|
Name |
Accession |
Description |
Interval |
E-value |
| Cpn60_TCP1 |
pfam00118 |
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ... |
24-511 |
2.67e-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: 510.98 E-value: 2.67e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 24 LADAIRTTLGPNGLDKMVVGENGTVIVTNDGSKIIEWMDITHPVGRLVEQAAAAQDNTVGDGTTTAVVLVGALLEEAATL 103
Cdd:pfam00118 1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELEIQHPAAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEEAEKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 104 RSAGLHPTTIIDGYGRAVEAALDQLAQYeRGLHSRQDDR--LTQIAKTAVTGRWDDASTDRFAELTLSALQAIG-----F 176
Cdd:pfam00118 81 LAAGVHPTTIIEGYEKALEKALEILDSI-ISIPVEDVDRedLLKVARTSLSSKIISRESDFLAKLVVDAVLAIPkndgsF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 177 DRSRLTLKSYPGGELRESVCLDGVLVDLETSSTSLntlshprTRTHDEPAIAMVDAEIGIEEPNNVESVELQDATQRNAF 256
Cdd:pfam00118 160 DLGNIGVVKILGGSLEDSELVDGVVLDKGPLHPDM-------PKRLENAKVLLLNCSLEYEKTETKATVVLSDAEQLERF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 257 QAHEQDRRTELVEQVVQSGVTVLLCQKSIDEAVRTALAQRGVLPVERTRRDEFDVIARATGSTPVMSVDDLTADDTGTVG 336
Cdd:pfam00118 233 LKAEEEQILEIVEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMALRRVKKRDLERLAKATGARAVSSLDDLTPDDLGTAG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 337 SVTQRTVGTAQTLVLQGCPEEHRATLLLRGGTPHVAEEVRRIVADCIDVTRVALDDGVFVPGGGAVPTALAMDLAALSRE 416
Cdd:pfam00118 313 KVEEEKIGDEKYTFIEGCKSPKAATILLRGATDHVLDEIERSIHDALCVVKNAIEDPRVVPGGGAVEMELARALREYAKS 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 417 IPDRTQLVFDGFGTALEALPRTLATNAGTDPLTTLTEIKQRHDAGAETVGVG-PDGHPRDMIDAGILEPAAVFRSALQRA 495
Cdd:pfam00118 393 VSGKEQLAIEAFAEALEVIPKTLAENAGLDPIEVLAELRAAHASGEKHAGIDvETGEIIDMKEAGVVDPLKVKRQALKSA 472
|
490
....*....|....*.
gi 499541764 496 VAVVTQILRVDDVVRT 511
Cdd:pfam00118 473 TEAASTILRIDDIIKA 488
|
|
| cpn60 |
cd03343 |
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ... |
20-512 |
9.83e-131 |
|
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: 390.86 E-value: 9.83e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 20 AAGELADAIRTTLGPNGLDKMVVGENGTVIVTNDGSKIIEWMDITHPVGRLVEQAAAAQDNTVGDGTTTAVVLVGALLEE 99
Cdd:cd03343 23 AAKAVAEAVRTTLGPKGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAKTQDEEVGDGTTTAVVLAGELLEK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 100 AATLRSAGLHPTTIIDGYGRAVEAALDQLAQYERGLHSRQDDRLTQIAKTAVTGRWDDASTDRFAELTLSALQAIG---- 175
Cdd:cd03343 103 AEDLLDQNIHPTVIIEGYRLAAEKALELLDEIAIKVDPDDKDTLRKIAKTSLTGKGAEAAKDKLADLVVDAVLQVAekrd 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 176 ----FDRSRLTLKSYPGGELRESVCLDGVLVDLETSstslntlsHPRT-RTHDEPAIAMVDAEIGIEEPNNVESVELQDA 250
Cdd:cd03343 183 gkyvVDLDNIKIEKKTGGSVDDTELIRGIVIDKEVV--------HPGMpKRVENAKIALLDAPLEVKKTEIDAKIRITSP 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 251 TQRNAFQAHEQDRRTELVEQVVQSGVTVLLCQKSIDEAVRTALAQRGVLPVERTRRDEFDVIARATGSTPVMSVDDLTAD 330
Cdd:cd03343 255 DQLQAFLEQEEAMLKEMVDKIADTGANVVFCQKGIDDLAQHYLAKAGILAVRRVKKSDMEKLARATGAKIVTNIDDLTPE 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 331 DTGTVGSVTQRTVGTAQTLVLQGCPEEHRATLLLRGGTPHVAEEVRRIVADCIDVTRVALDDGVFVPGGGAVPTALAMDL 410
Cdd:cd03343 335 DLGEAELVEERKVGDDKMVFVEGCKNPKAVTILLRGGTEHVVDELERALEDALRVVADALEDGKVVAGGGAVEIELAKRL 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 411 AALSREIPDRTQLVFDGFGTALEALPRTLATNAGTDPLTTLTEIKQRHDAGAETVGVGP-DGHPRDMIDAGILEPAAVFR 489
Cdd:cd03343 415 REYARSVGGREQLAVEAFADALEEIPRTLAENAGLDPIDTLVELRAAHEKGNKNAGLDVyTGEVVDMLEKGVIEPLRVKK 494
|
490 500
....*....|....*....|...
