|
Name |
Accession |
Description |
Interval |
E-value |
| TCP1_delta |
cd03338 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ... |
22-535 |
0e+00 |
|
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: 945.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 22 DNKRREDIRFANINSARAVSDAVRTSLGPKGMDKMISTANGEVIITNDGATILNKMEVLQPAAKMLVELSKSQDSAAGDG 101
Cdd:cd03338 2 DKEKPADVRLSNIQAAKAVADAIRTSLGPRGMDKMIQTGKGEVIITNDGATILKQMSVLHPAAKMLVELSKAQDIEAGDG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 102 TTTVVVIAGALLKECQSLLTNGIHPTVISDSLHKACGKAIDILTAMAVPVELTDRDSLVKSASTSLNSKVVSQYSTLLAP 181
Cdd:cd03338 82 TTSVVVLAGALLSACESLLKKGIHPTVISESFQIAAKKAVEILDSMSIPVDLNDRESLIKSATTSLNSKVVSQYSSLLAP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 182 LAVDAVLSVIDPEKPEIVDLRDIKIVKKLGGTVDDTHTVKGLVFDKKVSRAAGGPTRVENAKIAVIQFQISPPKTDIEQS 261
Cdd:cd03338 162 IAVDAVLKVIDPATATNVDLKDIRIVKKLGGTIEDTELVDGLVFTQKASKKAGGPTRIEKAKIGLIQFCLSPPKTDMDNN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 262 IVVSDYTQMDRILKEERNYILGMIKKIKATGCNVLLIQKSILRDAVTDLSLHYLAKAKIMVIKDVERDEIEFVTKTLNCL 341
Cdd:cd03338 242 IVVNDYAQMDRILREERKYILNMCKKIKKSGCNVLLIQKSILRDAVSDLALHFLAKLKIMVVKDIEREEIEFICKTIGCK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 342 PIANIEHFRAEKLGHADLVEEASLGDGKILKITGIKDMGRTTSVLVRGSNQLVLDEAERSLHDALCVVRCLVSKRFLIAG 421
Cdd:cd03338 322 PVASIDHFTEDKLGSADLVEEVSLGDGKIVKITGVKNPGKTVTILVRGSNKLVLDEAERSLHDALCVIRCLVKKRALIPG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 422 GGAPEIELSRQLGAWAKVLHGMEGYCVKSFAEALEVIPYTLAENAGLNPIAIVTELRNKHAQGEINAGINVRKGQITNIL 501
Cdd:cd03338 402 GGAPEIEIALQLSEWARTLTGVEQYCVRAFADALEVIPYTLAENAGLNPISIVTELRNRHAQGEKNAGINVRKGAITNIL 481
|
490 500 510
....*....|....*....|....*....|....
gi 15229595 502 EENVVQPLLVSTSAITLATECVRMILKIDDIVTV 535
Cdd:cd03338 482 EENVVQPLLVSTSAITLATETVRMILKIDDIVLA 515
|
|
| chap_CCT_delta |
TIGR02342 |
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ... |
20-536 |
0e+00 |
|
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: 820.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 20 FVDNKRREDIRFANINSARAVSDAVRTSLGPKGMDKMISTANGEVIITNDGATILNKMEVLQPAAKMLVELSKSQDSAAG 99
Cdd:TIGR02342 1 FQDKDKPQDVRTSNIVAAKAVADAIRTSLGPKGMDKMIQDGKGEVIITNDGATILKQMAVLHPAAKMLVELSKAQDIEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 100 DGTTTVVVIAGALLKECQSLLTNGIHPTVISDSLHKACGKAIDILTAMAVPVELTDRDSLVKSASTSLNSKVVSQYSTLL 179
Cdd:TIGR02342 81 DGTTSVVILAGALLGACERLLNKGIHPTIISESFQSAADEAIKILDEMSIPVDLSDREQLLKSATTSLSSKVVSQYSSLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 180 APLAVDAVLSVIDPEKPEIVDLRDIKIVKKLGGTVDDTHTVKGLVFDKKVSRAAGGPTRVENAKIAVIQFQISPPKTDIE 259
Cdd:TIGR02342 161 APLAVDAVLKVIDPENAKNVDLNDIKVVKKLGGTIDDTELIEGLVFTQKASKSAGGPTRIEKAKIGLIQFQISPPKTDME 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 260 QSIVVSDYTQMDRILKEERNYILGMIKKIKATGCNVLLIQKSILRDAVTDLSLHYLAKAKIMVIKDVERDEIEFVTKTLN 339
Cdd:TIGR02342 241 NQIIVNDYAQMDRVLKEERAYILNIVKKIKKTGCNVLLIQKSILRDAVNDLALHFLAKMKIMVVKDIEREEIEFICKTIG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 340 CLPIANIEHFRAEKLGHADLVEEASLGDGKILKITGIKDMGRTTSVLVRGSNQLVLDEAERSLHDALCVVRCLVSKRFLI 419
Cdd:TIGR02342 321 CKPIASIDHFTADKLGSAELVEEVDSDGGKIIKITGIQNAGKTVTVVVRGSNKLVIDEAERSLHDALCVIRCLVKKRGLI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 420 AGGGAPEIELSRQLGAWAKVLHGMEGYCVKSFAEALEVIPYTLAENAGLNPIAIVTELRNKHAQGEINAGINVRKGQITN 499
Cdd:TIGR02342 401 AGGGAPEIEIARRLSKYARTMKGVESYCVRAFADALEVIPYTLAENAGLNPIKVVTELRNRHANGEKTAGISVRKGGITN 480
|
490 500 510
....*....|....*....|....*....|....*..
gi 15229595 500 ILEENVVQPLLVSTSAITLATECVRMILKIDDIVTVR 536
Cdd:TIGR02342 481 MLEEHVLQPLLVTTSAITLASETVRSILKIDDIVFTR 517
|
|
| chaperonin_type_I_II |
cd00309 |
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ... |
22-534 |
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: 562.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 22 DNKRREDIRFANINSARAVSDAVRTSLGPKGMDKMISTANGEVIITNDGATILNKMEVLQPAAKMLVELSKSQDSAAGDG 101
Cdd:cd00309 2 EREFGEEARLSNINAAKALADAVKTTLGPKGMDKMLVDSLGDPTITNDGATILKEIEVEHPAAKLLVEVAKSQDDEVGDG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 102 TTTVVVIAGALLKECQSLLTNGIHPTVISDSLHKACGKAIDILTAMAVPVELTDRDSLVKSASTSLNSKVVSQYSTLLAP 181
Cdd:cd00309 82 TTTVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVPIDVEDREELLKVATTSLNSKLVSGGDDFLGE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 182 LAVDAVLSVIDPEkpEIVDLRDIKIVKKLGGTVDDTHTVKGLVFDKKVsRAAGGPTRVENAKIAVIQFQISPpktdieqs 261
Cdd:cd00309 162 LVVDAVLKVGKEN--GDVDLGVIRVEKKKGGSLEDSELVVGMVFDKGY-LSPYMPKRLENAKILLLDCKLEY-------- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 262 ivvsdytqmdrilkeernyilgmikkikatgcnVLLIQKSIlrdavTDLSLHYLAKAKIMVIKDVERDEIEFVTKTLNCL 341
Cdd:cd00309 231 ---------------------------------VVIAEKGI-----DDEALHYLAKLGIMAVRRVRKEDLERIAKATGAT 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 342 PIANIEHFRAEKLGHADLVEEASLGDGKILKITGIKDmGRTTSVLVRGSNQLVLDEAERSLHDALCVVRCLVSKRFLIAG 421
Cdd:cd00309 273 IVSRLEDLTPEDLGTAGLVEETKIGDEKYTFIEGCKG-GKVATILLRGATEVELDEAERSLHDALCAVRAAVEDGGIVPG 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 422 GGAPEIELSRQLGAWAKVLHGMEGYCVKSFAEALEVIPYTLAENAGLNPIAIVTELRNKHAQGEINAGINVRKGQITNIL 501
Cdd:cd00309 352 GGAAEIELSKALEELAKTLPGKEQLGIEAFADALEVIPRTLAENAGLDPIEVVTKLRAKHAEGGGNAGGDVETGEIVDMK 431
|
490 500 510
....*....|....*....|....*....|...
gi 15229595 502 EENVVQPLLVSTSAITLATECVRMILKIDDIVT 534
Cdd:cd00309 432 EAGIIDPLKVKRQALKSATEAASLILTIDDIIV 464
|
|
| Cpn60_TCP1 |
pfam00118 |
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ... |
40-533 |
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: 546.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 40 VSDAVRTSLGPKGMDKMISTANGEVIITNDGATILNKMEVLQPAAKMLVELSKSQDSAAGDGTTTVVVIAGALLKECQSL 119
Cdd:pfam00118 1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELEIQHPAAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEEAEKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 120 LTNGIHPTVISDSLHKACGKAIDILTAM-AVPVELTDRDSLVKSASTSLNSKVVSQYSTLLAPLAVDAVLSVidPEKPEI 198
Cdd:pfam00118 81 LAAGVHPTTIIEGYEKALEKALEILDSIiSIPVEDVDREDLLKVARTSLSSKIISRESDFLAKLVVDAVLAI--PKNDGS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 199 VDLRDIKIVKKLGGTVDDTHTVKGLVFDKKVSRAAGgPTRVENAKIAVIQFQISPPKTDIEQSIVVSDYTQMDRILKEER 278
Cdd:pfam00118 159 FDLGNIGVVKILGGSLEDSELVDGVVLDKGPLHPDM-PKRLENAKVLLLNCSLEYEKTETKATVVLSDAEQLERFLKAEE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 279 NYILGMIKKIKATGCNVLLIQKSIlrdavTDLSLHYLAKAKIMVIKDVERDEIEFVTKTLNCLPIANIEHFRAEKLGHAD 358
Cdd:pfam00118 238 EQILEIVEKIIDSGVNVVVCQKGI-----DDLALHFLAKNGIMALRRVKKRDLERLAKATGARAVSSLDDLTPDDLGTAG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 359 LVEEASLGDGKILKITGIKDmGRTTSVLVRGSNQLVLDEAERSLHDALCVVRCLVSKRFLIAGGGAPEIELSRQLGAWAK 438
Cdd:pfam00118 313 KVEEEKIGDEKYTFIEGCKS-PKAATILLRGATDHVLDEIERSIHDALCVVKNAIEDPRVVPGGGAVEMELARALREYAK 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 439 VLHGMEGYCVKSFAEALEVIPYTLAENAGLNPIAIVTELRNKHAQGEINAGINVRKGQITNILEENVVQPLLVSTSAITL 518
Cdd:pfam00118 392 SVSGKEQLAIEAFAEALEVIPKTLAENAGLDPIEVLAELRAAHASGEKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKS 471
|
490
....*....|....*
gi 15229595 519 ATECVRMILKIDDIV 533
Cdd:pfam00118 472 ATEAASTILRIDDII 486
|
|
| thermosome_alpha |
NF041082 |
thermosome subunit alpha; |
28-533 |
0e+00 |
|
thermosome subunit alpha;
Pssm-ID: 469009 Cd Length: 518 Bit Score: 526.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 28 DIRFANINSARAVSDAVRTSLGPKGMDKMISTANGEVIITNDGATILNKMEVLQPAAKMLVELSKSQDSAAGDGTTTVVV 107
Cdd:NF041082 17 DAQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDVVITNDGVTILKEMDIEHPAAKMIVEVAKTQDDEVGDGTTTAVV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 108 IAGALLKECQSLLTNGIHPTVISDSLHKACGKAIDILTAMAVPVELTDRDSLVKSASTSLNSKVVSQYSTLLAPLAVDAV 187
Cdd:NF041082 97 LAGELLKKAEELLDQDIHPTIIAEGYRLAAEKALEILDEIAIKVDPDDKETLKKIAATAMTGKGAEAAKDKLADLVVDAV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 188 LSVIDPEKPEIVDLRDIKIVKKLGGTVDDTHTVKGLVFDKKVSRaAGGPTRVENAKIAVIQFQISPPKTDIEQSIVVSDY 267
Cdd:NF041082 177 KAVAEKDGGYNVDLDNIKVEKKVGGSIEDSELVEGVVIDKERVH-PGMPKRVENAKIALLDAPLEVKKTEIDAKISITDP 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 268 TQMDRILKEERNYILGMIKKIKATGCNVLLIQKSIlrdavTDLSLHYLAKAKIMVIKDVERDEIEFVTKTLNCLPIANIE 347
Cdd:NF041082 256 DQLQAFLDQEEKMLKEMVDKIADSGANVVFCQKGI-----DDLAQHYLAKEGILAVRRVKKSDMEKLAKATGARIVTSID 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 348 HFRAEKLGHADLVEEASLGDGKILKITGIKDmGRTTSVLVRGSNQLVLDEAERSLHDALCVVRCLVSKRFLIAGGGAPEI 427
Cdd:NF041082 331 DLSPEDLGYAGLVEERKVGGDKMIFVEGCKN-PKAVTILLRGGTEHVVDEVERALEDALRVVRVVLEDGKVVAGGGAPEV 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 428 ELSRQLGAWAKVLHGMEGYCVKSFAEALEVIPYTLAENAGLNPIAIVTELRNKHAQGEINAGINVRKGQITNILEENVVQ 507
Cdd:NF041082 410 ELALRLREYAASVGGREQLAIEAFAEALEIIPRTLAENAGLDPIDALVELRSAHEKGNKTAGLDVYTGKVVDMLEIGVVE 489
|
490 500
....*....|....*....|....*.
