|
Name |
Accession |
Description |
Interval |
E-value |
| thermosome_beta |
NF041083 |
thermosome subunit beta; |
6-522 |
0e+00 |
|
thermosome subunit beta;
Pssm-ID: 469010 Cd Length: 519 Bit Score: 882.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 6 VPILVLKEGTQREQGKNAQRNNIEAAKAIADAVRTTLGPKGMDKMLVDSIGDIIISNDGATILKEMDVEHPTAKMIVEVS 85
Cdd:NF041083 1 QPVLILKEGTQRTKGRDAQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDIVITNDGATILKEMDVQHPAAKMLVEVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 86 KAQDTAVGDGTTTAVVLSGELLKQAETLLDQGVHPTVISNGYRLAVNEARKIIDEIAEKS--TDDATLRKIALTALSGKN 163
Cdd:NF041083 81 KTQDDEVGDGTTTAVVLAGELLKKAEELLDQNIHPTIIANGYRLAAEKAIEILDEIAEKVdpDDRETLKKIAETSLTSKG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 164 TGLSNDFLADLVVKAVNAVAEVRDGKTIVDTANIKVDKKNGGSVNDTQFISGIVIDKEKVHSKMPDVVKNAKIALIDSAL 243
Cdd:NF041083 161 VEEARDYLAEIAVKAVKQVAEKRDGKYYVDLDNIQIEKKHGGSIEDTQLIYGIVIDKEVVHPGMPKRVENAKIALLDAPL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 244 EIKKTEIEAKVQISDPSKIQDFLNQETNTFKQMVEKIKKSGANVVLCQKGIDDVAQHYLAKEGIYAVRRVKKSDMEKLAK 323
Cdd:NF041083 241 EVKKTEIDAEIRITDPDQLQKFLDQEEKMLKEMVDKIKATGANVVFCQKGIDDLAQHYLAKAGILAVRRVKKSDMEKLAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 324 ATGAKIVTDLDDLTPSVLGEAETVEERKIGDDRMTFVMGCKNPKAVSILIRGGTDHVVSEVERALNDAIRVVAITKEDGK 403
Cdd:NF041083 321 ATGARIVTNIDDLTPEDLGYAELVEERKVGDDKMVFVEGCKNPKAVTILIRGGTEHVVDEAERALEDALSVVADAVEDGK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 404 FLWGGGAVEAELAMRLAKYANSVGGREQLAIEAFAKALEIIPRTLAENAGIDPINTLIKLKADDEKGRISVGVDLDNNGV 483
Cdd:NF041083 401 IVAGGGAPEVELAKRLREYAATVGGREQLAVEAFAEALEIIPRTLAENAGLDPIDILVKLRSAHEKGKKWAGINVFTGEV 480
|
490 500 510
....*....|....*....|....*....|....*....
gi 4699707 484 GDMKAKGVVDPLRVKTHALESAVEVATMILRIDDVIASK 522
Cdd:NF041083 481 VDMWELGVIEPLRVKTQAIKSATEAATMILRIDDVIAAK 519
|
|
| thermosome_alpha |
NF041082 |
thermosome subunit alpha; |
6-522 |
0e+00 |
|
thermosome subunit alpha;
Pssm-ID: 469009 Cd Length: 518 Bit Score: 879.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 6 VPILVLKEGTQREQGKNAQRNNIEAAKAIADAVRTTLGPKGMDKMLVDSIGDIIISNDGATILKEMDVEHPTAKMIVEVS 85
Cdd:NF041082 1 QPILILKEGTQRTSGRDAQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDVVITNDGVTILKEMDIEHPAAKMIVEVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 86 KAQDTAVGDGTTTAVVLSGELLKQAETLLDQGVHPTVISNGYRLAVNEARKIIDEIAEKST--DDATLRKIALTALSGKN 163
Cdd:NF041082 81 KTQDDEVGDGTTTAVVLAGELLKKAEELLDQDIHPTIIAEGYRLAAEKALEILDEIAIKVDpdDKETLKKIAATAMTGKG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 164 TGLSNDFLADLVVKAVNAVAEvRDGKTIVDTANIKVDKKNGGSVNDTQFISGIVIDKEKVHSKMPDVVKNAKIALIDSAL 243
Cdd:NF041082 161 AEAAKDKLADLVVDAVKAVAE-KDGGYNVDLDNIKVEKKVGGSIEDSELVEGVVIDKERVHPGMPKRVENAKIALLDAPL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 244 EIKKTEIEAKVQISDPSKIQDFLNQETNTFKQMVEKIKKSGANVVLCQKGIDDVAQHYLAKEGIYAVRRVKKSDMEKLAK 323
Cdd:NF041082 240 EVKKTEIDAKISITDPDQLQAFLDQEEKMLKEMVDKIADSGANVVFCQKGIDDLAQHYLAKEGILAVRRVKKSDMEKLAK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 324 ATGAKIVTDLDDLTPSVLGEAETVEERKIGDDRMTFVMGCKNPKAVSILIRGGTDHVVSEVERALNDAIRVVAITKEDGK 403
Cdd:NF041082 320 ATGARIVTSIDDLSPEDLGYAGLVEERKVGGDKMIFVEGCKNPKAVTILLRGGTEHVVDEVERALEDALRVVRVVLEDGK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 404 FLWGGGAVEAELAMRLAKYANSVGGREQLAIEAFAKALEIIPRTLAENAGIDPINTLIKLKADDEKGRISVGVDLDNNGV 483
Cdd:NF041082 400 VVAGGGAPEVELALRLREYAASVGGREQLAIEAFAEALEIIPRTLAENAGLDPIDALVELRSAHEKGNKTAGLDVYTGKV 479
|
490 500 510
....*....|....*....|....*....|....*....
gi 4699707 484 GDMKAKGVVDPLRVKTHALESAVEVATMILRIDDVIASK 522
Cdd:NF041082 480 VDMLEIGVVEPLRVKTQAIKSATEAAVMILRIDDVIAAA 518
|
|
| cpn60 |
cd03343 |
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ... |
8-522 |
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: 840.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 8 ILVLKEGTQREQGKNAQRNNIEAAKAIADAVRTTLGPKGMDKMLVDSIGDIIISNDGATILKEMDVEHPTAKMIVEVSKA 87
Cdd:cd03343 1 VLILKEGTQRTSGRDAQRMNIAAAKAVAEAVRTTLGPKGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 88 QDTAVGDGTTTAVVLSGELLKQAETLLDQGVHPTVISNGYRLAVNEARKIIDEIAEKST--DDATLRKIALTALSGKNTG 165
Cdd:cd03343 81 QDEEVGDGTTTAVVLAGELLEKAEDLLDQNIHPTVIIEGYRLAAEKALELLDEIAIKVDpdDKDTLRKIAKTSLTGKGAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 166 LSNDFLADLVVKAVNAVAEVRDGKTIVDTANIKVDKKNGGSVNDTQFISGIVIDKEKVHSKMPDVVKNAKIALIDSALEI 245
Cdd:cd03343 161 AAKDKLADLVVDAVLQVAEKRDGKYVVDLDNIKIEKKTGGSVDDTELIRGIVIDKEVVHPGMPKRVENAKIALLDAPLEV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 246 KKTEIEAKVQISDPSKIQDFLNQETNTFKQMVEKIKKSGANVVLCQKGIDDVAQHYLAKEGIYAVRRVKKSDMEKLAKAT 325
Cdd:cd03343 241 KKTEIDAKIRITSPDQLQAFLEQEEAMLKEMVDKIADTGANVVFCQKGIDDLAQHYLAKAGILAVRRVKKSDMEKLARAT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 326 GAKIVTDLDDLTPSVLGEAETVEERKIGDDRMTFVMGCKNPKAVSILIRGGTDHVVSEVERALNDAIRVVAITKEDGKFL 405
Cdd:cd03343 321 GAKIVTNIDDLTPEDLGEAELVEERKVGDDKMVFVEGCKNPKAVTILLRGGTEHVVDELERALEDALRVVADALEDGKVV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 406 WGGGAVEAELAMRLAKYANSVGGREQLAIEAFAKALEIIPRTLAENAGIDPINTLIKLKADDEKGRISVGVDLDNNGVGD 485
Cdd:cd03343 401 AGGGAVEIELAKRLREYARSVGGREQLAVEAFADALEEIPRTLAENAGLDPIDTLVELRAAHEKGNKNAGLDVYTGEVVD 480
|
490 500 510
....*....|....*....|....*....|....*..
gi 4699707 486 MKAKGVVDPLRVKTHALESAVEVATMILRIDDVIASK 522
Cdd:cd03343 481 MLEKGVIEPLRVKKQAIKSATEAATMILRIDDVIAAK 517
|
|
| thermosome_arch |
TIGR02339 |
thermosome, various subunits, archaeal; Thermosome is the name given to the archaeal rather ... |
7-521 |
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: 736.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 7 PILVLKEGTQREQGKNAQRNNIEAAKAIADAVRTTLGPKGMDKMLVDSIGDIIISNDGATILKEMDVEHPTAKMIVEVSK 86
Cdd:TIGR02339 1 PVFILKEGTQRTSGRDAQRNNIAAAKAVAEAVKSTLGPRGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 87 AQDTAVGDGTTTAVVLSGELLKQAETLLDQGVHPTVISNGYRLAVNEARKIIDEIAEKST--DDATLRKIALTALSGKNT 164
Cdd:TIGR02339 81 TQDEEVGDGTTTAVVLAGELLEKAEDLLEQDIHPTVIIEGYRKAAEKALEIIDEIATKISpeDRDLLKKIAYTSLTSKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 165 G-LSNDFLADLVVKAVNAVAEVR-DGKTIVDTANIKVDKKNGGSVNDTQFISGIVIDKEKVHSKMPDVVKNAKIALIDSA 242
Cdd:TIGR02339 161 AeVAKDKLADLVVEAVKQVAELRgDGKYYVDLDNIKIVKKKGGSIEDTELVEGIVVDKEVVHPGMPKRVENAKIALLDAP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 243 LEIKKTEIEAKVQISDPSKIQDFLNQETNTFKQMVEKIKKSGANVVLCQKGIDDVAQHYLAKEGIYAVRRVKKSDMEKLA 322
Cdd:TIGR02339 241 LEVEKTEIDAKIRITDPDQIKKFLDQEEAMLKEMVDKIASAGANVVICQKGIDDVAQHYLAKAGILAVRRVKKSDIEKLA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 323 KATGAKIVTDLDDLTPSVLGEAETVEERKIGDDRMTFVMGCKNPKAVSILIRGGTDHVVSEVERALNDAIRVVAITKEDG 402
Cdd:TIGR02339 321 RATGARIVSSIDEITESDLGYAELVEERKVGEDKMVFVEGCKNPKAVTILLRGGTEHVVDELERSIQDALHVVANALEDG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 403 KFLWGGGAVEAELAMRLAKYANSVGGREQLAIEAFAKALEIIPRTLAENAGIDPINTLIKLKADDEKGRISVGVDLDNNG 482
Cdd:TIGR02339 401 KIVAGGGAVEIELALRLRSYARSVGGREQLAIEAFADALEEIPRILAENAGLDPIDALVDLRAKHEKGNKNAGINVFTGE 480
|
490 500 510
....*....|....*....|....*....|....*....
gi 4699707 483 VGDMKAKGVVDPLRVKTHALESAVEVATMILRIDDVIAS 521
Cdd:TIGR02339 481 IEDMLELGVIEPLRVKEQAIKSATEAATMILRIDDVIAA 519
|
|
| Cpn60_TCP1 |
pfam00118 |
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ... |
34-522 |
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: 648.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 34 IADAVRTTLGPKGMDKMLVDSIGDIIISNDGATILKEMDVEHPTAKMIVEVSKAQDTAVGDGTTTAVVLSGELLKQAETL 113
Cdd:pfam00118 1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELEIQHPAAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEEAEKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 114 LDQGVHPTVISNGYRLAVNEARKIIDEIAEKSTDDA---TLRKIALTALSGKNTGLSNDFLADLVVKAVNAVAEVRdgkT 190
Cdd:pfam00118 81 LAAGVHPTTIIEGYEKALEKALEILDSIISIPVEDVdreDLLKVARTSLSSKIISRESDFLAKLVVDAVLAIPKND---G 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 191 IVDTANIKVDKKNGGSVNDTQFISGIVIDKEKVHSKMPDVVKNAKIALIDSALEIKKTEIEAKVQISDPSKIQDFLNQET 270
Cdd:pfam00118 158 SFDLGNIGVVKILGGSLEDSELVDGVVLDKGPLHPDMPKRLENAKVLLLNCSLEYEKTETKATVVLSDAEQLERFLKAEE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 271 NTFKQMVEKIKKSGANVVLCQKGIDDVAQHYLAKEGIYAVRRVKKSDMEKLAKATGAKIVTDLDDLTPSVLGEAETVEER 350
Cdd:pfam00118 238 EQILEIVEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMALRRVKKRDLERLAKATGARAVSSLDDLTPDDLGTAGKVEEE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 351 KIGDDRMTFVMGCKNPKAVSILIRGGTDHVVSEVERALNDAIRVVAITKEDGKFLWGGGAVEAELAMRLAKYANSVGGRE 430
Cdd:pfam00118 318 KIGDEKYTFIEGCKSPKAATILLRGATDHVLDEIERSIHDALCVVKNAIEDPRVVPGGGAVEMELARALREYAKSVSGKE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 431 QLAIEAFAKALEIIPRTLAENAGIDPINTLIKLKADDEKGRISVGVDLDNNGVGDMKAKGVVDPLRVKTHALESAVEVAT 510
Cdd:pfam00118 398 QLAIEAFAEALEVIPKTLAENAGLDPIEVLAELRAAHASGEKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKSATEAAS 477
|
490
....*....|..
gi 4699707 511 MILRIDDVIASK 522
Cdd:pfam00118 478 TILRIDDIIKAK 489
|
|
| chaperonin_type_I_II |
cd00309 |
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ... |
15-520 |
0e+00 |
|
chaperonin families, type I and type II. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings, each composed of 7-9 subunits. There are 2 main chaperonin groups. The symmetry of type I is seven-fold and they are found in eubacteria (GroEL) and in organelles of eubacterial descent (hsp60 and RBP). The symmetry of type II is eight- or nine-fold and they are found in archea (thermosome), thermophilic bacteria (TF55) and in the eukaryotic cytosol (CTT). Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis.