gi 499541764 490 SALQRAVAVVTQILRVDDVVRTS 512
Cdd:cd03343 495 QAIKSATEAATMILRIDDVIAAK 517
|
|
| thermosome_alpha |
NF041082 |
thermosome subunit alpha; |
19-509 |
2.64e-126 |
|
thermosome subunit alpha;
Pssm-ID: 469009 Cd Length: 518 Bit Score: 379.23 E-value: 2.64e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 19 TAAGELADAIRTTLGPNGLDKMVVGENGTVIVTNDGSKIIEWMDITHPVGRLVEQAAAAQDNTVGDGTTTAVVLVGALLE 98
Cdd:NF041082 24 MAAKAVAEAVRTTLGPKGMDKMLVDSLGDVVITNDGVTILKEMDIEHPAAKMIVEVAKTQDDEVGDGTTTAVVLAGELLK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 99 EAATLRSAGLHPTTIIDGYGRAVEAALDQLAQYERGLHSRQDDRLTQIAKTAVTGRWDDASTDRFAELTLSALQAI---- 174
Cdd:NF041082 104 KAEELLDQDIHPTIIAEGYRLAAEKALEILDEIAIKVDPDDKETLKKIAATAMTGKGAEAAKDKLADLVVDAVKAVaekd 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 175 ---GFDRSRLTLKSYPGGELRESVCLDGVLVDLETsstslntlSHPRTRTHDEPA-IAMVDAEIGIEEPNNVESVELQDA 250
Cdd:NF041082 184 ggyNVDLDNIKVEKKVGGSIEDSELVEGVVIDKER--------VHPGMPKRVENAkIALLDAPLEVKKTEIDAKISITDP 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 251 TQRNAFQAHEQDRRTELVEQVVQSGVTVLLCQKSIDEAVRTALAQRGVLPVERTRRDEFDVIARATGSTPVMSVDDLTAD 330
Cdd:NF041082 256 DQLQAFLDQEEKMLKEMVDKIADSGANVVFCQKGIDDLAQHYLAKEGILAVRRVKKSDMEKLAKATGARIVTSIDDLSPE 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 331 DTGTVGSVTQRTVGTAQTLVLQGCPEEHRATLLLRGGTPHVAEEVRRIVADCIDVTRVALDDGVFVPGGGAVPTALAMDL 410
Cdd:NF041082 336 DLGYAGLVEERKVGGDKMIFVEGCKNPKAVTILLRGGTEHVVDEVERALEDALRVVRVVLEDGKVVAGGGAPEVELALRL 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 411 AALSREIPDRTQLVFDGFGTALEALPRTLATNAGTDPLTTLTEIKQRHDAGAETVGVGP-DGHPRDMIDAGILEPAAVFR 489
Cdd:NF041082 416 REYAASVGGREQLAIEAFAEALEIIPRTLAENAGLDPIDALVELRSAHEKGNKTAGLDVyTGKVVDMLEIGVVEPLRVKT 495
|
490 500
....*....|....*....|
gi 499541764 490 SALQRAVAVVTQILRVDDVV 509
Cdd:NF041082 496 QAIKSATEAAVMILRIDDVI 515
|
|
| thermosome_beta |
NF041083 |
thermosome subunit beta; |
19-512 |
7.32e-125 |
|
thermosome subunit beta;
Pssm-ID: 469010 Cd Length: 519 Bit Score: 375.83 E-value: 7.32e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 19 TAAGELADAIRTTLGPNGLDKMVVGENGTVIVTNDGSKIIEWMDITHPVGRLVEQAAAAQDNTVGDGTTTAVVLVGALLE 98
Cdd:NF041083 24 MAAKAVAEAVRTTLGPKGMDKMLVDSLGDIVITNDGATILKEMDVQHPAAKMLVEVAKTQDDEVGDGTTTAVVLAGELLK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 99 EAATLRSAGLHPTTIIDGYGRAVEAALDQLAQYERGLHSRQDDRLTQIAKTAVTGRWDDASTDRFAELTLSALQAIG--- 175
Cdd:NF041083 104 KAEELLDQNIHPTIIANGYRLAAEKAIEILDEIAEKVDPDDRETLKKIAETSLTSKGVEEARDYLAEIAVKAVKQVAekr 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 176 -----FDRSRLTLKSYPGGELRESVCLDGVLVDLETSstslntlsHPRTRTHDEPA-IAMVDAEIGIEEPNNVESVELQD 249
Cdd:NF041083 184 dgkyyVDLDNIQIEKKHGGSIEDTQLIYGIVIDKEVV--------HPGMPKRVENAkIALLDAPLEVKKTEIDAEIRITD 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 250 ATQRNAFQAHEQDRRTELVEQVVQSGVTVLLCQKSIDEAVRTALAQRGVLPVERTRRDEFDVIARATGSTPVMSVDDLTA 329
Cdd:NF041083 256 PDQLQKFLDQEEKMLKEMVDKIKATGANVVFCQKGIDDLAQHYLAKAGILAVRRVKKSDMEKLAKATGARIVTNIDDLTP 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 330 DDTGTVGSVTQRTVGTAQTLVLQGCPEEHRATLLLRGGTPHVAEEVRRIVADCIDVTRVALDDGVFVPGGGAVPTALAMD 409
Cdd:NF041083 336 EDLGYAELVEERKVGDDKMVFVEGCKNPKAVTILIRGGTEHVVDEAERALEDALSVVADAVEDGKIVAGGGAPEVELAKR 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 410 LAALSREIPDRTQLVFDGFGTALEALPRTLATNAGTDPLTTLTEIKQRHDAGAETVGVGP-DGHPRDMIDAGILEPAAVF 488
Cdd:NF041083 416 LREYAATVGGREQLAVEAFAEALEIIPRTLAENAGLDPIDILVKLRSAHEKGKKWAGINVfTGEVVDMWELGVIEPLRVK 495
|
490 500
....*....|....*....|....
gi 499541764 489 RSALQRAVAVVTQILRVDDVVRTS 512
Cdd:NF041083 496 TQAIKSATEAATMILRIDDVIAAK 519
|
|
| chaperonin_type_I_II |
cd00309 |
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ... |
20-510 |
4.24e-117 |
|
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: 353.66 E-value: 4.24e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 20 AAGELADAIRTTLGPNGLDKMVVGENGTVIVTNDGSKIIEWMDITHPVGRLVEQAAAAQDNTVGDGTTTAVVLVGALLEE 99
Cdd:cd00309 16 AAKALADAVKTTLGPKGMDKMLVDSLGDPTITNDGATILKEIEVEHPAAKLLVEVAKSQDDEVGDGTTTVVVLAGELLKE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 100 AATLRSAGLHPTTIIDGYGRAVEAALDQLAQYERGLHSRQDDRLTQIAKTAVTGRWDDASTDRFAELTLSALQAIG---- 175
Cdd:cd00309 96 AEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVPIDVEDREELLKVATTSLNSKLVSGGDDFLGELVVDAVLKVGkeng 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 176 -FDRSRLTLKSYPGGELRESVCLDGVLVDLETSStslntlSHPRTRTHDePAIAMVDAEIgieepnnvesvelqdatqrn 254
Cdd:cd00309 176 dVDLGVIRVEKKKGGSLEDSELVVGMVFDKGYLS------PYMPKRLEN-AKILLLDCKL-------------------- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 255 afqaheqdrrtelvEQVVqsgvtvlLCQKSIDEAVRTALAQRGVLPVERTRRDEFDVIARATGSTPVMSVDDLTADDTGT 334
Cdd:cd00309 229 --------------EYVV-------IAEKGIDDEALHYLAKLGIMAVRRVRKEDLERIAKATGATIVSRLEDLTPEDLGT 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 335 VGSVTQRTVGTAQTLVLQGCPEEHRATLLLRGGTPHVAEEVRRIVADCIDVTRVALDDGVFVPGGGAVPTALAMDLAALS 414
Cdd:cd00309 288 AGLVEETKIGDEKYTFIEGCKGGKVATILLRGATEVELDEAERSLHDALCAVRAAVEDGGIVPGGGAAEIELSKALEELA 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 415 REIPDRTQLVFDGFGTALEALPRTLATNAGTDPLTTLTEIKQRHDAGAETVGVGPD-GHPRDMIDAGILEPAAVFRSALQ 493
Cdd:cd00309 368 KTLPGKEQLGIEAFADALEVIPRTLAENAGLDPIEVVTKLRAKHAEGGGNAGGDVEtGEIVDMKEAGIIDPLKVKRQALK 447
|
490
....*....|....*..
