|
Name |
Accession |
Description |
Interval |
E-value |
| thermosome_alpha |
NF041082 |
thermosome subunit alpha; |
1-512 |
0e+00 |
|
thermosome subunit alpha;
Pssm-ID: 469009 Cd Length: 518 Bit Score: 839.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 1 VLPENMKRYMGRDAQRMNILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQE 80
Cdd:NF041082 5 ILKEGTQRTSGRDAQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDVVITNDGVTILKEMDIEHPAAKMIVEVAKTQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 81 KEVGDGTTTAVVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQDKEILTKIAMTSITGKGAEKA 160
Cdd:NF041082 85 DEVGDGTTTAVVLAGELLKKAEELLDQDIHPTIIAEGYRLAAEKALEILDEIAIKVDPDDKETLKKIAATAMTGKGAEAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 161 KEKLAEIIVEAVSAVVDDEG--KVDKDLIKIEKKSGASIDDTELIKGVLVDKERVSAQMPKKVTDAKIALLNCAIEIKET 238
Cdd:NF041082 165 KDKLADLVVDAVKAVAEKDGgyNVDLDNIKVEKKVGGSIEDSELVEGVVIDKERVHPGMPKRVENAKIALLDAPLEVKKT 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 239 ETDAEIRITDPAKLMEFIEQEEKMLKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATGAN 318
Cdd:NF041082 245 EIDAKISITDPDQLQAFLDQEEKMLKEMVDKIADSGANVVFCQKGIDDLAQHYLAKEGILAVRRVKKSDMEKLAKATGAR 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 319 VIAAIAALSAQDLGDAGLVEERKISGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIVSGG 398
Cdd:NF041082 325 IVTSIDDLSPEDLGYAGLVEERKVGGDKMIFVEGCKNPKAVTILLRGGTEHVVDEVERALEDALRVVRVVLEDGKVVAGG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 399 GSTEVELSMKLREYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHaSNGNKCAGLNVFTGAVEDMC 478
Cdd:NF041082 405 GAPEVELALRLREYAASVGGREQLAIEAFAEALEIIPRTLAENAGLDPIDALVELRSAH-EKGNKTAGLDVYTGKVVDML 483
|
490 500 510
....*....|....*....|....*....|....
3IZI_E 479 ENGVVEPLRVKTQAIQSAAESTEMLLRIDDVIAA 512
Cdd:NF041082 484 EIGVVEPLRVKTQAIKSATEAAVMILRIDDVIAA 517
|
|
| thermosome_beta |
NF041083 |
thermosome subunit beta; |
1-512 |
0e+00 |
|
thermosome subunit beta;
Pssm-ID: 469010 Cd Length: 519 Bit Score: 816.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 1 VLPENMKRYMGRDAQRMNILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQE 80
Cdd:NF041083 5 ILKEGTQRTKGRDAQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDIVITNDGATILKEMDVQHPAAKMLVEVAKTQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 81 KEVGDGTTTAVVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQDKEILTKIAMTSITGKGAEKA 160
Cdd:NF041083 85 DEVGDGTTTAVVLAGELLKKAEELLDQNIHPTIIANGYRLAAEKAIEILDEIAEKVDPDDRETLKKIAETSLTSKGVEEA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 161 KEKLAEIIVEAVSAVVDDEG---KVDKDLIKIEKKSGASIDDTELIKGVLVDKERVSAQMPKKVTDAKIALLNCAIEIKE 237
Cdd:NF041083 165 RDYLAEIAVKAVKQVAEKRDgkyYVDLDNIQIEKKHGGSIEDTQLIYGIVIDKEVVHPGMPKRVENAKIALLDAPLEVKK 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 238 TETDAEIRITDPAKLMEFIEQEEKMLKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATGA 317
Cdd:NF041083 245 TEIDAEIRITDPDQLQKFLDQEEKMLKEMVDKIKATGANVVFCQKGIDDLAQHYLAKAGILAVRRVKKSDMEKLAKATGA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 318 NVIAAIAALSAQDLGDAGLVEERKISGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIVSG 397
Cdd:NF041083 325 RIVTNIDDLTPEDLGYAELVEERKVGDDKMVFVEGCKNPKAVTILIRGGTEHVVDEAERALEDALSVVADAVEDGKIVAG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 398 GGSTEVELSMKLREYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHaSNGNKCAGLNVFTGAVEDM 477
Cdd:NF041083 405 GGAPEVELAKRLREYAATVGGREQLAVEAFAEALEIIPRTLAENAGLDPIDILVKLRSAH-EKGKKWAGINVFTGEVVDM 483
|
490 500 510
....*....|....*....|....*....|....*
3IZI_E 478 CENGVVEPLRVKTQAIQSAAESTEMLLRIDDVIAA 512
Cdd:NF041083 484 WELGVIEPLRVKTQAIKSATEAATMILRIDDVIAA 518
|
|
| cpn60 |
cd03343 |
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ... |
1-512 |
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: 784.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 1 VLPENMKRYMGRDAQRMNILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQE 80
Cdd:cd03343 3 ILKEGTQRTSGRDAQRMNIAAAKAVAEAVRTTLGPKGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAKTQD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 81 KEVGDGTTTAVVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQDKEILTKIAMTSITGKGAEKA 160
Cdd:cd03343 83 EEVGDGTTTAVVLAGELLEKAEDLLDQNIHPTVIIEGYRLAAEKALELLDEIAIKVDPDDKDTLRKIAKTSLTGKGAEAA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 161 KEKLAEIIVEAVSAVVDDEG---KVDKDLIKIEKKSGASIDDTELIKGVLVDKERVSAQMPKKVTDAKIALLNCAIEIKE 237
Cdd:cd03343 163 KDKLADLVVDAVLQVAEKRDgkyVVDLDNIKIEKKTGGSVDDTELIRGIVIDKEVVHPGMPKRVENAKIALLDAPLEVKK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 238 TETDAEIRITDPAKLMEFIEQEEKMLKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATGA 317
Cdd:cd03343 243 TEIDAKIRITSPDQLQAFLEQEEAMLKEMVDKIADTGANVVFCQKGIDDLAQHYLAKAGILAVRRVKKSDMEKLARATGA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 318 NVIAAIAALSAQDLGDAGLVEERKISGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIVSG 397
Cdd:cd03343 323 KIVTNIDDLTPEDLGEAELVEERKVGDDKMVFVEGCKNPKAVTILLRGGTEHVVDELERALEDALRVVADALEDGKVVAG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 398 GGSTEVELSMKLREYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHAsNGNKCAGLNVFTGAVEDM 477
Cdd:cd03343 403 GGAVEIELAKRLREYARSVGGREQLAVEAFADALEEIPRTLAENAGLDPIDTLVELRAAHE-KGNKNAGLDVYTGEVVDM 481
|
490 500 510
....*....|....*....|....*....|....*
3IZI_E 478 CENGVVEPLRVKTQAIQSAAESTEMLLRIDDVIAA 512
Cdd:cd03343 482 LEKGVIEPLRVKKQAIKSATEAATMILRIDDVIAA 516
|
|
| thermosome_arch |
TIGR02339 |
thermosome, various subunits, archaeal; Thermosome is the name given to the archaeal rather ... |
1-512 |
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: 700.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 1 VLPENMKRYMGRDAQRMNILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQE 80
Cdd:TIGR02339 4 ILKEGTQRTSGRDAQRNNIAAAKAVAEAVKSTLGPRGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAKTQD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 81 KEVGDGTTTAVVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQDKEILTKIAMTSITGKG-AEK 159
Cdd:TIGR02339 84 EEVGDGTTTAVVLAGELLEKAEDLLEQDIHPTVIIEGYRKAAEKALEIIDEIATKISPEDRDLLKKIAYTSLTSKAsAEV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 160 AKEKLAEIIVEAVSAVV----DDEGKVDKDLIKIEKKSGASIDDTELIKGVLVDKERVSAQMPKKVTDAKIALLNCAIEI 235
Cdd:TIGR02339 164 AKDKLADLVVEAVKQVAelrgDGKYYVDLDNIKIVKKKGGSIEDTELVEGIVVDKEVVHPGMPKRVENAKIALLDAPLEV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 236 KETETDAEIRITDPAKLMEFIEQEEKMLKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKAT 315
Cdd:TIGR02339 244 EKTEIDAKIRITDPDQIKKFLDQEEAMLKEMVDKIASAGANVVICQKGIDDVAQHYLAKAGILAVRRVKKSDIEKLARAT 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 316 GANVIAAIAALSAQDLGDAGLVEERKISGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIV 395
Cdd:TIGR02339 324 GARIVSSIDEITESDLGYAELVEERKVGEDKMVFVEGCKNPKAVTILLRGGTEHVVDELERSIQDALHVVANALEDGKIV 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 396 SGGGSTEVELSMKLREYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHAsNGNKCAGLNVFTGAVE 475
Cdd:TIGR02339 404 AGGGAVEIELALRLRSYARSVGGREQLAIEAFADALEEIPRILAENAGLDPIDALVDLRAKHE-KGNKNAGINVFTGEIE 482
|
490 500 510
....*....|....*....|....*....|....*..
3IZI_E 476 DMCENGVVEPLRVKTQAIQSAAESTEMLLRIDDVIAA 512
Cdd:TIGR02339 483 DMLELGVIEPLRVKEQAIKSATEAATMILRIDDVIAA 519
|
|
| Cpn60_TCP1 |
pfam00118 |
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ... |
25-512 |
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: 615.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 25 IAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQEKEVGDGTTTAVVVAGELLRKAEEL 104
Cdd:pfam00118 1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELEIQHPAAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEEAEKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 105 LDQNVHPTIVVKGYQAAAQKAQELLKTIAC-EVGAQDKEILTKIAMTSITGKGAEKAKEKLAEIIVEAVSAVVDDEGKVD 183
Cdd:pfam00118 81 LAAGVHPTTIIEGYEKALEKALEILDSIISiPVEDVDREDLLKVARTSLSSKIISRESDFLAKLVVDAVLAIPKNDGSFD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 184 KDLIKIEKKSGASIDDTELIKGVLVDKERVSAQMPKKVTDAKIALLNCAIEIKETETDAEIRITDPAKLMEFIEQEEKML 263
Cdd:pfam00118 161 LGNIGVVKILGGSLEDSELVDGVVLDKGPLHPDMPKRLENAKVLLLNCSLEYEKTETKATVVLSDAEQLERFLKAEEEQI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 264 KDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATGANVIAAIAALSAQDLGDAGLVEERKIS 343
Cdd:pfam00118 241 LEIVEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMALRRVKKRDLERLAKATGARAVSSLDDLTPDDLGTAGKVEEEKIG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 344 GDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIVSGGGSTEVELSMKLREYAEGISGREQLA 423
Cdd:pfam00118 321 DEKYTFIEGCKSPKAATILLRGATDHVLDEIERSIHDALCVVKNAIEDPRVVPGGGAVEMELARALREYAKSVSGKEQLA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 424 VRAFADALEVIPRTLAENAGLDAIEILVKVRAAHAsNGNKCAGLNVFTGAVEDMCENGVVEPLRVKTQAIQSAAESTEML 503
Cdd:pfam00118 401 IEAFAEALEVIPKTLAENAGLDPIEVLAELRAAHA-SGEKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKSATEAASTI 479
|
....*....