Pssm-ID: 238189 Cd Length: 464 Bit Score: 604.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 15 TQREQGKNAQRNNIEAAKAIADAVRTTLGPKGMDKMLVDSIGDIIISNDGATILKEMDVEHPTAKMIVEVSKAQDTAVGD 94
Cdd:cd00309 1 KEREFGEEARLSNINAAKALADAVKTTLGPKGMDKMLVDSLGDPTITNDGATILKEIEVEHPAAKLLVEVAKSQDDEVGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 95 GTTTAVVLSGELLKQAETLLDQGVHPTVISNGYRLAVNEARKIIDEIAEKS--TDDATLRKIALTALSGKNTGLSNDFLA 172
Cdd:cd00309 81 GTTTVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVPIdvEDREELLKVATTSLNSKLVSGGDDFLG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 173 DLVVKAVNAVAevrDGKTIVDTANIKVDKKNGGSVNDTQFISGIVIDKEKVHSKMPDVVKNAKIALIDSALEikkteiea 252
Cdd:cd00309 161 ELVVDAVLKVG---KENGDVDLGVIRVEKKKGGSLEDSELVVGMVFDKGYLSPYMPKRLENAKILLLDCKLE-------- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 253 kvqisdpskiqdflnqetntfkqmvekikksgaNVVLCQKGIDDVAQHYLAKEGIYAVRRVKKSDMEKLAKATGAKIVTD 332
Cdd:cd00309 230 ---------------------------------YVVIAEKGIDDEALHYLAKLGIMAVRRVRKEDLERIAKATGATIVSR 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 333 LDDLTPSVLGEAETVEERKIGDDRMTFVMGCKNPKAVSILIRGGTDHVVSEVERALNDAIRVVAITKEDGKFLWGGGAVE 412
Cdd:cd00309 277 LEDLTPEDLGTAGLVEETKIGDEKYTFIEGCKGGKVATILLRGATEVELDEAERSLHDALCAVRAAVEDGGIVPGGGAAE 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 413 AELAMRLAKYANSVGGREQLAIEAFAKALEIIPRTLAENAGIDPINTLIKLKADDEKGRISVGVDLDNNGVGDMKAKGVV 492
Cdd:cd00309 357 IELSKALEELAKTLPGKEQLGIEAFADALEVIPRTLAENAGLDPIEVVTKLRAKHAEGGGNAGGDVETGEIVDMKEAGII 436
|
490 500
....*....|....*....|....*...
gi 4699707 493 DPLRVKTHALESAVEVATMILRIDDVIA 520
Cdd:cd00309 437 DPLKVKRQALKSATEAASLILTIDDIIV 464
|
|
| GroEL |
COG0459 |
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ... |
20-527 |
0e+00 |
|
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227 Cd Length: 497 Bit Score: 525.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 20 GKNAQRNNIEAAKAIADAVRTTLGPKGMDKMLVDSIGDIIISNDGATILKEMDVEHP----TAKMIVEVSKAQDTAVGDG 95
Cdd:COG0459 8 GEDARRANIRGVKALADAVKVTLGPKGRNVMLVKSFGDPTITNDGVTIAKEIELEDPfenmGAQLVKEVASKTNDEAGDG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 96 TTTAVVLSGELLKQAETLLDQGVHPTVISNGYRLAVNEARKIIDEIAEKSTDDATLRKIALTALSGKntglsnDFLADLV 175
Cdd:COG0459 88 TTTATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPVDDKEELAQVATISANGD------EEIGELI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 176 VKAVNAVAEvrDGktivdtaNIKVDKKnGGSVNDTQFISGIVIDKEKVHS-------KMPDVVKNAKIALIDSALEIkkt 248
Cdd:COG0459 162 AEAMEKVGK--DG-------VITVEEG-KGLETELEVVEGMQFDKGYLSPyfvtdpeKMPAELENAYILLTDKKISS--- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 249 eieakvqisdpskIQDFLnqetntfkQMVEKIKKSGANVVLCQKGIDDVAQHYLAKEGIYAVRRV-----------KKSD 317
Cdd:COG0459 229 -------------IQDLL--------PLLEKVAQSGKPLLIIAEDIDGEALATLVVNGIRGVLRVvavkapgfgdrRKAM 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 318 MEKLAKATGAKIVTD-----LDDLTPSVLGEAETVEerkIGDDRMTFVMGCKNPKAVSILIRGGTDHVVSEVERALNDAI 392
Cdd:COG0459 288 LEDIAILTGGRVISEdlglkLEDVTLDDLGRAKRVE---VDKDNTTIVEGAGNPKAIVILVGAATEVEVKERKRRVEDAL 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 393 RVVAITKEDGkFLWGGGAVEAELAMRLAKYANSVGGREQLAIEAFAKALEIIPRTLAENAGIDPINTLIKLKADDEKGri 472
Cdd:COG0459 365 HATRAAVEEG-IVPGGGAALLRAARALRELAAKLEGDEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKVRAAKDKG-- 441
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 4699707 473 sVGVDLDNNGVGDMKAKGVVDPLRVKTHALESAVEVATMILRIDDVIASKKSTPP 527
Cdd:COG0459 442 -FGFDAATGEYVDMLEAGVIDPAKVKRSALQNAASVAGLILTTEAVIADKPEKEE 495
|
|
| TCP1_epsilon |
cd03339 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ... |
7-520 |
1.28e-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: 487.96 E-value: 1.28e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 7 PILVLKEGTQ--REQGKNAQRNNIEAAKAIADAVRTTLGPKGMDKMLVDSIGDIIISNDGATILKEMDVEHPTAKMIVEV 84
Cdd:cd03339 6 PFIIVREQEKkkRLKGLEAHKSHILAAKSVANILRTSLGPRGMDKILVSPDGEVTVTNDGATILEKMDVDHQIAKLLVEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 85 SKAQDTAVGDGTTTAVVLSGELLKQAETLLDQGVHPTVISNGYRLAVNEARKIIDEIAEKSTDDA----TLRKIALTALS 160
Cdd:cd03339 86 SKSQDDEIGDGTTGVVVLAGALLEQAEKLLDRGIHPIRIADGYEQACKIAVEHLEEIADKIEFSPdnkePLIQTAMTSLG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 161 GKNTGLSNDFLADLVVKAVNAVA--EVRDgktiVDTANIKVDKKNGGSVNDTQFISGIVIDKEKVHSKMPDVVKNAKIAL 238
Cdd:cd03339 166 SKIVSRCHRQFAEIAVDAVLSVAdlERKD----VNFELIKVEGKVGGRLEDTKLVKGIVIDKDFSHPQMPKEVKDAKIAI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 239 IDSALEIKKTEIEAKVQISDPSKIQDFLNQETNTFKQMVEKIKKSGANVVLCQKGIDDVAQHYLAKEGIYAVRRVKKSDM 318
Cdd:cd03339 242 LTCPFEPPKPKTKHKLDITSVEDYKKLQEYEQKYFREMVEQVKDAGANLVICQWGFDDEANHLLLQNGLPAVRWVGGVEI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 319 EKLAKATGAKIVTDLDDLTPSVLGEAETVEERKIG--DDRMTFVMGCKNPKAVSILIRGGTDHVVSEVERALNDAIRVVA 396
Cdd:cd03339 322 ELIAIATGGRIVPRFEDLSPEKLGKAGLVREISFGttKDKMLVIEGCPNSKAVTIFIRGGNKMIIEEAKRSLHDALCVVR 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 397 ITKEDGKFLWGGGAVEAELAMRLAKYANSVGGREQLAIEAFAKALEIIPRTLAENAGIDPINTLIKLKADDEKGRIS-VG 475
Cdd:cd03339 402 NLIRDNRIVYGGGAAEISCSLAVEKAADKCSGIEQYAMRAFADALESIPLALAENSGLNPIETLSEVKARQVKEKNPhLG 481
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 4699707 476 VDLDNNGVGDMKAKGVVDPLRVKTHALESAVEVATMILRIDDVIA 520
Cdd:cd03339 482 IDCLGRGTNDMKEQKVFETLISKKQQILLATQVVKMILKIDDVIV 526
|
|
| TCP1_alpha |
cd03335 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ... |
16-519 |
4.79e-160 |
|
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: 466.38 E-value: 4.79e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 16 QREQGKNAQRNNIEAAKAIADAVRTTLGPKGMDKMLVDSIGDIIISNDGATILKEMDVEHPTAKMIVEVSKAQDTAVGDG 95
Cdd:cd03335 2 ERTSGQDVRTQNVTAAMAIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDKEVGDG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 96 TTTAVVLSGELLKQAETLLDQGVHPTVISNGYRLAVNEARKIIDEIAEKSTDD---ATLRKIALTALSGKNTGLSNDFLA 172
Cdd:cd03335 82 TTSVVIIAAELLKRANELVKQKIHPTTIISGYRLACKEAVKYIKEHLSISVDNlgkESLINVAKTSMSSKIIGADSDFFA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 173 DLVVKAVNAVAEV-RDGKTIVDTANIKVDKKNGGSVNDTQFISGIVIDKEKVHSKMPDVVKNAKIALIDSALEIKKTEIE 251
Cdd:cd03335 162 NMVVDAILAVKTTnEKGKTKYPIKAVNILKAHGKSAKESYLVNGYALNCTRASQGMPTRVKNAKIACLDFNLQKTKMKLG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 252 AKVQISDPSKIQDFLNQETNTFKQMVEKIKKSGANVVLCQKGIDDVAQHYLAKEGIYAVRRVKKSDMEKLAKATGAKIVT 331
Cdd:cd03335 242 VQVVVTDPEKLEKIRQRESDITKERIKKILAAGANVVLTTGGIDDMCLKYFVEAGAMAVRRVKKEDLRRIAKATGATLVS 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 332 DLDDL------TPSVLGEAETVEERKIGDDRMTFVMGCKNPKAVSILIRGGTDHVVSEVERALNDAIRVVAITKEDGKFL 405
Cdd:cd03335 322 TLANLegeetfDPSYLGEAEEVVQERIGDDELILIKGTKKRSSASIILRGANDFMLDEMERSLHDALCVVKRTLESNSVV 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 406 WGGGAVEAELAMRLAKYANSVGGREQLAIEAFAKALEIIPRTLAENAGIDPINTLIKLKA--------DDEKGRISVGVD 477
Cdd:cd03335 402 PGGGAVETALSIYLENFATTLGSREQLAIAEFAEALLVIPKTLAVNAAKDATELVAKLRAyhaaaqvkPDKKHLKWYGLD 481
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 4699707 478 LDNNGVGDMKAKGVVDPLRVKTHALESAVEVATMILRIDDVI 519
Cdd:cd03335 482 LINGKVRDNLEAGVLEPTVSKIKSLKFATEAAITILRIDDLI 523
|
|
| TCP1_delta |
cd03338 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ... |
15-521 |
1.11e-159 |
|
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: 464.84 E-value: 1.11e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 15 TQREQGKNAQRNNIEAAKAIADAVRTTLGPKGMDKMLVDSIGDIIISNDGATILKEMDVEHPTAKMIVEVSKAQDTAVGD 94
Cdd:cd03338 1 TDKEKPADVRLSNIQAAKAVADAIRTSLGPRGMDKMIQTGKGEVIITNDGATILKQMSVLHPAAKMLVELSKAQDIEAGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 95 GTTTAVVLSGELLKQAETLLDQGVHPTVISNGYRLAVNEARKIIDEIAEK--STDDATLRKIALTALSGKNTGLSNDFLA 172
Cdd:cd03338 81 GTTSVVVLAGALLSACESLLKKGIHPTVISESFQIAAKKAVEILDSMSIPvdLNDRESLIKSATTSLNSKVVSQYSSLLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 173 DLvvkAVNAVAEVRDGK--TIVDTANIKVDKKNGGSVNDTQFISGIVIDKEKVHSK-MPDVVKNAKIALIDSALEIKKTE 249
Cdd:cd03338 161 PI---AVDAVLKVIDPAtaTNVDLKDIRIVKKLGGTIEDTELVDGLVFTQKASKKAgGPTRIEKAKIGLIQFCLSPPKTD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 250 IEAKVQISDPSKIQDFLNQETNTFKQMVEKIKKSGANVVLCQKGI-----DDVAQHYLAKEGIYAVRRVKKSDMEKLAKA 324
Cdd:cd03338 238 MDNNIVVNDYAQMDRILREERKYILNMCKKIKKSGCNVLLIQKSIlrdavSDLALHFLAKLKIMVVKDIEREEIEFICKT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 325 TGAKIVTDLDDLTPSVLGEAETVEERKIGDDRMTFVMGCKNP-KAVSILIRGGTDHVVSEVERALNDAIRVVAITKEDGK 403
Cdd:cd03338 318 IGCKPVASIDHFTEDKLGSADLVEEVSLGDGKIVKITGVKNPgKTVTILVRGSNKLVLDEAERSLHDALCVIRCLVKKRA 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 404 FLWGGGAVEAELAMRLAKYANSVGGREQLAIEAFAKALEIIPRTLAENAGIDPINTLIKLKADDEKGRISVGVDLDNNGV 483
Cdd:cd03338 398 LIPGGGAPEIEIALQLSEWARTLTGVEQYCVRAFADALEVIPYTLAENAGLNPISIVTELRNRHAQGEKNAGINVRKGAI 477
|
490 500 510
....*....|....*....|....*....|....*...
