILRGANDFMLDEMERSLHDALCVVKRTLESNSVV 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 380 SGGGSTEVELSMKLREYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHAS-------NGNKCAGLN 452
Cdd:cd03335 402 PGGGAVETALSIYLENFATTLGSREQLAIAEFAEALLVIPKTLAVNAAKDATELVAKLRAYHAAaqvkpdkKHLKWYGLD 481
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 299689058 453 VFTGAVEDMCENGVVEPLRVKTQAIQSAAESTEMLLRIDDVI 494
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 ... |
7-498 |
7.47e-138 |
|
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: 408.74 E-value: 7.47e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 7 VLPENMKRYMGRDAQRMNILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQE 86
Cdd:TIGR02344 4 VLNQNTKRESGRKAQLSNIQAAKAVADIIRTCLGPRSMLKMLLDPMGGIVMTNDGNAILREIDVAHPAAKSMIELSRTQD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 87 KEVGDGTTTAVVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQDKEILTKIAMTSITGKGAEKA 166
Cdd:TIGR02344 84 EEVGDGTTSVIILAGEMLSVAEPFLEQNIHPTVIIRAYRKALDDALSVLEEISIPVDVNDDAAMLKLIQSCIGTKFVSRW 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 167 KEKLAEIIVEAVSAVVDDEG---KVD-KDLIKIEKKSGASIDDTELIKGVLVDKERVSAQMPKKVTDAKIALLNCAIE-- 240
Cdd:TIGR02344 164 SDLMCDLALDAVRTVQRDENgrkEIDiKRYAKVEKIPGGDIEDSCVLKGVMINKDVTHPKMRRYIENPRIVLLDCPLEyk 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 241 ----ETASEMLKD----------------MVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATG 300
Cdd:TIGR02344 244 kgesQTNIEITKEedwnrilqmeeeyvqlMCEDIIAVKPDLVITEKGVSDLAQHYLLKANITAIRRVRKTDNNRIARACG 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 301 ANVITNIKDLSAQDLG-DAGLVEERKISGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIV 379
Cdd:TIGR02344 324 ATIVNRPEELRESDVGtGCGLFEVKKIGDEYFTFITECKDPKACTILLRGASKDILNEVERNLQDAMAVARNVLLDPKLV 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 380 SGGGSTEVELSMKLREYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHASNGNKCAGLNVFTGAVE 459
Cdd:TIGR02344 404 PGGGATEMAVSVALTEKSKKLEGVEQWPYRAVADALEIIPRTLAQNCGANVIRTLTELRAKHAQENNCTWGIDGETGKIV 483
|
490 500 510
....*....|....*....|....*....|....*....
gi 299689058 460 DMCENGVVEPLRVKTQAIQSAAESTEMLLRIDDVIAAEK 498
Cdd:TIGR02344 484 DMKEKGIWEPLAVKLQTYKTAIESACLLLRIDDIVSGVK 522
|
|
| chap_CCT_alpha |
TIGR02340 |
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ... |
13-494 |
9.23e-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: 393.32 E-value: 9.23e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 13 KRYMGRDAQRMNILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQEKEVGDG 92
Cdd:TIGR02340 6 ERTSGQDVRTQNVTAAMAIANIVKTSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDREVGDG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 93 TTTAVVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKA-QELLKTIACEVGAQDKEILTKIAMTSITGKGAEKAKEKLA 171
Cdd:TIGR02340 86 TTSVVIIAAELLKRADELVKNKIHPTSVISGYRLACKEAvKYIKENLSVSVDELGREALINVAKTSMSSKIIGLDSDFFS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 172 EIIVEAVSAV--VDDEGKVDKDL--IKIEKKSGASIDDTELIKGVLVDKERVSAQMPKKVTDAKIALLNC---------- 237
Cdd:TIGR02340 166 NIVVDAVLAVktTNENGETKYPIkaINILKAHGKSARESMLVKGYALNCTVASQQMPKRIKNAKIACLDFnlqkakmalg 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 238 ------------AIEETASEMLKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATGANVIT 305
Cdd:TIGR02340 246 vqivvddpekleQIRQREADITKERIKKILDAGANVVLTTGGIDDMCLKYFVEAGAMGVRRCKKEDLKRIAKATGATLVS 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 306 NIKDLSAQD------LGDAGLVEERKISGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIV 379
Cdd:TIGR02340 326 TLADLEGEEtfeasyLGFADEVVQERIADDECILIKGTKKRKSASIILRGANDFMLDEMERSLHDALCVVKRTLESNSVV 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 380 SGGGSTEVELSMKLREYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHAS-------NGNKCAGLN 452
Cdd:TIGR02340 406 PGGGAVEAALSIYLENFATTLGSREQLAIAEFARALLIIPKTLAVNAAKDSTELVAKLRAYHAAaqlkpekKHLKWYGLD 485
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 299689058 453 VFTGAVEDMCENGVVEPLRVKTQAIQSAAESTEMLLRIDDVI 494
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 ... |
19-496 |
3.71e-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: 386.06 E-value: 3.71e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 19 DAQRMNILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQEKEVGDGTTTAVV 98
Cdd:TIGR02342 9 DVRTSNIVAAKAVADAIRTSLGPKGMDKMIQDGKGEVIITNDGATILKQMAVLHPAAKMLVELSKAQDIEAGDGTTSVVI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 99 VAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQDKEILTKIAMTSITGKGAEKAKEKLAEIIVEAV 178
Cdd:TIGR02342 89 LAGALLGACERLLNKGIHPTIISESFQSAADEAIKILDEMSIPVDLSDREQLLKSATTSLSSKVVSQYSSLLAPLAVDAV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 179 SAVVDDEGKVDKDL--IKIEKKSGASIDDTELIKGVLVD-KERVSAQMPKKVTDAKIALLNCAIEETASEM--------- 246
Cdd:TIGR02342 169 LKVIDPENAKNVDLndIKVVKKLGGTIDDTELIEGLVFTqKASKSAGGPTRIEKAKIGLIQFQISPPKTDMenqiivndy 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 247 -------------LKDMVAEIKASGANVLFCQKGI-----DDLAQHYLAKEGIVAARRVKKSDMEKLAKATGANVITNIK 308
Cdd:TIGR02342 249 aqmdrvlkeerayILNIVKKIKKTGCNVLLIQKSIlrdavNDLALHFLAKMKIMVVKDIEREEIEFICKTIGCKPIASID 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 309 DLSAQDLGDAGLVEERKISGDSMIFVEECKHP-KAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIVSGGGSTEV 387
Cdd:TIGR02342 329 HFTADKLGSAELVEEVDSDGGKIIKITGIQNAgKTVTVVVRGSNKLVIDEAERSLHDALCVIRCLVKKRGLIAGGGAPEI 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 388 ELSMKLREYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHAsNGNKCAGLNVFTGAVEDMCENGVV 467
Cdd:TIGR02342 409 EIARRLSKYARTMKGVESYCVRAFADALEVIPYTLAENAGLNPIKVVTELRNRHA-NGEKTAGISVRKGGITNMLEEHVL 487
|
490 500
....*....|....*....|....*....