gi 499541764 494 RAVAVVTQILRVDDVVR 510
Cdd:cd00309 448 SATEAASLILTIDDIIV 464
|
|
| thermosome_arch |
TIGR02339 |
thermosome, various subunits, archaeal; Thermosome is the name given to the archaeal rather ... |
20-511 |
7.53e-117 |
|
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: 355.15 E-value: 7.53e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 20 AAGELADAIRTTLGPNGLDKMVVGENGTVIVTNDGSKIIEWMDITHPVGRLVEQAAAAQDNTVGDGTTTAVVLVGALLEE 99
Cdd:TIGR02339 24 AAKAVAEAVKSTLGPRGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAKTQDEEVGDGTTTAVVLAGELLEK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 100 AATLRSAGLHPTTIIDGYGRAVEAALDQLAQYERGLHSRQDDRLTQIAKTAVTGRWDDAST-DRFAELTLSALQAIG--- 175
Cdd:TIGR02339 104 AEDLLEQDIHPTVIIEGYRKAAEKALEIIDEIATKISPEDRDLLKKIAYTSLTSKASAEVAkDKLADLVVEAVKQVAelr 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 176 ------FDRSRLTLKSYPGGELRESVCLDGVLVDLETsstslntlSHPRT-RTHDEPAIAMVDAEIGIEEPNNVESVELQ 248
Cdd:TIGR02339 184 gdgkyyVDLDNIKIVKKKGGSIEDTELVEGIVVDKEV--------VHPGMpKRVENAKIALLDAPLEVEKTEIDAKIRIT 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 249 DATQRNAFQAHEQDRRTELVEQVVQSGVTVLLCQKSIDEAVRTALAQRGVLPVERTRRDEFDVIARATGSTPVMSVDDLT 328
Cdd:TIGR02339 256 DPDQIKKFLDQEEAMLKEMVDKIASAGANVVICQKGIDDVAQHYLAKAGILAVRRVKKSDIEKLARATGARIVSSIDEIT 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 329 ADDTGTVGSVTQRTVGTAQTLVLQGCPEEHRATLLLRGGTPHVAEEVRRIVADCIDVTRVALDDGVFVPGGGAVPTALAM 408
Cdd:TIGR02339 336 ESDLGYAELVEERKVGEDKMVFVEGCKNPKAVTILLRGGTEHVVDELERSIQDALHVVANALEDGKIVAGGGAVEIELAL 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 409 DLAALSREIPDRTQLVFDGFGTALEALPRTLATNAGTDPLTTLTEIKQRHDAGAETVGV-GPDGHPRDMIDAGILEPAAV 487
Cdd:TIGR02339 416 RLRSYARSVGGREQLAIEAFADALEEIPRILAENAGLDPIDALVDLRAKHEKGNKNAGInVFTGEIEDMLELGVIEPLRV 495
|
490 500
....*....|....*....|....
gi 499541764 488 FRSALQRAVAVVTQILRVDDVVRT 511
Cdd:TIGR02339 496 KEQAIKSATEAATMILRIDDVIAA 519
|
|
| GroEL |
COG0459 |
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ... |
24-509 |
3.10e-101 |
|
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227 Cd Length: 497 Bit Score: 313.94 E-value: 3.10e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 24 LADAIRTTLGPNGLDKMVVGENGTVIVTNDGSKIIEWMDITHPVG----RLVEQAAAAQDNTVGDGTTTAVVLVGALLEE 99
Cdd:COG0459 22 LADAVKVTLGPKGRNVMLVKSFGDPTITNDGVTIAKEIELEDPFEnmgaQLVKEVASKTNDEAGDGTTTATVLAGALLKE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 100 AATLRSAGLHPTTIIDGYGRAVEAALDQLAQYERGLHSRqdDRLTQIAKTAVTGRwddastDRFAELTLSALQAIGFDrS 179
Cdd:COG0459 102 GLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPVDDK--EELAQVATISANGD------EEIGELIAEAMEKVGKD-G 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 180 RLTLKsYPGGELRESVCLDGVLVDLETSSTSLNTLSHPRTRTHDEPAIAMVDAEIGIEEpnnvesvELQdatqrnafqah 259
Cdd:COG0459 173 VITVE-EGKGLETELEVVEGMQFDKGYLSPYFVTDPEKMPAELENAYILLTDKKISSIQ-------DLL----------- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 260 eqdrrtELVEQVVQSGVTVLLCQKSIDEAVRTALAQRGVLPVERT-----------RRDEFDVIARATGSTPV-----MS 323
Cdd:COG0459 234 ------PLLEKVAQSGKPLLIIAEDIDGEALATLVVNGIRGVLRVvavkapgfgdrRKAMLEDIAILTGGRVIsedlgLK 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 324 VDDLTADDTGTVGSVtqrTVGTAQTLVLQGCPEEHRATLLLRGGTPHVAEEVRRIVADCIDVTRVALDDGVfVPGGGAVP 403
Cdd:COG0459 308 LEDVTLDDLGRAKRV---EVDKDNTTIVEGAGNPKAIVILVGAATEVEVKERKRRVEDALHATRAAVEEGI-VPGGGAAL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 404 TALAMDLAALSREIPDRTQLVFDGFGTALEALPRTLATNAGTDPLTTLTEIKQrhdagAETVGVGPD---GHPRDMIDAG 480
Cdd:COG0459 384 LRAARALRELAAKLEGDEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKVRA-----AKDKGFGFDaatGEYVDMLEAG 458
|
490 500
....*....|....*....|....*....