gi 4699707 484 GDMKAKGVVDPLRVKTHALESAVEVATMILRIDDVIAS 521
Cdd:cd03338 478 TNILEENVVQPLLVSTSAITLATETVRMILKIDDIVLA 515
|
|
| TCP1_eta |
cd03340 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ... |
7-524 |
7.87e-159 |
|
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: 462.91 E-value: 7.87e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 7 PILVLKEGTQREQGKNAQRNNIEAAKAIADAVRTTLGPKGMDKMLVDSIGDIIISNDGATILKEMDVEHPTAKMIVEVSK 86
Cdd:cd03340 1 PIILLKEGTDTSQGKGQLISNINACQAIADAVRTTLGPRGMDKLIVDGRGKVTISNDGATILKLLDIVHPAAKTLVDIAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 87 AQDTAVGDGTTTAVVLSGELLKQAETLLDQGVHPTVISNGYRLAVNEARKIIDEIA----EKSTD--DATLRKIALTALS 160
Cdd:cd03340 81 SQDAEVGDGTTSVVVLAGEFLKEAKPFIEDGVHPQIIIRGYRKALQLAIEKIKEIAvnidKEDKEeqRELLEKCAATALN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 161 GKNTGLSNDFLADLVVKAVNAVAEVRDGKtivdtaNIKVDKKNGGSVNDTQFISGIVIDKE---KVHSKMPDVVKNAKIA 237
Cdd:cd03340 161 SKLIASEKEFFAKMVVDAVLSLDDDLDLD------MIGIKKVPGGSLEDSQLVNGVAFKKTfsyAGFEQQPKKFKNPKIL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 238 LIDSALEIKKTEIEAKVQISDPSKIQDFLNQETNTFKQMVEKIKKSGANVVLCQKGIDDVAQHYLAKEGIYAVRRVKKSD 317
Cdd:cd03340 235 LLNVELELKAEKDNAEVRVEDPEEYQAIVDAEWKIIYDKLEKIVKSGANVVLSKLPIGDLATQYFADRDIFCAGRVPEED 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 318 MEKLAKATGAKIVTDLDDLTPSVLGEAETVEERKIGDDRMTFVMGCKNPKAVSILIRGGTDHVVSEVERALNDAIRVVAI 397
Cdd:cd03340 315 LKRVAQATGGSIQTTVSNITDDVLGTCGLFEERQVGGERYNIFTGCPKAKTCTIILRGGAEQFIEEAERSLHDAIMIVRR 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 398 TKEDGKFLWGGGAVEAELAMRLAKYANSVGGREQLAIEAFAKALEIIPRTLAENAGIDPINTLIKLKADDEKG-RISVGV 476
Cdd:cd03340 395 AIKNDSVVAGGGAIEMELSKYLRDYSRTIAGKQQLVINAFAKALEIIPRQLCDNAGFDATDILNKLRQKHAQGgGKWYGV 474
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 4699707 477 DLDNNGVGDMKAKGVVDPLRVKTHALESAVEVATMILRIDDVIASKKS 524
Cdd:cd03340 475 DINNEGIADNFEAFVWEPSLVKINALTAATEAACLILSVDETIKNPKS 522
|
|
| TCP1_gamma |
cd03337 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ... |
7-521 |
6.17e-158 |
|
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: 459.07 E-value: 6.17e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 7 PILVLKEGTQREQGKNAQRNNIEAAKAIADAVRTTLGPKGMDKMLVDSIGDIIISNDGATILKEMDVEHPTAKMIVEVSK 86
Cdd:cd03337 1 PVLVLNQNTKRESGRKAQLGNIQAAKTVADVIRTCLGPRAMLKMLLDPMGGIVLTNDGNAILREIDVAHPAAKSMIELSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 87 AQDTAVGDGTTTAVVLSGELLKQAETLLDQGVHPTVISNGYRLAVNEARKIIDEIAEK--STDDATLRKIALTALSGKNT 164
Cdd:cd03337 81 TQDEEVGDGTTSVIILAGEILAVAEPFLERGIHPTVIIKAYRKALEDALKILEEISIPvdVNDRAQMLKIIKSCIGTKFV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 165 GLSNDFLADLVVKAVNAVA-EVRDGKTIVDTAN-IKVDKKNGGSVNDTQFISGIVIDKEKVHSKMPDVVKNAKIALIDSA 242
Cdd:cd03337 161 SRWSDLMCNLALDAVKTVAvEENGRKKEIDIKRyAKVEKIPGGEIEDSRVLDGVMLNKDVTHPKMRRRIENPRIVLLDCP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 243 LEIkkteieakvqisdpskiqdflnqetntfkqmvekikksganVVLCQKGIDDVAQHYLAKEGIYAVRRVKKSDMEKLA 322
Cdd:cd03337 241 LEY-----------------------------------------LVITEKGVSDLAQHYLVKAGITALRRVRKTDNNRIA 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 323 KATGAKIVTDLDDLTPSVLGEAETVEE-RKIGDDRMTFVMGCKNPKAVSILIRGGTDHVVSEVERALNDAIRVVAITKED 401
Cdd:cd03337 280 RACGATIVNRPEELTESDVGTGAGLFEvKKIGDEYFTFITECKDPKACTILLRGASKDVLNEVERNLQDAMAVARNIILN 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 402 GKFLWGGGAVEAELAMRLAKYANSVGGREQLAIEAFAKALEIIPRTLAENAGIDPINTLIKLKADD-EKGRISVGVDLDN 480
Cdd:cd03337 360 PKLVPGGGATEMAVSHALSEKAKSIEGVEQWPYKAVASALEVIPRTLAQNCGANVIRTLTELRAKHaQGENSTWGIDGET 439
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 4699707 481 NGVGDMKAKGVVDPLRVKTHALESAVEVATMILRIDDVIAS 521
Cdd:cd03337 440 GDIVDMKELGIWDPLAVKAQTYKTAIEAACMLLRIDDIVSG 480
|
|
| chap_CCT_gamma |
TIGR02344 |
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ... |
7-523 |
3.22e-154 |
|
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: 451.11 E-value: 3.22e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 7 PILVLKEGTQREQGKNAQRNNIEAAKAIADAVRTTLGPKGMDKMLVDSIGDIIISNDGATILKEMDVEHPTAKMIVEVSK 86
Cdd:TIGR02344 1 PVLVLNQNTKRESGRKAQLSNIQAAKAVADIIRTCLGPRSMLKMLLDPMGGIVMTNDGNAILREIDVAHPAAKSMIELSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 87 AQDTAVGDGTTTAVVLSGELLKQAETLLDQGVHPTVISNGYRLAVNEARKIIDEIAE--KSTDDATLRKIALTALSGKNT 164
Cdd:TIGR02344 81 TQDEEVGDGTTSVIILAGEMLSVAEPFLEQNIHPTVIIRAYRKALDDALSVLEEISIpvDVNDDAAMLKLIQSCIGTKFV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 165 GLSNDFLADLVVKAVNAVAEVRDGKTIVDTAN-IKVDKKNGGSVNDTQFISGIVIDKEKVHSKMPDVVKNAKIALIDSAL 243
Cdd:TIGR02344 161 SRWSDLMCDLALDAVRTVQRDENGRKEIDIKRyAKVEKIPGGDIEDSCVLKGVMINKDVTHPKMRRYIENPRIVLLDCPL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 244 EIKKTEIEAKVQISDPSKIQDFLNQETNTFKQMVEKIKKSGANVVLCQKGIDDVAQHYLAKEGIYAVRRVKKSDMEKLAK 323
Cdd:TIGR02344 241 EYKKGESQTNIEITKEEDWNRILQMEEEYVQLMCEDIIAVKPDLVITEKGVSDLAQHYLLKANITAIRRVRKTDNNRIAR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 324 ATGAKIVTDLDDLTPSVLGE-AETVEERKIGDDRMTFVMGCKNPKAVSILIRGGTDHVVSEVERALNDAIRVVAITKEDG 402
Cdd:TIGR02344 321 ACGATIVNRPEELRESDVGTgCGLFEVKKIGDEYFTFITECKDPKACTILLRGASKDILNEVERNLQDAMAVARNVLLDP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 403 KFLWGGGAVEAELAMRLAKYANSVGGREQLAIEAFAKALEIIPRTLAENAGIDPINTLIKLKADDEKGRI-SVGVDLDNN 481
Cdd:TIGR02344 401 KLVPGGGATEMAVSVALTEKSKKLEGVEQWPYRAVADALEIIPRTLAQNCGANVIRTLTELRAKHAQENNcTWGIDGETG 480
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 4699707 482 GVGDMKAKGVVDPLRVKTHALESAVEVATMILRIDDVIASKK 523
Cdd:TIGR02344 481 KIVDMKEKGIWEPLAVKLQTYKTAIESACLLLRIDDIVSGVK 522
|
|
| chap_CCT_alpha |
TIGR02340 |
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ... |
14-528 |
4.14e-153 |
|
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: 448.79 E-value: 4.14e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 14 GTQREQGKNAQRNNIEAAKAIADAVRTTLGPKGMDKMLVDSIGDIIISNDGATILKEMDVEHPTAKMIVEVSKAQDTAVG 93
Cdd:TIGR02340 4 GGERTSGQDVRTQNVTAAMAIANIVKTSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDREVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 94 DGTTTAVVLSGELLKQAETLLDQGVHPTVISNGYRLAVNEARKIIDEIAEKSTDD---ATLRKIALTALSGKNTGLSNDF 170
Cdd:TIGR02340 84 DGTTSVVIIAAELLKRADELVKNKIHPTSVISGYRLACKEAVKYIKENLSVSVDElgrEALINVAKTSMSSKIIGLDSDF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 171 LADLVVKAVNAVAEVRD-GKTIVDTANIKVDKKNGGSVNDTQFISGIVIDKEKVHSKMPDVVKNAKIALIDSALEIKKTE 249
Cdd:TIGR02340 164 FSNIVVDAVLAVKTTNEnGETKYPIKAINILKAHGKSARESMLVKGYALNCTVASQQMPKRIKNAKIACLDFNLQKAKMA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 250 IEAKVQISDPSKIQDFLNQETNTFKQMVEKIKKSGANVVLCQKGIDDVAQHYLAKEGIYAVRRVKKSDMEKLAKATGAKI 329
Cdd:TIGR02340 244 LGVQIVVDDPEKLEQIRQREADITKERIKKILDAGANVVLTTGGIDDMCLKYFVEAGAMGVRRCKKEDLKRIAKATGATL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 330 VTDLDDLT------PSVLGEAETVEERKIGDDRMTFVMGCKNPKAVSILIRGGTDHVVSEVERALNDAIRVVAITKEDGK 403
Cdd:TIGR02340 324 VSTLADLEgeetfeASYLGFADEVVQERIADDECILIKGTKKRKSASIILRGANDFMLDEMERSLHDALCVVKRTLESNS 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 404 FLWGGGAVEAELAMRLAKYANSVGGREQLAIEAFAKALEIIPRTLAENAGIDPINTLIKLKA--------DDEKGRISVG 475
Cdd:TIGR02340 404 VVPGGGAVEAALSIYLENFATTLGSREQLAIAEFARALLIIPKTLAVNAAKDSTELVAKLRAyhaaaqlkPEKKHLKWYG 483
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 4699707 476 VDLDNNGVGDMKAKGVVDPLRVKTHALESAVEVATMILRIDDVIASKKSTPPS 528
Cdd:TIGR02340 484 LDLVNGKIRDNKEAGVLEPTVSKVKSLKFATEAAITILRIDDLIKLNPEQSKG 536
|
|
| chap_CCT_epsi |
TIGR02343 |
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ... |
7-521 |
1.39e-149 |
|
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: 439.62 E-value: 1.39e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 7 PILVLKEGTQ--REQGKNAQRNNIEAAKAIADAVRTTLGPKGMDKMLVDSIGDIIISNDGATILKEMDVEHPTAKMIVEV 84