3IZI_E 504 LRIDDVIAA 512
Cdd:pfam00118 480 LRIDDIIKA 488
|
|
| chaperonin_type_I_II |
cd00309 |
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ... |
7-511 |
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: 587.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 7 KRYMGRDAQRMNILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQEKEVGDG 86
Cdd:cd00309 2 EREFGEEARLSNINAAKALADAVKTTLGPKGMDKMLVDSLGDPTITNDGATILKEIEVEHPAAKLLVEVAKSQDDEVGDG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 87 TTTAVVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQDKEILTKIAMTSITGKGAEKAKEKLAE 166
Cdd:cd00309 82 TTTVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVPIDVEDREELLKVATTSLNSKLVSGGDDFLGE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 167 IIVEAVSAVVDDEGKVDKDLIKIEKKSGASIDDTELIKGVLVDKERVSAQMPKKVTDAKIALLNCAIEiketetdaeiri 246
Cdd:cd00309 162 LVVDAVLKVGKENGDVDLGVIRVEKKKGGSLEDSELVVGMVFDKGYLSPYMPKRLENAKILLLDCKLE------------ 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 247 tdpaklmefieqeekmlkdmvaeikasgaNVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATGANVIAAIAAL 326
Cdd:cd00309 230 -----------------------------YVVIAEKGIDDEALHYLAKLGIMAVRRVRKEDLERIAKATGATIVSRLEDL 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 327 SAQDLGDAGLVEERKISGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIVSGGGSTEVELS 406
Cdd:cd00309 281 TPEDLGTAGLVEETKIGDEKYTFIEGCKGGKVATILLRGATEVELDEAERSLHDALCAVRAAVEDGGIVPGGGAAEIELS 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 407 MKLREYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHAsNGNKCAGLNVFTGAVEDMCENGVVEPL 486
Cdd:cd00309 361 KALEELAKTLPGKEQLGIEAFADALEVIPRTLAENAGLDPIEVVTKLRAKHA-EGGGNAGGDVETGEIVDMKEAGIIDPL 439
|
490 500
....*....|....*....|....*
3IZI_E 487 RVKTQAIQSAAESTEMLLRIDDVIA 511
Cdd:cd00309 440 KVKRQALKSATEAASLILTIDDIIV 464
|
|
| GroEL |
COG0459 |
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ... |
11-512 |
4.98e-173 |
|
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227 Cd Length: 497 Bit Score: 496.91 E-value: 4.98e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 11 GRDAQRMNILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHP----AAKMLIEVAKTQEKEVGDG 86
Cdd:COG0459 8 GEDARRANIRGVKALADAVKVTLGPKGRNVMLVKSFGDPTITNDGVTIAKEIELEDPfenmGAQLVKEVASKTNDEAGDG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 87 TTTAVVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVgaQDKEILTKIAMTSITGkgaekaKEKLAE 166
Cdd:COG0459 88 TTTATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPV--DDKEELAQVATISANG------DEEIGE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 167 IIVEAVSAVVDDegkvdkDLIKIEKKSGASiDDTELIKGVLVDKERVSAQ-------MPKKVTDAKIALLNCAIEIkete 239
Cdd:COG0459 160 LIAEAMEKVGKD------GVITVEEGKGLE-TELEVVEGMQFDKGYLSPYfvtdpekMPAELENAYILLTDKKISS---- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 240 tdaeiritdpaklmefieqeEKMLKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRV-----------KKSDM 308
Cdd:COG0459 229 --------------------IQDLLPLLEKVAQSGKPLLIIAEDIDGEALATLVVNGIRGVLRVvavkapgfgdrRKAML 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 309 EKLAKATGANVIA-----AIAALSAQDLGDAGLVEERKisgDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVG 383
Cdd:COG0459 289 EDIAILTGGRVISedlglKLEDVTLDDLGRAKRVEVDK---DNTTIVEGAGNPKAIVILVGAATEVEVKERKRRVEDALH 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 384 VVGCTIEDGrIVSGGGSTEVELSMKLREYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAhasnGNK 463
Cdd:COG0459 366 ATRAAVEEG-IVPGGGAALLRAARALRELAAKLEGDEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKVRAA----KDK 440
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
3IZI_E 464 CAGLNVFTGAVEDMCENGVVEPLRVKTQAIQSAAESTEMLLRIDDVIAA 512
Cdd:COG0459 441 GFGFDAATGEYVDMLEAGVIDPAKVKRSALQNAASVAGLILTTEAVIAD 489
|
|
| TCP1_epsilon |
cd03339 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ... |
4-511 |
4.92e-167 |
|
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: 482.95 E-value: 4.92e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 4 ENMKRYMGRDAQRMNILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQEKEV 83
Cdd:cd03339 14 EKKKRLKGLEAHKSHILAAKSVANILRTSLGPRGMDKILVSPDGEVTVTNDGATILEKMDVDHQIAKLLVELSKSQDDEI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 84 GDGTTTAVVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIA--CEVGAQDKEILTKIAMTSITGKGAEKAK 161
Cdd:cd03339 94 GDGTTGVVVLAGALLEQAEKLLDRGIHPIRIADGYEQACKIAVEHLEEIAdkIEFSPDNKEPLIQTAMTSLGSKIVSRCH 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 162 EKLAEIIVEAVSAVVDDEGK-VDKDLIKIEKKSGASIDDTELIKGVLVDKERVSAQMPKKVTDAKIALLNCAIEIKETET 240
Cdd:cd03339 174 RQFAEIAVDAVLSVADLERKdVNFELIKVEGKVGGRLEDTKLVKGIVIDKDFSHPQMPKEVKDAKIAILTCPFEPPKPKT 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 241 DAEIRITDPAKLMEFIEQEEKMLKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATGANVI 320
Cdd:cd03339 254 KHKLDITSVEDYKKLQEYEQKYFREMVEQVKDAGANLVICQWGFDDEANHLLLQNGLPAVRWVGGVEIELIAIATGGRIV 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 321 AAIAALSAQDLGDAGLVEERKI--SGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIVSGG 398
Cdd:cd03339 334 PRFEDLSPEKLGKAGLVREISFgtTKDKMLVIEGCPNSKAVTIFIRGGNKMIIEEAKRSLHDALCVVRNLIRDNRIVYGG 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 399 GSTEVELSMKLREYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHASNGNKCAGLNVFTGAVEDMC 478
Cdd:cd03339 414 GAAEISCSLAVEKAADKCSGIEQYAMRAFADALESIPLALAENSGLNPIETLSEVKARQVKEKNPHLGIDCLGRGTNDMK 493
|
490 500 510
....*....|....*....|....*....|...
3IZI_E 479 ENGVVEPLRVKTQAIQSAAESTEMLLRIDDVIA 511
Cdd:cd03339 494 EQKVFETLISKKQQILLATQVVKMILKIDDVIV 526
|
|
| TCP1_delta |
cd03338 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ... |
18-512 |
1.91e-155 |
|
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: 452.90 E-value: 1.91e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 18 NILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQEKEVGDGTTTAVVVAGEL 97
Cdd:cd03338 13 NIQAAKAVADAIRTSLGPRGMDKMIQTGKGEVIITNDGATILKQMSVLHPAAKMLVELSKAQDIEAGDGTTSVVVLAGAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 98 LRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQDKEILTKIAMTSITGKGAEKAKEKLAEIIVEAVSAVVD 177
Cdd:cd03338 93 LSACESLLKKGIHPTVISESFQIAAKKAVEILDSMSIPVDLNDRESLIKSATTSLNSKVVSQYSSLLAPIAVDAVLKVID 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 178 DEGKVDKDL--IKIEKKSGASIDDTELIKGVLVDKERV-SAQMPKKVTDAKIALLNCAIEIKETETDAEIRITDPAKLME 254
Cdd:cd03338 173 PATATNVDLkdIRIVKKLGGTIEDTELVDGLVFTQKASkKAGGPTRIEKAKIGLIQFCLSPPKTDMDNNIVVNDYAQMDR 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 255 FIEQEEKMLKDMVAEIKASGANVLFCQKGI-----DDLAQHYLAKEGIVAARRVKKSDMEKLAKATGANVIAAIAALSAQ 329
Cdd:cd03338 253 ILREERKYILNMCKKIKKSGCNVLLIQKSIlrdavSDLALHFLAKLKIMVVKDIEREEIEFICKTIGCKPVASIDHFTED 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 330 DLGDAGLVEERKISGDSMIFVEECKHP-KAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIVSGGGSTEVELSMK 408
Cdd:cd03338 333 KLGSADLVEEVSLGDGKIVKITGVKNPgKTVTILVRGSNKLVLDEAERSLHDALCVIRCLVKKRALIPGGGAPEIEIALQ 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 409 LREYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHAsNGNKCAGLNVFTGAVEDMCENGVVEPLRV 488
Cdd:cd03338 413 LSEWARTLTGVEQYCVRAFADALEVIPYTLAENAGLNPISIVTELRNRHA-QGEKNAGINVRKGAITNILEENVVQPLLV 491
|
490 500
....*....|....*....|....