gi 299689058 468 EPLRVKTQAIQSAAESTEMLLRIDDVIAA 496
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 ... |
24-498 |
2.11e-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: 384.50 E-value: 2.11e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 24 NILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQEKEVGDGTTTAVVVAGEL 103
Cdd:TIGR02345 23 NINACVAIAEALKTTLGPRGMDKLIVGSNGKATISNDGATILKLLDIVHPAAKTLVDIAKSQDAEVGDGTTSVTILAGEL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 104 LRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQD---KEILTKIAMTSITGKGAEKAKEKLAEIIVEAVSA 180
Cdd:TIGR02345 103 LKEAKPFIEEGVHPQLIIRCYREALSLAVEKIKEIAVTIDEEKgeqRELLEKCAATALSSKLISHNKEFFSKMIVDAVLS 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 181 VVDDEgkVDKDLIKIEKKSGASIDDTELIKGVLVDKERVSA---QMPKKVTDAKIALLNCAIEETAS------------- 244
Cdd:TIGR02345 183 LDRDD--LDLKLIGIKKVQGGALEDSQLVNGVAFKKTFSYAgfeQQPKKFANPKILLLNVELELKAEkdnaeirvedved 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 245 ---------EMLKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATGANVITNIKDLSAQDL 315
Cdd:TIGR02345 261 yqaivdaewAIIFRKLEKIVESGANVVLSKLPIGDLATQYFADRDIFCAGRVSAEDLKRVIKACGGSIQSTTSDLEADVL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 316 GDAGLVEERKISGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIVSGGGSTEVELSMKLRE 395
Cdd:TIGR02345 341 GTCALFEERQIGSERYNYFTGCPHAKTCTIILRGGAEQFIEEAERSLHDAIMIVRRALKNKKIVAGGGAIEMELSKCLRD 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 396 YAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHAsNGNKCAGLNVFTGAVEDMCENGVVEPLRVKTQ 475
Cdd:TIGR02345 421 YSKTIDGKQQLIINAFAKALEIIPRQLCENAGFDSIEILNKLRSRHA-KGGKWYGVDINTEDIGDNFEAFVWEPALVKIN 499
|
490 500
....*....|....*....|...
gi 299689058 476 AIQSAAESTEMLLRIDDVIAAEK 498
Cdd:TIGR02345 500 ALKAAFEAACTILSVDETITNPK 522
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
1-496 |
1.15e-121 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 367.43 E-value: 1.15e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 1 MSQQPGVLPENMKRYMGRDAQRMNILAGRIIAETVRSTLGPKGMDKMLV-----DDLGDVVVTNDGVTILREMSVEHPAA 75
Cdd:PTZ00212 4 ANVPPQVLKQGAQEEKGETARLQSFVGAIAVADLVKTTLGPKGMDKILQpmsegPRSGNVTVTNDGATILKSVWLDNPAA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 76 KMLIEVAKTQEKEVGDGTTTAVVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQD---KEILTK 152
Cdd:PTZ00212 84 KILVDISKTQDEEVGDGTTSVVVLAGELLREAEKLLDQKIHPQTIIEGWRMALDVARKALEEIAFDHGSDEekfKEDLLN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 153 IAMTSITGKGAEKAKEKLAEIiveAVSAVVDDEGKVDKDLIKIEKKSGASIDDTELIKGVLVDKeRVSAQMPKKVTDAKI 232
Cdd:PTZ00212 164 IARTTLSSKLLTVEKDHFAKL---AVDAVLRLKGSGNLDYIQIIKKPGGTLRDSYLEDGFILEK-KIGVGQPKRLENCKI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 233 ALLNCA-----------------------IEETASEMLKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVKK 289
Cdd:PTZ00212 240 LVANTPmdtdkikiygakvkvdsmekvaeIEAAEKEKMKNKVDKILAHGCNVFINRQLIYNYPEQLFAEAGIMAIEHADF 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 290 SDMEKLAKATGANVITNIKDLSAQDLGDAGLVEERKISGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVV 369
Cdd:PTZ00212 320 DGMERLAAALGAEIVSTFDTPEKVKLGHCDLIEEIMIGEDKLIRFSGCAKGEACTIVLRGASTHILDEAERSLHDALCVL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 370 GCTIEDGRIVSGGGSTEVELSMKLREYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHAsNGNKCA 449
Cdd:PTZ00212 400 SQTVKDTRVVLGGGCSEMLMANAVEELAKKVEGKKSLAIEAFAKALRQIPTIIADNGGYDSAELVSKLRAEHY-KGNKTA 478
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 299689058 450 GLNVFTGAVEDMCENGVVEPLRVKTQAIQSAAESTEMLLRIDDVIAA 496
Cdd:PTZ00212 479 GIDMEKGTVGDMKELGITESYKVKLSQLCSATEAAEMILRVDDIIRC 525
|
|
| TCP1_zeta |
cd03342 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
20-496 |
5.29e-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: 363.89 E-value: 5.29e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 20 AQRMNILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQEKEVGDGTTTAVVV 99
Cdd:cd03342 13 ALAVNISAAKGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLSEMQIQHPTASMIARAATAQDDITGDGTTSNVLL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 100 AGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVG-AQDKEILTKIAMTSITGKGAEKAKEKLAEIIVEAV 178
Cdd:cd03342 93 IGELLKQAERYIQEGVHPRIITEGFELAKNKALKFLESFKVPVEiDTDRELLLSVARTSLRTKLHADLADQLTEIVVDAV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 179 SAVVDDEGKVDKDLIKIEKKSGASIDDTELIKGVLVDKERVSAQMPKKVTDAKIALLNCAIEETASEmlkdmvaeIKASG 258
Cdd:cd03342 173 LAIYKPDEPIDLHMVEIMQMQHKSDSDTKLIRGLVLDHGARHPDMPKRVENAYILTCNVSLEYEKTE--------VNSGF 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 259 A-NVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATGANVITNIKDLSAQDLGDAGLVEERKISGDSMIFVEEC 337
Cdd:cd03342 245 FySVVINQKGIDPPSLDMLAKEGILALRRAKRRNMERLTLACGGVAMNSVDDLSPECLGYAGLVYERTLGEEKYTFIEGV 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 338 KHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIVSGGGSTEVELSMKLREYAEGISGREQLAVRAFADALEV 417
Cdd:cd03342 325 KNPKSCTILIKGPNDHTITQIKDAIRDGLRAVKNAIEDKCVVPGAGAFEVALYAHLKEFKKSVKGKAKLGVQAFADALLV 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 299689058 418 IPRTLAENAGLDAIEILVKVRAAHASnGNKCAGLNVFTGAVEDMCENGVVEPLRVKTQAIQSAAESTEMLLRIDDVIAA 496
Cdd:cd03342 405 IPKTLAENSGLDVQETLVKLQDEYAE-GGQVGGVDLDTGEPMDPESEGIWDNYSVKRQILHSATVIASQLLLVDEIIRA 482
|
|
| TCP1_theta |
cd03341 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ... |
24-496 |
7.59e-118 |
|
