|
Name |
Accession |
Description |
Interval |
E-value |
| thermosome_alpha |
NF041082 |
thermosome subunit alpha; |
7-518 |
0e+00 |
|
thermosome subunit alpha;
Pssm-ID: 469009 Cd Length: 518 Bit Score: 854.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 7 VLPENMKRYMGRDAQRMNILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQE 86
Cdd:NF041082 5 ILKEGTQRTSGRDAQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDVVITNDGVTILKEMDIEHPAAKMIVEVAKTQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 87 KEVGDGTTTAVVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQDKEILTKIAMTSITGKGAEKA 166
Cdd:NF041082 85 DEVGDGTTTAVVLAGELLKKAEELLDQDIHPTIIAEGYRLAAEKALEILDEIAIKVDPDDKETLKKIAATAMTGKGAEAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 167 KEKLAEIIVEAVSAVVDDEG--KVDKDLIKIEKKSGASIDDTELIKGVLVDKERVSAQMPKKVTDAKIALLNCAIEIKET 244
Cdd:NF041082 165 KDKLADLVVDAVKAVAEKDGgyNVDLDNIKVEKKVGGSIEDSELVEGVVIDKERVHPGMPKRVENAKIALLDAPLEVKKT 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 245 ETDAEIRITDPAKLMEFIEQEEKMLKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATGAN 324
Cdd:NF041082 245 EIDAKISITDPDQLQAFLDQEEKMLKEMVDKIADSGANVVFCQKGIDDLAQHYLAKEGILAVRRVKKSDMEKLAKATGAR 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 325 VITNIKDLSAQDLGDAGLVEERKISGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIVSGG 404
Cdd:NF041082 325 IVTSIDDLSPEDLGYAGLVEERKVGGDKMIFVEGCKNPKAVTILLRGGTEHVVDEVERALEDALRVVRVVLEDGKVVAGG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 405 GSTEVELSMKLREYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHaSNGNKCAGLNVFTGAVEDMC 484
Cdd:NF041082 405 GAPEVELALRLREYAASVGGREQLAIEAFAEALEIIPRTLAENAGLDPIDALVELRSAH-EKGNKTAGLDVYTGKVVDML 483
|
490 500 510
....*....|....*....|....*....|....
gi 291191278 485 ENGVVEPLRVKTQAIQSAAESTEMLLRIDDVIAA 518
Cdd:NF041082 484 EIGVVEPLRVKTQAIKSATEAAVMILRIDDVIAA 517
|
|
| thermosome_beta |
NF041083 |
thermosome subunit beta; |
7-518 |
0e+00 |
|
thermosome subunit beta;
Pssm-ID: 469010 Cd Length: 519 Bit Score: 830.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 7 VLPENMKRYMGRDAQRMNILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQE 86
Cdd:NF041083 5 ILKEGTQRTKGRDAQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDIVITNDGATILKEMDVQHPAAKMLVEVAKTQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 87 KEVGDGTTTAVVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQDKEILTKIAMTSITGKGAEKA 166
Cdd:NF041083 85 DEVGDGTTTAVVLAGELLKKAEELLDQNIHPTIIANGYRLAAEKAIEILDEIAEKVDPDDRETLKKIAETSLTSKGVEEA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 167 KEKLAEIIVEAVSAVVDDEG---KVDKDLIKIEKKSGASIDDTELIKGVLVDKERVSAQMPKKVTDAKIALLNCAIEIKE 243
Cdd:NF041083 165 RDYLAEIAVKAVKQVAEKRDgkyYVDLDNIQIEKKHGGSIEDTQLIYGIVIDKEVVHPGMPKRVENAKIALLDAPLEVKK 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 244 TETDAEIRITDPAKLMEFIEQEEKMLKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATGA 323
Cdd:NF041083 245 TEIDAEIRITDPDQLQKFLDQEEKMLKEMVDKIKATGANVVFCQKGIDDLAQHYLAKAGILAVRRVKKSDMEKLAKATGA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 324 NVITNIKDLSAQDLGDAGLVEERKISGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIVSG 403
Cdd:NF041083 325 RIVTNIDDLTPEDLGYAELVEERKVGDDKMVFVEGCKNPKAVTILIRGGTEHVVDEAERALEDALSVVADAVEDGKIVAG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 404 GGSTEVELSMKLREYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHaSNGNKCAGLNVFTGAVEDM 483
Cdd:NF041083 405 GGAPEVELAKRLREYAATVGGREQLAVEAFAEALEIIPRTLAENAGLDPIDILVKLRSAH-EKGKKWAGINVFTGEVVDM 483
|
490 500 510
....*....|....*....|....*....|....*
gi 291191278 484 CENGVVEPLRVKTQAIQSAAESTEMLLRIDDVIAA 518
Cdd:NF041083 484 WELGVIEPLRVKTQAIKSATEAATMILRIDDVIAA 518
|
|
| cpn60 |
cd03343 |
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ... |
7-518 |
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: 801.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 7 VLPENMKRYMGRDAQRMNILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQE 86
Cdd:cd03343 3 ILKEGTQRTSGRDAQRMNIAAAKAVAEAVRTTLGPKGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAKTQD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 87 KEVGDGTTTAVVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQDKEILTKIAMTSITGKGAEKA 166
Cdd:cd03343 83 EEVGDGTTTAVVLAGELLEKAEDLLDQNIHPTVIIEGYRLAAEKALELLDEIAIKVDPDDKDTLRKIAKTSLTGKGAEAA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 167 KEKLAEIIVEAVSAVVDDEG---KVDKDLIKIEKKSGASIDDTELIKGVLVDKERVSAQMPKKVTDAKIALLNCAIEIKE 243
Cdd:cd03343 163 KDKLADLVVDAVLQVAEKRDgkyVVDLDNIKIEKKTGGSVDDTELIRGIVIDKEVVHPGMPKRVENAKIALLDAPLEVKK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 244 TETDAEIRITDPAKLMEFIEQEEKMLKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATGA 323
Cdd:cd03343 243 TEIDAKIRITSPDQLQAFLEQEEAMLKEMVDKIADTGANVVFCQKGIDDLAQHYLAKAGILAVRRVKKSDMEKLARATGA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 324 NVITNIKDLSAQDLGDAGLVEERKISGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIVSG 403
Cdd:cd03343 323 KIVTNIDDLTPEDLGEAELVEERKVGDDKMVFVEGCKNPKAVTILLRGGTEHVVDELERALEDALRVVADALEDGKVVAG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 404 GGSTEVELSMKLREYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHAsNGNKCAGLNVFTGAVEDM 483
Cdd:cd03343 403 GGAVEIELAKRLREYARSVGGREQLAVEAFADALEEIPRTLAENAGLDPIDTLVELRAAHE-KGNKNAGLDVYTGEVVDM 481
|
490 500 510
....*....|....*....|....*....|....*
gi 291191278 484 CENGVVEPLRVKTQAIQSAAESTEMLLRIDDVIAA 518
Cdd:cd03343 482 LEKGVIEPLRVKKQAIKSATEAATMILRIDDVIAA 516
|
|
| thermosome_arch |
TIGR02339 |
thermosome, various subunits, archaeal; Thermosome is the name given to the archaeal rather ... |
7-518 |
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: 713.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 7 VLPENMKRYMGRDAQRMNILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQE 86
Cdd:TIGR02339 4 ILKEGTQRTSGRDAQRNNIAAAKAVAEAVKSTLGPRGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAKTQD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 87 KEVGDGTTTAVVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQDKEILTKIAMTSITGKG-AEK 165
Cdd:TIGR02339 84 EEVGDGTTTAVVLAGELLEKAEDLLEQDIHPTVIIEGYRKAAEKALEIIDEIATKISPEDRDLLKKIAYTSLTSKAsAEV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 166 AKEKLAEIIVEAVSAVV----DDEGKVDKDLIKIEKKSGASIDDTELIKGVLVDKERVSAQMPKKVTDAKIALLNCAIEI 241
Cdd:TIGR02339 164 AKDKLADLVVEAVKQVAelrgDGKYYVDLDNIKIVKKKGGSIEDTELVEGIVVDKEVVHPGMPKRVENAKIALLDAPLEV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 242 KETETDAEIRITDPAKLMEFIEQEEKMLKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKAT 321
Cdd:TIGR02339 244 EKTEIDAKIRITDPDQIKKFLDQEEAMLKEMVDKIASAGANVVICQKGIDDVAQHYLAKAGILAVRRVKKSDIEKLARAT 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 322 GANVITNIKDLSAQDLGDAGLVEERKISGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIV 401
Cdd:TIGR02339 324 GARIVSSIDEITESDLGYAELVEERKVGEDKMVFVEGCKNPKAVTILLRGGTEHVVDELERSIQDALHVVANALEDGKIV 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 402 SGGGSTEVELSMKLREYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHAsNGNKCAGLNVFTGAVE 481
Cdd:TIGR02339 404 AGGGAVEIELALRLRSYARSVGGREQLAIEAFADALEEIPRILAENAGLDPIDALVDLRAKHE-KGNKNAGINVFTGEIE 482
|
490 500 510
....*....|....*....|....*....|....*..
gi 291191278 482 DMCENGVVEPLRVKTQAIQSAAESTEMLLRIDDVIAA 518
Cdd:TIGR02339 483 DMLELGVIEPLRVKEQAIKSATEAATMILRIDDVIAA 519
|
|
| Cpn60_TCP1 |
pfam00118 |
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ... |
31-518 |
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: 621.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 31 IAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQEKEVGDGTTTAVVVAGELLRKAEEL 110
Cdd:pfam00118 1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELEIQHPAAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEEAEKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 111 LDQNVHPTIVVKGYQAAAQKAQELLKTIAC-EVGAQDKEILTKIAMTSITGKGAEKAKEKLAEIIVEAVSAVVDDEGKVD 189
Cdd:pfam00118 81 LAAGVHPTTIIEGYEKALEKALEILDSIISiPVEDVDREDLLKVARTSLSSKIISRESDFLAKLVVDAVLAIPKNDGSFD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 190 KDLIKIEKKSGASIDDTELIKGVLVDKERVSAQMPKKVTDAKIALLNCAIEIKETETDAEIRITDPAKLMEFIEQEEKML 269
Cdd:pfam00118 161 LGNIGVVKILGGSLEDSELVDGVVLDKGPLHPDMPKRLENAKVLLLNCSLEYEKTETKATVVLSDAEQLERFLKAEEEQI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 270 KDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATGANVITNIKDLSAQDLGDAGLVEERKIS 349
Cdd:pfam00118 241 LEIVEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMALRRVKKRDLERLAKATGARAVSSLDDLTPDDLGTAGKVEEEKIG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 350 GDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIVSGGGSTEVELSMKLREYAEGISGREQLA 429
Cdd:pfam00118 321 DEKYTFIEGCKSPKAATILLRGATDHVLDEIERSIHDALCVVKNAIEDPRVVPGGGAVEMELARALREYAKSVSGKEQLA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 430 VRAFADALEVIPRTLAENAGLDAIEILVKVRAAHAsNGNKCAGLNVFTGAVEDMCENGVVEPLRVKTQAIQSAAESTEML 509
Cdd:pfam00118 401 IEAFAEALEVIPKTLAENAGLDPIEVLAELRAAHA-SGEKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKSATEAASTI 479
|
....*....
