|
Name |
Accession |
Description |
Interval |
E-value |
| thermosome_beta |
NF041083 |
thermosome subunit beta; |
7-525 |
0e+00 |
|
thermosome subunit beta;
Pssm-ID: 469010 Cd Length: 519 Bit Score: 910.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 7 QPVVILPEGTQRYVGRDAQRLNILAARIIAETVRTTLGPKGMDKMLVDSLGDIVVTNDCATILDKIDLQHPAAKMMVEVA 86
Cdd:NF041083 1 QPVLILKEGTQRTKGRDAQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDIVITNDGATILKEMDVQHPAAKMLVEVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 87 KTQDKEAGDGTTTAVVIAGELLRKAEELLDQNIHPSIITKGYALAAEKAQEILDEIAIRVDPDDEETLLKIAATSITGKN 166
Cdd:NF041083 81 KTQDDEVGDGTTTAVVLAGELLKKAEELLDQNIHPTIIANGYRLAAEKAIEILDEIAEKVDPDDRETLKKIAETSLTSKG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 167 AESHKELLAKLAVEAVKQVAEKKDGKYVVDLDNIKFEKKAGEGVEESELVRGVVIDKEVVHPRMPKRVENAKIALINEAL 246
Cdd:NF041083 161 VEEARDYLAEIAVKAVKQVAEKRDGKYYVDLDNIQIEKKHGGSIEDTQLIYGIVIDKEVVHPGMPKRVENAKIALLDAPL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 247 EVKKTETDAKINITSPDQLMSFLEQEEKMLKDMVDHIAQTGANVVFVQKGIDDLAQHYLAKYGIMAVRRVKKSDMEKLAK 326
Cdd:NF041083 241 EVKKTEIDAEIRITDPDQLQKFLDQEEKMLKEMVDKIKATGANVVFCQKGIDDLAQHYLAKAGILAVRRVKKSDMEKLAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 327 ATGAKIVTNVKDLTPEDLGYAEVVEERKLAGENMIFVEGCKNPKAVTILIRGGTEHVIDEVERALEDAVKVVKDVMEDGA 406
Cdd:NF041083 321 ATGARIVTNIDDLTPEDLGYAELVEERKVGDDKMVFVEGCKNPKAVTILIRGGTEHVVDEAERALEDALSVVADAVEDGK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 407 VLPAGGAPEIELAIRLDEYAKQVGGKEALAIENFADALKIIPKTLAENAGLDTVEMLVKVISEHKNRGLGIGIDVFEGKP 486
Cdd:NF041083 401 IVAGGGAPEVELAKRLREYAATVGGREQLAVEAFAEALEIIPRTLAENAGLDPIDILVKLRSAHEKGKKWAGINVFTGEV 480
|
490 500 510
....*....|....*....|....*....|....*....
1Q2V_B 487 ADMLEKGIIEPLRVKKQAIKSASEAAIMILRIDDVIAAK 525
Cdd:NF041083 481 VDMWELGVIEPLRVKTQAIKSATEAATMILRIDDVIAAK 519
|
|
| thermosome_alpha |
NF041082 |
thermosome subunit alpha; |
7-525 |
0e+00 |
|
thermosome subunit alpha;
Pssm-ID: 469009 Cd Length: 518 Bit Score: 901.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 7 QPVVILPEGTQRYVGRDAQRLNILAARIIAETVRTTLGPKGMDKMLVDSLGDIVVTNDCATILDKIDLQHPAAKMMVEVA 86
Cdd:NF041082 1 QPILILKEGTQRTSGRDAQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDVVITNDGVTILKEMDIEHPAAKMIVEVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 87 KTQDKEAGDGTTTAVVIAGELLRKAEELLDQNIHPSIITKGYALAAEKAQEILDEIAIRVDPDDEETLLKIAATSITGKN 166
Cdd:NF041082 81 KTQDDEVGDGTTTAVVLAGELLKKAEELLDQDIHPTIIAEGYRLAAEKALEILDEIAIKVDPDDKETLKKIAATAMTGKG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 167 AESHKELLAKLAVEAVKQVAEKkDGKYVVDLDNIKFEKKAGEGVEESELVRGVVIDKEVVHPRMPKRVENAKIALINEAL 246
Cdd:NF041082 161 AEAAKDKLADLVVDAVKAVAEK-DGGYNVDLDNIKVEKKVGGSIEDSELVEGVVIDKERVHPGMPKRVENAKIALLDAPL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 247 EVKKTETDAKINITSPDQLMSFLEQEEKMLKDMVDHIAQTGANVVFVQKGIDDLAQHYLAKYGIMAVRRVKKSDMEKLAK 326
Cdd:NF041082 240 EVKKTEIDAKISITDPDQLQAFLDQEEKMLKEMVDKIADSGANVVFCQKGIDDLAQHYLAKEGILAVRRVKKSDMEKLAK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 327 ATGAKIVTNVKDLTPEDLGYAEVVEERKLAGENMIFVEGCKNPKAVTILIRGGTEHVIDEVERALEDAVKVVKDVMEDGA 406
Cdd:NF041082 320 ATGARIVTSIDDLSPEDLGYAGLVEERKVGGDKMIFVEGCKNPKAVTILLRGGTEHVVDEVERALEDALRVVRVVLEDGK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 407 VLPAGGAPEIELAIRLDEYAKQVGGKEALAIENFADALKIIPKTLAENAGLDTVEMLVKVISEHKNRGLGIGIDVFEGKP 486
Cdd:NF041082 400 VVAGGGAPEVELALRLREYAASVGGREQLAIEAFAEALEIIPRTLAENAGLDPIDALVELRSAHEKGNKTAGLDVYTGKV 479
|
490 500 510
....*....|....*....|....*....|....*....
1Q2V_B 487 ADMLEKGIIEPLRVKKQAIKSASEAAIMILRIDDVIAAK 525
Cdd:NF041082 480 VDMLEIGVVEPLRVKTQAIKSATEAAVMILRIDDVIAAA 518
|
|
| cpn60 |
cd03343 |
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ... |
9-525 |
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: 880.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 9 VVILPEGTQRYVGRDAQRLNILAARIIAETVRTTLGPKGMDKMLVDSLGDIVVTNDCATILDKIDLQHPAAKMMVEVAKT 88
Cdd:cd03343 1 VLILKEGTQRTSGRDAQRMNIAAAKAVAEAVRTTLGPKGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 89 QDKEAGDGTTTAVVIAGELLRKAEELLDQNIHPSIITKGYALAAEKAQEILDEIAIRVDPDDEETLLKIAATSITGKNAE 168
Cdd:cd03343 81 QDEEVGDGTTTAVVLAGELLEKAEDLLDQNIHPTVIIEGYRLAAEKALELLDEIAIKVDPDDKDTLRKIAKTSLTGKGAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 169 SHKELLAKLAVEAVKQVAEKKDGKYVVDLDNIKFEKKAGEGVEESELVRGVVIDKEVVHPRMPKRVENAKIALINEALEV 248
Cdd:cd03343 161 AAKDKLADLVVDAVLQVAEKRDGKYVVDLDNIKIEKKTGGSVDDTELIRGIVIDKEVVHPGMPKRVENAKIALLDAPLEV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 249 KKTETDAKINITSPDQLMSFLEQEEKMLKDMVDHIAQTGANVVFVQKGIDDLAQHYLAKYGIMAVRRVKKSDMEKLAKAT 328
Cdd:cd03343 241 KKTEIDAKIRITSPDQLQAFLEQEEAMLKEMVDKIADTGANVVFCQKGIDDLAQHYLAKAGILAVRRVKKSDMEKLARAT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 329 GAKIVTNVKDLTPEDLGYAEVVEERKLAGENMIFVEGCKNPKAVTILIRGGTEHVIDEVERALEDAVKVVKDVMEDGAVL 408
Cdd:cd03343 321 GAKIVTNIDDLTPEDLGEAELVEERKVGDDKMVFVEGCKNPKAVTILLRGGTEHVVDELERALEDALRVVADALEDGKVV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 409 PAGGAPEIELAIRLDEYAKQVGGKEALAIENFADALKIIPKTLAENAGLDTVEMLVKVISEHKNRGLGIGIDVFEGKPAD 488
Cdd:cd03343 401 AGGGAVEIELAKRLREYARSVGGREQLAVEAFADALEEIPRTLAENAGLDPIDTLVELRAAHEKGNKNAGLDVYTGEVVD 480
|
490 500 510
....*....|....*....|....*....|....*..
1Q2V_B 489 MLEKGIIEPLRVKKQAIKSASEAAIMILRIDDVIAAK 525
Cdd:cd03343 481 MLEKGVIEPLRVKKQAIKSATEAATMILRIDDVIAAK 517
|
|
| thermosome_arch |
TIGR02339 |
thermosome, various subunits, archaeal; Thermosome is the name given to the archaeal rather ... |
8-524 |
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: 765.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 8 PVVILPEGTQRYVGRDAQRLNILAARIIAETVRTTLGPKGMDKMLVDSLGDIVVTNDCATILDKIDLQHPAAKMMVEVAK 87
Cdd:TIGR02339 1 PVFILKEGTQRTSGRDAQRNNIAAAKAVAEAVKSTLGPRGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 88 TQDKEAGDGTTTAVVIAGELLRKAEELLDQNIHPSIITKGYALAAEKAQEILDEIAIRVDPDDEETLLKIAATSITGK-N 166
Cdd:TIGR02339 81 TQDEEVGDGTTTAVVLAGELLEKAEDLLEQDIHPTVIIEGYRKAAEKALEIIDEIATKISPEDRDLLKKIAYTSLTSKaS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 167 AESHKELLAKLAVEAVKQVAEKK-DGKYVVDLDNIKFEKKAGEGVEESELVRGVVIDKEVVHPRMPKRVENAKIALINEA 245
Cdd:TIGR02339 161 AEVAKDKLADLVVEAVKQVAELRgDGKYYVDLDNIKIVKKKGGSIEDTELVEGIVVDKEVVHPGMPKRVENAKIALLDAP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 246 LEVKKTETDAKINITSPDQLMSFLEQEEKMLKDMVDHIAQTGANVVFVQKGIDDLAQHYLAKYGIMAVRRVKKSDMEKLA 325
Cdd:TIGR02339 241 LEVEKTEIDAKIRITDPDQIKKFLDQEEAMLKEMVDKIASAGANVVICQKGIDDVAQHYLAKAGILAVRRVKKSDIEKLA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 326 KATGAKIVTNVKDLTPEDLGYAEVVEERKLAGENMIFVEGCKNPKAVTILIRGGTEHVIDEVERALEDAVKVVKDVMEDG 405
Cdd:TIGR02339 321 RATGARIVSSIDEITESDLGYAELVEERKVGEDKMVFVEGCKNPKAVTILLRGGTEHVVDELERSIQDALHVVANALEDG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 406 AVLPAGGAPEIELAIRLDEYAKQVGGKEALAIENFADALKIIPKTLAENAGLDTVEMLVKVISEHKNRGLGIGIDVFEGK 485
Cdd:TIGR02339 401 KIVAGGGAVEIELALRLRSYARSVGGREQLAIEAFADALEEIPRILAENAGLDPIDALVDLRAKHEKGNKNAGINVFTGE 480
|
490 500 510
....*....|....*....|....*....|....*....
1Q2V_B 486 PADMLEKGIIEPLRVKKQAIKSASEAAIMILRIDDVIAA 524
Cdd:TIGR02339 481 IEDMLELGVIEPLRVKEQAIKSATEAATMILRIDDVIAA 519
|
|
| Cpn60_TCP1 |
pfam00118 |
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ... |
35-525 |
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: 626.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 35 IAETVRTTLGPKGMDKMLVDSLGDIVVTNDCATILDKIDLQHPAAKMMVEVAKTQDKEAGDGTTTAVVIAGELLRKAEEL 114
Cdd:pfam00118 1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELEIQHPAAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEEAEKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 115 LDQNIHPSIITKGYALAAEKAQEILDEI-AIRVDPDDEETLLKIAATSITGKNAESHKELLAKLAVEAVKQVAEKKdgkY 193
Cdd:pfam00118 81 LAAGVHPTTIIEGYEKALEKALEILDSIiSIPVEDVDREDLLKVARTSLSSKIISRESDFLAKLVVDAVLAIPKND---G 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 194 VVDLDNIKFEKKAGEGVEESELVRGVVIDKEVVHPRMPKRVENAKIALINEALEVKKTETDAKINITSPDQLMSFLEQEE 273
Cdd:pfam00118 158 SFDLGNIGVVKILGGSLEDSELVDGVVLDKGPLHPDMPKRLENAKVLLLNCSLEYEKTETKATVVLSDAEQLERFLKAEE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 274 KMLKDMVDHIAQTGANVVFVQKGIDDLAQHYLAKYGIMAVRRVKKSDMEKLAKATGAKIVTNVKDLTPEDLGYAEVVEER 353
Cdd:pfam00118 238 EQILEIVEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMALRRVKKRDLERLAKATGARAVSSLDDLTPDDLGTAGKVEEE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 354 KLAGENMIFVEGCKNPKAVTILIRGGTEHVIDEVERALEDAVKVVKDVMEDGAVLPAGGAPEIELAIRLDEYAKQVGGKE 433
Cdd:pfam00118 318 KIGDEKYTFIEGCKSPKAATILLRGATDHVLDEIERSIHDALCVVKNAIEDPRVVPGGGAVEMELARALREYAKSVSGKE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 434 ALAIENFADALKIIPKTLAENAGLDTVEMLVKVISEHKNRGLGIGIDVFEGKPADMLEKGIIEPLRVKKQAIKSASEAAI 513
Cdd:pfam00118 398 QLAIEAFAEALEVIPKTLAENAGLDPIEVLAELRAAHASGEKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKSATEAAS 477
|
490
....*....|..