gi 15229595 508 PLLVSTSAITLATECVRMILKIDDIV 533
Cdd:NF041082 490 PLRVKTQAIKSATEAAVMILRIDDVI 515
|
|
| cpn60 |
cd03343 |
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ... |
27-533 |
1.40e-180 |
|
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: 517.97 E-value: 1.40e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 27 EDIRFANINSARAVSDAVRTSLGPKGMDKMISTANGEVIITNDGATILNKMEVLQPAAKMLVELSKSQDSAAGDGTTTVV 106
Cdd:cd03343 14 RDAQRMNIAAAKAVAEAVRTTLGPKGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAKTQDEEVGDGTTTAV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 107 VIAGALLKECQSLLTNGIHPTVISDSLHKACGKAIDILTAMAVPVELTDRDSLVKSASTSLNSKVVSQYSTLLAPLAVDA 186
Cdd:cd03343 94 VLAGELLEKAEDLLDQNIHPTVIIEGYRLAAEKALELLDEIAIKVDPDDKDTLRKIAKTSLTGKGAEAAKDKLADLVVDA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 187 VLSVIDPEKPEI-VDLRDIKIVKKLGGTVDDTHTVKGLVFDKKVSRaAGGPTRVENAKIAVIQFQISPPKTDIEQSIVVS 265
Cdd:cd03343 174 VLQVAEKRDGKYvVDLDNIKIEKKTGGSVDDTELIRGIVIDKEVVH-PGMPKRVENAKIALLDAPLEVKKTEIDAKIRIT 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 266 DYTQMDRILKEERNYILGMIKKIKATGCNVLLIQKSIlrdavTDLSLHYLAKAKIMVIKDVERDEIEFVTKTLNCLPIAN 345
Cdd:cd03343 253 SPDQLQAFLEQEEAMLKEMVDKIADTGANVVFCQKGI-----DDLAQHYLAKAGILAVRRVKKSDMEKLARATGAKIVTN 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 346 IEHFRAEKLGHADLVEEASLGDGKILKITGIKDmGRTTSVLVRGSNQLVLDEAERSLHDALCVVRCLVSKRFLIAGGGAP 425
Cdd:cd03343 328 IDDLTPEDLGEAELVEERKVGDDKMVFVEGCKN-PKAVTILLRGGTEHVVDELERALEDALRVVADALEDGKVVAGGGAV 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 426 EIELSRQLGAWAKVLHGMEGYCVKSFAEALEVIPYTLAENAGLNPIAIVTELRNKHAQGEINAGINVRKGQITNILEENV 505
Cdd:cd03343 407 EIELAKRLREYARSVGGREQLAVEAFADALEEIPRTLAENAGLDPIDTLVELRAAHEKGNKNAGLDVYTGEVVDMLEKGV 486
|
490 500
....*....|....*....|....*...
gi 15229595 506 VQPLLVSTSAITLATECVRMILKIDDIV 533
Cdd:cd03343 487 IEPLRVKKQAIKSATEAATMILRIDDVI 514
|
|
| thermosome_beta |
NF041083 |
thermosome subunit beta; |
28-533 |
2.51e-178 |
|
thermosome subunit beta;
Pssm-ID: 469010 Cd Length: 519 Bit Score: 512.19 E-value: 2.51e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 28 DIRFANINSARAVSDAVRTSLGPKGMDKMISTANGEVIITNDGATILNKMEVLQPAAKMLVELSKSQDSAAGDGTTTVVV 107
Cdd:NF041083 17 DAQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDIVITNDGATILKEMDVQHPAAKMLVEVAKTQDDEVGDGTTTAVV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 108 IAGALLKECQSLLTNGIHPTVISDSLHKACGKAIDILTAMAVPVELTDRDSLVKSASTSLNSKVVSQYSTLLAPLAVDAV 187
Cdd:NF041083 97 LAGELLKKAEELLDQNIHPTIIANGYRLAAEKAIEILDEIAEKVDPDDRETLKKIAETSLTSKGVEEARDYLAEIAVKAV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 188 LSVIDPEKPEI-VDLRDIKIVKKLGGTVDDTHTVKGLVFDKKVSRaAGGPTRVENAKIAVIQFQISPPKTDIEQSIVVSD 266
Cdd:NF041083 177 KQVAEKRDGKYyVDLDNIQIEKKHGGSIEDTQLIYGIVIDKEVVH-PGMPKRVENAKIALLDAPLEVKKTEIDAEIRITD 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 267 YTQMDRILKEERNYILGMIKKIKATGCNVLLIQKSIlrdavTDLSLHYLAKAKIMVIKDVERDEIEFVTKTLNCLPIANI 346
Cdd:NF041083 256 PDQLQKFLDQEEKMLKEMVDKIKATGANVVFCQKGI-----DDLAQHYLAKAGILAVRRVKKSDMEKLAKATGARIVTNI 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 347 EHFRAEKLGHADLVEEASLGDGKILKITGIKDmGRTTSVLVRGSNQLVLDEAERSLHDALCVVRCLVSKRFLIAGGGAPE 426
Cdd:NF041083 331 DDLTPEDLGYAELVEERKVGDDKMVFVEGCKN-PKAVTILIRGGTEHVVDEAERALEDALSVVADAVEDGKIVAGGGAPE 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 427 IELSRQLGAWAKVLHGMEGYCVKSFAEALEVIPYTLAENAGLNPIAIVTELRNKHAQGEINAGINVRKGQITNILEENVV 506
Cdd:NF041083 410 VELAKRLREYAATVGGREQLAVEAFAEALEIIPRTLAENAGLDPIDILVKLRSAHEKGKKWAGINVFTGEVVDMWELGVI 489
|
490 500
....*....|....*....|....*..
gi 15229595 507 QPLLVSTSAITLATECVRMILKIDDIV 533
Cdd:NF041083 490 EPLRVKTQAIKSATEAATMILRIDDVI 516
|
|
| thermosome_arch |
TIGR02339 |
thermosome, various subunits, archaeal; Thermosome is the name given to the archaeal rather ... |
28-533 |
1.37e-172 |
|
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: 497.67 E-value: 1.37e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 28 DIRFANINSARAVSDAVRTSLGPKGMDKMISTANGEVIITNDGATILNKMEVLQPAAKMLVELSKSQDSAAGDGTTTVVV 107
Cdd:TIGR02339 16 DAQRNNIAAAKAVAEAVKSTLGPRGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAKTQDEEVGDGTTTAVV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 108 IAGALLKECQSLLTNGIHPTVISDSLHKACGKAIDILTAMAVPVELTDRDSLVKSASTSLNSKVVSQYST-LLAPLAVDA 186
Cdd:TIGR02339 96 LAGELLEKAEDLLEQDIHPTVIIEGYRKAAEKALEIIDEIATKISPEDRDLLKKIAYTSLTSKASAEVAKdKLADLVVEA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 187 VLSVI--DPEKPEIVDLRDIKIVKKLGGTVDDTHTVKGLVFDKKVSRaAGGPTRVENAKIAVIQFQISPPKTDIEQSIVV 264
Cdd:TIGR02339 176 VKQVAelRGDGKYYVDLDNIKIVKKKGGSIEDTELVEGIVVDKEVVH-PGMPKRVENAKIALLDAPLEVEKTEIDAKIRI 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 265 SDYTQMDRILKEERNYILGMIKKIKATGCNVLLIQKSIlrdavTDLSLHYLAKAKIMVIKDVERDEIEFVTKTLNCLPIA 344
Cdd:TIGR02339 255 TDPDQIKKFLDQEEAMLKEMVDKIASAGANVVICQKGI-----DDVAQHYLAKAGILAVRRVKKSDIEKLARATGARIVS 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 345 NIEHFRAEKLGHADLVEEASLGDGKILKITGIKDmGRTTSVLVRGSNQLVLDEAERSLHDALCVVRCLVSKRFLIAGGGA 424
Cdd:TIGR02339 330 SIDEITESDLGYAELVEERKVGEDKMVFVEGCKN-PKAVTILLRGGTEHVVDELERSIQDALHVVANALEDGKIVAGGGA 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 425 PEIELSRQLGAWAKVLHGMEGYCVKSFAEALEVIPYTLAENAGLNPIAIVTELRNKHAQGEINAGINVRKGQITNILEEN 504
Cdd:TIGR02339 409 VEIELALRLRSYARSVGGREQLAIEAFADALEEIPRILAENAGLDPIDALVDLRAKHEKGNKNAGINVFTGEIEDMLELG 488
|
490 500
....*....|....*....|....*....