gi 291191278 510 LRIDDVIAA 518
Cdd:pfam00118 480 LRIDDIIKA 488
|
|
| chaperonin_type_I_II |
cd00309 |
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ... |
13-517 |
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: 595.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 13 KRYMGRDAQRMNILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQEKEVGDG 92
Cdd:cd00309 2 EREFGEEARLSNINAAKALADAVKTTLGPKGMDKMLVDSLGDPTITNDGATILKEIEVEHPAAKLLVEVAKSQDDEVGDG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 93 TTTAVVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQDKEILTKIAMTSITGKGAEKAKEKLAE 172
Cdd:cd00309 82 TTTVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVPIDVEDREELLKVATTSLNSKLVSGGDDFLGE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 173 IIVEAVSAVVDDEGKVDKDLIKIEKKSGASIDDTELIKGVLVDKERVSAQMPKKVTDAKIALLNCAIEiketetdaeiri 252
Cdd:cd00309 162 LVVDAVLKVGKENGDVDLGVIRVEKKKGGSLEDSELVVGMVFDKGYLSPYMPKRLENAKILLLDCKLE------------ 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 253 tdpaklmefieqeekmlkdmvaeikasgaNVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATGANVITNIKDL 332
Cdd:cd00309 230 -----------------------------YVVIAEKGIDDEALHYLAKLGIMAVRRVRKEDLERIAKATGATIVSRLEDL 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 333 SAQDLGDAGLVEERKISGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIVSGGGSTEVELS 412
Cdd:cd00309 281 TPEDLGTAGLVEETKIGDEKYTFIEGCKGGKVATILLRGATEVELDEAERSLHDALCAVRAAVEDGGIVPGGGAAEIELS 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 413 MKLREYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHAsNGNKCAGLNVFTGAVEDMCENGVVEPL 492
Cdd:cd00309 361 KALEELAKTLPGKEQLGIEAFADALEVIPRTLAENAGLDPIEVVTKLRAKHA-EGGGNAGGDVETGEIVDMKEAGIIDPL 439
|
490 500
....*....|....*....|....*
gi 291191278 493 RVKTQAIQSAAESTEMLLRIDDVIA 517
Cdd:cd00309 440 KVKRQALKSATEAASLILTIDDIIV 464
|
|
| GroEL |
COG0459 |
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ... |
17-520 |
5.85e-177 |
|
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227 Cd Length: 497 Bit Score: 508.08 E-value: 5.85e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 17 GRDAQRMNILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHP----AAKMLIEVAKTQEKEVGDG 92
Cdd:COG0459 8 GEDARRANIRGVKALADAVKVTLGPKGRNVMLVKSFGDPTITNDGVTIAKEIELEDPfenmGAQLVKEVASKTNDEAGDG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 93 TTTAVVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVgaQDKEILTKIAMTSITGkgaekaKEKLAE 172
Cdd:COG0459 88 TTTATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPV--DDKEELAQVATISANG------DEEIGE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 173 IIVEAVSAVVDDegkvdkDLIKIEKKSGASiDDTELIKGVLVDKERVSAQ-------MPKKVTDAKIALLNCAIEIkete 245
Cdd:COG0459 160 LIAEAMEKVGKD------GVITVEEGKGLE-TELEVVEGMQFDKGYLSPYfvtdpekMPAELENAYILLTDKKISS---- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 246 tdaeiritdpaklmefieqeEKMLKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRV-----------KKSDM 314
Cdd:COG0459 229 --------------------IQDLLPLLEKVAQSGKPLLIIAEDIDGEALATLVVNGIRGVLRVvavkapgfgdrRKAML 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 315 EKLAKATGANVITN-----IKDLSAQDLGDAGLVEERKisgDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVG 389
Cdd:COG0459 289 EDIAILTGGRVISEdlglkLEDVTLDDLGRAKRVEVDK---DNTTIVEGAGNPKAIVILVGAATEVEVKERKRRVEDALH 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 390 VVGCTIEDGrIVSGGGSTEVELSMKLREYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAhasnGNK 469
Cdd:COG0459 366 ATRAAVEEG-IVPGGGAALLRAARALRELAAKLEGDEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKVRAA----KDK 440
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 291191278 470 CAGLNVFTGAVEDMCENGVVEPLRVKTQAIQSAAESTEMLLRIDDVIAAEK 520
Cdd:COG0459 441 GFGFDAATGEYVDMLEAGVIDPAKVKRSALQNAASVAGLILTTEAVIADKP 491
|
|
| TCP1_epsilon |
cd03339 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ... |
10-517 |
4.76e-168 |
|
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: 486.42 E-value: 4.76e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 10 ENMKRYMGRDAQRMNILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQEKEV 89
Cdd:cd03339 14 EKKKRLKGLEAHKSHILAAKSVANILRTSLGPRGMDKILVSPDGEVTVTNDGATILEKMDVDHQIAKLLVELSKSQDDEI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 90 GDGTTTAVVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIA--CEVGAQDKEILTKIAMTSITGKGAEKAK 167
Cdd:cd03339 94 GDGTTGVVVLAGALLEQAEKLLDRGIHPIRIADGYEQACKIAVEHLEEIAdkIEFSPDNKEPLIQTAMTSLGSKIVSRCH 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 168 EKLAEIIVEAVSAVVDDEGK-VDKDLIKIEKKSGASIDDTELIKGVLVDKERVSAQMPKKVTDAKIALLNCAIEIKETET 246
Cdd:cd03339 174 RQFAEIAVDAVLSVADLERKdVNFELIKVEGKVGGRLEDTKLVKGIVIDKDFSHPQMPKEVKDAKIAILTCPFEPPKPKT 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 247 DAEIRITDPAKLMEFIEQEEKMLKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATGANVI 326
Cdd:cd03339 254 KHKLDITSVEDYKKLQEYEQKYFREMVEQVKDAGANLVICQWGFDDEANHLLLQNGLPAVRWVGGVEIELIAIATGGRIV 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 327 TNIKDLSAQDLGDAGLVEERKI--SGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIVSGG 404
Cdd:cd03339 334 PRFEDLSPEKLGKAGLVREISFgtTKDKMLVIEGCPNSKAVTIFIRGGNKMIIEEAKRSLHDALCVVRNLIRDNRIVYGG 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 405 GSTEVELSMKLREYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHASNGNKCAGLNVFTGAVEDMC 484
Cdd:cd03339 414 GAAEISCSLAVEKAADKCSGIEQYAMRAFADALESIPLALAENSGLNPIETLSEVKARQVKEKNPHLGIDCLGRGTNDMK 493
|
490 500 510
....*....|....*....|....*....|...
gi 291191278 485 ENGVVEPLRVKTQAIQSAAESTEMLLRIDDVIA 517
Cdd:cd03339 494 EQKVFETLISKKQQILLATQVVKMILKIDDVIV 526
|
|
| TCP1_delta |
cd03338 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ... |
24-518 |
2.58e-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: 453.67 E-value: 2.58e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 24 NILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQEKEVGDGTTTAVVVAGEL 103
Cdd:cd03338 13 NIQAAKAVADAIRTSLGPRGMDKMIQTGKGEVIITNDGATILKQMSVLHPAAKMLVELSKAQDIEAGDGTTSVVVLAGAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 104 LRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQDKEILTKIAMTSITGKGAEKAKEKLAEIIVEAVSAVVD 183
Cdd:cd03338 93 LSACESLLKKGIHPTVISESFQIAAKKAVEILDSMSIPVDLNDRESLIKSATTSLNSKVVSQYSSLLAPIAVDAVLKVID 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 184 DEGKVDKDL--IKIEKKSGASIDDTELIKGVLVDKERV-SAQMPKKVTDAKIALLNCAIEIKETETDAEIRITDPAKLME 260
Cdd:cd03338 173 PATATNVDLkdIRIVKKLGGTIEDTELVDGLVFTQKASkKAGGPTRIEKAKIGLIQFCLSPPKTDMDNNIVVNDYAQMDR 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 261 FIEQEEKMLKDMVAEIKASGANVLFCQKGI-----DDLAQHYLAKEGIVAARRVKKSDMEKLAKATGANVITNIKDLSAQ 335
Cdd:cd03338 253 ILREERKYILNMCKKIKKSGCNVLLIQKSIlrdavSDLALHFLAKLKIMVVKDIEREEIEFICKTIGCKPVASIDHFTED 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 336 DLGDAGLVEERKISGDSMIFVEECKHP-KAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIVSGGGSTEVELSMK 414
Cdd:cd03338 333 KLGSADLVEEVSLGDGKIVKITGVKNPgKTVTILVRGSNKLVLDEAERSLHDALCVIRCLVKKRALIPGGGAPEIEIALQ 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 415 LREYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHAsNGNKCAGLNVFTGAVEDMCENGVVEPLRV 494
Cdd:cd03338 413 LSEWARTLTGVEQYCVRAFADALEVIPYTLAENAGLNPISIVTELRNRHA-QGEKNAGINVRKGAITNILEENVVQPLLV 491
|
490 500
....*....|....*....|....
