|
Name |
Accession |
Description |
Interval |
E-value |
| TCP1_delta |
cd03338 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ... |
14-528 |
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: 883.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 14 NRNEKQNDVRLTNILAAKAVADVTRTSLGPKGMDKMIEDGKGGVIITNDGATILKEMAVAHPTAKMIVELSKAQDVEAGD 93
Cdd:cd03338 1 TDKEKPADVRLSNIQAAKAVADAIRTSLGPRGMDKMIQTGKGEVIITNDGATILKQMSVLHPAAKMLVELSKAQDIEAGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 94 GTTSVVVMCGSFLNVCKSLLDKNIHCQKISESFFEASLKSEEILREMSIPIDLNDKNMLIQNAITSLNSKVVSYNSSLLA 173
Cdd:cd03338 81 GTTSVVVLAGALLSACESLLKKGIHPTVISESFQIAAKKAVEILDSMSIPVDLNDRESLIKSATTSLNSKVVSQYSSLLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 174 PIAVDVILKITDINKDTNVDLNNVRIVKKLGGTIEDTEIVDGLIFTgNKISKKAQGLKNLTQAKIGLIQFCLSLPKTDMD 253
Cdd:cd03338 161 PIAVDAVLKVIDPATATNVDLKDIRIVKKLGGTIEDTELVDGLVFT-QKASKKAGGPTRIEKAKIGLIQFCLSPPKTDMD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 254 NTVVVKDYNSMDRLLREERLIIGKMIKKIASTGCNLLIIQKSILRDAVNDLALDFLAKAKIMVIKDIDREDIEFISKTCN 333
Cdd:cd03338 240 NNIVVNDYAQMDRILREERKYILNMCKKIKKSGCNVLLIQKSILRDAVSDLALHFLAKLKIMVVKDIEREEIEFICKTIG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 334 CIPVASLDYFTSDKLGYAENVTTESVGYGEIVKITGVES-KNTISVLLRASNNLMLDEAERSLHDALCVVRSLIKEKAVL 412
Cdd:cd03338 320 CKPVASIDHFTEDKLGSADLVEEVSLGDGKIVKITGVKNpGKTVTILVRGSNKLVLDEAERSLHDALCVIRCLVKKRALI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 413 PGGAAPEMELSQKLYQWANTLKGSKQICVKAFSDALELIPYTLAENAGLSPLHIVTELRNKHAEGHKYHGINIRTGTISN 492
Cdd:cd03338 400 PGGGAPEIEIALQLSEWARTLTGVEQYCVRAFADALEVIPYTLAENAGLNPISIVTELRNRHAQGEKNAGINVRKGAITN 479
|
490 500 510
....*....|....*....|....*....|....*.
gi 296005530 493 MIDENVIQPLLVTSTAIKLATETVMMILKIDDTVIC 528
Cdd:cd03338 480 ILEENVVQPLLVSTSAITLATETVRMILKIDDIVLA 515
|
|
| chap_CCT_delta |
TIGR02342 |
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ... |
14-529 |
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: 726.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 14 NRNEKQNDVRLTNILAAKAVADVTRTSLGPKGMDKMIEDGKGGVIITNDGATILKEMAVAHPTAKMIVELSKAQDVEAGD 93
Cdd:TIGR02342 2 QDKDKPQDVRTSNIVAAKAVADAIRTSLGPKGMDKMIQDGKGEVIITNDGATILKQMAVLHPAAKMLVELSKAQDIEAGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 94 GTTSVVVMCGSFLNVCKSLLDKNIHCQKISESFFEASLKSEEILREMSIPIDLNDKNMLIQNAITSLNSKVVSYNSSLLA 173
Cdd:TIGR02342 82 GTTSVVILAGALLGACERLLNKGIHPTIISESFQSAADEAIKILDEMSIPVDLSDREQLLKSATTSLSSKVVSQYSSLLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 174 PIAVDVILKITDINKDTNVDLNNVRIVKKLGGTIEDTEIVDGLIFTgNKISKKAQGLKNLTQAKIGLIQFCLSLPKTDMD 253
Cdd:TIGR02342 162 PLAVDAVLKVIDPENAKNVDLNDIKVVKKLGGTIDDTELIEGLVFT-QKASKSAGGPTRIEKAKIGLIQFQISPPKTDME 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 254 NTVVVKDYNSMDRLLREERLIIGKMIKKIASTGCNLLIIQKSILRDAVNDLALDFLAKAKIMVIKDIDREDIEFISKTCN 333
Cdd:TIGR02342 241 NQIIVNDYAQMDRVLKEERAYILNIVKKIKKTGCNVLLIQKSILRDAVNDLALHFLAKMKIMVVKDIEREEIEFICKTIG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 334 CIPVASLDYFTSDKLGYAENVTTESVGYGEIVKITGVESK-NTISVLLRASNNLMLDEAERSLHDALCVVRSLIKEKAVL 412
Cdd:TIGR02342 321 CKPIASIDHFTADKLGSAELVEEVDSDGGKIIKITGIQNAgKTVTVVVRGSNKLVIDEAERSLHDALCVIRCLVKKRGLI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 413 PGGAAPEMELSQKLYQWANTLKGSKQICVKAFSDALELIPYTLAENAGLSPLHIVTELRNKHAEGHKYHGINIRTGTISN 492
Cdd:TIGR02342 401 AGGGAPEIEIARRLSKYARTMKGVESYCVRAFADALEVIPYTLAENAGLNPIKVVTELRNRHANGEKTAGISVRKGGITN 480
|
490 500 510
....*....|....*....|....*....|....*..
gi 296005530 493 MIDENVIQPLLVTSTAIKLATETVMMILKIDDTVICR 529
Cdd:TIGR02342 481 MLEEHVLQPLLVTTSAITLASETVRSILKIDDIVFTR 517
|
|
| chaperonin_type_I_II |
cd00309 |
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ... |
17-526 |
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: 539.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 17 EKQNDVRLTNILAAKAVADVTRTSLGPKGMDKMIEDGKGGVIITNDGATILKEMAVAHPTAKMIVELSKAQDVEAGDGTT 96
Cdd:cd00309 4 EFGEEARLSNINAAKALADAVKTTLGPKGMDKMLVDSLGDPTITNDGATILKEIEVEHPAAKLLVEVAKSQDDEVGDGTT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 97 SVVVMCGSFLNVCKSLLDKNIHCQKISESFFEASLKSEEILREMSIPIDLNDKNMLIQNAITSLNSKVVSYNSSLLAPIA 176
Cdd:cd00309 84 TVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVPIDVEDREELLKVATTSLNSKLVSGGDDFLGELV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 177 VDVILKITDinKDTNVDLNNVRIVKKLGGTIEDTEIVDGLIFTGNKISkkAQGLKNLTQAKIGLIQFCLSlpktdmdntv 256
Cdd:cd00309 164 VDAVLKVGK--ENGDVDLGVIRVEKKKGGSLEDSELVVGMVFDKGYLS--PYMPKRLENAKILLLDCKLE---------- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 257 vvkdynsmdrllreerliigkmikkiastgcNLLIIQKSIlrdavNDLALDFLAKAKIMVIKDIDREDIEFISKTCNCIP 336
Cdd:cd00309 230 -------------------------------YVVIAEKGI-----DDEALHYLAKLGIMAVRRVRKEDLERIAKATGATI 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 337 VASLDYFTSDKLGYAENVTTESVGYGEIVKITGVESKNTISVLLRASNNLMLDEAERSLHDALCVVRSLIKEKAVLPGGA 416
Cdd:cd00309 274 VSRLEDLTPEDLGTAGLVEETKIGDEKYTFIEGCKGGKVATILLRGATEVELDEAERSLHDALCAVRAAVEDGGIVPGGG 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 417 APEMELSQKLYQWANTLKGSKQICVKAFSDALELIPYTLAENAGLSPLHIVTELRNKHAEGHKYHGINIRTGTISNMIDE 496
Cdd:cd00309 354 AAEIELSKALEELAKTLPGKEQLGIEAFADALEVIPRTLAENAGLDPIEVVTKLRAKHAEGGGNAGGDVETGEIVDMKEA 433
|
490 500 510
....*....|....*....|....*....|
gi 296005530 497 NVIQPLLVTSTAIKLATETVMMILKIDDTV 526
Cdd:cd00309 434 GIIDPLKVKRQALKSATEAASLILTIDDII 463
|
|
| Cpn60_TCP1 |
pfam00118 |
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ... |
33-529 |
6.71e-178 |
|
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: 509.82 E-value: 6.71e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 33 VADVTRTSLGPKGMDKMIEDGKGGVIITNDGATILKEMAVAHPTAKMIVELSKAQDVEAGDGTTSVVVMCGSFLNVCKSL 112
Cdd:pfam00118 1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELEIQHPAAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEEAEKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 113 LDKNIHCQKISESFFEASLKSEEILREM-SIPIDLNDKNMLIQNAITSLNSKVVSYNSSLLAPIAVDVILKITDinKDTN 191
Cdd:pfam00118 81 LAAGVHPTTIIEGYEKALEKALEILDSIiSIPVEDVDREDLLKVARTSLSSKIISRESDFLAKLVVDAVLAIPK--NDGS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 192 VDLNNVRIVKKLGGTIEDTEIVDGLIFTGNKISkkAQGLKNLTQAKIGLIQFCLSLPKTDMDNTVVVKDYNSMDRLLREE 271
Cdd:pfam00118 159 FDLGNIGVVKILGGSLEDSELVDGVVLDKGPLH--PDMPKRLENAKVLLLNCSLEYEKTETKATVVLSDAEQLERFLKAE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 272 RLIIGKMIKKIASTGCNLLIIQKSIlrdavNDLALDFLAKAKIMVIKDIDREDIEFISKTCNCIPVASLDYFTSDKLGYA 351
Cdd:pfam00118 237 EEQILEIVEKIIDSGVNVVVCQKGI-----DDLALHFLAKNGIMALRRVKKRDLERLAKATGARAVSSLDDLTPDDLGTA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 352 ENVTTESVGYGEIVKITGVESKNTISVLLRASNNLMLDEAERSLHDALCVVRSLIKEKAVLPGGAAPEMELSQKLYQWAN 431
Cdd:pfam00118 312 GKVEEEKIGDEKYTFIEGCKSPKAATILLRGATDHVLDEIERSIHDALCVVKNAIEDPRVVPGGGAVEMELARALREYAK 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 432 TLKGSKQICVKAFSDALELIPYTLAENAGLSPLHIVTELRNKHAEGHKYHGINIRTGTISNMIDENVIQPLLVTSTAIKL 511
Cdd:pfam00118 392 SVSGKEQLAIEAFAEALEVIPKTLAENAGLDPIEVLAELRAAHASGEKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKS 471
|
490
....*....|....*...