gi 15229595 505 VVQPLLVSTSAITLATECVRMILKIDDIV 533
Cdd:TIGR02339 489 VIEPLRVKEQAIKSATEAATMILRIDDVI 517
|
|
| TCP1_epsilon |
cd03339 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ... |
32-534 |
3.63e-145 |
|
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: 427.87 E-value: 3.63e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 32 ANINSARAVSDAVRTSLGPKGMDKMISTANGEVIITNDGATILNKMEVLQPAAKMLVELSKSQDSAAGDGTTTVVVIAGA 111
Cdd:cd03339 27 SHILAAKSVANILRTSLGPRGMDKILVSPDGEVTVTNDGATILEKMDVDHQIAKLLVELSKSQDDEIGDGTTGVVVLAGA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 112 LLKECQSLLTNGIHPTVISDSLHKACGKAIDILTAMA--VPVELTDRDSLVKSASTSLNSKVVSQYSTLLAPLAVDAVLS 189
Cdd:cd03339 107 LLEQAEKLLDRGIHPIRIADGYEQACKIAVEHLEEIAdkIEFSPDNKEPLIQTAMTSLGSKIVSRCHRQFAEIAVDAVLS 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 190 VIDPEKPEiVDLRDIKIVKKLGGTVDDTHTVKGLVFDKKVSRaAGGPTRVENAKIAVIQFQISPPKTDIEQSIVVSDYTQ 269
Cdd:cd03339 187 VADLERKD-VNFELIKVEGKVGGRLEDTKLVKGIVIDKDFSH-PQMPKEVKDAKIAILTCPFEPPKPKTKHKLDITSVED 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 270 MDRILKEERNYILGMIKKIKATGCNVLLIQKSIlrdavTDLSLHYLAKAKIMVIKDVERDEIEFVTKTLNCLPIANIEHF 349
Cdd:cd03339 265 YKKLQEYEQKYFREMVEQVKDAGANLVICQWGF-----DDEANHLLLQNGLPAVRWVGGVEIELIAIATGGRIVPRFEDL 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 350 RAEKLGHADLVEEASLG--DGKILKITGIKDmGRTTSVLVRGSNQLVLDEAERSLHDALCVVRCLVSKRFLIAGGGAPEI 427
Cdd:cd03339 340 SPEKLGKAGLVREISFGttKDKMLVIEGCPN-SKAVTIFIRGGNKMIIEEAKRSLHDALCVVRNLIRDNRIVYGGGAAEI 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 428 ELSRQLGAWAKVLHGMEGYCVKSFAEALEVIPYTLAENAGLNPIAIVTELRNKH-AQGEINAGINVRKGQITNILEENVV 506
Cdd:cd03339 419 SCSLAVEKAADKCSGIEQYAMRAFADALESIPLALAENSGLNPIETLSEVKARQvKEKNPHLGIDCLGRGTNDMKEQKVF 498
|
490 500
....*....|....*....|....*...
gi 15229595 507 QPLLVSTSAITLATECVRMILKIDDIVT 534
Cdd:cd03339 499 ETLISKKQQILLATQVVKMILKIDDVIV 526
|
|
| chap_CCT_epsi |
TIGR02343 |
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ... |
22-533 |
4.09e-126 |
|
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: 379.15 E-value: 4.09e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 22 DNKRR---EDIRFANINSARAVSDAVRTSLGPKGMDKMISTANGEVIITNDGATILNKMEVLQPAAKMLVELSKSQDSAA 98
Cdd:TIGR02343 18 DNKKRlkgLEAKKSNIAAAKSVASILRTSLGPKGMDKMLISPDGDITVTNDGATILSQMDVDNQIAKLMVELSKSQDDEI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 99 GDGTTTVVVIAGALLKECQSLLTNGIHPTVISDSLHKACGKAIDIL--TAMAVPVELTDRDSLVKSASTSLNSKVVSQYS 176
Cdd:TIGR02343 98 GDGTTGVVVLAGALLEQAEELLDKGIHPIKIADGFEEAARIAVEHLeeISDEISADNNNREPLIQAAKTSLGSKIVSKCH 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 177 TLLAPLAVDAVLSVIDPEKPEiVDLRDIKIVKKLGGTVDDTHTVKGLVFDKKVSRAAgGPTRVENAKIAVIQFQISPPKT 256
Cdd:TIGR02343 178 RRFAEIAVDAVLNVADMERRD-VDFDLIKVEGKVGGSLEDTKLIKGIIIDKDFSHPQ-MPKEVEDAKIAILTCPFEPPKP 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 257 DIEQSIVVSDYTQMDRILKEERNYILGMIKKIKATGCNVLLIQKSIlrdavTDLSLHYLAKAKIMVIKDVERDEIEFVTK 336
Cdd:TIGR02343 256 KTKHKLDISSVEEYKKLQKYEQQKFKEMIDDIKKSGANLVICQWGF-----DDEANHLLLQNDLPAVRWVGGQELELIAI 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 337 TLNCLPIANIEHFRAEKLGHADLVEEASLG--DGKILKITGIKDmGRTTSVLVRGSNQLVLDEAERSLHDALCVVRCLVS 414
Cdd:TIGR02343 331 ATGGRIVPRFQELSKDKLGKAGLVREISFGttKDRMLVIEQCKN-SKAVTIFIRGGNKMIIEEAKRSIHDALCVVRNLIK 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 415 KRFLIAGGGAPEIELSRQLGAWAKVLHGMEGYCVKSFAEALEVIPYTLAENAGLNPIAIVTELRNKHAQGEI-NAGINVR 493
Cdd:TIGR02343 410 DSRIVYGGGAAEISCSLAVSQEADKYPGVEQYAIRAFADALETIPMALAENSGLDPIGTLSTLKSLQLKEKNpNLGVDCL 489
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 15229595 494 KGQITNILEENVVQPLLVSTSAITLATECVRMILKIDDIV 533
Cdd:TIGR02343 490 GYGTNDMKEQFVFETLIGKKQQILLATQLVRMILKIDDVI 529
|
|
| TCP1_eta |
cd03340 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ... |
33-534 |
5.95e-120 |
|
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: 363.15 E-value: 5.95e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 33 NINSARAVSDAVRTSLGPKGMDKMISTANGEVIITNDGATILNKMEVLQPAAKMLVELSKSQDSAAGDGTTTVVVIAGAL 112
Cdd:cd03340 21 NINACQAIADAVRTTLGPRGMDKLIVDGRGKVTISNDGATILKLLDIVHPAAKTLVDIAKSQDAEVGDGTTSVVVLAGEF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 113 LKECQSLLTNGIHPTVISDSLHKACGKAIDILTAMAVPVELTD----RDSLVKSASTSLNSKVVSQYSTLLAPLAVDAVL 188
Cdd:cd03340 101 LKEAKPFIEDGVHPQIIIRGYRKALQLAIEKIKEIAVNIDKEDkeeqRELLEKCAATALNSKLIASEKEFFAKMVVDAVL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 189 SVIDpekpeIVDLRDIKIVKKLGGTVDDTHTVKGLVFDKKVSRAA--GGPTRVENAKIAV--IQFQISPPKTDIEqsIVV 264
Cdd:cd03340 181 SLDD-----DLDLDMIGIKKVPGGSLEDSQLVNGVAFKKTFSYAGfeQQPKKFKNPKILLlnVELELKAEKDNAE--VRV 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 265 SDYTQMDRILKEERNYILGMIKKIKATGCNVLLIQKSIlrdavTDLSLHYLAKAKIMVIKDVERDEIEFVTKTLNCLPIA 344
Cdd:cd03340 254 EDPEEYQAIVDAEWKIIYDKLEKIVKSGANVVLSKLPI-----GDLATQYFADRDIFCAGRVPEEDLKRVAQATGGSIQT 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 345 NIEHFRAEKLGHADLVEEASLGDGKILKITGIKdMGRTTSVLVRGSNQLVLDEAERSLHDALCVVRCLVSKRFLIAGGGA 424
Cdd:cd03340 329 TVSNITDDVLGTCGLFEERQVGGERYNIFTGCP-KAKTCTIILRGGAEQFIEEAERSLHDAIMIVRRAIKNDSVVAGGGA 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 425 PEIELSRQLGAWAKVLHGMEGYCVKSFAEALEVIPYTLAENAGLNPIAIVTELRNKHAQGE-INAGINVRKGQITNILEE 503
Cdd:cd03340 408 IEMELSKYLRDYSRTIAGKQQLVINAFAKALEIIPRQLCDNAGFDATDILNKLRQKHAQGGgKWYGVDINNEGIADNFEA 487
|
490 500 510
....*....|....*....|....*....|.
gi 15229595 504 NVVQPLLVSTSAITLATECVRMILKIDDIVT 534
Cdd:cd03340 488 FVWEPSLVKINALTAATEAACLILSVDETIK 518
|
|
| TCP1_alpha |
cd03335 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ... |
27-535 |
7.15e-118 |
|
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: 357.75 E-value: 7.15e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 27 EDIRFANINSARAVSDAVRTSLGPKGMDKMISTANGEVIITNDGATILNKMEVLQPAAKMLVELSKSQDSAAGDGTTTVV 106
Cdd:cd03335 7 QDVRTQNVTAAMAIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDKEVGDGTTSVV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 107 VIAGALLKECQSLLTNGIHPTVISDSLHKACGKAID-ILTAMAVPVELTDRDSLVKSASTSLNSKVVSQYSTLLAPLAVD 185
Cdd:cd03335 87 IIAAELLKRANELVKQKIHPTTIISGYRLACKEAVKyIKEHLSISVDNLGKESLINVAKTSMSSKIIGADSDFFANMVVD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 186 AVLSV--IDPEKPEIVDLRDIKIVKKLGGTVDDTHTVKGLVFDkkVSRAAGG-PTRVENAKIAVIQFQISPPKTDIEQSI 262
Cdd:cd03335 167 AILAVktTNEKGKTKYPIKAVNILKAHGKSAKESYLVNGYALN--CTRASQGmPTRVKNAKIACLDFNLQKTKMKLGVQV 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 263 VVSDYTQMDRILKEERNYILGMIKKIKATGCNVLLIQKSIlrdavTDLSLHYLAKAKIMVIKDVERDEIEFVTKTLN--- 339
Cdd:cd03335 245 VVTDPEKLEKIRQRESDITKERIKKILAAGANVVLTTGGI-----DDMCLKYFVEAGAMAVRRVKKEDLRRIAKATGatl 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 340 CLPIANI---EHFRAEKLGHADLVEEASLGDGKILKITGIKDmGRTTSVLVRGSNQLVLDEAERSLHDALCVV-RCLVSK 415
Cdd:cd03335 320 VSTLANLegeETFDPSYLGEAEEVVQERIGDDELILIKGTKK-RSSASIILRGANDFMLDEMERSLHDALCVVkRTLESN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 416 RfLIAGGGAPEIELSRQLGAWAKVLHGMEGYCVKSFAEALEVIPYTLAENAGLNPIAIVTELRNKHAQGEINA------- 488
Cdd:cd03335 399 S-VVPGGGAVETALSIYLENFATTLGSREQLAIAEFAEALLVIPKTLAVNAAKDATELVAKLRAYHAAAQVKPdkkhlkw 477
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 15229595 489 -GINVRKGQITNILEENVVQPLLVSTSAITLATECVRMILKIDDIVTV 535
Cdd:cd03335 478 yGLDLINGKVRDNLEAGVLEPTVSKIKSLKFATEAAITILRIDDLIKL 525
|
|
| TCP1_beta |
cd03336 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ... |
25-534 |
1.07e-113 |
|
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: 347.01 E-value: 1.07e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 25 RREDIRFANINSARAVSDAVRTSLGPKGMDKMISTAN--GEVIITNDGATILNKMEVLQPAAKMLVELSKSQDSAAGDGT 102
Cdd:cd03336 10 KGETARLSSFVGAIAIGDLVKTTLGPKGMDKILQSVGrsGGVTVTNDGATILKSIGVDNPAAKVLVDISKVQDDEVGDGT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 103 TTVVVIAGALLKECQSLLTNGIHPTVISDSLHKACGKAIDILTAMAVPV---ELTDRDSLVKSASTSLNSKVVSQYSTLL 179
Cdd:cd03336 90 TSVTVLAAELLREAEKLVAQKIHPQTIIEGYRMATAAAREALLSSAVDHssdEEAFREDLLNIARTTLSSKILTQDKEHF 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 180 APLAVDAVLSVIDPekpeiVDLRDIKIVKKLGGTVDDTHTVKGLVFDKKVSraAGGPTRVENAKIAVIQFQISPPKTDIE 259
Cdd:cd03336 170 AELAVDAVLRLKGS-----GNLDAIQIIKKLGGSLKDSYLDEGFLLDKKIG--VNQPKRIENAKILIANTPMDTDKIKIF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 260 QS-IVVSDYTQMDRILKEERNYILGMIKKIKATGCNVLliqksILRDAVTDLSLHYLAKAKIMVIKDVERDEIEFVTKTL 338
Cdd:cd03336 243 GAkVRVDSTAKVAEIEEAEKEKMKNKVEKILKHGINCF-----INRQLIYNYPEQLFADAGIMAIEHADFDGVERLALVT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 339 NCLPIANIEHFRAEKLGHADLVEEASLGDGKILKITGIKdMGRTTSVLVRGSNQLVLDEAERSLHDALCVVRCLVSKRFL 418
Cdd:cd03336 318 GGEIASTFDHPELVKLGTCKLIEEIMIGEDKLIRFSGVA-AGEACTIVLRGASQQILDEAERSLHDALCVLAQTVKDTRV 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 419 IAGGGAPEIELSRQLGAWAKVLHGMEGYCVKSFAEALEVIPYTLAENAGLNPIAIVTELRNKHAQGEINAGINVRKGQIT 498
Cdd:cd03336 397 VLGGGCSEMLMAKAVEELAKKTPGKKSLAIEAFAKALRQLPTIIADNAGYDSAELVAQLRAAHYNGNTTAGLDMRKGTVG 476
|
490 500 510
....*....|....*....|....*....|....*.