Cdd:TIGR02343 10 PFIIIKDQDNkkRLKGLEAKKSNIAAAKSVASILRTSLGPKGMDKMLISPDGDITVTNDGATILSQMDVDNQIAKLMVEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 85 SKAQDTAVGDGTTTAVVLSGELLKQAETLLDQGVHPTVISNGYRLAVNEARKIIDEIAEKSTDDA----TLRKIALTALS 160
Cdd:TIGR02343 90 SKSQDDEIGDGTTGVVVLAGALLEQAEELLDKGIHPIKIADGFEEAARIAVEHLEEISDEISADNnnrePLIQAAKTSLG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 161 GKNTGLSNDFLADLVVKAVNAVA--EVRDgktiVDTANIKVDKKNGGSVNDTQFISGIVIDKEKVHSKMPDVVKNAKIAL 238
Cdd:TIGR02343 170 SKIVSKCHRRFAEIAVDAVLNVAdmERRD----VDFDLIKVEGKVGGSLEDTKLIKGIIIDKDFSHPQMPKEVEDAKIAI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 239 IDSALEIKKTEIEAKVQISDPSKIQDFLNQETNTFKQMVEKIKKSGANVVLCQKGIDDVAQHYLAKEGIYAVRRVKKSDM 318
Cdd:TIGR02343 246 LTCPFEPPKPKTKHKLDISSVEEYKKLQKYEQQKFKEMIDDIKKSGANLVICQWGFDDEANHLLLQNDLPAVRWVGGQEL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 319 EKLAKATGAKIVTDLDDLTPSVLGEAETVEERKIG--DDRMTFVMGCKNPKAVSILIRGGTDHVVSEVERALNDAIRVVA 396
Cdd:TIGR02343 326 ELIAIATGGRIVPRFQELSKDKLGKAGLVREISFGttKDRMLVIEQCKNSKAVTIFIRGGNKMIIEEAKRSIHDALCVVR 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 397 ITKEDGKFLWGGGAVEAELAMRLAKYANSVGGREQLAIEAFAKALEIIPRTLAENAGIDPINTLIKLKADDEKGRIS-VG 475
Cdd:TIGR02343 406 NLIKDSRIVYGGGAAEISCSLAVSQEADKYPGVEQYAIRAFADALETIPMALAENSGLDPIGTLSTLKSLQLKEKNPnLG 485
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 4699707 476 VDLDNNGVGDMKAKGVVDPLRVKTHALESAVEVATMILRIDDVIAS 521
Cdd:TIGR02343 486 VDCLGYGTNDMKEQFVFETLIGKKQQILLATQLVRMILKIDDVISP 531
|
|
| chap_CCT_delta |
TIGR02342 |
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ... |
17-522 |
6.84e-144 |
|
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: 424.58 E-value: 6.84e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 17 REQGKNAQRNNIEAAKAIADAVRTTLGPKGMDKMLVDSIGDIIISNDGATILKEMDVEHPTAKMIVEVSKAQDTAVGDGT 96
Cdd:TIGR02342 4 KDKPQDVRTSNIVAAKAVADAIRTSLGPKGMDKMIQDGKGEVIITNDGATILKQMAVLHPAAKMLVELSKAQDIEAGDGT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 97 TTAVVLSGELLKQAETLLDQGVHPTVISNGYRLAVNEARKIIDEIAEK--STDDATLRKIALTALSGKNTGLSNDFLADL 174
Cdd:TIGR02342 84 TSVVILAGALLGACERLLNKGIHPTIISESFQSAADEAIKILDEMSIPvdLSDREQLLKSATTSLSSKVVSQYSSLLAPL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 175 vvkAVNAVAEVRDGKTI--VDTANIKVDKKNGGSVNDTQFISGIVIDKEKVHSK-MPDVVKNAKIALIDSALEIKKTEIE 251
Cdd:TIGR02342 164 ---AVDAVLKVIDPENAknVDLNDIKVVKKLGGTIDDTELIEGLVFTQKASKSAgGPTRIEKAKIGLIQFQISPPKTDME 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 252 AKVQISDPSKIQDFLNQETNTFKQMVEKIKKSGANVVLCQKGI-----DDVAQHYLAKEGIYAVRRVKKSDMEKLAKATG 326
Cdd:TIGR02342 241 NQIIVNDYAQMDRVLKEERAYILNIVKKIKKTGCNVLLIQKSIlrdavNDLALHFLAKMKIMVVKDIEREEIEFICKTIG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 327 AKIVTDLDDLTPSVLGEAETVEERKIGDDRMTFVMGCKNP-KAVSILIRGGTDHVVSEVERALNDAIRVV-AITKEDGkF 404
Cdd:TIGR02342 321 CKPIASIDHFTADKLGSAELVEEVDSDGGKIIKITGIQNAgKTVTVVVRGSNKLVIDEAERSLHDALCVIrCLVKKRG-L 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 405 LWGGGAVEAELAMRLAKYANSVGGREQLAIEAFAKALEIIPRTLAENAGIDPINTLIKLKADDEKGRISVGVDLDNNGVG 484
Cdd:TIGR02342 400 IAGGGAPEIEIARRLSKYARTMKGVESYCVRAFADALEVIPYTLAENAGLNPIKVVTELRNRHANGEKTAGISVRKGGIT 479
|
490 500 510
....*....|....*....|....*....|....*...
gi 4699707 485 DMKAKGVVDPLRVKTHALESAVEVATMILRIDDVIASK 522
Cdd:TIGR02342 480 NMLEEHVLQPLLVTTSAITLASETVRSILKIDDIVFTR 517
|
|
| chap_CCT_eta |
TIGR02345 |
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ... |
7-524 |
3.76e-143 |
|
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: 423.02 E-value: 3.76e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 7 PILVLKEGTQREQGKNAQRNNIEAAKAIADAVRTTLGPKGMDKMLVDSIGDIIISNDGATILKEMDVEHPTAKMIVEVSK 86
Cdd:TIGR02345 3 TIVLLKEGTDTSQGKGQLISNINACVAIAEALKTTLGPRGMDKLIVGSNGKATISNDGATILKLLDIVHPAAKTLVDIAK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 87 AQDTAVGDGTTTAVVLSGELLKQAETLLDQGVHPTVISNGYRLAVNEARKIIDEIA-----EKSTDDATLRKIALTALSG 161
Cdd:TIGR02345 83 SQDAEVGDGTTSVTILAGELLKEAKPFIEEGVHPQLIIRCYREALSLAVEKIKEIAvtideEKGEQRELLEKCAATALSS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 162 KNTGLSNDFLADLVVKAVNAVAevrdgKTIVDTANIKVDKKNGGSVNDTQFISGIVIDKE---KVHSKMPDVVKNAKIAL 238
Cdd:TIGR02345 163 KLISHNKEFFSKMIVDAVLSLD-----RDDLDLKLIGIKKVQGGALEDSQLVNGVAFKKTfsyAGFEQQPKKFANPKILL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 239 IDSALEIKKTEIEAKVQISDPSKIQDFLNQETNTFKQMVEKIKKSGANVVLCQKGIDDVAQHYLAKEGIYAVRRVKKSDM 318
Cdd:TIGR02345 238 LNVELELKAEKDNAEIRVEDVEDYQAIVDAEWAIIFRKLEKIVESGANVVLSKLPIGDLATQYFADRDIFCAGRVSAEDL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 319 EKLAKATGAKIVTDLDDLTPSVLGEAETVEERKIGDDRMTFVMGCKNPKAVSILIRGGTDHVVSEVERALNDAIRVVAIT 398
Cdd:TIGR02345 318 KRVIKACGGSIQSTTSDLEADVLGTCALFEERQIGSERYNYFTGCPHAKTCTIILRGGAEQFIEEAERSLHDAIMIVRRA 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 399 KEDGKFLWGGGAVEAELAMRLAKYANSVGGREQLAIEAFAKALEIIPRTLAENAGIDPINTLIKLKADDEKGRISVGVDL 478
Cdd:TIGR02345 398 LKNKKIVAGGGAIEMELSKCLRDYSKTIDGKQQLIINAFAKALEIIPRQLCENAGFDSIEILNKLRSRHAKGGKWYGVDI 477
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 4699707 479 DNNGVGDMKAKGVVDPLRVKTHALESAVEVATMILRIDDVIASKKS 524
Cdd:TIGR02345 478 NTEDIGDNFEAFVWEPALVKINALKAAFEAACTILSVDETITNPKS 523
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
1-519 |
2.86e-133 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 397.86 E-value: 2.86e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 1 MMTGQVPILVLKEGTQREQGKNAQRNNIEAAKAIADAVRTTLGPKGMDKMLVDS-----IGDIIISNDGATILKEMDVEH 75
Cdd:PTZ00212 1 MIMANVPPQVLKQGAQEEKGETARLQSFVGAIAVADLVKTTLGPKGMDKILQPMsegprSGNVTVTNDGATILKSVWLDN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 76 PTAKMIVEVSKAQDTAVGDGTTTAVVLSGELLKQAETLLDQGVHPTVISNGYRLAVNEARKIIDEIAEKSTDDAT----- 150
Cdd:PTZ00212 81 PAAKILVDISKTQDEEVGDGTTSVVVLAGELLREAEKLLDQKIHPQTIIEGWRMALDVARKALEEIAFDHGSDEEkfked 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 151 LRKIALTALSGKNTGLSNDFLADLvvkAVNAVAEVRDGKTIvdtANIKVDKKNGGSVNDTQFISGIVIDKeKVHSKMPDV 230
Cdd:PTZ00212 161 LLNIARTTLSSKLLTVEKDHFAKL---AVDAVLRLKGSGNL---DYIQIIKKPGGTLRDSYLEDGFILEK-KIGVGQPKR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 231 VKNAKIALIDSALEIKKTEI-EAKVQISDPSKIQDFLNQETNTFKQMVEKIKKSGANVVLCQKGIDDVAQHYLAKEGIYA 309
Cdd:PTZ00212 234 LENCKILVANTPMDTDKIKIyGAKVKVDSMEKVAEIEAAEKEKMKNKVDKILAHGCNVFINRQLIYNYPEQLFAEAGIMA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 310 VRRVKKSDMEKLAKATGAKIVTDLDDLTPSVLGEAETVEERKIGDDRMTFVMGCKNPKAVSILIRGGTDHVVSEVERALN 389
Cdd:PTZ00212 314 IEHADFDGMERLAAALGAEIVSTFDTPEKVKLGHCDLIEEIMIGEDKLIRFSGCAKGEACTIVLRGASTHILDEAERSLH 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 390 DAIRVVAITKEDGKFLWGGGAVEAELAMRLAKYANSVGGREQLAIEAFAKALEIIPRTLAENAGIDPINTLIKLKADDEK 469
Cdd:PTZ00212 394 DALCVLSQTVKDTRVVLGGGCSEMLMANAVEELAKKVEGKKSLAIEAFAKALRQIPTIIADNGGYDSAELVSKLRAEHYK 473
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 4699707 470 GRISVGVDLDNNGVGDMKAKGVVDPLRVKTHALESAVEVATMILRIDDVI 519
Cdd:PTZ00212 474 GNKTAGIDMEKGTVGDMKELGITESYKVKLSQLCSATEAAEMILRVDDII 523
|
|
| TCP1_zeta |
cd03342 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
13-519 |
8.14e-132 |
|
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: 392.39 E-value: 8.14e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 13 EGTQREQgknAQRNNIEAAKAIADAVRTTLGPKGMDKMLVDSIGDIIISNDGATILKEMDVEHPTAKMIVEVSKAQDTAV 92
Cdd:cd03342 6 EVLRRGQ---ALAVNISAAKGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLSEMQIQHPTASMIARAATAQDDIT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 93 GDGTTTAVVLSGELLKQAETLLDQGVHPTVISNGYRLAVNEARKIIDEIA---EKSTDDATLRKIALTALSGKNTGLSND 169
Cdd:cd03342 83 GDGTTSNVLLIGELLKQAERYIQEGVHPRIITEGFELAKNKALKFLESFKvpvEIDTDRELLLSVARTSLRTKLHADLAD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 170 FLADLVVKAVNAVaeVRDGKTIvDTANIKVDKKNGGSVNDTQFISGIVIDKEKVHSKMPDVVKNAKIALIDSALEIKKTE 249
Cdd:cd03342 163 QLTEIVVDAVLAI--YKPDEPI-DLHMVEIMQMQHKSDSDTKLIRGLVLDHGARHPDMPKRVENAYILTCNVSLEYEKTE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 250 IEAKVQISdpskiqdflnqetntfkqmvekikksganVVLCQKGIDDVAQHYLAKEGIYAVRRVKKSDMEKLAKATGAKI 329