gi 499541764 481 ILEPAAVFRSALQRAVAVVTQILRVDDVV 509
Cdd:COG0459 459 VIDPAKVKRSALQNAASVAGLILTTEAVI 487
|
|
| TCP1_epsilon |
cd03339 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ... |
19-510 |
4.82e-88 |
|
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: 280.72 E-value: 4.82e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 19 TAAGELADAIRTTLGPNGLDKMVVGENGTVIVTNDGSKIIEWMDITHPVGRLVEQAAAAQDNTVGDGTTTAVVLVGALLE 98
Cdd:cd03339 30 LAAKSVANILRTSLGPRGMDKILVSPDGEVTVTNDGATILEKMDVDHQIAKLLVELSKSQDDEIGDGTTGVVVLAGALLE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 99 EAATLRSAGLHPTTIIDGYGRAVEAALDQLAQY--ERGLHSRQDDRLTQIAKTAVTGRWDDASTDRFAELTLSALQAIGf 176
Cdd:cd03339 110 QAEKLLDRGIHPIRIADGYEQACKIAVEHLEEIadKIEFSPDNKEPLIQTAMTSLGSKIVSRCHRQFAEIAVDAVLSVA- 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 177 DRSR-------LTLKSYPGGELRESVCLDGVLVDLEtsstslntLSHPRTRThdepaiAMVDAEIGI-------EEPNNV 242
Cdd:cd03339 189 DLERkdvnfelIKVEGKVGGRLEDTKLVKGIVIDKD--------FSHPQMPK------EVKDAKIAIltcpfepPKPKTK 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 243 ESVELQDATQRNAFQAHEQDRRTELVEQVVQSGVTVLLCQKSIDEAVRTALAQRGVLPVERTRRDEFDVIARATGSTPVM 322
Cdd:cd03339 255 HKLDITSVEDYKKLQEYEQKYFREMVEQVKDAGANLVICQWGFDDEANHLLLQNGLPAVRWVGGVEIELIAIATGGRIVP 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 323 SVDDLTADDTGTVGSVTQRTVGTAQ--TLVLQGCPEEHRATLLLRGGTPHVAEEVRRIVADCIDVTRVALDDGVFVPGGG 400
Cdd:cd03339 335 RFEDLSPEKLGKAGLVREISFGTTKdkMLVIEGCPNSKAVTIFIRGGNKMIIEEAKRSLHDALCVVRNLIRDNRIVYGGG 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 401 AVPTALAMDLAALSREIPDRTQLVFDGFGTALEALPRTLATNAGTDPLTTLTEIKQRH------DAGAETVGVGPDghpr 474
Cdd:cd03339 415 AAEISCSLAVEKAADKCSGIEQYAMRAFADALESIPLALAENSGLNPIETLSEVKARQvkeknpHLGIDCLGRGTN---- 490
|
490 500 510
....*....|....*....|....*....|....*.
gi 499541764 475 DMIDAGILEPAAVFRSALQRAVAVVTQILRVDDVVR 510
Cdd:cd03339 491 DMKEQKVFETLISKKQQILLATQVVKMILKIDDVIV 526
|
|
| TCP1_delta |
cd03338 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ... |
20-509 |
1.73e-85 |
|
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: 273.78 E-value: 1.73e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 20 AAGELADAIRTTLGPNGLDKMVVGENGTVIVTNDGSKIIEWMDITHPVGRLVEQAAAAQDNTVGDGTTTAVVLVGALLEE 99
Cdd:cd03338 16 AAKAVADAIRTSLGPRGMDKMIQTGKGEVIITNDGATILKQMSVLHPAAKMLVELSKAQDIEAGDGTTSVVVLAGALLSA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 100 AATLRSAGLHPTTIIDGYGRAVEAALDQLAQYERGLHSRQDDRLTQIAKTAVTGRWDDASTDRFAELTLSALQAIG---- 175
Cdd:cd03338 96 CESLLKKGIHPTVISESFQIAAKKAVEILDSMSIPVDLNDRESLIKSATTSLNSKVVSQYSSLLAPIAVDAVLKVIdpat 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 176 ---FDRSRLTLKSYPGGELRESVCLDGVLVDLETSSTSLNTlshprtrTHDEPA-IAMVDAEIGIEEPNNVESVELQDAT 251
Cdd:cd03338 176 atnVDLKDIRIVKKLGGTIEDTELVDGLVFTQKASKKAGGP-------TRIEKAkIGLIQFCLSPPKTDMDNNIVVNDYA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 252 QRNAFQAHEQDRRTELVEQVVQSGVTVLLCQKSI-DEAVRTA----LAQRGVLPVERTRRDEFDVIARATGSTPVMSVDD 326
Cdd:cd03338 249 QMDRILREERKYILNMCKKIKKSGCNVLLIQKSIlRDAVSDLalhfLAKLKIMVVKDIEREEIEFICKTIGCKPVASIDH 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 327 LTADDTGTVGSVTQRTVGTAQTLVLQGCPEE-HRATLLLRGGTPHVAEEVRRIVADCIDVTRVALDDGVFVPGGGAVPTA 405
Cdd:cd03338 329 FTEDKLGSADLVEEVSLGDGKIVKITGVKNPgKTVTILVRGSNKLVLDEAERSLHDALCVIRCLVKKRALIPGGGAPEIE 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 406 LAMDLAALSREIPDRTQLVFDGFGTALEALPRTLATNAGTDPLTTLTEIKQRHDAGAETVGVG-PDGHPRDMIDAGILEP 484
Cdd:cd03338 409 IALQLSEWARTLTGVEQYCVRAFADALEVIPYTLAENAGLNPISIVTELRNRHAQGEKNAGINvRKGAITNILEENVVQP 488
|
490 500
....*....|....*....|....*
gi 499541764 485 AAVFRSALQRAVAVVTQILRVDDVV 509
Cdd:cd03338 489 LLVSTSAITLATETVRMILKIDDIV 513
|
|
| chap_CCT_epsi |
TIGR02343 |
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ... |
20-509 |
1.78e-84 |
|
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: 271.68 E-value: 1.78e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 20 AAGELADAIRTTLGPNGLDKMVVGENGTVIVTNDGSKIIEWMDITHPVGRLVEQAAAAQDNTVGDGTTTAVVLVGALLEE 99
Cdd:TIGR02343 35 AAKSVASILRTSLGPKGMDKMLISPDGDITVTNDGATILSQMDVDNQIAKLMVELSKSQDDEIGDGTTGVVVLAGALLEQ 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 100 AATLRSAGLHPTTIIDGYGRAVEAALDQLAQYERGLHSRQD--DRLTQIAKTAVTGRWDDASTDRFAELTLSALQAIGfD 177
Cdd:TIGR02343 115 AEELLDKGIHPIKIADGFEEAARIAVEHLEEISDEISADNNnrEPLIQAAKTSLGSKIVSKCHRRFAEIAVDAVLNVA-D 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 178 RSR-------LTLKSYPGGELRESVCLDGVLVDLEtsstslntLSHPRTRTHDEPA-IAMVDAEIGIEEPNNVESVELQD 249
Cdd:TIGR02343 194 MERrdvdfdlIKVEGKVGGSLEDTKLIKGIIIDKD--------FSHPQMPKEVEDAkIAILTCPFEPPKPKTKHKLDISS 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 250 ATQRNAFQAHEQDRRTELVEQVVQSGVTVLLCQKSIDEAVRTALAQRGVLPVERTRRDEFDVIARATGSTPVMSVDDLTA 329
Cdd:TIGR02343 266 VEEYKKLQKYEQQKFKEMIDDIKKSGANLVICQWGFDDEANHLLLQNDLPAVRWVGGQELELIAIATGGRIVPRFQELSK 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 330 DDTGTVGSVTQRTVGTA--QTLVLQGCPEEHRATLLLRGGTPHVAEEVRRIVADCIDVTRVALDDGVFVPGGGAVPTALA 407
Cdd:TIGR02343 346 DKLGKAGLVREISFGTTkdRMLVIEQCKNSKAVTIFIRGGNKMIIEEAKRSIHDALCVVRNLIKDSRIVYGGGAAEISCS 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 408 MDLAALSREIPDRTQLVFDGFGTALEALPRTLATNAGTDPLTTLTEIKQRHDA------GAETVGVGPDghprDMIDAGI 481
Cdd:TIGR02343 426 LAVSQEADKYPGVEQYAIRAFADALETIPMALAENSGLDPIGTLSTLKSLQLKeknpnlGVDCLGYGTN----DMKEQFV 501
|
490 500
....*....|....*....|....*...