gi 15229595 499 NILEENVVQPLLVSTSAITLATECVRMILKIDDIVT 534
Cdd:cd03336 477 DMKELGITESFKVKRQVLLSASEAAEMILRVDDIIK 512
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
25-533 |
1.47e-112 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 344.32 E-value: 1.47e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 25 RREDIRFANINSARAVSDAVRTSLGPKGMDKMISTAN-----GEVIITNDGATILNKMEVLQPAAKMLVELSKSQDSAAG 99
Cdd:PTZ00212 19 KGETARLQSFVGAIAVADLVKTTLGPKGMDKILQPMSegprsGNVTVTNDGATILKSVWLDNPAAKILVDISKTQDEEVG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 100 DGTTTVVVIAGALLKECQSLLTNGIHPTVISDSLHKACGKAIDILTAMAVPVELTD---RDSLVKSASTSLNSKVVSQYS 176
Cdd:PTZ00212 99 DGTTSVVVLAGELLREAEKLLDQKIHPQTIIEGWRMALDVARKALEEIAFDHGSDEekfKEDLLNIARTTLSSKLLTVEK 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 177 TLLAPLAVDAVLSVIDPekpeiVDLRDIKIVKKLGGTVDDTHTVKGLVFDKKVsrAAGGPTRVENAKIAVIQFQISPPKT 256
Cdd:PTZ00212 179 DHFAKLAVDAVLRLKGS-----GNLDYIQIIKKPGGTLRDSYLEDGFILEKKI--GVGQPKRLENCKILVANTPMDTDKI 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 257 DIEQSIV-VSDYTQMDRILKEERNYILGMIKKIKATGCNVLliqksILRDAVTDLSLHYLAKAKIMVIKDVERDEIEFVT 335
Cdd:PTZ00212 252 KIYGAKVkVDSMEKVAEIEAAEKEKMKNKVDKILAHGCNVF-----INRQLIYNYPEQLFAEAGIMAIEHADFDGMERLA 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 336 KTLNCLPIANIEHFRAEKLGHADLVEEASLGDGKILKITGIKDMGRTTSVLvRGSNQLVLDEAERSLHDALCVVRCLVSK 415
Cdd:PTZ00212 327 AALGAEIVSTFDTPEKVKLGHCDLIEEIMIGEDKLIRFSGCAKGEACTIVL-RGASTHILDEAERSLHDALCVLSQTVKD 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 416 RFLIAGGGAPEIELSRQLGAWAKVLHGMEGYCVKSFAEALEVIPYTLAENAGLNPIAIVTELRNKHAQGEINAGINVRKG 495
Cdd:PTZ00212 406 TRVVLGGGCSEMLMANAVEELAKKVEGKKSLAIEAFAKALRQIPTIIADNGGYDSAELVSKLRAEHYKGNKTAGIDMEKG 485
|
490 500 510
....*....|....*....|....*....|....*...
gi 15229595 496 QITNILEENVVQPLLVSTSAITLATECVRMILKIDDIV 533
Cdd:PTZ00212 486 TVGDMKELGITESYKVKLSQLCSATEAAEMILRVDDII 523
|
|
| chap_CCT_alpha |
TIGR02340 |
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ... |
27-535 |
9.68e-112 |
|
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: 342.47 E-value: 9.68e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 27 EDIRFANINSARAVSDAVRTSLGPKGMDKMISTANGEVIITNDGATILNKMEVLQPAAKMLVELSKSQDSAAGDGTTTVV 106
Cdd:TIGR02340 11 QDVRTQNVTAAMAIANIVKTSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDREVGDGTTSVV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 107 VIAGALLKECQSLLTNGIHPTVISDSLHKACGKAID-ILTAMAVPVELTDRDSLVKSASTSLNSKVVSQYSTLLAPLAVD 185
Cdd:TIGR02340 91 IIAAELLKRADELVKNKIHPTSVISGYRLACKEAVKyIKENLSVSVDELGREALINVAKTSMSSKIIGLDSDFFSNIVVD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 186 AVLSV--IDPEKPEIVDLRDIKIVKKLGGTVDDTHTVKGLVFDkkVSRAAGG-PTRVENAKIAVIQFQISPPKTDIEQSI 262
Cdd:TIGR02340 171 AVLAVktTNENGETKYPIKAINILKAHGKSARESMLVKGYALN--CTVASQQmPKRIKNAKIACLDFNLQKAKMALGVQI 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 263 VVSDYTQMDRILKEERNYILGMIKKIKATGCNVLLIQKSIlrdavTDLSLHYLAKAKIMVIKDVERDEIEFVTK----TL 338
Cdd:TIGR02340 249 VVDDPEKLEQIRQREADITKERIKKILDAGANVVLTTGGI-----DDMCLKYFVEAGAMGVRRCKKEDLKRIAKatgaTL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 339 nCLPIANI---EHFRAEKLGHADLVEEASLGDGKILKITGIKdmGRTT-SVLVRGSNQLVLDEAERSLHDALCVV-RCLV 413
Cdd:TIGR02340 324 -VSTLADLegeETFEASYLGFADEVVQERIADDECILIKGTK--KRKSaSIILRGANDFMLDEMERSLHDALCVVkRTLE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 414 SKRfLIAGGGAPEIELSRQLGAWAKVLHGMEGYCVKSFAEALEVIPYTLAENAGLNPIAIVTELRNKHAQGEINA----- 488
Cdd:TIGR02340 401 SNS-VVPGGGAVEAALSIYLENFATTLGSREQLAIAEFARALLIIPKTLAVNAAKDSTELVAKLRAYHAAAQLKPekkhl 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 15229595 489 ---GINVRKGQITNILEENVVQPLLVSTSAITLATECVRMILKIDDIVTV 535
Cdd:TIGR02340 480 kwyGLDLVNGKIRDNKEAGVLEPTVSKVKSLKFATEAAITILRIDDLIKL 529
|
|
| chap_CCT_theta |
TIGR02346 |
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ... |
27-533 |
1.11e-111 |
|
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: 342.08 E-value: 1.11e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 27 EDIRFANINSARAVSDAVRTSLGPKGMDKMISTANGEVIITNDGATILNKMEVLQPAAKMLVELSKSQDSAAGDGTTTVV 106
Cdd:TIGR02346 17 EEAVIKNIEACKELSQITRTSLGPNGMNKMVINHLEKLFVTNDAATILRELEVQHPAAKLLVMASEMQENEIGDGTNLVL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 107 VIAGALLKECQSLLTNGIHPTVISDSLHKACGKAIDILTAMAV--PVELTDRDSLVKSASTSLNSKVVSQYStLLAPLAV 184
Cdd:TIGR02346 97 VLAGELLNKAEELIRMGLHPSEIIKGYEMALKKAMEILEELVVweVKDLRDKDELIKALKASISSKQYGNED-FLAQLVA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 185 DAVLSVIdPEKPEIVDLRDIKIVKKLGGTVDDTHTVKGLVFDKKvsrAAGGPTRVENAKIAVIQFQISPPKTDIEQSIVV 264
Cdd:TIGR02346 176 QACSTVL-PKNPQNFNVDNIRVCKILGGSLSNSEVLKGMVFNRE---AEGSVKSVKNAKVAVFSCPLDTATTETKGTVLI 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 265 SDYTQMDRILKEERNYILGMIKKIKATGCNVLliqksILRDAVTDLSLHYLAKAKIMVIKDVERDEIEFVTKTLNCLPIA 344
Cdd:TIGR02346 252 HNAEELLNYSKGEENQIEAMIKAIADSGVNVI-----VTGGSVGDMALHYLNKYNIMVLKIPSKFELRRLCKTVGATPLP 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 345 NIEHFRAEKLGHADLVEEASLGDGKILKITGIKDMGRTTSVLVRGSNQLVLDEAERSLHDALCVVRCLVSKRFLIAGGGA 424
Cdd:TIGR02346 327 RLGAPTPEEIGYVDSVYVSEIGGDKVTVFKQENGDSKISTIILRGSTDNLLDDIERAIDDGVNTVKALVKDGRLLPGAGA 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 425 PEIELSRQLGAWAKVLHGMEGYCVKSFAEALEVIPYTLAENAGLNPIAIVTELRNKHAQGEINAGINVRKG--QITNILE 502
Cdd:TIGR02346 407 TEIELASRLTKYGEKLPGLDQYAIKKFAEAFEIIPRTLAENAGLNANEVIPKLYAAHKKGNKSKGIDIEAEsdGVKDASE 486
|
490 500 510
....*....|....*....|....*....|.
