|
Name |
Accession |
Description |
Interval |
E-value |
| thermosome_beta |
NF041083 |
thermosome subunit beta; |
14-546 |
0e+00 |
|
thermosome subunit beta;
Pssm-ID: 469010 Cd Length: 519 Bit Score: 873.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 14 VPVLILKEGTQRTYGREALRTNIMIVRAIAETLRTTYGPKGMDKMLVDSLGDITITNDGATILDKMDVQHPTAKLVVQIA 93
Cdd:NF041083 1 QPVLILKEGTQRTKGRDAQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDIVITNDGATILKEMDVQHPAAKMLVEVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 94 KGQDEEVGDGTKTAVIFAGELLRYAEELLDKNVHPTIIVSGYKKAAEEAVKKLHEIAEPIDINDEETLKKIAMTSLTSKA 173
Cdd:NF041083 81 KTQDDEVGDGTTTAVVLAGELLKKAEELLDQNIHPTIIANGYRLAAEKAIEILDEIAEKVDPDDRETLKKIAETSLTSKG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 174 VHGAREHLAEIVVKAVRQVAEKRGDKWYIDLDAIQIIKKHGGSLRDTKLIYGIVLDKEVVHPGMPKKVENAYIVLLDAPL 253
Cdd:NF041083 161 VEEARDYLAEIAVKAVKQVAEKRDGKYYVDLDNIQIEKKHGGSIEDTQLIYGIVIDKEVVHPGMPKRVENAKIALLDAPL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 254 EVEKPEIDAEIRINDPAFLKKFLEEEEKILEEMVNKIYNVAMErirkdgmegkagiVVITQKGIDEVAQHFLAKKGIMAV 333
Cdd:NF041083 241 EVKKTEIDAEIRITDPDQLQKFLDQEEKMLKEMVDKIKATGAN-------------VVFCQKGIDDLAQHYLAKAGILAV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 334 RRVKRSDIEKIARATGAKIVSNIDDLTPEDLGFAKLVEERKVGEDKMVFIEGCPNPRAVTILIRGGLERLVDEAERSIND 413
Cdd:NF041083 308 RRVKKSDMEKLAKATGARIVTNIDDLTPEDLGYAELVEERKVGDDKMVFVEGCKNPKAVTILIRGGTEHVVDEAERALED 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 414 ALHAVADAIRDGKIVAGGGAVEVEVAKYLREIAPKIGGKEQLAVEAFARALEGLPMALAENAGLEPVEIIMKLRAAHAKa 493
Cdd:NF041083 388 ALSVVADAVEDGKIVAGGGAPEVELAKRLREYAATVGGREQLAVEAFAEALEIIPRTLAENAGLDPIDILVKLRSAHEK- 466
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 500145658 494 EGKWVGVNVFKGDVDDMKKLGVIEPVSVKANAIKAGTEAATMVLRIDDIIAAA 546
Cdd:NF041083 467 GKKWAGINVFTGEVVDMWELGVIEPLRVKTQAIKSATEAATMILRIDDVIAAK 519
|
|
| cpn60 |
cd03343 |
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ... |
16-546 |
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: 800.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 16 VLILKEGTQRTYGREALRTNIMIVRAIAETLRTTYGPKGMDKMLVDSLGDITITNDGATILDKMDVQHPTAKLVVQIAKG 95
Cdd:cd03343 1 VLILKEGTQRTSGRDAQRMNIAAAKAVAEAVRTTLGPKGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 96 QDEEVGDGTKTAVIFAGELLRYAEELLDKNVHPTIIVSGYKKAAEEAVKKLHEIAEPIDINDEETLKKIAMTSLTSKAVH 175
Cdd:cd03343 81 QDEEVGDGTTTAVVLAGELLEKAEDLLDQNIHPTVIIEGYRLAAEKALELLDEIAIKVDPDDKDTLRKIAKTSLTGKGAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 176 GAREHLAEIVVKAVRQVAEKRGDKWYIDLDAIQIIKKHGGSLRDTKLIYGIVLDKEVVHPGMPKKVENAYIVLLDAPLEV 255
Cdd:cd03343 161 AAKDKLADLVVDAVLQVAEKRDGKYVVDLDNIKIEKKTGGSVDDTELIRGIVIDKEVVHPGMPKRVENAKIALLDAPLEV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 256 EKPEIDAEIRINDPAFLKKFLEEEEKILEEMVNKIYNVAMErirkdgmegkagiVVITQKGIDEVAQHFLAKKGIMAVRR 335
Cdd:cd03343 241 KKTEIDAKIRITSPDQLQAFLEQEEAMLKEMVDKIADTGAN-------------VVFCQKGIDDLAQHYLAKAGILAVRR 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 336 VKRSDIEKIARATGAKIVSNIDDLTPEDLGFAKLVEERKVGEDKMVFIEGCPNPRAVTILIRGGLERLVDEAERSINDAL 415
Cdd:cd03343 308 VKKSDMEKLARATGAKIVTNIDDLTPEDLGEAELVEERKVGDDKMVFVEGCKNPKAVTILLRGGTEHVVDELERALEDAL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 416 HAVADAIRDGKIVAGGGAVEVEVAKYLREIAPKIGGKEQLAVEAFARALEGLPMALAENAGLEPVEIIMKLRAAHAKaEG 495
Cdd:cd03343 388 RVVADALEDGKVVAGGGAVEIELAKRLREYARSVGGREQLAVEAFADALEEIPRTLAENAGLDPIDTLVELRAAHEK-GN 466
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 500145658 496 KWVGVNVFKGDVDDMKKLGVIEPVSVKANAIKAGTEAATMVLRIDDIIAAA 546
Cdd:cd03343 467 KNAGLDVYTGEVVDMLEKGVIEPLRVKKQAIKSATEAATMILRIDDVIAAK 517
|
|
| thermosome_alpha |
NF041082 |
thermosome subunit alpha; |
14-546 |
0e+00 |
|
thermosome subunit alpha;
Pssm-ID: 469009 Cd Length: 518 Bit Score: 787.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 14 VPVLILKEGTQRTYGREALRTNIMIVRAIAETLRTTYGPKGMDKMLVDSLGDITITNDGATILDKMDVQHPTAKLVVQIA 93
Cdd:NF041082 1 QPILILKEGTQRTSGRDAQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDVVITNDGVTILKEMDIEHPAAKMIVEVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 94 KGQDEEVGDGTKTAVIFAGELLRYAEELLDKNVHPTIIVSGYKKAAEEAVKKLHEIAEPIDINDEETLKKIAMTSLTSKA 173
Cdd:NF041082 81 KTQDDEVGDGTTTAVVLAGELLKKAEELLDQDIHPTIIAEGYRLAAEKALEILDEIAIKVDPDDKETLKKIAATAMTGKG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 174 VHGAREHLAEIVVKAVRQVAEKRGDkWYIDLDAIQIIKKHGGSLRDTKLIYGIVLDKEVVHPGMPKKVENAYIVLLDAPL 253
Cdd:NF041082 161 AEAAKDKLADLVVDAVKAVAEKDGG-YNVDLDNIKVEKKVGGSIEDSELVEGVVIDKERVHPGMPKRVENAKIALLDAPL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 254 EVEKPEIDAEIRINDPAFLKKFLEEEEKILEEMVNKIYNVAMErirkdgmegkagiVVITQKGIDEVAQHFLAKKGIMAV 333
Cdd:NF041082 240 EVKKTEIDAKISITDPDQLQAFLDQEEKMLKEMVDKIADSGAN-------------VVFCQKGIDDLAQHYLAKEGILAV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 334 RRVKRSDIEKIARATGAKIVSNIDDLTPEDLGFAKLVEERKVGEDKMVFIEGCPNPRAVTILIRGGLERLVDEAERSIND 413
Cdd:NF041082 307 RRVKKSDMEKLAKATGARIVTSIDDLSPEDLGYAGLVEERKVGGDKMIFVEGCKNPKAVTILLRGGTEHVVDEVERALED 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 414 ALHAVADAIRDGKIVAGGGAVEVEVAKYLREIAPKIGGKEQLAVEAFARALEGLPMALAENAGLEPVEIIMKLRAAHAKA 493
Cdd:NF041082 387 ALRVVRVVLEDGKVVAGGGAPEVELALRLREYAASVGGREQLAIEAFAEALEIIPRTLAENAGLDPIDALVELRSAHEKG 466
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 500145658 494 EgKWVGVNVFKGDVDDMKKLGVIEPVSVKANAIKAGTEAATMVLRIDDIIAAA 546
Cdd:NF041082 467 N-KTAGLDVYTGKVVDMLEIGVVEPLRVKTQAIKSATEAAVMILRIDDVIAAA 518
|
|
| thermosome_arch |
TIGR02339 |
thermosome, various subunits, archaeal; Thermosome is the name given to the archaeal rather ... |
15-545 |
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: 768.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 15 PVLILKEGTQRTYGREALRTNIMIVRAIAETLRTTYGPKGMDKMLVDSLGDITITNDGATILDKMDVQHPTAKLVVQIAK 94
Cdd:TIGR02339 1 PVFILKEGTQRTSGRDAQRNNIAAAKAVAEAVKSTLGPRGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 95 GQDEEVGDGTKTAVIFAGELLRYAEELLDKNVHPTIIVSGYKKAAEEAVKKLHEIAEPIDINDEETLKKIAMTSLTSKAV 174
Cdd:TIGR02339 81 TQDEEVGDGTTTAVVLAGELLEKAEDLLEQDIHPTVIIEGYRKAAEKALEIIDEIATKISPEDRDLLKKIAYTSLTSKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 175 HG-AREHLAEIVVKAVRQVAEKRGD-KWYIDLDAIQIIKKHGGSLRDTKLIYGIVLDKEVVHPGMPKKVENAYIVLLDAP 252
Cdd:TIGR02339 161 AEvAKDKLADLVVEAVKQVAELRGDgKYYVDLDNIKIVKKKGGSIEDTELVEGIVVDKEVVHPGMPKRVENAKIALLDAP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 253 LEVEKPEIDAEIRINDPAFLKKFLEEEEKILEEMVNKIYNVAMErirkdgmegkagiVVITQKGIDEVAQHFLAKKGIMA 332
Cdd:TIGR02339 241 LEVEKTEIDAKIRITDPDQIKKFLDQEEAMLKEMVDKIASAGAN-------------VVICQKGIDDVAQHYLAKAGILA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 333 VRRVKRSDIEKIARATGAKIVSNIDDLTPEDLGFAKLVEERKVGEDKMVFIEGCPNPRAVTILIRGGLERLVDEAERSIN 412
Cdd:TIGR02339 308 VRRVKKSDIEKLARATGARIVSSIDEITESDLGYAELVEERKVGEDKMVFVEGCKNPKAVTILLRGGTEHVVDELERSIQ 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 413 DALHAVADAIRDGKIVAGGGAVEVEVAKYLREIAPKIGGKEQLAVEAFARALEGLPMALAENAGLEPVEIIMKLRAAHAK 492
Cdd:TIGR02339 388 DALHVVANALEDGKIVAGGGAVEIELALRLRSYARSVGGREQLAIEAFADALEEIPRILAENAGLDPIDALVDLRAKHEK 467
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 500145658 493 AEgKWVGVNVFKGDVDDMKKLGVIEPVSVKANAIKAGTEAATMVLRIDDIIAA 545
Cdd:TIGR02339 468 GN-KNAGINVFTGEIEDMLELGVIEPLRVKEQAIKSATEAATMILRIDDVIAA 519
|
|
| chaperonin_type_I_II |
cd00309 |
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ... |
23-544 |
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: 618.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 23 TQRTYGREALRTNIMIVRAIAETLRTTYGPKGMDKMLVDSLGDITITNDGATILDKMDVQHPTAKLVVQIAKGQDEEVGD 102
Cdd:cd00309 1 KEREFGEEARLSNINAAKALADAVKTTLGPKGMDKMLVDSLGDPTITNDGATILKEIEVEHPAAKLLVEVAKSQDDEVGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 103 GTKTAVIFAGELLRYAEELLDKNVHPTIIVSGYKKAAEEAVKKLHEIAEPIDINDEETLKKIAMTSLTSKAVHGAREHLA 182
Cdd:cd00309 81 GTTTVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVPIDVEDREELLKVATTSLNSKLVSGGDDFLG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 183 EIVVKAVRQVAEKRGDkwyIDLDAIQIIKKHGGSLRDTKLIYGIVLDKEVVHPGMPKKVENAYIVLLDAPLEvekpeida 262
Cdd:cd00309 161 ELVVDAVLKVGKENGD---VDLGVIRVEKKKGGSLEDSELVVGMVFDKGYLSPYMPKRLENAKILLLDCKLE-------- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 263 eirindpaflkkfleeeekileemvnkiynvamerirkdgmegkagIVVITQKGIDEVAQHFLAKKGIMAVRRVKRSDIE 342
Cdd:cd00309 230 ----------------------------------------------YVVIAEKGIDDEALHYLAKLGIMAVRRVRKEDLE 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 343 KIARATGAKIVSNIDDLTPEDLGFAKLVEERKVGEDKMVFIEGCPNPRAVTILIRGGLERLVDEAERSINDALHAVADAI 422
Cdd:cd00309 264 RIAKATGATIVSRLEDLTPEDLGTAGLVEETKIGDEKYTFIEGCKGGKVATILLRGATEVELDEAERSLHDALCAVRAAV 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 423 RDGKIVAGGGAVEVEVAKYLREIAPKIGGKEQLAVEAFARALEGLPMALAENAGLEPVEIIMKLRAAHAKaEGKWVGVNV 502
Cdd:cd00309 344 EDGGIVPGGGAAEIELSKALEELAKTLPGKEQLGIEAFADALEVIPRTLAENAGLDPIEVVTKLRAKHAE-GGGNAGGDV 422
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 500145658 503 FKGDVDDMKKLGVIEPVSVKANAIKAGTEAATMVLRIDDIIA 544
Cdd:cd00309 423 ETGEIVDMKEAGIIDPLKVKRQALKSATEAASLILTIDDIIV 464
|
|
| Cpn60_TCP1 |
pfam00118 |
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ... |
42-545 |
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: 598.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 42 IAETLRTTYGPKGMDKMLVDSLGDITITNDGATILDKMDVQHPTAKLVVQIAKGQDEEVGDGTKTAVIFAGELLRYAEEL 121
Cdd:pfam00118 1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELEIQHPAAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEEAEKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 122 LDKNVHPTIIVSGYKKAAEEAVKKLHEIAE-PIDINDEETLKKIAMTSLTSKAVHGAREHLAEIVVKAVRQVAEKRGDkw 200
Cdd:pfam00118 81 LAAGVHPTTIIEGYEKALEKALEILDSIISiPVEDVDREDLLKVARTSLSSKIISRESDFLAKLVVDAVLAIPKNDGS-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 201 yIDLDAIQIIKKHGGSLRDTKLIYGIVLDKEVVHPGMPKKVENAYIVLLDAPLEVEKPEIDAEIRINDPAFLKKFLEEEE 280
Cdd:pfam00118 159 -FDLGNIGVVKILGGSLEDSELVDGVVLDKGPLHPDMPKRLENAKVLLLNCSLEYEKTETKATVVLSDAEQLERFLKAEE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 281 KILEEMVNKIYnvamerirkdgmegKAGI-VVITQKGIDEVAQHFLAKKGIMAVRRVKRSDIEKIARATGAKIVSNIDDL 359
Cdd:pfam00118 238 EQILEIVEKII--------------DSGVnVVVCQKGIDDLALHFLAKNGIMALRRVKKRDLERLAKATGARAVSSLDDL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 360 TPEDLGFAKLVEERKVGEDKMVFIEGCPNPRAVTILIRGGLERLVDEAERSINDALHAVADAIRDGKIVAGGGAVEVEVA 439
Cdd:pfam00118 304 TPDDLGTAGKVEEEKIGDEKYTFIEGCKSPKAATILLRGATDHVLDEIERSIHDALCVVKNAIEDPRVVPGGGAVEMELA 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 440 KYLREIAPKIGGKEQLAVEAFARALEGLPMALAENAGLEPVEIIMKLRAAHAKAEgKWVGVNVFKGDVDDMKKLGVIEPV 519
Cdd:pfam00118 384 RALREYAKSVSGKEQLAIEAFAEALEVIPKTLAENAGLDPIEVLAELRAAHASGE-KHAGIDVETGEIIDMKEAGVVDPL 462
|
490 500
....*....|....*....|....*.