Cdd:cd03342 240 VNSGFFYS-----------------------------VVINQKGIDPPSLDMLAKEGILALRRAKRRNMERLTLACGGVA 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 330 VTDLDDLTPSVLGEAETVEERKIGDDRMTFVMGCKNPKAVSILIRGGTDHVVSEVERALNDAIRVVAITKEDGKFLWGGG 409
Cdd:cd03342 291 MNSVDDLSPECLGYAGLVYERTLGEEKYTFIEGVKNPKSCTILIKGPNDHTITQIKDAIRDGLRAVKNAIEDKCVVPGAG 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 410 AVEAELAMRLAKYANSVGGREQLAIEAFAKALEIIPRTLAENAGIDPINTLIKLKADDEKGRISVGVDLDNNGVGDMKAK 489
Cdd:cd03342 371 AFEVALYAHLKEFKKSVKGKAKLGVQAFADALLVIPKTLAENSGLDVQETLVKLQDEYAEGGQVGGVDLDTGEPMDPESE 450
|
490 500 510
....*....|....*....|....*....|
gi 4699707 490 GVVDPLRVKTHALESAVEVATMILRIDDVI 519
Cdd:cd03342 451 GIWDNYSVKRQILHSATVIASQLLLVDEII 480
|
|
| TCP1_beta |
cd03336 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ... |
10-519 |
2.93e-128 |
|
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: 384.76 E-value: 2.93e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 10 VLKEGTQREQGKNAQRNNIEAAKAIADAVRTTLGPKGMDKML--VDSIGDIIISNDGATILKEMDVEHPTAKMIVEVSKA 87
Cdd:cd03336 1 ILKDGAQEEKGETARLSSFVGAIAIGDLVKTTLGPKGMDKILqsVGRSGGVTVTNDGATILKSIGVDNPAAKVLVDISKV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 88 QDTAVGDGTTTAVVLSGELLKQAETLLDQGVHPTVISNGYRLAVNEARKIIDEIAEKSTDDAT-----LRKIALTALSGK 162
Cdd:cd03336 81 QDDEVGDGTTSVTVLAAELLREAEKLVAQKIHPQTIIEGYRMATAAAREALLSSAVDHSSDEEafredLLNIARTTLSSK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 163 NTGLSNDFLADLvvkAVNAVAEVRDGktiVDTANIKVDKKNGGSVNDTQFISGIVIDKeKVHSKMPDVVKNAKIALIDSA 242
Cdd:cd03336 161 ILTQDKEHFAEL---AVDAVLRLKGS---GNLDAIQIIKKLGGSLKDSYLDEGFLLDK-KIGVNQPKRIENAKILIANTP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 243 LEIKKTEI-EAKVQISDPSKIQDFLNQETNTFKQMVEKIKKSGANVVLCQKGIDDVAQHYLAKEGIYAVRRVKKSDMEKL 321
Cdd:cd03336 234 MDTDKIKIfGAKVRVDSTAKVAEIEEAEKEKMKNKVEKILKHGINCFINRQLIYNYPEQLFADAGIMAIEHADFDGVERL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 322 AKATGAKIVTDLDDLTPSVLGEAETVEERKIGDDRMTFVMGCKNPKAVSILIRGGTDHVVSEVERALNDAIRVVAITKED 401
Cdd:cd03336 314 ALVTGGEIASTFDHPELVKLGTCKLIEEIMIGEDKLIRFSGVAAGEACTIVLRGASQQILDEAERSLHDALCVLAQTVKD 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 402 GKFLWGGGAVEAELAMRLAKYANSVGGREQLAIEAFAKALEIIPRTLAENAGIDPINTLIKLKADDEKGRISVGVDLDNN 481
Cdd:cd03336 394 TRVVLGGGCSEMLMAKAVEELAKKTPGKKSLAIEAFAKALRQLPTIIADNAGYDSAELVAQLRAAHYNGNTTAGLDMRKG 473
|
490 500 510
....*....|....*....|....*....|....*...
gi 4699707 482 GVGDMKAKGVVDPLRVKTHALESAVEVATMILRIDDVI 519
Cdd:cd03336 474 TVGDMKELGITESFKVKRQVLLSASEAAEMILRVDDII 511
|
|
| TCP1_theta |
cd03341 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ... |
26-522 |
3.12e-124 |
|
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: 372.71 E-value: 3.12e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 26 NNIEAAKAIADAVRTTLGPKGMDKMLVDSIGDIIISNDGATILKEMDVEHPTAKMIVEVSKAQDTAVGDGTTTAVVLSGE 105
Cdd:cd03341 12 RNIEACKELSQITRTSYGPNGMNKMVINHLEKLFVTSDAATILRELEVQHPAAKLLVMASQMQEEEIGDGTNLVVVLAGE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 106 LLKQAETLLDQGVHPTVISNGYRLAVNEARKIIDEIAEKSTDDA----TLRKIALTALSGKNTGLSnDFLADLVVKAVNA 181
Cdd:cd03341 92 LLEKAEELLRMGLHPSEIIEGYEKALKKALEILEELVVYKIEDLrnkeEVSKALKTAIASKQYGNE-DFLSPLVAEACIS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 182 VAEVRDGKTIVDtaNIKVDKKNGGSVNDTQFISGIVIDKEKVHSKMpdVVKNAKIALIDSALEIkkteieakvqisdpsk 261
Cdd:cd03341 171 VLPENIGNFNVD--NIRVVKILGGSLEDSKVVRGMVFKREPEGSVK--RVKKAKVAVFSCPFDI---------------- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 262 iqdflnqetntfkqmvekikksGANVVLCQKGIDDVAQHYLAKEGIYAVRRVKKSDMEKLAKATGAKIVTDLDDLTPSVL 341
Cdd:cd03341 231 ----------------------GVNVIVAGGSVGDLALHYCNKYGIMVIKINSKFELRRLCRTVGATPLPRLGAPTPEEI 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 342 GEAETVEERKIGDDRMTFVMGCKNPKAVS-ILIRGGTDHVVSEVERALNDAIRVVAITKEDGKFLWGGGAVEAELAMRLA 420
Cdd:cd03341 289 GYCDSVYVEEIGDTKVVVFRQNKEDSKIAtIVLRGATQNILDDVERAIDDGVNVFKSLTKDGRFVPGAGATEIELAKKLK 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 421 KYANSVGGREQLAIEAFAKALEIIPRTLAENAGIDPINTLIKLKADDEKGRISVGVDLDNN--GVGDMKAKGVVDPLRVK 498
Cdd:cd03341 369 EYGEKTPGLEQYAIKKFAEAFEVVPRTLAENAGLDATEVLSELYAAHQKGNKSAGVDIESGdeGTKDAKEAGIFDHLATK 448
|
490 500
....*....|....*....|....
gi 4699707 499 THALESAVEVATMILRIDDVIASK 522
Cdd:cd03341 449 KWAIKLATEAAVTVLRVDQIIMAK 472
|
|
| chap_CCT_theta |
TIGR02346 |
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ... |
10-527 |
6.50e-124 |
|
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: 374.05 E-value: 6.50e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 10 VLKEGTQREQG-KNAQRNNIEAAKAIADAVRTTLGPKGMDKMLVDSIGDIIISNDGATILKEMDVEHPTAKMIVEVSKAQ 88
Cdd:TIGR02346 5 LLKEGYRHFSGlEEAVIKNIEACKELSQITRTSLGPNGMNKMVINHLEKLFVTNDAATILRELEVQHPAAKLLVMASEMQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 89 DTAVGDGTTTAVVLSGELLKQAETLLDQGVHPTVISNGYRLAVNEARKIIDEI----AEKSTDDATLRKIALTALSGKNT 164
Cdd:TIGR02346 85 ENEIGDGTNLVLVLAGELLNKAEELIRMGLHPSEIIKGYEMALKKAMEILEELvvweVKDLRDKDELIKALKASISSKQY 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 165 GlSNDFLADLVVKAVNAVAEVRDGKTIVDtaNIKVDKKNGGSVNDTQFISGIVIDKEKVHSKMPdvVKNAKIALIDSALE 244
Cdd:TIGR02346 165 G-NEDFLAQLVAQACSTVLPKNPQNFNVD--NIRVCKILGGSLSNSEVLKGMVFNREAEGSVKS--VKNAKVAVFSCPLD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 245 IKKTEIEAKVQISDPSKIQDFLNQETNTFKQMVEKIKKSGANVVLCQKGIDDVAQHYLAKEGIYAVRRVKKSDMEKLAKA 324
Cdd:TIGR02346 240 TATTETKGTVLIHNAEELLNYSKGEENQIEAMIKAIADSGVNVIVTGGSVGDMALHYLNKYNIMVLKIPSKFELRRLCKT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 325 TGAKIVTDLDDLTPSVLGEAETVEERKIGDDRMTFVMGCKNPKAVS-ILIRGGTDHVVSEVERALNDAIRVVAITKEDGK 403
Cdd:TIGR02346 320 VGATPLPRLGAPTPEEIGYVDSVYVSEIGGDKVTVFKQENGDSKIStIILRGSTDNLLDDIERAIDDGVNTVKALVKDGR 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 404 FLWGGGAVEAELAMRLAKYANSVGGREQLAIEAFAKALEIIPRTLAENAGIDPINTLIKLKADDEKGRISVGVDLDNN-- 481
Cdd:TIGR02346 400 LLPGAGATEIELASRLTKYGEKLPGLDQYAIKKFAEAFEIIPRTLAENAGLNANEVIPKLYAAHKKGNKSKGIDIEAEsd 479
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 4699707 482 GVGDMKAKGVVDPLRVKTHALESAVEVATMILRIDDVIASKKSTPP 527
Cdd:TIGR02346 480 GVKDASEAGIYDMLATKKWAIKLATEAAVTVLRVDQIIMAKPAGGP 525
|
|
| chap_CCT_zeta |
TIGR02347 |
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ... |
27-525 |
8.56e-117 |
|
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: 355.58 E-value: 8.56e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 27 NIEAAKAIADAVRTTLGPKGMDKMLVDSIGDIIISNDGATILKEMDVEHPTAKMIVEVSKAQDTAVGDGTTTAVVLSGEL 106
Cdd:TIGR02347 21 NINAARGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEMQIQHPTASMIARAATAQDDITGDGTTSTVLLIGEL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 107 LKQAETLLDQGVHPTVISNGYRLAVNEARKIIDEIA---EKSTDDATLRKIALTALSGKNTGLSNDFLADLVVKAVNAVA 183
Cdd:TIGR02347 101 LKQAERYILEGVHPRIITEGFEIARKEALQFLDKFKvkkEDEVDREFLLNVARTSLRTKLPADLADQLTEIVVDAVLAIK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 184 evRDGKTIvDTANIKVDKKNGGSVNDTQFISGIVIDKEKVHSKMPDVVKNAKIALIDSALEIKKTEIEAKVQISDPSKIQ 263
Cdd:TIGR02347 181 --KDGEDI-DLFMVEIMEMKHKSATDTTLIRGLVLDHGARHPDMPRRVKNAYILTCNVSLEYEKTEVNSGFFYSSAEQRE 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 264 DFLNQETNTFKQMVEKI----KKSGAN------VVLCQKGIDDVAQHYLAKEGIYAVRRVKKSDMEKLAKATGAKIVTDL 333
Cdd:TIGR02347 258 KLVKAERKFVDDRVKKIielkKKVCGKspdkgfVVINQKGIDPPSLDLLAKEGIMALRRAKRRNMERLTLACGGEALNSV 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 334 DDLTPSVLGEAETVEERKIGDDRMTFVMGCKNPKAVSILIRGGTDHVVSEVERALNDAIRVVAITKEDGKFLWGGGAVEA 413
Cdd:TIGR02347 338 EDLTPECLGWAGLVYETTIGEEKYTFIEECKNPKSCTILIKGPNDHTIAQIKDAVRDGLRAVKNAIEDKCVVPGAGAFEI 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 414 ELAMRLAKYANSVGGREQLAIEAFAKALEIIPRTLAENAGIDPINTLIKLKADDEKGRISVGVDLDNNGVGDMKAKGVVD 493
Cdd:TIGR02347 418 AAYRHLKEYKKSVKGKAKLGVEAFANALLVIPKTLAENSGFDAQDTLVKLEDEHDEGGEVVGVDLNTGEPIDPEIKGIWD 497
|
490 500 510
....*....|....*....|....*....|..