3IZI_E 489 KTQAIQSAAESTEMLLRIDDVIAA 512
Cdd:cd03338 492 STSAITLATETVRMILKIDDIVLA 515
|
|
| chap_CCT_epsi |
TIGR02343 |
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ... |
4-513 |
2.06e-152 |
|
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: 445.79 E-value: 2.06e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 4 ENMKRYMGRDAQRMNILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQEKEV 83
Cdd:TIGR02343 18 DNKKRLKGLEAKKSNIAAAKSVASILRTSLGPKGMDKMLISPDGDITVTNDGATILSQMDVDNQIAKLMVELSKSQDDEI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 84 GDGTTTAVVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQD--KEILTKIAMTSITGKGAEKAK 161
Cdd:TIGR02343 98 GDGTTGVVVLAGALLEQAEELLDKGIHPIKIADGFEEAARIAVEHLEEISDEISADNnnREPLIQAAKTSLGSKIVSKCH 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 162 EKLAEIIVEAVSAVVDDEGK-VDKDLIKIEKKSGASIDDTELIKGVLVDKERVSAQMPKKVTDAKIALLNCAIEIKETET 240
Cdd:TIGR02343 178 RRFAEIAVDAVLNVADMERRdVDFDLIKVEGKVGGSLEDTKLIKGIIIDKDFSHPQMPKEVEDAKIAILTCPFEPPKPKT 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 241 DAEIRITDPAKLMEFIEQEEKMLKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATGANVI 320
Cdd:TIGR02343 258 KHKLDISSVEEYKKLQKYEQQKFKEMIDDIKKSGANLVICQWGFDDEANHLLLQNDLPAVRWVGGQELELIAIATGGRIV 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 321 AAIAALSAQDLGDAGLVEERKI--SGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIVSGG 398
Cdd:TIGR02343 338 PRFQELSKDKLGKAGLVREISFgtTKDRMLVIEQCKNSKAVTIFIRGGNKMIIEEAKRSIHDALCVVRNLIKDSRIVYGG 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 399 GSTEVELSMKLREYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHASNGNKCAGLNVFTGAVEDMC 478
Cdd:TIGR02343 418 GAAEISCSLAVSQEADKYPGVEQYAIRAFADALETIPMALAENSGLDPIGTLSTLKSLQLKEKNPNLGVDCLGYGTNDMK 497
|
490 500 510
....*....|....*....|....*....|....*
3IZI_E 479 ENGVVEPLRVKTQAIQSAAESTEMLLRIDDVIAAE 513
Cdd:TIGR02343 498 EQFVFETLIGKKQQILLATQLVRMILKIDDVISPG 532
|
|
| TCP1_eta |
cd03340 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ... |
18-513 |
8.21e-150 |
|
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: 438.64 E-value: 8.21e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 18 NILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQEKEVGDGTTTAVVVAGEL 97
Cdd:cd03340 21 NINACQAIADAVRTTLGPRGMDKLIVDGRGKVTISNDGATILKLLDIVHPAAKTLVDIAKSQDAEVGDGTTSVVVLAGEF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 98 LRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQDK----EILTKIAMTSITGKGAEKAKEKLAEIIVEAVS 173
Cdd:cd03340 101 LKEAKPFIEDGVHPQIIIRGYRKALQLAIEKIKEIAVNIDKEDKeeqrELLEKCAATALNSKLIASEKEFFAKMVVDAVL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 174 AVVDDegkVDKDLIKIEKKSGASIDDTELIKGVLVDKERVSA---QMPKKVTDAKIALLNCAIEIKETETDAEIRITDPA 250
Cdd:cd03340 181 SLDDD---LDLDMIGIKKVPGGSLEDSQLVNGVAFKKTFSYAgfeQQPKKFKNPKILLLNVELELKAEKDNAEVRVEDPE 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 251 KLMEFIEQEEKMLKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATGANVIAAIAALSAQD 330
Cdd:cd03340 258 EYQAIVDAEWKIIYDKLEKIVKSGANVVLSKLPIGDLATQYFADRDIFCAGRVPEEDLKRVAQATGGSIQTTVSNITDDV 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 331 LGDAGLVEERKISGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIVSGGGSTEVELSMKLR 410
Cdd:cd03340 338 LGTCGLFEERQVGGERYNIFTGCPKAKTCTIILRGGAEQFIEEAERSLHDAIMIVRRAIKNDSVVAGGGAIEMELSKYLR 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 411 EYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHASNGNKCAGLNVFTGAVEDMCENGVVEPLRVKT 490
Cdd:cd03340 418 DYSRTIAGKQQLVINAFAKALEIIPRQLCDNAGFDATDILNKLRQKHAQGGGKWYGVDINNEGIADNFEAFVWEPSLVKI 497
|
490 500
....*....|....*....|...
3IZI_E 491 QAIQSAAESTEMLLRIDDVIAAE 513
Cdd:cd03340 498 NALTAATEAACLILSVDETIKNP 520
|
|
| TCP1_alpha |
cd03335 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ... |
7-510 |
3.97e-144 |
|
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: 424.39 E-value: 3.97e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 7 KRYMGRDAQRMNILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQEKEVGDG 86
Cdd:cd03335 2 ERTSGQDVRTQNVTAAMAIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDKEVGDG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 87 TTTAVVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKA-QELLKTIACEVGAQDKEILTKIAMTSITGKGAEKAKEKLA 165
Cdd:cd03335 82 TTSVVIIAAELLKRANELVKQKIHPTTIISGYRLACKEAvKYIKEHLSISVDNLGKESLINVAKTSMSSKIIGADSDFFA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 166 EIIVEAVSAV--VDDEGKVDKDL--IKIEKKSGASIDDTELIKGVLVDKERVSAQMPKKVTDAKIALLNCAIEIKETETD 241
Cdd:cd03335 162 NMVVDAILAVktTNEKGKTKYPIkaVNILKAHGKSAKESYLVNGYALNCTRASQGMPTRVKNAKIACLDFNLQKTKMKLG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 242 AEIRITDPAKLMEFIEQEEKMLKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATGANVIA 321
Cdd:cd03335 242 VQVVVTDPEKLEKIRQRESDITKERIKKILAAGANVVLTTGGIDDMCLKYFVEAGAMAVRRVKKEDLRRIAKATGATLVS 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 322 AIAAL------SAQDLGDAGLVEERKISGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIV 395
Cdd:cd03335 322 TLANLegeetfDPSYLGEAEEVVQERIGDDELILIKGTKKRSSASIILRGANDFMLDEMERSLHDALCVVKRTLESNSVV 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 396 SGGGSTEVELSMKLREYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHAS-------NGNKCAGLN 468
Cdd:cd03335 402 PGGGAVETALSIYLENFATTLGSREQLAIAEFAEALLVIPKTLAVNAAKDATELVAKLRAYHAAaqvkpdkKHLKWYGLD 481
|
490 500 510 520
....*....|....*....|....*....|....*....|..
3IZI_E 469 VFTGAVEDMCENGVVEPLRVKTQAIQSAAESTEMLLRIDDVI 510
Cdd:cd03335 482 LINGKVRDNLEAGVLEPTVSKIKSLKFATEAAITILRIDDLI 523
|
|
| chap_CCT_gamma |
TIGR02344 |
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ... |
1-511 |
1.16e-143 |
|
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: 422.99 E-value: 1.16e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 1 VLPENMKRYMGRDAQRMNILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQE 80
Cdd:TIGR02344 4 VLNQNTKRESGRKAQLSNIQAAKAVADIIRTCLGPRSMLKMLLDPMGGIVMTNDGNAILREIDVAHPAAKSMIELSRTQD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 81 KEVGDGTTTAVVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQDKEILTKIAMTSITGKGAEKA 160
Cdd:TIGR02344 84 EEVGDGTTSVIILAGEMLSVAEPFLEQNIHPTVIIRAYRKALDDALSVLEEISIPVDVNDDAAMLKLIQSCIGTKFVSRW 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 161 KEKLAEIIVEAVSAVVDDEG---KVD-KDLIKIEKKSGASIDDTELIKGVLVDKERVSAQMPKKVTDAKIALLNCAIEIK 236
Cdd:TIGR02344 164 SDLMCDLALDAVRTVQRDENgrkEIDiKRYAKVEKIPGGDIEDSCVLKGVMINKDVTHPKMRRYIENPRIVLLDCPLEYK 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 237 ETETDAEIRITDPAKLMEFIEQEEKMLKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATG 316
Cdd:TIGR02344 244 KGESQTNIEITKEEDWNRILQMEEEYVQLMCEDIIAVKPDLVITEKGVSDLAQHYLLKANITAIRRVRKTDNNRIARACG 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 317 ANVIAAIAALSAQDLG-DAGLVEERKISGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIV 395
Cdd:TIGR02344 324 ATIVNRPEELRESDVGtGCGLFEVKKIGDEYFTFITECKDPKACTILLRGASKDILNEVERNLQDAMAVARNVLLDPKLV 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 396 SGGGSTEVELSMKLREYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHASNGNKCAGLNVFTGAVE 475
Cdd:TIGR02344 404 PGGGATEMAVSVALTEKSKKLEGVEQWPYRAVADALEIIPRTLAQNCGANVIRTLTELRAKHAQENNCTWGIDGETGKIV 483
|
490 500 510
....*....|....*....|....*....|....*.
3IZI_E 476 DMCENGVVEPLRVKTQAIQSAAESTEMLLRIDDVIA 511
Cdd:TIGR02344 484 DMKEKGIWEPLAVKLQTYKTAIESACLLLRIDDIVS 519
|
|
| TCP1_gamma |
cd03337 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ... |
1-512 |
1.84e-143 |
|
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: 420.93 E-value: 1.84e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 1 VLPENMKRYMGRDAQRMNILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQE 80
Cdd:cd03337 4 VLNQNTKRESGRKAQLGNIQAAKTVADVIRTCLGPRAMLKMLLDPMGGIVLTNDGNAILREIDVAHPAAKSMIELSRTQD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 81 KEVGDGTTTAVVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQDKEILTKIAMTSITGKGAEKA 160
Cdd:cd03337 84 EEVGDGTTSVIILAGEILAVAEPFLERGIHPTVIIKAYRKALEDALKILEEISIPVDVNDRAQMLKIIKSCIGTKFVSRW 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 161 KEKLAEIIVEAVSAV-VDDEGKVD----KDLIKIEKKSGASIDDTELIKGVLVDKERVSAQMPKKVTDAKIALLNCAIEI 235
Cdd:cd03337 164 SDLMCNLALDAVKTVaVEENGRKKeidiKRYAKVEKIPGGEIEDSRVLDGVMLNKDVTHPKMRRRIENPRIVLLDCPLEY 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 236 ketetdaeiritdpaklmefieqeekmlkdmvaeikasganVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKAT 315
Cdd:cd03337 244 -----------------------------------------LVITEKGVSDLAQHYLVKAGITALRRVRKTDNNRIARAC 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 316 GANVIAAIAALSAQDLGDAGLVEERKISGDSMI-FVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRI 394
Cdd:cd03337 283 GATIVNRPEELTESDVGTGAGLFEVKKIGDEYFtFITECKDPKACTILLRGASKDVLNEVERNLQDAMAVARNIILNPKL 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 395 VSGGGSTEVELSMKLREYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHASNGNKCAGLNVFTGAV 474
Cdd:cd03337 363 VPGGGATEMAVSHALSEKAKSIEGVEQWPYKAVASALEVIPRTLAQNCGANVIRTLTELRAKHAQGENSTWGIDGETGDI 442
|
490 500 510
....*....|....*....|....*....|....*...