gi 500145658 520 SVKANAIKAGTEAATMVLRIDDIIAA 545
Cdd:pfam00118 463 KVKRQALKSATEAASTILRIDDIIKA 488
|
|
| TCP1_epsilon |
cd03339 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ... |
13-544 |
1.84e-175 |
|
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: 506.45 E-value: 1.84e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 13 GVPVLILKEGTQ--RTYGREALRTNIMIVRAIAETLRTTYGPKGMDKMLVDSLGDITITNDGATILDKMDVQHPTAKLVV 90
Cdd:cd03339 4 GRPFIIVREQEKkkRLKGLEAHKSHILAAKSVANILRTSLGPRGMDKILVSPDGEVTVTNDGATILEKMDVDHQIAKLLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 91 QIAKGQDEEVGDGTKTAVIFAGELLRYAEELLDKNVHPTIIVSGYKKAAEEAVKKLHEIAEPIDI--NDEETLKKIAMTS 168
Cdd:cd03339 84 ELSKSQDDEIGDGTTGVVVLAGALLEQAEKLLDRGIHPIRIADGYEQACKIAVEHLEEIADKIEFspDNKEPLIQTAMTS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 169 LTSKAVHGAREHLAEIVVKAVRQVAE-KRGDkwyIDLDAIQIIKKHGGSLRDTKLIYGIVLDKEVVHPGMPKKVENAYIV 247
Cdd:cd03339 164 LGSKIVSRCHRQFAEIAVDAVLSVADlERKD---VNFELIKVEGKVGGRLEDTKLVKGIVIDKDFSHPQMPKEVKDAKIA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 248 LLDAPLEVEKPEIDAEIRINDPAFLKKFLEEEEKILEEMVnkiynvamERIRKDGMEgkagiVVITQKGIDEVAQHFLAK 327
Cdd:cd03339 241 ILTCPFEPPKPKTKHKLDITSVEDYKKLQEYEQKYFREMV--------EQVKDAGAN-----LVICQWGFDDEANHLLLQ 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 328 KGIMAVRRVKRSDIEKIARATGAKIVSNIDDLTPEDLGFAKLVEERKVG--EDKMVFIEGCPNPRAVTILIRGGLERLVD 405
Cdd:cd03339 308 NGLPAVRWVGGVEIELIAIATGGRIVPRFEDLSPEKLGKAGLVREISFGttKDKMLVIEGCPNSKAVTIFIRGGNKMIIE 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 406 EAERSINDALHAVADAIRDGKIVAGGGAVEVEVAKYLREIAPKIGGKEQLAVEAFARALEGLPMALAENAGLEPVEIIMK 485
Cdd:cd03339 388 EAKRSLHDALCVVRNLIRDNRIVYGGGAAEISCSLAVEKAADKCSGIEQYAMRAFADALESIPLALAENSGLNPIETLSE 467
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 500145658 486 LRAAHAKAEGKWVGVNVFKGDVDDMKKLGVIEPVSVKANAIKAGTEAATMVLRIDDIIA 544
Cdd:cd03339 468 VKARQVKEKNPHLGIDCLGRGTNDMKEQKVFETLISKKQQILLATQVVKMILKIDDVIV 526
|
|
| GroEL |
COG0459 |
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ... |
27-546 |
7.09e-173 |
|
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227 Cd Length: 497 Bit Score: 498.83 E-value: 7.09e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 27 YGREALRTNIMIVRAIAETLRTTYGPKGMDKMLVDSLGDITITNDGATILDKMDVQHP----TAKLVVQIAKGQDEEVGD 102
Cdd:COG0459 7 FGEDARRANIRGVKALADAVKVTLGPKGRNVMLVKSFGDPTITNDGVTIAKEIELEDPfenmGAQLVKEVASKTNDEAGD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 103 GTKTAVIFAGELLRYAEELLDKNVHPTIIVSGYKKAAEEAVKKLHEIAEPIDinDEETLKKIAMTSLTSKavhgarEHLA 182
Cdd:COG0459 87 GTTTATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPVD--DKEELAQVATISANGD------EEIG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 183 EIVVKAVRQVaekrGDKWYIdldaiqIIKKHGGSLRDTKLIYGIVLDKEVVHPG-------MPKKVENAYIVLLDAPLEV 255
Cdd:COG0459 159 ELIAEAMEKV----GKDGVI------TVEEGKGLETELEVVEGMQFDKGYLSPYfvtdpekMPAELENAYILLTDKKISS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 256 EKPeidaeirindpafLKKfleeeekileeMVNKIynvamerirkdgmeGKAGI-VVITQKGIDEVAQHFLAKKGIMAVR 334
Cdd:COG0459 229 IQD-------------LLP-----------LLEKV--------------AQSGKpLLIIAEDIDGEALATLVVNGIRGVL 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 335 RV-----------KRSDIEKIARATGAKIVSN-----IDDLTPEDLGFAKLVEerkVGEDKMVFIEGCPNPRAVTILIRG 398
Cdd:COG0459 271 RVvavkapgfgdrRKAMLEDIAILTGGRVISEdlglkLEDVTLDDLGRAKRVE---VDKDNTTIVEGAGNPKAIVILVGA 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 399 GLERLVDEAERSINDALHAVADAIRDGkIVAGGGAVEVEVAKYLREIAPKIGGKEQLAVEAFARALEGLPMALAENAGLE 478
Cdd:COG0459 348 ATEVEVKERKRRVEDALHATRAAVEEG-IVPGGGAALLRAARALRELAAKLEGDEQLGIEIVARALEAPLRQIAENAGLD 426
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500145658 479 PVEIIMKLRAahakAEGKWVGVNVFKGDVDDMKKLGVIEPVSVKANAIKAGTEAATMVLRIDDIIAAA 546
Cdd:COG0459 427 GSVVVEKVRA----AKDKGFGFDAATGEYVDMLEAGVIDPAKVKRSALQNAASVAGLILTTEAVIADK 490
|
|
| TCP1_eta |
cd03340 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ... |
15-543 |
4.46e-160 |
|
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: 467.15 E-value: 4.46e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 15 PVLILKEGTQRTYGREALRTNIMIVRAIAETLRTTYGPKGMDKMLVDSLGDITITNDGATILDKMDVQHPTAKLVVQIAK 94
Cdd:cd03340 1 PIILLKEGTDTSQGKGQLISNINACQAIADAVRTTLGPRGMDKLIVDGRGKVTISNDGATILKLLDIVHPAAKTLVDIAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 95 GQDEEVGDGTKTAVIFAGELLRYAEELLDKNVHPTIIVSGYKKAAEEAVKKLHEIAEPIDINDE----ETLKKIAMTSLT 170
Cdd:cd03340 81 SQDAEVGDGTTSVVVLAGEFLKEAKPFIEDGVHPQIIIRGYRKALQLAIEKIKEIAVNIDKEDKeeqrELLEKCAATALN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 171 SKAVHGAREHLAEIVVKAVRQVAEKrgdkwyIDLDAIQIIKKHGGSLRDTKLIYGIVLDKEVVHPGM---PKKVENAYIV 247
Cdd:cd03340 161 SKLIASEKEFFAKMVVDAVLSLDDD------LDLDMIGIKKVPGGSLEDSQLVNGVAFKKTFSYAGFeqqPKKFKNPKIL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 248 LLDAPLEVEKPEIDAEIRINDPaflKKFLEEEEKILEEMVNKiynvaMERIRKDGMEgkagiVVITQKGIDEVAQHFLAK 327
Cdd:cd03340 235 LLNVELELKAEKDNAEVRVEDP---EEYQAIVDAEWKIIYDK-----LEKIVKSGAN-----VVLSKLPIGDLATQYFAD 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 328 KGIMAVRRVKRSDIEKIARATGAKIVSNIDDLTPEDLGFAKLVEERKVGEDKMVFIEGCPNPRAVTILIRGGLERLVDEA 407
Cdd:cd03340 302 RDIFCAGRVPEEDLKRVAQATGGSIQTTVSNITDDVLGTCGLFEERQVGGERYNIFTGCPKAKTCTIILRGGAEQFIEEA 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 408 ERSINDALHAVADAIRDGKIVAGGGAVEVEVAKYLREIAPKIGGKEQLAVEAFARALEGLPMALAENAGLEPVEIIMKLR 487
Cdd:cd03340 382 ERSLHDAIMIVRRAIKNDSVVAGGGAIEMELSKYLRDYSRTIAGKQQLVINAFAKALEIIPRQLCDNAGFDATDILNKLR 461
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 500145658 488 AAHAKAEGKWVGVNVFKGDVDDMKKLGVIEPVSVKANAIKAGTEAATMVLRIDDII 543
Cdd:cd03340 462 QKHAQGGGKWYGVDINNEGIADNFEAFVWEPSLVKINALTAATEAACLILSVDETI 517
|
|
| chap_CCT_epsi |
TIGR02343 |
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ... |
8-544 |
1.76e-159 |
|
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: 465.82 E-value: 1.76e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 8 ALEPTGVPVLILKEGTQ--RTYGREALRTNIMIVRAIAETLRTTYGPKGMDKMLVDSLGDITITNDGATILDKMDVQHPT 85
Cdd:TIGR02343 3 AFDEYGRPFIIIKDQDNkkRLKGLEAKKSNIAAAKSVASILRTSLGPKGMDKMLISPDGDITVTNDGATILSQMDVDNQI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 86 AKLVVQIAKGQDEEVGDGTKTAVIFAGELLRYAEELLDKNVHPTIIVSGYKKAAEEAVKKLHEIAEPIDI--NDEETLKK 163
Cdd:TIGR02343 83 AKLMVELSKSQDDEIGDGTTGVVVLAGALLEQAEELLDKGIHPIKIADGFEEAARIAVEHLEEISDEISAdnNNREPLIQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 164 IAMTSLTSKAVHGAREHLAEIVVKAVRQVAEK-RGDkwyIDLDAIQIIKKHGGSLRDTKLIYGIVLDKEVVHPGMPKKVE 242
Cdd:TIGR02343 163 AAKTSLGSKIVSKCHRRFAEIAVDAVLNVADMeRRD---VDFDLIKVEGKVGGSLEDTKLIKGIIIDKDFSHPQMPKEVE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 243 NAYIVLLDAPLEVEKPEIDAEIRINDPAFLKKFLEEEEKILEEMVnkiynvamERIRKDGMEgkagiVVITQKGIDEVAQ 322
Cdd:TIGR02343 240 DAKIAILTCPFEPPKPKTKHKLDISSVEEYKKLQKYEQQKFKEMI--------DDIKKSGAN-----LVICQWGFDDEAN 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 323 HFLAKKGIMAVRRVKRSDIEKIARATGAKIVSNIDDLTPEDLGFAKLVEERKVG--EDKMVFIEGCPNPRAVTILIRGGL 400
Cdd:TIGR02343 307 HLLLQNDLPAVRWVGGQELELIAIATGGRIVPRFQELSKDKLGKAGLVREISFGttKDRMLVIEQCKNSKAVTIFIRGGN 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 401 ERLVDEAERSINDALHAVADAIRDGKIVAGGGAVEVEVAKYLREIAPKIGGKEQLAVEAFARALEGLPMALAENAGLEPV 480
Cdd:TIGR02343 387 KMIIEEAKRSIHDALCVVRNLIKDSRIVYGGGAAEISCSLAVSQEADKYPGVEQYAIRAFADALETIPMALAENSGLDPI 466
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 500145658 481 EIIMKLRAAHAKAEGKWVGVNVFKGDVDDMKKLGVIEPVSVKANAIKAGTEAATMVLRIDDIIA 544
Cdd:TIGR02343 467 GTLSTLKSLQLKEKNPNLGVDCLGYGTNDMKEQFVFETLIGKKQQILLATQLVRMILKIDDVIS 530
|
|
| TCP1_delta |
cd03338 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ... |
34-545 |
1.80e-159 |
|
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.