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: 355.37 E-value: 7.59e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 24 NILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQEKEVGDGTTTAVVVAGEL 103
Cdd:cd03341 13 NIEACKELSQITRTSYGPNGMNKMVINHLEKLFVTSDAATILRELEVQHPAAKLLVMASQMQEEEIGDGTNLVVVLAGEL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 104 LRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACE--VGAQDKEILTKIAMTSITGKGAEKAkEKLAEIIVEAVSAV 181
Cdd:cd03341 93 LEKAEELLRMGLHPSEIIEGYEKALKKALEILEELVVYkiEDLRNKEEVSKALKTAIASKQYGNE-DFLSPLVAEACISV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 182 V-DDEGKVDKDLIKIEKKSGASIDDTELIKGVLVDKErVSAQMpKKVTDAKIALLNCAIEEtasemlkdmvaeikasGAN 260
Cdd:cd03341 172 LpENIGNFNVDNIRVVKILGGSLEDSKVVRGMVFKRE-PEGSV-KRVKKAKVAVFSCPFDI----------------GVN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 261 VLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATGANVITNIKDLSAQDLGDAGLVEERKISGDSMIFVEECKHP 340
Cdd:cd03341 234 VIVAGGSVGDLALHYCNKYGIMVIKINSKFELRRLCRTVGATPLPRLGAPTPEEIGYCDSVYVEEIGDTKVVVFRQNKED 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 341 KAV-TMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIVSGGGSTEVELSMKLREYAEGISGREQLAVRAFADALEVIP 419
Cdd:cd03341 314 SKIaTIVLRGATQNILDDVERAIDDGVNVFKSLTKDGRFVPGAGATEIELAKKLKEYGEKTPGLEQYAIKKFAEAFEVVP 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 299689058 420 RTLAENAGLDAIEILVKVRAAHaSNGNKCAGLNVFTG--AVEDMCENGVVEPLRVKTQAIQSAAESTEMLLRIDDVIAA 496
Cdd:cd03341 394 RTLAENAGLDATEVLSELYAAH-QKGNKSAGVDIESGdeGTKDAKEAGIFDHLATKKWAIKLATEAAVTVLRVDQIIMA 471
|
|
| TCP1_beta |
cd03336 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ... |
7-496 |
2.94e-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: 352.79 E-value: 2.94e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 7 VLPENMKRYMGRDAQRMNILAGRIIAETVRSTLGPKGMDKML--VDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKT 84
Cdd:cd03336 1 ILKDGAQEEKGETARLSSFVGAIAIGDLVKTTLGPKGMDKILqsVGRSGGVTVTNDGATILKSIGVDNPAAKVLVDISKV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 85 QEKEVGDGTTTAVVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQD---KEILTKIAMTSITGK 161
Cdd:cd03336 81 QDDEVGDGTTSVTVLAAELLREAEKLVAQKIHPQTIIEGYRMATAAAREALLSSAVDHSSDEeafREDLLNIARTTLSSK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 162 GAEKAKEKLAEIiveAVSAVVDDEGKVDKDLIKIEKKSGASIDDTELIKGVLVDKeRVSAQMPKKVTDAKIALLNCA--- 238
Cdd:cd03336 161 ILTQDKEHFAEL---AVDAVLRLKGSGNLDAIQIIKKLGGSLKDSYLDEGFLLDK-KIGVNQPKRIENAKILIANTPmdt 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 239 --------------------IEETASEMLKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKA 298
Cdd:cd03336 237 dkikifgakvrvdstakvaeIEEAEKEKMKNKVEKILKHGINCFINRQLIYNYPEQLFADAGIMAIEHADFDGVERLALV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 299 TGANVITNIKDLSAQDLGDAGLVEERKISGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRI 378
Cdd:cd03336 317 TGGEIASTFDHPELVKLGTCKLIEEIMIGEDKLIRFSGVAAGEACTIVLRGASQQILDEAERSLHDALCVLAQTVKDTRV 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 379 VSGGGSTEVELSMKLREYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHAsNGNKCAGLNVFTGAV 458
Cdd:cd03336 397 VLGGGCSEMLMAKAVEELAKKTPGKKSLAIEAFAKALRQLPTIIADNAGYDSAELVAQLRAAHY-NGNTTAGLDMRKGTV 475
|
490 500 510
....*....|....*....|....*....|....*...
gi 299689058 459 EDMCENGVVEPLRVKTQAIQSAAESTEMLLRIDDVIAA 496
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 ... |
20-496 |
6.62e-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: 344.80 E-value: 6.62e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 20 AQRMNILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQEKEVGDGTTTAVVV 99
Cdd:TIGR02347 17 ALMMNINAARGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEMQIQHPTASMIARAATAQDDITGDGTTSTVLL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 100 AGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQ-DKEILTKIAMTSITGKGAEKAKEKLAEIIVEAV 178
Cdd:TIGR02347 97 IGELLKQAERYILEGVHPRIITEGFEIARKEALQFLDKFKVKKEDEvDREFLLNVARTSLRTKLPADLADQLTEIVVDAV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 179 SAVVDDEGKVDKDLIKIEKKSGASIDDTELIKGVLVDKERVSAQMPKKVTDAKIALLNCAIEETASEM------------ 246
Cdd:TIGR02347 177 LAIKKDGEDIDLFMVEIMEMKHKSATDTTLIRGLVLDHGARHPDMPRRVKNAYILTCNVSLEYEKTEVnsgffyssaeqr 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 247 --------------------LKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATGANVITN 306
Cdd:TIGR02347 257 eklvkaerkfvddrvkkiieLKKKVCGKSPDKGFVVINQKGIDPPSLDLLAKEGIMALRRAKRRNMERLTLACGGEALNS 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 307 IKDLSAQDLGDAGLVEERKISGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIVSGGGSTE 386
Cdd:TIGR02347 337 VEDLTPECLGWAGLVYETTIGEEKYTFIEECKNPKSCTILIKGPNDHTIAQIKDAVRDGLRAVKNAIEDKCVVPGAGAFE 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 387 VELSMKLREYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHaSNGNKCAGLNVFTGAVEDMCENGV 466
Cdd:TIGR02347 417 IAAYRHLKEYKKSVKGKAKLGVEAFANALLVIPKTLAENSGFDAQDTLVKLEDEH-DEGGEVVGVDLNTGEPIDPEIKGI 495
|
490 500 510
....*....|....*....|....*....|
gi 299689058 467 VEPLRVKTQAIQSAAESTEMLLRIDDVIAA 496
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 ... |
5-501 |
1.01e-105 |
|
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: 326.29 E-value: 1.01e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 5 PGVLPENMKRYMGRDAQRM-NILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAK 83
Cdd:TIGR02346 3 ASLLKEGYRHFSGLEEAVIkNIEACKELSQITRTSLGPNGMNKMVINHLEKLFVTNDAATILRELEVQHPAAKLLVMASE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 84 TQEKEVGDGTTTAVVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKT-IACEV-GAQDKEILTKIAMTSITGK 161