gi 15229595 503 ENVVQPLLVSTSAITLATECVRMILKIDDIV 533
Cdd:TIGR02346 487 AGIYDMLATKKWAIKLATEAAVTVLRVDQII 517
|
|
| TCP1_theta |
cd03341 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ... |
27-533 |
1.28e-111 |
|
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: 339.97 E-value: 1.28e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 27 EDIRFANINSARAVSDAVRTSLGPKGMDKMISTANGEVIITNDGATILNKMEVLQPAAKMLVELSKSQDSAAGDGTTTVV 106
Cdd:cd03341 7 EEAVLRNIEACKELSQITRTSYGPNGMNKMVINHLEKLFVTSDAATILRELEVQHPAAKLLVMASQMQEEEIGDGTNLVV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 107 VIAGALLKECQSLLTNGIHPTVISDSLHKACGKAIDILTAMAV-PVE-LTDRDSLVKSASTSLNSKVVSqYSTLLAPLAV 184
Cdd:cd03341 87 VLAGELLEKAEELLRMGLHPSEIIEGYEKALKKALEILEELVVyKIEdLRNKEEVSKALKTAIASKQYG-NEDFLSPLVA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 185 DAVLSVIdPEKPEIVDLRDIKIVKKLGGTVDDTHTVKGLVFDKKVSraaGGPTRVENAKIAViqfqisppktdieqsivv 264
Cdd:cd03341 166 EACISVL-PENIGNFNVDNIRVVKILGGSLEDSKVVRGMVFKREPE---GSVKRVKKAKVAV------------------ 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 265 sdytqmdrilkeernYILGMikkikATGCNVLLIQKSilrdaVTDLSLHYLAKAKIMVIKDVERDEIEFVTKTLNCLPIA 344
Cdd:cd03341 224 ---------------FSCPF-----DIGVNVIVAGGS-----VGDLALHYCNKYGIMVIKINSKFELRRLCRTVGATPLP 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 345 NIEHFRAEKLGHADLVEEASLGDGKILKITGIKDMGRTTSVLVRGSNQLVLDEAERSLHDALCVVRCLVSKRFLIAGGGA 424
Cdd:cd03341 279 RLGAPTPEEIGYCDSVYVEEIGDTKVVVFRQNKEDSKIATIVLRGATQNILDDVERAIDDGVNVFKSLTKDGRFVPGAGA 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 425 PEIELSRQLGAWAKVLHGMEGYCVKSFAEALEVIPYTLAENAGLNPIAIVTELRNKHAQGEINAGINVRKG--QITNILE 502
Cdd:cd03341 359 TEIELAKKLKEYGEKTPGLEQYAIKKFAEAFEVVPRTLAENAGLDATEVLSELYAAHQKGNKSAGVDIESGdeGTKDAKE 438
|
490 500 510
....*....|....*....|....*....|.
gi 15229595 503 ENVVQPLLVSTSAITLATECVRMILKIDDIV 533
Cdd:cd03341 439 AGIFDHLATKKWAIKLATEAAVTVLRVDQII 469
|
|
| GroEL |
COG0459 |
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ... |
26-534 |
6.79e-110 |
|
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227 Cd Length: 497 Bit Score: 336.28 E-value: 6.79e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 26 REDIRFANINSARAVSDAVRTSLGPKGMDKMISTANGEVIITNDGATILNKMEVLQP----AAKMLVELSKSQDSAAGDG 101
Cdd:COG0459 8 GEDARRANIRGVKALADAVKVTLGPKGRNVMLVKSFGDPTITNDGVTIAKEIELEDPfenmGAQLVKEVASKTNDEAGDG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 102 TTTVVVIAGALLKECQSLLTNGIHPTVISDSLHKACGKAIDILTAMAVPVEltDRDSLVKSASTSLNSKvvsqysTLLAP 181
Cdd:COG0459 88 TTTATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPVD--DKEELAQVATISANGD------EEIGE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 182 LAVDAVLSVIdpEKPEIvdlrdikIVKKLGGTVDDTHTVKGLVFDK------KVSRAAGGPTRVENAKIAVIQFQISPPK 255
Cdd:COG0459 160 LIAEAMEKVG--KDGVI-------TVEEGKGLETELEVVEGMQFDKgylspyFVTDPEKMPAELENAYILLTDKKISSIQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 256 TdieqsivvsdytqmdrilkeernyILGMIKKIKATGCNVLLIQKSIlrdavTDLSLHYLAKAKIMVIK----------- 324
Cdd:COG0459 231 D------------------------LLPLLEKVAQSGKPLLIIAEDI-----DGEALATLVVNGIRGVLrvvavkapgfg 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 325 DVERDEIE---------FVTKTLNclpiANIEHFRAEKLGHADLVEEaslGDGKILKITGIKDmGRTTSVLVRGSNQLVL 395
Cdd:COG0459 282 DRRKAMLEdiailtggrVISEDLG----LKLEDVTLDDLGRAKRVEV---DKDNTTIVEGAGN-PKAIVILVGAATEVEV 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 396 DEAERSLHDALCVVRCLVSKRFLiAGGGAPEIELSRQLGAWAKVLHGMEGYCVKSFAEALEVIPYTLAENAGLNPIAIVT 475
Cdd:COG0459 354 KERKRRVEDALHATRAAVEEGIV-PGGGAALLRAARALRELAAKLEGDEQLGIEIVARALEAPLRQIAENAGLDGSVVVE 432
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 15229595 476 ELRnkhAQGEINAGINVRKGQITNILEENVVQPLLVSTSAITLATECVRMILKIDDIVT 534
Cdd:COG0459 433 KVR---AAKDKGFGFDAATGEYVDMLEAGVIDPAKVKRSALQNAASVAGLILTTEAVIA 488
|
|
| chap_CCT_eta |
TIGR02345 |
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ... |
32-534 |
9.94e-109 |
|
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: 334.42 E-value: 9.94e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 32 ANINSARAVSDAVRTSLGPKGMDKMISTANGEVIITNDGATILNKMEVLQPAAKMLVELSKSQDSAAGDGTTTVVVIAGA 111
Cdd:TIGR02345 22 SNINACVAIAEALKTTLGPRGMDKLIVGSNGKATISNDGATILKLLDIVHPAAKTLVDIAKSQDAEVGDGTTSVTILAGE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 112 LLKECQSLLTNGIHPTVISDSLHKACGKAIDILTAMAVPVELTD---RDSLVKSASTSLNSKVVSQYSTLLAPLAVDAVL 188
Cdd:TIGR02345 102 LLKEAKPFIEEGVHPQLIIRCYREALSLAVEKIKEIAVTIDEEKgeqRELLEKCAATALSSKLISHNKEFFSKMIVDAVL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 189 SVIDpekpEIVDLRDIKIVKKLGGTVDDTHTVKGLVFDKKVSRAA--GGPTRVENAKIAVIQFQISPPKTDIEQSIVVSD 266
Cdd:TIGR02345 182 SLDR----DDLDLKLIGIKKVQGGALEDSQLVNGVAFKKTFSYAGfeQQPKKFANPKILLLNVELELKAEKDNAEIRVED 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 267 YTQMDRILKEERNYILGMIKKIKATGCNVLLIQKSIlrdavTDLSLHYLAKAKIMVIKDVERDEIEFVTKTLNCLPIANI 346
Cdd:TIGR02345 258 VEDYQAIVDAEWAIIFRKLEKIVESGANVVLSKLPI-----GDLATQYFADRDIFCAGRVSAEDLKRVIKACGGSIQSTT 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 347 EHFRAEKLGHADLVEEASLGDGKILKITGIKDmGRTTSVLVRGSNQLVLDEAERSLHDALCVVRCLVSKRFLIAGGGAPE 426
Cdd:TIGR02345 333 SDLEADVLGTCALFEERQIGSERYNYFTGCPH-AKTCTIILRGGAEQFIEEAERSLHDAIMIVRRALKNKKIVAGGGAIE 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 427 IELSRQLGAWAKVLHGMEGYCVKSFAEALEVIPYTLAENAGLNPIAIVTELRNKHAQGEINAGINVRKGQITNILEENVV 506
Cdd:TIGR02345 412 MELSKCLRDYSKTIDGKQQLIINAFAKALEIIPRQLCENAGFDSIEILNKLRSRHAKGGKWYGVDINTEDIGDNFEAFVW 491
|
490 500
....*....|....*....|....*...
gi 15229595 507 QPLLVSTSAITLATECVRMILKIDDIVT 534
Cdd:TIGR02345 492 EPALVKINALKAAFEAACTILSVDETIT 519
|
|
| chap_CCT_gamma |
TIGR02344 |
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ... |
22-534 |
3.57e-101 |
|
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: 314.75 E-value: 3.57e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 22 DNKRREDIR---FANINSARAVSDAVRTSLGPKGMDKMISTANGEVIITNDGATILNKMEVLQPAAKMLVELSKSQDSAA 98
Cdd:TIGR02344 7 QNTKRESGRkaqLSNIQAAKAVADIIRTCLGPRSMLKMLLDPMGGIVMTNDGNAILREIDVAHPAAKSMIELSRTQDEEV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 99 GDGTTTVVVIAGALLKECQSLLTNGIHPTVISDSLHKACGKAIDILTAMAVPVELTDRDSLVKSASTSLNSKVVSQYSTL 178
Cdd:TIGR02344 87 GDGTTSVIILAGEMLSVAEPFLEQNIHPTVIIRAYRKALDDALSVLEEISIPVDVNDDAAMLKLIQSCIGTKFVSRWSDL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 179 LAPLAVDAVLSVIDPEKP--EIVDLRDIKIVKKLGGTVDDTHTVKGLVFDK-----KVSRaaggptRVENAKIAVIQFQI 251
Cdd:TIGR02344 167 MCDLALDAVRTVQRDENGrkEIDIKRYAKVEKIPGGDIEDSCVLKGVMINKdvthpKMRR------YIENPRIVLLDCPL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 252 SPPKTDIEQSIVVSDYTQMDRILKEERNYILGMIKKIKATGCNVLLIQKsilrdAVTDLSLHYLAKAKIMVIKDVERDEI 331
Cdd:TIGR02344 241 EYKKGESQTNIEITKEEDWNRILQMEEEYVQLMCEDIIAVKPDLVITEK-----GVSDLAQHYLLKANITAIRRVRKTDN 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 332 EFVTKTLNCLPIANIEHFRAEKLG-HADLVEEASLGDGKILKITGIKDmGRTTSVLVRGSNQLVLDEAERSLHDALCVVR 410
Cdd:TIGR02344 316 NRIARACGATIVNRPEELRESDVGtGCGLFEVKKIGDEYFTFITECKD-PKACTILLRGASKDILNEVERNLQDAMAVAR 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 411 CLVSKRFLIAGGGAPEIELSRQLGAWAKVLHGMEGYCVKSFAEALEVIPYTLAENAGLNPIAIVTELRNKHAQGEI-NAG 489
Cdd:TIGR02344 395 NVLLDPKLVPGGGATEMAVSVALTEKSKKLEGVEQWPYRAVADALEIIPRTLAQNCGANVIRTLTELRAKHAQENNcTWG 474
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 15229595 490 INVRKGQITNILEENVVQPLLVSTSAITLATECVRMILKIDDIVT 534
Cdd:TIGR02344 475 IDGETGKIVDMKEKGIWEPLAVKLQTYKTAIESACLLLRIDDIVS 519
|
|
| TCP1_gamma |
cd03337 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ... |
22-533 |
1.57e-97 |
|
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: 303.83 E-value: 1.57e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 22 DNKRRED---IRFANINSARAVSDAVRTSLGPKGMDKMISTANGEVIITNDGATILNKMEVLQPAAKMLVELSKSQDSAA 98
Cdd:cd03337 7 QNTKRESgrkAQLGNIQAAKTVADVIRTCLGPRAMLKMLLDPMGGIVLTNDGNAILREIDVAHPAAKSMIELSRTQDEEV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 99 GDGTTTVVVIAGALLKECQSLLTNGIHPTVISDSLHKACGKAIDILTAMAVPVELTDRDSLVKSASTSLNSKVVSQYSTL 178
Cdd:cd03337 87 GDGTTSVIILAGEILAVAEPFLERGIHPTVIIKAYRKALEDALKILEEISIPVDVNDRAQMLKIIKSCIGTKFVSRWSDL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 179 LAPLAVDAVLSVIDPE--KPEIVDL-RDIKIVKKLGGTVDDTHTVKGLVFDKKVsraaggptrvenakiaviqfqISPpk 255
Cdd:cd03337 167 MCNLALDAVKTVAVEEngRKKEIDIkRYAKVEKIPGGEIEDSRVLDGVMLNKDV---------------------THP-- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 256 tdieqsivvsdytQMDRILKEERNYILgmikkikatGCNVLLIqkSILRDAVTDLSLHYLAKAKIMVIKDVERDEIEFVT 335
Cdd:cd03337 224 -------------KMRRRIENPRIVLL---------DCPLEYL--VITEKGVSDLAQHYLVKAGITALRRVRKTDNNRIA 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 336 KTLNCLPIANIEHFRAEKLGH-ADLVEEASLGDGKILKITGIKDmGRTTSVLVRGSNQLVLDEAERSLHDALCVVRCLVS 414
Cdd:cd03337 280 RACGATIVNRPEELTESDVGTgAGLFEVKKIGDEYFTFITECKD-PKACTILLRGASKDVLNEVERNLQDAMAVARNIIL 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 415 KRFLIAGGGAPEIELSRQLGAWAKVLHGMEGYCVKSFAEALEVIPYTLAENAGLNPIAIVTELRNKHAQGEINA-GINVR 493
Cdd:cd03337 359 NPKLVPGGGATEMAVSHALSEKAKSIEGVEQWPYKAVASALEVIPRTLAQNCGANVIRTLTELRAKHAQGENSTwGIDGE 438
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 15229595 494 KGQITNILEENVVQPLLVSTSAITLATECVRMILKIDDIV 533
Cdd:cd03337 439 TGDIVDMKELGIWDPLAVKAQTYKTAIEAACMLLRIDDIV 478
|
|
| chap_CCT_beta |
TIGR02341 |
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ... |
21-536 |
1.86e-93 |
|
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT beta chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.