gi 296005530 512 ATETVMMILKIDDTVICR 529
Cdd:pfam00118 472 ATEAASTILRIDDIIKAK 489
|
|
| thermosome_alpha |
NF041082 |
thermosome subunit alpha; |
21-527 |
1.65e-166 |
|
thermosome subunit alpha;
Pssm-ID: 469009 Cd Length: 518 Bit Score: 481.69 E-value: 1.65e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 21 DVRLTNILAAKAVADVTRTSLGPKGMDKMIEDGKGGVIITNDGATILKEMAVAHPTAKMIVELSKAQDVEAGDGTTSVVV 100
Cdd:NF041082 17 DAQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDVVITNDGVTILKEMDIEHPAAKMIVEVAKTQDDEVGDGTTTAVV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 101 MCGSFLNVCKSLLDKNIHCQKISESFFEASLKSEEILREMSIPIDLNDKNMLIQNAITSLNSKVVSYNSSLLAPIAVDVI 180
Cdd:NF041082 97 LAGELLKKAEELLDQDIHPTIIAEGYRLAAEKALEILDEIAIKVDPDDKETLKKIAATAMTGKGAEAAKDKLADLVVDAV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 181 LKITDINKDTNVDLNNVRIVKKLGGTIEDTEIVDGLIFTGNKISKKAQglKNLTQAKIGLIQFCLSLPKTDMDNTVVVKD 260
Cdd:NF041082 177 KAVAEKDGGYNVDLDNIKVEKKVGGSIEDSELVEGVVIDKERVHPGMP--KRVENAKIALLDAPLEVKKTEIDAKISITD 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 261 YNSMDRLLREERLIIGKMIKKIASTGCNLLIIQKSIlrdavNDLALDFLAKAKIMVIKDIDREDIEFISKTCNCIPVASL 340
Cdd:NF041082 255 PDQLQAFLDQEEKMLKEMVDKIADSGANVVFCQKGI-----DDLAQHYLAKEGILAVRRVKKSDMEKLAKATGARIVTSI 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 341 DYFTSDKLGYAENVTTESVGYGEIVKITGVESKNTISVLLRASNNLMLDEAERSLHDALCVVRSLIKEKAVLPGGAAPEM 420
Cdd:NF041082 330 DDLSPEDLGYAGLVEERKVGGDKMIFVEGCKNPKAVTILLRGGTEHVVDEVERALEDALRVVRVVLEDGKVVAGGGAPEV 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 421 ELSQKLYQWANTLKGSKQICVKAFSDALELIPYTLAENAGLSPLHIVTELRNKHAEGHKYHGINIRTGTISNMIDENVIQ 500
Cdd:NF041082 410 ELALRLREYAASVGGREQLAIEAFAEALEIIPRTLAENAGLDPIDALVELRSAHEKGNKTAGLDVYTGKVVDMLEIGVVE 489
|
490 500
....*....|....*....|....*..
gi 296005530 501 PLLVTSTAIKLATETVMMILKIDDtVI 527
Cdd:NF041082 490 PLRVKTQAIKSATEAAVMILRIDD-VI 515
|
|
| thermosome_beta |
NF041083 |
thermosome subunit beta; |
25-524 |
3.47e-165 |
|
thermosome subunit beta;
Pssm-ID: 469010 Cd Length: 519 Bit Score: 478.29 E-value: 3.47e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 25 TNILAAKAVADVTRTSLGPKGMDKMIEDGKGGVIITNDGATILKEMAVAHPTAKMIVELSKAQDVEAGDGTTSVVVMCGS 104
Cdd:NF041083 21 NNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDIVITNDGATILKEMDVQHPAAKMLVEVAKTQDDEVGDGTTTAVVLAGE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 105 FLNVCKSLLDKNIHCQKISESFFEASLKSEEILREMSIPIDLNDKNMLIQNAITSLNSKVVSYNSSLLAPIAVDVILKIT 184
Cdd:NF041083 101 LLKKAEELLDQNIHPTIIANGYRLAAEKAIEILDEIAEKVDPDDRETLKKIAETSLTSKGVEEARDYLAEIAVKAVKQVA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 185 DINKDTN-VDLNNVRIVKKLGGTIEDTEIVDGLIFTGNKISKKAQglKNLTQAKIGLIQFCLSLPKTDMDNTVVVKDYNS 263
Cdd:NF041083 181 EKRDGKYyVDLDNIQIEKKHGGSIEDTQLIYGIVIDKEVVHPGMP--KRVENAKIALLDAPLEVKKTEIDAEIRITDPDQ 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 264 MDRLLREERLIIGKMIKKIASTGCNLLIIQKSIlrdavNDLALDFLAKAKIMVIKDIDREDIEFISKTCNCIPVASLDYF 343
Cdd:NF041083 259 LQKFLDQEEKMLKEMVDKIKATGANVVFCQKGI-----DDLAQHYLAKAGILAVRRVKKSDMEKLAKATGARIVTNIDDL 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 344 TSDKLGYAENVTTESVGYGEIVKITGVESKNTISVLLRASNNLMLDEAERSLHDALCVVRSLIKEKAVLPGGAAPEMELS 423
Cdd:NF041083 334 TPEDLGYAELVEERKVGDDKMVFVEGCKNPKAVTILIRGGTEHVVDEAERALEDALSVVADAVEDGKIVAGGGAPEVELA 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 424 QKLYQWANTLKGSKQICVKAFSDALELIPYTLAENAGLSPLHIVTELRNKHAEGHKYHGINIRTGTISNMIDENVIQPLL 503
Cdd:NF041083 414 KRLREYAATVGGREQLAVEAFAEALEIIPRTLAENAGLDPIDILVKLRSAHEKGKKWAGINVFTGEVVDMWELGVIEPLR 493
|
490 500
....*....|....*....|.
gi 296005530 504 VTSTAIKLATETVMMILKIDD 524
Cdd:NF041083 494 VKTQAIKSATEAATMILRIDD 514
|
|
| cpn60 |
cd03343 |
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ... |
20-524 |
1.53e-163 |
|
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: 474.06 E-value: 1.53e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 20 NDVRLTNILAAKAVADVTRTSLGPKGMDKMIEDGKGGVIITNDGATILKEMAVAHPTAKMIVELSKAQDVEAGDGTTSVV 99
Cdd:cd03343 14 RDAQRMNIAAAKAVAEAVRTTLGPKGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAKTQDEEVGDGTTTAV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 100 VMCGSFLNVCKSLLDKNIHCQKISESFFEASLKSEEILREMSIPIDLNDKNMLIQNAITSLNSKVVSYNSSLLAPIAVDV 179
Cdd:cd03343 94 VLAGELLEKAEDLLDQNIHPTVIIEGYRLAAEKALELLDEIAIKVDPDDKDTLRKIAKTSLTGKGAEAAKDKLADLVVDA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 180 ILKITDINKD-TNVDLNNVRIVKKLGGTIEDTEIVDGLIFtgNKISKKAQGLKNLTQAKIGLIQFCLSLPKTDMDNTVVV 258
Cdd:cd03343 174 VLQVAEKRDGkYVVDLDNIKIEKKTGGSVDDTELIRGIVI--DKEVVHPGMPKRVENAKIALLDAPLEVKKTEIDAKIRI 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 259 KDYNSMDRLLREERLIIGKMIKKIASTGCNLLIIQKSIlrdavNDLALDFLAKAKIMVIKDIDREDIEFISKTCNCIPVA 338
Cdd:cd03343 252 TSPDQLQAFLEQEEAMLKEMVDKIADTGANVVFCQKGI-----DDLAQHYLAKAGILAVRRVKKSDMEKLARATGAKIVT 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 339 SLDYFTSDKLGYAENVTTESVGYGEIVKITGVESKNTISVLLRASNNLMLDEAERSLHDALCVVRSLIKEKAVLPGGAAP 418
Cdd:cd03343 327 NIDDLTPEDLGEAELVEERKVGDDKMVFVEGCKNPKAVTILLRGGTEHVVDELERALEDALRVVADALEDGKVVAGGGAV 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 419 EMELSQKLYQWANTLKGSKQICVKAFSDALELIPYTLAENAGLSPLHIVTELRNKHAEGHKYHGINIRTGTISNMIDENV 498
Cdd:cd03343 407 EIELAKRLREYARSVGGREQLAVEAFADALEEIPRTLAENAGLDPIDTLVELRAAHEKGNKNAGLDVYTGEVVDMLEKGV 486
|
490 500
....*....|....*....|....*.
gi 296005530 499 IQPLLVTSTAIKLATETVMMILKIDD 524
Cdd:cd03343 487 IEPLRVKKQAIKSATEAATMILRIDD 512
|
|
| thermosome_arch |
TIGR02339 |
thermosome, various subunits, archaeal; Thermosome is the name given to the archaeal rather ... |
17-526 |
3.31e-155 |
|
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: 452.99 E-value: 3.31e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 17 EKQNDVRLTNILAAKAVADVTRTSLGPKGMDKMIEDGKGGVIITNDGATILKEMAVAHPTAKMIVELSKAQDVEAGDGTT 96
Cdd:TIGR02339 12 TSGRDAQRNNIAAAKAVAEAVKSTLGPRGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAKTQDEEVGDGTT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 97 SVVVMCGSFLNVCKSLLDKNIHCQKISESFFEASLKSEEILREMSIPIDLNDKNMLIQNAITSLNSKVVS-YNSSLLAPI 175
Cdd:TIGR02339 92 TAVVLAGELLEKAEDLLEQDIHPTVIIEGYRKAAEKALEIIDEIATKISPEDRDLLKKIAYTSLTSKASAeVAKDKLADL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 176 AVDVILKIT--DINKDTNVDLNNVRIVKKLGGTIEDTEIVDGLIFTGNKISKKAQglKNLTQAKIGLIQFCLSLPKTDMD 253
Cdd:TIGR02339 172 VVEAVKQVAelRGDGKYYVDLDNIKIVKKKGGSIEDTELVEGIVVDKEVVHPGMP--KRVENAKIALLDAPLEVEKTEID 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 254 NTVVVKDYNSMDRLLREERLIIGKMIKKIASTGCNLLIIQKSIlrdavNDLALDFLAKAKIMVIKDIDREDIEFISKTCN 333
Cdd:TIGR02339 250 AKIRITDPDQIKKFLDQEEAMLKEMVDKIASAGANVVICQKGI-----DDVAQHYLAKAGILAVRRVKKSDIEKLARATG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 334 CIPVASLDYFTSDKLGYAENVTTESVGYGEIVKITGVESKNTISVLLRASNNLMLDEAERSLHDALCVVRSLIKEKAVLP 413
Cdd:TIGR02339 325 ARIVSSIDEITESDLGYAELVEERKVGEDKMVFVEGCKNPKAVTILLRGGTEHVVDELERSIQDALHVVANALEDGKIVA 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 414 GGAAPEMELSQKLYQWANTLKGSKQICVKAFSDALELIPYTLAENAGLSPLHIVTELRNKHAEGHKYHGINIRTGTISNM 493
Cdd:TIGR02339 405 GGGAVEIELALRLRSYARSVGGREQLAIEAFADALEEIPRILAENAGLDPIDALVDLRAKHEKGNKNAGINVFTGEIEDM 484
|
490 500 510
....*....|....*....|....*....|...