gi 499541764 482 LEPAAVFRSALQRAVAVVTQILRVDDVV 509
Cdd:TIGR02343 502 FETLIGKKQQILLATQLVRMILKIDDVI 529
|
|
| TCP1_eta |
cd03340 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ... |
25-510 |
2.48e-83 |
|
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: 268.39 E-value: 2.48e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 25 ADAIRTTLGPNGLDKMVVGENGTVIVTNDGSKIIEWMDITHPVGRLVEQAAAAQDNTVGDGTTTAVVLVGALLEEAATLR 104
Cdd:cd03340 29 ADAVRTTLGPRGMDKLIVDGRGKVTISNDGATILKLLDIVHPAAKTLVDIAKSQDAEVGDGTTSVVVLAGEFLKEAKPFI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 105 SAGLHPTTIIDGYGRAVEAALDQLA----QYERGLHSRQDDRLTQIAKTAVTGRWDDASTDRFAELTLSALQAIG--FDR 178
Cdd:cd03340 109 EDGVHPQIIIRGYRKALQLAIEKIKeiavNIDKEDKEEQRELLEKCAATALNSKLIASEKEFFAKMVVDAVLSLDddLDL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 179 SRLTLKSYPGGELRESVCLDGVLVDletsstslNTLSHP----RTRTHDEPAIAMVDAEIGIE-EPNNVEsVELQDATQR 253
Cdd:cd03340 189 DMIGIKKVPGGSLEDSQLVNGVAFK--------KTFSYAgfeqQPKKFKNPKILLLNVELELKaEKDNAE-VRVEDPEEY 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 254 NAFQAHEQDRRTELVEQVVQSGVTVLLCQKSIDEAVRTALAQRGVLPVERTRRDEFDVIARATGSTPVMSVDDLTADDTG 333
Cdd:cd03340 260 QAIVDAEWKIIYDKLEKIVKSGANVVLSKLPIGDLATQYFADRDIFCAGRVPEEDLKRVAQATGGSIQTTVSNITDDVLG 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 334 TVGSVTQRTVGTAQTLVLQGCPEEHRATLLLRGGTPHVAEEVRRIVADCIDVTRVALDDGVFVPGGGAVPTALAMDLAAL 413
Cdd:cd03340 340 TCGLFEERQVGGERYNIFTGCPKAKTCTIILRGGAEQFIEEAERSLHDAIMIVRRAIKNDSVVAGGGAIEMELSKYLRDY 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 414 SREIPDRTQLVFDGFGTALEALPRTLATNAGTDPLTTLTEIKQRHdAGAETVGVGPDGHP---RDMIDAGILEPAAVFRS 490
Cdd:cd03340 420 SRTIAGKQQLVINAFAKALEIIPRQLCDNAGFDATDILNKLRQKH-AQGGGKWYGVDINNegiADNFEAFVWEPSLVKIN 498
|
490 500
....*....|....*....|
gi 499541764 491 ALQRAVAVVTQILRVDDVVR 510
Cdd:cd03340 499 ALTAATEAACLILSVDETIK 518
|
|
| chap_CCT_eta |
TIGR02345 |
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ... |
24-510 |
8.17e-82 |
|
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: 264.70 E-value: 8.17e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 24 LADAIRTTLGPNGLDKMVVGENGTVIVTNDGSKIIEWMDITHPVGRLVEQAAAAQDNTVGDGTTTAVVLVGALLEEAATL 103
Cdd:TIGR02345 30 IAEALKTTLGPRGMDKLIVGSNGKATISNDGATILKLLDIVHPAAKTLVDIAKSQDAEVGDGTTSVTILAGELLKEAKPF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 104 RSAGLHPTTIIDGYGRAVEAALDQLAQYERGLHSRQDDR---LTQIAKTAVTGRWDDASTDRFAELTLSALQAIGFDRSR 180
Cdd:TIGR02345 110 IEEGVHPQLIIRCYREALSLAVEKIKEIAVTIDEEKGEQrelLEKCAATALSSKLISHNKEFFSKMIVDAVLSLDRDDLD 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 181 LTL---KSYPGGELRESVCLDGVLvdLETSSTSLNTLSHPRtRTHDePAIAMVDAEIGIE-EPNNVEsVELQDATQRNAF 256
Cdd:TIGR02345 190 LKLigiKKVQGGALEDSQLVNGVA--FKKTFSYAGFEQQPK-KFAN-PKILLLNVELELKaEKDNAE-IRVEDVEDYQAI 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 257 QAHEQDRRTELVEQVVQSGVTVLLCQKSIDEAVRTALAQRGVLPVERTRRDEFDVIARATGSTPVMSVDDLTADDTGTVG 336
Cdd:TIGR02345 265 VDAEWAIIFRKLEKIVESGANVVLSKLPIGDLATQYFADRDIFCAGRVSAEDLKRVIKACGGSIQSTTSDLEADVLGTCA 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 337 SVTQRTVGTAQTLVLQGCPEEHRATLLLRGGTPHVAEEVRRIVADCIDVTRVALDDGVFVPGGGAVPTALAMDLAALSRE 416
Cdd:TIGR02345 345 LFEERQIGSERYNYFTGCPHAKTCTIILRGGAEQFIEEAERSLHDAIMIVRRALKNKKIVAGGGAIEMELSKCLRDYSKT 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 417 IPDRTQLVFDGFGTALEALPRTLATNAGTDPLTTLTEIKQRHDAGAETVGVGPDG-HPRDMIDAGILEPAAVFRSALQRA 495
Cdd:TIGR02345 425 IDGKQQLIINAFAKALEIIPRQLCENAGFDSIEILNKLRSRHAKGGKWYGVDINTeDIGDNFEAFVWEPALVKINALKAA 504
|
490
....*....|....*
gi 499541764 496 VAVVTQILRVDDVVR 510
Cdd:TIGR02345 505 FEAACTILSVDETIT 519
|
|
| chap_CCT_delta |
TIGR02342 |
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ... |
20-511 |
1.38e-80 |
|
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: 261.26 E-value: 1.38e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 20 AAGELADAIRTTLGPNGLDKMVVGENGTVIVTNDGSKIIEWMDITHPVGRLVEQAAAAQDNTVGDGTTTAVVLVGALLEE 99
Cdd:TIGR02342 17 AAKAVADAIRTSLGPKGMDKMIQDGKGEVIITNDGATILKQMAVLHPAAKMLVELSKAQDIEAGDGTTSVVILAGALLGA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 100 AATLRSAGLHPTTIIDGYGRAVEAALDQLAQYERGLHSRQDDRLTQIAKTAVTGRWDDASTDRFAELTLSAL-------Q 172
Cdd:TIGR02342 97 CERLLNKGIHPTIISESFQSAADEAIKILDEMSIPVDLSDREQLLKSATTSLSSKVVSQYSSLLAPLAVDAVlkvidpeN 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 173 AIGFDRSRLTLKSYPGGELRESVCLDGVLVDLETSSTSlntlSHPrTRTHDePAIAMVDAEIGIEEPNNVESVELQDATQ 252
Cdd:TIGR02342 177 AKNVDLNDIKVVKKLGGTIDDTELIEGLVFTQKASKSA----GGP-TRIEK-AKIGLIQFQISPPKTDMENQIIVNDYAQ 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 253 RNAFQAHEQDRRTELVEQVVQSGVTVLLCQKSI--DEAVRTA---LAQRGVLPVERTRRDEFDVIARATGSTPVMSVDDL 327
Cdd:TIGR02342 251 MDRVLKEERAYILNIVKKIKKTGCNVLLIQKSIlrDAVNDLAlhfLAKMKIMVVKDIEREEIEFICKTIGCKPIASIDHF 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 328 TADDTGTVGSVTQRTVGTAQTLVLQGCPEE-HRATLLLRGGTPHVAEEVRRIVADCIDVTRVALDDGVFVPGGGAVPTAL 406
Cdd:TIGR02342 331 TADKLGSAELVEEVDSDGGKIIKITGIQNAgKTVTVVVRGSNKLVIDEAERSLHDALCVIRCLVKKRGLIAGGGAPEIEI 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 407 AMDLAALSREIPDRTQLVFDGFGTALEALPRTLATNAGTDPLTTLTEIKQRHDAGAETVGVG-PDGHPRDMIDAGILEPA 485
Cdd:TIGR02342 411 ARRLSKYARTMKGVESYCVRAFADALEVIPYTLAENAGLNPIKVVTELRNRHANGEKTAGISvRKGGITNMLEEHVLQPL 490
|
490 500
....*....|....*....|....*.