Pssm-ID: 274082 Cd Length: 519 Bit Score: 294.84 E-value: 1.86e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 21 VDNKRREDIRFANINSARAVSDAVRTSLGPKGMDKMISTAN--GEVIITNDGATILNKMEVLQPAAKMLVELSKSQDSAA 98
Cdd:TIGR02341 7 ADEERAENARLSSFVGAIAIGDLVKSTLGPKGMDKILQSSSsdASIMVTNDGATILKSIGVDNPAAKVLVDMSKVQDDEV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 99 GDGTTTVVVIAGALLKECQSLLTNGIHPTVISDSLHKACGKAIDILTAMAVPV---ELTDRDSLVKSASTSLNSKVVSQY 175
Cdd:TIGR02341 87 GDGTTSVTVLAAELLREAEKLINQKIHPQTIIAGYREATKAARDALLKSAVDNgsdEVKFRQDLMNIARTTLSSKILSQH 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 176 STLLAPLAVDAVLSVIDPekpeiVDLRDIKIVKKLGGTVDDTHTVKGLVFDKKVsrAAGGPTRVENAKIAVIQFQISPPK 255
Cdd:TIGR02341 167 KDHFAQLAVDAVLRLKGS-----GNLEAIQIIKKLGGSLADSYLDEGFLLDKKI--GVNQPKRIENAKILIANTGMDTDK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 256 TDIEQSIVVSDYT-QMDRILKEERNYILGMIKKIKATGCNVLliqksILRDAVTDLSLHYLAKAKIMVIKDVERDEIEFV 334
Cdd:TIGR02341 240 VKIFGSRVRVDSTaKVAELEHAEKEKMKEKVEKILKHGINCF-----INRQLIYNYPEQLFADAGVMAIEHADFEGVERL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 335 TKTLNCLPIANIEHFRAEKLGHADLVEEASLGDGKILKITGIKdMGRTTSVLVRGSNQLVLDEAERSLHDALCVVRCLVS 414
Cdd:TIGR02341 315 ALVTGGEIVSTFDHPELVKLGSCDLIEEIMIGEDKLLKFSGVK-LGEACTIVLRGATQQILDEAERSLHDALCVLSQTVK 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 415 KRFLIAGGGAPEIELSRQLGAWAKVLHGMEGYCVKSFAEALEVIPYTLAENAGLNPIAIVTELRNKHAQGEINAGINVRK 494
Cdd:TIGR02341 394 ESRTVLGGGCSEMLMSKAVTQEAQRTPGKEALAVEAFARALRQLPTIIADNAGFDSAELVAQLRAAHYNGNTTMGLDMNE 473
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 15229595 495 GQITNILEENVVQPLLVSTSAITLATECVRMILKIDDIVTVR 536
Cdd:TIGR02341 474 GTIADMRQLGITESYKVKRAVVSSAAEAAEVILRVDNIIKAA 515
|
|
| TCP1_zeta |
cd03342 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
23-533 |
3.21e-81 |
|
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: 261.81 E-value: 3.21e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 23 NKRREDIRFA-----NINSARAVSDAVRTSLGPKGMDKMISTANGEVIITNDGATILNKMEVLQPAAKMLVELSKSQDSA 97
Cdd:cd03342 2 NPKAEVLRRGqalavNISAAKGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLSEMQIQHPTASMIARAATAQDDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 98 AGDGTTTVVVIAGALLKECQSLLTNGIHPTVISDSLHKACGKAIDILTAMAVPVE-LTDRDSLVKSASTSLNSKVVSQYS 176
Cdd:cd03342 82 TGDGTTSNVLLIGELLKQAERYIQEGVHPRIITEGFELAKNKALKFLESFKVPVEiDTDRELLLSVARTSLRTKLHADLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 177 TLLAPLAVDAVLSVIDPEKPeiVDLRDIKIVKKLGGTVDDTHTVKGLVFDKKvSRAAGGPTRVENAKIAVIQFQISPPKT 256
Cdd:cd03342 162 DQLTEIVVDAVLAIYKPDEP--IDLHMVEIMQMQHKSDSDTKLIRGLVLDHG-ARHPDMPKRVENAYILTCNVSLEYEKT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 257 DIEQSIVVSdytqmdrilkeernyilgmikkikatgcnVLLIQKSIlrdavtD-LSLHYLAKAKIMVIKDVERDEIEFVT 335
Cdd:cd03342 239 EVNSGFFYS-----------------------------VVINQKGI------DpPSLDMLAKEGILALRRAKRRNMERLT 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 336 KTLNCLPIANIEHFRAEKLGHADLVEEASLGDGKILKITGIKDmGRTTSVLVRGSNQLVLDEAERSLHDALCVVRCLVSK 415
Cdd:cd03342 284 LACGGVAMNSVDDLSPECLGYAGLVYERTLGEEKYTFIEGVKN-PKSCTILIKGPNDHTITQIKDAIRDGLRAVKNAIED 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 416 RFLIAGGGAPEIELSRQLGAWAKVLHGMEGYCVKSFAEALEVIPYTLAENAGLNPIAIVTELRNKHAQGEINAGINVRKG 495
Cdd:cd03342 363 KCVVPGAGAFEVALYAHLKEFKKSVKGKAKLGVQAFADALLVIPKTLAENSGLDVQETLVKLQDEYAEGGQVGGVDLDTG 442
|
490 500 510
....*....|....*....|....*....|....*...
gi 15229595 496 QITNILEENVVQPLLVSTSAITLATECVRMILKIDDIV 533
Cdd:cd03342 443 EPMDPESEGIWDNYSVKRQILHSATVIASQLLLVDEII 480
|
|
| chap_CCT_zeta |
TIGR02347 |
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ... |
15-533 |
2.37e-76 |
|
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: 250.42 E-value: 2.37e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 15 SKAESFvdnkRREDIRFANINSARAVSDAVRTSLGPKGMDKMISTANGEVIITNDGATILNKMEVLQPAAKMLVELSKSQ 94
Cdd:TIGR02347 7 PKAESL----RRDAALMMNINAARGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEMQIQHPTASMIARAATAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 95 DSAAGDGTTTVVVIAGALLKECQSLLTNGIHPTVISDSLHKACGKAIDILTAMAVPVELT-DRDSLVKSASTSLNSKVVS 173
Cdd:TIGR02347 83 DDITGDGTTSTVLLIGELLKQAERYILEGVHPRIITEGFEIARKEALQFLDKFKVKKEDEvDREFLLNVARTSLRTKLPA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 174 QYSTLLAPLAVDAVLSVIDPEKPeiVDLRDIKIVKKLGGTVDDTHTVKGLVFDKKvSRAAGGPTRVENAKIAVIQFQISP 253
Cdd:TIGR02347 163 DLADQLTEIVVDAVLAIKKDGED--IDLFMVEIMEMKHKSATDTTLIRGLVLDHG-ARHPDMPRRVKNAYILTCNVSLEY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 254 PKTDIEQSIVVSDYTQMDRILKEERNYILGMIKKI---------KATGCNVLLI-QKSIlrdavTDLSLHYLAKAKIMVI 323
Cdd:TIGR02347 240 EKTEVNSGFFYSSAEQREKLVKAERKFVDDRVKKIielkkkvcgKSPDKGFVVInQKGI-----DPPSLDLLAKEGIMAL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 324 KDVERDEIEFVTKTLNCLPIANIEHFRAEKLGHADLVEEASLGDGKILKITGIKDmGRTTSVLVRGSNQLVLDEAERSLH 403
Cdd:TIGR02347 315 RRAKRRNMERLTLACGGEALNSVEDLTPECLGWAGLVYETTIGEEKYTFIEECKN-PKSCTILIKGPNDHTIAQIKDAVR 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 404 DALCVVRCLVSKRFLIAGGGAPEIELSRQLGAWAKVLHGMEGYCVKSFAEALEVIPYTLAENAGLNPIAIVTELRNKHAQ 483
Cdd:TIGR02347 394 DGLRAVKNAIEDKCVVPGAGAFEIAAYRHLKEYKKSVKGKAKLGVEAFANALLVIPKTLAENSGFDAQDTLVKLEDEHDE 473
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 15229595 484 GEINAGINVRKGQITNILEENVVQPLLVSTSAITLATECVRMILKIDDIV 533
Cdd:TIGR02347 474 GGEVVGVDLNTGEPIDPEIKGIWDNYRVKKQLIQSATVIASQLLLVDEVM 523
|
|
| chaperonin_like |
cd03333 |
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ... |
156-413 |
3.46e-61 |
|
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: 200.39 E-value: 3.46e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 156 RDSLVKSASTSLNSKVvSQYSTLLAPLAVDAVLSVIDPEkpEIVDLRDIKIVKKLGGTVDDTHTVKGLVFDKKVSRAaGG 235
Cdd:cd03333 1 RELLLQVATTSLNSKL-SSWDDFLGKLVVDAVLKVGPDN--RMDDLGVIKVEKIPGGSLEDSELVVGVVFDKGYASP-YM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 236 PTRVENAKIAVIQFQISPpktdieqsivvsdytqmdrilkeernyilgmikkikatgcnVLLIQKSIlrdavTDLSLHYL 315
Cdd:cd03333 77 PKRLENAKILLLDCPLEY-----------------------------------------VVIAEKGI-----DDLALHYL 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 316 AKAKIMVIKDVERDEIEFVTKTLNCLPIANIEHFRAEKLGHADLVEEASLGDGKILKITGIKDmGRTTSVLVRGSNQLVL 395
Cdd:cd03333 111 AKAGIMAVRRVKKEDLERIARATGATIVSSLEDLTPEDLGTAELVEETKIGEEKLTFIEGCKG-GKAATILLRGATEVEL 189
|
250
....*....|....*...