Cdd:TIGR02346 83 MQENEIGDGTNLVLVLAGELLNKAEELIRMGLHPSEIIKGYEMALKKAMEILEElVVWEVkDLRDKDELIKALKASISSK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 162 --GAEkakEKLAEIIVEAVSAVV-DDEGKVDKDLIKIEKKSGASIDDTELIKGVLVDKERVSAQmpKKVTDAKIALLNCA 238
Cdd:TIGR02346 163 qyGNE---DFLAQLVAQACSTVLpKNPQNFNVDNIRVCKILGGSLSNSEVLKGMVFNREAEGSV--KSVKNAKVAVFSCP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 239 IEETASE----------------------MLKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLA 296
Cdd:TIGR02346 238 LDTATTEtkgtvlihnaeellnyskgeenQIEAMIKAIADSGVNVIVTGGSVGDMALHYLNKYNIMVLKIPSKFELRRLC 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 297 KATGANVITNIKDLSAQDLGDAGLVEERKISGDSM-IFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIED 375
Cdd:TIGR02346 318 KTVGATPLPRLGAPTPEEIGYVDSVYVSEIGGDKVtVFKQENGDSKISTIILRGSTDNLLDDIERAIDDGVNTVKALVKD 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 376 GRIVSGGGSTEVELSMKLREYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHASnGNKCAGLNVFT 455
Cdd:TIGR02346 398 GRLLPGAGATEIELASRLTKYGEKLPGLDQYAIKKFAEAFEIIPRTLAENAGLNANEVIPKLYAAHKK-GNKSKGIDIEA 476
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 299689058 456 G--AVEDMCENGVVEPLRVKTQAIQSAAESTEMLLRIDDVIAAEKLRG 501
Cdd:TIGR02346 477 EsdGVKDASEAGIYDMLATKKWAIKLATEAAVTVLRVDQIIMAKPAGG 524
|
|
| chap_CCT_beta |
TIGR02341 |
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ... |
22-496 |
1.80e-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: 283.67 E-value: 1.80e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 22 RMNILAGRI-IAETVRSTLGPKGMDKMLVDD--LGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQEKEVGDGTTTAVV 98
Cdd:TIGR02341 16 RLSSFVGAIaIGDLVKSTLGPKGMDKILQSSssDASIMVTNDGATILKSIGVDNPAAKVLVDMSKVQDDEVGDGTTSVTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 99 VAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQDKEI---LTKIAMTSITGKGAEKAKEKLAEIiv 175
Cdd:TIGR02341 96 LAAELLREAEKLINQKIHPQTIIAGYREATKAARDALLKSAVDNGSDEVKFrqdLMNIARTTLSSKILSQHKDHFAQL-- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 176 eAVSAVVDDEGKVDKDLIKIEKKSGASIDDTELIKGVLVDKeRVSAQMPKKVTDAKIALLNCA----------------- 238
Cdd:TIGR02341 174 -AVDAVLRLKGSGNLEAIQIIKKLGGSLADSYLDEGFLLDK-KIGVNQPKRIENAKILIANTGmdtdkvkifgsrvrvds 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 239 ------IEETASEMLKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATGANVITNIKDLSA 312
Cdd:TIGR02341 252 takvaeLEHAEKEKMKEKVEKILKHGINCFINRQLIYNYPEQLFADAGVMAIEHADFEGVERLALVTGGEIVSTFDHPEL 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 313 QDLGDAGLVEERKISGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIVSGGGSTEVELSMK 392
Cdd:TIGR02341 332 VKLGSCDLIEEIMIGEDKLLKFSGVKLGEACTIVLRGATQQILDEAERSLHDALCVLSQTVKESRTVLGGGCSEMLMSKA 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 393 LREYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHAsNGNKCAGLNVFTGAVEDMCENGVVEPLRV 472
Cdd:TIGR02341 412 VTQEAQRTPGKEALAVEAFARALRQLPTIIADNAGFDSAELVAQLRAAHY-NGNTTMGLDMNEGTIADMRQLGITESYKV 490
|
490 500
....*....|....*....|....
gi 299689058 473 KTQAIQSAAESTEMLLRIDDVIAA 496
Cdd:TIGR02341 491 KRAVVSSAAEAAEVILRVDNIIKA 514
|
|
| chaperonin_like |
cd03333 |
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ... |
147-375 |
1.00e-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: 237.75 E-value: 1.00e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 147 KEILTKIAMTSITGKGaEKAKEKLAEIIVEAVSAVVDDEGKVDKDLIKIEKKSGASIDDTELIKGVLVDKERVSAQMPKK 226
Cdd:cd03333 1 RELLLQVATTSLNSKL-SSWDDFLGKLVVDAVLKVGPDNRMDDLGVIKVEKIPGGSLEDSELVVGVVFDKGYASPYMPKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 227 VTDAKIALLNCAIEetasemlkdmvaeikasgaNVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATGANVITN 306
Cdd:cd03333 80 LENAKILLLDCPLE-------------------YVVIAEKGIDDLALHYLAKAGIMAVRRVKKEDLERIARATGATIVSS 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 299689058 307 IKDLSAQDLGDAGLVEERKISGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIED 375
Cdd:cd03333 141 LEDLTPEDLGTAELVEETKIGEEKLTFIEGCKGGKAATILLRGATEVELDEVKRSLHDALCAVRAAVEE 209
|
|
| GroEL |
cd03344 |
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ... |
22-481 |
1.32e-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: 133.74 E-value: 1.32e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 22 RMNILAG-RIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHP----AAKMLIEVAKTQEKEVGDGTTTA 96
Cdd:cd03344 10 RKALLRGvNKLADAVKVTLGPKGRNVVIEKSFGSPKITKDGVTVAKEIELEDPfenmGAQLVKEVASKTNDVAGDGTTTA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 97 VVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVgaQDKEILTKIAMTSITGkgaekaKEKLAEIIVE 176
Cdd:cd03344 90 TVLARAIIKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKPV--KTKEEIAQVATISANG------DEEIGELIAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 177 AVSavvddegKVDKD-LIKIEkkSGASIDDT-ELIKGVLVDKERVSaqmPKKVTDAkiallncaieetasemlKDMVAEI 254
Cdd:cd03344 162 AME-------KVGKDgVITVE--EGKTLETElEVVEGMQFDRGYLS---PYFVTDP-----------------EKMEVEL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 255 kaSGANVLFCQKGIDDLAQHYLAKEGIVAARR------------------------------VK--------KSDMEKLA 296
Cdd:cd03344 213 --ENPYILLTDKKISSIQELLPILELVAKAGRplliiaedvegealatlvvnklrgglkvcaVKapgfgdrrKAMLEDIA 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 297 KATGANVITN-----IKDLSAQDLGDAGLVEerkISGDSMIFVEECKHPKAV---------------------------- 343