gi 499541764 486 AVFRSALQRAVAVVTQILRVDDVVRT 511
Cdd:TIGR02342 491 LVTTSAITLASETVRSILKIDDIVFT 516
|
|
| chap_CCT_gamma |
TIGR02344 |
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ... |
19-509 |
1.44e-79 |
|
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: 258.51 E-value: 1.44e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 19 TAAGELADAIRTTLGPNGLDKMVVGENGTVIVTNDGSKIIEWMDITHPVGRLVEQAAAAQDNTVGDGTTTAVVLVGALLE 98
Cdd:TIGR02344 23 QAAKAVADIIRTCLGPRSMLKMLLDPMGGIVMTNDGNAILREIDVAHPAAKSMIELSRTQDEEVGDGTTSVIILAGEMLS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 99 EAATLRSAGLHPTTIIDGYGRAVEAALDQLAQYERGLHSRQDDRLTQIAK----TAVTGRWDDASTDrfaeLTLSALQAI 174
Cdd:TIGR02344 103 VAEPFLEQNIHPTVIIRAYRKALDDALSVLEEISIPVDVNDDAAMLKLIQscigTKFVSRWSDLMCD----LALDAVRTV 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 175 GFD---RSRLTLKSY------PGGELRESVCLDGVLVDLEtsstslntLSHPRTRTHDE-PAIAMVDAEIGIEEPNNVES 244
Cdd:TIGR02344 179 QRDengRKEIDIKRYakvekiPGGDIEDSCVLKGVMINKD--------VTHPKMRRYIEnPRIVLLDCPLEYKKGESQTN 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 245 VELQDATQRNAFQAHEQDRRTELVEQVVQSGVTVLLCQKSIDEAVRTALAQRGVLPVERTRRDEFDVIARATGSTPVMSV 324
Cdd:TIGR02344 251 IEITKEEDWNRILQMEEEYVQLMCEDIIAVKPDLVITEKGVSDLAQHYLLKANITAIRRVRKTDNNRIARACGATIVNRP 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 325 DDLTADDTGT-VGSVTQRTVGTAQTLVLQGCPEEHRATLLLRGGTPHVAEEVRRIVADCIDVTRVALDDGVFVPGGGAVP 403
Cdd:TIGR02344 331 EELRESDVGTgCGLFEVKKIGDEYFTFITECKDPKACTILLRGASKDILNEVERNLQDAMAVARNVLLDPKLVPGGGATE 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 404 TALAMDLAALSREIPDRTQLVFDGFGTALEALPRTLATNAGTDPLTTLTEIKQRHDAGA-ETVGV-GPDGHPRDMIDAGI 481
Cdd:TIGR02344 411 MAVSVALTEKSKKLEGVEQWPYRAVADALEIIPRTLAQNCGANVIRTLTELRAKHAQENnCTWGIdGETGKIVDMKEKGI 490
|
490 500
....*....|....*....|....*...