gi 296005530 494 IDENVIQPLLVTSTAIKLATETVMMILKIDDTV 526
Cdd:TIGR02339 485 LELGVIEPLRVKEQAIKSATEAATMILRIDDVI 517
|
|
| TCP1_epsilon |
cd03339 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ... |
25-526 |
1.27e-122 |
|
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: 369.71 E-value: 1.27e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 25 TNILAAKAVADVTRTSLGPKGMDKMIEDGKGGVIITNDGATILKEMAVAHPTAKMIVELSKAQDVEAGDGTTSVVVMCGS 104
Cdd:cd03339 27 SHILAAKSVANILRTSLGPRGMDKILVSPDGEVTVTNDGATILEKMDVDHQIAKLLVELSKSQDDEIGDGTTGVVVLAGA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 105 FLNVCKSLLDKNIHCQKISESFFEASLKSEEILREMS--IPIDLNDKNMLIQNAITSLNSKVVSYNSSLLAPIAVDVILK 182
Cdd:cd03339 107 LLEQAEKLLDRGIHPIRIADGYEQACKIAVEHLEEIAdkIEFSPDNKEPLIQTAMTSLGSKIVSRCHRQFAEIAVDAVLS 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 183 ITDIN-KDTNVDLnnVRIVKKLGGTIEDTEIVDGLIFtgNKISKKAQGLKNLTQAKIGLIQFCLSLPKTDMDNTVVVKDY 261
Cdd:cd03339 187 VADLErKDVNFEL--IKVEGKVGGRLEDTKLVKGIVI--DKDFSHPQMPKEVKDAKIAILTCPFEPPKPKTKHKLDITSV 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 262 NSMDRLLREERLIIGKMIKKIASTGCNLLIIQKSIlrdavNDLALDFLAKAKIMVIKDIDREDIEFISKTCNCIPVASLD 341
Cdd:cd03339 263 EDYKKLQEYEQKYFREMVEQVKDAGANLVICQWGF-----DDEANHLLLQNGLPAVRWVGGVEIELIAIATGGRIVPRFE 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 342 YFTSDKLGYAENVttESVGYG----EIVKITGVESKNTISVLLRASNNLMLDEAERSLHDALCVVRSLIKEKAVLPGGAA 417
Cdd:cd03339 338 DLSPEKLGKAGLV--REISFGttkdKMLVIEGCPNSKAVTIFIRGGNKMIIEEAKRSLHDALCVVRNLIRDNRIVYGGGA 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 418 PEMELSQKLYQWANTLKGSKQICVKAFSDALELIPYTLAENAGLSPLHIVTELRNKH-AEGHKYHGINIRTGTISNMIDE 496
Cdd:cd03339 416 AEISCSLAVEKAADKCSGIEQYAMRAFADALESIPLALAENSGLNPIETLSEVKARQvKEKNPHLGIDCLGRGTNDMKEQ 495
|
490 500 510
....*....|....*....|....*....|
gi 296005530 497 NVIQPLLVTSTAIKLATETVMMILKIDDTV 526
Cdd:cd03339 496 KVFETLISKKQQILLATQVVKMILKIDDVI 525
|
|
| TCP1_eta |
cd03340 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ... |
24-526 |
1.30e-110 |
|
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: 338.88 E-value: 1.30e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 24 LTNILAAKAVADVTRTSLGPKGMDKMIEDGKGGVIITNDGATILKEMAVAHPTAKMIVELSKAQDVEAGDGTTSVVVMCG 103
Cdd:cd03340 19 ISNINACQAIADAVRTTLGPRGMDKLIVDGRGKVTISNDGATILKLLDIVHPAAKTLVDIAKSQDAEVGDGTTSVVVLAG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 104 SFLNVCKSLLDKNIHCQKISESFFEASLKSEEILREMSIPIDLNDKN----MLIQNAITSLNSKVVSYNSSLLAPIAVDV 179
Cdd:cd03340 99 EFLKEAKPFIEDGVHPQIIIRGYRKALQLAIEKIKEIAVNIDKEDKEeqreLLEKCAATALNSKLIASEKEFFAKMVVDA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 180 ILKItdinkDTNVDLNNVRIVKKLGGTIEDTEIVDGLIFtgnkisKKA-------QGLKNLTQAKIGLIQFCLSLpKTDM 252
Cdd:cd03340 179 VLSL-----DDDLDLDMIGIKKVPGGSLEDSQLVNGVAF------KKTfsyagfeQQPKKFKNPKILLLNVELEL-KAEK 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 253 DNTVV----VKDYNSmdrLLREERLIIGKMIKKIASTGCNLLIIQKSIlrdavNDLALDFLAKAKIMVIKDIDREDIEFI 328
Cdd:cd03340 247 DNAEVrvedPEEYQA---IVDAEWKIIYDKLEKIVKSGANVVLSKLPI-----GDLATQYFADRDIFCAGRVPEEDLKRV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 329 SKTCNCIPVASLDYFTSDKLGYAENVTTESVGyGEIVKI-TGVESKNTISVLLRASNNLMLDEAERSLHDALCVVRSLIK 407
Cdd:cd03340 319 AQATGGSIQTTVSNITDDVLGTCGLFEERQVG-GERYNIfTGCPKAKTCTIILRGGAEQFIEEAERSLHDAIMIVRRAIK 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 408 EKAVLPGGAAPEMELSQKLYQWANTLKGSKQICVKAFSDALELIPYTLAENAGLSPLHIVTELRNKHAEG-HKYHGINIR 486
Cdd:cd03340 398 NDSVVAGGGAIEMELSKYLRDYSRTIAGKQQLVINAFAKALEIIPRQLCDNAGFDATDILNKLRQKHAQGgGKWYGVDIN 477
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 296005530 487 TGTISNMIDENVIQPLLVTSTAIKLATETVMMILKIDDTV 526
Cdd:cd03340 478 NEGIADNFEAFVWEPSLVKINALTAATEAACLILSVDETI 517
|
|
| TCP1_gamma |
cd03337 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ... |
6-526 |
1.44e-110 |
|
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: 337.35 E-value: 1.44e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 6 KNKNTEKlnrnEKQNDVRLTNILAAKAVADVTRTSLGPKGMDKMIEDGKGGVIITNDGATILKEMAVAHPTAKMIVELSK 85
Cdd:cd03337 5 LNQNTKR----ESGRKAQLGNIQAAKTVADVIRTCLGPRAMLKMLLDPMGGIVLTNDGNAILREIDVAHPAAKSMIELSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 86 AQDVEAGDGTTSVVVMCGSFLNVCKSLLDKNIHCQKISESFFEASLKSEEILREMSIPIDLNDKNMLIQNAITSLNSKVV 165
Cdd:cd03337 81 TQDEEVGDGTTSVIILAGEILAVAEPFLERGIHPTVIIKAYRKALEDALKILEEISIPVDVNDRAQMLKIIKSCIGTKFV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 166 SYNSSLLAPIAVDVILKITDINKDTNVDL---NNVRIVKKLGGTIEDTEIVDGLIFTgnkiskkaqglKNLTQAKigliq 242
Cdd:cd03337 161 SRWSDLMCNLALDAVKTVAVEENGRKKEIdikRYAKVEKIPGGEIEDSRVLDGVMLN-----------KDVTHPK----- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 243 fclslpktdmdntvvvkdynsMDRLLREERLIIgkmikkiasTGCNL--LIIQKsilrDAVNDLALDFLAKAKIMVIKDI 320
Cdd:cd03337 225 ---------------------MRRRIENPRIVL---------LDCPLeyLVITE----KGVSDLAQHYLVKAGITALRRV 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 321 DREDIEFISKTCNCIPVASLDYFTSDKLGyaenvtteSVGYGEIVKITG-------VESKN--TISVLLRASNNLMLDEA 391
Cdd:cd03337 271 RKTDNNRIARACGATIVNRPEELTESDVG--------TGAGLFEVKKIGdeyftfiTECKDpkACTILLRGASKDVLNEV 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 392 ERSLHDALCVVRSLIKEKAVLPGGAAPEMELSQKLYQWANTLKGSKQICVKAFSDALELIPYTLAENAGLSPLHIVTELR 471
Cdd:cd03337 343 ERNLQDAMAVARNIILNPKLVPGGGATEMAVSHALSEKAKSIEGVEQWPYKAVASALEVIPRTLAQNCGANVIRTLTELR 422
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 296005530 472 NKHAEGHK-YHGINIRTGTISNMIDENVIQPLLVTSTAIKLATETVMMILKIDDTV 526
Cdd:cd03337 423 AKHAQGENsTWGIDGETGDIVDMKELGIWDPLAVKAQTYKTAIEAACMLLRIDDIV 478
|
|
| chap_CCT_epsi |
TIGR02343 |
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ... |
21-527 |
4.29e-110 |
|
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: 337.93 E-value: 4.29e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 21 DVRLTNILAAKAVADVTRTSLGPKGMDKMIEDGKGGVIITNDGATILKEMAVAHPTAKMIVELSKAQDVEAGDGTTSVVV 100
Cdd:TIGR02343 27 EAKKSNIAAAKSVASILRTSLGPKGMDKMLISPDGDITVTNDGATILSQMDVDNQIAKLMVELSKSQDDEIGDGTTGVVV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 101 MCGSFLNVCKSLLDKNIHCQKISESFFEASLKSEEILREMS--IPIDLNDKNMLIQNAITSLNSKVVSYNSSLLAPIAVD 178
Cdd:TIGR02343 107 LAGALLEQAEELLDKGIHPIKIADGFEEAARIAVEHLEEISdeISADNNNREPLIQAAKTSLGSKIVSKCHRRFAEIAVD 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 179 VILKITDIN-KDTNVDLnnVRIVKKLGGTIEDTEIVDGLIFtgNKISKKAQGLKNLTQAKIGLIQFCLSLPKTDMDNTVV 257
Cdd:TIGR02343 187 AVLNVADMErRDVDFDL--IKVEGKVGGSLEDTKLIKGIII--DKDFSHPQMPKEVEDAKIAILTCPFEPPKPKTKHKLD 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 258 VKDYNSMDRLLREERLIIGKMIKKIASTGCNLLIIQKSIlrdavNDLALDFLAKAKIMVIKDIDREDIEFISKTCNCIPV 337
Cdd:TIGR02343 263 ISSVEEYKKLQKYEQQKFKEMIDDIKKSGANLVICQWGF-----DDEANHLLLQNDLPAVRWVGGQELELIAIATGGRIV 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 338 ASLDYFTSDKLGYAENVTTESVGYGE--IVKITGVESKNTISVLLRASNNLMLDEAERSLHDALCVVRSLIKEKAVLPGG 415
Cdd:TIGR02343 338 PRFQELSKDKLGKAGLVREISFGTTKdrMLVIEQCKNSKAVTIFIRGGNKMIIEEAKRSIHDALCVVRNLIKDSRIVYGG 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 416 AAPEMELSQKLYQWANTLKGSKQICVKAFSDALELIPYTLAENAGLSPLHIVTELRNKHAEGHKYH-GINIRTGTISNMI 494
Cdd:TIGR02343 418 GAAEISCSLAVSQEADKYPGVEQYAIRAFADALETIPMALAENSGLDPIGTLSTLKSLQLKEKNPNlGVDCLGYGTNDMK 497
|
490 500 510
....*....|....*....|....*....|...