1Q2V_B 514 MILRIDDVIAAK 525
Cdd:pfam00118 478 TILRIDDIIKAK 489
|
|
| chaperonin_type_I_II |
cd00309 |
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ... |
16-523 |
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: 625.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 16 TQRYVGRDAQRLNILAARIIAETVRTTLGPKGMDKMLVDSLGDIVVTNDCATILDKIDLQHPAAKMMVEVAKTQDKEAGD 95
Cdd:cd00309 1 KEREFGEEARLSNINAAKALADAVKTTLGPKGMDKMLVDSLGDPTITNDGATILKEIEVEHPAAKLLVEVAKSQDDEVGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 96 GTTTAVVIAGELLRKAEELLDQNIHPSIITKGYALAAEKAQEILDEIAIRVDPDDEETLLKIAATSITGKNAESHKELLA 175
Cdd:cd00309 81 GTTTVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVPIDVEDREELLKVATTSLNSKLVSGGDDFLG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 176 KLAVEAVKQVAEKKDgkyVVDLDNIKFEKKAGEGVEESELVRGVVIDKEVVHPRMPKRVENAKIALINEALEvkktetda 255
Cdd:cd00309 161 ELVVDAVLKVGKENG---DVDLGVIRVEKKKGGSLEDSELVVGMVFDKGYLSPYMPKRLENAKILLLDCKLE-------- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 256 kinitspdqlmsfleqeekmlkdmvdhiaqtgaNVVFVQKGIDDLAQHYLAKYGIMAVRRVKKSDMEKLAKATGAKIVTN 335
Cdd:cd00309 230 ---------------------------------YVVIAEKGIDDEALHYLAKLGIMAVRRVRKEDLERIAKATGATIVSR 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 336 VKDLTPEDLGYAEVVEERKLAGENMIFVEGCKNPKAVTILIRGGTEHVIDEVERALEDAVKVVKDVMEDGAVLPAGGAPE 415
Cdd:cd00309 277 LEDLTPEDLGTAGLVEETKIGDEKYTFIEGCKGGKVATILLRGATEVELDEAERSLHDALCAVRAAVEDGGIVPGGGAAE 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 416 IELAIRLDEYAKQVGGKEALAIENFADALKIIPKTLAENAGLDTVEMLVKVISEHKNRGLGIGIDVFEGKPADMLEKGII 495
Cdd:cd00309 357 IELSKALEELAKTLPGKEQLGIEAFADALEVIPRTLAENAGLDPIEVVTKLRAKHAEGGGNAGGDVETGEIVDMKEAGII 436
|
490 500
....*....|....*....|....*...
1Q2V_B 496 EPLRVKKQAIKSASEAAIMILRIDDVIA 523
Cdd:cd00309 437 DPLKVKRQALKSATEAASLILTIDDIIV 464
|
|
| GroEL |
COG0459 |
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ... |
21-530 |
0e+00 |
|
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227 Cd Length: 497 Bit Score: 532.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 21 GRDAQRLNILAARIIAETVRTTLGPKGMDKMLVDSLGDIVVTNDCATILDKIDLQHP----AAKMMVEVAKTQDKEAGDG 96
Cdd:COG0459 8 GEDARRANIRGVKALADAVKVTLGPKGRNVMLVKSFGDPTITNDGVTIAKEIELEDPfenmGAQLVKEVASKTNDEAGDG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 97 TTTAVVIAGELLRKAEELLDQNIHPSIITKGYALAAEKAQEILDEIAIRVdpDDEETLLKIAATSITGknaeshKELLAK 176
Cdd:COG0459 88 TTTATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPV--DDKEELAQVATISANG------DEEIGE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 177 LAVEAVKQVAekKDGKYVVDldnikfekKAGEGVEESELVRGVVIDKEVVHP-------RMPKRVENAKIALINEALEVk 249
Cdd:COG0459 160 LIAEAMEKVG--KDGVITVE--------EGKGLETELEVVEGMQFDKGYLSPyfvtdpeKMPAELENAYILLTDKKISS- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 250 ktetdakinitspdqlmsfleqeEKMLKDMVDHIAQTGANVVFVQKGIDDLAQHYLAKYGIMAVRRV-----------KK 318
Cdd:COG0459 229 -----------------------IQDLLPLLEKVAQSGKPLLIIAEDIDGEALATLVVNGIRGVLRVvavkapgfgdrRK 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 319 SDMEKLAKATGAKIVTN-----VKDLTPEDLGYAEVVEERKlagENMIFVEGCKNPKAVTILIRGGTEHVIDEVERALED 393
Cdd:COG0459 286 AMLEDIAILTGGRVISEdlglkLEDVTLDDLGRAKRVEVDK---DNTTIVEGAGNPKAIVILVGAATEVEVKERKRRVED 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 394 AVKVVKDVMEDGaVLPAGGAPEIELAIRLDEYAKQVGGKEALAIENFADALKIIPKTLAENAGLDTVEMLVKVISEhknR 473
Cdd:COG0459 363 ALHATRAAVEEG-IVPGGGAALLRAARALRELAAKLEGDEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKVRAA---K 438
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
1Q2V_B 474 GLGIGIDVFEGKPADMLEKGIIEPLRVKKQAIKSASEAAIMILRIDDVIAAKATKPE 530
Cdd:COG0459 439 DKGFGFDAATGEYVDMLEAGVIDPAKVKRSALQNAASVAGLILTTEAVIADKPEKEE 495
|
|
| TCP1_epsilon |
cd03339 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ... |
6-523 |
1.23e-170 |
|
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: 493.35 E-value: 1.23e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 6 GQPVVILPEGTQ--RYVGRDAQRLNILAARIIAETVRTTLGPKGMDKMLVDSLGDIVVTNDCATILDKIDLQHPAAKMMV 83
Cdd:cd03339 4 GRPFIIVREQEKkkRLKGLEAHKSHILAAKSVANILRTSLGPRGMDKILVSPDGEVTVTNDGATILEKMDVDHQIAKLLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 84 EVAKTQDKEAGDGTTTAVVIAGELLRKAEELLDQNIHPSIITKGYALAAEKAQEILDEIA--IRVDPDDEETLLKIAATS 161
Cdd:cd03339 84 ELSKSQDDEIGDGTTGVVVLAGALLEQAEKLLDRGIHPIRIADGYEQACKIAVEHLEEIAdkIEFSPDNKEPLIQTAMTS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 162 ITGKNAESHKELLAKLAVEAVKQVA--EKKDgkyvVDLDNIKFEKKAGEGVEESELVRGVVIDKEVVHPRMPKRVENAKI 239
Cdd:cd03339 164 LGSKIVSRCHRQFAEIAVDAVLSVAdlERKD----VNFELIKVEGKVGGRLEDTKLVKGIVIDKDFSHPQMPKEVKDAKI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 240 ALINEALEVKKTETDAKINITSPDQLMSFLEQEEKMLKDMVDHIAQTGANVVFVQKGIDDLAQHYLAKYGIMAVRRVKKS 319
Cdd:cd03339 240 AILTCPFEPPKPKTKHKLDITSVEDYKKLQEYEQKYFREMVEQVKDAGANLVICQWGFDDEANHLLLQNGLPAVRWVGGV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 320 DMEKLAKATGAKIVTNVKDLTPEDLGYAEVVEERKLAGEN--MIFVEGCKNPKAVTILIRGGTEHVIDEVERALEDAVKV 397
Cdd:cd03339 320 EIELIAIATGGRIVPRFEDLSPEKLGKAGLVREISFGTTKdkMLVIEGCPNSKAVTIFIRGGNKMIIEEAKRSLHDALCV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 398 VKDVMEDGAVLPAGGAPEIELAIRLDEYAKQVGGKEALAIENFADALKIIPKTLAENAGLDTVEMLVKVISEH-KNRGLG 476
Cdd:cd03339 400 VRNLIRDNRIVYGGGAAEISCSLAVEKAADKCSGIEQYAMRAFADALESIPLALAENSGLNPIETLSEVKARQvKEKNPH 479
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
1Q2V_B 477 IGIDVFEGKPADMLEKGIIEPLRVKKQAIKSASEAAIMILRIDDVIA 523
Cdd:cd03339 480 LGIDCLGRGTNDMKEQKVFETLISKKQQILLATQVVKMILKIDDVIV 526
|
|
| TCP1_delta |
cd03338 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ... |
28-524 |
1.38e-167 |
|
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: 485.25 E-value: 1.38e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 28 NILAARIIAETVRTTLGPKGMDKMLVDSLGDIVVTNDCATILDKIDLQHPAAKMMVEVAKTQDKEAGDGTTTAVVIAGEL 107
Cdd:cd03338 13 NIQAAKAVADAIRTSLGPRGMDKMIQTGKGEVIITNDGATILKQMSVLHPAAKMLVELSKAQDIEAGDGTTSVVVLAGAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 108 LRKAEELLDQNIHPSIITKGYALAAEKAQEILDEIAIRVDPDDEETLLKIAATSITGKNAESHKELLAKLAVEAVKQVAE 187
Cdd:cd03338 93 LSACESLLKKGIHPTVISESFQIAAKKAVEILDSMSIPVDLNDRESLIKSATTSLNSKVVSQYSSLLAPIAVDAVLKVID 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 188 KKDGKYvVDLDNIKFEKKAGEGVEESELVRGVVIDKEVVH-PRMPKRVENAKIALINEALEVKKTETDAKINITSPDQLM 266
Cdd:cd03338 173 PATATN-VDLKDIRIVKKLGGTIEDTELVDGLVFTQKASKkAGGPTRIEKAKIGLIQFCLSPPKTDMDNNIVVNDYAQMD 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 267 SFLEQEEKMLKDMVDHIAQTGANVVFVQKGI-----DDLAQHYLAKYGIMAVRRVKKSDMEKLAKATGAKIVTNVKDLTP 341
Cdd:cd03338 252 RILREERKYILNMCKKIKKSGCNVLLIQKSIlrdavSDLALHFLAKLKIMVVKDIEREEIEFICKTIGCKPVASIDHFTE 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 342 EDLGYAEVVEERKLAGENMIFVEGCKNP-KAVTILIRGGTEHVIDEVERALEDAVKVVKDVMEDGAVLPAGGAPEIELAI 420
Cdd:cd03338 332 DKLGSADLVEEVSLGDGKIVKITGVKNPgKTVTILVRGSNKLVLDEAERSLHDALCVIRCLVKKRALIPGGGAPEIEIAL 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 421 RLDEYAKQVGGKEALAIENFADALKIIPKTLAENAGLDTVEMLVKVISEHKNRGLGIGIDVFEGKPADMLEKGIIEPLRV 500
Cdd:cd03338 412 QLSEWARTLTGVEQYCVRAFADALEVIPYTLAENAGLNPISIVTELRNRHAQGEKNAGINVRKGAITNILEENVVQPLLV 491
|
490 500
....*....|....*....|....