Pssm-ID: 239454 [Multi-domain] Cd Length: 515 Bit Score: 465.22 E-value: 1.80e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 34 TNIMIVRAIAETLRTTYGPKGMDKMLVDSLGDITITNDGATILDKMDVQHPTAKLVVQIAKGQDEEVGDGTKTAVIFAGE 113
Cdd:cd03338 12 SNIQAAKAVADAIRTSLGPRGMDKMIQTGKGEVIITNDGATILKQMSVLHPAAKMLVELSKAQDIEAGDGTTSVVVLAGA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 114 LLRYAEELLDKNVHPTIIVSGYKKAAEEAVKKLHEIAEPIDINDEETLKKIAMTSLTSKAVHGAREHLAEIVVKAVRQVA 193
Cdd:cd03338 92 LLSACESLLKKGIHPTVISESFQIAAKKAVEILDSMSIPVDLNDRESLIKSATTSLNSKVVSQYSSLLAPIAVDAVLKVI 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 194 EKRGDKwYIDLDAIQIIKKHGGSLRDTKLIYGIVLDKEVVH-PGMPKKVENAYIVLLDAPLEVEKPEIDAEIRINDPAFL 272
Cdd:cd03338 172 DPATAT-NVDLKDIRIVKKLGGTIEDTELVDGLVFTQKASKkAGGPTRIEKAKIGLIQFCLSPPKTDMDNNIVVNDYAQM 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 273 KKFLEEEEKILEEMVNKIynvamerirkdgmeGKAGI-VVITQKGI-----DEVAQHFLAKKGIMAVRRVKRSDIEKIAR 346
Cdd:cd03338 251 DRILREERKYILNMCKKI--------------KKSGCnVLLIQKSIlrdavSDLALHFLAKLKIMVVKDIEREEIEFICK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 347 ATGAKIVSNIDDLTPEDLGFAKLVEERKVGEDKMVFIEGCPNP-RAVTILIRGGLERLVDEAERSINDALHAVADAIRDG 425
Cdd:cd03338 317 TIGCKPVASIDHFTEDKLGSADLVEEVSLGDGKIVKITGVKNPgKTVTILVRGSNKLVLDEAERSLHDALCVIRCLVKKR 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 426 KIVAGGGAVEVEVAKYLREIAPKIGGKEQLAVEAFARALEGLPMALAENAGLEPVEIIMKLRAAHAKAEgKWVGVNVFKG 505
Cdd:cd03338 397 ALIPGGGAPEIEIALQLSEWARTLTGVEQYCVRAFADALEVIPYTLAENAGLNPISIVTELRNRHAQGE-KNAGINVRKG 475
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 500145658 506 DVDDMKKLGVIEPVSVKANAIKAGTEAATMVLRIDDIIAA 545
Cdd:cd03338 476 AITNILEENVVQPLLVSTSAITLATETVRMILKIDDIVLA 515
|
|
| TCP1_gamma |
cd03337 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ... |
15-545 |
4.83e-153 |
|
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: 447.51 E-value: 4.83e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 15 PVLILKEGTQRTYGREALRTNIMIVRAIAETLRTTYGPKGMDKMLVDSLGDITITNDGATILDKMDVQHPTAKLVVQIAK 94
Cdd:cd03337 1 PVLVLNQNTKRESGRKAQLGNIQAAKTVADVIRTCLGPRAMLKMLLDPMGGIVLTNDGNAILREIDVAHPAAKSMIELSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 95 GQDEEVGDGTKTAVIFAGELLRYAEELLDKNVHPTIIVSGYKKAAEEAVKKLHEIAEPIDINDEETLKKIAMTSLTSKAV 174
Cdd:cd03337 81 TQDEEVGDGTTSVIILAGEILAVAEPFLERGIHPTVIIKAYRKALEDALKILEEISIPVDVNDRAQMLKIIKSCIGTKFV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 175 HGAREHLAEIVVKAVRQVAEKRGD-KWYIDLDA-IQIIKKHGGSLRDTKLIYGIVLDKEVVHPGMPKKVENAYIVLLDAP 252
Cdd:cd03337 161 SRWSDLMCNLALDAVKTVAVEENGrKKEIDIKRyAKVEKIPGGEIEDSRVLDGVMLNKDVTHPKMRRRIENPRIVLLDCP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 253 LEvekpeidaeirindpaflkkfleeeekileemvnkiYnvamerirkdgmegkagiVVITQKGIDEVAQHFLAKKGIMA 332
Cdd:cd03337 241 LE------------------------------------Y------------------LVITEKGVSDLAQHYLVKAGITA 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 333 VRRVKRSDIEKIARATGAKIVSNIDDLTPEDLG-FAKLVEERKVGEDKMVFIEGCPNPRAVTILIRGGLERLVDEAERSI 411
Cdd:cd03337 267 LRRVRKTDNNRIARACGATIVNRPEELTESDVGtGAGLFEVKKIGDEYFTFITECKDPKACTILLRGASKDVLNEVERNL 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 412 NDALHAVADAIRDGKIVAGGGAVEVEVAKYLREIAPKIGGKEQLAVEAFARALEGLPMALAENAGLEPVEIIMKLRAAHA 491
Cdd:cd03337 347 QDAMAVARNIILNPKLVPGGGATEMAVSHALSEKAKSIEGVEQWPYKAVASALEVIPRTLAQNCGANVIRTLTELRAKHA 426
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 500145658 492 KAEGKWVGVNVFKGDVDDMKKLGVIEPVSVKANAIKAGTEAATMVLRIDDIIAA 545
Cdd:cd03337 427 QGENSTWGIDGETGDIVDMKELGIWDPLAVKAQTYKTAIEAACMLLRIDDIVSG 480
|
|
| TCP1_alpha |
cd03335 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ... |
24-543 |
5.54e-152 |
|
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: 446.35 E-value: 5.54e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 24 QRTYGREALRTNIMIVRAIAETLRTTYGPKGMDKMLVDSLGDITITNDGATILDKMDVQHPTAKLVVQIAKGQDEEVGDG 103
Cdd:cd03335 2 ERTSGQDVRTQNVTAAMAIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDKEVGDG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 104 TKTAVIFAGELLRYAEELLDKNVHPTIIVSGYKKAAEEAVKKLHE-IAEPIDINDEETLKKIAMTSLTSKAVHGAREHLA 182
Cdd:cd03335 82 TTSVVIIAAELLKRANELVKQKIHPTTIISGYRLACKEAVKYIKEhLSISVDNLGKESLINVAKTSMSSKIIGADSDFFA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 183 EIVVKAVRQV--AEKRGDKWYiDLDAIQIIKKHGGSLRDTKLIYGIVLDKEVVHPGMPKKVENAYIVLLDAPLEVEKPEI 260
Cdd:cd03335 162 NMVVDAILAVktTNEKGKTKY-PIKAVNILKAHGKSAKESYLVNGYALNCTRASQGMPTRVKNAKIACLDFNLQKTKMKL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 261 DAEIRINDPAFLKKFLEEEEKILEEMVNKIYnvamerirkdgmegKAGI-VVITQKGIDEVAQHFLAKKGIMAVRRVKRS 339
Cdd:cd03335 241 GVQVVVTDPEKLEKIRQRESDITKERIKKIL--------------AAGAnVVLTTGGIDDMCLKYFVEAGAMAVRRVKKE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 340 DIEKIARATGAKIVSNIDDLTPED------LGFAKLVEERKVGEDKMVFIEGCPNPRAVTILIRGGLERLVDEAERSIND 413
Cdd:cd03335 307 DLRRIAKATGATLVSTLANLEGEEtfdpsyLGEAEEVVQERIGDDELILIKGTKKRSSASIILRGANDFMLDEMERSLHD 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 414 ALHAVADAIRDGKIVAGGGAVEVEVAKYLREIAPKIGGKEQLAVEAFARALEGLPMALAENAGLEPVEIIMKLRAAHAKA 493
Cdd:cd03335 387 ALCVVKRTLESNSVVPGGGAVETALSIYLENFATTLGSREQLAIAEFAEALLVIPKTLAVNAAKDATELVAKLRAYHAAA 466
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 500145658 494 -------EGKWVGVNVFKGDVDDMKKLGVIEPVSVKANAIKAGTEAATMVLRIDDII 543
Cdd:cd03335 467 qvkpdkkHLKWYGLDLINGKVRDNLEAGVLEPTVSKIKSLKFATEAAITILRIDDLI 523
|
|
| chap_CCT_gamma |
TIGR02344 |
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ... |
15-548 |
1.57e-149 |
|
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: 440.33 E-value: 1.57e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 15 PVLILKEGTQRTYGREALRTNIMIVRAIAETLRTTYGPKGMDKMLVDSLGDITITNDGATILDKMDVQHPTAKLVVQIAK 94
Cdd:TIGR02344 1 PVLVLNQNTKRESGRKAQLSNIQAAKAVADIIRTCLGPRSMLKMLLDPMGGIVMTNDGNAILREIDVAHPAAKSMIELSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 95 GQDEEVGDGTKTAVIFAGELLRYAEELLDKNVHPTIIVSGYKKAAEEAVKKLHEIAEPIDINDEETLKKIAMTSLTSKAV 174
Cdd:TIGR02344 81 TQDEEVGDGTTSVIILAGEMLSVAEPFLEQNIHPTVIIRAYRKALDDALSVLEEISIPVDVNDDAAMLKLIQSCIGTKFV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 175 HGAREHLAEIVVKAVRQVAEKRGDKWYIDLDA-IQIIKKHGGSLRDTKLIYGIVLDKEVVHPGMPKKVENAYIVLLDAPL 253
Cdd:TIGR02344 161 SRWSDLMCDLALDAVRTVQRDENGRKEIDIKRyAKVEKIPGGDIEDSCVLKGVMINKDVTHPKMRRYIENPRIVLLDCPL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 254 EVEKPEIDAEIRINDPAFLKKFLEEEEKILEEMVNKIYNVameriRKDgmegkagiVVITQKGIDEVAQHFLAKKGIMAV 333
Cdd:TIGR02344 241 EYKKGESQTNIEITKEEDWNRILQMEEEYVQLMCEDIIAV-----KPD--------LVITEKGVSDLAQHYLLKANITAI 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 334 RRVKRSDIEKIARATGAKIVSNIDDLTPEDLGF-AKLVEERKVGEDKMVFIEGCPNPRAVTILIRGGLERLVDEAERSIN 412
Cdd:TIGR02344 308 RRVRKTDNNRIARACGATIVNRPEELRESDVGTgCGLFEVKKIGDEYFTFITECKDPKACTILLRGASKDILNEVERNLQ 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 413 DALHAVADAIRDGKIVAGGGAVEVEVAKYLREIAPKIGGKEQLAVEAFARALEGLPMALAENAGLEPVEIIMKLRAAHAK 492
Cdd:TIGR02344 388 DAMAVARNVLLDPKLVPGGGATEMAVSVALTEKSKKLEGVEQWPYRAVADALEIIPRTLAQNCGANVIRTLTELRAKHAQ 467
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 500145658 493 AEGKWVGVNVFKGDVDDMKKLGVIEPVSVKANAIKAGTEAATMVLRIDDIIAAARR 548
Cdd:TIGR02344 468 ENNCTWGIDGETGKIVDMKEKGIWEPLAVKLQTYKTAIESACLLLRIDDIVSGVKK 523
|
|
| chap_CCT_eta |
TIGR02345 |
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ... |
15-547 |
2.99e-143 |
|
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT eta chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.