gi 296005530 495 DENVIQPLLVTSTAIKLATETVMMILKIDDTVI 527
Cdd:TIGR02343 498 EQFVFETLIGKKQQILLATQLVRMILKIDDVIS 530
|
|
| chap_CCT_alpha |
TIGR02340 |
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ... |
20-527 |
1.97e-109 |
|
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: 336.31 E-value: 1.97e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 20 NDVRLTNILAAKAVADVTRTSLGPKGMDKMIEDGKGGVIITNDGATILKEMAVAHPTAKMIVELSKAQDVEAGDGTTSVV 99
Cdd:TIGR02340 11 QDVRTQNVTAAMAIANIVKTSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDREVGDGTTSVV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 100 VMCGSFLNVCKSLLDKNIHCQKISESFFEASLKSEEILRE-MSIPIDLNDKNMLIQNAITSLNSKVVSYNSSLLAPIAVD 178
Cdd:TIGR02340 91 IIAAELLKRADELVKNKIHPTSVISGYRLACKEAVKYIKEnLSVSVDELGREALINVAKTSMSSKIIGLDSDFFSNIVVD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 179 VIL--KITDINKDTNVDLNNVRIVKKLGGTIEDTEIVDGLIFtgnKISKKAQGL-KNLTQAKIGLIQFCLSLPKTDMDNT 255
Cdd:TIGR02340 171 AVLavKTTNENGETKYPIKAINILKAHGKSARESMLVKGYAL---NCTVASQQMpKRIKNAKIACLDFNLQKAKMALGVQ 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 256 VVVKDYNSMDRLLREERLIIGKMIKKIASTGCNLLIIQKSIlrdavNDLALDFLAKAKIMVIKDIDREDIEFISKTCNCI 335
Cdd:TIGR02340 248 IVVDDPEKLEQIRQREADITKERIKKILDAGANVVLTTGGI-----DDMCLKYFVEAGAMGVRRCKKEDLKRIAKATGAT 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 336 PVASL------DYFTSDKLGYAENVTTESVGYGEIVKITGVESKNTISVLLRASNNLMLDEAERSLHDALCVVRSLIKEK 409
Cdd:TIGR02340 323 LVSTLadlegeETFEASYLGFADEVVQERIADDECILIKGTKKRKSASIILRGANDFMLDEMERSLHDALCVVKRTLESN 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 410 AVLPGGAAPEMELSQKLYQWANTLKGSKQICVKAFSDALELIPYTLAENAGLSPLHIVTELRNKHA--------EGHKYH 481
Cdd:TIGR02340 403 SVVPGGGAVEAALSIYLENFATTLGSREQLAIAEFARALLIIPKTLAVNAAKDSTELVAKLRAYHAaaqlkpekKHLKWY 482
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 296005530 482 GINIRTGTISNMIDENVIQPLLVTSTAIKLATETVMMILKIDDTVI 527
Cdd:TIGR02340 483 GLDLVNGKIRDNKEAGVLEPTVSKVKSLKFATEAAITILRIDDLIK 528
|
|
| TCP1_alpha |
cd03335 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ... |
20-527 |
4.45e-108 |
|
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: 332.33 E-value: 4.45e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 20 NDVRLTNILAAKAVADVTRTSLGPKGMDKMIEDGKGGVIITNDGATILKEMAVAHPTAKMIVELSKAQDVEAGDGTTSVV 99
Cdd:cd03335 7 QDVRTQNVTAAMAIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDKEVGDGTTSVV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 100 VMCGSFLNVCKSLLDKNIHCQKISESFFEASLKSEEILRE-MSIPIDLNDKNMLIQNAITSLNSKVVSYNSSLLAPIAVD 178
Cdd:cd03335 87 IIAAELLKRANELVKQKIHPTTIISGYRLACKEAVKYIKEhLSISVDNLGKESLINVAKTSMSSKIIGADSDFFANMVVD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 179 VIL--KITDINKDTNVDLNNVRIVKKLGGTIEDTEIVDGLIFTgnkISKKAQGL-KNLTQAKIGLIQFCLSLPKTDMDNT 255
Cdd:cd03335 167 AILavKTTNEKGKTKYPIKAVNILKAHGKSAKESYLVNGYALN---CTRASQGMpTRVKNAKIACLDFNLQKTKMKLGVQ 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 256 VVVKDYNSMDRLLREERLIIGKMIKKIASTGCNLLIIQKSIlrdavNDLALDFLAKAKIMVIKDIDREDIEFISKTCN-- 333
Cdd:cd03335 244 VVVTDPEKLEKIRQRESDITKERIKKILAAGANVVLTTGGI-----DDMCLKYFVEAGAMAVRRVKKEDLRRIAKATGat 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 334 -CIPVASLD---YFTSDKLGYAENVTTESVGYGEIVKITGVESKNTISVLLRASNNLMLDEAERSLHDALCVVRSLIKEK 409
Cdd:cd03335 319 lVSTLANLEgeeTFDPSYLGEAEEVVQERIGDDELILIKGTKKRSSASIILRGANDFMLDEMERSLHDALCVVKRTLESN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 410 AVLPGGAAPEMELSQKLYQWANTLKGSKQICVKAFSDALELIPYTLAENAGLSPLHIVTELRNKHAEGH--------KYH 481
Cdd:cd03335 399 SVVPGGGAVETALSIYLENFATTLGSREQLAIAEFAEALLVIPKTLAVNAAKDATELVAKLRAYHAAAQvkpdkkhlKWY 478
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 296005530 482 GINIRTGTISNMIDENVIQPLLVTSTAIKLATETVMMILKIDDTVI 527
Cdd:cd03335 479 GLDLINGKVRDNLEAGVLEPTVSKIKSLKFATEAAITILRIDDLIK 524
|
|
| chap_CCT_eta |
TIGR02345 |
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ... |
24-526 |
1.03e-105 |
|
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: 326.33 E-value: 1.03e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 24 LTNILAAKAVADVTRTSLGPKGMDKMIEDGKGGVIITNDGATILKEMAVAHPTAKMIVELSKAQDVEAGDGTTSVVVMCG 103
Cdd:TIGR02345 21 ISNINACVAIAEALKTTLGPRGMDKLIVGSNGKATISNDGATILKLLDIVHPAAKTLVDIAKSQDAEVGDGTTSVTILAG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 104 SFLNVCKSLLDKNIHCQKISESFFEASLKSEEILREMSIPIDLND---KNMLIQNAITSLNSKVVSYNSSLLAPIAVDVI 180
Cdd:TIGR02345 101 ELLKEAKPFIEEGVHPQLIIRCYREALSLAVEKIKEIAVTIDEEKgeqRELLEKCAATALSSKLISHNKEFFSKMIVDAV 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 181 LKItdinKDTNVDLNNVRIVKKLGGTIEDTEIVDGLIFtgnkisKKA-------QGLKNLTQAKIGLIQFCLSLpKTDMD 253
Cdd:TIGR02345 181 LSL----DRDDLDLKLIGIKKVQGGALEDSQLVNGVAF------KKTfsyagfeQQPKKFANPKILLLNVELEL-KAEKD 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 254 NTVV-VKDYNSMDRLLREERLIIGKMIKKIASTGCNLLIIQKSIlrdavNDLALDFLAKAKIMVIKDIDREDIEFISKTC 332
Cdd:TIGR02345 250 NAEIrVEDVEDYQAIVDAEWAIIFRKLEKIVESGANVVLSKLPI-----GDLATQYFADRDIFCAGRVSAEDLKRVIKAC 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 333 NCIPVASLDYFTSDKLGYAENVTTESVGYGEIVKITGVESKNTISVLLRASNNLMLDEAERSLHDALCVVRSLIKEKAVL 412
Cdd:TIGR02345 325 GGSIQSTTSDLEADVLGTCALFEERQIGSERYNYFTGCPHAKTCTIILRGGAEQFIEEAERSLHDAIMIVRRALKNKKIV 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 413 PGGAAPEMELSQKLYQWANTLKGSKQICVKAFSDALELIPYTLAENAGLSPLHIVTELRNKHAEGHKYHGINIRTGTISN 492
Cdd:TIGR02345 405 AGGGAIEMELSKCLRDYSKTIDGKQQLIINAFAKALEIIPRQLCENAGFDSIEILNKLRSRHAKGGKWYGVDINTEDIGD 484
|
490 500 510
....*....|....*....|....*....|....
gi 296005530 493 MIDENVIQPLLVTSTAIKLATETVMMILKIDDTV 526
Cdd:TIGR02345 485 NFEAFVWEPALVKINALKAAFEAACTILSVDETI 518
|
|
| chap_CCT_theta |
TIGR02346 |
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ... |
24-527 |
1.02e-103 |
|
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: 321.28 E-value: 1.02e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 24 LTNILAAKAVADVTRTSLGPKGMDKMIEDGKGGVIITNDGATILKEMAVAHPTAKMIVELSKAQDVEAGDGTTSVVVMCG 103
Cdd:TIGR02346 21 IKNIEACKELSQITRTSLGPNGMNKMVINHLEKLFVTNDAATILRELEVQHPAAKLLVMASEMQENEIGDGTNLVLVLAG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 104 SFLNVCKSLLDKNIHCQKISESFFEASLKSEEILREMSI--PIDLNDKNMLIQNAITSLNSKVVSyNSSLLAPIAVDVIL 181
Cdd:TIGR02346 101 ELLNKAEELIRMGLHPSEIIKGYEMALKKAMEILEELVVweVKDLRDKDELIKALKASISSKQYG-NEDFLAQLVAQACS 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 182 KITDINkDTNVDLNNVRIVKKLGGTIEDTEIVDGLIFTgnkisKKAQG-LKNLTQAKIGLIQFCLSLPKTDMDNTVVVKD 260
Cdd:TIGR02346 180 TVLPKN-PQNFNVDNIRVCKILGGSLSNSEVLKGMVFN-----REAEGsVKSVKNAKVAVFSCPLDTATTETKGTVLIHN 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 261 YNSMDRLLREERLIIGKMIKKIASTGCNLLIIQKSIlrdavNDLALDFLAKAKIMVIKDIDREDIEFISKTCNCIPVASL 340
Cdd:TIGR02346 254 AEELLNYSKGEENQIEAMIKAIADSGVNVIVTGGSV-----GDMALHYLNKYNIMVLKIPSKFELRRLCKTVGATPLPRL 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 341 DYFTSDKLGYAENVTTESVGygeIVKITGVESKNTIS----VLLRASNNLMLDEAERSLHDALCVVRSLIKEKAVLPGGA 416
Cdd:TIGR02346 329 GAPTPEEIGYVDSVYVSEIG---GDKVTVFKQENGDSkistIILRGSTDNLLDDIERAIDDGVNTVKALVKDGRLLPGAG 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 417 APEMELSQKLYQWANTLKGSKQICVKAFSDALELIPYTLAENAGLSPLHIVTELRNKHAEGHKYHGINIRTGTIS--NMI 494
Cdd:TIGR02346 406 ATEIELASRLTKYGEKLPGLDQYAIKKFAEAFEIIPRTLAENAGLNANEVIPKLYAAHKKGNKSKGIDIEAESDGvkDAS 485
|
490 500 510
....*....|....*....|....*....|...