gi 291191278 495 KTQAIQSAAESTEMLLRIDDVIAA 518
Cdd:cd03338 492 STSAITLATETVRMILKIDDIVLA 515
|
|
| chap_CCT_epsi |
TIGR02343 |
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ... |
10-519 |
5.16e-153 |
|
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: 448.48 E-value: 5.16e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 10 ENMKRYMGRDAQRMNILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQEKEV 89
Cdd:TIGR02343 18 DNKKRLKGLEAKKSNIAAAKSVASILRTSLGPKGMDKMLISPDGDITVTNDGATILSQMDVDNQIAKLMVELSKSQDDEI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 90 GDGTTTAVVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQD--KEILTKIAMTSITGKGAEKAK 167
Cdd:TIGR02343 98 GDGTTGVVVLAGALLEQAEELLDKGIHPIKIADGFEEAARIAVEHLEEISDEISADNnnREPLIQAAKTSLGSKIVSKCH 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 168 EKLAEIIVEAVSAVVDDEGK-VDKDLIKIEKKSGASIDDTELIKGVLVDKERVSAQMPKKVTDAKIALLNCAIEIKETET 246
Cdd:TIGR02343 178 RRFAEIAVDAVLNVADMERRdVDFDLIKVEGKVGGSLEDTKLIKGIIIDKDFSHPQMPKEVEDAKIAILTCPFEPPKPKT 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 247 DAEIRITDPAKLMEFIEQEEKMLKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATGANVI 326
Cdd:TIGR02343 258 KHKLDISSVEEYKKLQKYEQQKFKEMIDDIKKSGANLVICQWGFDDEANHLLLQNDLPAVRWVGGQELELIAIATGGRIV 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 327 TNIKDLSAQDLGDAGLVEERKI--SGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIVSGG 404
Cdd:TIGR02343 338 PRFQELSKDKLGKAGLVREISFgtTKDRMLVIEQCKNSKAVTIFIRGGNKMIIEEAKRSIHDALCVVRNLIKDSRIVYGG 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 405 GSTEVELSMKLREYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHASNGNKCAGLNVFTGAVEDMC 484
Cdd:TIGR02343 418 GAAEISCSLAVSQEADKYPGVEQYAIRAFADALETIPMALAENSGLDPIGTLSTLKSLQLKEKNPNLGVDCLGYGTNDMK 497
|
490 500 510
....*....|....*....|....*....|....*
gi 291191278 485 ENGVVEPLRVKTQAIQSAAESTEMLLRIDDVIAAE 519
Cdd:TIGR02343 498 EQFVFETLIGKKQQILLATQLVRMILKIDDVISPG 532
|
|
| TCP1_eta |
cd03340 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ... |
24-520 |
1.08e-151 |
|
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: 444.81 E-value: 1.08e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 24 NILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQEKEVGDGTTTAVVVAGEL 103
Cdd:cd03340 21 NINACQAIADAVRTTLGPRGMDKLIVDGRGKVTISNDGATILKLLDIVHPAAKTLVDIAKSQDAEVGDGTTSVVVLAGEF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 104 LRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQDK----EILTKIAMTSITGKGAEKAKEKLAEIIVEAVS 179
Cdd:cd03340 101 LKEAKPFIEDGVHPQIIIRGYRKALQLAIEKIKEIAVNIDKEDKeeqrELLEKCAATALNSKLIASEKEFFAKMVVDAVL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 180 AVVDDegkVDKDLIKIEKKSGASIDDTELIKGVLVDKERVSA---QMPKKVTDAKIALLNCAIEIKETETDAEIRITDPA 256
Cdd:cd03340 181 SLDDD---LDLDMIGIKKVPGGSLEDSQLVNGVAFKKTFSYAgfeQQPKKFKNPKILLLNVELELKAEKDNAEVRVEDPE 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 257 KLMEFIEQEEKMLKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATGANVITNIKDLSAQD 336
Cdd:cd03340 258 EYQAIVDAEWKIIYDKLEKIVKSGANVVLSKLPIGDLATQYFADRDIFCAGRVPEEDLKRVAQATGGSIQTTVSNITDDV 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 337 LGDAGLVEERKISGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIVSGGGSTEVELSMKLR 416
Cdd:cd03340 338 LGTCGLFEERQVGGERYNIFTGCPKAKTCTIILRGGAEQFIEEAERSLHDAIMIVRRAIKNDSVVAGGGAIEMELSKYLR 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 417 EYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHASNGNKCAGLNVFTGAVEDMCENGVVEPLRVKT 496
Cdd:cd03340 418 DYSRTIAGKQQLVINAFAKALEIIPRQLCDNAGFDATDILNKLRQKHAQGGGKWYGVDINNEGIADNFEAFVWEPSLVKI 497
|
490 500
....*....|....*....|....
gi 291191278 497 QAIQSAAESTEMLLRIDDVIAAEK 520
Cdd:cd03340 498 NALTAATEAACLILSVDETIKNPK 521
|
|
| chap_CCT_gamma |
TIGR02344 |
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ... |
7-520 |
3.17e-145 |
|
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: 428.39 E-value: 3.17e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 7 VLPENMKRYMGRDAQRMNILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQE 86
Cdd:TIGR02344 4 VLNQNTKRESGRKAQLSNIQAAKAVADIIRTCLGPRSMLKMLLDPMGGIVMTNDGNAILREIDVAHPAAKSMIELSRTQD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 87 KEVGDGTTTAVVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQDKEILTKIAMTSITGKGAEKA 166
Cdd:TIGR02344 84 EEVGDGTTSVIILAGEMLSVAEPFLEQNIHPTVIIRAYRKALDDALSVLEEISIPVDVNDDAAMLKLIQSCIGTKFVSRW 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 167 KEKLAEIIVEAVSAVVDDEG---KVD-KDLIKIEKKSGASIDDTELIKGVLVDKERVSAQMPKKVTDAKIALLNCAIEIK 242
Cdd:TIGR02344 164 SDLMCDLALDAVRTVQRDENgrkEIDiKRYAKVEKIPGGDIEDSCVLKGVMINKDVTHPKMRRYIENPRIVLLDCPLEYK 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 243 ETETDAEIRITDPAKLMEFIEQEEKMLKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATG 322
Cdd:TIGR02344 244 KGESQTNIEITKEEDWNRILQMEEEYVQLMCEDIIAVKPDLVITEKGVSDLAQHYLLKANITAIRRVRKTDNNRIARACG 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 323 ANVITNIKDLSAQDLG-DAGLVEERKISGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIV 401
Cdd:TIGR02344 324 ATIVNRPEELRESDVGtGCGLFEVKKIGDEYFTFITECKDPKACTILLRGASKDILNEVERNLQDAMAVARNVLLDPKLV 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 402 SGGGSTEVELSMKLREYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHASNGNKCAGLNVFTGAVE 481
Cdd:TIGR02344 404 PGGGATEMAVSVALTEKSKKLEGVEQWPYRAVADALEIIPRTLAQNCGANVIRTLTELRAKHAQENNCTWGIDGETGKIV 483
|
490 500 510
....*....|....*....|....*....|....*....
gi 291191278 482 DMCENGVVEPLRVKTQAIQSAAESTEMLLRIDDVIAAEK 520
Cdd:TIGR02344 484 DMKEKGIWEPLAVKLQTYKTAIESACLLLRIDDIVSGVK 522
|
|
| TCP1_alpha |
cd03335 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ... |
13-516 |
6.85e-145 |
|
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: 427.47 E-value: 6.85e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 13 KRYMGRDAQRMNILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQEKEVGDG 92
Cdd:cd03335 2 ERTSGQDVRTQNVTAAMAIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDKEVGDG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 93 TTTAVVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKA-QELLKTIACEVGAQDKEILTKIAMTSITGKGAEKAKEKLA 171
Cdd:cd03335 82 TTSVVIIAAELLKRANELVKQKIHPTTIISGYRLACKEAvKYIKEHLSISVDNLGKESLINVAKTSMSSKIIGADSDFFA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 172 EIIVEAVSAV--VDDEGKVDKDL--IKIEKKSGASIDDTELIKGVLVDKERVSAQMPKKVTDAKIALLNCAIEIKETETD 247
Cdd:cd03335 162 NMVVDAILAVktTNEKGKTKYPIkaVNILKAHGKSAKESYLVNGYALNCTRASQGMPTRVKNAKIACLDFNLQKTKMKLG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 248 AEIRITDPAKLMEFIEQEEKMLKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATGANVIT 327
Cdd:cd03335 242 VQVVVTDPEKLEKIRQRESDITKERIKKILAAGANVVLTTGGIDDMCLKYFVEAGAMAVRRVKKEDLRRIAKATGATLVS 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 328 NIKDL------SAQDLGDAGLVEERKISGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIV 401
Cdd:cd03335 322 TLANLegeetfDPSYLGEAEEVVQERIGDDELILIKGTKKRSSASIILRGANDFMLDEMERSLHDALCVVKRTLESNSVV 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 402 SGGGSTEVELSMKLREYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHAS-------NGNKCAGLN 474
Cdd:cd03335 402 PGGGAVETALSIYLENFATTLGSREQLAIAEFAEALLVIPKTLAVNAAKDATELVAKLRAYHAAaqvkpdkKHLKWYGLD 481
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 291191278 475 VFTGAVEDMCENGVVEPLRVKTQAIQSAAESTEMLLRIDDVI 516
Cdd:cd03335 482 LINGKVRDNLEAGVLEPTVSKIKSLKFATEAAITILRIDDLI 523
|
|
| TCP1_gamma |
cd03337 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ... |
7-518 |
1.08e-144 |
|
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: 425.17 E-value: 1.08e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 7 VLPENMKRYMGRDAQRMNILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQE 86
Cdd:cd03337 4 VLNQNTKRESGRKAQLGNIQAAKTVADVIRTCLGPRAMLKMLLDPMGGIVLTNDGNAILREIDVAHPAAKSMIELSRTQD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 87 KEVGDGTTTAVVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQDKEILTKIAMTSITGKGAEKA 166
Cdd:cd03337 84 EEVGDGTTSVIILAGEILAVAEPFLERGIHPTVIIKAYRKALEDALKILEEISIPVDVNDRAQMLKIIKSCIGTKFVSRW 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 167 KEKLAEIIVEAVSAV-VDDEGKVD----KDLIKIEKKSGASIDDTELIKGVLVDKERVSAQMPKKVTDAKIALLNCAIEI 241
Cdd:cd03337 164 SDLMCNLALDAVKTVaVEENGRKKeidiKRYAKVEKIPGGEIEDSRVLDGVMLNKDVTHPKMRRRIENPRIVLLDCPLEY 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 242 ketetdaeiritdpaklmefieqeekmlkdmvaeikasganVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKAT 321
Cdd:cd03337 244 -----------------------------------------LVITEKGVSDLAQHYLVKAGITALRRVRKTDNNRIARAC 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 322 GANVITNIKDLSAQDLGDAGLVEERKISGDSMI-FVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRI 400
Cdd:cd03337 283 GATIVNRPEELTESDVGTGAGLFEVKKIGDEYFtFITECKDPKACTILLRGASKDVLNEVERNLQDAMAVARNIILNPKL 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 401 VSGGGSTEVELSMKLREYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHASNGNKCAGLNVFTGAV 480
Cdd:cd03337 363 VPGGGATEMAVSHALSEKAKSIEGVEQWPYKAVASALEVIPRTLAQNCGANVIRTLTELRAKHAQGENSTWGIDGETGDI 442
|
490 500 510
....*....|....*....|....*....|....*...
gi 291191278 481 EDMCENGVVEPLRVKTQAIQSAAESTEMLLRIDDVIAA 518
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 ... |
24-520 |
3.12e-139 |
|
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: 413.00 E-value: 3.12e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 24 NILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQEKEVGDGTTTAVVVAGEL 103
Cdd:TIGR02345 23 NINACVAIAEALKTTLGPRGMDKLIVGSNGKATISNDGATILKLLDIVHPAAKTLVDIAKSQDAEVGDGTTSVTILAGEL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 104 LRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQD---KEILTKIAMTSITGKGAEKAKEKLAEIIVEAVSA 180
Cdd:TIGR02345 103 LKEAKPFIEEGVHPQLIIRCYREALSLAVEKIKEIAVTIDEEKgeqRELLEKCAATALSSKLISHNKEFFSKMIVDAVLS 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 181 VVDDEgkVDKDLIKIEKKSGASIDDTELIKGVLVDKERVSA---QMPKKVTDAKIALLNCAIEIKETETDAEIRITDPAK 257
Cdd:TIGR02345 183 LDRDD--LDLKLIGIKKVQGGALEDSQLVNGVAFKKTFSYAgfeQQPKKFANPKILLLNVELELKAEKDNAEIRVEDVED 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 258 LMEFIEQEEKMLKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATGANVITNIKDLSAQDL 337
Cdd:TIGR02345 261 YQAIVDAEWAIIFRKLEKIVESGANVVLSKLPIGDLATQYFADRDIFCAGRVSAEDLKRVIKACGGSIQSTTSDLEADVL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 338 GDAGLVEERKISGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIVSGGGSTEVELSMKLRE 417
Cdd:TIGR02345 341 GTCALFEERQIGSERYNYFTGCPHAKTCTIILRGGAEQFIEEAERSLHDAIMIVRRALKNKKIVAGGGAIEMELSKCLRD 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 418 YAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHAsNGNKCAGLNVFTGAVEDMCENGVVEPLRVKTQ 497
Cdd:TIGR02345 421 YSKTIDGKQQLIINAFAKALEIIPRQLCENAGFDSIEILNKLRSRHA-KGGKWYGVDINTEDIGDNFEAFVWEPALVKIN 499
|
490 500
....*....|....*....|...