1Q2V_B 501 KKQAIKSASEAAIMILRIDDVIAA 524
Cdd:cd03338 492 STSAITLATETVRMILKIDDIVLA 515
|
|
| TCP1_gamma |
cd03337 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ... |
8-524 |
5.05e-162 |
|
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: 469.85 E-value: 5.05e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 8 PVVILPEGTQRYVGRDAQRLNILAARIIAETVRTTLGPKGMDKMLVDSLGDIVVTNDCATILDKIDLQHPAAKMMVEVAK 87
Cdd:cd03337 1 PVLVLNQNTKRESGRKAQLGNIQAAKTVADVIRTCLGPRAMLKMLLDPMGGIVLTNDGNAILREIDVAHPAAKSMIELSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 88 TQDKEAGDGTTTAVVIAGELLRKAEELLDQNIHPSIITKGYALAAEKAQEILDEIAIRVDPDDEETLLKIAATSITGKNA 167
Cdd:cd03337 81 TQDEEVGDGTTSVIILAGEILAVAEPFLERGIHPTVIIKAYRKALEDALKILEEISIPVDVNDRAQMLKIIKSCIGTKFV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 168 ESHKELLAKLAVEAVKQVA-EKKDGKYVVDLDN-IKFEKKAGEGVEESELVRGVVIDKEVVHPRMPKRVENAKIALINEA 245
Cdd:cd03337 161 SRWSDLMCNLALDAVKTVAvEENGRKKEIDIKRyAKVEKIPGGEIEDSRVLDGVMLNKDVTHPKMRRRIENPRIVLLDCP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 246 LEVkktetdakinitspdqlmsfleqeekmlkdmvdhiaqtganVVFVQKGIDDLAQHYLAKYGIMAVRRVKKSDMEKLA 325
Cdd:cd03337 241 LEY-----------------------------------------LVITEKGVSDLAQHYLVKAGITALRRVRKTDNNRIA 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 326 KATGAKIVTNVKDLTPEDLG-YAEVVEERKLAGENMIFVEGCKNPKAVTILIRGGTEHVIDEVERALEDAVKVVKDVMED 404
Cdd:cd03337 280 RACGATIVNRPEELTESDVGtGAGLFEVKKIGDEYFTFITECKDPKACTILLRGASKDVLNEVERNLQDAMAVARNIILN 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 405 GAVLPAGGAPEIELAIRLDEYAKQVGGKEALAIENFADALKIIPKTLAENAGLDTVEMLVKVISEHK-NRGLGIGIDVFE 483
Cdd:cd03337 360 PKLVPGGGATEMAVSHALSEKAKSIEGVEQWPYKAVASALEVIPRTLAQNCGANVIRTLTELRAKHAqGENSTWGIDGET 439
|
490 500 510 520
....*....|....*....|....*....|....*....|.
1Q2V_B 484 GKPADMLEKGIIEPLRVKKQAIKSASEAAIMILRIDDVIAA 524
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 ... |
8-523 |
6.87e-160 |
|
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: 465.75 E-value: 6.87e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 8 PVVILPEGTQRYVGRDAQRLNILAARIIAETVRTTLGPKGMDKMLVDSLGDIVVTNDCATILDKIDLQHPAAKMMVEVAK 87
Cdd:TIGR02344 1 PVLVLNQNTKRESGRKAQLSNIQAAKAVADIIRTCLGPRSMLKMLLDPMGGIVMTNDGNAILREIDVAHPAAKSMIELSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 88 TQDKEAGDGTTTAVVIAGELLRKAEELLDQNIHPSIITKGYALAAEKAQEILDEIAIRVDPDDEETLLKIAATSITGKNA 167
Cdd:TIGR02344 81 TQDEEVGDGTTSVIILAGEMLSVAEPFLEQNIHPTVIIRAYRKALDDALSVLEEISIPVDVNDDAAMLKLIQSCIGTKFV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 168 ESHKELLAKLAVEAVKQVAEKKDGKYVVDLDN-IKFEKKAGEGVEESELVRGVVIDKEVVHPRMPKRVENAKIALINEAL 246
Cdd:TIGR02344 161 SRWSDLMCDLALDAVRTVQRDENGRKEIDIKRyAKVEKIPGGDIEDSCVLKGVMINKDVTHPKMRRYIENPRIVLLDCPL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 247 EVKKTETDAKINITSPDQLMSFLEQEEKMLKDMVDHIAQTGANVVFVQKGIDDLAQHYLAKYGIMAVRRVKKSDMEKLAK 326
Cdd:TIGR02344 241 EYKKGESQTNIEITKEEDWNRILQMEEEYVQLMCEDIIAVKPDLVITEKGVSDLAQHYLLKANITAIRRVRKTDNNRIAR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 327 ATGAKIVTNVKDLTPEDLGY-AEVVEERKLAGENMIFVEGCKNPKAVTILIRGGTEHVIDEVERALEDAVKVVKDVMEDG 405
Cdd:TIGR02344 321 ACGATIVNRPEELRESDVGTgCGLFEVKKIGDEYFTFITECKDPKACTILLRGASKDILNEVERNLQDAMAVARNVLLDP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 406 AVLPAGGAPEIELAIRLDEYAKQVGGKEALAIENFADALKIIPKTLAENAGLDTVEMLVKVISEHKNRGL-GIGIDVFEG 484
Cdd:TIGR02344 401 KLVPGGGATEMAVSVALTEKSKKLEGVEQWPYRAVADALEIIPRTLAQNCGANVIRTLTELRAKHAQENNcTWGIDGETG 480
|
490 500 510
....*....|....*....|....*....|....*....
1Q2V_B 485 KPADMLEKGIIEPLRVKKQAIKSASEAAIMILRIDDVIA 523
Cdd:TIGR02344 481 KIVDMKEKGIWEPLAVKLQTYKTAIESACLLLRIDDIVS 519
|
|
| TCP1_alpha |
cd03335 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ... |
17-522 |
8.04e-159 |
|
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: 463.29 E-value: 8.04e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 17 QRYVGRDAQRLNILAARIIAETVRTTLGPKGMDKMLVDSLGDIVVTNDCATILDKIDLQHPAAKMMVEVAKTQDKEAGDG 96
Cdd:cd03335 2 ERTSGQDVRTQNVTAAMAIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDKEVGDG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 97 TTTAVVIAGELLRKAEELLDQNIHPSIITKGYALAAEKA-QEILDEIAIRVDPDDEETLLKIAATSITGKNAESHKELLA 175
Cdd:cd03335 82 TTSVVIIAAELLKRANELVKQKIHPTTIISGYRLACKEAvKYIKEHLSISVDNLGKESLINVAKTSMSSKIIGADSDFFA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 176 KLAVEA---VKQVAEKKDGKYVVDLDNIKfeKKAGEGVEESELVRGVVIDKEVVHPRMPKRVENAKIALINEALEVKKTE 252
Cdd:cd03335 162 NMVVDAilaVKTTNEKGKTKYPIKAVNIL--KAHGKSAKESYLVNGYALNCTRASQGMPTRVKNAKIACLDFNLQKTKMK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 253 TDAKINITSPDQLMSFLEQEEKMLKDMVDHIAQTGANVVFVQKGIDDLAQHYLAKYGIMAVRRVKKSDMEKLAKATGAKI 332
Cdd:cd03335 240 LGVQVVVTDPEKLEKIRQRESDITKERIKKILAAGANVVLTTGGIDDMCLKYFVEAGAMAVRRVKKEDLRRIAKATGATL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 333 VTNVKDLTPED------LGYAEVVEERKLAGENMIFVEGCKNPKAVTILIRGGTEHVIDEVERALEDAVKVVKDVMEDGA 406
Cdd:cd03335 320 VSTLANLEGEEtfdpsyLGEAEEVVQERIGDDELILIKGTKKRSSASIILRGANDFMLDEMERSLHDALCVVKRTLESNS 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 407 VLPAGGAPEIELAIRLDEYAKQVGGKEALAIENFADALKIIPKTLAENAGLDTVEMLVKVISEHKNRGLG--------IG 478
Cdd:cd03335 400 VVPGGGAVETALSIYLENFATTLGSREQLAIAEFAEALLVIPKTLAVNAAKDATELVAKLRAYHAAAQVKpdkkhlkwYG 479
|
490 500 510 520
....*....|....*....|....*....|....*....|....
1Q2V_B 479 IDVFEGKPADMLEKGIIEPLRVKKQAIKSASEAAIMILRIDDVI 522
Cdd:cd03335 480 LDLINGKVRDNLEAGVLEPTVSKIKSLKFATEAAITILRIDDLI 523
|
|
| chap_CCT_delta |
TIGR02342 |
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ... |
23-525 |
5.37e-152 |
|
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: 445.38 E-value: 5.37e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 23 DAQRLNILAARIIAETVRTTLGPKGMDKMLVDSLGDIVVTNDCATILDKIDLQHPAAKMMVEVAKTQDKEAGDGTTTAVV 102
Cdd:TIGR02342 9 DVRTSNIVAAKAVADAIRTSLGPKGMDKMIQDGKGEVIITNDGATILKQMAVLHPAAKMLVELSKAQDIEAGDGTTSVVI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 103 IAGELLRKAEELLDQNIHPSIITKGYALAAEKAQEILDEIAIRVDPDDEETLLKIAATSITGKNAESHKELLAKLAVEAV 182
Cdd:TIGR02342 89 LAGALLGACERLLNKGIHPTIISESFQSAADEAIKILDEMSIPVDLSDREQLLKSATTSLSSKVVSQYSSLLAPLAVDAV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 183 KQVAEKKDGKYvVDLDNIKFEKKAGEGVEESELVRGVVIDKEVVHPR-MPKRVENAKIALINEALEVKKTETDAKINITS 261
Cdd:TIGR02342 169 LKVIDPENAKN-VDLNDIKVVKKLGGTIDDTELIEGLVFTQKASKSAgGPTRIEKAKIGLIQFQISPPKTDMENQIIVND 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 262 PDQLMSFLEQEEKMLKDMVDHIAQTGANVVFVQKGI-----DDLAQHYLAKYGIMAVRRVKKSDMEKLAKATGAKIVTNV 336
Cdd:TIGR02342 248 YAQMDRVLKEERAYILNIVKKIKKTGCNVLLIQKSIlrdavNDLALHFLAKMKIMVVKDIEREEIEFICKTIGCKPIASI 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 337 KDLTPEDLGYAEVVEERKLAGENMIFVEGCKNP-KAVTILIRGGTEHVIDEVERALEDAVKVVKDVMEDGAVLPAGGAPE 415
Cdd:TIGR02342 328 DHFTADKLGSAELVEEVDSDGGKIIKITGIQNAgKTVTVVVRGSNKLVIDEAERSLHDALCVIRCLVKKRGLIAGGGAPE 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 416 IELAIRLDEYAKQVGGKEALAIENFADALKIIPKTLAENAGLDTVEMLVKVISEHKNRGLGIGIDVFEGKPADMLEKGII 495
Cdd:TIGR02342 408 IEIARRLSKYARTMKGVESYCVRAFADALEVIPYTLAENAGLNPIKVVTELRNRHANGEKTAGISVRKGGITNMLEEHVL 487
|
490 500 510
....*....|....*....|....*....|
1Q2V_B 496 EPLRVKKQAIKSASEAAIMILRIDDVIAAK 525
Cdd:TIGR02342 488 QPLLVTTSAITLASETVRSILKIDDIVFTR 517
|
|
| chap_CCT_alpha |
TIGR02340 |
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ... |
15-530 |
2.77e-151 |
|
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: 444.16 E-value: 2.77e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 15 GTQRYVGRDAQRLNILAARIIAETVRTTLGPKGMDKMLVDSLGDIVVTNDCATILDKIDLQHPAAKMMVEVAKTQDKEAG 94
Cdd:TIGR02340 4 GGERTSGQDVRTQNVTAAMAIANIVKTSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDREVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 95 DGTTTAVVIAGELLRKAEELLDQNIHPSIITKGYALAAEKA-QEILDEIAIRVDPDDEETLLKIAATSITGKNAESHKEL 173
Cdd:TIGR02340 84 DGTTSVVIIAAELLKRADELVKNKIHPTSVISGYRLACKEAvKYIKENLSVSVDELGREALINVAKTSMSSKIIGLDSDF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 174 LAKL---AVEAVKQVAEKKDGKYVVdlDNIKFEKKAGEGVEESELVRGVVIDKEVVHPRMPKRVENAKIALINEALEVKK 250
Cdd:TIGR02340 164 FSNIvvdAVLAVKTTNENGETKYPI--KAINILKAHGKSARESMLVKGYALNCTVASQQMPKRIKNAKIACLDFNLQKAK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 251 TETDAKINITSPDQLMSFLEQEEKMLKDMVDHIAQTGANVVFVQKGIDDLAQHYLAKYGIMAVRRVKKSDMEKLAKATGA 330
Cdd:TIGR02340 242 MALGVQIVVDDPEKLEQIRQREADITKERIKKILDAGANVVLTTGGIDDMCLKYFVEAGAMGVRRCKKEDLKRIAKATGA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 331 KIVTNVKDLTPED------LGYAEVVEERKLAGENMIFVEGCKNPKAVTILIRGGTEHVIDEVERALEDAVKVVKDVMED 404
Cdd:TIGR02340 322 TLVSTLADLEGEEtfeasyLGFADEVVQERIADDECILIKGTKKRKSASIILRGANDFMLDEMERSLHDALCVVKRTLES 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 405 GAVLPAGGAPEIELAIRLDEYAKQVGGKEALAIENFADALKIIPKTLAENAGLDTVEMLVKVISEH-------KNRGLG- 476
Cdd:TIGR02340 402 NSVVPGGGAVEAALSIYLENFATTLGSREQLAIAEFARALLIIPKTLAVNAAKDSTELVAKLRAYHaaaqlkpEKKHLKw 481
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
1Q2V_B 477 IGIDVFEGKPADMLEKGIIEPLRVKKQAIKSASEAAIMILRIDDVIAAKATKPE 530
Cdd:TIGR02340 482 YGLDLVNGKIRDNKEAGVLEPTVSKVKSLKFATEAAITILRIDDLIKLNPEQSK 535
|
|
| TCP1_eta |
cd03340 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ... |
8-527 |
4.45e-150 |
|
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.