gi 296005530 495 DENVIQPLLVTSTAIKLATETVMMILKIDDTVI 527
Cdd:TIGR02346 486 EAGIYDMLATKKWAIKLATEAAVTVLRVDQIIM 518
|
|
| TCP1_beta |
cd03336 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ... |
17-529 |
3.64e-102 |
|
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: 316.96 E-value: 3.64e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 17 EKQNDVRLTNILAAKAVADVTRTSLGPKGMDKMIEDG--KGGVIITNDGATILKEMAVAHPTAKMIVELSKAQDVEAGDG 94
Cdd:cd03336 9 EKGETARLSSFVGAIAIGDLVKTTLGPKGMDKILQSVgrSGGVTVTNDGATILKSIGVDNPAAKVLVDISKVQDDEVGDG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 95 TTSVVVMCGSFLNVCKSLLDKNIHCQKISESFFEASLKSEEILREMSIPIDLND---KNMLIQNAITSLNSKVVSYNSSL 171
Cdd:cd03336 89 TTSVTVLAAELLREAEKLVAQKIHPQTIIEGYRMATAAAREALLSSAVDHSSDEeafREDLLNIARTTLSSKILTQDKEH 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 172 LAPIAVDVILKITDinkdtNVDLNNVRIVKKLGGTIEDTEIVDGLIFtgnkisKKAQGL---KNLTQAKIgLIQfclslp 248
Cdd:cd03336 169 FAELAVDAVLRLKG-----SGNLDAIQIIKKLGGSLKDSYLDEGFLL------DKKIGVnqpKRIENAKI-LIA------ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 249 KTDMDnTVVVKDY------NSMDRLL---REERLIIGKMIKKIASTGCNLLIIqksilRDAVNDLALDFLAKAKIMVIKD 319
Cdd:cd03336 231 NTPMD-TDKIKIFgakvrvDSTAKVAeieEAEKEKMKNKVEKILKHGINCFIN-----RQLIYNYPEQLFADAGIMAIEH 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 320 IDREDIEFISKTCNCIPVASLDYFTSDKLGYAENVTTESVGYGEIVKITGVESKNTISVLLRASNNLMLDEAERSLHDAL 399
Cdd:cd03336 305 ADFDGVERLALVTGGEIASTFDHPELVKLGTCKLIEEIMIGEDKLIRFSGVAAGEACTIVLRGASQQILDEAERSLHDAL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 400 CVVRSLIKEKAVLPGGAAPEMELSQKLYQWANTLKGSKQICVKAFSDALELIPYTLAENAGLSPLHIVTELRNKHAEGHK 479
Cdd:cd03336 385 CVLAQTVKDTRVVLGGGCSEMLMAKAVEELAKKTPGKKSLAIEAFAKALRQLPTIIADNAGYDSAELVAQLRAAHYNGNT 464
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 296005530 480 YHGINIRTGTISNMIDENVIQPLLVTSTAIKLATETVMMILKIDDTVICR 529
Cdd:cd03336 465 TAGLDMRKGTVGDMKELGITESFKVKRQVLLSASEAAEMILRVDDIIKCA 514
|
|
| GroEL |
COG0459 |
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ... |
21-526 |
2.08e-101 |
|
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227 Cd Length: 497 Bit Score: 314.32 E-value: 2.08e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 21 DVRLTNILAAKAVADVTRTSLGPKGMDKMIEDGKGGVIITNDGATILKEMAVAHP----TAKMIVELSKAQDVEAGDGTT 96
Cdd:COG0459 10 DARRANIRGVKALADAVKVTLGPKGRNVMLVKSFGDPTITNDGVTIAKEIELEDPfenmGAQLVKEVASKTNDEAGDGTT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 97 SVVVMCGSFLNVCKSLLDKNIHCQKISESFFEASLKSEEILREMSIPIDlnDKNMLIQNAITSLNskvvsyNSSLLAPIA 176
Cdd:COG0459 90 TATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPVD--DKEELAQVATISAN------GDEEIGELI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 177 VDVILKITdinKDTNVdlnnvrIVKKLGGTIEDTEIVDGLIF-----TGNKISKKAQGLKNLTQAKIgLIqfclslpkTD 251
Cdd:COG0459 162 AEAMEKVG---KDGVI------TVEEGKGLETELEVVEGMQFdkgylSPYFVTDPEKMPAELENAYI-LL--------TD 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 252 mdntvvvKDYNSMDRLLreerliigKMIKKIASTGCNLLIIQKSIlrdavNDLALDFLAKAKIMVIKDI---------DR 322
Cdd:COG0459 224 -------KKISSIQDLL--------PLLEKVAQSGKPLLIIAEDI-----DGEALATLVVNGIRGVLRVvavkapgfgDR 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 323 -----EDI------EFISKTCNcipvASLDYFTSDKLGYAENVTtesVGYGEIVKITGVESKNTISVLLRASNNLMLDEA 391
Cdd:COG0459 284 rkamlEDIailtggRVISEDLG----LKLEDVTLDDLGRAKRVE---VDKDNTTIVEGAGNPKAIVILVGAATEVEVKER 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 392 ERSLHDALCVVRSLIKEKaVLPGGAAPEMELSQKLYQWANTLKGSKQICVKAFSDALELIPYTLAENAGLSPLHIVTELR 471
Cdd:COG0459 357 KRRVEDALHATRAAVEEG-IVPGGGAALLRAARALRELAAKLEGDEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKVR 435
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 296005530 472 nkhAEGHKYHGINIRTGTISNMIDENVIQPLLVTSTAIKLATETVMMILKIDDTV 526
Cdd:COG0459 436 ---AAKDKGFGFDAATGEYVDMLEAGVIDPAKVKRSALQNAASVAGLILTTEAVI 487
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
17-528 |
4.72e-101 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 314.66 E-value: 4.72e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 17 EKQNDVRLTNILAAKAVADVTRTSLGPKGMDKMIE-----DGKGGVIITNDGATILKEMAVAHPTAKMIVELSKAQDVEA 91
Cdd:PTZ00212 18 EKGETARLQSFVGAIAVADLVKTTLGPKGMDKILQpmsegPRSGNVTVTNDGATILKSVWLDNPAAKILVDISKTQDEEV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 92 GDGTTSVVVMCGSFLNVCKSLLDKNIHCQKISESFFEASLKSEEILREMSIPIDLND---KNMLIQNAITSLNSKVVSYN 168
Cdd:PTZ00212 98 GDGTTSVVVLAGELLREAEKLLDQKIHPQTIIEGWRMALDVARKALEEIAFDHGSDEekfKEDLLNIARTTLSSKLLTVE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 169 SSLLAPIAVDVILKITDinkdtNVDLNNVRIVKKLGGTIEDTEIVDGLIFtgnkisKKAQGL---KNLTQAKIgLIQfcl 245
Cdd:PTZ00212 178 KDHFAKLAVDAVLRLKG-----SGNLDYIQIIKKPGGTLRDSYLEDGFIL------EKKIGVgqpKRLENCKI-LVA--- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 246 slpKTDMDnTVVVKDY------NSMDRLLREERLIIGKMIKK---IASTGCNLLIIqksilRDAVNDLALDFLAKAKIMV 316
Cdd:PTZ00212 243 ---NTPMD-TDKIKIYgakvkvDSMEKVAEIEAAEKEKMKNKvdkILAHGCNVFIN-----RQLIYNYPEQLFAEAGIMA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 317 IKDIDREDIEFISKTCNCIPVASLDYFTSDKLGYAENVTTESVGYGEIVKITGVESKNTISVLLRASNNLMLDEAERSLH 396
Cdd:PTZ00212 314 IEHADFDGMERLAAALGAEIVSTFDTPEKVKLGHCDLIEEIMIGEDKLIRFSGCAKGEACTIVLRGASTHILDEAERSLH 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 397 DALCVVRSLIKEKAVLPGGAAPEMELSQKLYQWANTLKGSKQICVKAFSDALELIPYTLAENAGLSPLHIVTELRNKHAE 476
Cdd:PTZ00212 394 DALCVLSQTVKDTRVVLGGGCSEMLMANAVEELAKKVEGKKSLAIEAFAKALRQIPTIIADNGGYDSAELVSKLRAEHYK 473
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 296005530 477 GHKYHGINIRTGTISNMIDENVIQPLLVTSTAIKLATETVMMILKIDDTVIC 528
Cdd:PTZ00212 474 GNKTAGIDMEKGTVGDMKELGITESYKVKLSQLCSATEAAEMILRVDDIIRC 525
|
|
| chap_CCT_gamma |
TIGR02344 |
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ... |
7-526 |
4.94e-100 |
|
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: 311.67 E-value: 4.94e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 7 NKNTEKlnrnEKQNDVRLTNILAAKAVADVTRTSLGPKGMDKMIEDGKGGVIITNDGATILKEMAVAHPTAKMIVELSKA 86
Cdd:TIGR02344 6 NQNTKR----ESGRKAQLSNIQAAKAVADIIRTCLGPRSMLKMLLDPMGGIVMTNDGNAILREIDVAHPAAKSMIELSRT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 87 QDVEAGDGTTSVVVMCGSFLNVCKSLLDKNIHCQKISESFFEASLKSEEILREMSIPIDLNDKNMLIQNAITSLNSKVVS 166
Cdd:TIGR02344 82 QDEEVGDGTTSVIILAGEMLSVAEPFLEQNIHPTVIIRAYRKALDDALSVLEEISIPVDVNDDAAMLKLIQSCIGTKFVS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 167 YNSSLLAPIAVDVILKIT-DINKDTNVDLNNVRIVKKL-GGTIEDTEIVDGLIFtgNKISKKAQGLKNLTQAKIGLIQFC 244
Cdd:TIGR02344 162 RWSDLMCDLALDAVRTVQrDENGRKEIDIKRYAKVEKIpGGDIEDSCVLKGVMI--NKDVTHPKMRRYIENPRIVLLDCP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 245 LSLPKTDMDNTVVVKDYNSMDRLLREERLIIGKMIKKIASTGCNLLIIQKsilrdAVNDLALDFLAKAKIMVIKDIDRED 324
Cdd:TIGR02344 240 LEYKKGESQTNIEITKEEDWNRILQMEEEYVQLMCEDIIAVKPDLVITEK-----GVSDLAQHYLLKANITAIRRVRKTD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 325 IEFISKTCNCIPVASLdyftsdklgyaENVTTESVGYG----EIVKI--------TGVESKNTISVLLRASNNLMLDEAE 392
Cdd:TIGR02344 315 NNRIARACGATIVNRP-----------EELRESDVGTGcglfEVKKIgdeyftfiTECKDPKACTILLRGASKDILNEVE 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 393 RSLHDALCVVRSLIKEKAVLPGGAAPEMELSQKLYQWANTLKGSKQICVKAFSDALELIPYTLAENAGLSPLHIVTELRN 472
Cdd:TIGR02344 384 RNLQDAMAVARNVLLDPKLVPGGGATEMAVSVALTEKSKKLEGVEQWPYRAVADALEIIPRTLAQNCGANVIRTLTELRA 463
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 296005530 473 KHAEGHKYH-GINIRTGTISNMIDENVIQPLLVTSTAIKLATETVMMILKIDDTV 526
Cdd:TIGR02344 464 KHAQENNCTwGIDGETGKIVDMKEKGIWEPLAVKLQTYKTAIESACLLLRIDDIV 518
|
|
| TCP1_theta |
cd03341 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ... |
24-523 |
4.44e-96 |
|
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: 299.52 E-value: 4.44e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 24 LTNILAAKAVADVTRTSLGPKGMDKMIEDGKGGVIITNDGATILKEMAVAHPTAKMIVELSKAQDVEAGDGTTSVVVMCG 103
Cdd:cd03341 11 LRNIEACKELSQITRTSYGPNGMNKMVINHLEKLFVTSDAATILRELEVQHPAAKLLVMASQMQEEEIGDGTNLVVVLAG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 104 SFLNVCKSLLDKNIHCQKISESFFEASLKSEEILREMSIP--IDLNDKNMLIQNAITSLNSKVvSYNSSLLAPIAVDVIL 181
Cdd:cd03341 91 ELLEKAEELLRMGLHPSEIIEGYEKALKKALEILEELVVYkiEDLRNKEEVSKALKTAIASKQ-YGNEDFLSPLVAEACI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 182 KItdINKDT---NVDlnNVRIVKKLGGTIEDTEIVDGLIFtgnkiSKKAQG-LKNLTQAKIGLiqfcLSLPKtdmdntvv 257
Cdd:cd03341 170 SV--LPENIgnfNVD--NIRVVKILGGSLEDSKVVRGMVF-----KREPEGsVKRVKKAKVAV----FSCPF-------- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 258 vkdynsmdrllreerliigkmikkiaSTGCNLLIIQKSilrdaVNDLALDFLAKAKIMVIKDIDREDIEFISKTCNCIPV 337
Cdd:cd03341 229 --------------------------DIGVNVIVAGGS-----VGDLALHYCNKYGIMVIKINSKFELRRLCRTVGATPL 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 338 ASLDYFTSDKLGYAENVTTESVGYGEIVKITGVESKNTIS-VLLRASNNLMLDEAERSLHDALCVVRSLIKEKAVLPGGA 416
Cdd:cd03341 278 PRLGAPTPEEIGYCDSVYVEEIGDTKVVVFRQNKEDSKIAtIVLRGATQNILDDVERAIDDGVNVFKSLTKDGRFVPGAG 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 417 APEMELSQKLYQWANTLKGSKQICVKAFSDALELIPYTLAENAGLSPLHIVTELRNKHAEGHKYHGINIRTGTIS--NMI 494
Cdd:cd03341 358 ATEIELAKKLKEYGEKTPGLEQYAIKKFAEAFEVVPRTLAENAGLDATEVLSELYAAHQKGNKSAGVDIESGDEGtkDAK 437
|
490 500
....*....|....*....|....*....