Cdd:cd03344 291 ILTGGTVISEelglkLEDVTLEDLGRAKKVV---VTKDDTTIIGGAGDKAAIkariaqirkqieettsdydkeklqerla 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 344 -----TMLIR--GTTEHVIEEVARAVDDAVGVVGCTIEDGrIVSGGGSTEVELSMKLrEYAEGISGREQLAVRAFADALE 416
Cdd:cd03344 368 klsggVAVIKvgGATEVELKEKKDRVEDALNATRAAVEEG-IVPGGGVALLRASPAL-DKLKALNGDEKLGIEIVRRALE 445
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 299689058 417 VIPRTLAENAGLDAIEILVKVRaahasNGNKCAGLNVFTGAVEDMCENGVVEPLRVKTQAIQSAA 481
Cdd:cd03344 446 APLRQIAENAGVDGSVVVEKVL-----ESPDGFGYDAATGEYVDMIEAGIIDPTKVVRSALQNAA 505
|
|
| groEL |
PRK12849 |
chaperonin GroEL; Reviewed |
18-495 |
2.39e-31 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237230 Cd Length: 542 Bit Score: 127.23 E-value: 2.39e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 18 RDAQRMNILAG-RIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHP----AAKMLIEVAKTQEKEVGDG 92
Cdd:PRK12849 8 DEEARRALERGvNKLADAVKVTLGPKGRNVVIDKSFGAPTITKDGVSIAKEIELEDPfenlGAQLVKEVASKTNDVAGDG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 93 TTTAVVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVgaQDKEILTKIAMTSITGKgaekakEKLAE 172
Cdd:PRK12849 88 TTTATVLAQALVQEGLKNVAAGANPMDLKRGIDKAVEAVVEELKALARPV--SGSEEIAQVATISANGD------EEIGE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 173 IIVEAVSavvddegKVDKD-LIKIEKKSGASiDDTELIKGVLVDKERVSAQMpkkVTDAkiallncaieETasemlkdMV 251
Cdd:PRK12849 160 LIAEAME-------KVGKDgVITVEESKTLE-TELEVTEGMQFDRGYLSPYF---VTDP----------ER-------ME 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 252 AEIKasGANVLFCQKGIDDLAQ--HYLAK---------------EG------IVAARR-------VK--------KSDME 293
Cdd:PRK12849 212 AVLE--DPLILLTDKKISSLQDllPLLEKvaqsgkplliiaedvEGealatlVVNKLRgglkvaaVKapgfgdrrKAMLE 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 294 KLAKATGANVIT-----NIKDLSAQDLGDAGLVEerkISGDSMIFVEECKHPKAV------------------------- 343
Cdd:PRK12849 290 DIAILTGGTVISedlglKLEEVTLDDLGRAKRVT---ITKDNTTIVDGAGDKEAIearvaqirrqieettsdydreklqe 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 344 --------TMLIR--GTTEHVIEEVARAVDDAVGVVGCTIEDGrIVSGGGSTEVELSMKLREYAeGISGREQLAVRAFAD 413
Cdd:PRK12849 367 rlaklaggVAVIKvgAATEVELKERKDRVEDALNATRAAVEEG-IVPGGGVALLRAAKALDELA-GLNGDQAAGVEIVRR 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 414 ALEVIPRTLAENAGLDAIEILVKVRAahasnGNKCAGLNVFTGAVEDMCENGVVEPLRVKTQAIQSAAESTEMLLRIDDV 493
Cdd:PRK12849 445 ALEAPLRQIAENAGLDGSVVVAKVLE-----LEDGFGFNAATGEYGDLIAAGIIDPVKVTRSALQNAASVAGLLLTTEAL 519
|
..
gi 299689058 494 IA 495
Cdd:PRK12849 520 VA 521
|
|
| GroEL |
TIGR02348 |
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ... |
22-495 |
1.20e-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: 116.24 E-value: 1.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 22 RMNILAG-RIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHP----AAKMLIEVAKTQEKEVGDGTTTA 96
Cdd:TIGR02348 11 RKALLRGvDKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDKfenmGAQLVKEVASKTNDVAGDGTTTA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 97 VVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGaqDKEILTKIAMTSITGkgaekaKEKLAEIIVE 176
Cdd:TIGR02348 91 TVLAQAIVKEGLKNVAAGANPIELKRGIEKAVEAVVEELKKLSKPVK--GKKEIAQVATISANN------DEEIGSLIAE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 177 AVSavvddegKVDKD-LIKIEKKSGAsIDDTELIKGVLVDKERVSaqmPKKVTDAK--IALLNCA---IEETASEMLKDM 250
Cdd:TIGR02348 163 AME-------KVGKDgVITVEESKSL-ETELEVVEGMQFDRGYIS---PYFVTDAEkmEVELENPyilITDKKISNIKDL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 251 V---AEIKASGANVLFCQKGIDDLAQHYLA---KEGIVAARRVK--------KSDMEKLAKATGANVIT-----NIKDLS 311
Cdd:TIGR02348 232 LpllEKVAQSGKPLLIIAEDVEGEALATLVvnkLRGTLNVCAVKapgfgdrrKAMLEDIAILTGGQVISeelglKLEEVT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 312 AQDLGDAGLVeerKISGDSMIFVEECKHPKAVTMLIR-----------------------------------GTTEHVIE 356
Cdd:TIGR02348 312 LDDLGKAKKV---TVDKDNTTIVEGAGDKAAIKARVAqikaqieettsdydreklqerlaklaggvavikvgAATETEMK 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 357 EVARAVDDAVGVVGCTIEDGrIVSGGGSTEVELSMKLrEYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVK 436
Cdd:TIGR02348 389 EKKLRIEDALNATRAAVEEG-IVPGGGVALLRAAAAL-EGLKGDGEDEAIGIDIVKRALEAPLRQIAENAGLDGAVVAEK 466
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 299689058 437 VRaahASNGNKcaGLNVFTGAVEDMCENGVVEPLRVKTQAIQSAAESTEMLLRIDDVIA 495
Cdd:TIGR02348 467 VK---ELKGNF--GFNAATGEYEDLVEAGIIDPTKVTRSALQNAASIAGLLLTTEAVVA 520
|
|
| groEL |
PRK12850 |
chaperonin GroEL; Reviewed |
30-502 |
7.11e-25 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237231 Cd Length: 544 Bit Score: 108.27 E-value: 7.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 30 IIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHP----AAKMLIEVAKTQEKEVGDGTTTAVVVAGELLR 105
Cdd:PRK12850 22 ILANAVKVTLGPKGRNVVLEKSFGAPRITKDGVTVAKEIELEDKfenmGAQMVKEVASKTNDLAGDGTTTATVLAQAIVR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 106 KAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQDKeiLTKIAMTSITGkgaekaKEKLAEIIVEAVSavvdde 185
Cdd:PRK12850 102 EGAKLVAAGMNPMDLKRGIDLAVAAVVDELKKIAKKVTSSKE--IAQVATISANG------DESIGEMIAEAMD------ 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 186 gKVDKD-LIKIEKKSGASiDDTELIKGVLVDKERVSaqmPKKVTDAK--IALLN---CAIEETASEMLKDMVAEIKA--- 256
Cdd:PRK12850 168 -KVGKEgVITVEEAKTLG-TELDVVEGMQFDRGYLS---PYFVTNPEkmRAELEdpyILLHEKKISNLQDLLPILEAvvq 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 257 SGANVLFCQKGIDDLAQHYLAKEGI-----VAARRV------KKSDMEKLAKATGANVI---TNIK--DLSAQDLGDAGL 320