gi 15229595 396 DEAERSLHDALCVVRCLV 413
Cdd:cd03333 190 DEVKRSLHDALCAVRAAV 207
|
|
| groEL |
PRK12849 |
chaperonin GroEL; Reviewed |
38-527 |
1.21e-15 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237230 Cd Length: 542 Bit Score: 79.47 E-value: 1.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 38 RAVSDAVRTSLGPKGMDKMISTANGEVIITNDGATILNKMEVLQP----AAKMLVELSKSQDSAAGDGTTTVVVIAGALL 113
Cdd:PRK12849 20 NKLADAVKVTLGPKGRNVVIDKSFGAPTITKDGVSIAKEIELEDPfenlGAQLVKEVASKTNDVAGDGTTTATVLAQALV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 114 KECQSLLTNGIHPTVISDSLHKACGKAIDILTAMAVPVEltDRDSLVKSASTSLNSkvvsqystllaplavDAVLSVIDP 193
Cdd:PRK12849 100 QEGLKNVAAGANPMDLKRGIDKAVEAVVEELKALARPVS--GSEEIAQVATISANG---------------DEEIGELIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 194 EKPEIVDLRDIKIVKKLGGTVDDTHTVKGLVFDKK------VSRAAGGPTRVENAKIAVIQFQISppktDIEQSIVVSDY 267
Cdd:PRK12849 163 EAMEKVGKDGVITVEESKTLETELEVTEGMQFDRGylspyfVTDPERMEAVLEDPLILLTDKKIS----SLQDLLPLLEK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 268 T-QMDR---ILKEE----------RNYILGMIK--KIKA-----------------TGCNVLLIQKSILRDAVTdlsLHY 314
Cdd:PRK12849 239 VaQSGKpllIIAEDvegealatlvVNKLRGGLKvaAVKApgfgdrrkamlediailTGGTVISEDLGLKLEEVT---LDD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 315 LAKA-KIMVIKDV--------ERDEIEfvtktlnclpiANIEHFRAEkLGHAD-------LVEeaslgdgKILKITG--- 375
Cdd:PRK12849 316 LGRAkRVTITKDNttivdgagDKEAIE-----------ARVAQIRRQ-IEETTsdydrekLQE-------RLAKLAGgva 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 376 -IKdMGRTTSVLVRGSNQLVldeaerslHDALCVVRCLVsKRFLIAGGGAPEIELSRQLGAwAKVLHGMEGYCVKSFAEA 454
Cdd:PRK12849 377 vIK-VGAATEVELKERKDRV--------EDALNATRAAV-EEGIVPGGGVALLRAAKALDE-LAGLNGDQAAGVEIVRRA 445
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15229595 455 LEVIPYTLAENAGLNPIAIVtelrNKHAQGEINAGINVRKGQITNILEENVVQPLLVSTSAITLATECVRMIL 527
Cdd:PRK12849 446 LEAPLRQIAENAGLDGSVVV----AKVLELEDGFGFNAATGEYGDLIAAGIIDPVKVTRSALQNAASVAGLLL 514
|
|
| groEL |
CHL00093 |
chaperonin GroEL |
42-533 |
1.52e-15 |
|
chaperonin GroEL
Pssm-ID: 177025 Cd Length: 529 Bit Score: 79.38 E-value: 1.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 42 DAVRTSLGPKGMDKMISTANGEVIITNDGATILNKMEVLQPAAKMLVEL-----SKSQDsAAGDGTTTVVVIAGALLKEC 116
Cdd:CHL00093 24 EAVSVTLGPKGRNVVLEKKYGSPQIVNDGVTIAKEIELEDHIENTGVALirqaaSKTND-VAGDGTTTATVLAYAIVKQG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 117 QSLLTNGIHPTVISDSLHKACGKAIDILTAMAVPVEltDRDSLVKSASTSL-NSKVVSQystllapLAVDAVLSVidpEK 195
Cdd:CHL00093 103 MKNVAAGANPISLKRGIEKATQYVVSQIAEYARPVE--DIQAITQVASISAgNDEEVGS-------MIADAIEKV---GR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 196 PEIVDLRDIKivkklgGTVDDTHTVKGLVFDKK------VSRAAGGPTRVENA-------KIAVIQFQISPPKTDIEQS- 261
Cdd:CHL00093 171 EGVISLEEGK------STVTELEITEGMRFEKGfispyfVTDTERMEVVQENPyilltdkKITLVQQDLLPILEQVTKTk 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 262 ----IVVSDytqmdrILKEER-----NYILGMIK--KIKATGCNVLliQKSILRD----------------AVTDLSLHY 314
Cdd:CHL00093 245 rpllIIAED------VEKEALatlvlNKLRGIVNvvAVRAPGFGDR--RKAMLEDiailtggqvitedaglSLETIQLDL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 315 LAKAKIMVIKdveRDEIEFVTKTLNCLPIANIEHFRAEKLGHADLVEEASLGDgKILKITG----IKdmgrttsvlVRGS 390
Cdd:CHL00093 317 LGQARRIIVT---KDSTTIIADGNEEQVKARCEQLRKQIEIADSSYEKEKLQE-RLAKLSGgvavIK---------VGAA 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 391 NQLVLDEAERSLHDALCVVRCLVSKRfLIAGGGAPEIELSRQLGAWAKV-LHGME---GYCV-KSFAEALEVIpytlAEN 465
Cdd:CHL00093 384 TETEMKDKKLRLEDAINATKAAVEEG-IVPGGGATLVHLSENLKTWAKNnLKEDEligALIVaRAILAPLKRI----AEN 458
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15229595 466 AGLNPIAIVTELRNKhaqgEINAGINVRKGQITNILEENVVQPLLVSTSAITLATECVRMILKIDDIV 533
Cdd:CHL00093 459 AGKNGSVIIEKVQEQ----DFEIGYNAANNKFVNMYEAGIIDPAKVTRSALQNAASIASMILTTECII 522
|
|
| PTZ00114 |
PTZ00114 |
Heat shock protein 60; Provisional |
28-527 |
2.67e-15 |
|
Heat shock protein 60; Provisional
Pssm-ID: 185455 Cd Length: 555 Bit Score: 78.80 E-value: 2.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 28 DIRFAN------INSARAVSDAVRTSLGPKGMDKMISTANGEVIITNDGATIL------NKMEVLqpAAKMLVELSKSQD 95
Cdd:PTZ00114 16 EIRFGDearqslLKGIERLADAVAVTLGPKGRNVIIEQEYGSPKITKDGVTVAkaiefsDRFENV--GAQLIRQVASKTN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 96 SAAGDGTTTVVVIAGALLKE-CQSLLTnGIHPTVISDSLHKACGKAIDILTAMAVPVELTDRDSLVKSASTSLNSKVVSQ 174
Cdd:PTZ00114 94 DKAGDGTTTATILARAIFREgCKAVAA-GLNPMDLKRGIDLAVKVVLESLKEQSRPVKTKEDILNVATISANGDVEIGSL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 175 YSTLLAPLAVDAVLSVIDpekpeivdlrdikivkklGGTVDDT-HTVKGLVFDkkvsRAAGGPTRVENAKIAVIQFQiSP 253
Cdd:PTZ00114 173 IADAMDKVGKDGTITVED------------------GKTLEDElEVVEGMSFD----RGYISPYFVTNEKTQKVELE-NP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 254 pktdieqSIVVSDY--TQMDRILKeernyILGMIKKIKAtgcNVLLIQKSILRDAVTDLSLHYL-AKAKIMVIK-----D 325
Cdd:PTZ00114 230 -------LILVTDKkiSSIQSILP-----ILEHAVKNKR---PLLIIAEDVEGEALQTLIINKLrGGLKVCAVKapgfgD 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 326 VERDEIEFVTKTLNCLPIAN------IEHFRAEKLGHADLVE----EASLGDGKILK------ITGIKD-MGRTTS---- 384
Cdd:PTZ00114 295 NRKDILQDIAVLTGATVVSEdnvglkLDDFDPSMLGSAKKVTvtkdETVILTGGGDKaeikerVELLRSqIERTTSeydk 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 385 ----------------VLVRGSNQLVLDEAERSLHDALCVVRCLVSKRFLiAGGGAPEIELSRQLGAWA--KVLHGMEGY 446
Cdd:PTZ00114 375 eklkerlaklsggvavIKVGGASEVEVNEKKDRIEDALNATRAAVEEGIV-PGGGVALLRASKLLDKLEedNELTPDQRT 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 447 CVKSFAEALEVIPYTLAENAGLNPIAIVTELRNKhaqGEINAGINVRKGQITNILEENVVQPLLVSTSAITLATECVRMI 526
Cdd:PTZ00114 454 GVKIVRNALRLPTKQIAENAGVEGAVVVEKILEK---KDPSFGYDAQTGEYVNMFEAGIIDPTKVVRSALVDAASVASLM 530
|
.
gi 15229595 527 L 527
Cdd:PTZ00114 531 L 531
|
|
| Fab1_TCP |
cd03334 |
TCP-1 like domain of the eukaryotic phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinase Fab1. ... |
174-409 |
4.62e-15 |
|
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: 75.34 E-value: 4.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 174 QYSTLLAPLAVDAVLSV-IDPEKPEIVDLRD-IKIVKKLGGTVDDTHTVKGLVFDKKV-SRAAggPTRVENAKIAVIQFq 250
Cdd:cd03334 18 SWLDILLPLVWKAASNVkPDVRAGDDMDIRQyVKIKKIPGGSPSDSEVVDGVVFTKNVaHKRM--PSKIKNPRILLLQG- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 251 isppktDIEQSIVVSDYTQMDRILKEERNYILGMIKKIKATGCNVLLIQKSILRDAvtdlsLHYLAKAKIMVIKDVERDE 330
Cdd:cd03334 95 ------PLEYQRVENKLLSLDPVILQEKEYLKNLVSRIVALRPDVILVEKSVSRIA-----QDLLLEAGITLVLNVKPSV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 331 IEFVTKTLNCLPIANIEHFRAE-KLGHADLVEeaslgdgkILKITGIKDMGRT------------TSVLVRGSNQLVLDE 397
Cdd:cd03334 164 LERISRCTGADIISSMDDLLTSpKLGTCESFR--------VRTYVEEHGRSKTlmffegcpkelgCTILLRGGDLEELKK 235
|
250
....*....|..