gi 4699707 494 PLRVKTHALESAVEVATMILRIDDVIASKKST 525
Cdd:TIGR02347 498 NYRVKKQLIQSATVIASQLLLVDEVMRAGRSM 529
|
|
| chap_CCT_beta |
TIGR02341 |
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ... |
10-519 |
5.46e-102 |
|
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: 317.19 E-value: 5.46e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 10 VLKEGTQREQGKNAQRNNIEAAKAIADAVRTTLGPKGMDKMLV--DSIGDIIISNDGATILKEMDVEHPTAKMIVEVSKA 87
Cdd:TIGR02341 2 IFKDGADEERAENARLSSFVGAIAIGDLVKSTLGPKGMDKILQssSSDASIMVTNDGATILKSIGVDNPAAKVLVDMSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 88 QDTAVGDGTTTAVVLSGELLKQAETLLDQGVHPTVISNGYRLAVNEARKIIDEIAEKSTDDAT-----LRKIALTALSGK 162
Cdd:TIGR02341 82 QDDEVGDGTTSVTVLAAELLREAEKLINQKIHPQTIIAGYREATKAARDALLKSAVDNGSDEVkfrqdLMNIARTTLSSK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 163 NTGLSNDFLADLvvkAVNAVAEVRdGKTIVDtaNIKVDKKNGGSVNDTQFISGIVIDKeKVHSKMPDVVKNAKIALIDSA 242
Cdd:TIGR02341 162 ILSQHKDHFAQL---AVDAVLRLK-GSGNLE--AIQIIKKLGGSLADSYLDEGFLLDK-KIGVNQPKRIENAKILIANTG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 243 LEIKKTEI-EAKVQISDPSKIQDFLNQETNTFKQMVEKIKKSGANVVLCQKGIDDVAQHYLAKEGIYAVRRVKKSDMEKL 321
Cdd:TIGR02341 235 MDTDKVKIfGSRVRVDSTAKVAELEHAEKEKMKEKVEKILKHGINCFINRQLIYNYPEQLFADAGVMAIEHADFEGVERL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 322 AKATGAKIVTDLDDLTPSVLGEAETVEERKIGDDRMTFVMGCKNPKAVSILIRGGTDHVVSEVERALNDAIRVVAITKED 401
Cdd:TIGR02341 315 ALVTGGEIVSTFDHPELVKLGSCDLIEEIMIGEDKLLKFSGVKLGEACTIVLRGATQQILDEAERSLHDALCVLSQTVKE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 402 GKFLWGGGAVEAELAMRLAKYANSVGGREQLAIEAFAKALEIIPRTLAENAGIDPINTLIKLKADDEKGRISVGVDLDNN 481
Cdd:TIGR02341 395 SRTVLGGGCSEMLMSKAVTQEAQRTPGKEALAVEAFARALRQLPTIIADNAGFDSAELVAQLRAAHYNGNTTMGLDMNEG 474
|
490 500 510
....*....|....*....|....*....|....*...
gi 4699707 482 GVGDMKAKGVVDPLRVKTHALESAVEVATMILRIDDVI 519
Cdd:TIGR02341 475 TIADMRQLGITESYKVKRAVVSSAAEAAEVILRVDNII 512
|
|
| chaperonin_like |
cd03333 |
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ... |
148-401 |
1.93e-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: 229.66 E-value: 1.93e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 148 DATLRKIALTALSGKNTGLSnDFLADLVVKAVNAVAevrDGKTIVDTANIKVDKKNGGSVNDTQFISGIVIDKEKVHSKM 227
Cdd:cd03333 1 RELLLQVATTSLNSKLSSWD-DFLGKLVVDAVLKVG---PDNRMDDLGVIKVEKIPGGSLEDSELVVGVVFDKGYASPYM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 228 PDVVKNAKIALIDSALEikkteieakvqisdpskiqdflnqetntfkqmvekikksgaNVVLCQKGIDDVAQHYLAKEGI 307
Cdd:cd03333 77 PKRLENAKILLLDCPLE-----------------------------------------YVVIAEKGIDDLALHYLAKAGI 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 308 YAVRRVKKSDMEKLAKATGAKIVTDLDDLTPSVLGEAETVEERKIGDDRMTFVMGCKNPKAVSILIRGGTDHVVSEVERA 387
Cdd:cd03333 116 MAVRRVKKEDLERIARATGATIVSSLEDLTPEDLGTAELVEETKIGEEKLTFIEGCKGGKAATILLRGATEVELDEVKRS 195
|
250
....*....|....
gi 4699707 388 LNDAIRVVAITKED 401
Cdd:cd03333 196 LHDALCAVRAAVEE 209
|
|
| GroEL |
cd03344 |
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ... |
20-513 |
2.86e-32 |
|
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: 129.88 E-value: 2.86e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 20 GKNAQRNNIEAAKAIADAVRTTLGPKGMDKMLVDSIGDIIISNDGATILKEMDVEHPT----AKMIVEVSKAQDTAVGDG 95
Cdd:cd03344 6 GEEARKALLRGVNKLADAVKVTLGPKGRNVVIEKSFGSPKITKDGVTVAKEIELEDPFenmgAQLVKEVASKTNDVAGDG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 96 TTTAVVLSGELLKQAETLLDQGVHPTVISNGYRLAVneaRKIIDEIAEKSTDDATLRKIALTA-LSGKNtglsNDFLADL 174
Cdd:cd03344 86 TTTATVLARAIIKEGLKAVAAGANPMDLKRGIEKAV---EAVVEELKKLSKPVKTKEEIAQVAtISANG----DEEIGEL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 175 VVKAVNAVAE-----VRDGKTIVDTanikvdkknggsvndTQFISGIVIDKEKVHSKMPDVVKNAKIALIDsaleikkte 249
Cdd:cd03344 159 IAEAMEKVGKdgvitVEEGKTLETE---------------LEVVEGMQFDRGYLSPYFVTDPEKMEVELEN--------- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 250 ieAKVQISDpSKIqdflnqetNTFKQMV---EKIKKSGANVVLcqkgI-DDVAQHYLA------KEGIYAVRRVK----- 314
Cdd:cd03344 215 --PYILLTD-KKI--------SSIQELLpilELVAKAGRPLLI----IaEDVEGEALAtlvvnkLRGGLKVCAVKapgfg 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 315 ---KSDMEKLAKATGAKIVTD-----LDDLTPSVLGEAETVEerkIGDDRMTFVMGCKNPKAVS---------------- 370
Cdd:cd03344 280 drrKAMLEDIAILTGGTVISEelglkLEDVTLEDLGRAKKVV---VTKDDTTIIGGAGDKAAIKariaqirkqieettsd 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 371 -------------------ILIRGGTDHVVSEVERALNDAIRVVAITKEDGkFLWGGGAVEAELAMRLAKYANSVGGrEQ 431
Cdd:cd03344 357 ydkeklqerlaklsggvavIKVGGATEVELKEKKDRVEDALNATRAAVEEG-IVPGGGVALLRASPALDKLKALNGD-EK 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 432 LAIEAFAKALEIIPRTLAENAGIDP---INTLIKLKADdekgrisVGVDLDNNGVGDMKAKGVVDPLRVKTHALESAVEV 508
Cdd:cd03344 435 LGIEIVRRALEAPLRQIAENAGVDGsvvVEKVLESPDG-------FGYDAATGEYVDMIEAGIIDPTKVVRSALQNAASV 507
|
....*
gi 4699707 509 ATMIL 513
Cdd:cd03344 508 ASLLL 512
|
|
| PTZ00114 |
PTZ00114 |
Heat shock protein 60; Provisional |
20-513 |
1.07e-29 |
|
Heat shock protein 60; Provisional
Pssm-ID: 185455 Cd Length: 555 Bit Score: 122.71 E-value: 1.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 20 GKNAQRNNIEAAKAIADAVRTTLGPKGMDKMLVDSIGDIIISNDGATILKEMDVEHPT----AKMIVEVSKAQDTAVGDG 95
Cdd:PTZ00114 20 GDEARQSLLKGIERLADAVAVTLGPKGRNVIIEQEYGSPKITKDGVTVAKAIEFSDRFenvgAQLIRQVASKTNDKAGDG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 96 TTTAVVLSGELLKQAETLLDQGVHPTVISNGYRLAVNEARKIIDEIAEKSTDDATLRKIALTALSGkntglsNDFLADLV 175
Cdd:PTZ00114 100 TTTATILARAIFREGCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQSRPVKTKEDILNVATISANG------DVEIGSLI 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 176 VKA-----VNAVAEVRDGKTIVDTANikvdkknggsvndtqFISGIVIDKEKVHSKMPDVVKNAKIALIDSALEIKKTEI 250
Cdd:PTZ00114 174 ADAmdkvgKDGTITVEDGKTLEDELE---------------VVEGMSFDRGYISPYFVTNEKTQKVELENPLILVTDKKI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 251 eakvqisdpSKIQDFLNqetntfkqMVEKIKKSGANVVLCQKGIDDVAQHYLA------KEGIYAVR-----RVKKSDME 319
Cdd:PTZ00114 239 ---------SSIQSILP--------ILEHAVKNKRPLLIIAEDVEGEALQTLIinklrgGLKVCAVKapgfgDNRKDILQ 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 320 KLAKATGAKIV------TDLDDLTPSVLGEAETVEERKigdDRMTFVMGCKNPKAVS----------------------- 370
Cdd:PTZ00114 302 DIAVLTGATVVsednvgLKLDDFDPSMLGSAKKVTVTK---DETVILTGGGDKAEIKervellrsqierttseydkeklk 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 371 ------------ILIRGGTDHVVSEVERALNDAIRVVAITKEDGkFLWGGGA--VEAELAMRLAKYANSVGGREQLAIEA 436
Cdd:PTZ00114 379 erlaklsggvavIKVGGASEVEVNEKKDRIEDALNATRAAVEEG-IVPGGGValLRASKLLDKLEEDNELTPDQRTGVKI 457
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4699707 437 FAKALEIIPRTLAENAGIDPINTLIKLKaddEKGRISVGVDLDNNGVGDMKAKGVVDPLRVKTHALESAVEVATMIL 513
Cdd:PTZ00114 458 VRNALRLPTKQIAENAGVEGAVVVEKIL---EKKDPSFGYDAQTGEYVNMFEAGIIDPTKVVRSALVDAASVASLML 531
|
|
| Fab1_TCP |
cd03334 |
TCP-1 like domain of the eukaryotic phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinase Fab1. ... |
169-386 |
6.26e-29 |
|
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: 115.40 E-value: 6.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 169 DFLADLVVKAVNAV-AEVRDGKTIVDTANIKVDKKNGGSVNDTQFISGIVIDKEKVHSKMPDVVKNAKIALIDSALEIKK 247
Cdd:cd03334 21 DILLPLVWKAASNVkPDVRAGDDMDIRQYVKIKKIPGGSPSDSEVVDGVVFTKNVAHKRMPSKIKNPRILLLQGPLEYQR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 248 teIEAKVQISDPskiqdFLNQETNTFKQMVEKIKKSGANVVLCQKGIDDVAQHYLAKEGIYAVRRVKKSDMEKLAKATGA 327
Cdd:cd03334 101 --VENKLLSLDP-----VILQEKEYLKNLVSRIVALRPDVILVEKSVSRIAQDLLLEAGITLVLNVKPSVLERISRCTGA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4699707 328 KIVTDLDDL-TPSVLGEAETVEERKIGDDR-----MTFVMGCKNPKAVSILIRGGTDHVVSEVER 386
Cdd:cd03334 174 DIISSMDDLlTSPKLGTCESFRVRTYVEEHgrsktLMFFEGCPKELGCTILLRGGDLEELKKVKR 238
|
|
| groEL |
PRK12849 |
chaperonin GroEL; Reviewed |
33-522 |
9.58e-29 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237230 Cd Length: 542 Bit Score: 119.91 E-value: 9.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 33 AIADAVRTTLGPKGMDKMLVDSIGDIIISNDGATILKEMDVEHP----TAKMIVEVSKAQDTAVGDGTTTAVVLSGELLK 108
Cdd:PRK12849 21 KLADAVKVTLGPKGRNVVIDKSFGAPTITKDGVSIAKEIELEDPfenlGAQLVKEVASKTNDVAGDGTTTATVLAQALVQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 109 QAETLLDQGVHPTVISNGYRLAVNEARKIIDEIAEKSTDDATLRKIALTALSGkntglsNDFLADLVVKAVNAVAE---- 184
Cdd:PRK12849 101 EGLKNVAAGANPMDLKRGIDKAVEAVVEELKALARPVSGSEEIAQVATISANG------DEEIGELIAEAMEKVGKdgvi 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 185 -VRDGKTIVDTANIkvdkknggsVNDTQFISG-----IVIDKEkvhsKMPDVVKNAKIALIDSALeikkteieakvqisd 258
Cdd:PRK12849 175 tVEESKTLETELEV---------TEGMQFDRGylspyFVTDPE----RMEAVLEDPLILLTDKKI--------------- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 259 pSKIQDFLnqetntfkQMVEKIKKSGANVVLCQkgiDDVAQHYLAK------EGIYAVRRVK--------KSDMEKLAKA 324
Cdd:PRK12849 227 -SSLQDLL--------PLLEKVAQSGKPLLIIA---EDVEGEALATlvvnklRGGLKVAAVKapgfgdrrKAMLEDIAIL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 325 TGAKIVTD-----LDDLTPSVLGEAETVEerkIGDDRMTFVMGCKNPKAVS---ILIRGGTDHVVSEVER---------- 386
Cdd:PRK12849 295 TGGTVISEdlglkLEEVTLDDLGRAKRVT---ITKDNTTIVDGAGDKEAIEarvAQIRRQIEETTSDYDReklqerlakl 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 387 ----------------------ALNDAIRVVAITKEDGkFLWGGGAVEAELAMRLAKYANSVGGrEQLAIEAFAKALEII 444
Cdd:PRK12849 372 aggvavikvgaatevelkerkdRVEDALNATRAAVEEG-IVPGGGVALLRAAKALDELAGLNGD-QAAGVEIVRRALEAP 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 445 PRTLAENAGIDP---INTLIKLKAddekgriSVGVDLDNNGVGDMKAKGVVDPLRVKTHALESAVEVATMILRIDDVIAS 521
Cdd:PRK12849 450 LRQIAENAGLDGsvvVAKVLELED-------GFGFNAATGEYGDLIAAGIIDPVKVTRSALQNAASVAGLLLTTEALVAD 522
|
.