Cdd:PRK12850 243 SGRPLLIIAEDVEGEALATLVVNKLrgglkSVAVKApgfgdrRKAMLEDIAVLTGGQVIsedLGIKleNVTLDMLGRAKR 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 321 VEerkISGDSMIFVEECKHPKAV---------------------------------TMLIR--GTTEHVIEEVARAVDDA 365
Cdd:PRK12850 323 VL---ITKENTTIIDGAGDKKNIearvkqiraqieettsdydreklqerlaklaggVAVIRvgGATEVEVKEKKDRVDDA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 366 VGVVGCTIEDGrIVSGGGSTEVELSMKLREyAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRaahasNG 445
Cdd:PRK12850 400 LHATRAAVEEG-IVPGGGVALLRARSALRG-LKGANADETAGIDIVRRALEEPLRQIATNAGFEGSVVVGKVA-----EL 472
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 299689058 446 NKCAGLNVFTGAVEDMCENGVVEPLRVKTQAIQSAAESTEMLLRIDDVIAAEKLRGA 502
Cdd:PRK12850 473 PGNFGFNAQTGEYGDMVEAGIIDPAKVTRTALQDAASIAALLITTEAMVAEAPKKAA 529
|
|
| Fab1_TCP |
cd03334 |
TCP-1 like domain of the eukaryotic phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinase Fab1. ... |
160-369 |
1.02e-24 |
|
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: 1.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 160 GKGAEKAKEKLAEIIVEAVSAVVDDEGKVDKDLI----KIEKKSGASIDDTELIKGVLVDKERVSAQMPKKVTDAKIALL 235
Cdd:cd03334 13 ISNDESWLDILLPLVWKAASNVKPDVRAGDDMDIrqyvKIKKIPGGSPSDSEVVDGVVFTKNVAHKRMPSKIKNPRILLL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 236 NCAIE---------------ETASEMLKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATG 300
Cdd:cd03334 93 QGPLEyqrvenkllsldpviLQEKEYLKNLVSRIVALRPDVILVEKSVSRIAQDLLLEAGITLVLNVKPSVLERISRCTG 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 299689058 301 ANVITNIKDLSA-QDLGDAGLVEERKI-----SGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVV 369
Cdd:cd03334 173 ADIISSMDDLLTsPKLGTCESFRVRTYveehgRSKTLMFFEGCPKELGCTILLRGGDLEELKKVKRVVEFMVFAA 247
|
|
| groEL |
PRK12851 |
chaperonin GroEL; Reviewed |
13-495 |
9.22e-22 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 171770 Cd Length: 541 Bit Score: 98.66 E-value: 9.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 13 KRYMGRDAQRMNILAG-RIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHP----AAKMLIEVAKTQEK 87
Cdd:PRK12851 4 KEVKFHVEAREKMLRGvNILADAVKVTLGPKGRNVVIDKSFGAPTITNDGVTIAKEIELEDKfenmGAQMVREVASKTND 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 88 EVGDGTTTAVVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQDKeiltKIAMTSITGKGaekaK 167
Cdd:PRK12851 84 VAGDGTTTATVLAQAIVREGAKAVAAGANPMDLKRGIDRAVAAVVEELKANARPVTTNAE----IAQVATISANG----D 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 168 EKLAEIIVEAVsavvddeGKVDKDLIKIEKKSGASIDDTELIKGVLVDKERVSA-------QMPKKVTDAKIALLNCAIE 240
Cdd:PRK12851 156 AEIGRLVAEAM-------EKVGNEGVITVEESKTAETELEVVEGMQFDRGYLSPyfvtdadKMEAELEDPYILIHEKKIS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 241 EtasemLKDMVA---EIKASGANVLFCQKGIDDLAQHYLAKEGI-----VAARRV------KKSDMEKLAKATGANVIT- 305
Cdd:PRK12851 229 N-----LQDLLPvleAVVQSGKPLLIIAEDVEGEALATLVVNKLrgglkVAAVKApgfgdrRKAMLEDIAILTGGTVISe 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 306 ----NIKDLSAQDLGDAGLVEERKI-------SGDSMIFVEECKHPKAV-----------------------TMLIR--G 349
Cdd:PRK12851 304 dlgiKLENVTLEQLGRAKKVVVEKEnttiidgAGSKTEIEGRVAQIRAQieettsdydreklqerlaklaggVAVIRvgA 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 350 TTEHVIEEVARAVDDAVGVVGCTIEDGrIVSGGGSTEVELSMKLREyAEGISGREQLAVRAFADALEVIPRTLAENAGLD 429
Cdd:PRK12851 384 STEVEVKEKKDRVDDALHATRAAVEEG-IVPGGGVALLRAVKALDK-LETANGDQRTGVEIVRRALEAPVRQIAENAGAE 461
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 299689058 430 AIEILVKVRaahasNGNKCAGLNVFTGAVEDMCENGVVEPLRVKTQAIQSAAESTEMLLRIDDVIA 495
Cdd:PRK12851 462 GSVVVGKLR-----EKPGGYGFNAATNEYGDLYAQGVIDPVKVVRTALQNAASVAGLLLTTEAMVA 522
|
|
| PTZ00114 |
PTZ00114 |
Heat shock protein 60; Provisional |
22-488 |
1.10e-21 |
|
Heat shock protein 60; Provisional
Pssm-ID: 185455 Cd Length: 555 Bit Score: 98.45 E-value: 1.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 22 RMNILAG-RIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILR--EMS--VEHPAAKMLIEVAKTQEKEVGDGTTTA 96
Cdd:PTZ00114 24 RQSLLKGiERLADAVAVTLGPKGRNVIIEQEYGSPKITKDGVTVAKaiEFSdrFENVGAQLIRQVASKTNDKAGDGTTTA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 97 VVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVgaQDKEILTKIAMTSITGkgaekaKEKLAEIIVE 176
Cdd:PTZ00114 104 TILARAIFREGCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQSRPV--KTKEDILNVATISANG------DVEIGSLIAD 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 177 AVsavvddeGKVDKD-LIKIEkkSGASIDDT-ELIKGVLVDKERVSaqmPKKVTDA---KIALLNCAIEETASEMLKdmV 251
Cdd:PTZ00114 176 AM-------DKVGKDgTITVE--DGKTLEDElEVVEGMSFDRGYIS---PYFVTNEktqKVELENPLILVTDKKISS--I 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 252 AEI-------KASGANVLFCQKGIDDLAQHYLA----KEGI-VAARRV------KKSDMEKLAKATGANVITN------I 307
Cdd:PTZ00114 242 QSIlpilehaVKNKRPLLIIAEDVEGEALQTLIinklRGGLkVCAVKApgfgdnRKDILQDIAVLTGATVVSEdnvglkL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 308 KDLSAQDLGDAGLVEerkISGDSMIFVEECKHPKAV-----------------------------------TMLIRGTTE 352
Cdd:PTZ00114 322 DDFDPSMLGSAKKVT---VTKDETVILTGGGDKAEIkervellrsqierttseydkeklkerlaklsggvaVIKVGGASE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 353 HVIEEVARAVDDAVGVVGCTIEDGrIVSGGGSTEVELSMKLREYAEG--ISGREQLAVRAFADALEVIPRTLAENAGLDA 430
Cdd:PTZ00114 399 VEVNEKKDRIEDALNATRAAVEEG-IVPGGGVALLRASKLLDKLEEDneLTPDQRTGVKIVRNALRLPTKQIAENAGVEG 477
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 299689058 431 IEILVKVraahASNGNKCAGLNVFTGAVEDMCENGVVEPLRVKTQAIQSAAESTEMLL 488
Cdd:PTZ00114 478 AVVVEKI----LEKKDPSFGYDAQTGEYVNMFEAGIIDPTKVVRSALVDAASVASLML 531