3IZI_E 475 EDMCENGVVEPLRVKTQAIQSAAESTEMLLRIDDVIAA 512
Cdd:cd03337 443 VDMKELGIWDPLAVKAQTYKTAIEAACMLLRIDDIVSG 480
|
|
| chap_CCT_eta |
TIGR02345 |
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ... |
18-513 |
2.26e-138 |
|
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: 409.53 E-value: 2.26e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 18 NILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQEKEVGDGTTTAVVVAGEL 97
Cdd:TIGR02345 23 NINACVAIAEALKTTLGPRGMDKLIVGSNGKATISNDGATILKLLDIVHPAAKTLVDIAKSQDAEVGDGTTSVTILAGEL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 98 LRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQD---KEILTKIAMTSITGKGAEKAKEKLAEIIVEAVSA 174
Cdd:TIGR02345 103 LKEAKPFIEEGVHPQLIIRCYREALSLAVEKIKEIAVTIDEEKgeqRELLEKCAATALSSKLISHNKEFFSKMIVDAVLS 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 175 VVDDEgkVDKDLIKIEKKSGASIDDTELIKGVLVDKERVSA---QMPKKVTDAKIALLNCAIEIKETETDAEIRITDPAK 251
Cdd:TIGR02345 183 LDRDD--LDLKLIGIKKVQGGALEDSQLVNGVAFKKTFSYAgfeQQPKKFANPKILLLNVELELKAEKDNAEIRVEDVED 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 252 LMEFIEQEEKMLKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATGANVIAAIAALSAQDL 331
Cdd:TIGR02345 261 YQAIVDAEWAIIFRKLEKIVESGANVVLSKLPIGDLATQYFADRDIFCAGRVSAEDLKRVIKACGGSIQSTTSDLEADVL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 332 GDAGLVEERKISGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIVSGGGSTEVELSMKLRE 411
Cdd:TIGR02345 341 GTCALFEERQIGSERYNYFTGCPHAKTCTIILRGGAEQFIEEAERSLHDAIMIVRRALKNKKIVAGGGAIEMELSKCLRD 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 412 YAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHAsNGNKCAGLNVFTGAVEDMCENGVVEPLRVKTQ 491
Cdd:TIGR02345 421 YSKTIDGKQQLIINAFAKALEIIPRQLCENAGFDSIEILNKLRSRHA-KGGKWYGVDINTEDIGDNFEAFVWEPALVKIN 499
|
490 500
....*....|....*....|..
3IZI_E 492 AIQSAAESTEMLLRIDDVIAAE 513
Cdd:TIGR02345 500 ALKAAFEAACTILSVDETITNP 521
|
|
| chap_CCT_delta |
TIGR02342 |
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ... |
13-512 |
5.01e-137 |
|
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: 406.09 E-value: 5.01e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 13 DAQRMNILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQEKEVGDGTTTAVV 92
Cdd:TIGR02342 9 DVRTSNIVAAKAVADAIRTSLGPKGMDKMIQDGKGEVIITNDGATILKQMAVLHPAAKMLVELSKAQDIEAGDGTTSVVI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 93 VAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQDKEILTKIAMTSITGKGAEKAKEKLAEIIVEAV 172
Cdd:TIGR02342 89 LAGALLGACERLLNKGIHPTIISESFQSAADEAIKILDEMSIPVDLSDREQLLKSATTSLSSKVVSQYSSLLAPLAVDAV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 173 SAVVDDEGKVDKDL--IKIEKKSGASIDDTELIKGVLVD-KERVSAQMPKKVTDAKIALLNCAIEIKETETDAEIRITDP 249
Cdd:TIGR02342 169 LKVIDPENAKNVDLndIKVVKKLGGTIDDTELIEGLVFTqKASKSAGGPTRIEKAKIGLIQFQISPPKTDMENQIIVNDY 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 250 AKLMEFIEQEEKMLKDMVAEIKASGANVLFCQKGI-----DDLAQHYLAKEGIVAARRVKKSDMEKLAKATGANVIAAIA 324
Cdd:TIGR02342 249 AQMDRVLKEERAYILNIVKKIKKTGCNVLLIQKSIlrdavNDLALHFLAKMKIMVVKDIEREEIEFICKTIGCKPIASID 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 325 ALSAQDLGDAGLVEERKISGDSMIFVEECKHP-KAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIVSGGGSTEV 403
Cdd:TIGR02342 329 HFTADKLGSAELVEEVDSDGGKIIKITGIQNAgKTVTVVVRGSNKLVIDEAERSLHDALCVIRCLVKKRGLIAGGGAPEI 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 404 ELSMKLREYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHAsNGNKCAGLNVFTGAVEDMCENGVV 483
Cdd:TIGR02342 409 EIARRLSKYARTMKGVESYCVRAFADALEVIPYTLAENAGLNPIKVVTELRNRHA-NGEKTAGISVRKGGITNMLEEHVL 487
|
490 500
....*....|....*....|....*....
3IZI_E 484 EPLRVKTQAIQSAAESTEMLLRIDDVIAA 512
Cdd:TIGR02342 488 QPLLVTTSAITLASETVRSILKIDDIVFT 516
|
|
| chap_CCT_alpha |
TIGR02340 |
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ... |
7-510 |
5.37e-137 |
|
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: 406.41 E-value: 5.37e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 7 KRYMGRDAQRMNILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQEKEVGDG 86
Cdd:TIGR02340 6 ERTSGQDVRTQNVTAAMAIANIVKTSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDREVGDG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 87 TTTAVVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKA-QELLKTIACEVGAQDKEILTKIAMTSITGKGAEKAKEKLA 165
Cdd:TIGR02340 86 TTSVVIIAAELLKRADELVKNKIHPTSVISGYRLACKEAvKYIKENLSVSVDELGREALINVAKTSMSSKIIGLDSDFFS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 166 EIIVEAVSAV--VDDEGKVDKDL--IKIEKKSGASIDDTELIKGVLVDKERVSAQMPKKVTDAKIALLNCAIEIKETETD 241
Cdd:TIGR02340 166 NIVVDAVLAVktTNENGETKYPIkaINILKAHGKSARESMLVKGYALNCTVASQQMPKRIKNAKIACLDFNLQKAKMALG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 242 AEIRITDPAKLMEFIEQEEKMLKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATGANVIA 321
Cdd:TIGR02340 246 VQIVVDDPEKLEQIRQREADITKERIKKILDAGANVVLTTGGIDDMCLKYFVEAGAMGVRRCKKEDLKRIAKATGATLVS 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 322 AIAALSAQD------LGDAGLVEERKISGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIV 395
Cdd:TIGR02340 326 TLADLEGEEtfeasyLGFADEVVQERIADDECILIKGTKKRKSASIILRGANDFMLDEMERSLHDALCVVKRTLESNSVV 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 396 SGGGSTEVELSMKLREYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHAS-------NGNKCAGLN 468
Cdd:TIGR02340 406 PGGGAVEAALSIYLENFATTLGSREQLAIAEFARALLIIPKTLAVNAAKDSTELVAKLRAYHAAaqlkpekKHLKWYGLD 485
|
490 500 510 520
....*....|....*....|....*....|....*....|..
3IZI_E 469 VFTGAVEDMCENGVVEPLRVKTQAIQSAAESTEMLLRIDDVI 510
Cdd:TIGR02340 486 LVNGKIRDNKEAGVLEPTVSKVKSLKFATEAAITILRIDDLI 527
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
1-512 |
4.43e-122 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 368.20 E-value: 4.43e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 1 VLPENMKRYMGRDAQRMNILAGRIIAETVRSTLGPKGMDKMLV-----DDLGDVVVTNDGVTILREMSVEHPAAKMLIEV 75
Cdd:PTZ00212 10 VLKQGAQEEKGETARLQSFVGAIAVADLVKTTLGPKGMDKILQpmsegPRSGNVTVTNDGATILKSVWLDNPAAKILVDI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 76 AKTQEKEVGDGTTTAVVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQD---KEILTKIAMTSI 152
Cdd:PTZ00212 90 SKTQDEEVGDGTTSVVVLAGELLREAEKLLDQKIHPQTIIEGWRMALDVARKALEEIAFDHGSDEekfKEDLLNIARTTL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 153 TGKGAEKAKEKLAEIiveAVSAVVDDEGKVDKDLIKIEKKSGASIDDTELIKGVLVDKeRVSAQMPKKVTDAKIALLNCA 232
Cdd:PTZ00212 170 SSKLLTVEKDHFAKL---AVDAVLRLKGSGNLDYIQIIKKPGGTLRDSYLEDGFILEK-KIGVGQPKRLENCKILVANTP 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 233 IEiketeTD------AEIRITDPAKLMEfIEQEEKM-LKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVKK 305
Cdd:PTZ00212 246 MD-----TDkikiygAKVKVDSMEKVAE-IEAAEKEkMKNKVDKILAHGCNVFINRQLIYNYPEQLFAEAGIMAIEHADF 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 306 SDMEKLAKATGANVIAAIAALSAQDLGDAGLVEERKISGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVV 385
Cdd:PTZ00212 320 DGMERLAAALGAEIVSTFDTPEKVKLGHCDLIEEIMIGEDKLIRFSGCAKGEACTIVLRGASTHILDEAERSLHDALCVL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 386 GCTIEDGRIVSGGGSTEVELSMKLREYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHAsNGNKCA 465
Cdd:PTZ00212 400 SQTVKDTRVVLGGGCSEMLMANAVEELAKKVEGKKSLAIEAFAKALRQIPTIIADNGGYDSAELVSKLRAEHY-KGNKTA 478
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
3IZI_E 466 GLNVFTGAVEDMCENGVVEPLRVKTQAIQSAAESTEMLLRIDDVIAA 512
Cdd:PTZ00212 479 GIDMEKGTVGDMKELGITESYKVKLSQLCSATEAAEMILRVDDIIRC 525
|
|
| TCP1_beta |
cd03336 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ... |
1-512 |
4.91e-119 |
|
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: 359.72 E-value: 4.91e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 1 VLPENMKRYMGRDAQRMNILAGRIIAETVRSTLGPKGMDKML--VDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKT 78
Cdd:cd03336 1 ILKDGAQEEKGETARLSSFVGAIAIGDLVKTTLGPKGMDKILqsVGRSGGVTVTNDGATILKSIGVDNPAAKVLVDISKV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 79 QEKEVGDGTTTAVVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQD---KEILTKIAMTSITGK 155
Cdd:cd03336 81 QDDEVGDGTTSVTVLAAELLREAEKLVAQKIHPQTIIEGYRMATAAAREALLSSAVDHSSDEeafREDLLNIARTTLSSK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 156 GAEKAKEKLAEIiveAVSAVVDDEGKVDKDLIKIEKKSGASIDDTELIKGVLVDKeRVSAQMPKKVTDAKIALLNCAIei 235
Cdd:cd03336 161 ILTQDKEHFAEL---AVDAVLRLKGSGNLDAIQIIKKLGGSLKDSYLDEGFLLDK-KIGVNQPKRIENAKILIANTPM-- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 236 ketETD------AEIRITDPAKLMEfIEQEEKM-LKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDM 308
Cdd:cd03336 235 ---DTDkikifgAKVRVDSTAKVAE-IEEAEKEkMKNKVEKILKHGINCFINRQLIYNYPEQLFADAGIMAIEHADFDGV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 309 EKLAKATGANVIAAIAALSAQDLGDAGLVEERKISGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCT 388
Cdd:cd03336 311 ERLALVTGGEIASTFDHPELVKLGTCKLIEEIMIGEDKLIRFSGVAAGEACTIVLRGASQQILDEAERSLHDALCVLAQT 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 389 IEDGRIVSGGGSTEVELSMKLREYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHAsNGNKCAGLN 468
Cdd:cd03336 391 VKDTRVVLGGGCSEMLMAKAVEELAKKTPGKKSLAIEAFAKALRQLPTIIADNAGYDSAELVAQLRAAHY-NGNTTAGLD 469
|
490 500 510 520
....*....|....*....|....*....|....*....|....