Pssm-ID: 274086 [Multi-domain] Cd Length: 523 Bit Score: 424.17 E-value: 2.99e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 15 PVLILKEGTQRTYGREALRTNIMIVRAIAETLRTTYGPKGMDKMLVDSLGDITITNDGATILDKMDVQHPTAKLVVQIAK 94
Cdd:TIGR02345 3 TIVLLKEGTDTSQGKGQLISNINACVAIAEALKTTLGPRGMDKLIVGSNGKATISNDGATILKLLDIVHPAAKTLVDIAK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 95 GQDEEVGDGTKTAVIFAGELLRYAEELLDKNVHPTIIVSGYKKAAEEAVKKLHEIAEPIDIND---EETLKKIAMTSLTS 171
Cdd:TIGR02345 83 SQDAEVGDGTTSVTILAGELLKEAKPFIEEGVHPQLIIRCYREALSLAVEKIKEIAVTIDEEKgeqRELLEKCAATALSS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 172 KAVHGAREHLAEIVVKAVRQVaekrgDKWYIDLDAIQIIKKHGGSLRDTKLIYGIVLDKEVVHPG---MPKKVENAYIVL 248
Cdd:TIGR02345 163 KLISHNKEFFSKMIVDAVLSL-----DRDDLDLKLIGIKKVQGGALEDSQLVNGVAFKKTFSYAGfeqQPKKFANPKILL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 249 LDAPLEVEKPEIDAEIRINDPaflKKFLEeeekileeMVNKIYNVAMERIRKdgMEGKAGIVVITQKGIDEVAQHFLAKK 328
Cdd:TIGR02345 238 LNVELELKAEKDNAEIRVEDV---EDYQA--------IVDAEWAIIFRKLEK--IVESGANVVLSKLPIGDLATQYFADR 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 329 GIMAVRRVKRSDIEKIARATGAKIVSNIDDLTPEDLGFAKLVEERKVGEDKMVFIEGCPNPRAVTILIRGGLERLVDEAE 408
Cdd:TIGR02345 305 DIFCAGRVSAEDLKRVIKACGGSIQSTTSDLEADVLGTCALFEERQIGSERYNYFTGCPHAKTCTIILRGGAEQFIEEAE 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 409 RSINDALHAVADAIRDGKIVAGGGAVEVEVAKYLREIAPKIGGKEQLAVEAFARALEGLPMALAENAGLEPVEIIMKLRA 488
Cdd:TIGR02345 385 RSLHDAIMIVRRALKNKKIVAGGGAIEMELSKCLRDYSKTIDGKQQLIINAFAKALEIIPRQLCENAGFDSIEILNKLRS 464
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 500145658 489 AHAKaEGKWVGVNVFKGDVDDMKKLGVIEPVSVKANAIKAGTEAATMVLRIDDIIAAAR 547
Cdd:TIGR02345 465 RHAK-GGKWYGVDINTEDIGDNFEAFVWEPALVKINALKAAFEAACTILSVDETITNPK 522
|
|
| chap_CCT_alpha |
TIGR02340 |
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ... |
22-543 |
3.59e-143 |
|
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: 424.52 E-value: 3.59e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 22 GTQRTYGREALRTNIMIVRAIAETLRTTYGPKGMDKMLVDSLGDITITNDGATILDKMDVQHPTAKLVVQIAKGQDEEVG 101
Cdd:TIGR02340 4 GGERTSGQDVRTQNVTAAMAIANIVKTSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDREVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 102 DGTKTAVIFAGELLRYAEELLDKNVHPTIIVSGYKKAAEEAVKKLHE-IAEPIDINDEETLKKIAMTSLTSKAVHGAREH 180
Cdd:TIGR02340 84 DGTTSVVIIAAELLKRADELVKNKIHPTSVISGYRLACKEAVKYIKEnLSVSVDELGREALINVAKTSMSSKIIGLDSDF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 181 LAEIVV---KAVRQVAEKRGDKWYIdlDAIQIIKKHGGSLRDTKLIYGIVLDKEVVHPGMPKKVENAYIVLLDAPLEVEK 257
Cdd:TIGR02340 164 FSNIVVdavLAVKTTNENGETKYPI--KAINILKAHGKSARESMLVKGYALNCTVASQQMPKRIKNAKIACLDFNLQKAK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 258 PEIDAEIRINDPAFLKKFLEEEEKILEEMVNKIYnvamerirkdgmegKAGI-VVITQKGIDEVAQHFLAKKGIMAVRRV 336
Cdd:TIGR02340 242 MALGVQIVVDDPEKLEQIRQREADITKERIKKIL--------------DAGAnVVLTTGGIDDMCLKYFVEAGAMGVRRC 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 337 KRSDIEKIARATGAKIVSNIDDLTPED------LGFAKLVEERKVGEDKMVFIEGCPNPRAVTILIRGGLERLVDEAERS 410
Cdd:TIGR02340 308 KKEDLKRIAKATGATLVSTLADLEGEEtfeasyLGFADEVVQERIADDECILIKGTKKRKSASIILRGANDFMLDEMERS 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 411 INDALHAVADAIRDGKIVAGGGAVEVEVAKYLREIAPKIGGKEQLAVEAFARALEGLPMALAENAGLEPVEIIMKLRAAH 490
Cdd:TIGR02340 388 LHDALCVVKRTLESNSVVPGGGAVEAALSIYLENFATTLGSREQLAIAEFARALLIIPKTLAVNAAKDSTELVAKLRAYH 467
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 491 AKA-------EGKWVGVNVFKGDVDDMKKLGVIEPVSVKANAIKAGTEAATMVLRIDDII 543
Cdd:TIGR02340 468 AAAqlkpekkHLKWYGLDLVNGKIRDNKEAGVLEPTVSKVKSLKFATEAAITILRIDDLI 527
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
14-548 |
1.36e-142 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 422.90 E-value: 1.36e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 14 VPVLILKEGTQRTYGREALRTNIMIVRAIAETLRTTYGPKGMDKMLVDS-----LGDITITNDGATILDKMDVQHPTAKL 88
Cdd:PTZ00212 6 VPPQVLKQGAQEEKGETARLQSFVGAIAVADLVKTTLGPKGMDKILQPMsegprSGNVTVTNDGATILKSVWLDNPAAKI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 89 VVQIAKGQDEEVGDGTKTAVIFAGELLRYAEELLDKNVHPTIIVSGYKKAAEEAVKKLHEIAEPIDINDE---ETLKKIA 165
Cdd:PTZ00212 86 LVDISKTQDEEVGDGTTSVVVLAGELLREAEKLLDQKIHPQTIIEGWRMALDVARKALEEIAFDHGSDEEkfkEDLLNIA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 166 MTSLTSKAVHGAREHLAEIVVKAVRQVAEKrgdkwyIDLDAIQIIKKHGGSLRDTKLIYGIVLDKEVvHPGMPKKVENAY 245
Cdd:PTZ00212 166 RTTLSSKLLTVEKDHFAKLAVDAVLRLKGS------GNLDYIQIIKKPGGTLRDSYLEDGFILEKKI-GVGQPKRLENCK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 246 IVLLDAPLEVEKPEI-DAEIRINDpafLKKFLEEEEKILEEMVNKIynvamERIRKDGMEgkagiVVITQKGIDEVAQHF 324
Cdd:PTZ00212 239 ILVANTPMDTDKIKIyGAKVKVDS---MEKVAEIEAAEKEKMKNKV-----DKILAHGCN-----VFINRQLIYNYPEQL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 325 LAKKGIMAVRRVKRSDIEKIARATGAKIVSNIDDLTPEDLGFAKLVEERKVGEDKMVFIEGCPNPRAVTILIRGGLERLV 404
Cdd:PTZ00212 306 FAEAGIMAIEHADFDGMERLAAALGAEIVSTFDTPEKVKLGHCDLIEEIMIGEDKLIRFSGCAKGEACTIVLRGASTHIL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 405 DEAERSINDALHAVADAIRDGKIVAGGGAVEVEVAKYLREIAPKIGGKEQLAVEAFARALEGLPMALAENAGLEPVEIIM 484
Cdd:PTZ00212 386 DEAERSLHDALCVLSQTVKDTRVVLGGGCSEMLMANAVEELAKKVEGKKSLAIEAFAKALRQIPTIIADNGGYDSAELVS 465
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 500145658 485 KLRAAHAKAEgKWVGVNVFKGDVDDMKKLGVIEPVSVKANAIKAGTEAATMVLRIDDIIAAARR 548
Cdd:PTZ00212 466 KLRAEHYKGN-KTAGIDMEKGTVGDMKELGITESYKVKLSQLCSATEAAEMILRVDDIIRCAPR 528
|
|
| chap_CCT_delta |
TIGR02342 |
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ... |
34-546 |
1.91e-136 |
|
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT delta chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.