|
|
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
17-495 |
8.44e-20 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 92.49 E-value: 8.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 17 GRDAQRmNILAG-RIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHP----AAKMLIEVA-KTQEKeVG 90
Cdd:PRK00013 8 GEDARR-KLLRGvNKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDPfenmGAQLVKEVAsKTNDV-AG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 91 DGTTTAVVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQDKeiltkIAMT-SITGKGAEKakek 169
Cdd:PRK00013 86 DGTTTATVLAQAIVREGLKNVAAGANPMDLKRGIDKAVEAAVEELKKISKPVEDKEE-----IAQVaTISANGDEE---- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 170 LAEIIVEAVSavvddegKVDKD-LIKIEKKSGASiDDTELIKGVLVDKERVSAQMpkkVTDAK--IALLNCA---IEETA 243
Cdd:PRK00013 157 IGKLIAEAME-------KVGKEgVITVEESKGFE-TELEVVEGMQFDRGYLSPYF---VTDPEkmEAELENPyilITDKK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 244 SEMLKDMVA---EIKASGANVLFCQKGIDDLAQHYLAKEGI-----VAA--------RRvkKSDMEKLAKATGANVIT-- 305
Cdd:PRK00013 226 ISNIQDLLPvleQVAQSGKPLLIIAEDVEGEALATLVVNKLrgtlkVVAvkapgfgdRR--KAMLEDIAILTGGTVISee 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 306 ---NIKDLSAQDLGDAGLVeerKISGDSMIFVEECKHPKAVT---MLIRGTTEH----------------------VI-- 355
Cdd:PRK00013 304 lglKLEDATLEDLGQAKKV---VVTKDNTTIVDGAGDKEAIKarvAQIKAQIEEttsdydreklqerlaklaggvaVIkv 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 356 ---------EEVARaVDDAVGVVGCTIEDGrIVSGGGSTEVELSMKLrEYAEGISGREQLAVRAFADALEVIPRTLAENA 426
Cdd:PRK00013 381 gaatevemkEKKDR-VEDALHATRAAVEEG-IVPGGGVALLRAAPAL-EALKGLNGDEATGINIVLRALEAPLRQIAENA 457
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 299689058 427 GLDAIEILVKVRAAHASNgnkcAGLNVFTGAVEDMCENGVVEPLRVKTQAIQSAAESTEMLLRIDDVIA 495
Cdd:PRK00013 458 GLEGSVVVEKVKNGKGKG----YGYNAATGEYVDMIEAGIIDPTKVTRSALQNAASVAGLLLTTEAVVA 522
|
|
| groEL |
CHL00093 |
chaperonin GroEL |
30-498 |
6.30e-19 |
|
chaperonin GroEL
Pssm-ID: 177025 Cd Length: 529 Bit Score: 89.78 E-value: 6.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 30 IIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKM---LIEVAKTQEKEV-GDGTTTAVVVAGELLR 105
Cdd:CHL00093 21 ILAEAVSVTLGPKGRNVVLEKKYGSPQIVNDGVTIAKEIELEDHIENTgvaLIRQAASKTNDVaGDGTTTATVLAYAIVK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 106 KAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVgaQDKEILTKIAMTSiTGKGAEkakekLAEIIVEAVSavvdde 185
Cdd:CHL00093 101 QGMKNVAAGANPISLKRGIEKATQYVVSQIAEYARPV--EDIQAITQVASIS-AGNDEE-----VGSMIADAIE------ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 186 gKVDKD-LIKIEKKSGASIdDTELIKGVLVDKERVSaqmPKKVTDA---KIALLNCAIEETASEM------LKDMVAEIK 255
Cdd:CHL00093 167 -KVGREgVISLEEGKSTVT-ELEITEGMRFEKGFIS---PYFVTDTermEVVQENPYILLTDKKItlvqqdLLPILEQVT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 256 ASGANVLFCQKGIDD--LAQHYLAK-EGI--VAARRV------KKSDMEKLAKATGANVITNIKDLSAQDLGDAGLVEER 324
Cdd:CHL00093 242 KTKRPLLIIAEDVEKeaLATLVLNKlRGIvnVVAVRApgfgdrRKAMLEDIAILTGGQVITEDAGLSLETIQLDLLGQAR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 325 KI--SGDSMIFVEEcKHPKAVTM---------------------------------LIR--GTTEHVIEEVARAVDDAVG 367
Cdd:CHL00093 322 RIivTKDSTTIIAD-GNEEQVKArceqlrkqieiadssyekeklqerlaklsggvaVIKvgAATETEMKDKKLRLEDAIN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 368 VVGCTIEDGrIVSGGGSTEVELSMKLREYAE-GISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRaahasNGN 446
Cdd:CHL00093 401 ATKAAVEEG-IVPGGGATLVHLSENLKTWAKnNLKEDELIGALIVARAILAPLKRIAENAGKNGSVIIEKVQ-----EQD 474
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 299689058 447 KCAGLNVFTGAVEDMCENGVVEPLRVKTQAIQSAAESTEMLLRIDDVIAAEK 498
Cdd:CHL00093 475 FEIGYNAANNKFVNMYEAGIIDPAKVTRSALQNAASIASMILTTECIIVDKK 526
|
|
| groEL |
PRK12852 |
chaperonin GroEL; Reviewed |
30-495 |
2.73e-16 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237232 Cd Length: 545 Bit Score: 81.43 E-value: 2.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 30 IIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSV----EHPAAKMLIEVAKTQEKEVGDGTTTAVVVAGELLR 105
Cdd:PRK12852 22 ILANAVKVTLGPKGRNVVIEKSFGAPRITKDGVTVAKEIELedkfENMGAQMVREVASKTNDLAGDGTTTATVLAQAIVR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 106 KAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQ-------------DKEILTKIA--MTSITGKGAEKAKE-K 169
Cdd:PRK12852 102 EGAKAVAAGMNPMDLKRGIDIAVAAVVKDIEKRAKPVASSaeiaqvgtisangDAAIGKMIAqaMQKVGNEGVITVEEnK 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 170 LAEIIVEAVSAVVDDEGKVDKDLIKIEKKSGASIDDTElikgVLVDKERVS---AQMP--KKVTDAKIALLNCAiEETAS 244
Cdd:PRK12852 182 SLETEVDIVEGMKFDRGYLSPYFVTNAEKMTVELDDAY----ILLHEKKLSglqAMLPvlEAVVQSGKPLLIIA-EDVEG 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 245 EMLKDMV----------AEIKASGAN-----------VLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKlAKATGANV 303
Cdd:PRK12852 257 EALATLVvnrlrgglkvAAVKAPGFGdrrkamlediaILTGGQLISEDLGIKLENVTLKMLGRAKKVVIDK-ENTTIVNG 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 304 ITNIKDLSAQDLGDAGLVEERKISGDSMIFVEECKHPKAVTMLIR--GTTEHVIEEVARAVDDAVGVVGCTIEDGrIVSG 381
Cdd:PRK12852 336 AGKKADIEARVGQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRvgGATEVEVKEKKDRVEDALNATRAAVQEG-IVPG 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 382 GGsteVELsMKLREYAEGISGR---EQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRaahaSNGNKCAGLNVFTGAV 458
Cdd:PRK12852 415 GG---VAL-LRAKKAVGRINNDnadVQAGINIVLKALEAPIRQIAENAGVEGSIVVGKIL----ENKSETFGFDAQTEEY 486
|
490 500 510
....*....|....*....|....*....|....*..