3IZI_E 469 VFTGAVEDMCENGVVEPLRVKTQAIQSAAESTEMLLRIDDVIAA 512
Cdd:cd03336 470 MRKGTVGDMKELGITESFKVKRQVLLSASEAAEMILRVDDIIKC 513
|
|
| TCP1_zeta |
cd03342 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
14-512 |
4.52e-117 |
|
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: 353.49 E-value: 4.52e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 14 AQRMNILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQEKEVGDGTTTAVVV 93
Cdd:cd03342 13 ALAVNISAAKGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLSEMQIQHPTASMIARAATAQDDITGDGTTSNVLL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 94 AGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVG-AQDKEILTKIAMTSITGKGAEKAKEKLAEIIVEAV 172
Cdd:cd03342 93 IGELLKQAERYIQEGVHPRIITEGFELAKNKALKFLESFKVPVEiDTDRELLLSVARTSLRTKLHADLADQLTEIVVDAV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 173 SAVVDDEGKVDKDLIKIEKKSGASIDDTELIKGVLVDKERVSAQMPKKVTDAKIALLNCAIEIKETETDAEiritdpakl 252
Cdd:cd03342 173 LAIYKPDEPIDLHMVEIMQMQHKSDSDTKLIRGLVLDHGARHPDMPKRVENAYILTCNVSLEYEKTEVNSG--------- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 253 meFIeqeekmlkdmvaeikasgANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATGANVIAAIAALSAQDLG 332
Cdd:cd03342 244 --FF------------------YSVVINQKGIDPPSLDMLAKEGILALRRAKRRNMERLTLACGGVAMNSVDDLSPECLG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 333 DAGLVEERKISGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIVSGGGSTEVELSMKLREY 412
Cdd:cd03342 304 YAGLVYERTLGEEKYTFIEGVKNPKSCTILIKGPNDHTITQIKDAIRDGLRAVKNAIEDKCVVPGAGAFEVALYAHLKEF 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 413 AEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHASnGNKCAGLNVFTGAVEDMCENGVVEPLRVKTQA 492
Cdd:cd03342 384 KKSVKGKAKLGVQAFADALLVIPKTLAENSGLDVQETLVKLQDEYAE-GGQVGGVDLDTGEPMDPESEGIWDNYSVKRQI 462
|
490 500
....*....|....*....|
3IZI_E 493 IQSAAESTEMLLRIDDVIAA 512
Cdd:cd03342 463 LHSATVIASQLLLVDEIIRA 482
|
|
| chap_CCT_theta |
TIGR02346 |
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ... |
18-512 |
7.63e-115 |
|
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: 349.40 E-value: 7.63e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 18 NILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQEKEVGDGTTTAVVVAGEL 97
Cdd:TIGR02346 23 NIEACKELSQITRTSLGPNGMNKMVINHLEKLFVTNDAATILRELEVQHPAAKLLVMASEMQENEIGDGTNLVLVLAGEL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 98 LRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKT-IACEV-GAQDKEILTKIAMTSITGKGAEKAkEKLAEIIVEAVSAV 175
Cdd:TIGR02346 103 LNKAEELIRMGLHPSEIIKGYEMALKKAMEILEElVVWEVkDLRDKDELIKALKASISSKQYGNE-DFLAQLVAQACSTV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 176 V-DDEGKVDKDLIKIEKKSGASIDDTELIKGVLVDKERVSAQmpKKVTDAKIALLNCAIEIKETETDAEIRITDPAKLME 254
Cdd:TIGR02346 182 LpKNPQNFNVDNIRVCKILGGSLSNSEVLKGMVFNREAEGSV--KSVKNAKVAVFSCPLDTATTETKGTVLIHNAEELLN 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 255 FIEQEEKMLKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATGANVIAAIAALSAQDLGDA 334
Cdd:TIGR02346 260 YSKGEENQIEAMIKAIADSGVNVIVTGGSVGDMALHYLNKYNIMVLKIPSKFELRRLCKTVGATPLPRLGAPTPEEIGYV 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 335 GLVEERKISGDSM-IFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIVSGGGSTEVELSMKLREYA 413
Cdd:TIGR02346 340 DSVYVSEIGGDKVtVFKQENGDSKISTIILRGSTDNLLDDIERAIDDGVNTVKALVKDGRLLPGAGATEIELASRLTKYG 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 414 EGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHASnGNKCAGLNVFTG--AVEDMCENGVVEPLRVKTQ 491
Cdd:TIGR02346 420 EKLPGLDQYAIKKFAEAFEIIPRTLAENAGLNANEVIPKLYAAHKK-GNKSKGIDIEAEsdGVKDASEAGIYDMLATKKW 498
|
490 500
....*....|....*....|.
3IZI_E 492 AIQSAAESTEMLLRIDDVIAA 512
Cdd:TIGR02346 499 AIKLATEAAVTVLRVDQIIMA 519
|
|
| chap_CCT_zeta |
TIGR02347 |
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ... |
14-512 |
1.13e-114 |
|
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: 349.03 E-value: 1.13e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 14 AQRMNILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQEKEVGDGTTTAVVV 93
Cdd:TIGR02347 17 ALMMNINAARGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEMQIQHPTASMIARAATAQDDITGDGTTSTVLL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 94 AGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQ-DKEILTKIAMTSITGKGAEKAKEKLAEIIVEAV 172
Cdd:TIGR02347 97 IGELLKQAERYILEGVHPRIITEGFEIARKEALQFLDKFKVKKEDEvDREFLLNVARTSLRTKLPADLADQLTEIVVDAV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 173 SAVVDDEGKVDKDLIKIEKKSGASIDDTELIKGVLVDKERVSAQMPKKVTDAKIALLNCAIEIKETETDAEIRITDPAKL 252
Cdd:TIGR02347 177 LAIKKDGEDIDLFMVEIMEMKHKSATDTTLIRGLVLDHGARHPDMPRRVKNAYILTCNVSLEYEKTEVNSGFFYSSAEQR 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 253 MEFIEQEEKMLKDMVAEI-----KASGAN-----VLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATGANVIAA 322
Cdd:TIGR02347 257 EKLVKAERKFVDDRVKKIielkkKVCGKSpdkgfVVINQKGIDPPSLDLLAKEGIMALRRAKRRNMERLTLACGGEALNS 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 323 IAALSAQDLGDAGLVEERKISGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIVSGGGSTE 402
Cdd:TIGR02347 337 VEDLTPECLGWAGLVYETTIGEEKYTFIEECKNPKSCTILIKGPNDHTIAQIKDAVRDGLRAVKNAIEDKCVVPGAGAFE 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 403 VELSMKLREYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHaSNGNKCAGLNVFTGAVEDMCENGV 482
Cdd:TIGR02347 417 IAAYRHLKEYKKSVKGKAKLGVEAFANALLVIPKTLAENSGFDAQDTLVKLEDEH-DEGGEVVGVDLNTGEPIDPEIKGI 495
|
490 500 510
....*....|....*....|....*....|
3IZI_E 483 VEPLRVKTQAIQSAAESTEMLLRIDDVIAA 512
Cdd:TIGR02347 496 WDNYRVKKQLIQSATVIASQLLLVDEVMRA 525
|
|
| TCP1_theta |
cd03341 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ... |
18-512 |
1.35e-114 |
|
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: 346.90 E-value: 1.35e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 18 NILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQEKEVGDGTTTAVVVAGEL 97
Cdd:cd03341 13 NIEACKELSQITRTSYGPNGMNKMVINHLEKLFVTSDAATILRELEVQHPAAKLLVMASQMQEEEIGDGTNLVVVLAGEL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 98 LRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACE--VGAQDKEILTKIAMTSITGKGAEKAkEKLAEIIVEAVSAV 175
Cdd:cd03341 93 LEKAEELLRMGLHPSEIIEGYEKALKKALEILEELVVYkiEDLRNKEEVSKALKTAIASKQYGNE-DFLSPLVAEACISV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 176 V-DDEGKVDKDLIKIEKKSGASIDDTELIKGVLVDKErVSAQMpKKVTDAKIALLNCAIEIketetdaeiritdpaklme 254
Cdd:cd03341 172 LpENIGNFNVDNIRVVKILGGSLEDSKVVRGMVFKRE-PEGSV-KRVKKAKVAVFSCPFDI------------------- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 255 fieqeekmlkdmvaeikasGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATGANVIAAIAALSAQDLGDA 334
Cdd:cd03341 231 -------------------GVNVIVAGGSVGDLALHYCNKYGIMVIKINSKFELRRLCRTVGATPLPRLGAPTPEEIGYC 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 335 GLVEERKISGDSMIFVEECKHPKAV-TMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIVSGGGSTEVELSMKLREYA 413
Cdd:cd03341 292 DSVYVEEIGDTKVVVFRQNKEDSKIaTIVLRGATQNILDDVERAIDDGVNVFKSLTKDGRFVPGAGATEIELAKKLKEYG 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 414 EGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHaSNGNKCAGLNVFTG--AVEDMCENGVVEPLRVKTQ 491
Cdd:cd03341 372 EKTPGLEQYAIKKFAEAFEVVPRTLAENAGLDATEVLSELYAAH-QKGNKSAGVDIESGdeGTKDAKEAGIFDHLATKKW 450
|
490 500
....*....|....*....|.
3IZI_E 492 AIQSAAESTEMLLRIDDVIAA 512
Cdd:cd03341 451 AIKLATEAAVTVLRVDQIIMA 471
|
|
| chap_CCT_beta |
TIGR02341 |
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ... |
16-512 |
1.74e-93 |
|
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT beta chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.
Pssm-ID: 274082 Cd Length: 519 Bit Score: 294.07 E-value: 1.74e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 16 RMNILAGRI-IAETVRSTLGPKGMDKMLVDD--LGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQEKEVGDGTTTAVV 92
Cdd:TIGR02341 16 RLSSFVGAIaIGDLVKSTLGPKGMDKILQSSssDASIMVTNDGATILKSIGVDNPAAKVLVDMSKVQDDEVGDGTTSVTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 93 VAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQDKEI---LTKIAMTSITGKGAEKAKEKLAEIiv 169
Cdd:TIGR02341 96 LAAELLREAEKLINQKIHPQTIIAGYREATKAARDALLKSAVDNGSDEVKFrqdLMNIARTTLSSKILSQHKDHFAQL-- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 170 eAVSAVVDDEGKVDKDLIKIEKKSGASIDDTELIKGVLVDKeRVSAQMPKKVTDAKIALLNCAIEIKETET-DAEIRITD 248
Cdd:TIGR02341 174 -AVDAVLRLKGSGNLEAIQIIKKLGGSLADSYLDEGFLLDK-KIGVNQPKRIENAKILIANTGMDTDKVKIfGSRVRVDS 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 249 PAKLMEFIEQEEKMLKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATGANVIAAIAALSA 328
Cdd:TIGR02341 252 TAKVAELEHAEKEKMKEKVEKILKHGINCFINRQLIYNYPEQLFADAGVMAIEHADFEGVERLALVTGGEIVSTFDHPEL 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 329 QDLGDAGLVEERKISGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIVSGGGSTEVELSMK 408
Cdd:TIGR02341 332 VKLGSCDLIEEIMIGEDKLLKFSGVKLGEACTIVLRGATQQILDEAERSLHDALCVLSQTVKESRTVLGGGCSEMLMSKA 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 409 LREYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHAsNGNKCAGLNVFTGAVEDMCENGVVEPLRV 488
Cdd:TIGR02341 412 VTQEAQRTPGKEALAVEAFARALRQLPTIIADNAGFDSAELVAQLRAAHY-NGNTTMGLDMNEGTIADMRQLGITESYKV 490
|
490 500
....*....|....*....|....