Pssm-ID: 274083 Cd Length: 517 Bit Score: 406.48 E-value: 1.91e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 34 TNIMIVRAIAETLRTTYGPKGMDKMLVDSLGDITITNDGATILDKMDVQHPTAKLVVQIAKGQDEEVGDGTKTAVIFAGE 113
Cdd:TIGR02342 13 SNIVAAKAVADAIRTSLGPKGMDKMIQDGKGEVIITNDGATILKQMAVLHPAAKMLVELSKAQDIEAGDGTTSVVILAGA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 114 LLRYAEELLDKNVHPTIIVSGYKKAAEEAVKKLHEIAEPIDINDEETLKKIAMTSLTSKAVHGAREHLAEIVVKAVRQVA 193
Cdd:TIGR02342 93 LLGACERLLNKGIHPTIISESFQSAADEAIKILDEMSIPVDLSDREQLLKSATTSLSSKVVSQYSSLLAPLAVDAVLKVI 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 194 EKRGDKwYIDLDAIQIIKKHGGSLRDTKLIYGIVLDKEVVHP-GMPKKVENAYIVLLDAPLEVEKPEIDAEIRINDPAFL 272
Cdd:TIGR02342 173 DPENAK-NVDLNDIKVVKKLGGTIDDTELIEGLVFTQKASKSaGGPTRIEKAKIGLIQFQISPPKTDMENQIIVNDYAQM 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 273 KKFLEEEEKILEEMVNKIynvamerirkdgmeGKAGI-VVITQKGI-----DEVAQHFLAKKGIMAVRRVKRSDIEKIAR 346
Cdd:TIGR02342 252 DRVLKEERAYILNIVKKI--------------KKTGCnVLLIQKSIlrdavNDLALHFLAKMKIMVVKDIEREEIEFICK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 347 ATGAKIVSNIDDLTPEDLGFAKLVEERKVGEDKMVFIEGCPNPR-AVTILIRGGLERLVDEAERSINDALHAVADAIRDG 425
Cdd:TIGR02342 318 TIGCKPIASIDHFTADKLGSAELVEEVDSDGGKIIKITGIQNAGkTVTVVVRGSNKLVIDEAERSLHDALCVIRCLVKKR 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 426 KIVAGGGAVEVEVAKYLREIAPKIGGKEQLAVEAFARALEGLPMALAENAGLEPVEIIMKLRAAHAKAEgKWVGVNVFKG 505
Cdd:TIGR02342 398 GLIAGGGAPEIEIARRLSKYARTMKGVESYCVRAFADALEVIPYTLAENAGLNPIKVVTELRNRHANGE-KTAGISVRKG 476
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 500145658 506 DVDDMKKLGVIEPVSVKANAIKAGTEAATMVLRIDDIIAAA 546
Cdd:TIGR02342 477 GITNMLEEHVLQPLLVTTSAITLASETVRSILKIDDIVFTR 517
|
|
| TCP1_beta |
cd03336 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ... |
18-548 |
2.14e-136 |
|
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: 406.33 E-value: 2.14e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 18 ILKEGTQRTYGREALRTNIMIVRAIAETLRTTYGPKGMDKML--VDSLGDITITNDGATILDKMDVQHPTAKLVVQIAKG 95
Cdd:cd03336 1 ILKDGAQEEKGETARLSSFVGAIAIGDLVKTTLGPKGMDKILqsVGRSGGVTVTNDGATILKSIGVDNPAAKVLVDISKV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 96 QDEEVGDGTKTAVIFAGELLRYAEELLDKNVHPTIIVSGYKKAAEEAVKKLHEIAEPIDINDE---ETLKKIAMTSLTSK 172
Cdd:cd03336 81 QDDEVGDGTTSVTVLAAELLREAEKLVAQKIHPQTIIEGYRMATAAAREALLSSAVDHSSDEEafrEDLLNIARTTLSSK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 173 AVHGAREHLAEIVVKAVRQVaekrgdKWYIDLDAIQIIKKHGGSLRDTKLIYGIVLDKEVvHPGMPKKVENAYIVLLDAP 252
Cdd:cd03336 161 ILTQDKEHFAELAVDAVLRL------KGSGNLDAIQIIKKLGGSLKDSYLDEGFLLDKKI-GVNQPKRIENAKILIANTP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 253 LEVEKPEI-DAEIRINDPAflkKFLEEEEKILEEMVNKIynvamERIRKDGMEgkagiVVITQKGIDEVAQHFLAKKGIM 331
Cdd:cd03336 234 MDTDKIKIfGAKVRVDSTA---KVAEIEEAEKEKMKNKV-----EKILKHGIN-----CFINRQLIYNYPEQLFADAGIM 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 332 AVRRVKRSDIEKIARATGAKIVSNIDDLTPEDLGFAKLVEERKVGEDKMVFIEGCPNPRAVTILIRGGLERLVDEAERSI 411
Cdd:cd03336 301 AIEHADFDGVERLALVTGGEIASTFDHPELVKLGTCKLIEEIMIGEDKLIRFSGVAAGEACTIVLRGASQQILDEAERSL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 412 NDALHAVADAIRDGKIVAGGGAVEVEVAKYLREIAPKIGGKEQLAVEAFARALEGLPMALAENAGLEPVEIIMKLRAAHA 491
Cdd:cd03336 381 HDALCVLAQTVKDTRVVLGGGCSEMLMAKAVEELAKKTPGKKSLAIEAFAKALRQLPTIIADNAGYDSAELVAQLRAAHY 460
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 500145658 492 KaEGKWVGVNVFKGDVDDMKKLGVIEPVSVKANAIKAGTEAATMVLRIDDIIAAARR 548
Cdd:cd03336 461 N-GNTTAGLDMRKGTVGDMKELGITESFKVKRQVLLSASEAAEMILRVDDIIKCAPR 516
|
|
| TCP1_zeta |
cd03342 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
30-547 |
9.06e-133 |
|
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: 395.86 E-value: 9.06e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 30 EALRTNIMIVRAIAETLRTTYGPKGMDKMLVDSLGDITITNDGATILDKMDVQHPTAKLVVQIAKGQDEEVGDGTKTAVI 109
Cdd:cd03342 12 QALAVNISAAKGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLSEMQIQHPTASMIARAATAQDDITGDGTTSNVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 110 FAGELLRYAEELLDKNVHPTIIVSGYKKAAEEAVKKLHEIAEPIDI-NDEETLKKIAMTSLTSKAVHGAREHLAEIVVKA 188
Cdd:cd03342 92 LIGELLKQAERYIQEGVHPRIITEGFELAKNKALKFLESFKVPVEIdTDRELLLSVARTSLRTKLHADLADQLTEIVVDA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 189 VRQVaeKRGDKwYIDLDAIQIIKKHGGSLRDTKLIYGIVLDKEVVHPGMPKKVENAYIVLLDAPLEVEKPEIDAEIrind 268
Cdd:cd03342 172 VLAI--YKPDE-PIDLHMVEIMQMQHKSDSDTKLIRGLVLDHGARHPDMPKRVENAYILTCNVSLEYEKTEVNSGF---- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 269 paflkkfleeeekileemvnkIYNVamerirkdgmegkagivVITQKGIDEVAQHFLAKKGIMAVRRVKRSDIEKIARAT 348
Cdd:cd03342 245 ---------------------FYSV-----------------VINQKGIDPPSLDMLAKEGILALRRAKRRNMERLTLAC 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 349 GAKIVSNIDDLTPEDLGFAKLVEERKVGEDKMVFIEGCPNPRAVTILIRGGLERLVDEAERSINDALHAVADAIRDGKIV 428
Cdd:cd03342 287 GGVAMNSVDDLSPECLGYAGLVYERTLGEEKYTFIEGVKNPKSCTILIKGPNDHTITQIKDAIRDGLRAVKNAIEDKCVV 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 429 AGGGAVEVEVAKYLREIAPKIGGKEQLAVEAFARALEGLPMALAENAGLEPVEIIMKLRAAHAKAeGKWVGVNVFKGDVD 508
Cdd:cd03342 367 PGAGAFEVALYAHLKEFKKSVKGKAKLGVQAFADALLVIPKTLAENSGLDVQETLVKLQDEYAEG-GQVGGVDLDTGEPM 445
|
490 500 510
....*....|....*....|....*....|....*....
gi 500145658 509 DMKKLGVIEPVSVKANAIKAGTEAATMVLRIDDIIAAAR 547
Cdd:cd03342 446 DPESEGIWDNYSVKRQILHSATVIASQLLLVDEIIRAGR 484
|
|
| chap_CCT_zeta |
TIGR02347 |
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ... |
31-547 |
4.61e-127 |
|
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: 382.93 E-value: 4.61e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 31 ALRTNIMIVRAIAETLRTTYGPKGMDKMLVDSLGDITITNDGATILDKMDVQHPTAKLVVQIAKGQDEEVGDGTKTAVIF 110
Cdd:TIGR02347 17 ALMMNINAARGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEMQIQHPTASMIARAATAQDDITGDGTTSTVLL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 111 AGELLRYAEELLDKNVHPTIIVSGYKKAAEEAVKKLHEI-AEPIDINDEETLKKIAMTSLTSKAVHGAREHLAEIVVKAV 189
Cdd:TIGR02347 97 IGELLKQAERYILEGVHPRIITEGFEIARKEALQFLDKFkVKKEDEVDREFLLNVARTSLRTKLPADLADQLTEIVVDAV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 190 RQVaekRGDKWYIDLDAIQIIKKHGGSLRDTKLIYGIVLDKEVVHPGMPKKVENAYIVLLDAPLEVEKPEIDAEIRINDP 269
Cdd:TIGR02347 177 LAI---KKDGEDIDLFMVEIMEMKHKSATDTTLIRGLVLDHGARHPDMPRRVKNAYILTCNVSLEYEKTEVNSGFFYSSA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 270 AFLKKFLEEEEKILEEMVNKIYNVAMERIrkdGMEGKAGIVVITQKGIDEVAQHFLAKKGIMAVRRVKRSDIEKIARATG 349
Cdd:TIGR02347 254 EQREKLVKAERKFVDDRVKKIIELKKKVC---GKSPDKGFVVINQKGIDPPSLDLLAKEGIMALRRAKRRNMERLTLACG 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 350 AKIVSNIDDLTPEDLGFAKLVEERKVGEDKMVFIEGCPNPRAVTILIRGGLERLVDEAERSINDALHAVADAIRDGKIVA 429
Cdd:TIGR02347 331 GEALNSVEDLTPECLGWAGLVYETTIGEEKYTFIEECKNPKSCTILIKGPNDHTIAQIKDAVRDGLRAVKNAIEDKCVVP 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 430 GGGAVEVEVAKYLREIAPKIGGKEQLAVEAFARALEGLPMALAENAGLEPVEIIMKLRAAHAKAeGKWVGVNVFKGDVDD 509
Cdd:TIGR02347 411 GAGAFEIAAYRHLKEYKKSVKGKAKLGVEAFANALLVIPKTLAENSGFDAQDTLVKLEDEHDEG-GEVVGVDLNTGEPID 489
|
490 500 510
....*....|....*....|....*....|....*...
gi 500145658 510 MKKLGVIEPVSVKANAIKAGTEAATMVLRIDDIIAAAR 547
Cdd:TIGR02347 490 PEIKGIWDNYRVKKQLIQSATVIASQLLLVDEVMRAGR 527
|
|
| TCP1_theta |
cd03341 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ... |
30-545 |
2.48e-115 |
|
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: 350.75 E-value: 2.48e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 30 EALRTNIMIVRAIAETLRTTYGPKGMDKMLVDSLGDITITNDGATILDKMDVQHPTAKLVVQIAKGQDEEVGDGTKTAVI 109
Cdd:cd03341 8 EAVLRNIEACKELSQITRTSYGPNGMNKMVINHLEKLFVTSDAATILRELEVQHPAAKLLVMASQMQEEEIGDGTNLVVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 110 FAGELLRYAEELLDKNVHPTIIVSGYKKAAEEAVKKLHEIA--EPIDINDEETLKKIAMTSLTSKaVHGAREHLAEIVVK 187
Cdd:cd03341 88 LAGELLEKAEELLRMGLHPSEIIEGYEKALKKALEILEELVvyKIEDLRNKEEVSKALKTAIASK-QYGNEDFLSPLVAE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 188 AVRQVAEKrgDKWYIDLDAIQIIKKHGGSLRDTKLIYGIVLDKEVVhpGMPKKVENAYIVLLDAPLEVekpeidaeirin 267
Cdd:cd03341 167 ACISVLPE--NIGNFNVDNIRVVKILGGSLEDSKVVRGMVFKREPE--GSVKRVKKAKVAVFSCPFDI------------ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 268 dpaflkkfleeeekileemvnkiynvamerirkdgmegkaGI-VVITQKGIDEVAQHFLAKKGIMAVRRVKRSDIEKIAR 346
Cdd:cd03341 231 ----------------------------------------GVnVIVAGGSVGDLALHYCNKYGIMVIKINSKFELRRLCR 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 347 ATGAKIVSNIDDLTPEDLGFAKLVEERKVGEDKMVFIEGCPNPRAV-TILIRGGLERLVDEAERSINDALHAVADAIRDG 425
Cdd:cd03341 271 TVGATPLPRLGAPTPEEIGYCDSVYVEEIGDTKVVVFRQNKEDSKIaTIVLRGATQNILDDVERAIDDGVNVFKSLTKDG 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 426 KIVAGGGAVEVEVAKYLREIAPKIGGKEQLAVEAFARALEGLPMALAENAGLEPVEIIMKLRAAHAKaEGKWVGVNVFKG 505
Cdd:cd03341 351 RFVPGAGATEIELAKKLKEYGEKTPGLEQYAIKKFAEAFEVVPRTLAENAGLDATEVLSELYAAHQK-GNKSAGVDIESG 429
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 500145658 506 D--VDDMKKLGVIEPVSVKANAIKAGTEAATMVLRIDDIIAA 545
Cdd:cd03341 430 DegTKDAKEAGIFDHLATKKWAIKLATEAAVTVLRVDQIIMA 471
|
|
| chap_CCT_theta |
TIGR02346 |
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ... |
18-545 |
1.64e-106 |
|
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: 329.75 E-value: 1.64e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 18 ILKEGTQRTYG-REALRTNIMIVRAIAETLRTTYGPKGMDKMLVDSLGDITITNDGATILDKMDVQHPTAKLVVQIAKGQ 96
Cdd:TIGR02346 5 LLKEGYRHFSGlEEAVIKNIEACKELSQITRTSLGPNGMNKMVINHLEKLFVTNDAATILRELEVQHPAAKLLVMASEMQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 97 DEEVGDGTKTAVIFAGELLRYAEELLDKNVHPTIIVSGYKKAAEEAVKKLHEIA--EPIDINDEETLKKIAMTSLTSKAV 174