gi 4699707 522 K 522
Cdd:PRK12849 523 K 523
|
|
| groEL |
PRK12850 |
chaperonin GroEL; Reviewed |
33-527 |
1.20e-26 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237231 Cd Length: 544 Bit Score: 113.66 E-value: 1.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 33 AIADAVRTTLGPKGMDKMLVDSIGDIIISNDGATILKEMDVEHP----TAKMIVEVSKAQDTAVGDGTTTAVVLSGELLK 108
Cdd:PRK12850 22 ILANAVKVTLGPKGRNVVLEKSFGAPRITKDGVTVAKEIELEDKfenmGAQMVKEVASKTNDLAGDGTTTATVLAQAIVR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 109 QAETLLDQGVHPTVISNGYRLAVNEARKIIDEIAEKSTDDATLRKIALTALSGKNTglSNDFLADLVVKAVN-AVAEVRD 187
Cdd:PRK12850 102 EGAKLVAAGMNPMDLKRGIDLAVAAVVDELKKIAKKVTSSKEIAQVATISANGDES--IGEMIAEAMDKVGKeGVITVEE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 188 GKTIVDTANIkVDkkngGSVNDTQFISG-IVIDKEKVHSKMPD---VVKNAKIALIDSALEIkkteIEAKVQISDPSKI- 262
Cdd:PRK12850 180 AKTLGTELDV-VE----GMQFDRGYLSPyFVTNPEKMRAELEDpyiLLHEKKISNLQDLLPI----LEAVVQSGRPLLIi 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 263 -QDFLNQETNTFkqMVEKIKKSGANVVLCQKGIDDvaqhylakegiyavRRvkKSDMEKLAKATGAKIVTD-----LDDL 336
Cdd:PRK12850 251 aEDVEGEALATL--VVNKLRGGLKSVAVKAPGFGD--------------RR--KAMLEDIAVLTGGQVISEdlgikLENV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 337 TPSVLGEAETVEerkIGDDRMTFVMGCKNPKavsiLIRGGTDHVVSEVERALNDA------------------IRVVAIT 398
Cdd:PRK12850 313 TLDMLGRAKRVL---ITKENTTIIDGAGDKK----NIEARVKQIRAQIEETTSDYdreklqerlaklaggvavIRVGGAT 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 399 K---------------------EDGKFLWGGGA-VEAELAMRLAKYANsvgGREQLAIEAFAKALEIIPRTLAENAGIDP 456
Cdd:PRK12850 386 EvevkekkdrvddalhatraavEEGIVPGGGVAlLRARSALRGLKGAN---ADETAGIDIVRRALEEPLRQIATNAGFEG 462
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4699707 457 INTLIKLKaddeKGRISVGVDLDNNGVGDMKAKGVVDPLRVKTHALESAVEVATMILRIDDVIASKKSTPP 527
Cdd:PRK12850 463 SVVVGKVA----ELPGNFGFNAQTGEYGDMVEAGIIDPAKVTRTALQDAASIAALLITTEAMVAEAPKKAA 529
|
|
| GroEL |
TIGR02348 |
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ... |
32-523 |
1.07e-25 |
|
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES cytosolic chaperonin. It is found in bacteria, organelles derived from bacteria, and occasionally in the Archaea. The bacterial GroEL/GroES group I chaperonin is replaced a group II chaperonin, usually called the thermosome in the Archaeota and CCT (chaperone-containing TCP) in the Eukaryota. GroEL, thermosome subunits, and CCT subunits all fall under the scope of pfam00118. [Protein fate, Protein folding and stabilization]
Pssm-ID: 274089 Cd Length: 524 Bit Score: 110.46 E-value: 1.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 32 KAIADAVRTTLGPKGMDKMLVDSIGDIIISNDGATILKEMDVEHP----TAKMIVEV-SKAQDTAvGDGTTTAVVLSGEL 106
Cdd:TIGR02348 19 DKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDKfenmGAQLVKEVaSKTNDVA-GDGTTTATVLAQAI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 107 LKQAETLLDQGVHPTVISNGYRLAVNearKIIDEIAEKSTDDATLRKIALTA-LSGKNTGLSNDFLADLVVK-AVNAVAE 184
Cdd:TIGR02348 98 VKEGLKNVAAGANPIELKRGIEKAVE---AVVEELKKLSKPVKGKKEIAQVAtISANNDEEIGSLIAEAMEKvGKDGVIT 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 185 VRDGKTIVDTANIkvdkknggsVNDTQFISG-----IVIDKEkvhsKMPDVVKNAKIALIDSALeikkteieakvqisdp 259
Cdd:TIGR02348 175 VEESKSLETELEV---------VEGMQFDRGyispyFVTDAE----KMEVELENPYILITDKKI---------------- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 260 SKIQDFLnqetntfkQMVEKIKKSGANVVLCQKGIDDVAQHYLA---KEGIYAVRRVK--------KSDMEKLAKATGAK 328
Cdd:TIGR02348 226 SNIKDLL--------PLLEKVAQSGKPLLIIAEDVEGEALATLVvnkLRGTLNVCAVKapgfgdrrKAMLEDIAILTGGQ 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 329 IVTD-----LDDLTPSVLGEAETVeerKIGDDRMTFVMGCKNPKAVS--------------------------------- 370
Cdd:TIGR02348 298 VISEelglkLEEVTLDDLGKAKKV---TVDKDNTTIVEGAGDKAAIKarvaqikaqieettsdydreklqerlaklaggv 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 371 --ILIRGGTDHVVSEVERALNDAIRVVAITKEDGkFLWGGGAVEAELAMRLAKyANSVGGREQLAIEAFAKALEIIPRTL 448
Cdd:TIGR02348 375 avIKVGAATETEMKEKKLRIEDALNATRAAVEEG-IVPGGGVALLRAAAALEG-LKGDGEDEAIGIDIVKRALEAPLRQI 452
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4699707 449 AENAGIDPINTLIKLKADDEkgriSVGVDLDNNGVGDMKAKGVVDPLRVKTHALESAVEVATMILRIDDVIASKK 523
Cdd:TIGR02348 453 AENAGLDGAVVAEKVKELKG----NFGFNAATGEYEDLVEAGIIDPTKVTRSALQNAASIAGLLLTTEAVVADKP 523
|
|
| groEL |
PRK12851 |
chaperonin GroEL; Reviewed |
23-522 |
8.88e-25 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 171770 Cd Length: 541 Bit Score: 107.91 E-value: 8.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 23 AQRNNIEAAKAIADAVRTTLGPKGMDKMLVDSIGDIIISNDGATILKEMDVEHP----TAKMIVEVSKAQDTAVGDGTTT 98
Cdd:PRK12851 12 AREKMLRGVNILADAVKVTLGPKGRNVVIDKSFGAPTITNDGVTIAKEIELEDKfenmGAQMVREVASKTNDVAGDGTTT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 99 AVVLSGELLKQAETLLDQGVHPTVISNGYRLAVNEARKIIDEIAEKSTDDATLRKIAltALSGKNTGLSNDFLADLVVKA 178
Cdd:PRK12851 92 ATVLAQAIVREGAKAVAAGANPMDLKRGIDRAVAAVVEELKANARPVTTNAEIAQVA--TISANGDAEIGRLVAEAMEKV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 179 VN-AVAEVRDGKTIVDTANIkvdkknggsVNDTQFISG-----IVIDKEKVHSKMPD---VVKNAKIALIDSALEIkkte 249
Cdd:PRK12851 170 GNeGVITVEESKTAETELEV---------VEGMQFDRGylspyFVTDADKMEAELEDpyiLIHEKKISNLQDLLPV---- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 250 IEAKVQISDPSKI--QDFLNQETNTFkqMVEKIKKSGANVVLCQKGIDDvaqhylakegiyavRRvkKSDMEKLAKATGA 327
Cdd:PRK12851 237 LEAVVQSGKPLLIiaEDVEGEALATL--VVNKLRGGLKVAAVKAPGFGD--------------RR--KAMLEDIAILTGG 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 328 KIVTD-----LDDLTPSVLGEAETVEERKigdDRMTFVMGCKNPKAvsilIRGGTDHVVSEVERALND------------ 390
Cdd:PRK12851 299 TVISEdlgikLENVTLEQLGRAKKVVVEK---ENTTIIDGAGSKTE----IEGRVAQIRAQIEETTSDydreklqerlak 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 391 ------AIRVVAITKEDGK--------------------FLWGGG-----AVEAELAMRLAKyansvgGREQLAIEAFAK 439
Cdd:PRK12851 372 laggvaVIRVGASTEVEVKekkdrvddalhatraaveegIVPGGGvallrAVKALDKLETAN------GDQRTGVEIVRR 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 440 ALEIIPRTLAENAGIDPINTLIKLKADDEkgriSVGVDLDNNGVGDMKAKGVVDPLRVKTHALESAVEVATMILRIDDVI 519
Cdd:PRK12851 446 ALEAPVRQIAENAGAEGSVVVGKLREKPG----GYGFNAATNEYGDLYAQGVIDPVKVVRTALQNAASVAGLLLTTEAMV 521
|
...