Pssm-ID: 239456 [Multi-domain] Cd Length: 522 Bit Score: 440.57 E-value: 4.45e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 8 PVVILPEGTQRYVGRDAQRLNILAARIIAETVRTTLGPKGMDKMLVDSLGDIVVTNDCATILDKIDLQHPAAKMMVEVAK 87
Cdd:cd03340 1 PIILLKEGTDTSQGKGQLISNINACQAIADAVRTTLGPRGMDKLIVDGRGKVTISNDGATILKLLDIVHPAAKTLVDIAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 88 TQDKEAGDGTTTAVVIAGELLRKAEELLDQNIHPSIITKGYALAAEKAQEILDEIAIRVDPDDE----ETLLKIAATSIT 163
Cdd:cd03340 81 SQDAEVGDGTTSVVVLAGEFLKEAKPFIEDGVHPQIIIRGYRKALQLAIEKIKEIAVNIDKEDKeeqrELLEKCAATALN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 164 GKNAESHKELLAKLAVEAVKQVAEKkdgkyvVDLDNIKFEKKAGEGVEESELVRGVVIDKEVV---HPRMPKRVENAKIA 240
Cdd:cd03340 161 SKLIASEKEFFAKMVVDAVLSLDDD------LDLDMIGIKKVPGGSLEDSQLVNGVAFKKTFSyagFEQQPKKFKNPKIL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 241 LINEALEVKKTETDAKINITSPDQLMSFLEQEEKMLKDMVDHIAQTGANVVFVQKGIDDLAQHYLAKYGIMAVRRVKKSD 320
Cdd:cd03340 235 LLNVELELKAEKDNAEVRVEDPEEYQAIVDAEWKIIYDKLEKIVKSGANVVLSKLPIGDLATQYFADRDIFCAGRVPEED 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 321 MEKLAKATGAKIVTNVKDLTPEDLGYAEVVEERKLAGENMIFVEGCKNPKAVTILIRGGTEHVIDEVERALEDAVKVVKD 400
Cdd:cd03340 315 LKRVAQATGGSIQTTVSNITDDVLGTCGLFEERQVGGERYNIFTGCPKAKTCTIILRGGAEQFIEEAERSLHDAIMIVRR 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 401 VMEDGAVLPAGGAPEIELAIRLDEYAKQVGGKEALAIENFADALKIIPKTLAENAGLDTVEMLVKVISEH-KNRGLGIGI 479
Cdd:cd03340 395 AIKNDSVVAGGGAIEMELSKYLRDYSRTIAGKQQLVINAFAKALEIIPRQLCDNAGFDATDILNKLRQKHaQGGGKWYGV 474
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
1Q2V_B 480 DVFEGKPADMLEKGIIEPLRVKKQAIKSASEAAIMILRIDDVIAAKAT 527
Cdd:cd03340 475 DINNEGIADNFEAFVWEPSLVKINALTAATEAACLILSVDETIKNPKS 522
|
|
| chap_CCT_epsi |
TIGR02343 |
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ... |
6-523 |
1.52e-148 |
|
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: 437.31 E-value: 1.52e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 6 GQPVVILPEGTQ--RYVGRDAQRLNILAARIIAETVRTTLGPKGMDKMLVDSLGDIVVTNDCATILDKIDLQHPAAKMMV 83
Cdd:TIGR02343 8 GRPFIIIKDQDNkkRLKGLEAKKSNIAAAKSVASILRTSLGPKGMDKMLISPDGDITVTNDGATILSQMDVDNQIAKLMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 84 EVAKTQDKEAGDGTTTAVVIAGELLRKAEELLDQNIHPSIITKGYALAAEKAQEILDEIA--IRVDPDDEETLLKIAATS 161
Cdd:TIGR02343 88 ELSKSQDDEIGDGTTGVVVLAGALLEQAEELLDKGIHPIKIADGFEEAARIAVEHLEEISdeISADNNNREPLIQAAKTS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 162 ITGKNAESHKELLAKLAVEAVKQVA--EKKDgkyvVDLDNIKFEKKAGEGVEESELVRGVVIDKEVVHPRMPKRVENAKI 239
Cdd:TIGR02343 168 LGSKIVSKCHRRFAEIAVDAVLNVAdmERRD----VDFDLIKVEGKVGGSLEDTKLIKGIIIDKDFSHPQMPKEVEDAKI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 240 ALINEALEVKKTETDAKINITSPDQLMSFLEQEEKMLKDMVDHIAQTGANVVFVQKGIDDLAQHYLAKYGIMAVRRVKKS 319
Cdd:TIGR02343 244 AILTCPFEPPKPKTKHKLDISSVEEYKKLQKYEQQKFKEMIDDIKKSGANLVICQWGFDDEANHLLLQNDLPAVRWVGGQ 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 320 DMEKLAKATGAKIVTNVKDLTPEDLGYAEVVEERKLAGEN--MIFVEGCKNPKAVTILIRGGTEHVIDEVERALEDAVKV 397
Cdd:TIGR02343 324 ELELIAIATGGRIVPRFQELSKDKLGKAGLVREISFGTTKdrMLVIEQCKNSKAVTIFIRGGNKMIIEEAKRSIHDALCV 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 398 VKDVMEDGAVLPAGGAPEIELAIRLDEYAKQVGGKEALAIENFADALKIIPKTLAENAGLDTVEMLVKVISEH-KNRGLG 476
Cdd:TIGR02343 404 VRNLIKDSRIVYGGGAAEISCSLAVSQEADKYPGVEQYAIRAFADALETIPMALAENSGLDPIGTLSTLKSLQlKEKNPN 483
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
1Q2V_B 477 IGIDVFEGKPADMLEKGIIEPLRVKKQAIKSASEAAIMILRIDDVIA 523
Cdd:TIGR02343 484 LGVDCLGYGTNDMKEQFVFETLIGKKQQILLATQLVRMILKIDDVIS 530
|
|
| chap_CCT_theta |
TIGR02346 |
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ... |
11-525 |
3.41e-136 |
|
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: 405.64 E-value: 3.41e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 11 ILPEGTQRYVGRDAQRL-NILAARIIAETVRTTLGPKGMDKMLVDSLGDIVVTNDCATILDKIDLQHPAAKMMVEVAKTQ 89
Cdd:TIGR02346 5 LLKEGYRHFSGLEEAVIkNIEACKELSQITRTSLGPNGMNKMVINHLEKLFVTNDAATILRELEVQHPAAKLLVMASEMQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 90 DKEAGDGTTTAVVIAGELLRKAEELLDQNIHPSIITKGYALAAEKAQEILDEIAI--RVDPDDEETLLKIAATSITGKNA 167
Cdd:TIGR02346 85 ENEIGDGTNLVLVLAGELLNKAEELIRMGLHPSEIIKGYEMALKKAMEILEELVVweVKDLRDKDELIKALKASISSKQY 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 168 eSHKELLAKLAVEAVKQVAEKKDGKYvvDLDNIKFEKKAGEGVEESELVRGVVIDKEVVHprMPKRVENAKIALINEALE 247
Cdd:TIGR02346 165 -GNEDFLAQLVAQACSTVLPKNPQNF--NVDNIRVCKILGGSLSNSEVLKGMVFNREAEG--SVKSVKNAKVAVFSCPLD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 248 VKKTETDAKINITSPDQLMSFLEQEEKMLKDMVDHIAQTGANVVFVQKGIDDLAQHYLAKYGIMAVRRVKKSDMEKLAKA 327
Cdd:TIGR02346 240 TATTETKGTVLIHNAEELLNYSKGEENQIEAMIKAIADSGVNVIVTGGSVGDMALHYLNKYNIMVLKIPSKFELRRLCKT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 328 TGAKIVTNVKDLTPEDLGYAEVVEERKLAGENM-IFVEGCKNPKAVTILIRGGTEHVIDEVERALEDAVKVVKDVMEDGA 406
Cdd:TIGR02346 320 VGATPLPRLGAPTPEEIGYVDSVYVSEIGGDKVtVFKQENGDSKISTIILRGSTDNLLDDIERAIDDGVNTVKALVKDGR 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 407 VLPAGGAPEIELAIRLDEYAKQVGGKEALAIENFADALKIIPKTLAENAGLDTVEMLVKVISEHKNRGLGIGIDVFEGKP 486
Cdd:TIGR02346 400 LLPGAGATEIELASRLTKYGEKLPGLDQYAIKKFAEAFEIIPRTLAENAGLNANEVIPKLYAAHKKGNKSKGIDIEAESD 479
|
490 500 510 520
....*....|....*....|....*....|....*....|.
1Q2V_B 487 A--DMLEKGIIEPLRVKKQAIKSASEAAIMILRIDDVIAAK 525
Cdd:TIGR02346 480 GvkDASEAGIYDMLATKKWAIKLATEAAVTVLRVDQIIMAK 520
|
|
| chap_CCT_eta |
TIGR02345 |
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ... |
7-525 |
1.12e-134 |
|
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: 401.44 E-value: 1.12e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 7 QPVVILPEGTQRYVGRDAQRLNILAARIIAETVRTTLGPKGMDKMLVDSLGDIVVTNDCATILDKIDLQHPAAKMMVEVA 86
Cdd:TIGR02345 2 PTIVLLKEGTDTSQGKGQLISNINACVAIAEALKTTLGPRGMDKLIVGSNGKATISNDGATILKLLDIVHPAAKTLVDIA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 87 KTQDKEAGDGTTTAVVIAGELLRKAEELLDQNIHPSIITKGYALAAEKAQEILDEIAIRVDPDD---EETLLKIAATSIT 163
Cdd:TIGR02345 82 KSQDAEVGDGTTSVTILAGELLKEAKPFIEEGVHPQLIIRCYREALSLAVEKIKEIAVTIDEEKgeqRELLEKCAATALS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 164 GKNAESHKELLAKLAVEAVKQVAEKkdgkyVVDLDNIKFEKKAGEGVEESELVRGVVIDKEVV---HPRMPKRVENAKIA 240
Cdd:TIGR02345 162 SKLISHNKEFFSKMIVDAVLSLDRD-----DLDLKLIGIKKVQGGALEDSQLVNGVAFKKTFSyagFEQQPKKFANPKIL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 241 LINEALEVKKTETDAKINITSPDQLMSFLEQEEKMLKDMVDHIAQTGANVVFVQKGIDDLAQHYLAKYGIMAVRRVKKSD 320
Cdd:TIGR02345 237 LLNVELELKAEKDNAEIRVEDVEDYQAIVDAEWAIIFRKLEKIVESGANVVLSKLPIGDLATQYFADRDIFCAGRVSAED 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 321 MEKLAKATGAKIVTNVKDLTPEDLGYAEVVEERKLAGENMIFVEGCKNPKAVTILIRGGTEHVIDEVERALEDAVKVVKD 400
Cdd:TIGR02345 317 LKRVIKACGGSIQSTTSDLEADVLGTCALFEERQIGSERYNYFTGCPHAKTCTIILRGGAEQFIEEAERSLHDAIMIVRR 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 401 VMEDGAVLPAGGAPEIELAIRLDEYAKQVGGKEALAIENFADALKIIPKTLAENAGLDTVEMLVKVISEHKNRGLGIGID 480
Cdd:TIGR02345 397 ALKNKKIVAGGGAIEMELSKCLRDYSKTIDGKQQLIINAFAKALEIIPRQLCENAGFDSIEILNKLRSRHAKGGKWYGVD 476
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
1Q2V_B 481 VFEGKPADMLEKGIIEPLRVKKQAIKSASEAAIMILRIDDVIAAK 525
Cdd:TIGR02345 477 INTEDIGDNFEAFVWEPALVKINALKAAFEAACTILSVDETITNP 521
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
2-524 |
9.51e-133 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 396.71 E-value: 9.51e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 2 AQLSGQPVVILPEGTQRYVGRDAQRLNILAARIIAETVRTTLGPKGMDKMLVDS-----LGDIVVTNDCATILDKIDLQH 76
Cdd:PTZ00212 1 MIMANVPPQVLKQGAQEEKGETARLQSFVGAIAVADLVKTTLGPKGMDKILQPMsegprSGNVTVTNDGATILKSVWLDN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 77 PAAKMMVEVAKTQDKEAGDGTTTAVVIAGELLRKAEELLDQNIHPSIITKGYALAAEKAQEILDEIAIRVDPDDE---ET 153
Cdd:PTZ00212 81 PAAKILVDISKTQDEEVGDGTTSVVVLAGELLREAEKLLDQKIHPQTIIEGWRMALDVARKALEEIAFDHGSDEEkfkED 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 154 LLKIAATSITGKNAESHKELLAKLAVEAVKQVAEKKDgkyvvdLDNIKFEKKAGEGVEESELVRGVVIDKEVvHPRMPKR 233