Cdd:TIGR02346 85 ENEIGDGTNLVLVLAGELLNKAEELIRMGLHPSEIIKGYEMALKKAMEILEELVvwEVKDLRDKDELIKALKASISSKQY 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 175 HGArEHLAEIVVKAVRQVAEKRGDKWyiDLDAIQIIKKHGGSLRDTKLIYGIVLDKEVVhpGMPKKVENAYIVLLDAPLE 254
Cdd:TIGR02346 165 GNE-DFLAQLVAQACSTVLPKNPQNF--NVDNIRVCKILGGSLSNSEVLKGMVFNREAE--GSVKSVKNAKVAVFSCPLD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 255 VEKPEIDAEIRINDPAFLKKFLEEEEKILEEMVNKIYnvamerirkdgmegKAGI-VVITQKGIDEVAQHFLAKKGIMAV 333
Cdd:TIGR02346 240 TATTETKGTVLIHNAEELLNYSKGEENQIEAMIKAIA--------------DSGVnVIVTGGSVGDMALHYLNKYNIMVL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 334 RRVKRSDIEKIARATGAKIVSNIDDLTPEDLGFAKLVEERKVGEDKMVFIEGCPNPRAV-TILIRGGLERLVDEAERSIN 412
Cdd:TIGR02346 306 KIPSKFELRRLCKTVGATPLPRLGAPTPEEIGYVDSVYVSEIGGDKVTVFKQENGDSKIsTIILRGSTDNLLDDIERAID 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 413 DALHAVADAIRDGKIVAGGGAVEVEVAKYLREIAPKIGGKEQLAVEAFARALEGLPMALAENAGLEPVEIIMKLRAAHAK 492
Cdd:TIGR02346 386 DGVNTVKALVKDGRLLPGAGATEIELASRLTKYGEKLPGLDQYAIKKFAEAFEIIPRTLAENAGLNANEVIPKLYAAHKK 465
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 500145658 493 AEgKWVGVNVFKGD--VDDMKKLGVIEPVSVKANAIKAGTEAATMVLRIDDIIAA 545
Cdd:TIGR02346 466 GN-KSKGIDIEAESdgVKDASEAGIYDMLATKKWAIKLATEAAVTVLRVDQIIMA 519
|
|
| chap_CCT_beta |
TIGR02341 |
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ... |
18-548 |
3.65e-105 |
|
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: 326.05 E-value: 3.65e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 18 ILKEGTQRTYGREALRTNIMIVRAIAETLRTTYGPKGMDKMLV--DSLGDITITNDGATILDKMDVQHPTAKLVVQIAKG 95
Cdd:TIGR02341 2 IFKDGADEERAENARLSSFVGAIAIGDLVKSTLGPKGMDKILQssSSDASIMVTNDGATILKSIGVDNPAAKVLVDMSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 96 QDEEVGDGTKTAVIFAGELLRYAEELLDKNVHPTIIVSGYKKAAEEAVKKLHEIAepIDINDEET-----LKKIAMTSLT 170
Cdd:TIGR02341 82 QDDEVGDGTTSVTVLAAELLREAEKLINQKIHPQTIIAGYREATKAARDALLKSA--VDNGSDEVkfrqdLMNIARTTLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 171 SKAVHGAREHLAEIVVKAVRQVaekrgdKWYIDLDAIQIIKKHGGSLRDTKLIYGIVLDKEvvhPGM--PKKVENAYIVL 248
Cdd:TIGR02341 160 SKILSQHKDHFAQLAVDAVLRL------KGSGNLEAIQIIKKLGGSLADSYLDEGFLLDKK---IGVnqPKRIENAKILI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 249 LDAPLEVEKPEI-DAEIRINDPAflkKFLEEEEKILEEMVNKIynvamERIRKDGMEgkagiVVITQKGIDEVAQHFLAK 327
Cdd:TIGR02341 231 ANTGMDTDKVKIfGSRVRVDSTA---KVAELEHAEKEKMKEKV-----EKILKHGIN-----CFINRQLIYNYPEQLFAD 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 328 KGIMAVRRVKRSDIEKIARATGAKIVSNIDDLTPEDLGFAKLVEERKVGEDKMVFIEGCPNPRAVTILIRGGLERLVDEA 407
Cdd:TIGR02341 298 AGVMAIEHADFEGVERLALVTGGEIVSTFDHPELVKLGSCDLIEEIMIGEDKLLKFSGVKLGEACTIVLRGATQQILDEA 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 408 ERSINDALHAVADAIRDGKIVAGGGAVEVEVAKYLREIAPKIGGKEQLAVEAFARALEGLPMALAENAGLEPVEIIMKLR 487
Cdd:TIGR02341 378 ERSLHDALCVLSQTVKESRTVLGGGCSEMLMSKAVTQEAQRTPGKEALAVEAFARALRQLPTIIADNAGFDSAELVAQLR 457
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500145658 488 AAHAKAEGKwVGVNVFKGDVDDMKKLGVIEPVSVKANAIKAGTEAATMVLRIDDIIAAARR 548
Cdd:TIGR02341 458 AAHYNGNTT-MGLDMNEGTIADMRQLGITESYKVKRAVVSSAAEAAEVILRVDNIIKAAPR 517
|
|
| chaperonin_like |
cd03333 |
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ... |
158-424 |
1.34e-78 |
|
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: 246.22 E-value: 1.34e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 158 EETLKKIAMTSLTSKAVHGArEHLAEIVVKAVRQVAEKRGDkwyIDLDAIQIIKKHGGSLRDTKLIYGIVLDKEVVHPGM 237
Cdd:cd03333 1 RELLLQVATTSLNSKLSSWD-DFLGKLVVDAVLKVGPDNRM---DDLGVIKVEKIPGGSLEDSELVVGVVFDKGYASPYM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 238 PKKVENAYIVLLDAPLEVekpeidaeirindpaflkkfleeeekileemvnkiynvamerirkdgmegkagiVVITQKGI 317
Cdd:cd03333 77 PKRLENAKILLLDCPLEY------------------------------------------------------VVIAEKGI 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 318 DEVAQHFLAKKGIMAVRRVKRSDIEKIARATGAKIVSNIDDLTPEDLGFAKLVEERKVGEDKMVFIEGCPNPRAVTILIR 397
Cdd:cd03333 103 DDLALHYLAKAGIMAVRRVKKEDLERIARATGATIVSSLEDLTPEDLGTAELVEETKIGEEKLTFIEGCKGGKAATILLR 182
|
250 260
....*....|....*....|....*..
gi 500145658 398 GGLERLVDEAERSINDALHAVADAIRD 424
Cdd:cd03333 183 GATEVELDEVKRSLHDALCAVRAAVEE 209
|
|
| Fab1_TCP |
cd03334 |
TCP-1 like domain of the eukaryotic phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinase Fab1. ... |
183-403 |
2.46e-28 |
|
TCP-1 like domain of the eukaryotic phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinase Fab1. Fab1p is important for vacuole size regulation, presumably by modulating PtdIns(3,5)P2 effector activity. In the human homolog p235/PIKfyve deletion of this domain leads to loss of catalytic activity. However no exact function this domain has been defined. In general, chaperonins are involved in productive folding of proteins.
Pssm-ID: 239450 [Multi-domain] Cd Length: 261 Bit Score: 113.86 E-value: 2.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 183 EIVVKAVRQVAE------KRGDKWYIdLDAIQIIKKHGGSLRDTKLIYGIVLDKEVVHPGMPKKVENAYIVLLDAPLEVE 256
Cdd:cd03334 21 DILLPLVWKAASnvkpdvRAGDDMDI-RQYVKIKKIPGGSPSDSEVVDGVVFTKNVAHKRMPSKIKNPRILLLQGPLEYQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 257 KPE-----IDAEIRINDpAFLKKfleeeekileeMVNKIynvamERIRKDgmegkagiVVITQKGIDEVAQHFLAKKGIM 331
Cdd:cd03334 100 RVEnkllsLDPVILQEK-EYLKN-----------LVSRI-----VALRPD--------VILVEKSVSRIAQDLLLEAGIT 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 500145658 332 AVRRVKRSDIEKIARATGAKIVSNIDDL-TPEDLGFAKLVEERKVGEDKMV-----FIEGCPNPRAVTILIRGG-LERL 403
Cdd:cd03334 155 LVLNVKPSVLERISRCTGADIISSMDDLlTSPKLGTCESFRVRTYVEEHGRsktlmFFEGCPKELGCTILLRGGdLEEL 233
|
|
| GroEL |
cd03344 |
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ... |
39-537 |
1.94e-26 |
|
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: 112.93 E-value: 1.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 39 VRAIAETLRTTYGPKGMDKMLVDSLGDITITNDGATILDKMDVQHPT----AKLVVQIAKGQDEEVGDGTKTAVIFAGEL 114
Cdd:cd03344 17 VNKLADAVKVTLGPKGRNVVIEKSFGSPKITKDGVTVAKEIELEDPFenmgAQLVKEVASKTNDVAGDGTTTATVLARAI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 115 LRYAEELLDKNVHPTIIVSGYKKAAEEAVKKLHEIAEPidINDEETLKKIAMTSLtskavhGAREHLAEIVVKAVRQVAE 194
Cdd:cd03344 97 IKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKP--VKTKEEIAQVATISA------NGDEEIGELIAEAMEKVGK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 195 krgdkwyidlDAIqIIKKHGGSLRDT-KLIYGIVLDKEVVHPGM---PKK----VENAYIVLLDAPLEVEKPEIdaeiri 266
Cdd:cd03344 169 ----------DGV-ITVEEGKTLETElEVVEGMQFDRGYLSPYFvtdPEKmeveLENPYILLTDKKISSIQELL------ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 267 ndpaflkkfleeeekileemvnkiynVAMERIRKdgmEGKAgiVVITQKGIDEVAQHFLA---KKGIMAVRRVK------ 337
Cdd:cd03344 232 --------------------------PILELVAK---AGRP--LLIIAEDVEGEALATLVvnkLRGGLKVCAVKapgfgd 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 338 -RSDI-EKIARATGAKIVSN-----IDDLTPEDLGFAKLVEerkVGEDKMVFIEGCPNPRAV------------------ 392
Cdd:cd03344 281 rRKAMlEDIAILTGGTVISEelglkLEDVTLEDLGRAKKVV---VTKDDTTIIGGAGDKAAIkariaqirkqieettsdy 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 393 -----------------TILIRGGLERLVDEAERSINDALHAVADAIRDGkIVAGGGAVEVEVAKYLREIAPKIGGkEQL 455
Cdd:cd03344 358 dkeklqerlaklsggvaVIKVGGATEVELKEKKDRVEDALNATRAAVEEG-IVPGGGVALLRASPALDKLKALNGD-EKL 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 456 AVEAFARALEGLPMALAENAGLEPVEIIMKLRaahaKAEGKWvGVNVFKGDVDDMKKLGVIEPVSVKANAIKAGTEAATM 535
Cdd:cd03344 436 GIEIVRRALEAPLRQIAENAGVDGSVVVEKVL----ESPDGF-GYDAATGEYVDMIEAGIIDPTKVVRSALQNAASVASL 510
|
..
gi 500145658 536 VL 537
Cdd:cd03344 511 LL 512
|
|
| groEL |
PRK12849 |
chaperonin GroEL; Reviewed |
39-544 |
7.58e-23 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237230 Cd Length: 542 Bit Score: 102.19 E-value: 7.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 39 VRAIAETLRTTYGPKGMDKMLVDSLGDITITNDGATILDKMDVQHP----TAKLVVQIAKGQDEEVGDGTKTAVIFAGEL 114
Cdd:PRK12849 19 VNKLADAVKVTLGPKGRNVVIDKSFGAPTITKDGVSIAKEIELEDPfenlGAQLVKEVASKTNDVAGDGTTTATVLAQAL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 115 LRYAEELLDKNVHPTIIVSGYKKAAEEAVKKLHEIAEPIDinDEETLKKIAMTSLTSKavhgarEHLAEIVVKAVRQVae 194
Cdd:PRK12849 99 VQEGLKNVAAGANPMDLKRGIDKAVEAVVEELKALARPVS--GSEEIAQVATISANGD------EEIGELIAEAMEKV-- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 195 krgdkwyiDLDAIqIIKKHGGSLRDT-KLIYGIVLDKEVVHPGM---PKK----VENAYIVLLDaplevekpeidaeiri 266
Cdd:PRK12849 169 --------GKDGV-ITVEESKTLETElEVTEGMQFDRGYLSPYFvtdPERmeavLEDPLILLTD---------------- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 267 ndpaflkkfleeeekileemvNKIYNV-AMERIRKDGMEGKAGIVVITqkgiDEVAQHFLAK------KGIMAVRRVK-- 337
Cdd:PRK12849 224 ---------------------KKISSLqDLLPLLEKVAQSGKPLLIIA----EDVEGEALATlvvnklRGGLKVAAVKap 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 338 ------RSDIEKIARATGAKIVS-----NIDDLTPEDLGFAKLVEerkVGEDKMVFIEGCPNPRAV-------------- 392
Cdd:PRK12849 279 gfgdrrKAMLEDIAILTGGTVISedlglKLEEVTLDDLGRAKRVT---ITKDNTTIVDGAGDKEAIearvaqirrqieet 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 393 ---------------------TILIRGGLERLVDEAERSINDALHAVADAIRDGkIVAGGGAVEVEVAKYLREIApKIGG 451
Cdd:PRK12849 356 tsdydreklqerlaklaggvaVIKVGAATEVELKERKDRVEDALNATRAAVEEG-IVPGGGVALLRAAKALDELA-GLNG 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 452 KEQLAVEAFARALEGLPMALAENAGLEPVEIIMKLRAAHAKaegkwVGVNVFKGDVDDMKKLGVIEPVSVKANAIKAGTE 531
Cdd:PRK12849 434 DQAAGVEIVRRALEAPLRQIAENAGLDGSVVVAKVLELEDG-----FGFNAATGEYGDLIAAGIIDPVKVTRSALQNAAS 508
|
570
....*....|...