gi 296005530 495 DENVIQPLLVTSTAIKLATETVMMILKID 523
Cdd:cd03341 438 EAGIFDHLATKKWAIKLATEAAVTVLRVD 466
|
|
| chap_CCT_beta |
TIGR02341 |
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ... |
17-526 |
5.70e-77 |
|
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: 251.32 E-value: 5.70e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 17 EKQNDVRLTNILAAKAVADVTRTSLGPKGMDKMIEDG--KGGVIITNDGATILKEMAVAHPTAKMIVELSKAQDVEAGDG 94
Cdd:TIGR02341 10 ERAENARLSSFVGAIAIGDLVKSTLGPKGMDKILQSSssDASIMVTNDGATILKSIGVDNPAAKVLVDMSKVQDDEVGDG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 95 TTSVVVMCGSFLNVCKSLLDKNIHCQKISESFFEASLKSEEILREMSIPiDLNDKNM----LIQNAITSLNSKVVSYNSS 170
Cdd:TIGR02341 90 TTSVTVLAAELLREAEKLINQKIHPQTIIAGYREATKAARDALLKSAVD-NGSDEVKfrqdLMNIARTTLSSKILSQHKD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 171 LLAPIAVDVILKITDinkdtNVDLNNVRIVKKLGGTIEDTEIVDGLIFtgNKISKKAQGlKNLTQAKIGLIQFCLSLPKT 250
Cdd:TIGR02341 169 HFAQLAVDAVLRLKG-----SGNLEAIQIIKKLGGSLADSYLDEGFLL--DKKIGVNQP-KRIENAKILIANTGMDTDKV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 251 DMDNTVV-VKDYNSMDRLLREERLIIGKMIKKIASTGCNLLIIqksilRDAVNDLALDFLAKAKIMVIKDIDREDIEFIS 329
Cdd:TIGR02341 241 KIFGSRVrVDSTAKVAELEHAEKEKMKEKVEKILKHGINCFIN-----RQLIYNYPEQLFADAGVMAIEHADFEGVERLA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 330 KTCNCIPVASLDYFTSDKLGYAENVTTESVGYGEIVKITGVESKNTISVLLRASNNLMLDEAERSLHDALCVVRSLIKEK 409
Cdd:TIGR02341 316 LVTGGEIVSTFDHPELVKLGSCDLIEEIMIGEDKLLKFSGVKLGEACTIVLRGATQQILDEAERSLHDALCVLSQTVKES 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 410 AVLPGGAAPEMELSQKLYQWANTLKGSKQICVKAFSDALELIPYTLAENAGLSPLHIVTELRNKHAEGHKYHGINIRTGT 489
Cdd:TIGR02341 396 RTVLGGGCSEMLMSKAVTQEAQRTPGKEALAVEAFARALRQLPTIIADNAGFDSAELVAQLRAAHYNGNTTMGLDMNEGT 475
|
490 500 510
....*....|....*....|....*....|....*..
gi 296005530 490 ISNMIDENVIQPLLVTSTAIKLATETVMMILKIDDTV 526
Cdd:TIGR02341 476 IADMRQLGITESYKVKRAVVSSAAEAAEVILRVDNII 512
|
|
| chap_CCT_zeta |
TIGR02347 |
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ... |
7-528 |
5.75e-75 |
|
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: 246.57 E-value: 5.75e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 7 NKNTEKLNRNEkqndVRLTNILAAKAVADVTRTSLGPKGMDKMIEDGKGGVIITNDGATILKEMAVAHPTAKMIVELSKA 86
Cdd:TIGR02347 6 NPKAESLRRDA----ALMMNINAARGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEMQIQHPTASMIARAATA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 87 QDVEAGDGTTSVVVMCGSFLNVCKSLLDKNIHCQKISESFFEASLKSEEILREMSIPI-DLNDKNMLIQNAITSLNSKVV 165
Cdd:TIGR02347 82 QDDITGDGTTSTVLLIGELLKQAERYILEGVHPRIITEGFEIARKEALQFLDKFKVKKeDEVDREFLLNVARTSLRTKLP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 166 SYNSSLLAPIAVDVILKITDINKDtnVDLNNVRIVKKLGGTIEDTEIVDGLIFtgNKISKKAQGLKNLTQAKIGLIQFCL 245
Cdd:TIGR02347 162 ADLADQLTEIVVDAVLAIKKDGED--IDLFMVEIMEMKHKSATDTTLIRGLVL--DHGARHPDMPRRVKNAYILTCNVSL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 246 SLPKTDMDNTVVVKDYNSMDRLLREERLIIGKMIKKIA---------STGCNLLII-QKSIlrdavNDLALDFLAKAKIM 315
Cdd:TIGR02347 238 EYEKTEVNSGFFYSSAEQREKLVKAERKFVDDRVKKIIelkkkvcgkSPDKGFVVInQKGI-----DPPSLDLLAKEGIM 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 316 VIKDIDREDIEFISKTCNCIPVASLDYFTSDKLGYAENVTTESVGYGEIVKITGVESKNTISVLLRASNNLMLDEAERSL 395
Cdd:TIGR02347 313 ALRRAKRRNMERLTLACGGEALNSVEDLTPECLGWAGLVYETTIGEEKYTFIEECKNPKSCTILIKGPNDHTIAQIKDAV 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 396 HDALCVVRSLIKEKAVLPGGAAPEMELSQKLYQWANTLKGSKQICVKAFSDALELIPYTLAENAGLSPLHIVTELRNKHA 475
Cdd:TIGR02347 393 RDGLRAVKNAIEDKCVVPGAGAFEIAAYRHLKEYKKSVKGKAKLGVEAFANALLVIPKTLAENSGFDAQDTLVKLEDEHD 472
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 296005530 476 EGHKYHGINIRTGTISNMIDENVIQPLLVTSTAIKLATETVMMILKIDDTVIC 528
Cdd:TIGR02347 473 EGGEVVGVDLNTGEPIDPEIKGIWDNYRVKKQLIQSATVIASQLLLVDEVMRA 525
|
|
| TCP1_zeta |
cd03342 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
25-523 |
1.96e-72 |
|
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: 238.31 E-value: 1.96e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 25 TNILAAKAVADVTRTSLGPKGMDKMIEDGKGGVIITNDGATILKEMAVAHPTAKMIVELSKAQDVEAGDGTTSVVVMCGS 104
Cdd:cd03342 16 VNISAAKGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLSEMQIQHPTASMIARAATAQDDITGDGTTSNVLLIGE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 105 FLNVCKSLLDKNIHCQKISESFFEASLKSEEILREMSIPID-LNDKNMLIQNAITSLNSKVVSYNSSLLAPIAVDVILKI 183
Cdd:cd03342 96 LLKQAERYIQEGVHPRIITEGFELAKNKALKFLESFKVPVEiDTDRELLLSVARTSLRTKLHADLADQLTEIVVDAVLAI 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 184 TDINKdtNVDLNNVRIVKKLGGTIEDTEIVDGLIFtgNKISKKAQGLKNLTQAKIGLIQFCLSLPKTDMDNTVVVKdyns 263
Cdd:cd03342 176 YKPDE--PIDLHMVEIMQMQHKSDSDTKLIRGLVL--DHGARHPDMPKRVENAYILTCNVSLEYEKTEVNSGFFYS---- 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 264 mdrllreerliigkmikkiastgcnLLIIQKSIlrdavNDLALDFLAKAKIMVIKDIDREDIEFISKTCNCIPVASLDYF 343
Cdd:cd03342 248 -------------------------VVINQKGI-----DPPSLDMLAKEGILALRRAKRRNMERLTLACGGVAMNSVDDL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 344 TSDKLGYAENVTTESVGYGEIVKITGVESKNTISVLLRASNNLMLDEAERSLHDALCVVRSLIKEKAVLPGGAAPEMELS 423
Cdd:cd03342 298 SPECLGYAGLVYERTLGEEKYTFIEGVKNPKSCTILIKGPNDHTITQIKDAIRDGLRAVKNAIEDKCVVPGAGAFEVALY 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 424 QKLYQWANTLKGSKQICVKAFSDALELIPYTLAENAGLSPLHIVTELRNKHAEGHKYHGINIRTGTISNMIDENVIQPLL 503
Cdd:cd03342 378 AHLKEFKKSVKGKAKLGVQAFADALLVIPKTLAENSGLDVQETLVKLQDEYAEGGQVGGVDLDTGEPMDPESEGIWDNYS 457
|
490 500
....*....|....*....|
gi 296005530 504 VTSTAIKLATETVMMILKID 523
Cdd:cd03342 458 VKRQILHSATVIASQLLLVD 477
|
|
| chaperonin_like |
cd03333 |
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ... |
149-408 |
1.46e-56 |
|
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: 188.06 E-value: 1.46e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 149 KNMLIQNAITSLNSKVvSYNSSLLAPIAVDVILKITDinKDTNVDLNNVRIVKKLGGTIEDTEIVDGLIFTGNKISKkaQ 228
Cdd:cd03333 1 RELLLQVATTSLNSKL-SSWDDFLGKLVVDAVLKVGP--DNRMDDLGVIKVEKIPGGSLEDSELVVGVVFDKGYASP--Y 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 229 GLKNLTQAKIGLIQFCLSlpktdmdntvvvkdynsmdrllreerliigkmikkiastgcNLLIIQKSIlrdavNDLALDF 308
Cdd:cd03333 76 MPKRLENAKILLLDCPLE-----------------------------------------YVVIAEKGI-----DDLALHY 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 309 LAKAKIMVIKDIDREDIEFISKTCNCIPVASLDYFTSDKLGYAENVTTESVGYGEIVKITGVESKNTISVLLRASNNLML 388
Cdd:cd03333 110 LAKAGIMAVRRVKKEDLERIARATGATIVSSLEDLTPEDLGTAELVEETKIGEEKLTFIEGCKGGKAATILLRGATEVEL 189
|
250 260
....*....|....*....|
gi 296005530 389 DEAERSLHDALCVVRSLIKE 408
Cdd:cd03333 190 DEVKRSLHDALCAVRAAVEE 209
|
|
| Fab1_TCP |
cd03334 |
TCP-1 like domain of the eukaryotic phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinase Fab1. ... |
169-412 |
2.85e-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: 75.72 E-value: 2.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 169 SSLLAPIAVDVILKIT-DINKDTNVDLNN-VRIVKKLGGTIEDTEIVDGLIFTGNKISKK-AQGLKNltqAKIGLIQFCL 245
Cdd:cd03334 20 LDILLPLVWKAASNVKpDVRAGDDMDIRQyVKIKKIPGGSPSDSEVVDGVVFTKNVAHKRmPSKIKN---PRILLLQGPL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 246 SLPKtdmdntvVVKDYNSMDRLLREERLIIGKMIKKIASTGCNLLIIQKSILRdavndLALDFLAKAKIMVIKDIDREDI 325
Cdd:cd03334 97 EYQR-------VENKLLSLDPVILQEKEYLKNLVSRIVALRPDVILVEKSVSR-----IAQDLLLEAGITLVLNVKPSVL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 326 EFISKTCNCIPVASLD-YFTSDKLGYAENVTTESVGYGEIVK-----ITGVESKNTISVLLRASNNLMLDEAERSLHDAL 399
Cdd:cd03334 165 ERISRCTGADIISSMDdLLTSPKLGTCESFRVRTYVEEHGRSktlmfFEGCPKELGCTILLRGGDLEELKKVKRVVEFMV 244
|
250
....*....|...