Cdd:PTZ00212 161 LLNIARTTLSSKLLTVEKDHFAKLAVDAVLRLKGSGN------LDYIQIIKKPGGTLRDSYLEDGFILEKKI-GVGQPKR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 234 VENAKIALINEALEVKKTET-DAKINITSPDQLMSFLEQEEKMLKDMVDHIAQTGANVVFVQKGIDDLAQHYLAKYGIMA 312
Cdd:PTZ00212 234 LENCKILVANTPMDTDKIKIyGAKVKVDSMEKVAEIEAAEKEKMKNKVDKILAHGCNVFINRQLIYNYPEQLFAEAGIMA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 313 VRRVKKSDMEKLAKATGAKIVTNVKDLTPEDLGYAEVVEERKLAGENMIFVEGCKNPKAVTILIRGGTEHVIDEVERALE 392
Cdd:PTZ00212 314 IEHADFDGMERLAAALGAEIVSTFDTPEKVKLGHCDLIEEIMIGEDKLIRFSGCAKGEACTIVLRGASTHILDEAERSLH 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 393 DAVKVVKDVMEDGAVLPAGGAPEIELAIRLDEYAKQVGGKEALAIENFADALKIIPKTLAENAGLDTVEMLVKVISEHKN 472
Cdd:PTZ00212 394 DALCVLSQTVKDTRVVLGGGCSEMLMANAVEELAKKVEGKKSLAIEAFAKALRQIPTIIADNGGYDSAELVSKLRAEHYK 473
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
1Q2V_B 473 RGLGIGIDVFEGKPADMLEKGIIEPLRVKKQAIKSASEAAIMILRIDDVIAA 524
Cdd:PTZ00212 474 GNKTAGIDMEKGTVGDMKELGITESYKVKLSQLCSATEAAEMILRVDDIIRC 525
|
|
| TCP1_theta |
cd03341 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ... |
28-525 |
2.06e-131 |
|
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: 391.20 E-value: 2.06e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 28 NILAARIIAETVRTTLGPKGMDKMLVDSLGDIVVTNDCATILDKIDLQHPAAKMMVEVAKTQDKEAGDGTTTAVVIAGEL 107
Cdd:cd03341 13 NIEACKELSQITRTSYGPNGMNKMVINHLEKLFVTSDAATILRELEVQHPAAKLLVMASQMQEEEIGDGTNLVVVLAGEL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 108 LRKAEELLDQNIHPSIITKGYALAAEKAQEILDEIAIR--VDPDDEETLLKIAATSITGKNAeSHKELLAKLAVEAVKQV 185
Cdd:cd03341 93 LEKAEELLRMGLHPSEIIEGYEKALKKALEILEELVVYkiEDLRNKEEVSKALKTAIASKQY-GNEDFLSPLVAEACISV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 186 AEKKDGKYvvDLDNIKFEKKAGEGVEESELVRGVVIDKEVVHprMPKRVENAKIALINEALEvkktetdakinitspdql 265
Cdd:cd03341 172 LPENIGNF--NVDNIRVVKILGGSLEDSKVVRGMVFKREPEG--SVKRVKKAKVAVFSCPFD------------------ 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 266 msfleqeekmlkdmvdhiaqTGANVVFVQKGIDDLAQHYLAKYGIMAVRRVKKSDMEKLAKATGAKIVTNVKDLTPEDLG 345
Cdd:cd03341 230 --------------------IGVNVIVAGGSVGDLALHYCNKYGIMVIKINSKFELRRLCRTVGATPLPRLGAPTPEEIG 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 346 YAEVVEERKLAGENMIFVEGCKNPKAV-TILIRGGTEHVIDEVERALEDAVKVVKDVMEDGAVLPAGGAPEIELAIRLDE 424
Cdd:cd03341 290 YCDSVYVEEIGDTKVVVFRQNKEDSKIaTIVLRGATQNILDDVERAIDDGVNVFKSLTKDGRFVPGAGATEIELAKKLKE 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 425 YAKQVGGKEALAIENFADALKIIPKTLAENAGLDTVEMLVKVISEHKNRGLGIGIDVFEGKPA--DMLEKGIIEPLRVKK 502
Cdd:cd03341 370 YGEKTPGLEQYAIKKFAEAFEVVPRTLAENAGLDATEVLSELYAAHQKGNKSAGVDIESGDEGtkDAKEAGIFDHLATKK 449
|
490 500
....*....|....*....|...
1Q2V_B 503 QAIKSASEAAIMILRIDDVIAAK 525
Cdd:cd03341 450 WAIKLATEAAVTVLRVDQIIMAK 472
|
|
| TCP1_zeta |
cd03342 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
24-524 |
2.75e-130 |
|
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: 388.92 E-value: 2.75e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 24 AQRLNILAARIIAETVRTTLGPKGMDKMLVDSLGDIVVTNDCATILDKIDLQHPAAKMMVEVAKTQDKEAGDGTTTAVVI 103
Cdd:cd03342 13 ALAVNISAAKGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLSEMQIQHPTASMIARAATAQDDITGDGTTSNVLL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 104 AGELLRKAEELLDQNIHPSIITKGYALAAEKAQEILDEIAIRVDPD-DEETLLKIAATSITGKNAESHKELLAKLAVEAV 182
Cdd:cd03342 93 IGELLKQAERYIQEGVHPRIITEGFELAKNKALKFLESFKVPVEIDtDRELLLSVARTSLRTKLHADLADQLTEIVVDAV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 183 KQVaeKKDGKYVvDLDNIKFEKKAGEGVEESELVRGVVIDKEVVHPRMPKRVENAKIALINEALEVKKTETDAkinitsp 262
Cdd:cd03342 173 LAI--YKPDEPI-DLHMVEIMQMQHKSDSDTKLIRGLVLDHGARHPDMPKRVENAYILTCNVSLEYEKTEVNS------- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 263 dqlmSFLeqeekmlkdmvdhiaqtgANVVFVQKGIDDLAQHYLAKYGIMAVRRVKKSDMEKLAKATGAKIVTNVKDLTPE 342
Cdd:cd03342 243 ----GFF------------------YSVVINQKGIDPPSLDMLAKEGILALRRAKRRNMERLTLACGGVAMNSVDDLSPE 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 343 DLGYAEVVEERKLAGENMIFVEGCKNPKAVTILIRGGTEHVIDEVERALEDAVKVVKDVMEDGAVLPAGGAPEIELAIRL 422
Cdd:cd03342 301 CLGYAGLVYERTLGEEKYTFIEGVKNPKSCTILIKGPNDHTITQIKDAIRDGLRAVKNAIEDKCVVPGAGAFEVALYAHL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 423 DEYAKQVGGKEALAIENFADALKIIPKTLAENAGLDTVEMLVKVISEHKNRGLGIGIDVFEGKPADMLEKGIIEPLRVKK 502
Cdd:cd03342 381 KEFKKSVKGKAKLGVQAFADALLVIPKTLAENSGLDVQETLVKLQDEYAEGGQVGGVDLDTGEPMDPESEGIWDNYSVKR 460
|
490 500
....*....|....*....|..
1Q2V_B 503 QAIKSASEAAIMILRIDDVIAA 524
Cdd:cd03342 461 QILHSATVIASQLLLVDEIIRA 482
|
|
| TCP1_beta |
cd03336 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ... |
11-525 |
9.01e-130 |
|
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: 388.61 E-value: 9.01e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 11 ILPEGTQRYVGRDAQRLNILAARIIAETVRTTLGPKGMDKML--VDSLGDIVVTNDCATILDKIDLQHPAAKMMVEVAKT 88
Cdd:cd03336 1 ILKDGAQEEKGETARLSSFVGAIAIGDLVKTTLGPKGMDKILqsVGRSGGVTVTNDGATILKSIGVDNPAAKVLVDISKV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 89 QDKEAGDGTTTAVVIAGELLRKAEELLDQNIHPSIITKGYALAAEKAQEILDEIAIRVDPDDE---ETLLKIAATSITGK 165
Cdd:cd03336 81 QDDEVGDGTTSVTVLAAELLREAEKLVAQKIHPQTIIEGYRMATAAAREALLSSAVDHSSDEEafrEDLLNIARTTLSSK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 166 NAESHKELLAKLAVEAVKQVaeKKDGkyvvDLDNIKFEKKAGEGVEESELVRGVVIDKEV-VHprMPKRVENAKIALINE 244
Cdd:cd03336 161 ILTQDKEHFAELAVDAVLRL--KGSG----NLDAIQIIKKLGGSLKDSYLDEGFLLDKKIgVN--QPKRIENAKILIANT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 245 ALEVKKTET-DAKINITSPDQLMSfLEQEEKM-LKDMVDHIAQTGANVVFVQKGIDDLAQHYLAKYGIMAVRRVKKSDME 322
Cdd:cd03336 233 PMDTDKIKIfGAKVRVDSTAKVAE-IEEAEKEkMKNKVEKILKHGINCFINRQLIYNYPEQLFADAGIMAIEHADFDGVE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 323 KLAKATGAKIVTNVKDLTPEDLGYAEVVEERKLAGENMIFVEGCKNPKAVTILIRGGTEHVIDEVERALEDAVKVVKDVM 402
Cdd:cd03336 312 RLALVTGGEIASTFDHPELVKLGTCKLIEEIMIGEDKLIRFSGVAAGEACTIVLRGASQQILDEAERSLHDALCVLAQTV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 403 EDGAVLPAGGAPEIELAIRLDEYAKQVGGKEALAIENFADALKIIPKTLAENAGLDTVEMLVKVISEHKNRGLGIGIDVF 482
Cdd:cd03336 392 KDTRVVLGGGCSEMLMAKAVEELAKKTPGKKSLAIEAFAKALRQLPTIIADNAGYDSAELVAQLRAAHYNGNTTAGLDMR 471
|
490 500 510 520
....*....|....*....|....*....|....*....|...
1Q2V_B 483 EGKPADMLEKGIIEPLRVKKQAIKSASEAAIMILRIDDVIAAK 525
Cdd:cd03336 472 KGTVGDMKELGITESFKVKRQVLLSASEAAEMILRVDDIIKCA 514
|
|
| chap_CCT_zeta |
TIGR02347 |
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ... |
24-524 |
1.99e-123 |
|
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: 372.92 E-value: 1.99e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 24 AQRLNILAARIIAETVRTTLGPKGMDKMLVDSLGDIVVTNDCATILDKIDLQHPAAKMMVEVAKTQDKEAGDGTTTAVVI 103
Cdd:TIGR02347 17 ALMMNINAARGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEMQIQHPTASMIARAATAQDDITGDGTTSTVLL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 104 AGELLRKAEELLDQNIHPSIITKGYALAAEKAQEILDEIAIRV-DPDDEETLLKIAATSITGKNAESHKELLAKLAVEAV 182
Cdd:TIGR02347 97 IGELLKQAERYILEGVHPRIITEGFEIARKEALQFLDKFKVKKeDEVDREFLLNVARTSLRTKLPADLADQLTEIVVDAV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 183 KQVaeKKDGKyVVDLDNIKFEKKAGEGVEESELVRGVVIDKEVVHPRMPKRVENAKIALINEALEVKKTETDAKINITSP 262
Cdd:TIGR02347 177 LAI--KKDGE-DIDLFMVEIMEMKHKSATDTTLIRGLVLDHGARHPDMPRRVKNAYILTCNVSLEYEKTEVNSGFFYSSA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 263 DQLMSFLEQEEKMLKDMVDHIAQTGANV----------VFVQKGIDDLAQHYLAKYGIMAVRRVKKSDMEKLAKATGAKI 332
Cdd:TIGR02347 254 EQREKLVKAERKFVDDRVKKIIELKKKVcgkspdkgfvVINQKGIDPPSLDLLAKEGIMALRRAKRRNMERLTLACGGEA 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 333 VTNVKDLTPEDLGYAEVVEERKLAGENMIFVEGCKNPKAVTILIRGGTEHVIDEVERALEDAVKVVKDVMEDGAVLPAGG 412
Cdd:TIGR02347 334 LNSVEDLTPECLGWAGLVYETTIGEEKYTFIEECKNPKSCTILIKGPNDHTIAQIKDAVRDGLRAVKNAIEDKCVVPGAG 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 413 APEIELAIRLDEYAKQVGGKEALAIENFADALKIIPKTLAENAGLDTVEMLVKVISEHKNRGLGIGIDVFEGKPADMLEK 492
Cdd:TIGR02347 414 AFEIAAYRHLKEYKKSVKGKAKLGVEAFANALLVIPKTLAENSGFDAQDTLVKLEDEHDEGGEVVGVDLNTGEPIDPEIK 493
|
490 500 510
....*....|....*....|....*....|..