gi 500145658 532 AATMVLRIDDIIA 544
Cdd:PRK12849 509 VAGLLLTTEALVA 521
|
|
| GroEL |
TIGR02348 |
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ... |
27-544 |
4.17e-21 |
|
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: 96.98 E-value: 4.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 27 YGREALRTNIMIVRAIAETLRTTYGPKGMDKMLVDSLGDITITNDGATILDKMDVQHP----TAKLVVQIAKGQDEEVGD 102
Cdd:TIGR02348 6 FDEEARKALLRGVDKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDKfenmGAQLVKEVASKTNDVAGD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 103 GTKTAVIFAGELLRYAEELLDKNVHPTIIVSGYKKAAEEAVKKLHEIAEPidINDEETLKKIAMTSltskavHGAREHLA 182
Cdd:TIGR02348 86 GTTTATVLAQAIVKEGLKNVAAGANPIELKRGIEKAVEAVVEELKKLSKP--VKGKKEIAQVATIS------ANNDEEIG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 183 EIVVKAVRQVAeKRGdkwyidldaiqIIKKHGGSLRDTKLIY--GIVLDKEVVHP-------GMPKKVENAYIVLLDAPL 253
Cdd:TIGR02348 158 SLIAEAMEKVG-KDG-----------VITVEESKSLETELEVveGMQFDRGYISPyfvtdaeKMEVELENPYILITDKKI 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 254 EVEK---PEIDAEIRINDPAFlkkfleeeekileemvnkiynVAMERIrkDGmEGKAGIVVITQKGIDEVAqhflakkgi 330
Cdd:TIGR02348 226 SNIKdllPLLEKVAQSGKPLL---------------------IIAEDV--EG-EALATLVVNKLRGTLNVC--------- 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 331 mAVR-----RVKRSDIEKIARATGAKIVS-----NIDDLTPEDLGFAKLVeerKVGEDKMVFIEGCPNPRAVTILIR--- 397
Cdd:TIGR02348 273 -AVKapgfgDRRKAMLEDIAILTGGQVISeelglKLEEVTLDDLGKAKKV---TVDKDNTTIVEGAGDKAAIKARVAqik 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 398 -----------------------GGL---------ERLVDEAERSINDALHAVADAIRDGkIVAGGGAVEVEVAKYLrEI 445
Cdd:TIGR02348 349 aqieettsdydreklqerlaklaGGVavikvgaatETEMKEKKLRIEDALNATRAAVEEG-IVPGGGVALLRAAAAL-EG 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 446 APKIGGKEQLAVEAFARALEGLPMALAENAGLEPVEIIMKLRAAHAKaegkwVGVNVFKGDVDDMKKLGVIEPVSVKANA 525
Cdd:TIGR02348 427 LKGDGEDEAIGIDIVKRALEAPLRQIAENAGLDGAVVAEKVKELKGN-----FGFNAATGEYEDLVEAGIIDPTKVTRSA 501
|
570
....*....|....*....
gi 500145658 526 IKAGTEAATMVLRIDDIIA 544
Cdd:TIGR02348 502 LQNAASIAGLLLTTEAVVA 520
|
|
| PTZ00114 |
PTZ00114 |
Heat shock protein 60; Provisional |
27-537 |
2.96e-19 |
|
Heat shock protein 60; Provisional
Pssm-ID: 185455 Cd Length: 555 Bit Score: 91.13 E-value: 2.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 27 YGREAlRTNIMI-VRAIAETLRTTYGPKGMDKMLVDSLGDITITNDGATILDKMDVQHPT----AKLVVQIAKGQDEEVG 101
Cdd:PTZ00114 19 FGDEA-RQSLLKgIERLADAVAVTLGPKGRNVIIEQEYGSPKITKDGVTVAKAIEFSDRFenvgAQLIRQVASKTNDKAG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 102 DGTKTAVIFAGELLRYAEELLDKNVHPTIIVSGYKKAAEEAVKKLHEIAEPidINDEETLKKIAMTSLTSKavhgarEHL 181
Cdd:PTZ00114 98 DGTTTATILARAIFREGCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQSRP--VKTKEDILNVATISANGD------VEI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 182 AEIVVKAVrqvaEKRGDKWYIDLDaiqiikkHGGSLRDTKLIY-GIVLDKEVVHP-----GMPKKVE--NAYIVLLDAPL 253
Cdd:PTZ00114 170 GSLIADAM----DKVGKDGTITVE-------DGKTLEDELEVVeGMSFDRGYISPyfvtnEKTQKVEleNPLILVTDKKI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 254 EVEK---PEIDAEIRINDPAFLkkfleeeekileeMVNKIYNVAMERIRKDGMEGKAGIVVITQKGIDEvaqhflakkgi 330
Cdd:PTZ00114 239 SSIQsilPILEHAVKNKRPLLI-------------IAEDVEGEALQTLIINKLRGGLKVCAVKAPGFGD----------- 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 331 mavrrVKRSDIEKIARATGAKIVSN------IDDLTPEDLGFAKLVEerkVGEDKMVFIEGCPNPRAVTI---LIRGGLE 401
Cdd:PTZ00114 295 -----NRKDILQDIAVLTGATVVSEdnvglkLDDFDPSMLGSAKKVT---VTKDETVILTGGGDKAEIKErveLLRSQIE 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 402 RLVDEAERS--------------------------------INDALHAVADAIRDGkIVAGGGAVEVEVAKYLREIA--P 447
Cdd:PTZ00114 367 RTTSEYDKEklkerlaklsggvavikvggasevevnekkdrIEDALNATRAAVEEG-IVPGGGVALLRASKLLDKLEedN 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 448 KIGGKEQLAVEAFARALEGLPMALAENAGLEPVEIIMKLraahAKAEGKWVGVNVFKGDVDDMKKLGVIEPVSVKANAIK 527
Cdd:PTZ00114 446 ELTPDQRTGVKIVRNALRLPTKQIAENAGVEGAVVVEKI----LEKKDPSFGYDAQTGEYVNMFEAGIIDPTKVVRSALV 521
|
570
....*....|
gi 500145658 528 AGTEAATMVL 537
Cdd:PTZ00114 522 DAASVASLML 531
|
|
| groEL |
PRK12850 |
chaperonin GroEL; Reviewed |
39-544 |
1.55e-16 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237231 Cd Length: 544 Bit Score: 82.84 E-value: 1.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 39 VRAIAETLRTTYGPKGMDKMLVDSLGDITITNDGATILDKMDVQHP----TAKLVVQIAKGQDEEVGDGTKTAVIFAGEL 114
Cdd:PRK12850 20 VNILANAVKVTLGPKGRNVVLEKSFGAPRITKDGVTVAKEIELEDKfenmGAQMVKEVASKTNDLAGDGTTTATVLAQAI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 115 LRYAEELLDKNVHPTIIVSGYKKAAEEAVKKLHEIAEPIDINDEetLKKIAMTSLTSKAVHGarehlaEIVVKAVRQVAe 194
Cdd:PRK12850 100 VREGAKLVAAGMNPMDLKRGIDLAVAAVVDELKKIAKKVTSSKE--IAQVATISANGDESIG------EMIAEAMDKVG- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 195 KRGdkwyidldaiqIIKKHGGSLRDTKL--IYGIVLDKEVVHPGM---PKK----VENAYIVLLDAPLEVEK---PEIDA 262
Cdd:PRK12850 171 KEG-----------VITVEEAKTLGTELdvVEGMQFDRGYLSPYFvtnPEKmraeLEDPYILLHEKKISNLQdllPILEA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 263 EIRINDPAFLKKFLEEEEKILEEMVNKiynvamerirkdgMEGKAGIVVITQKGIDEvaqhflakkgimavRRVkrSDIE 342
Cdd:PRK12850 240 VVQSGRPLLIIAEDVEGEALATLVVNK-------------LRGGLKSVAVKAPGFGD--------------RRK--AMLE 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 343 KIARATGAKIVS-----NIDDLTPEDLGFAKLVEerkVGEDKMVFIEGCPNPRAV------------------------- 392
Cdd:PRK12850 291 DIAVLTGGQVISedlgiKLENVTLDMLGRAKRVL---ITKENTTIIDGAGDKKNIearvkqiraqieettsdydreklqe 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 393 ----------TILIRGGLERLVDEAERSINDALHAVADAIRDGkIVAGGGAVEVEVAKYLREIAPkIGGKEQLAVEAFAR 462
Cdd:PRK12850 368 rlaklaggvaVIRVGGATEVEVKEKKDRVDDALHATRAAVEEG-IVPGGGVALLRARSALRGLKG-ANADETAGIDIVRR 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 463 ALEGLPMALAENAGLEPVEIIMKLraahAKAEGKWvGVNVFKGDVDDMKKLGVIEPVSVKANAIKAGTEAATMVLRIDDI 542
Cdd:PRK12850 446 ALEEPLRQIATNAGFEGSVVVGKV----AELPGNF-GFNAQTGEYGDMVEAGIIDPAKVTRTALQDAASIAALLITTEAM 520
|
..
gi 500145658 543 IA 544
Cdd:PRK12850 521 VA 522
|
|
| groEL |
PRK12852 |
chaperonin GroEL; Reviewed |
39-544 |
5.41e-15 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237232 Cd Length: 545 Bit Score: 77.96 E-value: 5.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 39 VRAIAETLRTTYGPKGMDKMLVDSLGDITITNDGATILDKMDV----QHPTAKLVVQIAKGQDEEVGDGTKTAVIFAGEL 114
Cdd:PRK12852 20 VDILANAVKVTLGPKGRNVVIEKSFGAPRITKDGVTVAKEIELedkfENMGAQMVREVASKTNDLAGDGTTTATVLAQAI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 115 LRYAEELLDKNVHPTIIVSGYKKAAEEAVKKLHEIAEPIDINDEetLKKIAMTSLTSKAVHGarehlaeivvKAVRQVAE 194
Cdd:PRK12852 100 VREGAKAVAAGMNPMDLKRGIDIAVAAVVKDIEKRAKPVASSAE--IAQVGTISANGDAAIG----------KMIAQAMQ 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 195 KRGDKWYIDLDAIQIIKKhggslrDTKLIYGIVLDKEVVHP-------GMPKKVENAYIVLLD---APLEVEKPEIDAEI 264
Cdd:PRK12852 168 KVGNEGVITVEENKSLET------EVDIVEGMKFDRGYLSPyfvtnaeKMTVELDDAYILLHEkklSGLQAMLPVLEAVV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 265 RINDPAFLKKFLEEEEKILEEMVNKI---YNVAMERIRKDGMEGKA---GIVVITQ-KGIDEVAQHFLAKKGIMAVRRVK 337
Cdd:PRK12852 242 QSGKPLLIIAEDVEGEALATLVVNRLrggLKVAAVKAPGFGDRRKAmleDIAILTGgQLISEDLGIKLENVTLKMLGRAK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 338 RSDIEK----IARATGAK---------IVSNIDDLTPEdlgfaklvEERKVGEDKMVFIEGcpnpRAVTILIRGGLERLV 404
Cdd:PRK12852 322 KVVIDKenttIVNGAGKKadiearvgqIKAQIEETTSD--------YDREKLQERLAKLAG----GVAVIRVGGATEVEV 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 405 DEAERSINDALHAVADAIRDGkIVAGGGAVEVEVAKYLREIAPKiGGKEQLAVEAFARALEGLPMALAENAGLEPVEIIM 484
Cdd:PRK12852 390 KEKKDRVEDALNATRAAVQEG-IVPGGGVALLRAKKAVGRINND-NADVQAGINIVLKALEAPIRQIAENAGVEGSIVVG 467
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 485 KLRAAHAKAegkwVGVNVFKGDVDDMKKLGVIEPVSVKANAIKAGTEAATMVLRIDDIIA 544
Cdd:PRK12852 468 KILENKSET----FGFDAQTEEYVDMVAKGIIDPAKVVRTALQDAASVAGLLVTTEAMVA 523
|
|
| groEL |
PRK12851 |
chaperonin GroEL; Reviewed |
39-544 |
3.08e-14 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 171770 Cd Length: 541 Bit Score: 75.55 E-value: 3.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 39 VRAIAETLRTTYGPKGMDKMLVDSLGDITITNDGATILDKMDVQHP----TAKLVVQIAKGQDEEVGDGTKTAVIFAGEL 114
Cdd:PRK12851 20 VNILADAVKVTLGPKGRNVVIDKSFGAPTITNDGVTIAKEIELEDKfenmGAQMVREVASKTNDVAGDGTTTATVLAQAI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 115 LRYAEELLDKNVHPTIIVSGYKKAAEEAVKKLHEIAEPIDINDEetlkkiaMTSLTSKAVHGAREhLAEIVVKAVRQVAE 194
Cdd:PRK12851 100 VREGAKAVAAGANPMDLKRGIDRAVAAVVEELKANARPVTTNAE-------IAQVATISANGDAE-IGRLVAEAMEKVGN 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 195 krgdkwyidlDAIQIIKKHGGSLRDTKLIYGIVLDKEVVHP-------GMPKKVENAYIVLLDAPLEVEK---PEIDAEI 264