gi 499541764 482 LEPAAVFRSALQRAVAVVTQILRVDDVV 509
Cdd:TIGR02344 491 WEPLAVKLQTYKTAIESACLLLRIDDIV 518
|
|
| chap_CCT_alpha |
TIGR02340 |
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ... |
1-510 |
3.61e-73 |
|
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: 242.32 E-value: 3.61e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 1 MLGETTDDDSNNEPNPTQTAAgeLADAIRTTLGPNGLDKMVVGENGTVIVTNDGSKIIEWMDITHPVGRLVEQAAAAQDN 80
Cdd:TIGR02340 3 LGGERTSGQDVRTQNVTAAMA--IANIVKTSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 81 TVGDGTTTAVVLVGALLEEAATLRSAGLHPTTIIDGYGRAVEAAL----DQLAQYERGLHSrqdDRLTQIAKTAVTGRWD 156
Cdd:TIGR02340 81 EVGDGTTSVVIIAAELLKRADELVKNKIHPTSVISGYRLACKEAVkyikENLSVSVDELGR---EALINVAKTSMSSKII 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 157 DASTDRFAELTLSALQAIGFDRSRLTLKsYP----------GGELRESVCLDGVLVDletssTSLNTLSHPRTRThdEPA 226
Cdd:TIGR02340 158 GLDSDFFSNIVVDAVLAVKTTNENGETK-YPikainilkahGKSARESMLVKGYALN-----CTVASQQMPKRIK--NAK 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 227 IAMVD-----------AEIGIEEPNNVESVElqdatQRnafqahEQDRRTELVEQVVQSGVTVLLCQKSIDEAVRTALAQ 295
Cdd:TIGR02340 230 IACLDfnlqkakmalgVQIVVDDPEKLEQIR-----QR------EADITKERIKKILDAGANVVLTTGGIDDMCLKYFVE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 296 RGVLPVERTRRDEFDVIARATGSTPVMSVDDLTADDT------GTVGSVTQRTVGTAQTLVLQGCPEEHRATLLLRGGTP 369
Cdd:TIGR02340 299 AGAMGVRRCKKEDLKRIAKATGATLVSTLADLEGEETfeasylGFADEVVQERIADDECILIKGTKKRKSASIILRGAND 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 370 HVAEEVRRIVADCIDVTRVALDDGVFVPGGGAVPTALAMDLAALSREIPDRTQLVFDGFGTALEALPRTLATNAGTDPLT 449
Cdd:TIGR02340 379 FMLDEMERSLHDALCVVKRTLESNSVVPGGGAVEAALSIYLENFATTLGSREQLAIAEFARALLIIPKTLAVNAAKDSTE 458
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 450 TLTEIKQRHDAG------AETVGVGPD---GHPRDMIDAGILEPAAVFRSALQRAVAVVTQILRVDDVVR 510
Cdd:TIGR02340 459 LVAKLRAYHAAAqlkpekKHLKWYGLDlvnGKIRDNKEAGVLEPTVSKVKSLKFATEAAITILRIDDLIK 528
|
|
| TCP1_alpha |
cd03335 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ... |
19-510 |
9.20e-72 |
|
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: 238.34 E-value: 9.20e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 19 TAAGELADAIRTTLGPNGLDKMVVGENGTVIVTNDGSKIIEWMDITHPVGRLVEQAAAAQDNTVGDGTTTAVVLVGALLE 98
Cdd:cd03335 15 TAAMAIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDKEVGDGTTSVVIIAAELLK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 99 EAATLRSAGLHPTTIIDGYGRAVEAAL----DQLAQYERGLHSrqdDRLTQIAKTAVTGRWDDASTDRFAELTLSALQAI 174
Cdd:cd03335 95 RANELVKQKIHPTTIISGYRLACKEAVkyikEHLSISVDNLGK---ESLINVAKTSMSSKIIGADSDFFANMVVDAILAV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 175 GFDRSRLTLKsYP----------GGELRESVCLDGVLVDLETSSTSLNTlshpRTRthdEPAIAMVD-------AEIGIe 237
Cdd:cd03335 172 KTTNEKGKTK-YPikavnilkahGKSAKESYLVNGYALNCTRASQGMPT----RVK---NAKIACLDfnlqktkMKLGV- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 238 epnnveSVELQDATQRNAFQAHEQDRRTELVEQVVQSGVTVLLCQKSIDEAVRTALAQRGVLPVERTRRDEFDVIARATG 317
Cdd:cd03335 243 ------QVVVTDPEKLEKIRQRESDITKERIKKILAAGANVVLTTGGIDDMCLKYFVEAGAMAVRRVKKEDLRRIAKATG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 318 STPVMSVDDLTADDT------GTVGSVTQRTVGTAQTLVLQGCPEEHRATLLLRGGTPHVAEEVRRIVADCIDVTRVALD 391
Cdd:cd03335 317 ATLVSTLANLEGEETfdpsylGEAEEVVQERIGDDELILIKGTKKRSSASIILRGANDFMLDEMERSLHDALCVVKRTLE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 392 DGVFVPGGGAVPTALAMDLAALSREIPDRTQLVFDGFGTALEALPRTLATNAGTDPLTTLTEIKQRHdAGAETVGVGPD- 470
Cdd:cd03335 397 SNSVVPGGGAVETALSIYLENFATTLGSREQLAIAEFAEALLVIPKTLAVNAAKDATELVAKLRAYH-AAAQVKPDKKHl 475
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 499541764 471 ---------GHPRDMIDAGILEPAAVFRSALQRAVAVVTQILRVDDVVR 510
Cdd:cd03335 476 kwygldlinGKVRDNLEAGVLEPTVSKIKSLKFATEAAITILRIDDLIK 524
|
|
| TCP1_gamma |
cd03337 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ... |
19-509 |
4.33e-71 |
|
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: 235.27 E-value: 4.33e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 19 TAAGELADAIRTTLGPNGLDKMVVGENGTVIVTNDGSKIIEWMDITHPVGRLVEQAAAAQDNTVGDGTTTAVVLVGALLE 98
Cdd:cd03337 23 QAAKTVADVIRTCLGPRAMLKMLLDPMGGIVLTNDGNAILREIDVAHPAAKSMIELSRTQDEEVGDGTTSVIILAGEILA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 99 EAATLRSAGLHPTTIIDGYGRAVEAALDQLAQYERGLHSRQDDRLTQIAKTAV----TGRWDDAstdrFAELTLSALQAI 174
Cdd:cd03337 103 VAEPFLERGIHPTVIIKAYRKALEDALKILEEISIPVDVNDRAQMLKIIKSCIgtkfVSRWSDL----MCNLALDAVKTV 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 175 GFD----RSRLTLKSY------PGGELRESVCLDGVLVDLEtsstslntLSHPRTRTHdepaiamvdaeigIEEPNNVes 244
Cdd:cd03337 179 AVEengrKKEIDIKRYakvekiPGGEIEDSRVLDGVMLNKD--------VTHPKMRRR-------------IENPRIV-- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 245 veLQDATqrnafqaheqdrrtelVEQVVqsgvtvlLCQKSIDEAVRTALAQRGVLPVERTRRDEFDVIARATGSTPVMSV 324
Cdd:cd03337 236 --LLDCP----------------LEYLV-------ITEKGVSDLAQHYLVKAGITALRRVRKTDNNRIARACGATIVNRP 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 325 DDLTADDTGTVGSVTQRTVGTAQTLV-LQGCPEEHRATLLLRGGTPHVAEEVRRIVADCIDVTRVALDDGVFVPGGGAVP 403
Cdd:cd03337 291 EELTESDVGTGAGLFEVKKIGDEYFTfITECKDPKACTILLRGASKDVLNEVERNLQDAMAVARNIILNPKLVPGGGATE 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 404 TALAMDLAALSREIPDRTQLVFDGFGTALEALPRTLATNAGTDPLTTLTEIKQRH-DAGAETVGV-GPDGHPRDMIDAGI 481
Cdd:cd03337 371 MAVSHALSEKAKSIEGVEQWPYKAVASALEVIPRTLAQNCGANVIRTLTELRAKHaQGENSTWGIdGETGDIVDMKELGI 450
|
490 500
....*....|....*....|....*...