1Q2V_B 493 GIIEPLRVKKQAIKSASEAAIMILRIDDVIAA 524
Cdd:TIGR02347 494 GIWDNYRVKKQLIQSATVIASQLLLVDEVMRA 525
|
|
| chap_CCT_beta |
TIGR02341 |
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ... |
11-524 |
1.10e-99 |
|
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: 311.41 E-value: 1.10e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 11 ILPEGTQRYVGRDAQRLNILAARIIAETVRTTLGPKGMDKMLV--DSLGDIVVTNDCATILDKIDLQHPAAKMMVEVAKT 88
Cdd:TIGR02341 2 IFKDGADEERAENARLSSFVGAIAIGDLVKSTLGPKGMDKILQssSSDASIMVTNDGATILKSIGVDNPAAKVLVDMSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 89 QDKEAGDGTTTAVVIAGELLRKAEELLDQNIHPSIITKGYALAAEKAQEILDEIAIRVDPDD---EETLLKIAATSITGK 165
Cdd:TIGR02341 82 QDDEVGDGTTSVTVLAAELLREAEKLINQKIHPQTIIAGYREATKAARDALLKSAVDNGSDEvkfRQDLMNIARTTLSSK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 166 NAESHKELLAKLAVEAVKQVaekkdgKYVVDLDNIKFEKKAGEGVEESELVRGVVIDKEVvHPRMPKRVENAKIALINEA 245
Cdd:TIGR02341 162 ILSQHKDHFAQLAVDAVLRL------KGSGNLEAIQIIKKLGGSLADSYLDEGFLLDKKI-GVNQPKRIENAKILIANTG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 246 LEVKKTET-DAKINITSPDQLMSFLEQEEKMLKDMVDHIAQTGANVVFVQKGIDDLAQHYLAKYGIMAVRRVKKSDMEKL 324
Cdd:TIGR02341 235 MDTDKVKIfGSRVRVDSTAKVAELEHAEKEKMKEKVEKILKHGINCFINRQLIYNYPEQLFADAGVMAIEHADFEGVERL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 325 AKATGAKIVTNVKDLTPEDLGYAEVVEERKLAGENMIFVEGCKNPKAVTILIRGGTEHVIDEVERALEDAVKVVKDVMED 404
Cdd:TIGR02341 315 ALVTGGEIVSTFDHPELVKLGSCDLIEEIMIGEDKLLKFSGVKLGEACTIVLRGATQQILDEAERSLHDALCVLSQTVKE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 405 GAVLPAGGAPEIELAIRLDEYAKQVGGKEALAIENFADALKIIPKTLAENAGLDTVEMLVKVISEHKNRGLGIGIDVFEG 484
Cdd:TIGR02341 395 SRTVLGGGCSEMLMSKAVTQEAQRTPGKEALAVEAFARALRQLPTIIADNAGFDSAELVAQLRAAHYNGNTTMGLDMNEG 474
|
490 500 510 520
....*....|....*....|....*....|....*....|
1Q2V_B 485 KPADMLEKGIIEPLRVKKQAIKSASEAAIMILRIDDVIAA 524
Cdd:TIGR02341 475 TIADMRQLGITESYKVKRAVVSSAAEAAEVILRVDNIIKA 514
|
|
| chaperonin_like |
cd03333 |
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ... |
151-404 |
2.87e-81 |
|
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: 252.77 E-value: 2.87e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 151 EETLLKIAATSITGKNaESHKELLAKLAVEAVKQVAEKKDgkyVVDLDNIKFEKKAGEGVEESELVRGVVIDKEVVHPRM 230
Cdd:cd03333 1 RELLLQVATTSLNSKL-SSWDDFLGKLVVDAVLKVGPDNR---MDDLGVIKVEKIPGGSLEDSELVVGVVFDKGYASPYM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 231 PKRVENAKIALINEALEvkktetdakinitspdqlmsfleqeekmlkdmvdhiaqtgaNVVFVQKGIDDLAQHYLAKYGI 310
Cdd:cd03333 77 PKRLENAKILLLDCPLE-----------------------------------------YVVIAEKGIDDLALHYLAKAGI 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 311 MAVRRVKKSDMEKLAKATGAKIVTNVKDLTPEDLGYAEVVEERKLAGENMIFVEGCKNPKAVTILIRGGTEHVIDEVERA 390
Cdd:cd03333 116 MAVRRVKKEDLERIARATGATIVSSLEDLTPEDLGTAELVEETKIGEEKLTFIEGCKGGKAATILLRGATEVELDEVKRS 195
|
250
....*....|....
1Q2V_B 391 LEDAVKVVKDVMED 404
Cdd:cd03333 196 LHDALCAVRAAVEE 209
|
|
| Fab1_TCP |
cd03334 |
TCP-1 like domain of the eukaryotic phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinase Fab1. ... |
164-398 |
5.42e-35 |
|
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: 132.35 E-value: 5.42e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 164 GKNAESHKELLAKLAVEAVKQVaeKKDGKYVVDLDN---IKFEKKAGEGVEESELVRGVVIDKEVVHPRMPKRVENAKIA 240
Cdd:cd03334 13 ISNDESWLDILLPLVWKAASNV--KPDVRAGDDMDIrqyVKIKKIPGGSPSDSEVVDGVVFTKNVAHKRMPSKIKNPRIL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 241 LINEALEVKKTETdakinitspdQLMSF---LEQEEKMLKDMVDHIAQTGANVVFVQKGIDDLAQHYLAKYGIMAVRRVK 317
Cdd:cd03334 91 LLQGPLEYQRVEN----------KLLSLdpvILQEKEYLKNLVSRIVALRPDVILVEKSVSRIAQDLLLEAGITLVLNVK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 318 KSDMEKLAKATGAKIVTNVKDL-TPEDLGYAE------VVEERKLaGENMIFVEGCKNPKAVTILIRGGTEHVIDEVERA 390
Cdd:cd03334 161 PSVLERISRCTGADIISSMDDLlTSPKLGTCEsfrvrtYVEEHGR-SKTLMFFEGCPKELGCTILLRGGDLEELKKVKRV 239
|
....*...
1Q2V_B 391 LEDAVKVV 398
Cdd:cd03334 240 VEFMVFAA 247
|
|
| GroEL |
cd03344 |
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ... |
21-516 |
1.77e-33 |
|
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings, each composed of 7-9 subunits. The symmetry of type I is seven-fold and they are found in eubacteria (GroEL) and in organelles of eubacterial descent (hsp60 and RBP). With the aid of cochaperonin GroES, GroEL encapsulates non-native substrate proteins inside the cavity of the GroEL-ES complex and promotes folding by using energy derived from ATP hydrolysis.
Pssm-ID: 239460 Cd Length: 520 Bit Score: 133.74 E-value: 1.77e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 21 GRDAQRLNILAARIIAETVRTTLGPKGMDKMLVDSLGDIVVTNDCATILDKIDLQHP----AAKMMVEVAKTQDKEAGDG 96
Cdd:cd03344 6 GEEARKALLRGVNKLADAVKVTLGPKGRNVVIEKSFGSPKITKDGVTVAKEIELEDPfenmGAQLVKEVASKTNDVAGDG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 97 TTTAVVIAGELLRKAEELLDQNIHPSIITKGYALAAEKAQEILDEIAIRVdpDDEETLLKIAATSITGknaeshKELLAK 176
Cdd:cd03344 86 TTTATVLARAIIKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKPV--KTKEEIAQVATISANG------DEEIGE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 177 LAVEAVKQVAekKDGkyVVDLDNikfekkaGEGVE-ESELVRGVVIDKEVVHPRMPKRVENAKIALINEALEVkkteTDA 255
Cdd:cd03344 158 LIAEAMEKVG--KDG--VITVEE-------GKTLEtELEVVEGMQFDRGYLSPYFVTDPEKMEVELENPYILL----TDK 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 256 KINitSPDQLMSFLEQeekmlkdmvdhIAQTGANVVFVQKGIDDLAQHYLA---KYGIMAVRRVK--------KSDMEKL 324
Cdd:cd03344 223 KIS--SIQELLPILEL-----------VAKAGRPLLIIAEDVEGEALATLVvnkLRGGLKVCAVKapgfgdrrKAMLEDI 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 325 AKATGAKIVTN-----VKDLTPEDLGYAEVVEERKlagENMIFVEGCKNPKAV--------------------------- 372
Cdd:cd03344 290 AILTGGTVISEelglkLEDVTLEDLGRAKKVVVTK---DDTTIIGGAGDKAAIkariaqirkqieettsdydkeklqerl 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 373 --------TILIRGGTEHVIDEVERALEDAVKVVKDVMEDGaVLPAGGAPEIELAIRLDEYAKQVGGkEALAIENFADAL 444
Cdd:cd03344 367 aklsggvaVIKVGGATEVELKEKKDRVEDALNATRAAVEEG-IVPGGGVALLRASPALDKLKALNGD-EKLGIEIVRRAL 444
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
1Q2V_B 445 KIIPKTLAENAGLDTVEMLVKVIsEHKNrglGIGIDVFEGKPADMLEKGIIEPLRVKKQAIKSASEAAIMIL 516
Cdd:cd03344 445 EAPLRQIAENAGVDGSVVVEKVL-ESPD---GFGYDAATGEYVDMIEAGIIDPTKVVRSALQNAASVASLLL 512
|
|
| groEL |
PRK12849 |
chaperonin GroEL; Reviewed |
33-530 |
2.67e-29 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237230 Cd Length: 542 Bit Score: 121.45 E-value: 2.67e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 33 RIIAETVRTTLGPKGMDKMLVDSLGDIVVTNDCATILDKIDLQHP----AAKMMVEVA-KTQDKeAGDGTTTAVVIAGEL 107
Cdd:PRK12849 20 NKLADAVKVTLGPKGRNVVIDKSFGAPTITKDGVSIAKEIELEDPfenlGAQLVKEVAsKTNDV-AGDGTTTATVLAQAL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 108 LRKAEELLDQNIHPSIITKGYALAAEKAQEILDEIAIRVDPDDEetLLKIAATSITGknaeshKELLAKLAVEAVKQVAe 187
Cdd:PRK12849 99 VQEGLKNVAAGANPMDLKRGIDKAVEAVVEELKALARPVSGSEE--IAQVATISANG------DEEIGELIAEAMEKVG- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 188 kKDGkyVVDLDNikfekkaGEGVE-ESELVRGVVIDKEVVHP-------RMPKRVENAKIALinealevkkteTDAKinI 259
Cdd:PRK12849 170 -KDG--VITVEE-------SKTLEtELEVTEGMQFDRGYLSPyfvtdpeRMEAVLEDPLILL-----------TDKK--I 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 260 TSPDQLMSFLEQeekmlkdmvdhIAQTGANVVFVQkgiDDLAQHYLAKY------GIMAVRRVK--------KSDMEKLA 325
Cdd:PRK12849 227 SSLQDLLPLLEK-----------VAQSGKPLLIIA---EDVEGEALATLvvnklrGGLKVAAVKapgfgdrrKAMLEDIA 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 326 KATGAKIVT-----NVKDLTPEDLGYAEVVEERKlagENMIFVEGCKNPKAV---------------------------- 372
Cdd:PRK12849 293 ILTGGTVISedlglKLEEVTLDDLGRAKRVTITK---DNTTIVDGAGDKEAIearvaqirrqieettsdydreklqerla 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 373 -------TILIRGGTEHVIDEVERALEDAVKVVKDVMEDGaVLPAGGAPEIELAIRLDEYaKQVGGKEALAIENFADALK 445
Cdd:PRK12849 370 klaggvaVIKVGAATEVELKERKDRVEDALNATRAAVEEG-IVPGGGVALLRAAKALDEL-AGLNGDQAAGVEIVRRALE 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 446 IIPKTLAENAGLDTvEMLVKVISEHKNrglGIGIDVFEGKPADMLEKGIIEPLRVKKQAIKSASEAAIMILRIDDVIAAK 525
Cdd:PRK12849 448 APLRQIAENAGLDG-SVVVAKVLELED---GFGFNAATGEYGDLIAAGIIDPVKVTRSALQNAASVAGLLLTTEALVADK 523
|
....*
1Q2V_B 526 ATKPE 530
Cdd:PRK12849 524 PEEED 528
|
|
| PTZ00114 |
PTZ00114 |
Heat shock protein 60; Provisional |
35-516 |
1.10e-26 |
|
Heat shock protein 60; Provisional
Pssm-ID: 185455 Cd Length: 555 Bit Score: 113.85 E-value: 1.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 35 IAETVRTTLGPKGMDKMLVDSLGDIVVTNDCATILDKIDLQHPA----AKMMVEVAKTQDKEAGDGTTTAVVIAGELLRK 110
Cdd:PTZ00114 34 LADAVAVTLGPKGRNVIIEQEYGSPKITKDGVTVAKAIEFSDRFenvgAQLIRQVASKTNDKAGDGTTTATILARAIFRE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 111 AEELLDQNIHPSIITKGYALAAEKAQEILDEIAIRVDPDDEetLLKIAATSITGknaeshKELLAKLAVEAVKQVAekKD 190
Cdd:PTZ00114 114 GCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQSRPVKTKED--ILNVATISANG------DVEIGSLIADAMDKVG--KD 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 191 GKYVVDldnikfEKKAGEgvEESELVRGVVIDKEVVHPRMPKRVENAKIALINEALEVkkteTDAKINitSPDQLMSFLE 270
Cdd:PTZ00114 184 GTITVE------DGKTLE--DELEVVEGMSFDRGYISPYFVTNEKTQKVELENPLILV----TDKKIS--SIQSILPILE 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 271 qeekmlkdmvdHIAQTGANVVFVQKGIDDLAQHYLA------KYGIMAVR-----RVKKSDMEKLAKATGAKIVTNVK-- 337
Cdd:PTZ00114 250 -----------HAVKNKRPLLIIAEDVEGEALQTLIinklrgGLKVCAVKapgfgDNRKDILQDIAVLTGATVVSEDNvg 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 338 ----DLTPEDLGYAEVVEERKlagENMIFVEGCKNPKAV-----------------------------------TILIRG 378
Cdd:PTZ00114 319 lkldDFDPSMLGSAKKVTVTK---DETVILTGGGDKAEIkervellrsqierttseydkeklkerlaklsggvaVIKVGG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 379 GTEHVIDEVERALEDAVKVVKDVMEDGaVLPAGGAPEIELAIRLDEYA--KQVGGKEALAIENFADALKIIPKTLAENAG 456