Cdd:PRK12851 172 ----------EGVITVEESKTAETELEVVEGMQFDRGYLSPyfvtdadKMEAELEDPYILIHEKKISNLQdllPVLEAVV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 265 RINDPAFLKKFLEEEEKILEEMVNKIynvamerirkdgmEGKAGIVVITQKGIDEvaqhflakkgimavRRvkRSDIEKI 344
Cdd:PRK12851 242 QSGKPLLIIAEDVEGEALATLVVNKL-------------RGGLKVAAVKAPGFGD--------------RR--KAMLEDI 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 345 ARATGAKIVS-----NIDDLTPEDLGFAKLVEerkVGEDKMVFIEGCPNPRAV--------------------------- 392
Cdd:PRK12851 293 AILTGGTVISedlgiKLENVTLEQLGRAKKVV---VEKENTTIIDGAGSKTEIegrvaqiraqieettsdydreklqerl 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 393 --------TILIRGGLERLVDEAERSINDALHAVADAIRDGkIVAGGGAVEVEVAKYLREIApKIGGKEQLAVEAFARAL 464
Cdd:PRK12851 370 aklaggvaVIRVGASTEVEVKEKKDRVDDALHATRAAVEEG-IVPGGGVALLRAVKALDKLE-TANGDQRTGVEIVRRAL 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 465 EGLPMALAENAGLEPVEIIMKLRaahaKAEGKWvGVNVFKGDVDDMKKLGVIEPVSVKANAIKAGTEAATMVLRIDDIIA 544
Cdd:PRK12851 448 EAPVRQIAENAGAEGSVVVGKLR----EKPGGY-GFNAATNEYGDLYAQGVIDPVKVVRTALQNAASVAGLLLTTEAMVA 522
|
|
| groEL |
CHL00093 |
chaperonin GroEL |
29-544 |
3.99e-13 |
|
chaperonin GroEL
Pssm-ID: 177025 Cd Length: 529 Bit Score: 71.67 E-value: 3.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 29 REALRTNIMIvraIAETLRTTYGPKGMDKMLVDSLGDITITNDGATILDKMDVQHPT----AKLVVQIAKGQDEEVGDGT 104
Cdd:CHL00093 12 RRALERGMDI---LAEAVSVTLGPKGRNVVLEKKYGSPQIVNDGVTIAKEIELEDHIentgVALIRQAASKTNDVAGDGT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 105 KTAVIFAGELLRYAEELLDKNVHPTIIVSGYKKAAEEAVKKLHEIAEPIDinDEETLKKIAMTSltskavHGAREHLAEI 184
Cdd:CHL00093 89 TTATVLAYAIVKQGMKNVAAGANPISLKRGIEKATQYVVSQIAEYARPVE--DIQAITQVASIS------AGNDEEVGSM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 185 VVKAVRQVAEkrgdkwyidlDAIQIIKKHGGSLRDTKLIYGIVLDKEVVHP-------GMPKKVENAYIVLLDAPLEVEK 257
Cdd:CHL00093 161 IADAIEKVGR----------EGVISLEEGKSTVTELEITEGMRFEKGFISPyfvtdteRMEVVQENPYILLTDKKITLVQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 258 ----PEIDAEIRINDPAFLKKFLEEEEKILEEMVNK---IYNVAMER------IRKDGMEGKA---GIVVITQ---KGID 318
Cdd:CHL00093 231 qdllPILEQVTKTKRPLLIIAEDVEKEALATLVLNKlrgIVNVVAVRapgfgdRRKAMLEDIAiltGGQVITEdagLSLE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 319 EVAQHFLAKkgimaVRR--VKRSDIEKIARATGAKIVSNIDDLTPEdLGFAKLVEERKVGEDKMVFIEGcpnprAVTILI 396
Cdd:CHL00093 311 TIQLDLLGQ-----ARRiiVTKDSTTIIADGNEEQVKARCEQLRKQ-IEIADSSYEKEKLQERLAKLSG-----GVAVIK 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 397 RGGL-ERLVDEAERSINDALHAVADAIRDGkIVAGGGAVEVEVAKYLREIAPK-IGGKEQLAVEAFARALEGLPMALAEN 474
Cdd:CHL00093 380 VGAAtETEMKDKKLRLEDAINATKAAVEEG-IVPGGGATLVHLSENLKTWAKNnLKEDELIGALIVARAILAPLKRIAEN 458
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 475 AGLEPVEIIMKLRAAHAKaegkwVGVNVFKGDVDDMKKLGVIEPVSVKANAIKAGTEAATMVLRIDDIIA 544
Cdd:CHL00093 459 AGKNGSVIIEKVQEQDFE-----IGYNAANNKFVNMYEAGIIDPAKVTRSALQNAASIASMILTTECIIV 523
|
|
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
39-544 |
8.48e-13 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 70.92 E-value: 8.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 39 VRAIAETLRTTYGPKGMDKMLVDSLGDITITNDGATILDKMDVQHPT----AKLVVQIAKGQDEEVGDGTKTAVIFAGEL 114
Cdd:PRK00013 19 VNKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDPFenmgAQLVKEVASKTNDVAGDGTTTATVLAQAI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 115 LRyaeELLdKNV----HPTIIVSGYKKAAEEAVKKLHEIAEPIdindeETLKKIAMTSLTSKavhGAREHLAEIVVKAVr 190
Cdd:PRK00013 99 VR---EGL-KNVaagaNPMDLKRGIDKAVEAAVEELKKISKPV-----EDKEEIAQVATISA---NGDEEIGKLIAEAM- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 191 qvaEKRGDKWYIDLDaiqiikkHGGSLRDT-KLIYGIVLDKEVVHPGM---PKK----VENAYIVLLDaplevekpeida 262
Cdd:PRK00013 166 ---EKVGKEGVITVE-------ESKGFETElEVVEGMQFDRGYLSPYFvtdPEKmeaeLENPYILITD------------ 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 263 eirindpaflkkfleeeekileemvNKIYNV-----AMERIRKDG---------MEGKA--GIVVITQKGIDEVAqhfla 326
Cdd:PRK00013 224 -------------------------KKISNIqdllpVLEQVAQSGkplliiaedVEGEAlaTLVVNKLRGTLKVV----- 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 327 kkgimAV-------RRvkRSDIEKIARATGAKIVS-----NIDDLTPEDLGFAKLVeerKVGEDKMVFIEGCPNPRAVTI 394
Cdd:PRK00013 274 -----AVkapgfgdRR--KAMLEDIAILTGGTVISeelglKLEDATLEDLGQAKKV---VVTKDNTTIVDGAGDKEAIKA 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 395 ---LIRGGL-------------ERL-----------------VDEAERS--INDALHAVADAIRDGkIVAGGGAVEVEVA 439
Cdd:PRK00013 344 rvaQIKAQIeettsdydreklqERLaklaggvavikvgaateVEMKEKKdrVEDALHATRAAVEEG-IVPGGGVALLRAA 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 440 KYLREIApKIGGKEQLAVEAFARALEGLPMALAENAGLEPVEIIMKLRaahaKAEGKWVGVNVFKGDVDDMKKLGVIEPV 519
Cdd:PRK00013 423 PALEALK-GLNGDEATGINIVLRALEAPLRQIAENAGLEGSVVVEKVK----NGKGKGYGYNAATGEYVDMIEAGIIDPT 497
|
570 580
....*....|....*....|....*
gi 500145658 520 SVKANAIKAGTEAATMVLRIDDIIA 544
Cdd:PRK00013 498 KVTRSALQNAASVAGLLLTTEAVVA 522
|
|
| PRK14104 |
PRK14104 |
chaperonin GroEL; Provisional |
27-544 |
2.22e-12 |
|
chaperonin GroEL; Provisional
Pssm-ID: 172594 Cd Length: 546 Bit Score: 69.67 E-value: 2.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 27 YGREALRTNIMIVRAIAETLRTTYGPKGMDKMLVDSLGDITITNDGATILDKMDV----QHPTAKLVVQIAKGQDEEVGD 102
Cdd:PRK14104 8 FGVDARDRMLRGVDILANAVKVTLGPKGRNVVLDKSFGAPRITKDGVTVAKEIELedkfENMGAQMVREVASKSADAAGD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 103 GTKTAVIFAGELLRYAEELLDKNVHPTIIVSGYKKAAEEAVKKLHEIAEPIDINDEetlkkiaMTSLTSKAVHGAREhLA 182
Cdd:PRK14104 88 GTTTATVLAQAIVREGAKSVAAGMNPMDLKRGIDLAVEAVVADLVKNSKKVTSNDE-------IAQVGTISANGDAE-IG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 183 EIVVKAVRQVaekrGDKWYIDLDAIQIIKKhggslrDTKLIYGIVLDKEVVHP-------GMPKKVENAYIVLLDAPLEV 255
Cdd:PRK14104 160 KFLADAMKKV----GNEGVITVEEAKSLET------ELDVVEGMQFDRGYISPyfvtnadKMRVEMDDAYILINEKKLSS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 256 EK---PEIDAEIRINDPAFLKKFLEEEEKILEEMVNKI---YNVAMERIRKDGMEGKA---GIVVITQ-KGIDEVAQHFL 325
Cdd:PRK14104 230 LNellPLLEAVVQTGKPLVIVAEDVEGEALATLVVNRLrggLKVAAVKAPGFGDRRKAmlqDIAILTGgQAISEDLGIKL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 326 AKKGIMAVRRVKRSDIEK----IARATGAKIvsnidDLTPEDLGFAKLVEERKVGEDKMVFIEGCPNPRAVTILIR--GG 399
Cdd:PRK14104 310 ENVTLQMLGRAKKVMIDKenttIVNGAGKKA-----DIEARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRvgGA 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 400 LERLVDEAERSINDALHAVADAIRDGkIVAGGGAVEVEVAKYLREIAPKiGGKEQLAVEAFARALEGLPMALAENAGLEP 479
Cdd:PRK14104 385 TEVEVKERKDRVDDAMHATRAAVEEG-IVPGGGVALLRASEQLKGIKTK-NDDQKTGVEIVRKALSAPARQIAINAGEDG 462
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 500145658 480 VEIIMKLraahAKAEGKWVGVNVFKGDVDDMKKLGVIEPVSVKANAIKAGTEAATMVLRIDDIIA 544
Cdd:PRK14104 463 SVIVGKI----LEKEQYSYGFDSQTGEYGNLVSKGIIDPTKVVRTAIQNAASVAALLITTEAMVA 523
|
|
| PLN03167 |
PLN03167 |
Chaperonin-60 beta subunit; Provisional |
39-521 |
5.25e-11 |
|
Chaperonin-60 beta subunit; Provisional
Pssm-ID: 215611 [Multi-domain] Cd Length: 600 Bit Score: 65.33 E-value: 5.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 39 VRAIAETLRTTYGPKGMDKMLVDSLGDITITNDGATILDKMDVQHPT----AKLVVQIAKGQDEEVGDGTKTAVIFAGEL 114
Cdd:PLN03167 75 VNKLADLVGVTLGPKGRNVVLESKYGSPKIVNDGVTVAKEVELEDPVenigAKLVRQAAAKTNDLAGDGTTTSVVLAQGL 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 115 LRYAEELLDKNVHPTIIVSGYKKAAEEAVKKLHEIAEpiDINDEEtLKKIAMTSLtskavhGAREHLAEIVVKAVRQVAE 194
Cdd:PLN03167 155 IAEGVKVVAAGANPVQITRGIEKTAKALVKELKKMSK--EVEDSE-LADVAAVSA------GNNYEVGNMIAEAMSKVGR 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 195 KrgdkwyidldAIQIIKKHGGSLRDTKLIYGIVLDKEVVHP-------GMPKKVENAYIVLLDAPLEVEKPEI---DAEI 264
Cdd:PLN03167 226 K----------GVVTLEEGKSAENNLYVVEGMQFDRGYISPyfvtdseKMSVEYDNCKLLLVDKKITNARDLIgilEDAI 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 265 RINDPAFLKKFLEEEEKILEEMVNKIynvamerirkdgmEGKAGIVVITQKGIDEVAQHFLAKKGIMAVRRVKRSDI--- 341
Cdd:PLN03167 296 RGGYPLLIIAEDIEQEALATLVVNKL-------------RGSLKIAALKAPGFGERKSQYLDDIAILTGGTVIREEVgls 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 342 -EKIAR---ATGAKIVSNIDDLTPEDLGFAKLVEERKVGEDKMVfIEGCP--------NPR-------AVTILIRGGLER 402
Cdd:PLN03167 363 lDKVGKevlGTAAKVVLTKDTTTIVGDGSTQEAVNKRVAQIKNL-IEAAEqdyekeklNERiaklsggVAVIQVGAQTET 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500145658 403 LVDEAERSINDALHAVADAIRDGkIVAGGGAVEVEVAKYLREIAPKIGGKEQ-LAVEAFARALeGLPMAL-AENAGLEPV 480
Cdd:PLN03167 442 ELKEKKLRVEDALNATKAAVEEG-IVVGGGCTLLRLASKVDAIKDTLENDEQkVGADIVKRAL-SYPLKLiAKNAGVNGS 519
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 500145658 481 EIIMKLRAahakAEGKWVGVNVFKGDVDDMKKLGVIEPVSV 521
Cdd:PLN03167 520 VVSEKVLS----NDNPKFGYNAATGKYEDLMAAGIIDPTKV 556
|
|
| |