gi 299689058 459 EDMCENGVVEPLRVKTQAIQSAAESTEMLLRIDDVIA 495
Cdd:PRK12852 487 VDMVAKGIIDPAKVVRTALQDAASVAGLLVTTEAMVA 523
|
|
| PLN03167 |
PLN03167 |
Chaperonin-60 beta subunit; Provisional |
31-494 |
6.87e-16 |
|
Chaperonin-60 beta subunit; Provisional
Pssm-ID: 215611 [Multi-domain] Cd Length: 600 Bit Score: 80.35 E-value: 6.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 31 IAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHP----AAKMLIEVAKTQEKEVGDGTTTAVVVAGELLRK 106
Cdd:PLN03167 78 LADLVGVTLGPKGRNVVLESKYGSPKIVNDGVTVAKEVELEDPveniGAKLVRQAAAKTNDLAGDGTTTSVVLAQGLIAE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 107 AEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEV------------GAQDKEILTKI--AMTSITGKGAEKAKE-KLA 171
Cdd:PLN03167 158 GVKVVAAGANPVQITRGIEKTAKALVKELKKMSKEVedseladvaavsAGNNYEVGNMIaeAMSKVGRKGVVTLEEgKSA 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 172 EIIVEAVSAVVDDEGKVDKDLIKIEKKSGASIDDTELIkgvLVDkervsaqmpKKVTDAK--IALLNCAI---------- 239
Cdd:PLN03167 238 ENNLYVVEGMQFDRGYISPYFVTDSEKMSVEYDNCKLL---LVD---------KKITNARdlIGILEDAIrggyplliia 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 240 EETASEMLKDMVA-EIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSD----MEKLAK---ATGANVI------T 305
Cdd:PLN03167 306 EDIEQEALATLVVnKLRGSLKIAALKAPGFGERKSQYLDDIAILTGGTVIREEvglsLDKVGKevlGTAAKVVltkdttT 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 306 NIKDLSAQDlgdagLVEERKISGDSMIFVEECKHPK-------------AVTMLIRGTTEHVIEEVARAVDDAVGVVGCT 372
Cdd:PLN03167 386 IVGDGSTQE-----AVNKRVAQIKNLIEAAEQDYEKeklneriaklsggVAVIQVGAQTETELKEKKLRVEDALNATKAA 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 373 IEDGrIVSGGGSTEVELSMKLREYAEGISGREQ-LAVRAFADALEVIPRTLAENAGLDAIEILVKVraahASNGNKCAGL 451
Cdd:PLN03167 461 VEEG-IVVGGGCTLLRLASKVDAIKDTLENDEQkVGADIVKRALSYPLKLIAKNAGVNGSVVSEKV----LSNDNPKFGY 535
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 299689058 452 NVFTGAVEDMCENGVVEPLRVKTQAIQSAAESTEMLLRIDDVI 494
Cdd:PLN03167 536 NAATGKYEDLMAAGIIDPTKVVRCCLEHAASVAKTFLTSDCVV 578
|
|
| PRK14104 |
PRK14104 |
chaperonin GroEL; Provisional |
17-502 |
1.81e-13 |
|
chaperonin GroEL; Provisional
Pssm-ID: 172594 Cd Length: 546 Bit Score: 72.76 E-value: 1.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 17 GRDAQRMNILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSV----EHPAAKMLIEVAKTQEKEVGDG 92
Cdd:PRK14104 9 GVDARDRMLRGVDILANAVKVTLGPKGRNVVLDKSFGAPRITKDGVTVAKEIELedkfENMGAQMVREVASKSADAAGDG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 93 TTTAVVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELL-----KTIACEVGAQ--------DKEI--LTKIAMTS 157
Cdd:PRK14104 89 TTTATVLAQAIVREGAKSVAAGMNPMDLKRGIDLAVEAVVADLvknskKVTSNDEIAQvgtisangDAEIgkFLADAMKK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 158 ITGKGAEKAKE-KLAEIIVEAVSAVVDDEGKVDKDLIKIEKKSGASIDDTElikgVLVDKERVSA-----QMPKKVTDAK 231
Cdd:PRK14104 169 VGNEGVITVEEaKSLETELDVVEGMQFDRGYISPYFVTNADKMRVEMDDAY----ILINEKKLSSlnellPLLEAVVQTG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 232 IALLNCAiEETASEMLKDM----------VAEIKASGAN-----------VLFCQKGIDDLAQHYLAKEGIVAARRVKKS 290
Cdd:PRK14104 245 KPLVIVA-EDVEGEALATLvvnrlrgglkVAAVKAPGFGdrrkamlqdiaILTGGQAISEDLGIKLENVTLQMLGRAKKV 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 291 DMEKlAKATGANVITNIKDLSAQDLGDAGLVEERKISGDSMIFVEECKHPKAVTMLIR--GTTEHVIEEVARAVDDAVGV 368
Cdd:PRK14104 324 MIDK-ENTTIVNGAGKKADIEARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRvgGATEVEVKERKDRVDDAMHA 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299689058 369 VGCTIEDGrIVSGGGSTEVELSMKLREYAEGiSGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVraahASNGNKC 448
Cdd:PRK14104 403 TRAAVEEG-IVPGGGVALLRASEQLKGIKTK-NDDQKTGVEIVRKALSAPARQIAINAGEDGSVIVGKI----LEKEQYS 476
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 299689058 449 AGLNVFTGAVEDMCENGVVEPLRVKTQAIQSAAESTEMLLRIDDVIAAEKLRGA 502
Cdd:PRK14104 477 YGFDSQTGEYGNLVSKGIIDPTKVVRTAIQNAASVAALLITTEAMVAELPKKGG 530
|
|
| |