gi 291191278 498 AIQSAAESTEMLLRIDDVIAAEK 520
Cdd:TIGR02345 500 ALKAAFEAACTILSVDETITNPK 522
|
|
| chap_CCT_alpha |
TIGR02340 |
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ... |
13-516 |
9.60e-138 |
|
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: 409.50 E-value: 9.60e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 13 KRYMGRDAQRMNILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQEKEVGDG 92
Cdd:TIGR02340 6 ERTSGQDVRTQNVTAAMAIANIVKTSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDREVGDG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 93 TTTAVVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKA-QELLKTIACEVGAQDKEILTKIAMTSITGKGAEKAKEKLA 171
Cdd:TIGR02340 86 TTSVVIIAAELLKRADELVKNKIHPTSVISGYRLACKEAvKYIKENLSVSVDELGREALINVAKTSMSSKIIGLDSDFFS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 172 EIIVEAVSAV--VDDEGKVDKDL--IKIEKKSGASIDDTELIKGVLVDKERVSAQMPKKVTDAKIALLNCAIEIKETETD 247
Cdd:TIGR02340 166 NIVVDAVLAVktTNENGETKYPIkaINILKAHGKSARESMLVKGYALNCTVASQQMPKRIKNAKIACLDFNLQKAKMALG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 248 AEIRITDPAKLMEFIEQEEKMLKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATGANVIT 327
Cdd:TIGR02340 246 VQIVVDDPEKLEQIRQREADITKERIKKILDAGANVVLTTGGIDDMCLKYFVEAGAMGVRRCKKEDLKRIAKATGATLVS 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 328 NIKDLSAQD------LGDAGLVEERKISGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIV 401
Cdd:TIGR02340 326 TLADLEGEEtfeasyLGFADEVVQERIADDECILIKGTKKRKSASIILRGANDFMLDEMERSLHDALCVVKRTLESNSVV 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 402 SGGGSTEVELSMKLREYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHAS-------NGNKCAGLN 474
Cdd:TIGR02340 406 PGGGAVEAALSIYLENFATTLGSREQLAIAEFARALLIIPKTLAVNAAKDSTELVAKLRAYHAAaqlkpekKHLKWYGLD 485
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 291191278 475 VFTGAVEDMCENGVVEPLRVKTQAIQSAAESTEMLLRIDDVI 516
Cdd:TIGR02340 486 LVNGKIRDNKEAGVLEPTVSKVKSLKFATEAAITILRIDDLI 527
|
|
| chap_CCT_delta |
TIGR02342 |
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ... |
19-518 |
1.52e-136 |
|
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: 405.71 E-value: 1.52e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 19 DAQRMNILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQEKEVGDGTTTAVV 98
Cdd:TIGR02342 9 DVRTSNIVAAKAVADAIRTSLGPKGMDKMIQDGKGEVIITNDGATILKQMAVLHPAAKMLVELSKAQDIEAGDGTTSVVI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 99 VAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQDKEILTKIAMTSITGKGAEKAKEKLAEIIVEAV 178
Cdd:TIGR02342 89 LAGALLGACERLLNKGIHPTIISESFQSAADEAIKILDEMSIPVDLSDREQLLKSATTSLSSKVVSQYSSLLAPLAVDAV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 179 SAVVDDEGKVDKDL--IKIEKKSGASIDDTELIKGVLVD-KERVSAQMPKKVTDAKIALLNCAIEIKETETDAEIRITDP 255
Cdd:TIGR02342 169 LKVIDPENAKNVDLndIKVVKKLGGTIDDTELIEGLVFTqKASKSAGGPTRIEKAKIGLIQFQISPPKTDMENQIIVNDY 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 256 AKLMEFIEQEEKMLKDMVAEIKASGANVLFCQKGI-----DDLAQHYLAKEGIVAARRVKKSDMEKLAKATGANVITNIK 330
Cdd:TIGR02342 249 AQMDRVLKEERAYILNIVKKIKKTGCNVLLIQKSIlrdavNDLALHFLAKMKIMVVKDIEREEIEFICKTIGCKPIASID 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 331 DLSAQDLGDAGLVEERKISGDSMIFVEECKHP-KAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIVSGGGSTEV 409
Cdd:TIGR02342 329 HFTADKLGSAELVEEVDSDGGKIIKITGIQNAgKTVTVVVRGSNKLVIDEAERSLHDALCVIRCLVKKRGLIAGGGAPEI 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 410 ELSMKLREYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHAsNGNKCAGLNVFTGAVEDMCENGVV 489
Cdd:TIGR02342 409 EIARRLSKYARTMKGVESYCVRAFADALEVIPYTLAENAGLNPIKVVTELRNRHA-NGEKTAGISVRKGGITNMLEEHVL 487
|
490 500
....*....|....*....|....*....
gi 291191278 490 EPLRVKTQAIQSAAESTEMLLRIDDVIAA 518
Cdd:TIGR02342 488 QPLLVTTSAITLASETVRSILKIDDIVFT 516
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
1-518 |
1.43e-123 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 373.21 E-value: 1.43e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 1 MSQQPGVLPENMKRYMGRDAQRMNILAGRIIAETVRSTLGPKGMDKMLV-----DDLGDVVVTNDGVTILREMSVEHPAA 75
Cdd:PTZ00212 4 ANVPPQVLKQGAQEEKGETARLQSFVGAIAVADLVKTTLGPKGMDKILQpmsegPRSGNVTVTNDGATILKSVWLDNPAA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 76 KMLIEVAKTQEKEVGDGTTTAVVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQD---KEILTK 152
Cdd:PTZ00212 84 KILVDISKTQDEEVGDGTTSVVVLAGELLREAEKLLDQKIHPQTIIEGWRMALDVARKALEEIAFDHGSDEekfKEDLLN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 153 IAMTSITGKGAEKAKEKLAEIiveAVSAVVDDEGKVDKDLIKIEKKSGASIDDTELIKGVLVDKeRVSAQMPKKVTDAKI 232
Cdd:PTZ00212 164 IARTTLSSKLLTVEKDHFAKL---AVDAVLRLKGSGNLDYIQIIKKPGGTLRDSYLEDGFILEK-KIGVGQPKRLENCKI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 233 ALLNCAIEiketeTD------AEIRITDPAKLMEfIEQEEKM-LKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVA 305
Cdd:PTZ00212 240 LVANTPMD-----TDkikiygAKVKVDSMEKVAE-IEAAEKEkMKNKVDKILAHGCNVFINRQLIYNYPEQLFAEAGIMA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 306 ARRVKKSDMEKLAKATGANVITNIKDLSAQDLGDAGLVEERKISGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVD 385
Cdd:PTZ00212 314 IEHADFDGMERLAAALGAEIVSTFDTPEKVKLGHCDLIEEIMIGEDKLIRFSGCAKGEACTIVLRGASTHILDEAERSLH 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 386 DAVGVVGCTIEDGRIVSGGGSTEVELSMKLREYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHAs 465
Cdd:PTZ00212 394 DALCVLSQTVKDTRVVLGGGCSEMLMANAVEELAKKVEGKKSLAIEAFAKALRQIPTIIADNGGYDSAELVSKLRAEHY- 472
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 291191278 466 NGNKCAGLNVFTGAVEDMCENGVVEPLRVKTQAIQSAAESTEMLLRIDDVIAA 518
Cdd:PTZ00212 473 KGNKTAGIDMEKGTVGDMKELGITESYKVKLSQLCSATEAAEMILRVDDIIRC 525
|
|
| TCP1_beta |
cd03336 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ... |
7-518 |
1.60e-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: 362.03 E-value: 1.60e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 7 VLPENMKRYMGRDAQRMNILAGRIIAETVRSTLGPKGMDKML--VDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKT 84
Cdd:cd03336 1 ILKDGAQEEKGETARLSSFVGAIAIGDLVKTTLGPKGMDKILqsVGRSGGVTVTNDGATILKSIGVDNPAAKVLVDISKV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 85 QEKEVGDGTTTAVVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQD---KEILTKIAMTSITGK 161
Cdd:cd03336 81 QDDEVGDGTTSVTVLAAELLREAEKLVAQKIHPQTIIEGYRMATAAAREALLSSAVDHSSDEeafREDLLNIARTTLSSK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 162 GAEKAKEKLAEIiveAVSAVVDDEGKVDKDLIKIEKKSGASIDDTELIKGVLVDKeRVSAQMPKKVTDAKIALLNCAIEi 241
Cdd:cd03336 161 ILTQDKEHFAEL---AVDAVLRLKGSGNLDAIQIIKKLGGSLKDSYLDEGFLLDK-KIGVNQPKRIENAKILIANTPMD- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 242 keteTD------AEIRITDPAKLMEfIEQEEKM-LKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDM 314
Cdd:cd03336 236 ----TDkikifgAKVRVDSTAKVAE-IEEAEKEkMKNKVEKILKHGINCFINRQLIYNYPEQLFADAGIMAIEHADFDGV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 315 EKLAKATGANVITNIKDLSAQDLGDAGLVEERKISGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCT 394
Cdd:cd03336 311 ERLALVTGGEIASTFDHPELVKLGTCKLIEEIMIGEDKLIRFSGVAAGEACTIVLRGASQQILDEAERSLHDALCVLAQT 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 395 IEDGRIVSGGGSTEVELSMKLREYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHAsNGNKCAGLN 474
Cdd:cd03336 391 VKDTRVVLGGGCSEMLMAKAVEELAKKTPGKKSLAIEAFAKALRQLPTIIADNAGYDSAELVAQLRAAHY-NGNTTAGLD 469
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 291191278 475 VFTGAVEDMCENGVVEPLRVKTQAIQSAAESTEMLLRIDDVIAA 518
Cdd:cd03336 470 MRKGTVGDMKELGITESFKVKRQVLLSASEAAEMILRVDDIIKC 513
|
|
| TCP1_zeta |
cd03342 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
20-518 |
3.82e-119 |
|
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: 360.03 E-value: 3.82e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 20 AQRMNILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQEKEVGDGTTTAVVV 99
Cdd:cd03342 13 ALAVNISAAKGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLSEMQIQHPTASMIARAATAQDDITGDGTTSNVLL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 100 AGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVG-AQDKEILTKIAMTSITGKGAEKAKEKLAEIIVEAV 178
Cdd:cd03342 93 IGELLKQAERYIQEGVHPRIITEGFELAKNKALKFLESFKVPVEiDTDRELLLSVARTSLRTKLHADLADQLTEIVVDAV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 179 SAVVDDEGKVDKDLIKIEKKSGASIDDTELIKGVLVDKERVSAQMPKKVTDAKIALLNCAIEIKETETDAEiritdpakl 258