Cdd:PTZ00114 396 ASEVEVNEKKDRIEDALNATRAAVEEG-IVPGGGVALLRASKLLDKLEedNELTPDQRTGVKIVRNALRLPTKQIAENAG 474
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 457 LDTvEMLVKVISEHKNRglGIGIDVFEGKPADMLEKGIIEPLRVKKQAIKSASEAAIMIL 516
Cdd:PTZ00114 475 VEG-AVVVEKILEKKDP--SFGYDAQTGEYVNMFEAGIIDPTKVVRSALVDAASVASLML 531
|
|
| GroEL |
TIGR02348 |
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ... |
35-525 |
1.43e-24 |
|
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: 107.38 E-value: 1.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 35 IAETVRTTLGPKGMDKMLVDSLGDIVVTNDCATILDKIDLQHP----AAKMMVEVA-KTQDKeAGDGTTTAVVIAGELLR 109
Cdd:TIGR02348 21 LADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDKfenmGAQLVKEVAsKTNDV-AGDGTTTATVLAQAIVK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 110 KAEELLDQNIHPSIITKGYALAAEKAQEILDEIAIRVDPDDEetllkIAAT-SITGKNAESHKELLAklavEAVKQVaeK 188
Cdd:TIGR02348 100 EGLKNVAAGANPIELKRGIEKAVEAVVEELKKLSKPVKGKKE-----IAQVaTISANNDEEIGSLIA----EAMEKV--G 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 189 KDGKYVVDldnikfEKKAGEgvEESELVRGVVIDKEVVHP-------RMPKRVENAKIALinealevkkteTDAKinITS 261
Cdd:TIGR02348 169 KDGVITVE------ESKSLE--TELEVVEGMQFDRGYISPyfvtdaeKMEVELENPYILI-----------TDKK--ISN 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 262 PDQLMSFLEQeekmlkdmvdhIAQTGANVVFVQKGIDDLAQHYLA---KYGIMAVRRVK--------KSDMEKLAKATGA 330
Cdd:TIGR02348 228 IKDLLPLLEK-----------VAQSGKPLLIIAEDVEGEALATLVvnkLRGTLNVCAVKapgfgdrrKAMLEDIAILTGG 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 331 KIVT-----NVKDLTPEDLGYAEVVEERKlagENMIFVEGCKNPKAV--------------------------------- 372
Cdd:TIGR02348 297 QVISeelglKLEEVTLDDLGKAKKVTVDK---DNTTIVEGAGDKAAIkarvaqikaqieettsdydreklqerlaklagg 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 373 --TILIRGGTEHVIDEVERALEDAVKVVKDVMEDGaVLPAGGAPEIELAIRLDEyAKQVGGKEALAIENFADALKIIPKT 450
Cdd:TIGR02348 374 vaVIKVGAATETEMKEKKLRIEDALNATRAAVEEG-IVPGGGVALLRAAAALEG-LKGDGEDEAIGIDIVKRALEAPLRQ 451
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
1Q2V_B 451 LAENAGLDTVEMLVKVISEHKNRGLGIGIDVFEgkpaDMLEKGIIEPLRVKKQAIKSASEAAIMILRIDDVIAAK 525
Cdd:TIGR02348 452 IAENAGLDGAVVAEKVKELKGNFGFNAATGEYE----DLVEAGIIDPTKVTRSALQNAASIAGLLLTTEAVVADK 522
|
|
| groEL |
PRK12851 |
chaperonin GroEL; Reviewed |
23-525 |
3.91e-22 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 171770 Cd Length: 541 Bit Score: 99.82 E-value: 3.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 23 DAQRLNILAARIIAETVRTTLGPKGMDKMLVDSLGDIVVTNDCATILDKIDLQHP----AAKMMVEVAKTQDKEAGDGTT 98
Cdd:PRK12851 11 EAREKMLRGVNILADAVKVTLGPKGRNVVIDKSFGAPTITNDGVTIAKEIELEDKfenmGAQMVREVASKTNDVAGDGTT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 99 TAVVIAGELLRKAEELLDQNIHPSIITKGYALAAEKAQEILDEIAIRVDPDDEetllKIAATSITGKNAESHKELLAkla 178
Cdd:PRK12851 91 TATVLAQAIVREGAKAVAAGANPMDLKRGIDRAVAAVVEELKANARPVTTNAE----IAQVATISANGDAEIGRLVA--- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 179 vEAVKQVAekKDGKYVVDldnikfEKKAGEgvEESELVRGVVIDKEVVHP-------RMPKRVENAKIALINEalevkkt 251
Cdd:PRK12851 164 -EAMEKVG--NEGVITVE------ESKTAE--TELEVVEGMQFDRGYLSPyfvtdadKMEAELEDPYILIHEK------- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 252 etdakiNITSPDQLMSFLEQeekmlkdmvdhIAQTGANVVFVQKGIDDLAQHYLAKYGIMAVRRV-----------KKSD 320
Cdd:PRK12851 226 ------KISNLQDLLPVLEA-----------VVQSGKPLLIIAEDVEGEALATLVVNKLRGGLKVaavkapgfgdrRKAM 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 321 MEKLAKATGAKIVT-----NVKDLTPEDLGYAEVVEERKlagENMIFVEGCKNPKAV----------------------- 372
Cdd:PRK12851 289 LEDIAILTGGTVISedlgiKLENVTLEQLGRAKKVVVEK---ENTTIIDGAGSKTEIegrvaqiraqieettsdydrekl 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 373 ------------TILIRGGTEHVIDEVERALEDAVKVVKDVMEDGaVLPAGGAPEIELAIRLDEyAKQVGGKEALAIENF 440
Cdd:PRK12851 366 qerlaklaggvaVIRVGASTEVEVKEKKDRVDDALHATRAAVEEG-IVPGGGVALLRAVKALDK-LETANGDQRTGVEIV 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 441 ADALKIIPKTLAENAGLDTVEMLVKVISEHKnrglGIGIDVFEGKPADMLEKGIIEPLRVKKQAIKSASEAAIMILRIDD 520
Cdd:PRK12851 444 RRALEAPVRQIAENAGAEGSVVVGKLREKPG----GYGFNAATNEYGDLYAQGVIDPVKVVRTALQNAASVAGLLLTTEA 519
|
....*
1Q2V_B 521 VIAAK 525
Cdd:PRK12851 520 MVAEK 524
|
|
| groEL |
PRK12850 |
chaperonin GroEL; Reviewed |
34-530 |
5.58e-21 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237231 Cd Length: 544 Bit Score: 96.33 E-value: 5.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 34 IIAETVRTTLGPKGMDKMLVDSLGDIVVTNDCATILDKIDLQHPAAKM---MV-EVAKTQDKEAGDGTTTAVVIAGELLR 109
Cdd:PRK12850 22 ILANAVKVTLGPKGRNVVLEKSFGAPRITKDGVTVAKEIELEDKFENMgaqMVkEVASKTNDLAGDGTTTATVLAQAIVR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 110 KAEELLDQNIHPSIITKGYALAAEKAQEILDEIAIRVDPDDEetllkIAAT-SITGKNAESHKELLAklavEAVKQVAek 188
Cdd:PRK12850 102 EGAKLVAAGMNPMDLKRGIDLAVAAVVDELKKIAKKVTSSKE-----IAQVaTISANGDESIGEMIA----EAMDKVG-- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 189 KDGKYVVDldnikfEKKAGEgvEESELVRGVVIDKEVVHP-------RMPKRVENAKIALINealevKKtetdakinITS 261
Cdd:PRK12850 171 KEGVITVE------EAKTLG--TELDVVEGMQFDRGYLSPyfvtnpeKMRAELEDPYILLHE-----KK--------ISN 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 262 PDQLMSFLEQeekmlkdmvdhIAQTGANVVFVQKGIDDLAQHYLAK---YGIMAVRRVK--------KSDMEKLAKATGA 330
Cdd:PRK12850 230 LQDLLPILEA-----------VVQSGRPLLIIAEDVEGEALATLVVnklRGGLKSVAVKapgfgdrrKAMLEDIAVLTGG 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 331 KIVT-----NVKDLTPEDLGYAEVVEERKlagENMIFVEGCKNPKAV--------------------------------- 372
Cdd:PRK12850 299 QVISedlgiKLENVTLDMLGRAKRVLITK---ENTTIIDGAGDKKNIearvkqiraqieettsdydreklqerlaklagg 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 373 --TILIRGGTEHVIDEVERALEDAVKVVKDVMEDGAVlPAGGAPEIELAIRLDEyAKQVGGKEALAIENFADALKIIPKT 450
Cdd:PRK12850 376 vaVIRVGGATEVEVKEKKDRVDDALHATRAAVEEGIV-PGGGVALLRARSALRG-LKGANADETAGIDIVRRALEEPLRQ 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 451 LAENAGLDTVEMLVKVisehKNRGLGIGIDVFEGKPADMLEKGIIEPLRVKKQAIKSASEAAIMILRIDDVIAAKATKPE 530
Cdd:PRK12850 454 IATNAGFEGSVVVGKV----AELPGNFGFNAQTGEYGDMVEAGIIDPAKVTRTALQDAASIAALLITTEAMVAEAPKKAA 529
|
|
| groEL |
CHL00093 |
chaperonin GroEL |
34-528 |
1.38e-20 |
|
chaperonin GroEL
Pssm-ID: 177025 Cd Length: 529 Bit Score: 95.17 E-value: 1.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 34 IIAETVRTTLGPKGMDKMLVDSLGDIVVTNDCATILDKIDLQHPAAKMMVEV-----AKTQDKeAGDGTTTAVVIAGELL 108
Cdd:CHL00093 21 ILAEAVSVTLGPKGRNVVLEKKYGSPQIVNDGVTIAKEIELEDHIENTGVALirqaaSKTNDV-AGDGTTTATVLAYAIV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 109 RKAEELLDQNIHPSIITKGYALAAEKAQEILDEIAIRVDpdDEETLLKIAATSiTGKNAEshkelLAKLAVEAVKQVAek 188
Cdd:CHL00093 100 KQGMKNVAAGANPISLKRGIEKATQYVVSQIAEYARPVE--DIQAITQVASIS-AGNDEE-----VGSMIADAIEKVG-- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 189 KDGkyVVDLDNIKfekkagEGVEESELVRGVVIDKEVVHP-------RMPKRVENAKIALinealevkkteTDAKINITS 261
Cdd:CHL00093 170 REG--VISLEEGK------STVTELEITEGMRFEKGFISPyfvtdteRMEVVQENPYILL-----------TDKKITLVQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 262 PDqLMSFLEQeekmlkdmvdhIAQTGANVVFVQKGIDD--LAQHYLAKY-GIMAVRRV--------KKSDMEKLAKATGA 330
Cdd:CHL00093 231 QD-LLPILEQ-----------VTKTKRPLLIIAEDVEKeaLATLVLNKLrGIVNVVAVrapgfgdrRKAMLEDIAILTGG 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 331 KIVT-----NVKDLTPEDLGYAEVVEERKlaGENMIFVEG--------CKNPK--------------------------A 371
Cdd:CHL00093 299 QVITedaglSLETIQLDLLGQARRIIVTK--DSTTIIADGneeqvkarCEQLRkqieiadssyekeklqerlaklsggvA 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 372 VtILIRGGTEHVIDEVERALEDAVKVVKDVMEDGAVlPAGGAPEIELAIRLDEYAKQ-VGGKEALAIENFADALKIIPKT 450
Cdd:CHL00093 377 V-IKVGAATETEMKDKKLRLEDAINATKAAVEEGIV-PGGGATLVHLSENLKTWAKNnLKEDELIGALIVARAILAPLKR 454
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
1Q2V_B 451 LAENAGLDTVEMLVKVisehKNRGLGIGIDVFEGKPADMLEKGIIEPLRVKKQAIKSASEAAIMILRIDDVIAAKATK 528
Cdd:CHL00093 455 IAENAGKNGSVIIEKV----QEQDFEIGYNAANNKFVNMYEAGIIDPAKVTRSALQNAASIASMILTTECIIVDKKES 528
|
|
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
34-530 |
2.14e-18 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 88.26 E-value: 2.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 34 IIAETVRTTLGPKGMDKMLVDSLGDIVVTNDCATILDKIDLQHP----AAKMMVEVA-KTQDKeAGDGTTTAVVIAGELL 108
Cdd:PRK00013 21 KLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDPfenmGAQLVKEVAsKTNDV-AGDGTTTATVLAQAIV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 109 RKAEELLDQNIHPSIITKGYALAAEKAQEILDEIAIRVDPDDEetllkIAAT-SITGKNAESHKELLAklavEAVKQVAe 187
Cdd:PRK00013 100 REGLKNVAAGANPMDLKRGIDKAVEAAVEELKKISKPVEDKEE-----IAQVaTISANGDEEIGKLIA----EAMEKVG- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 188 kKDGKYVVDldnikfEKKAGEgvEESELVRGVVIDKEVVHP-------RMPKRVENAKIaLInealevkkteTDAKINit 260
Cdd:PRK00013 170 -KEGVITVE------ESKGFE--TELEVVEGMQFDRGYLSPyfvtdpeKMEAELENPYI-LI----------TDKKIS-- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 261 SPDQLMSFLEQeekmlkdmvdhIAQTGANVVFVQKGIDDLAQHYLAK---YGIMAVRRVK--------KSDMEKLAKATG 329
Cdd:PRK00013 228 NIQDLLPVLEQ-----------VAQSGKPLLIIAEDVEGEALATLVVnklRGTLKVVAVKapgfgdrrKAMLEDIAILTG 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 330 AKIVT-----NVKDLTPEDLGYAEVVEERKlagENMIFVEGCKNPKAVT------------------------------- 373
Cdd:PRK00013 297 GTVISeelglKLEDATLEDLGQAKKVVVTK---DNTTIVDGAGDKEAIKarvaqikaqieettsdydreklqerlaklag 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 374 ----ILIRGGTEHVIDEVERALEDAVKVVKDVMEDGaVLPAGGAPEIELAIRLDEyAKQVGGKEALAIENFADALKIIPK 449
Cdd:PRK00013 374 gvavIKVGAATEVEMKEKKDRVEDALHATRAAVEEG-IVPGGGVALLRAAPALEA-LKGLNGDEATGINIVLRALEAPLR 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 450 TLAENAGLDTVEMLVKVISEHknrGLGIGIDVFEGKPADMLEKGIIEPLRVKKQAIKSASEAAIMILRIDDVIaakATKP 529
Cdd:PRK00013 452 QIAENAGLEGSVVVEKVKNGK---GKGYGYNAATGEYVDMIEAGIIDPTKVTRSALQNAASVAGLLLTTEAVV---ADKP 525
|
.