3IZI_E 489 KTQAIQSAAESTEMLLRIDDVIAA 512
Cdd:TIGR02341 491 KRAVVSSAAEAAEVILRVDNIIKA 514
|
|
| chaperonin_like |
cd03333 |
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ... |
141-391 |
5.60e-70 |
|
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: 222.34 E-value: 5.60e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 141 KEILTKIAMTSITGKGaEKAKEKLAEIIVEAVSAVVDDEGKVDKDLIKIEKKSGASIDDTELIKGVLVDKERVSAQMPKK 220
Cdd:cd03333 1 RELLLQVATTSLNSKL-SSWDDFLGKLVVDAVLKVGPDNRMDDLGVIKVEKIPGGSLEDSELVVGVVFDKGYASPYMPKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 221 VTDAKIALLNCAIEiketetdaeiritdpaklmefieqeekmlkdmvaeikasgaNVLFCQKGIDDLAQHYLAKEGIVAA 300
Cdd:cd03333 80 LENAKILLLDCPLE-----------------------------------------YVVIAEKGIDDLALHYLAKAGIMAV 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 301 RRVKKSDMEKLAKATGANVIAAIAALSAQDLGDAGLVEERKISGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDD 380
Cdd:cd03333 119 RRVKKEDLERIARATGATIVSSLEDLTPEDLGTAELVEETKIGEEKLTFIEGCKGGKAATILLRGATEVELDEVKRSLHD 198
|
250
....*....|.
3IZI_E 381 AVGVVGCTIED 391
Cdd:cd03333 199 ALCAVRAAVEE 209
|
|
| GroEL |
cd03344 |
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ... |
16-497 |
7.22e-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: 131.42 E-value: 7.22e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 16 RMNILAG-RIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHP----AAKMLIEVAKTQEKEVGDGTTTA 90
Cdd:cd03344 10 RKALLRGvNKLADAVKVTLGPKGRNVVIEKSFGSPKITKDGVTVAKEIELEDPfenmGAQLVKEVASKTNDVAGDGTTTA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 91 VVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVgaQDKEILTKIAMTSITGkgaekaKEKLAEIIVE 170
Cdd:cd03344 90 TVLARAIIKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKPV--KTKEEIAQVATISANG------DEEIGELIAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 171 AVSavvddegKVDKD-LIKIEkkSGASIDDT-ELIKGVLVDKERVSaqmPKKVTDAK---IALLNCAIEIketeTDAEIR 245
Cdd:cd03344 162 AME-------KVGKDgVITVE--EGKTLETElEVVEGMQFDRGYLS---PYFVTDPEkmeVELENPYILL----TDKKIS 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 246 -ITDPAKLMEFIEQEEKMLKdMVAEikasganvlfcqkgidDLAQHYLA------KEGIVAARRVK--------KSDMEK 310
Cdd:cd03344 226 sIQELLPILELVAKAGRPLL-IIAE----------------DVEGEALAtlvvnkLRGGLKVCAVKapgfgdrrKAMLED 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 311 LAKATGANVIA-----AIAALSAQDLGDAGLVEerkISGDSMIFVEECKHPKAV-------------------------- 359
Cdd:cd03344 289 IAILTGGTVISeelglKLEDVTLEDLGRAKKVV---VTKDDTTIIGGAGDKAAIkariaqirkqieettsdydkeklqer 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 360 -------TMLIR--GTTEHVIEEVARAVDDAVGVVGCTIEDGrIVSGGGSTEVELSMKLrEYAEGISGREQLAVRAFADA 430
Cdd:cd03344 366 laklsggVAVIKvgGATEVELKEKKDRVEDALNATRAAVEEG-IVPGGGVALLRASPAL-DKLKALNGDEKLGIEIVRRA 443
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
3IZI_E 431 LEVIPRTLAENAGLDAIEILVKVRaahasNGNKCAGLNVFTGAVEDMCENGVVEPLRVKTQAIQSAA 497
Cdd:cd03344 444 LEAPLRQIAENAGVDGSVVVEKVL-----ESPDGFGYDAATGEYVDMIEAGIIDPTKVVRSALQNAA 505
|
|
| groEL |
PRK12849 |
chaperonin GroEL; Reviewed |
12-511 |
7.06e-31 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237230 Cd Length: 542 Bit Score: 125.69 E-value: 7.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 12 RDAQRMNILAG-RIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHP----AAKMLIEVAKTQEKEVGDG 86
Cdd:PRK12849 8 DEEARRALERGvNKLADAVKVTLGPKGRNVVIDKSFGAPTITKDGVSIAKEIELEDPfenlGAQLVKEVASKTNDVAGDG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 87 TTTAVVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVgaQDKEILTKIAMTSITGkgaekaKEKLAE 166
Cdd:PRK12849 88 TTTATVLAQALVQEGLKNVAAGANPMDLKRGIDKAVEAVVEELKALARPV--SGSEEIAQVATISANG------DEEIGE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 167 IIVEAVSavvddegKVDKD-LIKIEKKSGASiDDTELIKGVLVDKERVSAQMpkkVTDAK--IALL-NCAIEIketeTDA 242
Cdd:PRK12849 160 LIAEAME-------KVGKDgVITVEESKTLE-TELEVTEGMQFDRGYLSPYF---VTDPErmEAVLeDPLILL----TDK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 243 EIR-ITDPAKLMEFIEQEEKMLKdMVAEikasganvlfcqkgidDLAQHYLA-------KEGI-VAA--------RRvkK 305
Cdd:PRK12849 225 KISsLQDLLPLLEKVAQSGKPLL-IIAE----------------DVEGEALAtlvvnklRGGLkVAAvkapgfgdRR--K 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 306 SDMEKLAKATGANVIA-----AIAALSAQDLGDAGLVEerkISGDSMIFVEECKHPKAV--------------------- 359
Cdd:PRK12849 286 AMLEDIAILTGGTVISedlglKLEEVTLDDLGRAKRVT---ITKDNTTIVDGAGDKEAIearvaqirrqieettsdydre 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 360 ------------TMLIR--GTTEHVIEEVARAVDDAVGVVGCTIEDGrIVSGGGSTEVELSMKLREYAeGISGREQLAVR 425
Cdd:PRK12849 363 klqerlaklaggVAVIKvgAATEVELKERKDRVEDALNATRAAVEEG-IVPGGGVALLRAAKALDELA-GLNGDQAAGVE 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 426 AFADALEVIPRTLAENAGLDAIEILVKVRAahasnGNKCAGLNVFTGAVEDMCENGVVEPLRVKTQAIQSAAESTEMLLR 505
Cdd:PRK12849 441 IVRRALEAPLRQIAENAGLDGSVVVAKVLE-----LEDGFGFNAATGEYGDLIAAGIIDPVKVTRSALQNAASVAGLLLT 515
|
....*.
3IZI_E 506 IDDVIA 511
Cdd:PRK12849 516 TEALVA 521
|
|
| Fab1_TCP |
cd03334 |
TCP-1 like domain of the eukaryotic phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinase Fab1. ... |
154-385 |
4.45e-26 |
|
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: 106.92 E-value: 4.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 154 GKGAEKAKEKLAEIIVEAVSAVVDDEGKVDKDLI----KIEKKSGASIDDTELIKGVLVDKERVSAQMPKKVTDAKIALL 229
Cdd:cd03334 13 ISNDESWLDILLPLVWKAASNVKPDVRAGDDMDIrqyvKIKKIPGGSPSDSEVVDGVVFTKNVAHKRMPSKIKNPRILLL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 230 NCAIEIKETETdaeiritdpaKLMEF---IEQEEKMLKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKS 306
Cdd:cd03334 93 QGPLEYQRVEN----------KLLSLdpvILQEKEYLKNLVSRIVALRPDVILVEKSVSRIAQDLLLEAGITLVLNVKPS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 307 DMEKLAKATGANVIAAIAALSA-QDLGDAGLVEERKI-----SGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDD 380
Cdd:cd03334 163 VLERISRCTGADIISSMDDLLTsPKLGTCESFRVRTYveehgRSKTLMFFEGCPKELGCTILLRGGDLEELKKVKRVVEF 242
|
....*
3IZI_E 381 AVGVV 385
Cdd:cd03334 243 MVFAA 247
|
|
| GroEL |
TIGR02348 |
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ... |
7-511 |
1.47e-25 |
|
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: 110.08 E-value: 1.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 7 KRYMGRDAQRMNILAG-RIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHP----AAKMLIEVAKTQEK 81
Cdd:TIGR02348 2 KQIKFDEEARKALLRGvDKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDKfenmGAQLVKEVASKTND 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 82 EVGDGTTTAVVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGaqDKEILTKIAMTSITGkgaekaK 161
Cdd:TIGR02348 82 VAGDGTTTATVLAQAIVKEGLKNVAAGANPIELKRGIEKAVEAVVEELKKLSKPVK--GKKEIAQVATISANN------D 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 162 EKLAEIIVEAVSavvddegKVDKD-LIKIEKKSGAsIDDTELIKGVLVDKERVSaqmPKKVTDAkiallncaiEIKETE- 239
Cdd:TIGR02348 154 EEIGSLIAEAME-------KVGKDgVITVEESKSL-ETELEVVEGMQFDRGYIS---PYFVTDA---------EKMEVEl 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 240 TDAEIRITDpaklmefieQEEKMLKDMV---AEIKASGANVLFCQKGIDDLAQHYLA---KEGIVAARRVK--------K 305
Cdd:TIGR02348 214 ENPYILITD---------KKISNIKDLLpllEKVAQSGKPLLIIAEDVEGEALATLVvnkLRGTLNVCAVKapgfgdrrK 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 306 SDMEKLAKATGANVIA-----AIAALSAQDLGDAGLVeerKISGDSMIFVEECKHPKAVTMLIR---------------- 364
Cdd:TIGR02348 285 AMLEDIAILTGGQVISeelglKLEEVTLDDLGKAKKV---TVDKDNTTIVEGAGDKAAIKARVAqikaqieettsdydre 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 365 -------------------GTTEHVIEEVARAVDDAVGVVGCTIEDGrIVSGGGSTEVELSMKLrEYAEGISGREQLAVR 425
Cdd:TIGR02348 362 klqerlaklaggvavikvgAATETEMKEKKLRIEDALNATRAAVEEG-IVPGGGVALLRAAAAL-EGLKGDGEDEAIGID 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 426 AFADALEVIPRTLAENAGLDAIEILVKVRaahASNGNKcaGLNVFTGAVEDMCENGVVEPLRVKTQAIQSAAESTEMLLR 505
Cdd:TIGR02348 440 IVKRALEAPLRQIAENAGLDGAVVAEKVK---ELKGNF--GFNAATGEYEDLVEAGIIDPTKVTRSALQNAASIAGLLLT 514
|
....*.