gi 296005530 400 CVVRSLIKEKAVL 412
Cdd:cd03334 245 FAAYHLKLETSFL 257
|
|
| PTZ00114 |
PTZ00114 |
Heat shock protein 60; Provisional |
31-520 |
7.20e-15 |
|
Heat shock protein 60; Provisional
Pssm-ID: 185455 Cd Length: 555 Bit Score: 77.26 E-value: 7.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 31 KAVADVTRTSLGPKGMDKMIEDGKGGVIITNDGATILKEMAVAHPT----AKMIVELSKAQDVEAGDGTTSVVVMCGSFL 106
Cdd:PTZ00114 32 ERLADAVAVTLGPKGRNVIIEQEYGSPKITKDGVTVAKAIEFSDRFenvgAQLIRQVASKTNDKAGDGTTTATILARAIF 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 107 NV-CKSLLDK----------NIHCQKISESffeaslkseeiLREMSIPIdlNDKNMLIQNAITSLNskvvsYNSSLLAPI 175
Cdd:PTZ00114 112 REgCKAVAAGlnpmdlkrgiDLAVKVVLES-----------LKEQSRPV--KTKEDILNVATISAN-----GDVEIGSLI 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 176 AvDVILKitdINKDTNVDLNNvrivkklGGTIEDT-EIVDGLIFTGNKISKK-AQGLKNLtqakigliqfclslpKTDMD 253
Cdd:PTZ00114 174 A-DAMDK---VGKDGTITVED-------GKTLEDElEVVEGMSFDRGYISPYfVTNEKTQ---------------KVELE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 254 NTVVvkdynsmdrllreerLIIGKMIKKIAS----------TGCNLLIIQKSILRDAVNDLALDFL-AKAKIMVIK---- 318
Cdd:PTZ00114 228 NPLI---------------LVTDKKISSIQSilpilehavkNKRPLLIIAEDVEGEALQTLIINKLrGGLKVCAVKapgf 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 319 -DIDREDIEFISKTCNCIPV------ASLDYFTSDKLGYAENVTtesVGYGEIVKITGVESKNTIsvllRASNNLMLDEA 391
Cdd:PTZ00114 293 gDNRKDILQDIAVLTGATVVsednvgLKLDDFDPSMLGSAKKVT---VTKDETVILTGGGDKAEI----KERVELLRSQI 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 392 ERSLH---------------------------------------DALCVVRSLIKEkAVLPGGAAPEMELSQKL--YQWA 430
Cdd:PTZ00114 366 ERTTSeydkeklkerlaklsggvavikvggasevevnekkdrieDALNATRAAVEE-GIVPGGGVALLRASKLLdkLEED 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 431 NTLKGSKQICVKAFSDALELIPYTLAENAGLSPLHIVTELRNkhaEGHKYHGINIRTGTISNMIDENVIQPLLVTSTAIK 510
Cdd:PTZ00114 445 NELTPDQRTGVKIVRNALRLPTKQIAENAGVEGAVVVEKILE---KKDPSFGYDAQTGEYVNMFEAGIIDPTKVVRSALV 521
|
570
....*....|
gi 296005530 511 LATETVMMIL 520
Cdd:PTZ00114 522 DAASVASLML 531
|
|
| GroEL |
cd03344 |
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ... |
30-517 |
1.78e-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: 1.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 30 AKAVADVTRTSLGPKGMDKMIEDGKGGVIITNDGATILKEMAVAHPTAKMIVEL-----SKAQDVeAGDGTTSVVVMCGS 104
Cdd:cd03344 17 VNKLADAVKVTLGPKGRNVVIEKSFGSPKITKDGVTVAKEIELEDPFENMGAQLvkevaSKTNDV-AGDGTTTATVLARA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 105 -FLNVCKSlLDKNIHCQKISESFFEASLKSEEILREMSIPIdlNDKNMLIQNAITSLNskvvsyNSSLLAPIAVDVILKi 183
Cdd:cd03344 96 iIKEGLKA-VAAGANPMDLKRGIEKAVEAVVEELKKLSKPV--KTKEEIAQVATISAN------GDEEIGELIAEAMEK- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 184 tdinkdtnVDLNNVrIVKKLGGTIEDT-EIVDGLIFTGNKIS---------KKAQgLKN----LTQAKIGLIQfclslpk 249
Cdd:cd03344 166 --------VGKDGV-ITVEEGKTLETElEVVEGMQFDRGYLSpyfvtdpekMEVE-LENpyilLTDKKISSIQ------- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 250 tdmdntvvvkdynSMDRLLReerliigkmikKIASTGCNLLIIQKSILRDAVNDLALDFL-AKAKIMVIKDI---DR--- 322
Cdd:cd03344 229 -------------ELLPILE-----------LVAKAGRPLLIIAEDVEGEALATLVVNKLrGGLKVCAVKAPgfgDRrka 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 323 --EDI------EFISKTCNcipvASLDYFTSDKLGYAENVT--------TESVGYGEIVKitgvESKNTISVLLRASNNL 386
Cdd:cd03344 285 mlEDIailtggTVISEELG----LKLEDVTLEDLGRAKKVVvtkddttiIGGAGDKAAIK----ARIAQIRKQIEETTSD 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 387 MLDE--AER--------------------------SLHDALCVVRSLIKEkAVLPGGAAPEMELSQKLYQWAnTLKGSKQ 438
Cdd:cd03344 357 YDKEklQERlaklsggvavikvggatevelkekkdRVEDALNATRAAVEE-GIVPGGGVALLRASPALDKLK-ALNGDEK 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 439 ICVKAFSDALELIPYTLAENAGLSPLHIVTELRNKHAEghkyHGINIRTGTISNMIDENVIQPLLVTSTAIK-------- 510
Cdd:cd03344 435 LGIEIVRRALEAPLRQIAENAGVDGSVVVEKVLESPDG----FGYDAATGEYVDMIEAGIIDPTKVVRSALQnaasvasl 510
|
....*...