1Q2V_B 530 E 530
Cdd:PRK00013 526 E 526
|
|
| PRK14104 |
PRK14104 |
chaperonin GroEL; Provisional |
21-523 |
2.95e-18 |
|
chaperonin GroEL; Provisional
Pssm-ID: 172594 Cd Length: 546 Bit Score: 87.78 E-value: 2.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 21 GRDAQRLNILAARIIAETVRTTLGPKGMDKMLVDSLGDIVVTNDCATILDKIDL----QHPAAKMMVEVAKTQDKEAGDG 96
Cdd:PRK14104 9 GVDARDRMLRGVDILANAVKVTLGPKGRNVVLDKSFGAPRITKDGVTVAKEIELedkfENMGAQMVREVASKSADAAGDG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 97 TTTAVVIAGELLRKAEELLDQNIHPSIITKGYALAAEKAQEILDEIAIRVDPDDEetllkIAATSITGKNAESHkelLAK 176
Cdd:PRK14104 89 TTTATVLAQAIVREGAKSVAAGMNPMDLKRGIDLAVEAVVADLVKNSKKVTSNDE-----IAQVGTISANGDAE---IGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 177 LAVEAVKQVAekKDGKYVVDldnikfEKKAGEgvEESELVRGVVIDKEVVHP-------RMPKRVENAKIaLINEAlevk 249
Cdd:PRK14104 161 FLADAMKKVG--NEGVITVE------EAKSLE--TELDVVEGMQFDRGYISPyfvtnadKMRVEMDDAYI-LINEK---- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 250 ktetdakiNITSPDQLMSFLEQeekmlkdmvdhIAQTGANVVFVQKGIDDLAQHYLAK---YGIMAVRRVK--------K 318
Cdd:PRK14104 226 --------KLSSLNELLPLLEA-----------VVQTGKPLVIVAEDVEGEALATLVVnrlRGGLKVAAVKapgfgdrrK 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 319 SDMEKLAKATGAKIVT-----NVKDLTPEDLGYAEVVEERKlagENMIFVEGCKNPKAV--------------------- 372
Cdd:PRK14104 287 AMLQDIAILTGGQAISedlgiKLENVTLQMLGRAKKVMIDK---ENTTIVNGAGKKADIearvaqikaqieettsdydre 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 373 --------------TILIRGGTEHVIDEVERALEDAVKVVKDVMEDGaVLPAGGAPEIELAIRLDEYAKQvGGKEALAIE 438
Cdd:PRK14104 364 klqerlaklaggvaVIRVGGATEVEVKERKDRVDDAMHATRAAVEEG-IVPGGGVALLRASEQLKGIKTK-NDDQKTGVE 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 439 NFADALKIIPKTLAENAGLDTVEMLVKVISEHKnrgLGIGIDVFEGKPADMLEKGIIEPLRVKKQAIKSASEAAIMILRI 518
Cdd:PRK14104 442 IVRKALSAPARQIAINAGEDGSVIVGKILEKEQ---YSYGFDSQTGEYGNLVSKGIIDPTKVVRTAIQNAASVAALLITT 518
|
....*
1Q2V_B 519 DDVIA 523
Cdd:PRK14104 519 EAMVA 523
|
|
| groEL |
PRK12852 |
chaperonin GroEL; Reviewed |
23-528 |
1.48e-15 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237232 Cd Length: 545 Bit Score: 79.50 E-value: 1.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 23 DAQRLNILAARIIAETVRTTLGPKGMDKMLVDSLGDIVVTNDCATILDKIDL----QHPAAKMMVEVAKTQDKEAGDGTT 98
Cdd:PRK12852 11 DARDRMLRGVDILANAVKVTLGPKGRNVVIEKSFGAPRITKDGVTVAKEIELedkfENMGAQMVREVASKTNDLAGDGTT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 99 TAVVIAGELLRKAEELLDQNIHPSIITKGYALAAEKaqeILDEIAIRVDP-DDEETLLKIAATSITGKNAeshkelLAKL 177
Cdd:PRK12852 91 TATVLAQAIVREGAKAVAAGMNPMDLKRGIDIAVAA---VVKDIEKRAKPvASSAEIAQVGTISANGDAA------IGKM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 178 AVEAVKQVAekKDGKYVVDldnikfEKKAGEgvEESELVRGVVIDKEVVHPRMpkrVENAKialinealevkktetdaKI 257
Cdd:PRK12852 162 IAQAMQKVG--NEGVITVE------ENKSLE--TEVDIVEGMKFDRGYLSPYF---VTNAE-----------------KM 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 258 NITSPDQLMSFLEQEEKMLKDMV---DHIAQTGANVVFVQKGIDDLAQHYLA---KYGIMAVRRVK--------KSDMEK 323
Cdd:PRK12852 212 TVELDDAYILLHEKKLSGLQAMLpvlEAVVQSGKPLLIIAEDVEGEALATLVvnrLRGGLKVAAVKapgfgdrrKAMLED 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 324 LAKATGAKIVTN-----VKDLTPEDLGYAEVVEERKlagENMIFVEGCKNPKAV-------------------------- 372
Cdd:PRK12852 292 IAILTGGQLISEdlgikLENVTLKMLGRAKKVVIDK---ENTTIVNGAGKKADIearvgqikaqieettsdydreklqer 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 373 ---------TILIRGGTEHVIDEVERALEDAVKVVKDVMEDGaVLPAGGAPEIELAIRLDEYAKQVGGKEAlAIENFADA 443
Cdd:PRK12852 369 laklaggvaVIRVGGATEVEVKEKKDRVEDALNATRAAVQEG-IVPGGGVALLRAKKAVGRINNDNADVQA-GINIVLKA 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 444 LKIIPKTLAENAGLDTVEMLVKVISehkNRGLGIGIDVFEGKPADMLEKGIIEPLRVKKQAIKSASEAAIMILRIDDVIA 523
Cdd:PRK12852 447 LEAPIRQIAENAGVEGSIVVGKILE---NKSETFGFDAQTEEYVDMVAKGIIDPAKVVRTALQDAASVAGLLVTTEAMVA 523
|
....*
1Q2V_B 524 AKATK 528
Cdd:PRK12852 524 ELPKK 528
|
|
| PLN03167 |
PLN03167 |
Chaperonin-60 beta subunit; Provisional |
17-530 |
9.58e-15 |
|
Chaperonin-60 beta subunit; Provisional
Pssm-ID: 215611 [Multi-domain] Cd Length: 600 Bit Score: 76.89 E-value: 9.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 17 QRYVGRDAQRLNILAARI--IAETVRTTLGPKGMDKMLVDSLGDIVVTNDCATILDKIDLQHP----AAKMMVEVAKTQD 90
Cdd:PLN03167 58 ELHFNKDGSAIKKLQAGVnkLADLVGVTLGPKGRNVVLESKYGSPKIVNDGVTVAKEVELEDPveniGAKLVRQAAAKTN 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 91 KEAGDGTTTAVVIAGELLRKAEELLDQNIHPSIITKGYALAAEKAQEILDEIAIRVdpDDEEtLLKIAATSiTGKNAEsh 170
Cdd:PLN03167 138 DLAGDGTTTSVVLAQGLIAEGVKVVAAGANPVQITRGIEKTAKALVKELKKMSKEV--EDSE-LADVAAVS-AGNNYE-- 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 171 kelLAKLAVEAVKQVAEKKdgkyVVDLDNIKFEKKAGEGVEESELVRGVVIDKEVVHP-RMPKRVENAKIAL----INEA 245
Cdd:PLN03167 212 ---VGNMIAEAMSKVGRKG----VVTLEEGKSAENNLYVVEGMQFDRGYISPYFVTDSeKMSVEYDNCKLLLvdkkITNA 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 246 LEVKKTETDAkINITSPDQLMSFLEQEEKMLKDMVDHIAQTGANVVFVQKGIDDLAQHYLAKYGIMAVRRVKKSD----M 321
Cdd:PLN03167 285 RDLIGILEDA-IRGGYPLLIIAEDIEQEALATLVVNKLRGSLKIAALKAPGFGERKSQYLDDIAILTGGTVIREEvglsL 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 322 EKLAK---ATGAKIVTNvKDLTP--EDLGYAEVVEERKLAGENMIFVEGCKNPK-------------AVTILIRGGTEHV 383
Cdd:PLN03167 364 DKVGKevlGTAAKVVLT-KDTTTivGDGSTQEAVNKRVAQIKNLIEAAEQDYEKeklneriaklsggVAVIQVGAQTETE 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q2V_B 384 IDEVERALEDAVKVVKDVMEDGAVLpAGGAPEIELAIRLDEYAKQVGGKE-ALAIENFADALKIIPKTLAENAGLDTVEM 462
Cdd:PLN03167 443 LKEKKLRVEDALNATKAAVEEGIVV-GGGCTLLRLASKVDAIKDTLENDEqKVGADIVKRALSYPLKLIAKNAGVNGSVV 521
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
1Q2V_B 463 LVKVISehkNRGLGIGIDVFEGKPADMLEKGIIEPLRVKKQAIKSASEAAIMILrIDDVIAAKATKPE 530
Cdd:PLN03167 522 SEKVLS---NDNPKFGYNAATGKYEDLMAAGIIDPTKVVRCCLEHAASVAKTFL-TSDCVVVEIKEPE 585
|
|
| |