gi 15229595 398 AERSLHDALCVV 409
Cdd:cd03334 236 VKRVVEFMVFAA 247
|
|
| GroEL |
TIGR02348 |
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ... |
39-169 |
1.70e-14 |
|
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: 76.18 E-value: 1.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 39 AVSDAVRTSLGPKGMDKMISTANGEVIITNDGATILNKMEVLQP----AAKMLVELSKSQDSAAGDGTTTVVVIAGALLK 114
Cdd:TIGR02348 20 KLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDKfenmGAQLVKEVASKTNDVAGDGTTTATVLAQAIVK 99
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 15229595 115 ECQSLLTNGIHPTVISDSLHKACGKAIDILTAMAVPVEltDRDSLVKSASTSLNS 169
Cdd:TIGR02348 100 EGLKNVAAGANPIELKRGIEKAVEAVVEELKKLSKPVK--GKKEIAQVATISANN 152
|
|
| GroEL |
cd03344 |
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ... |
26-523 |
1.88e-14 |
|
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: 75.96 E-value: 1.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 26 REDIRFANINSARAVSDAVRTSLGPKGMDKMISTANGEVIITNDGATILNKMEVLQP----AAKMLVELSKSQDSAAGDG 101
Cdd:cd03344 6 GEEARKALLRGVNKLADAVKVTLGPKGRNVVIEKSFGSPKITKDGVTVAKEIELEDPfenmGAQLVKEVASKTNDVAGDG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 102 TTTVVVIAGALLKECQSLLTNGIHPTVISDSLHKACGKAIDILTAMAVPVelTDRDSLVKSASTSLNSkvvsqystllap 181
Cdd:cd03344 86 TTTATVLARAIIKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKPV--KTKEEIAQVATISANG------------ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 182 lavdavlsviDPEKPEIVdlrdIKIVKKLGG----TVDDTHT-------VKGLVFDKK------VSRAAGGPTRVENAKI 244
Cdd:cd03344 152 ----------DEEIGELI----AEAMEKVGKdgviTVEEGKTletelevVEGMQFDRGylspyfVTDPEKMEVELENPYI 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 245 AVIQFQISppktDIEQsivvsdytqmdrilkeernyILGMIKKIKATGCNVLLIQKSILRDAVTDLSLHYL-AKAKIMVI 323
Cdd:cd03344 218 LLTDKKIS----SIQE--------------------LLPILELVAKAGRPLLIIAEDVEGEALATLVVNKLrGGLKVCAV 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 324 K-----DVERDEIE---------FVTKTLNclpiANIEHFRAEKLGHADLV----EEASLGDGKILK------ITGIKD- 378
Cdd:cd03344 274 KapgfgDRRKAMLEdiailtggtVISEELG----LKLEDVTLEDLGRAKKVvvtkDDTTIIGGAGDKaaikarIAQIRKq 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 379 MGRTTS--------------------VLVRGSNQLVLDEAERSLHDALCVVRCLVSKRfLIAGGGAPEIELSRQLGAWaK 438
Cdd:cd03344 350 IEETTSdydkeklqerlaklsggvavIKVGGATEVELKEKKDRVEDALNATRAAVEEG-IVPGGGVALLRASPALDKL-K 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 439 VLHGMEGYCVKSFAEALEVIPYTLAENAGLNPIAIVTELRNkhaqGEINAGINVRKGQITNILEENVVQPLLVSTSAIT- 517
Cdd:cd03344 428 ALNGDEKLGIEIVRRALEAPLRQIAENAGVDGSVVVEKVLE----SPDGFGYDAATGEYVDMIEAGIIDPTKVVRSALQn 503
|
570
....*....|....
gi 15229595 518 --------LATECV 523
Cdd:cd03344 504 aasvasllLTTEAL 517
|
|
| groEL |
PRK12851 |
chaperonin GroEL; Reviewed |
20-168 |
6.12e-14 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 171770 Cd Length: 541 Bit Score: 74.39 E-value: 6.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 20 FVDNKRREDIRFANInsaraVSDAVRTSLGPKGMDKMISTANGEVIITNDGATILNKMEVLQP----AAKMLVELSKSQD 95
Cdd:PRK12851 8 FHVEAREKMLRGVNI-----LADAVKVTLGPKGRNVVIDKSFGAPTITNDGVTIAKEIELEDKfenmGAQMVREVASKTN 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15229595 96 SAAGDGTTTVVVIAGALLKECQSLLTNGIHPTVISDSLHKACGKAIDILTAMAVPVEltDRDSLVKSASTSLN 168
Cdd:PRK12851 83 DVAGDGTTTATVLAQAIVREGAKAVAAGANPMDLKRGIDRAVAAVVEELKANARPVT--TNAEIAQVATISAN 153
|
|
| groEL |
PRK12850 |
chaperonin GroEL; Reviewed |
28-168 |
1.09e-13 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237231 Cd Length: 544 Bit Score: 73.60 E-value: 1.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 28 DIRFANINSAR------AVSDAVRTSLGPKGMDKMISTANGEVIITNDGATILNKMEVLQP----AAKMLVELSKSQDSA 97
Cdd:PRK12850 5 EIRFSTDARDRllrgvnILANAVKVTLGPKGRNVVLEKSFGAPRITKDGVTVAKEIELEDKfenmGAQMVKEVASKTNDL 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15229595 98 AGDGTTTVVVIAGALLKECQSLLTNGIHPTVISDSLHKACGKAIDILTAMAVPVelTDRDSLVKSASTSLN 168
Cdd:PRK12850 85 AGDGTTTATVLAQAIVREGAKLVAAGMNPMDLKRGIDLAVAAVVDELKKIAKKV--TSSKEIAQVATISAN 153
|
|
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
39-169 |
3.85e-12 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 68.61 E-value: 3.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 39 AVSDAVRTSLGPKGMDKMISTANGEVIITNDGATILNKMEVLQPAAKMLVEL-----SKSQDsAAGDGTTTVVVIAGALL 113
Cdd:PRK00013 21 KLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDPFENMGAQLvkevaSKTND-VAGDGTTTATVLAQAIV 99
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 15229595 114 KECQSLLTNGIHPTVISDSLHKACGKAIDILTAMAVPVEltDRDSLVKSASTSLNS 169
Cdd:PRK00013 100 REGLKNVAAGANPMDLKRGIDKAVEAAVEELKKISKPVE--DKEEIAQVATISANG 153
|
|
| groEL |
PRK12852 |
chaperonin GroEL; Reviewed |
15-151 |
8.72e-11 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237232 Cd Length: 545 Bit Score: 64.48 E-value: 8.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 15 SKAESFVDNKRREDIRFANInsaraVSDAVRTSLGPKGMDKMISTANGEVIITNDGATILNKMEVLQP----AAKMLVEL 90
Cdd:PRK12852 3 AKDVKFSGDARDRMLRGVDI-----LANAVKVTLGPKGRNVVIEKSFGAPRITKDGVTVAKEIELEDKfenmGAQMVREV 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15229595 91 SKSQDSAAGDGTTTVVVIAGALLKECQSLLTNGIHPTVISDSLHKACGKAIDILTAMAVPV 151
Cdd:PRK12852 78 ASKTNDLAGDGTTTATVLAQAIVREGAKAVAAGMNPMDLKRGIDIAVAAVVKDIEKRAKPV 138
|
|
| PRK14104 |
PRK14104 |
chaperonin GroEL; Provisional |
40-533 |
1.49e-09 |
|
chaperonin GroEL; Provisional
Pssm-ID: 172594 Cd Length: 546 Bit Score: 60.43 E-value: 1.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 40 VSDAVRTSLGPKGMDKMISTANGEVIITNDGATILNKMEVLQP----AAKMLVELSKSQDSAAGDGTTTVVVIAGALLKE 115
Cdd:PRK14104 23 LANAVKVTLGPKGRNVVLDKSFGAPRITKDGVTVAKEIELEDKfenmGAQMVREVASKSADAAGDGTTTATVLAQAIVRE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 116 CQSLLTNGIHPTVISDSLHKACGKAIDILTAMAVPVELTDRDSLVKSASTSLNSKVVSQYSTLLAPLAVDAVLSVIDPEK 195
Cdd:PRK14104 103 GAKSVAAGMNPMDLKRGIDLAVEAVVADLVKNSKKVTSNDEIAQVGTISANGDAEIGKFLADAMKKVGNEGVITVEEAKS 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 196 PEIvdlrdikivkklggtvdDTHTVKGLVFDKK------VSRAAGGPTRVENAKIAVIQFQIS------PPKTDIEQS-- 261
Cdd:PRK14104 183 LET-----------------ELDVVEGMQFDRGyispyfVTNADKMRVEMDDAYILINEKKLSslnellPLLEAVVQTgk 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 262 --IVVSDYTQMDRILKEERNYILGMIK--KIKATG-----------CNVLLIQKSILRD---AVTDLSLHYLAKAKIMVI 323
Cdd:PRK14104 246 plVIVAEDVEGEALATLVVNRLRGGLKvaAVKAPGfgdrrkamlqdIAILTGGQAISEDlgiKLENVTLQMLGRAKKVMI 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 324 KDVERDEIEFVTKTlnclpiANIEHFRAEKlgHADLVEEASLGDGKILKITGIKDMGRTTSVLVRGSNQLVLDEAERSLH 403
Cdd:PRK14104 326 DKENTTIVNGAGKK------ADIEARVAQI--KAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKERKDRVD 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 404 DALCVVRCLVSKRfLIAGGGAPEIELSRQLGAwAKVLHGMEGYCVKSFAEALEVIPYTLAENAGLNPIAIVTELRNKHaq 483
Cdd:PRK14104 398 DAMHATRAAVEEG-IVPGGGVALLRASEQLKG-IKTKNDDQKTGVEIVRKALSAPARQIAINAGEDGSVIVGKILEKE-- 473
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 15229595 484 gEINAGINVRKGQITNILEENVVQPLLVSTSAITLATECVRMILKIDDIV 533
Cdd:PRK14104 474 -QYSYGFDSQTGEYGNLVSKGIIDPTKVVRTAIQNAASVAALLITTEAMV 522
|
|
| PLN03167 |
PLN03167 |
Chaperonin-60 beta subunit; Provisional |
4-152 |
6.46e-09 |
|
Chaperonin-60 beta subunit; Provisional
Pssm-ID: 215611 [Multi-domain] Cd Length: 600 Bit Score: 58.40 E-value: 6.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229595 4 VAAPMASKPRGSKAESFVDNKRREDIRFANiNSARAVSDAVRTSLGPKGMDKMISTANGEVIITNDGATILNKMEVLQP- 82
Cdd:PLN03167 43 VRLRRSRSPKVKAAKELHFNKDGSAIKKLQ-AGVNKLADLVGVTLGPKGRNVVLESKYGSPKIVNDGVTVAKEVELEDPv 121
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15229595 83 ---AAKMLVELSKSQDSAAGDGTTTVVVIAGALLKECQSLLTNGIHPTVISDSLHKACGKAIDILTAMAVPVE 152
Cdd:PLN03167 122 eniGAKLVRQAAAKTNDLAGDGTTTSVVLAQGLIAEGVKVVAAGANPVQITRGIEKTAKALVKELKKMSKEVE 194
|
|
| |