3IZI_E 506 IDDVIA 511
Cdd:TIGR02348 515 TEAVVA 520
|
|
| groEL |
PRK12850 |
chaperonin GroEL; Reviewed |
24-513 |
1.40e-23 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237231 Cd Length: 544 Bit Score: 104.03 E-value: 1.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 24 IIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHP----AAKMLIEVAKTQEKEVGDGTTTAVVVAGELLR 99
Cdd:PRK12850 22 ILANAVKVTLGPKGRNVVLEKSFGAPRITKDGVTVAKEIELEDKfenmGAQMVKEVASKTNDLAGDGTTTATVLAQAIVR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 100 KAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQDKeiLTKIAMTSITGkgaekaKEKLAEIIVEAVSavvdde 179
Cdd:PRK12850 102 EGAKLVAAGMNPMDLKRGIDLAVAAVVDELKKIAKKVTSSKE--IAQVATISANG------DESIGEMIAEAMD------ 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 180 gKVDKD-LIKIEKKSGASiDDTELIKGVLVDKERVSaqmPKKVTDAKiallncaieiketetDAEIRITDPAKLMEfiEQ 258
Cdd:PRK12850 168 -KVGKEgVITVEEAKTLG-TELDVVEGMQFDRGYLS---PYFVTNPE---------------KMRAELEDPYILLH--EK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 259 EEKMLKDMVAEIKA---SGANVLFCQKGIDDLAQHYLAKEGI-----VAARRV------KKSDMEKLAKATGANVIA--- 321
Cdd:PRK12850 226 KISNLQDLLPILEAvvqSGRPLLIIAEDVEGEALATLVVNKLrgglkSVAVKApgfgdrRKAMLEDIAVLTGGQVISedl 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 322 --AIAALSAQDLGDAGLVEerkISGDSMIFVEECKHPKAV---------------------------------TMLIR-- 364
Cdd:PRK12850 306 giKLENVTLDMLGRAKRVL---ITKENTTIIDGAGDKKNIearvkqiraqieettsdydreklqerlaklaggVAVIRvg 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 365 GTTEHVIEEVARAVDDAVGVVGCTIEDGrIVSGGGSTEVELSMKLREyAEGISGREQLAVRAFADALEVIPRTLAENAGL 444
Cdd:PRK12850 383 GATEVEVKEKKDRVDDALHATRAAVEEG-IVPGGGVALLRARSALRG-LKGANADETAGIDIVRRALEEPLRQIATNAGF 460
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
3IZI_E 445 DAIEILVKVRaahasNGNKCAGLNVFTGAVEDMCENGVVEPLRVKTQAIQSAAESTEMLLRIDDVIAAE 513
Cdd:PRK12850 461 EGSVVVGKVA-----ELPGNFGFNAQTGEYGDMVEAGIIDPAKVTRTALQDAASIAALLITTEAMVAEA 524
|
|
| groEL |
PRK12851 |
chaperonin GroEL; Reviewed |
7-511 |
3.12e-21 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 171770 Cd Length: 541 Bit Score: 96.73 E-value: 3.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 7 KRYMGRDAQRMNILAG-RIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHP----AAKMLIEVAKTQEK 81
Cdd:PRK12851 4 KEVKFHVEAREKMLRGvNILADAVKVTLGPKGRNVVIDKSFGAPTITNDGVTIAKEIELEDKfenmGAQMVREVASKTND 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 82 EVGDGTTTAVVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQDKeiltKIAMTSITGKGAEKAK 161
Cdd:PRK12851 84 VAGDGTTTATVLAQAIVREGAKAVAAGANPMDLKRGIDRAVAAVVEELKANARPVTTNAE----IAQVATISANGDAEIG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 162 EKLAEIIveavsavvddeGKVDKDLIKIEKKSGASIDDTELIKGVLVDKERVSaqmPKKVTDAKiallncaieiketetD 241
Cdd:PRK12851 160 RLVAEAM-----------EKVGNEGVITVEESKTAETELEVVEGMQFDRGYLS---PYFVTDAD---------------K 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 242 AEIRITDPAKLMefIEQEEKMLKDMVA---EIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRV-----------KKSD 307
Cdd:PRK12851 211 MEAELEDPYILI--HEKKISNLQDLLPvleAVVQSGKPLLIIAEDVEGEALATLVVNKLRGGLKVaavkapgfgdrRKAM 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 308 MEKLAKATGANVIAAIAALSAQD--LGDAGLVEERKISGDSMIFVEECKHPKAV-------------------------- 359
Cdd:PRK12851 289 LEDIAILTGGTVISEDLGIKLENvtLEQLGRAKKVVVEKENTTIIDGAGSKTEIegrvaqiraqieettsdydreklqer 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 360 -------TMLIR--GTTEHVIEEVARAVDDAVGVVGCTIEDGrIVSGGGSTEVELSMKLREyAEGISGREQLAVRAFADA 430
Cdd:PRK12851 369 laklaggVAVIRvgASTEVEVKEKKDRVDDALHATRAAVEEG-IVPGGGVALLRAVKALDK-LETANGDQRTGVEIVRRA 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 431 LEVIPRTLAENAGLDAIEILVKVRaahasNGNKCAGLNVFTGAVEDMCENGVVEPLRVKTQAIQSAAESTEMLLRIDDVI 510
Cdd:PRK12851 447 LEAPVRQIAENAGAEGSVVVGKLR-----EKPGGYGFNAATNEYGDLYAQGVIDPVKVVRTALQNAASVAGLLLTTEAMV 521
|
.
3IZI_E 511 A 511
Cdd:PRK12851 522 A 522
|
|
| PTZ00114 |
PTZ00114 |
Heat shock protein 60; Provisional |
16-504 |
6.01e-21 |
|
Heat shock protein 60; Provisional
Pssm-ID: 185455 Cd Length: 555 Bit Score: 96.13 E-value: 6.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 16 RMNILAG-RIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILR--EMS--VEHPAAKMLIEVAKTQEKEVGDGTTTA 90
Cdd:PTZ00114 24 RQSLLKGiERLADAVAVTLGPKGRNVIIEQEYGSPKITKDGVTVAKaiEFSdrFENVGAQLIRQVASKTNDKAGDGTTTA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 91 VVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVgaQDKEILTKIAMTSITGkgaekaKEKLAEIIVE 170
Cdd:PTZ00114 104 TILARAIFREGCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQSRPV--KTKEDILNVATISANG------DVEIGSLIAD 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 171 AVsavvddeGKVDKD-LIKIEkkSGASIDDT-ELIKGVLVDKERVSaqmPKKVTDA---KIALLNCAIEIKETETDAeir 245
Cdd:PTZ00114 176 AM-------DKVGKDgTITVE--DGKTLEDElEVVEGMSFDRGYIS---PYFVTNEktqKVELENPLILVTDKKISS--- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 246 ITDPAKLMEFIEQEEKMLKDMVAEIKASGANVLFCQKgiddlaqhylAKEGI-VAARRV------KKSDMEKLAKATGAN 318
Cdd:PTZ00114 241 IQSILPILEHAVKNKRPLLIIAEDVEGEALQTLIINK----------LRGGLkVCAVKApgfgdnRKDILQDIAVLTGAT 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 319 VI------AAIAALSAQDLGDAGLVEerkISGDSMIFVEECKHPKAV--------------------------------- 359
Cdd:PTZ00114 311 VVsednvgLKLDDFDPSMLGSAKKVT---VTKDETVILTGGGDKAEIkervellrsqierttseydkeklkerlaklsgg 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 360 --TMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGrIVSGGGSTEVELSMKLREYAEG--ISGREQLAVRAFADALEVIP 435
Cdd:PTZ00114 388 vaVIKVGGASEVEVNEKKDRIEDALNATRAAVEEG-IVPGGGVALLRASKLLDKLEEDneLTPDQRTGVKIVRNALRLPT 466
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
3IZI_E 436 RTLAENAGLDAIEILVKVraahASNGNKCAGLNVFTGAVEDMCENGVVEPLRVKTQAIQSAAESTEMLL 504
Cdd:PTZ00114 467 KQIAENAGVEGAVVVEKI----LEKKDPSFGYDAQTGEYVNMFEAGIIDPTKVVRSALVDAASVASLML 531
|
|
| groEL |
CHL00093 |
chaperonin GroEL |
24-504 |
1.10e-19 |
|
chaperonin GroEL
Pssm-ID: 177025 Cd Length: 529 Bit Score: 92.09 E-value: 1.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 24 IIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKM---LIEVAKTQEKEV-GDGTTTAVVVAGELLR 99
Cdd:CHL00093 21 ILAEAVSVTLGPKGRNVVLEKKYGSPQIVNDGVTIAKEIELEDHIENTgvaLIRQAASKTNDVaGDGTTTATVLAYAIVK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 100 KAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVgaQDKEILTKIAMTSiTGKGAEkakekLAEIIVEAVSavvdde 179
Cdd:CHL00093 101 QGMKNVAAGANPISLKRGIEKATQYVVSQIAEYARPV--EDIQAITQVASIS-AGNDEE-----VGSMIADAIE------ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 180 gKVDKD-LIKIEKKSGASIdDTELIKGVLVDKERVSaqmPKKVTDA---KIALLNCAIEIketeTDAEIRIT--DPAKLM 253
Cdd:CHL00093 167 -KVGREgVISLEEGKSTVT-ELEITEGMRFEKGFIS---PYFVTDTermEVVQENPYILL----TDKKITLVqqDLLPIL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 254 EFIEQEEKMLKDMVAEIKASGANVLFCQK--GIDDlaqhylakegIVAAR-----RVKKSDMEKLAKATGANVIAAIAAL 326
Cdd:CHL00093 238 EQVTKTKRPLLIIAEDVEKEALATLVLNKlrGIVN----------VVAVRapgfgDRRKAMLEDIAILTGGQVITEDAGL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 327 SAQDLGDAGLVEERKI--SGDSMIFVEEcKHPKAVTM---------------------------------LIR--GTTEH 369
Cdd:CHL00093 308 SLETIQLDLLGQARRIivTKDSTTIIAD-GNEEQVKArceqlrkqieiadssyekeklqerlaklsggvaVIKvgAATET 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 370 VIEEVARAVDDAVGVVGCTIEDGrIVSGGGSTEVELSMKLREYAE-GISGREQLAVRAFADALEVIPRTLAENAGLDAIE 448
Cdd:CHL00093 387 EMKDKKLRLEDAINATKAAVEEG-IVPGGGATLVHLSENLKTWAKnNLKEDELIGALIVARAILAPLKRIAENAGKNGSV 465
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
3IZI_E 449 ILVKVRaahasNGNKCAGLNVFTGAVEDMCENGVVEPLRVKTQAIQSAAESTEMLL 504
Cdd:CHL00093 466 IIEKVQ-----EQDFEIGYNAANNKFVNMYEAGIIDPAKVTRSALQNAASIASMIL 516
|
|
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
11-511 |
3.30e-17 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 84.40 E-value: 3.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 11 GRDAQRmNILAG-RIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHP----AAKMLIEVA-KTQEKeVG 84
Cdd:PRK00013 8 GEDARR-KLLRGvNKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDPfenmGAQLVKEVAsKTNDV-AG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 85 DGTTTAVVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQDkeiltKIAMT-SITGKGaekaKEK 163
Cdd:PRK00013 86 DGTTTATVLAQAIVREGLKNVAAGANPMDLKRGIDKAVEAAVEELKKISKPVEDKE-----EIAQVaTISANG----DEE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 164 LAEIIVEAVSavvddegKVDKD-LIKIEKKSGASiDDTELIKGVLVDKERVSAQMpkkVTDAkiallncaiEIKETE-TD 241
Cdd:PRK00013 157 IGKLIAEAME-------KVGKEgVITVEESKGFE-TELEVVEGMQFDRGYLSPYF---VTDP---------EKMEAElEN 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 242 AEIRITDpAKLmefieqeeKMLKDMVA---EIKASGANVLFCQKGIDDLAQHYLAKEGI-----VAA--------RRvkK 305
Cdd:PRK00013 217 PYILITD-KKI--------SNIQDLLPvleQVAQSGKPLLIIAEDVEGEALATLVVNKLrgtlkVVAvkapgfgdRR--K 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 306 SDMEKLAKATGANVIAAIAALS-----AQDLGDAGLVeerKISGDSMIFVEECKHPKAVT---MLIRGTTEH-------- 369
Cdd:PRK00013 286 AMLEDIAILTGGTVISEELGLKledatLEDLGQAKKV---VVTKDNTTIVDGAGDKEAIKarvAQIKAQIEEttsdydre 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 370 --------------VI-----------EEVARaVDDAVGVVGCTIEDGrIVSGGGSTEVELSMKLrEYAEGISGREQLAV 424
Cdd:PRK00013 363 klqerlaklaggvaVIkvgaatevemkEKKDR-VEDALHATRAAVEEG-IVPGGGVALLRAAPAL-EALKGLNGDEATGI 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 425 RAFADALEVIPRTLAENAGLDAIEILVKVRAAHASNgnkcAGLNVFTGAVEDMCENGVVEPLRVKTQAIQSAAESTEMLL 504
Cdd:PRK00013 440 NIVLRALEAPLRQIAENAGLEGSVVVEKVKNGKGKG----YGYNAATGEYVDMIEAGIIDPTKVTRSALQNAASVAGLLL 515
|
....*..