gi 296005530 511 -LATETVM 517
Cdd:cd03344 511 lLTTEALV 518
|
|
| groEL |
CHL00093 |
chaperonin GroEL |
30-520 |
9.08e-13 |
|
chaperonin GroEL
Pssm-ID: 177025 Cd Length: 529 Bit Score: 70.52 E-value: 9.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 30 AKAVAdVTrtsLGPKGMDKMIEDGKGGVIITNDGATILKEMAVAHPTAKMIVEL-----SKAQDVeAGDGTTSVVVMCGS 104
Cdd:CHL00093 23 AEAVS-VT---LGPKGRNVVLEKKYGSPQIVNDGVTIAKEIELEDHIENTGVALirqaaSKTNDV-AGDGTTTATVLAYA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 105 FlnVCKSLldKNIHCQK----ISESFFEASLKSEEILREMSIPIDlnDKNMLIQNA-ITSLNSKVVSynsSLLApiavDV 179
Cdd:CHL00093 98 I--VKQGM--KNVAAGAnpisLKRGIEKATQYVVSQIAEYARPVE--DIQAITQVAsISAGNDEEVG---SMIA----DA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 180 ILKItdiNKDTNVDLNNVRivkklgGTIEDTEIVDGLIFTGNKIS--------KKAQGLKN----LTQAKIGLIQFCLsL 247
Cdd:CHL00093 165 IEKV---GREGVISLEEGK------STVTELEITEGMRFEKGFISpyfvtdteRMEVVQENpyilLTDKKITLVQQDL-L 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 248 PktdmdntvVVKDYNSMDRLLreerLIIGKMIKKIA-STgcnlLIIQKsiLRDAVNDLAL---DFLAKAKIMVikdidrE 323
Cdd:CHL00093 235 P--------ILEQVTKTKRPL----LIIAEDVEKEAlAT----LVLNK--LRGIVNVVAVrapGFGDRRKAML------E 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 324 DIEFISKTCNCIPVA--SLDYFTSDKLGYA-------ENVTTESVGYGEIVKITGVESKNTISV-------------LLR 381
Cdd:CHL00093 291 DIAILTGGQVITEDAglSLETIQLDLLGQArriivtkDSTTIIADGNEEQVKARCEQLRKQIEIadssyekeklqerLAK 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 382 ASNNL------------MLDEAERsLHDALCVVRSLIKEkAVLPGGAAPEMELSQKLYQWA-NTLKGSKQICVKAFSDAL 448
Cdd:CHL00093 371 LSGGVavikvgaateteMKDKKLR-LEDAINATKAAVEE-GIVPGGGATLVHLSENLKTWAkNNLKEDELIGALIVARAI 448
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 296005530 449 ELIPYTLAENAGLSPLHIVTELRNKHAEghkyHGINIRTGTISNMIDENVIQPLLVTSTAIKLATETVMMIL 520
Cdd:CHL00093 449 LAPLKRIAENAGKNGSVIIEKVQEQDFE----IGYNAANNKFVNMYEAGIIDPAKVTRSALQNAASIASMIL 516
|
|
| groEL |
PRK12849 |
chaperonin GroEL; Reviewed |
32-520 |
1.78e-11 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237230 Cd Length: 542 Bit Score: 66.37 E-value: 1.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 32 AVADVTRTSLGPKGMDKMIEDGKGGVIITNDGATILKEMAVAHP----TAKMIVE-LSKAQDVeAGDGTTSVVVMCGSFL 106
Cdd:PRK12849 21 KLADAVKVTLGPKGRNVVIDKSFGAPTITKDGVSIAKEIELEDPfenlGAQLVKEvASKTNDV-AGDGTTTATVLAQALV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 107 -----NVCKSL----LDKNIHcqkisesffEASLKSEEILREMSIPIDlnDKNMLIQNAITSLNskvvsyNSSLLAPIAV 177
Cdd:PRK12849 100 qeglkNVAAGAnpmdLKRGID---------KAVEAVVEELKALARPVS--GSEEIAQVATISAN------GDEEIGELIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 178 DVILKitdinkdtnVDLNNVrIVKKLGGTIEDT-EIVDGLIFTGNKIS--------KKAQGLKN----LTQAKIGLIQFC 244
Cdd:PRK12849 163 EAMEK---------VGKDGV-ITVEESKTLETElEVTEGMQFDRGYLSpyfvtdpeRMEAVLEDplilLTDKKISSLQDL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 245 LSLPKT-------------DMD----------------NTVVVKDYNSMDRllREErliigkMIKKIAS-TGCNLLIIQK 294
Cdd:PRK12849 233 LPLLEKvaqsgkplliiaeDVEgealatlvvnklrgglKVAAVKAPGFGDR--RKA------MLEDIAIlTGGTVISEDL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 295 SILRDAVNdlaLDFLAKA-KIMVIKD---I-----DREDIEF-ISKTCNCIPVASLDYfTSDKLGyaENVTTESVGYGEI 364
Cdd:PRK12849 305 GLKLEEVT---LDDLGRAkRVTITKDnttIvdgagDKEAIEArVAQIRRQIEETTSDY-DREKLQ--ERLAKLAGGVAVI 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 365 vKITG---VESKNTIsvlLRasnnlmldeaersLHDALCVVRSLIKEkAVLPGGAAPEMELSQKLYQWANtLKGSKQICV 441
Cdd:PRK12849 379 -KVGAateVELKERK---DR-------------VEDALNATRAAVEE-GIVPGGGVALLRAAKALDELAG-LNGDQAAGV 439
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 296005530 442 KAFSDALELIPYTLAENAGLSPLHIVtelrNKHAEGHKYHGINIRTGTISNMIDENVIQPLLVTSTAIKLATETVMMIL 520
Cdd:PRK12849 440 EIVRRALEAPLRQIAENAGLDGSVVV----AKVLELEDGFGFNAATGEYGDLIAAGIIDPVKVTRSALQNAASVAGLLL 514
|
|
| groEL |
PRK12850 |
chaperonin GroEL; Reviewed |
32-101 |
1.31e-08 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237231 Cd Length: 544 Bit Score: 57.42 E-value: 1.31e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 296005530 32 AVADVTRTSLGPKGMDKMIEDGKGGVIITNDGATILKEMAVAHPTAKMIVEL-----SKAQDVeAGDGTTSVVVM 101
Cdd:PRK12850 22 ILANAVKVTLGPKGRNVVLEKSFGAPRITKDGVTVAKEIELEDKFENMGAQMvkevaSKTNDL-AGDGTTTATVL 95
|
|
| GroEL |
TIGR02348 |
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ... |
31-101 |
1.93e-08 |
|
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: 56.92 E-value: 1.93e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 296005530 31 KAVADVTRTSLGPKGMDKMIEDGKGGVIITNDGATILKEMAVAHP----TAKMIVEL-SKAQDVeAGDGTTSVVVM 101
Cdd:TIGR02348 19 DKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDKfenmGAQLVKEVaSKTNDV-AGDGTTTATVL 93
|
|
| groEL |
PRK12851 |
chaperonin GroEL; Reviewed |
30-101 |
7.34e-08 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 171770 Cd Length: 541 Bit Score: 55.13 E-value: 7.34e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 296005530 30 AKAVADVTRTSLGPKGMDKMIEDGKGGVIITNDGATILKEMAVAHPTAKMIVEL-----SKAQDVeAGDGTTSVVVM 101
Cdd:PRK12851 20 VNILADAVKVTLGPKGRNVVIDKSFGAPTITNDGVTIAKEIELEDKFENMGAQMvrevaSKTNDV-AGDGTTTATVL 95
|
|
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
32-96 |
2.24e-07 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 53.59 E-value: 2.24e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 32 AVADVTRTSLGPKGMDKMIEDGKGGVIITNDGATILKEMAVAHPTAKMIVEL-----SKAQDVeAGDGTT 96
Cdd:PRK00013 21 KLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDPFENMGAQLvkevaSKTNDV-AGDGTT 89
|
|
| groEL |
PRK12852 |
chaperonin GroEL; Reviewed |
12-106 |
2.20e-06 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237232 Cd Length: 545 Bit Score: 50.23 E-value: 2.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 12 KLNRNEKQNDVRLTNILAakavaDVTRTSLGPKGMDKMIEDGKGGVIITNDGATILKEMAVA----HPTAKMIVEL-SKA 86
Cdd:PRK12852 7 KFSGDARDRMLRGVDILA-----NAVKVTLGPKGRNVVIEKSFGAPRITKDGVTVAKEIELEdkfeNMGAQMVREVaSKT 81
|
90 100
....*....|....*....|
gi 296005530 87 QDVeAGDGTTSVVVMCGSFL 106
Cdd:PRK12852 82 NDL-AGDGTTTATVLAQAIV 100
|
|
| PLN03167 |
PLN03167 |
Chaperonin-60 beta subunit; Provisional |
33-107 |
1.41e-05 |
|
Chaperonin-60 beta subunit; Provisional
Pssm-ID: 215611 [Multi-domain] Cd Length: 600 Bit Score: 47.61 E-value: 1.41e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 296005530 33 VADVTRTSLGPKGMDKMIEDGKGGVIITNDGATILKEMAVAHPT----AKMIVELSKAQDVEAGDGTTSVVVMCGSFLN 107
Cdd:PLN03167 78 LADLVGVTLGPKGRNVVLESKYGSPKIVNDGVTVAKEVELEDPVenigAKLVRQAAAKTNDLAGDGTTTSVVLAQGLIA 156
|
|
| PRK14104 |
PRK14104 |
chaperonin GroEL; Provisional |
21-526 |
4.19e-05 |
|
chaperonin GroEL; Provisional
Pssm-ID: 172594 Cd Length: 546 Bit Score: 46.18 E-value: 4.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 21 DVRLTNILAAKAVADVTRTSLGPKGMDKMIEDGKGGVIITNDGATILKEMAV----AHPTAKMIVEL-SKAQDVeAGDGT 95
Cdd:PRK14104 11 DARDRMLRGVDILANAVKVTLGPKGRNVVLDKSFGAPRITKDGVTVAKEIELedkfENMGAQMVREVaSKSADA-AGDGT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 96 TSVVVMCGSFLNVCKSLLDKNIHcqkisesffeaslkseeilremsiPIDLNDK-NMLIQNAITSL--NSKVVSYNssll 172
Cdd:PRK14104 90 TTATVLAQAIVREGAKSVAAGMN------------------------PMDLKRGiDLAVEAVVADLvkNSKKVTSN---- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 173 apiavDVILKITDI--NKDTNVDLNNVRIVKKLGG----TIEDT-------EIVDGLIFTGNKISKKAqgLKNLTQAKIg 239
Cdd:PRK14104 142 -----DEIAQVGTIsaNGDAEIGKFLADAMKKVGNegviTVEEAksletelDVVEGMQFDRGYISPYF--VTNADKMRV- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 240 liqfclslpktDMDNTVVV---KDYNSMDRLLreerliigKMIKKIASTGCNLLIIQKSILRDAVNDLALDFLAKA-KIM 315
Cdd:PRK14104 214 -----------EMDDAYILineKKLSSLNELL--------PLLEAVVQTGKPLVIVAEDVEGEALATLVVNRLRGGlKVA 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 316 VIKDIDREDIEfiSKTCNCIPVASLDYFTSDKLGYA-ENVTTESVGYGEIVKI--------TGVESKNTIS--------- 377
Cdd:PRK14104 275 AVKAPGFGDRR--KAMLQDIAILTGGQAISEDLGIKlENVTLQMLGRAKKVMIdkenttivNGAGKKADIEarvaqikaq 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 378 ------------------------VLLRASNNLMLDEAERS--LHDALCVVRSLIkEKAVLPGGAAPEMELSQKLyQWAN 431
Cdd:PRK14104 353 ieettsdydreklqerlaklaggvAVIRVGGATEVEVKERKdrVDDAMHATRAAV-EEGIVPGGGVALLRASEQL-KGIK 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 432 TLKGSKQICVKAFSDALELIPYTLAENAGLSPLHIVTELRNKhaEGHKYhGINIRTGTISNMIDENVIQPLLVTSTAIKL 511
Cdd:PRK14104 431 TKNDDQKTGVEIVRKALSAPARQIAINAGEDGSVIVGKILEK--EQYSY-GFDSQTGEYGNLVSKGIIDPTKVVRTAIQN 507
|
570
....*....|....*
gi 296005530 512 ATETVMMILKIDDTV 526
Cdd:PRK14104 508 AASVAALLITTEAMV 522
|
|
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
397-512 |
1.37e-04 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 44.34 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296005530 397 DALCVVRSLIKEkAVLPGGAAPEMELSQKLyQWANTLKGSKQICVKAFSDALELIPYTLAENAGLSPLHIVTELRNKHAE 476
Cdd:PRK00013 397 DALHATRAAVEE-GIVPGGGVALLRAAPAL-EALKGLNGDEATGINIVLRALEAPLRQIAENAGLEGSVVVEKVKNGKGK 474
|
90 100 110
....*....|....*....|....*....|....*.
gi 296005530 477 GhkyHGINIRTGTISNMIDENVIQPLLVTSTAIKLA 512
Cdd:PRK00013 475 G---YGYNAATGEYVDMIEAGIIDPTKVTRSALQNA 507
|
|
| |