Cdd:cd03342 173 LAIYKPDEPIDLHMVEIMQMQHKSDSDTKLIRGLVLDHGARHPDMPKRVENAYILTCNVSLEYEKTEVNSG--------- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 259 meFIeqeekmlkdmvaeikasgANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATGANVITNIKDLSAQDLG 338
Cdd:cd03342 244 --FF------------------YSVVINQKGIDPPSLDMLAKEGILALRRAKRRNMERLTLACGGVAMNSVDDLSPECLG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 339 DAGLVEERKISGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIVSGGGSTEVELSMKLREY 418
Cdd:cd03342 304 YAGLVYERTLGEEKYTFIEGVKNPKSCTILIKGPNDHTITQIKDAIRDGLRAVKNAIEDKCVVPGAGAFEVALYAHLKEF 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 419 AEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHASnGNKCAGLNVFTGAVEDMCENGVVEPLRVKTQA 498
Cdd:cd03342 384 KKSVKGKAKLGVQAFADALLVIPKTLAENSGLDVQETLVKLQDEYAE-GGQVGGVDLDTGEPMDPESEGIWDNYSVKRQI 462
|
490 500
....*....|....*....|
gi 291191278 499 IQSAAESTEMLLRIDDVIAA 518
Cdd:cd03342 463 LHSATVIASQLLLVDEIIRA 482
|
|
| chap_CCT_zeta |
TIGR02347 |
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ... |
20-518 |
1.44e-116 |
|
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: 354.81 E-value: 1.44e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 20 AQRMNILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQEKEVGDGTTTAVVV 99
Cdd:TIGR02347 17 ALMMNINAARGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEMQIQHPTASMIARAATAQDDITGDGTTSTVLL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 100 AGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQ-DKEILTKIAMTSITGKGAEKAKEKLAEIIVEAV 178
Cdd:TIGR02347 97 IGELLKQAERYILEGVHPRIITEGFEIARKEALQFLDKFKVKKEDEvDREFLLNVARTSLRTKLPADLADQLTEIVVDAV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 179 SAVVDDEGKVDKDLIKIEKKSGASIDDTELIKGVLVDKERVSAQMPKKVTDAKIALLNCAIEIKETETDAEIRITDPAKL 258
Cdd:TIGR02347 177 LAIKKDGEDIDLFMVEIMEMKHKSATDTTLIRGLVLDHGARHPDMPRRVKNAYILTCNVSLEYEKTEVNSGFFYSSAEQR 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 259 MEFIEQEEKMLKDMVAEI-----KASGAN-----VLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATGANVITN 328
Cdd:TIGR02347 257 EKLVKAERKFVDDRVKKIielkkKVCGKSpdkgfVVINQKGIDPPSLDLLAKEGIMALRRAKRRNMERLTLACGGEALNS 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 329 IKDLSAQDLGDAGLVEERKISGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIVSGGGSTE 408
Cdd:TIGR02347 337 VEDLTPECLGWAGLVYETTIGEEKYTFIEECKNPKSCTILIKGPNDHTIAQIKDAVRDGLRAVKNAIEDKCVVPGAGAFE 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 409 VELSMKLREYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHaSNGNKCAGLNVFTGAVEDMCENGV 488
Cdd:TIGR02347 417 IAAYRHLKEYKKSVKGKAKLGVEAFANALLVIPKTLAENSGFDAQDTLVKLEDEH-DEGGEVVGVDLNTGEPIDPEIKGI 495
|
490 500 510
....*....|....*....|....*....|
gi 291191278 489 VEPLRVKTQAIQSAAESTEMLLRIDDVIAA 518
Cdd:TIGR02347 496 WDNYRVKKQLIQSATVIASQLLLVDEVMRA 525
|
|
| TCP1_theta |
cd03341 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ... |
24-518 |
1.44e-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: 347.67 E-value: 1.44e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 24 NILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQEKEVGDGTTTAVVVAGEL 103
Cdd:cd03341 13 NIEACKELSQITRTSYGPNGMNKMVINHLEKLFVTSDAATILRELEVQHPAAKLLVMASQMQEEEIGDGTNLVVVLAGEL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 104 LRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACE--VGAQDKEILTKIAMTSITGKGAEKAkEKLAEIIVEAVSAV 181
Cdd:cd03341 93 LEKAEELLRMGLHPSEIIEGYEKALKKALEILEELVVYkiEDLRNKEEVSKALKTAIASKQYGNE-DFLSPLVAEACISV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 182 V-DDEGKVDKDLIKIEKKSGASIDDTELIKGVLVDKErVSAQMpKKVTDAKIALLNCAIEIketetdaeiritdpaklme 260
Cdd:cd03341 172 LpENIGNFNVDNIRVVKILGGSLEDSKVVRGMVFKRE-PEGSV-KRVKKAKVAVFSCPFDI------------------- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 261 fieqeekmlkdmvaeikasGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATGANVITNIKDLSAQDLGDA 340
Cdd:cd03341 231 -------------------GVNVIVAGGSVGDLALHYCNKYGIMVIKINSKFELRRLCRTVGATPLPRLGAPTPEEIGYC 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 341 GLVEERKISGDSMIFVEECKHPKAV-TMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIVSGGGSTEVELSMKLREYA 419
Cdd:cd03341 292 DSVYVEEIGDTKVVVFRQNKEDSKIaTIVLRGATQNILDDVERAIDDGVNVFKSLTKDGRFVPGAGATEIELAKKLKEYG 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 420 EGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHaSNGNKCAGLNVFTG--AVEDMCENGVVEPLRVKTQ 497
Cdd:cd03341 372 EKTPGLEQYAIKKFAEAFEVVPRTLAENAGLDATEVLSELYAAH-QKGNKSAGVDIESGdeGTKDAKEAGIFDHLATKKW 450
|
490 500
....*....|....*....|.
gi 291191278 498 AIQSAAESTEMLLRIDDVIAA 518
Cdd:cd03341 451 AIKLATEAAVTVLRVDQIIMA 471
|
|
| chap_CCT_theta |
TIGR02346 |
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ... |
5-523 |
1.44e-114 |
|
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: 349.78 E-value: 1.44e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 5 PGVLPENMKRYMGRDAQRM-NILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAK 83
Cdd:TIGR02346 3 ASLLKEGYRHFSGLEEAVIkNIEACKELSQITRTSLGPNGMNKMVINHLEKLFVTNDAATILRELEVQHPAAKLLVMASE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 84 TQEKEVGDGTTTAVVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKT-IACEV-GAQDKEILTKIAMTSITGK 161
Cdd:TIGR02346 83 MQENEIGDGTNLVLVLAGELLNKAEELIRMGLHPSEIIKGYEMALKKAMEILEElVVWEVkDLRDKDELIKALKASISSK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 162 GAEKAkEKLAEIIVEAVSAVV-DDEGKVDKDLIKIEKKSGASIDDTELIKGVLVDKERVSAQmpKKVTDAKIALLNCAIE 240
Cdd:TIGR02346 163 QYGNE-DFLAQLVAQACSTVLpKNPQNFNVDNIRVCKILGGSLSNSEVLKGMVFNREAEGSV--KSVKNAKVAVFSCPLD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 241 IKETETDAEIRITDPAKLMEFIEQEEKMLKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKA 320
Cdd:TIGR02346 240 TATTETKGTVLIHNAEELLNYSKGEENQIEAMIKAIADSGVNVIVTGGSVGDMALHYLNKYNIMVLKIPSKFELRRLCKT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 321 TGANVITNIKDLSAQDLGDAGLVEERKISGDSM-IFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGR 399
Cdd:TIGR02346 320 VGATPLPRLGAPTPEEIGYVDSVYVSEIGGDKVtVFKQENGDSKISTIILRGSTDNLLDDIERAIDDGVNTVKALVKDGR 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 400 IVSGGGSTEVELSMKLREYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHASnGNKCAGLNVFTG- 478
Cdd:TIGR02346 400 LLPGAGATEIELASRLTKYGEKLPGLDQYAIKKFAEAFEIIPRTLAENAGLNANEVIPKLYAAHKK-GNKSKGIDIEAEs 478
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 291191278 479 -AVEDMCENGVVEPLRVKTQAIQSAAESTEMLLRIDDVIAAEKLRG 523
Cdd:TIGR02346 479 dGVKDASEAGIYDMLATKKWAIKLATEAAVTVLRVDQIIMAKPAGG 524
|
|
| chap_CCT_beta |
TIGR02341 |
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ... |
22-518 |
7.89e-94 |
|
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: 296.00 E-value: 7.89e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 22 RMNILAGRI-IAETVRSTLGPKGMDKMLVDD--LGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQEKEVGDGTTTAVV 98
Cdd:TIGR02341 16 RLSSFVGAIaIGDLVKSTLGPKGMDKILQSSssDASIMVTNDGATILKSIGVDNPAAKVLVDMSKVQDDEVGDGTTSVTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 99 VAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQDKEI---LTKIAMTSITGKGAEKAKEKLAEIiv 175
Cdd:TIGR02341 96 LAAELLREAEKLINQKIHPQTIIAGYREATKAARDALLKSAVDNGSDEVKFrqdLMNIARTTLSSKILSQHKDHFAQL-- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 176 eAVSAVVDDEGKVDKDLIKIEKKSGASIDDTELIKGVLVDKeRVSAQMPKKVTDAKIALLNCAIEIKETET-DAEIRITD 254
Cdd:TIGR02341 174 -AVDAVLRLKGSGNLEAIQIIKKLGGSLADSYLDEGFLLDK-KIGVNQPKRIENAKILIANTGMDTDKVKIfGSRVRVDS 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 255 PAKLMEFIEQEEKMLKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATGANVITNIKDLSA 334
Cdd:TIGR02341 252 TAKVAELEHAEKEKMKEKVEKILKHGINCFINRQLIYNYPEQLFADAGVMAIEHADFEGVERLALVTGGEIVSTFDHPEL 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 335 QDLGDAGLVEERKISGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIVSGGGSTEVELSMK 414
Cdd:TIGR02341 332 VKLGSCDLIEEIMIGEDKLLKFSGVKLGEACTIVLRGATQQILDEAERSLHDALCVLSQTVKESRTVLGGGCSEMLMSKA 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 415 LREYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHAsNGNKCAGLNVFTGAVEDMCENGVVEPLRV 494
Cdd:TIGR02341 412 VTQEAQRTPGKEALAVEAFARALRQLPTIIADNAGFDSAELVAQLRAAHY-NGNTTMGLDMNEGTIADMRQLGITESYKV 490
|
490 500
....*....|....*....|....