3IZI_E 505 RIDDVIA 511
Cdd:PRK00013 516 TTEAVVA 522
|
|
| groEL |
PRK12852 |
chaperonin GroEL; Reviewed |
24-511 |
5.97e-16 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237232 Cd Length: 545 Bit Score: 80.66 E-value: 5.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 24 IIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSV----EHPAAKMLIEVAKTQEKEVGDGTTTAVVVAGELLR 99
Cdd:PRK12852 22 ILANAVKVTLGPKGRNVVIEKSFGAPRITKDGVTVAKEIELedkfENMGAQMVREVASKTNDLAGDGTTTATVLAQAIVR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 100 KAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQ-------------DKEILTKI--AMTSITGKGAEKAKE-K 163
Cdd:PRK12852 102 EGAKAVAAGMNPMDLKRGIDIAVAAVVKDIEKRAKPVASSaeiaqvgtisangDAAIGKMIaqAMQKVGNEGVITVEEnK 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 164 LAEIIVEAVSAVVDDEGKVDKDLIKIEKKSGASIDDTElikgVLVDKERVS---AQMP--KKVTDAKIALLNCAIEIkET 238
Cdd:PRK12852 182 SLETEVDIVEGMKFDRGYLSPYFVTNAEKMTVELDDAY----ILLHEKKLSglqAMLPvlEAVVQSGKPLLIIAEDV-EG 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 239 ETDAEIRITD--------PAKLMEFIEQEEKMLKDMVAeikASGANVLFCQKGIDdlaqhyLAKEGIVAARRVKKSDMEK 310
Cdd:PRK12852 257 EALATLVVNRlrgglkvaAVKAPGFGDRRKAMLEDIAI---LTGGQLISEDLGIK------LENVTLKMLGRAKKVVIDK 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 311 LAK------ATGANVIAAIAALSAQdlgdaglVEERKISGDSMIFVEECKHPKAVTMLIR--GTTEHVIEEVARAVDDAV 382
Cdd:PRK12852 328 ENTtivngaGKKADIEARVGQIKAQ-------IEETTSDYDREKLQERLAKLAGGVAVIRvgGATEVEVKEKKDRVEDAL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 383 GVVGCTIEDGrIVSGGGsteVELsMKLREYAEGISGR---EQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRaahaS 459
Cdd:PRK12852 401 NATRAAVQEG-IVPGGG---VAL-LRAKKAVGRINNDnadVQAGINIVLKALEAPIRQIAENAGVEGSIVVGKIL----E 471
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
3IZI_E 460 NGNKCAGLNVFTGAVEDMCENGVVEPLRVKTQAIQSAAESTEMLLRIDDVIA 511
Cdd:PRK12852 472 NKSETFGFDAQTEEYVDMVAKGIIDPAKVVRTALQDAASVAGLLVTTEAMVA 523
|
|
| PLN03167 |
PLN03167 |
Chaperonin-60 beta subunit; Provisional |
25-510 |
3.58e-15 |
|
Chaperonin-60 beta subunit; Provisional
Pssm-ID: 215611 [Multi-domain] Cd Length: 600 Bit Score: 78.04 E-value: 3.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 25 IAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHP----AAKMLIEVAKTQEKEVGDGTTTAVVVAGELLRK 100
Cdd:PLN03167 78 LADLVGVTLGPKGRNVVLESKYGSPKIVNDGVTVAKEVELEDPveniGAKLVRQAAAKTNDLAGDGTTTSVVLAQGLIAE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 101 AEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVgaQDKEiLTKIAMTSiTGKGAEkakekLAEIIVEAVS------A 174
Cdd:PLN03167 158 GVKVVAAGANPVQITRGIEKTAKALVKELKKMSKEV--EDSE-LADVAAVS-AGNNYE-----VGNMIAEAMSkvgrkgV 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 175 VVDDEGK-VDKDLIKIEkksGASIDDTELIKGVLVDKERVSAQMPK---KVTDAKIALLNCAIEIKEtetDAeIRITDPA 250
Cdd:PLN03167 229 VTLEEGKsAENNLYVVE---GMQFDRGYISPYFVTDSEKMSVEYDNcklLLVDKKITNARDLIGILE---DA-IRGGYPL 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 251 KLM-EFIEQeEKMLKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATGANVIAAIAAL--- 326
Cdd:PLN03167 302 LIIaEDIEQ-EALATLVVNKLRGSLKIAALKAPGFGERKSQYLDDIAILTGGTVIREEVGLSLDKVGKEVLGTAAKVvlt 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 327 --SAQDLGDAGL---VEERKISGDSMIFVEECKHPK-------------AVTMLIRGTTEHVIEEVARAVDDAVGVVGCT 388
Cdd:PLN03167 381 kdTTTIVGDGSTqeaVNKRVAQIKNLIEAAEQDYEKeklneriaklsggVAVIQVGAQTETELKEKKLRVEDALNATKAA 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 389 IEDGrIVSGGGSTEVELSMKLREYAEGISGREQ-LAVRAFADALEVIPRTLAENAGLDAIEILVKVraahASNGNKCAGL 467
Cdd:PLN03167 461 VEEG-IVVGGGCTLLRLASKVDAIKDTLENDEQkVGADIVKRALSYPLKLIAKNAGVNGSVVSEKV----LSNDNPKFGY 535
|
490 500 510 520
....*....|....*....|....*....|....*....|...
3IZI_E 468 NVFTGAVEDMCENGVVEPLRVKTQAIQSAAESTEMLLRIDDVI 510
Cdd:PLN03167 536 NAATGKYEDLMAAGIIDPTKVVRCCLEHAASVAKTFLTSDCVV 578
|
|
| PRK14104 |
PRK14104 |
chaperonin GroEL; Provisional |
11-511 |
8.89e-14 |
|
chaperonin GroEL; Provisional
Pssm-ID: 172594 Cd Length: 546 Bit Score: 73.53 E-value: 8.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 11 GRDAQRMNILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSV----EHPAAKMLIEVAKTQEKEVGDG 86
Cdd:PRK14104 9 GVDARDRMLRGVDILANAVKVTLGPKGRNVVLDKSFGAPRITKDGVTVAKEIELedkfENMGAQMVREVASKSADAAGDG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 87 TTTAVVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQDKeiLTKIAMTSITGkgaekaKEKLAE 166
Cdd:PRK14104 89 TTTATVLAQAIVREGAKSVAAGMNPMDLKRGIDLAVEAVVADLVKNSKKVTSNDE--IAQVGTISANG------DAEIGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 167 IIVEAVSAvVDDEGkvdkdLIKIEKksgASIDDTEL--IKGVLVDKERVSAQMPKKVTDAKIALLNCAIEIKETETDAei 244
Cdd:PRK14104 161 FLADAMKK-VGNEG-----VITVEE---AKSLETELdvVEGMQFDRGYISPYFVTNADKMRVEMDDAYILINEKKLSS-- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 245 rITDPAKLMEFIEQEEKMLKDMVAEIKASGANVLFCQK-------------GIDDLAQHYLAKEGIVAA----------- 300
Cdd:PRK14104 230 -LNELLPLLEAVVQTGKPLVIVAEDVEGEALATLVVNRlrgglkvaavkapGFGDRRKAMLQDIAILTGgqaisedlgik 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 301 ---------RRVKKS--DMEKLAKATGANVIAAIAALSAQDLGDaglVEERKISGDSMIFVEECKHPKAVTMLIR--GTT 367
Cdd:PRK14104 309 lenvtlqmlGRAKKVmiDKENTTIVNGAGKKADIEARVAQIKAQ---IEETTSDYDREKLQERLAKLAGGVAVIRvgGAT 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3IZI_E 368 EHVIEEVARAVDDAVGVVGCTIEDGrIVSGGGSTEVELSMKLREYAEGiSGREQLAVRAFADALEVIPRTLAENAGLDAI 447
Cdd:PRK14104 386 EVEVKERKDRVDDAMHATRAAVEEG-IVPGGGVALLRASEQLKGIKTK-NDDQKTGVEIVRKALSAPARQIAINAGEDGS 463
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
3IZI_E 448 EILVKVraahASNGNKCAGLNVFTGAVEDMCENGVVEPLRVKTQAIQSAAESTEMLLRIDDVIA 511
Cdd:PRK14104 464 VIVGKI----LEKEQYSYGFDSQTGEYGNLVSKGIIDPTKVVRTAIQNAASVAALLITTEAMVA 523
|
|
| |