gi 4699707 520 ASK 522
Cdd:PRK12851 522 AEK 524
|
|
| groEL |
CHL00093 |
chaperonin GroEL |
34-525 |
4.30e-23 |
|
chaperonin GroEL
Pssm-ID: 177025 Cd Length: 529 Bit Score: 102.88 E-value: 4.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 34 IADAVRTTLGPKGMDKMLVDSIGDIIISNDGATILKEMDVEHPTAKMIVEV-----SKAQDTAvGDGTTTAVVLSGELLK 108
Cdd:CHL00093 22 LAEAVSVTLGPKGRNVVLEKKYGSPQIVNDGVTIAKEIELEDHIENTGVALirqaaSKTNDVA-GDGTTTATVLAYAIVK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 109 QAETLLDQGVHPTVISNGYRLAVNEARKIIDEIAEKSTDDATLRKIAltALSGKNTGLSNDFLADLVVK-AVNAVAEVRD 187
Cdd:CHL00093 101 QGMKNVAAGANPISLKRGIEKATQYVVSQIAEYARPVEDIQAITQVA--SISAGNDEEVGSMIADAIEKvGREGVISLEE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 188 GKTIVD----TANIKVDKKnggsvndtqFISG-IVIDKEkvhsKMPDVVKNAKIALIDSALEIKKTEIeakVQIsdpski 262
Cdd:CHL00093 179 GKSTVTeleiTEGMRFEKG---------FISPyFVTDTE----RMEVVQENPYILLTDKKITLVQQDL---LPI------ 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 263 qdfLNQETNTFKQMV---EKIKKSG-ANVVLCQ-KGIDDVAqhylakegiyAVR-----RVKKSDMEKLAKATGAKIVTD 332
Cdd:CHL00093 237 ---LEQVTKTKRPLLiiaEDVEKEAlATLVLNKlRGIVNVV----------AVRapgfgDRRKAMLEDIAILTGGQVITE 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 333 -----LDDLTPSVLGEAETVEerkIGDDRMTFVmGCKNPKAVSI---------------------------------LIR 374
Cdd:CHL00093 304 daglsLETIQLDLLGQARRII---VTKDSTTII-ADGNEEQVKArceqlrkqieiadssyekeklqerlaklsggvaVIK 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 375 GG--TDHVVSEVERALNDAIRVVAITKEDGkFLWGGGAVEAELAMRLAKYA-NSVGGREQLAIEAFAKALEIIPRTLAEN 451
Cdd:CHL00093 380 VGaaTETEMKDKKLRLEDAINATKAAVEEG-IVPGGGATLVHLSENLKTWAkNNLKEDELIGALIVARAILAPLKRIAEN 458
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4699707 452 AGIDPINTLIKLKADDekgrISVGVDLDNNGVGDMKAKGVVDPLRVKTHALESAVEVATMILRIDDVIASKKST 525
Cdd:CHL00093 459 AGKNGSVIIEKVQEQD----FEIGYNAANNKFVNMYEAGIIDPAKVTRSALQNAASIASMILTTECIIVDKKES 528
|
|
| groEL |
PRK12852 |
chaperonin GroEL; Reviewed |
34-528 |
3.11e-21 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237232 Cd Length: 545 Bit Score: 97.22 E-value: 3.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 34 IADAVRTTLGPKGMDKMLVDSIGDIIISNDGATILKEMDV----EHPTAKMIVEV-SKAQDTAvGDGTTTAVVLSGELLK 108
Cdd:PRK12852 23 LANAVKVTLGPKGRNVVIEKSFGAPRITKDGVTVAKEIELedkfENMGAQMVREVaSKTNDLA-GDGTTTATVLAQAIVR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 109 QAETLLDQGVHPTVISNGYRLAVNearKIIDEIAEKSTDDATLRKIA-LTALSGKNTGLSNDFLADLVVKAVN-AVAEVR 186
Cdd:PRK12852 102 EGAKAVAAGMNPMDLKRGIDIAVA---AVVKDIEKRAKPVASSAEIAqVGTISANGDAAIGKMIAQAMQKVGNeGVITVE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 187 DGKtivdTANIKVDKKNGGSVNDTQFISGIVIDKEKVHSKMPDV---VKNAKIALIDSALEIkkteIEAKVQISDPSKI- 262
Cdd:PRK12852 179 ENK----SLETEVDIVEGMKFDRGYLSPYFVTNAEKMTVELDDAyilLHEKKLSGLQAMLPV----LEAVVQSGKPLLIi 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 263 -QDFLNQETNTFkqmvekikksganVVLCQKGIDDVAQhylAKEGIYAVRRvkKSDMEKLAKATGAKIVTD-----LDDL 336
Cdd:PRK12852 251 aEDVEGEALATL-------------VVNRLRGGLKVAA---VKAPGFGDRR--KAMLEDIAILTGGQLISEdlgikLENV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 337 TPSVLGEAETVEerkIGDDRMTFVMGCKNPKAVS-----------------------------------ILIRGGTDHVV 381
Cdd:PRK12852 313 TLKMLGRAKKVV---IDKENTTIVNGAGKKADIEarvgqikaqieettsdydreklqerlaklaggvavIRVGGATEVEV 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 382 SEVERALNDAIRVVAITKEDGKFLWGGGAVeaelaMRLAKYANSVGGR---EQLAIEAFAKALEIIPRTLAENAGIDPin 458
Cdd:PRK12852 390 KEKKDRVEDALNATRAAVQEGIVPGGGVAL-----LRAKKAVGRINNDnadVQAGINIVLKALEAPIRQIAENAGVEG-- 462
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4699707 459 TLIKLKADDEKGRiSVGVDLDNNGVGDMKAKGVVDPLRVKTHALESAVEVATMILRIDDVIAS--KKSTPPS 528
Cdd:PRK12852 463 SIVVGKILENKSE-TFGFDAQTEEYVDMVAKGIIDPAKVVRTALQDAASVAGLLVTTEAMVAElpKKDAAPA 533
|
|
| PRK14104 |
PRK14104 |
chaperonin GroEL; Provisional |
20-520 |
6.37e-19 |
|
chaperonin GroEL; Provisional
Pssm-ID: 172594 Cd Length: 546 Bit Score: 90.09 E-value: 6.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 20 GKNAQRNNIEAAKAIADAVRTTLGPKGMDKMLVDSIGDIIISNDGATILKEMDV----EHPTAKMIVEVSKAQDTAVGDG 95
Cdd:PRK14104 9 GVDARDRMLRGVDILANAVKVTLGPKGRNVVLDKSFGAPRITKDGVTVAKEIELedkfENMGAQMVREVASKSADAAGDG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 96 TTTAVVLSGELLKQAETLLDQGVHPTVISNGYRLAVNEARKIIDEIAEKSTDDATLRKIALTALSGKNTglSNDFLADLV 175
Cdd:PRK14104 89 TTTATVLAQAIVREGAKSVAAGMNPMDLKRGIDLAVEAVVADLVKNSKKVTSNDEIAQVGTISANGDAE--IGKFLADAM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 176 VKAVN-AVAEVRDGKTIvdtaNIKVDKKNGGSVNDTQFISGIVIDKEKVHSKMPD---VVKNAKIALIDSALEIkkteIE 251
Cdd:PRK14104 167 KKVGNeGVITVEEAKSL----ETELDVVEGMQFDRGYISPYFVTNADKMRVEMDDayiLINEKKLSSLNELLPL----LE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 252 AKVQISDPSKI--QDFLNQETNTFkqMVEKIKKSGANVVLCQKGIDDvaqhylakegiyavRRvkKSDMEKLAKATGAKI 329
Cdd:PRK14104 239 AVVQTGKPLVIvaEDVEGEALATL--VVNRLRGGLKVAAVKAPGFGD--------------RR--KAMLQDIAILTGGQA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 330 VTD-----LDDLTPSVLGEAETVeerKIGDDRMTFVMGCKNPKAVS---------------------------------- 370
Cdd:PRK14104 301 ISEdlgikLENVTLQMLGRAKKV---MIDKENTTIVNGAGKKADIEarvaqikaqieettsdydreklqerlaklaggva 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 371 -ILIRGGTDHVVSEVERALNDAIRVVAITKEDGkfLWGGGAVEAELAMRLAKYANSVGGREQLAIEAFAKALEIIPRTLA 449
Cdd:PRK14104 378 vIRVGGATEVEVKERKDRVDDAMHATRAAVEEG--IVPGGGVALLRASEQLKGIKTKNDDQKTGVEIVRKALSAPARQIA 455
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4699707 450 ENAGIDPINTLIKLKaddEKGRISVGVDLDNNGVGDMKAKGVVDPLRVKTHALESAVEVATMILRIDDVIA 520
Cdd:PRK14104 456 INAGEDGSVIVGKIL---EKEQYSYGFDSQTGEYGNLVSKGIIDPTKVVRTAIQNAASVAALLITTEAMVA 523
|
|
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
20-523 |
2.05e-18 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 88.26 E-value: 2.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 20 GKNAQRNNIEAAKAIADAVRTTLGPKGMDKMLVDSIGDIIISNDGATILKEMDVEHPT----AKMIVEV-SKAQDTAvGD 94
Cdd:PRK00013 8 GEDARRKLLRGVNKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDPFenmgAQLVKEVaSKTNDVA-GD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 95 GTTTAVVLSGELLKQAETLLDQGVHPTVISNGYRLAVNearKIIDEIAEKSTDDATLRKIALTALSGKNtglSNDFLADL 174
Cdd:PRK00013 87 GTTTATVLAQAIVREGLKNVAAGANPMDLKRGIDKAVE---AAVEELKKISKPVEDKEEIAQVATISAN---GDEEIGKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 175 VVKAVNAVAE-----VRDGKTIVDTANIkvdkknggsVNDTQFISG-----IVIDKEkvhsKMPDVVKNAKIALIDsale 244
Cdd:PRK00013 161 IAEAMEKVGKegvitVEESKGFETELEV---------VEGMQFDRGylspyFVTDPE----KMEAELENPYILITD---- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 245 iKKTeieakvqisdpSKIQDFLnqetntfkQMVEKIKKSGANVVLcqkgI-DDVAQHYLAK------EGIYAVRRVK--- 314
Cdd:PRK00013 224 -KKI-----------SNIQDLL--------PVLEQVAQSGKPLLI----IaEDVEGEALATlvvnklRGTLKVVAVKapg 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 315 -----KSDMEKLAKATGAKIVTD-----LDDLTPSVLGEAETVeerKIGDDRMTFVMGCKNPKAVSI---LIRGGTDHVV 381
Cdd:PRK00013 280 fgdrrKAMLEDIAILTGGTVISEelglkLEDATLEDLGQAKKV---VVTKDNTTIVDGAGDKEAIKArvaQIKAQIEETT 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 382 SE------------------------------------VERALNDAIRVVaitkEDGkFLWGGGAVEAELAMRLAKyANS 425
Cdd:PRK00013 357 SDydreklqerlaklaggvavikvgaatevemkekkdrVEDALHATRAAV----EEG-IVPGGGVALLRAAPALEA-LKG 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 426 VGGREQLAIEAFAKALEIIPRTLAENAGIDPINTLIKLKADDEKGrisVGVDLDNNGVGDMKAKGVVDPLRVKTHALESA 505
Cdd:PRK00013 431 LNGDEATGINIVLRALEAPLRQIAENAGLEGSVVVEKVKNGKGKG---YGYNAATGEYVDMIEAGIIDPTKVTRSALQNA 507
|
570
....*....|....*...
gi 4699707 506 VEVATMILRIDDVIASKK 523
Cdd:PRK00013 508 ASVAGLLLTTEAVVADKP 525
|
|
| PLN03167 |
PLN03167 |
Chaperonin-60 beta subunit; Provisional |
34-527 |
5.36e-14 |
|
Chaperonin-60 beta subunit; Provisional
Pssm-ID: 215611 [Multi-domain] Cd Length: 600 Bit Score: 74.58 E-value: 5.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 34 IADAVRTTLGPKGMDKMLVDSIGDIIISNDGATILKEMDVEHPT----AKMIVEVSKAQDTAVGDGTTTAVVLSGELLKQ 109
Cdd:PLN03167 78 LADLVGVTLGPKGRNVVLESKYGSPKIVNDGVTVAKEVELEDPVenigAKLVRQAAAKTNDLAGDGTTTSVVLAQGLIAE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 110 AETLLDQGVHPTVISNGYRlavNEARKIIDEIAE--KSTDDATLRKIAltALSGKNtglsNDFLADLVVKAVNAVAEvrd 187
Cdd:PLN03167 158 GVKVVAAGANPVQITRGIE---KTAKALVKELKKmsKEVEDSELADVA--AVSAGN----NYEVGNMIAEAMSKVGR--- 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 188 gKTIVDTANIKVDKKNGGSVNDTQFISG-----IVIDKEkvhsKMPDVVKNAKIALIDSALEIKKTEI---EAKVQISDP 259
Cdd:PLN03167 226 -KGVVTLEEGKSAENNLYVVEGMQFDRGyispyFVTDSE----KMSVEYDNCKLLLVDKKITNARDLIgilEDAIRGGYP 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 260 SKI--QDFLNQETNTFkqMVEKIKKSGANVVLCQKGIDDVAQHYLAKEGIYAVRRVKKSD----MEKLAK---ATGAKIV 330
Cdd:PLN03167 301 LLIiaEDIEQEALATL--VVNKLRGSLKIAALKAPGFGERKSQYLDDIAILTGGTVIREEvglsLDKVGKevlGTAAKVV 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 331 TDLDdlTPSVLGEAETVE--------------------ERKIGDDRMTFVMGcknpkAVSILIRGG-TDHVVSEVERALN 389
Cdd:PLN03167 379 LTKD--TTTIVGDGSTQEavnkrvaqiknlieaaeqdyEKEKLNERIAKLSG-----GVAVIQVGAqTETELKEKKLRVE 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699707 390 DAIRVVAITKEDGkFLWGGGAVEAELAMRLAKYANSVGGREQ-LAIEAFAKALEIIPRTLAENAGIDPINTLIKLKADDE 468
Cdd:PLN03167 452 DALNATKAAVEEG-IVVGGGCTLLRLASKVDAIKDTLENDEQkVGADIVKRALSYPLKLIAKNAGVNGSVVSEKVLSNDN 530
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 4699707 469 kgrISVGVDLDNNGVGDMKAKGVVDPLRVKTHALESAVEVATMILRIDDVIASKKSTPP 527
Cdd:PLN03167 531 ---PKFGYNAATGKYEDLMAAGIIDPTKVVRCCLEHAASVAKTFLTSDCVVVEIKEPEP 586
|
|
| |