gi 291191278 495 KTQAIQSAAESTEMLLRIDDVIAA 518
Cdd:TIGR02341 491 KRAVVSSAAEAAEVILRVDNIIKA 514
|
|
| chaperonin_like |
cd03333 |
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ... |
147-397 |
4.27e-72 |
|
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: 228.89 E-value: 4.27e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 147 KEILTKIAMTSITGKGaEKAKEKLAEIIVEAVSAVVDDEGKVDKDLIKIEKKSGASIDDTELIKGVLVDKERVSAQMPKK 226
Cdd:cd03333 1 RELLLQVATTSLNSKL-SSWDDFLGKLVVDAVLKVGPDNRMDDLGVIKVEKIPGGSLEDSELVVGVVFDKGYASPYMPKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 227 VTDAKIALLNCAIEiketetdaeiritdpaklmefieqeekmlkdmvaeikasgaNVLFCQKGIDDLAQHYLAKEGIVAA 306
Cdd:cd03333 80 LENAKILLLDCPLE-----------------------------------------YVVIAEKGIDDLALHYLAKAGIMAV 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 307 RRVKKSDMEKLAKATGANVITNIKDLSAQDLGDAGLVEERKISGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDD 386
Cdd:cd03333 119 RRVKKEDLERIARATGATIVSSLEDLTPEDLGTAELVEETKIGEEKLTFIEGCKGGKAATILLRGATEVELDEVKRSLHD 198
|
250
....*....|.
gi 291191278 387 AVGVVGCTIED 397
Cdd:cd03333 199 ALCAVRAAVEE 209
|
|
| GroEL |
cd03344 |
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ... |
22-503 |
2.70e-34 |
|
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: 136.05 E-value: 2.70e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 22 RMNILAG-RIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHP----AAKMLIEVAKTQEKEVGDGTTTA 96
Cdd:cd03344 10 RKALLRGvNKLADAVKVTLGPKGRNVVIEKSFGSPKITKDGVTVAKEIELEDPfenmGAQLVKEVASKTNDVAGDGTTTA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 97 VVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVgaQDKEILTKIAMTSITGkgaekaKEKLAEIIVE 176
Cdd:cd03344 90 TVLARAIIKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKPV--KTKEEIAQVATISANG------DEEIGELIAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 177 AVSavvddegKVDKD-LIKIEkkSGASIDDT-ELIKGVLVDKERVSaqmPKKVTDAK---IALLNCAIEIketeTDAEIR 251
Cdd:cd03344 162 AME-------KVGKDgVITVE--EGKTLETElEVVEGMQFDRGYLS---PYFVTDPEkmeVELENPYILL----TDKKIS 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 252 -ITDPAKLMEFIEQEEKMLKdMVAEikasganvlfcqkgidDLAQHYLA------KEGIVAARRVK--------KSDMEK 316
Cdd:cd03344 226 sIQELLPILELVAKAGRPLL-IIAE----------------DVEGEALAtlvvnkLRGGLKVCAVKapgfgdrrKAMLED 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 317 LAKATGANVITN-----IKDLSAQDLGDAGLVEerkISGDSMIFVEECKHPKAV-------------------------- 365
Cdd:cd03344 289 IAILTGGTVISEelglkLEDVTLEDLGRAKKVV---VTKDDTTIIGGAGDKAAIkariaqirkqieettsdydkeklqer 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 366 -------TMLIR--GTTEHVIEEVARAVDDAVGVVGCTIEDGrIVSGGGSTEVELSMKLrEYAEGISGREQLAVRAFADA 436
Cdd:cd03344 366 laklsggVAVIKvgGATEVELKEKKDRVEDALNATRAAVEEG-IVPGGGVALLRASPAL-DKLKALNGDEKLGIEIVRRA 443
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 291191278 437 LEVIPRTLAENAGLDAIEILVKVRaahasNGNKCAGLNVFTGAVEDMCENGVVEPLRVKTQAIQSAA 503
Cdd:cd03344 444 LEAPLRQIAENAGVDGSVVVEKVL-----ESPDGFGYDAATGEYVDMIEAGIIDPTKVVRSALQNAA 505
|
|
| groEL |
PRK12849 |
chaperonin GroEL; Reviewed |
18-517 |
2.67e-31 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237230 Cd Length: 542 Bit Score: 127.62 E-value: 2.67e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 18 RDAQRMNILAG-RIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHP----AAKMLIEVAKTQEKEVGDG 92
Cdd:PRK12849 8 DEEARRALERGvNKLADAVKVTLGPKGRNVVIDKSFGAPTITKDGVSIAKEIELEDPfenlGAQLVKEVASKTNDVAGDG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 93 TTTAVVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVgaQDKEILTKIAMTSITGKgaekakEKLAE 172
Cdd:PRK12849 88 TTTATVLAQALVQEGLKNVAAGANPMDLKRGIDKAVEAVVEELKALARPV--SGSEEIAQVATISANGD------EEIGE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 173 IIVEAVSavvddegKVDKD-LIKIEKKSGASiDDTELIKGVLVDKERVSAQMpkkVTDAK--IALL-NCAIEIketeTDA 248
Cdd:PRK12849 160 LIAEAME-------KVGKDgVITVEESKTLE-TELEVTEGMQFDRGYLSPYF---VTDPErmEAVLeDPLILL----TDK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 249 EIR-ITDPAKLMEFIEQEEKMLKdMVAEikasganvlfcqkgidDLAQHYLA-------KEGI-VAA--------RRvkK 311
Cdd:PRK12849 225 KISsLQDLLPLLEKVAQSGKPLL-IIAE----------------DVEGEALAtlvvnklRGGLkVAAvkapgfgdRR--K 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 312 SDMEKLAKATGANVIT-----NIKDLSAQDLGDAGLVEerkISGDSMIFVEECKHPKAV--------------------- 365
Cdd:PRK12849 286 AMLEDIAILTGGTVISedlglKLEEVTLDDLGRAKRVT---ITKDNTTIVDGAGDKEAIearvaqirrqieettsdydre 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 366 ------------TMLIR--GTTEHVIEEVARAVDDAVGVVGCTIEDGrIVSGGGSTEVELSMKLREYAeGISGREQLAVR 431
Cdd:PRK12849 363 klqerlaklaggVAVIKvgAATEVELKERKDRVEDALNATRAAVEEG-IVPGGGVALLRAAKALDELA-GLNGDQAAGVE 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 432 AFADALEVIPRTLAENAGLDAIEILVKVRAahasnGNKCAGLNVFTGAVEDMCENGVVEPLRVKTQAIQSAAESTEMLLR 511
Cdd:PRK12849 441 IVRRALEAPLRQIAENAGLDGSVVVAKVLE-----LEDGFGFNAATGEYGDLIAAGIIDPVKVTRSALQNAASVAGLLLT 515
|
....*.
gi 291191278 512 IDDVIA 517
Cdd:PRK12849 516 TEALVA 521
|
|
| Fab1_TCP |
cd03334 |
TCP-1 like domain of the eukaryotic phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinase Fab1. ... |
160-391 |
9.11e-28 |
|
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: 111.93 E-value: 9.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 160 GKGAEKAKEKLAEIIVEAVSAVVDDEGKVDKDLI----KIEKKSGASIDDTELIKGVLVDKERVSAQMPKKVTDAKIALL 235
Cdd:cd03334 13 ISNDESWLDILLPLVWKAASNVKPDVRAGDDMDIrqyvKIKKIPGGSPSDSEVVDGVVFTKNVAHKRMPSKIKNPRILLL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 236 NCAIEIKETETdaeiritdpaKLMEF---IEQEEKMLKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKS 312
Cdd:cd03334 93 QGPLEYQRVEN----------KLLSLdpvILQEKEYLKNLVSRIVALRPDVILVEKSVSRIAQDLLLEAGITLVLNVKPS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 313 DMEKLAKATGANVITNIKDLSA-QDLGDAGLVEERKI-----SGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDD 386
Cdd:cd03334 163 VLERISRCTGADIISSMDDLLTsPKLGTCESFRVRTYveehgRSKTLMFFEGCPKELGCTILLRGGDLEELKKVKRVVEF 242
|
....*
gi 291191278 387 AVGVV 391
Cdd:cd03334 243 MVFAA 247
|
|
| GroEL |
TIGR02348 |
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ... |
13-517 |
3.54e-27 |
|
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES cytosolic chaperonin. It is found in bacteria, organelles derived from bacteria, and occasionally in the Archaea. The bacterial GroEL/GroES group I chaperonin is replaced a group II chaperonin, usually called the thermosome in the Archaeota and CCT (chaperone-containing TCP) in the Eukaryota. GroEL, thermosome subunits, and CCT subunits all fall under the scope of pfam00118. [Protein fate, Protein folding and stabilization]
Pssm-ID: 274089 Cd Length: 524 Bit Score: 115.08 E-value: 3.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 13 KRYMGRDAQRMNILAG-RIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHP----AAKMLIEVAKTQEK 87
Cdd:TIGR02348 2 KQIKFDEEARKALLRGvDKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDKfenmGAQLVKEVASKTND 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 88 EVGDGTTTAVVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGaqDKEILTKIAMTSITGkgaekaK 167
Cdd:TIGR02348 82 VAGDGTTTATVLAQAIVKEGLKNVAAGANPIELKRGIEKAVEAVVEELKKLSKPVK--GKKEIAQVATISANN------D 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 168 EKLAEIIVEAVSavvddegKVDKD-LIKIEKKSGAsIDDTELIKGVLVDKERVSaqmPKKVTDAkiallncaiEIKETE- 245
Cdd:TIGR02348 154 EEIGSLIAEAME-------KVGKDgVITVEESKSL-ETELEVVEGMQFDRGYIS---PYFVTDA---------EKMEVEl 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 246 TDAEIRITDpaklmefieQEEKMLKDMV---AEIKASGANVLFCQKGIDDLAQHYLA---KEGIVAARRVK--------K 311
Cdd:TIGR02348 214 ENPYILITD---------KKISNIKDLLpllEKVAQSGKPLLIIAEDVEGEALATLVvnkLRGTLNVCAVKapgfgdrrK 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 312 SDMEKLAKATGANVIT-----NIKDLSAQDLGDAGLVeerKISGDSMIFVEECKHPKAVTMLIR---------------- 370
Cdd:TIGR02348 285 AMLEDIAILTGGQVISeelglKLEEVTLDDLGKAKKV---TVDKDNTTIVEGAGDKAAIKARVAqikaqieettsdydre 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 371 -------------------GTTEHVIEEVARAVDDAVGVVGCTIEDGrIVSGGGSTEVELSMKLrEYAEGISGREQLAVR 431
Cdd:TIGR02348 362 klqerlaklaggvavikvgAATETEMKEKKLRIEDALNATRAAVEEG-IVPGGGVALLRAAAAL-EGLKGDGEDEAIGID 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 432 AFADALEVIPRTLAENAGLDAIEILVKVRaahASNGNKcaGLNVFTGAVEDMCENGVVEPLRVKTQAIQSAAESTEMLLR 511
Cdd:TIGR02348 440 IVKRALEAPLRQIAENAGLDGAVVAEKVK---ELKGNF--GFNAATGEYEDLVEAGIIDPTKVTRSALQNAASIAGLLLT 514
|
....*.
gi 291191278 512 IDDVIA 517
Cdd:TIGR02348 515 TEAVVA 520
|
|
| groEL |
PRK12850 |
chaperonin GroEL; Reviewed |
30-524 |
1.43e-24 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237231 Cd Length: 544 Bit Score: 107.50 E-value: 1.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 30 IIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHP----AAKMLIEVAKTQEKEVGDGTTTAVVVAGELLR 105
Cdd:PRK12850 22 ILANAVKVTLGPKGRNVVLEKSFGAPRITKDGVTVAKEIELEDKfenmGAQMVKEVASKTNDLAGDGTTTATVLAQAIVR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 106 KAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQDKeiLTKIAMTSITGkgaekaKEKLAEIIVEAVSavvdde 185
Cdd:PRK12850 102 EGAKLVAAGMNPMDLKRGIDLAVAAVVDELKKIAKKVTSSKE--IAQVATISANG------DESIGEMIAEAMD------ 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 186 gKVDKD-LIKIEKKSGASiDDTELIKGVLVDKERVSaqmPKKVTDAKiallncaieiketetDAEIRITDPAKLMEfiEQ 264
Cdd:PRK12850 168 -KVGKEgVITVEEAKTLG-TELDVVEGMQFDRGYLS---PYFVTNPE---------------KMRAELEDPYILLH--EK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 265 EEKMLKDMVAEIKA---SGANVLFCQKGIDDLAQHYLAKEGI-----VAARRV------KKSDMEKLAKATGANVI---T 327
Cdd:PRK12850 226 KISNLQDLLPILEAvvqSGRPLLIIAEDVEGEALATLVVNKLrgglkSVAVKApgfgdrRKAMLEDIAVLTGGQVIsedL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 328 NIK--DLSAQDLGDAGLVEerkISGDSMIFVEECKHPKAV---------------------------------TMLIR-- 370
Cdd:PRK12850 306 GIKleNVTLDMLGRAKRVL---ITKENTTIIDGAGDKKNIearvkqiraqieettsdydreklqerlaklaggVAVIRvg 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 371 GTTEHVIEEVARAVDDAVGVVGCTIEDGrIVSGGGSTEVELSMKLREyAEGISGREQLAVRAFADALEVIPRTLAENAGL 450
Cdd:PRK12850 383 GATEVEVKEKKDRVDDALHATRAAVEEG-IVPGGGVALLRARSALRG-LKGANADETAGIDIVRRALEEPLRQIATNAGF 460
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 291191278 451 DAIEILVKVRaahasNGNKCAGLNVFTGAVEDMCENGVVEPLRVKTQAIQSAAESTEMLLRIDDVIAAEKLRGA 524
Cdd:PRK12850 461 EGSVVVGKVA-----ELPGNFGFNAQTGEYGDMVEAGIIDPAKVTRTALQDAASIAALLITTEAMVAEAPKKAA 529
|
|
| PTZ00114 |
PTZ00114 |
Heat shock protein 60; Provisional |
22-510 |
1.19e-21 |
|
Heat shock protein 60; Provisional
Pssm-ID: 185455 Cd Length: 555 Bit Score: 98.45 E-value: 1.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 22 RMNILAG-RIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILR--EMS--VEHPAAKMLIEVAKTQEKEVGDGTTTA 96
Cdd:PTZ00114 24 RQSLLKGiERLADAVAVTLGPKGRNVIIEQEYGSPKITKDGVTVAKaiEFSdrFENVGAQLIRQVASKTNDKAGDGTTTA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 97 VVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVgaQDKEILTKIAMTSITGkgaekaKEKLAEIIVE 176
Cdd:PTZ00114 104 TILARAIFREGCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQSRPV--KTKEDILNVATISANG------DVEIGSLIAD 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 177 AVsavvddeGKVDKD-LIKIEkkSGASIDDT-ELIKGVLVDKERVSaqmPKKVTDA---KIALLNCAIEIKETETDAeir 251
Cdd:PTZ00114 176 AM-------DKVGKDgTITVE--DGKTLEDElEVVEGMSFDRGYIS---PYFVTNEktqKVELENPLILVTDKKISS--- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 252 ITDPAKLMEFIEQEEKMLKDMVAEIKASGANVLFCQKgiddlaqhylAKEGI-VAARRV------KKSDMEKLAKATGAN 324
Cdd:PTZ00114 241 IQSILPILEHAVKNKRPLLIIAEDVEGEALQTLIINK----------LRGGLkVCAVKApgfgdnRKDILQDIAVLTGAT 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 325 VITN------IKDLSAQDLGDAGLVEerkISGDSMIFVEECKHPKAV--------------------------------- 365
Cdd:PTZ00114 311 VVSEdnvglkLDDFDPSMLGSAKKVT---VTKDETVILTGGGDKAEIkervellrsqierttseydkeklkerlaklsgg 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 366 --TMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGrIVSGGGSTEVELSMKLREYAEG--ISGREQLAVRAFADALEVIP 441
Cdd:PTZ00114 388 vaVIKVGGASEVEVNEKKDRIEDALNATRAAVEEG-IVPGGGVALLRASKLLDKLEEDneLTPDQRTGVKIVRNALRLPT 466
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 291191278 442 RTLAENAGLDAIEILVKVraahASNGNKCAGLNVFTGAVEDMCENGVVEPLRVKTQAIQSAAESTEMLL 510
Cdd:PTZ00114 467 KQIAENAGVEGAVVVEKI----LEKKDPSFGYDAQTGEYVNMFEAGIIDPTKVVRSALVDAASVASLML 531
|
|
| groEL |
PRK12851 |
chaperonin GroEL; Reviewed |
13-517 |
1.91e-21 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 171770 Cd Length: 541 Bit Score: 97.89 E-value: 1.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 13 KRYMGRDAQRMNILAG-RIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHP----AAKMLIEVAKTQEK 87
Cdd:PRK12851 4 KEVKFHVEAREKMLRGvNILADAVKVTLGPKGRNVVIDKSFGAPTITNDGVTIAKEIELEDKfenmGAQMVREVASKTND 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 88 EVGDGTTTAVVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQDKeiltKIAMTSITGKGaekaK 167
Cdd:PRK12851 84 VAGDGTTTATVLAQAIVREGAKAVAAGANPMDLKRGIDRAVAAVVEELKANARPVTTNAE----IAQVATISANG----D 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 168 EKLAEIIVEAVsavvddeGKVDKDLIKIEKKSGASIDDTELIKGVLVDKERVSaqmPKKVTDAKiallncaieiketetD 247
Cdd:PRK12851 156 AEIGRLVAEAM-------EKVGNEGVITVEESKTAETELEVVEGMQFDRGYLS---PYFVTDAD---------------K 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 248 AEIRITDPAKLMefIEQEEKMLKDMVA---EIKASGANVLFCQKGIDDLAQHYLAKEGI-----VAARRV------KKSD 313
Cdd:PRK12851 211 MEAELEDPYILI--HEKKISNLQDLLPvleAVVQSGKPLLIIAEDVEGEALATLVVNKLrgglkVAAVKApgfgdrRKAM 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 314 MEKLAKATGANVIT-----NIKDLSAQDLGDAGLVEERKI-------SGDSMIFVEECKHPKAV---------------- 365
Cdd:PRK12851 289 LEDIAILTGGTVISedlgiKLENVTLEQLGRAKKVVVEKEnttiidgAGSKTEIEGRVAQIRAQieettsdydreklqer 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 366 -------TMLIR--GTTEHVIEEVARAVDDAVGVVGCTIEDGrIVSGGGSTEVELSMKLREyAEGISGREQLAVRAFADA 436
Cdd:PRK12851 369 laklaggVAVIRvgASTEVEVKEKKDRVDDALHATRAAVEEG-IVPGGGVALLRAVKALDK-LETANGDQRTGVEIVRRA 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 437 LEVIPRTLAENAGLDAIEILVKVRaahasNGNKCAGLNVFTGAVEDMCENGVVEPLRVKTQAIQSAAESTEMLLRIDDVI 516
Cdd:PRK12851 447 LEAPVRQIAENAGAEGSVVVGKLR-----EKPGGYGFNAATNEYGDLYAQGVIDPVKVVRTALQNAASVAGLLLTTEAMV 521
|
.
gi 291191278 517 A 517
Cdd:PRK12851 522 A 522
|
|
| groEL |
CHL00093 |
chaperonin GroEL |
30-520 |
1.74e-19 |
|
chaperonin GroEL
Pssm-ID: 177025 Cd Length: 529 Bit Score: 91.70 E-value: 1.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 30 IIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKM---LIEVAKTQEKEV-GDGTTTAVVVAGELLR 105
Cdd:CHL00093 21 ILAEAVSVTLGPKGRNVVLEKKYGSPQIVNDGVTIAKEIELEDHIENTgvaLIRQAASKTNDVaGDGTTTATVLAYAIVK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 106 KAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVgaQDKEILTKIAMTSiTGKGAEkakekLAEIIVEAVSavvdde 185
Cdd:CHL00093 101 QGMKNVAAGANPISLKRGIEKATQYVVSQIAEYARPV--EDIQAITQVASIS-AGNDEE-----VGSMIADAIE------ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 186 gKVDKD-LIKIEKKSGASIdDTELIKGVLVDKERVSaqmPKKVTDA---KIALLNCAIEIketeTDAEIRIT--DPAKLM 259
Cdd:CHL00093 167 -KVGREgVISLEEGKSTVT-ELEITEGMRFEKGFIS---PYFVTDTermEVVQENPYILL----TDKKITLVqqDLLPIL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 260 EFIEQEEKMLKDMVAEIKASGANVLFCQK--GIDDlaqhylakegIVAAR-----RVKKSDMEKLAKATGANVITNIKDL 332
Cdd:CHL00093 238 EQVTKTKRPLLIIAEDVEKEALATLVLNKlrGIVN----------VVAVRapgfgDRRKAMLEDIAILTGGQVITEDAGL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 333 SAQDLGDAGLVEERKI--SGDSMIFVEEcKHPKAVTM---------------------------------LIR--GTTEH 375
Cdd:CHL00093 308 SLETIQLDLLGQARRIivTKDSTTIIAD-GNEEQVKArceqlrkqieiadssyekeklqerlaklsggvaVIKvgAATET 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 376 VIEEVARAVDDAVGVVGCTIEDGrIVSGGGSTEVELSMKLREYAE-GISGREQLAVRAFADALEVIPRTLAENAGLDAIE 454
Cdd:CHL00093 387 EMKDKKLRLEDAINATKAAVEEG-IVPGGGATLVHLSENLKTWAKnNLKEDELIGALIVARAILAPLKRIAENAGKNGSV 465
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 291191278 455 ILVKVRaahasNGNKCAGLNVFTGAVEDMCENGVVEPLRVKTQAIQSAAESTEMLLRIDDVIAAEK 520
Cdd:CHL00093 466 IIEKVQ-----EQDFEIGYNAANNKFVNMYEAGIIDPAKVTRSALQNAASIASMILTTECIIVDKK 526
|
|
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
17-517 |
3.21e-19 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 90.95 E-value: 3.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 17 GRDAQRmNILAG-RIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHP----AAKMLIEVA-KTQEKeVG 90
Cdd:PRK00013 8 GEDARR-KLLRGvNKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDPfenmGAQLVKEVAsKTNDV-AG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 91 DGTTTAVVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQDKeiltkIAMT-SITGKGAEKakek 169
Cdd:PRK00013 86 DGTTTATVLAQAIVREGLKNVAAGANPMDLKRGIDKAVEAAVEELKKISKPVEDKEE-----IAQVaTISANGDEE---- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 170 LAEIIVEAVSavvddegKVDKD-LIKIEKKSGASiDDTELIKGVLVDKERVSAQMpkkVTDAkiallncaiEIKETE-TD 247
Cdd:PRK00013 157 IGKLIAEAME-------KVGKEgVITVEESKGFE-TELEVVEGMQFDRGYLSPYF---VTDP---------EKMEAElEN 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 248 AEIRITDpAKLmefieqeeKMLKDMVA---EIKASGANVLFCQKGIDDLAQHYLAKEGI-----VAA--------RRvkK 311
Cdd:PRK00013 217 PYILITD-KKI--------SNIQDLLPvleQVAQSGKPLLIIAEDVEGEALATLVVNKLrgtlkVVAvkapgfgdRR--K 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 312 SDMEKLAKATGANVIT-----NIKDLSAQDLGDAGLVeerKISGDSMIFVEECKHPKAVT---MLIRGTTEH-------- 375
Cdd:PRK00013 286 AMLEDIAILTGGTVISeelglKLEDATLEDLGQAKKV---VVTKDNTTIVDGAGDKEAIKarvAQIKAQIEEttsdydre 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 376 --------------VI-----------EEVARaVDDAVGVVGCTIEDGrIVSGGGSTEVELSMKLrEYAEGISGREQLAV 430
Cdd:PRK00013 363 klqerlaklaggvaVIkvgaatevemkEKKDR-VEDALHATRAAVEEG-IVPGGGVALLRAAPAL-EALKGLNGDEATGI 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 431 RAFADALEVIPRTLAENAGLDAIEILVKVRAAHASNgnkcAGLNVFTGAVEDMCENGVVEPLRVKTQAIQSAAESTEMLL 510
Cdd:PRK00013 440 NIVLRALEAPLRQIAENAGLEGSVVVEKVKNGKGKG----YGYNAATGEYVDMIEAGIIDPTKVTRSALQNAASVAGLLL 515
|
....*..
gi 291191278 511 RIDDVIA 517
Cdd:PRK00013 516 TTEAVVA 522
|
|
| groEL |
PRK12852 |
chaperonin GroEL; Reviewed |
30-517 |
5.51e-16 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237232 Cd Length: 545 Bit Score: 80.66 E-value: 5.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 30 IIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSV----EHPAAKMLIEVAKTQEKEVGDGTTTAVVVAGELLR 105
Cdd:PRK12852 22 ILANAVKVTLGPKGRNVVIEKSFGAPRITKDGVTVAKEIELedkfENMGAQMVREVASKTNDLAGDGTTTATVLAQAIVR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 106 KAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQ-------------DKEILTKIA--MTSITGKGAEKAKE-K 169
Cdd:PRK12852 102 EGAKAVAAGMNPMDLKRGIDIAVAAVVKDIEKRAKPVASSaeiaqvgtisangDAAIGKMIAqaMQKVGNEGVITVEEnK 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 170 LAEIIVEAVSAVVDDEGKVDKDLIKIEKKSGASIDDTElikgVLVDKERVS---AQMP--KKVTDAKIALLNCAIEIkET 244
Cdd:PRK12852 182 SLETEVDIVEGMKFDRGYLSPYFVTNAEKMTVELDDAY----ILLHEKKLSglqAMLPvlEAVVQSGKPLLIIAEDV-EG 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 245 ETDAEIRITD--------PAKLMEFIEQEEKMLKDMVAeikASGANVLFCQKGIDdlaqhyLAKEGIVAARRVKKSDMEK 316
Cdd:PRK12852 257 EALATLVVNRlrgglkvaAVKAPGFGDRRKAMLEDIAI---LTGGQLISEDLGIK------LENVTLKMLGRAKKVVIDK 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 317 lAKATGANVITNIKDLSAQDLGDAGLVEERKISGDSMIFVEECKHPKAVTMLIR--GTTEHVIEEVARAVDDAVGVVGCT 394
Cdd:PRK12852 328 -ENTTIVNGAGKKADIEARVGQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRvgGATEVEVKEKKDRVEDALNATRAA 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 395 IEDGrIVSGGGsteVELsMKLREYAEGISGR---EQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRaahaSNGNKCA 471
Cdd:PRK12852 407 VQEG-IVPGGG---VAL-LRAKKAVGRINNDnadVQAGINIVLKALEAPIRQIAENAGVEGSIVVGKIL----ENKSETF 477
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 291191278 472 GLNVFTGAVEDMCENGVVEPLRVKTQAIQSAAESTEMLLRIDDVIA 517
Cdd:PRK12852 478 GFDAQTEEYVDMVAKGIIDPAKVVRTALQDAASVAGLLVTTEAMVA 523
|
|
| PLN03167 |
PLN03167 |
Chaperonin-60 beta subunit; Provisional |
31-516 |
2.04e-15 |
|
Chaperonin-60 beta subunit; Provisional
Pssm-ID: 215611 [Multi-domain] Cd Length: 600 Bit Score: 79.20 E-value: 2.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 31 IAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHP----AAKMLIEVAKTQEKEVGDGTTTAVVVAGELLRK 106
Cdd:PLN03167 78 LADLVGVTLGPKGRNVVLESKYGSPKIVNDGVTVAKEVELEDPveniGAKLVRQAAAKTNDLAGDGTTTSVVLAQGLIAE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 107 AEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVgaQDKEiLTKIAMTSiTGKGAEkakekLAEIIVEAVS------A 180
Cdd:PLN03167 158 GVKVVAAGANPVQITRGIEKTAKALVKELKKMSKEV--EDSE-LADVAAVS-AGNNYE-----VGNMIAEAMSkvgrkgV 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 181 VVDDEGK-VDKDLIKIEkksGASIDDTELIKGVLVDKERVSAQMPK---KVTDAKIALLNCAIEIKEtetDAeIRITDPA 256
Cdd:PLN03167 229 VTLEEGKsAENNLYVVE---GMQFDRGYISPYFVTDSEKMSVEYDNcklLLVDKKITNARDLIGILE---DA-IRGGYPL 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 257 KLM-EFIEQeEKMLKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSD----MEKLAK---ATGANVI-- 326
Cdd:PLN03167 302 LIIaEDIEQ-EALATLVVNKLRGSLKIAALKAPGFGERKSQYLDDIAILTGGTVIREEvglsLDKVGKevlGTAAKVVlt 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 327 ----TNIKDLSAQDlgdagLVEERKISGDSMIFVEECKHPK-------------AVTMLIRGTTEHVIEEVARAVDDAVG 389
Cdd:PLN03167 381 kdttTIVGDGSTQE-----AVNKRVAQIKNLIEAAEQDYEKeklneriaklsggVAVIQVGAQTETELKEKKLRVEDALN 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 390 VVGCTIEDGrIVSGGGSTEVELSMKLREYAEGISGREQ-LAVRAFADALEVIPRTLAENAGLDAIEILVKVraahASNGN 468
Cdd:PLN03167 456 ATKAAVEEG-IVVGGGCTLLRLASKVDAIKDTLENDEQkVGADIVKRALSYPLKLIAKNAGVNGSVVSEKV----LSNDN 530
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 291191278 469 KCAGLNVFTGAVEDMCENGVVEPLRVKTQAIQSAAESTEMLLRIDDVI 516
Cdd:PLN03167 531 PKFGYNAATGKYEDLMAAGIIDPTKVVRCCLEHAASVAKTFLTSDCVV 578
|
|
| PRK14104 |
PRK14104 |
chaperonin GroEL; Provisional |
17-524 |
6.72e-14 |
|
chaperonin GroEL; Provisional
Pssm-ID: 172594 Cd Length: 546 Bit Score: 74.30 E-value: 6.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 17 GRDAQRMNILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSV----EHPAAKMLIEVAKTQEKEVGDG 92
Cdd:PRK14104 9 GVDARDRMLRGVDILANAVKVTLGPKGRNVVLDKSFGAPRITKDGVTVAKEIELedkfENMGAQMVREVASKSADAAGDG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 93 TTTAVVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQDKeiLTKIAMTSITGkgaekaKEKLAE 172
Cdd:PRK14104 89 TTTATVLAQAIVREGAKSVAAGMNPMDLKRGIDLAVEAVVADLVKNSKKVTSNDE--IAQVGTISANG------DAEIGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 173 IIVEAVSAvVDDEGkvdkdLIKIEKksgASIDDTEL--IKGVLVDKERVSAQMPKKVTDAKIALLNCAIEIKETETDAei 250
Cdd:PRK14104 161 FLADAMKK-VGNEG-----VITVEE---AKSLETELdvVEGMQFDRGYISPYFVTNADKMRVEMDDAYILINEKKLSS-- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 251 rITDPAKLMEFIEQEEKMLKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARrvkKSDMEKLAKATGANVIT--- 327
Cdd:PRK14104 230 -LNELLPLLEAVVQTGKPLVIVAEDVEGEALATLVVNRLRGGLKVAAVKAPGFGDRR---KAMLQDIAILTGGQAISedl 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 328 --NIKDLSAQDLGDA------------------------------GLVEERKISGDSMIFVEECKHPKAVTMLIR--GTT 373
Cdd:PRK14104 306 giKLENVTLQMLGRAkkvmidkenttivngagkkadiearvaqikAQIEETTSDYDREKLQERLAKLAGGVAVIRvgGAT 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291191278 374 EHVIEEVARAVDDAVGVVGCTIEDGrIVSGGGSTEVELSMKLREYAEGiSGREQLAVRAFADALEVIPRTLAENAGLDAI 453
Cdd:PRK14104 386 EVEVKERKDRVDDAMHATRAAVEEG-IVPGGGVALLRASEQLKGIKTK-NDDQKTGVEIVRKALSAPARQIAINAGEDGS 463
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 291191278 454 EILVKVraahASNGNKCAGLNVFTGAVEDMCENGVVEPLRVKTQAIQSAAESTEMLLRIDDVIAAEKLRGA 524
Cdd:PRK14104 464 VIVGKI----LEKEQYSYGFDSQTGEYGNLVSKGIIDPTKVVRTAIQNAASVAALLITTEAMVAELPKKGG 530
|
|
| |