gi 499541764 482 LEPAAVFRSALQRAVAVVTQILRVDDVV 509
Cdd:cd03337 451 WDPLAVKAQTYKTAIEAACMLLRIDDIV 478
|
|
| chap_CCT_zeta |
TIGR02347 |
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ... |
19-516 |
4.40e-64 |
|
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: 218.06 E-value: 4.40e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 19 TAAGELADAIRTTLGPNGLDKMVVGENGTVIVTNDGSKIIEWMDITHPVGRLVEQAAAAQDNTVGDGTTTAVVLVGALLE 98
Cdd:TIGR02347 23 NAARGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEMQIQHPTASMIARAATAQDDITGDGTTSTVLLIGELLK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 99 EAATLRSAGLHPTTIIDGYGRAVEAALDQLAQYERGLHSRQD-DRLTQIAKTAVTGRWDDASTDRFAELTLSALQAIGFD 177
Cdd:TIGR02347 103 QAERYILEGVHPRIITEGFEIARKEALQFLDKFKVKKEDEVDrEFLLNVARTSLRTKLPADLADQLTEIVVDAVLAIKKD 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 178 RSRLTLKSYPGGELRESVCLDGVLVD---LETSStslntlSHPRTRTHDEPAIAM---VDAEIGIEEPNNveSVELQDAT 251
Cdd:TIGR02347 183 GEDIDLFMVEIMEMKHKSATDTTLIRglvLDHGA------RHPDMPRRVKNAYILtcnVSLEYEKTEVNS--GFFYSSAE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 252 QRNAFQAHEQ---DRRT----ELVEQVVQSGVT---VLLCQKSIDEAVRTALAQRGVLPVERTRRDEFDVIARATGSTPV 321
Cdd:TIGR02347 255 QREKLVKAERkfvDDRVkkiiELKKKVCGKSPDkgfVVINQKGIDPPSLDLLAKEGIMALRRAKRRNMERLTLACGGEAL 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 322 MSVDDLTADDTGTVGSVTQRTVGTAQTLVLQGCPEEHRATLLLRGGTPHVAEEVRRIVADCIDVTRVALDDGVFVPGGGA 401
Cdd:TIGR02347 335 NSVEDLTPECLGWAGLVYETTIGEEKYTFIEECKNPKSCTILIKGPNDHTIAQIKDAVRDGLRAVKNAIEDKCVVPGAGA 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 402 VPTALAMDLAALSREIPDRTQLVFDGFGTALEALPRTLATNAGTDPLTTLTEIKQRHDAGAETVGVGPD-GHPRDMIDAG 480
Cdd:TIGR02347 415 FEIAAYRHLKEYKKSVKGKAKLGVEAFANALLVIPKTLAENSGFDAQDTLVKLEDEHDEGGEVVGVDLNtGEPIDPEIKG 494
|
490 500 510
....*....|....*....|....*....|....*.
gi 499541764 481 ILEPAAVFRSALQRAVAVVTQILRVDDVVRTSTNER 516
Cdd:TIGR02347 495 IWDNYRVKKQLIQSATVIASQLLLVDEVMRAGRSML 530
|
|
| TCP1_theta |
cd03341 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ... |
20-509 |
6.64e-64 |
|
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: 215.93 E-value: 6.64e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 20 AAGELADAIRTTLGPNGLDKMVVGENGTVIVTNDGSKIIEWMDITHPVGRLVEQAAAAQDNTVGDGTTTAVVLVGALLEE 99
Cdd:cd03341 16 ACKELSQITRTSYGPNGMNKMVINHLEKLFVTSDAATILRELEVQHPAAKLLVMASQMQEEEIGDGTNLVVVLAGELLEK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 100 AATLRSAGLHPTTIIDGYGRAVEAA---LDQLAQYE-RGLHSRQDdrLTQIAKTAVTGRWDDAStDRFAELTLSALQAI- 174
Cdd:cd03341 96 AEELLRMGLHPSEIIEGYEKALKKAleiLEELVVYKiEDLRNKEE--VSKALKTAIASKQYGNE-DFLSPLVAEACISVl 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 175 -----GFDRSRLTLKSYPGGELRESVCLDGVLVDLETSSTSLNtlshprtrthdepaiaMVDAEIGIeepnnvesvelqd 249
Cdd:cd03341 173 penigNFNVDNIRVVKILGGSLEDSKVVRGMVFKREPEGSVKR----------------VKKAKVAV------------- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 250 atqrnafqaheqdrrtelVEQVVQSGVTVLLCQKSIDEAVRTALAQRGVLPVERTRRDEFDVIARATGSTPVMSVDDLTA 329
Cdd:cd03341 224 ------------------FSCPFDIGVNVIVAGGSVGDLALHYCNKYGIMVIKINSKFELRRLCRTVGATPLPRLGAPTP 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 330 DDTGTVGSVTQRTVGTAQTLVLQGCPEEHR-ATLLLRGGTPHVAEEVRRIVADCIDVTRVALDDGVFVPGGGAVPTALAM 408
Cdd:cd03341 286 EEIGYCDSVYVEEIGDTKVVVFRQNKEDSKiATIVLRGATQNILDDVERAIDDGVNVFKSLTKDGRFVPGAGATEIELAK 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 409 DLAALSREIPDRTQLVFDGFGTALEALPRTLATNAGTDPLTTLTEIKQRHDAGAETVGVGPDGH---PRDMIDAGILEPA 485
Cdd:cd03341 366 KLKEYGEKTPGLEQYAIKKFAEAFEVVPRTLAENAGLDATEVLSELYAAHQKGNKSAGVDIESGdegTKDAKEAGIFDHL 445
|
490 500
....*....|....*....|....
gi 499541764 486 AVFRSALQRAVAVVTQILRVDDVV 509
Cdd:cd03341 446 ATKKWAIKLATEAAVTVLRVDQII 469
|
|
| TCP1_zeta |
cd03342 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
19-510 |
1.16e-61 |
|
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: 210.19 E-value: 1.16e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 19 TAAGELADAIRTTLGPNGLDKMVVGENGTVIVTNDGSKIIEWMDITHPVGRLVEQAAAAQDNTVGDGTTTAVVLVGALLE 98
Cdd:cd03342 19 SAAKGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLSEMQIQHPTASMIARAATAQDDITGDGTTSNVLLIGELLK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 99 EAATLRSAGLHPTTIIDGYGRAVEAALDQLAQYERGLHSRQD-DRLTQIAKTAVTGRWDDASTDRFAELTLSALQAIgfd 177
Cdd:cd03342 99 QAERYIQEGVHPRIITEGFELAKNKALKFLESFKVPVEIDTDrELLLSVARTSLRTKLHADLADQLTEIVVDAVLAI--- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 178 rsrltlksYPGGELresvcLDGVLVDLET--SSTSLNT-------LSHPrTRTHDEPAIaMVDAEIGIeepNNVeSVELQ 248
Cdd:cd03342 176 --------YKPDEP-----IDLHMVEIMQmqHKSDSDTklirglvLDHG-ARHPDMPKR-VENAYILT---CNV-SLEYE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 249 datqrnafqaheqdrRTElveqvVQSGV--TVLLCQKSIDEAVRTALAQRGVLPVERTRRDEFDVIARATGSTPVMSVDD 326
Cdd:cd03342 237 ---------------KTE-----VNSGFfySVVINQKGIDPPSLDMLAKEGILALRRAKRRNMERLTLACGGVAMNSVDD 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 327 LTADDTGTVGSVTQRTVGTAQTLVLQGCPEEHRATLLLRGGTPHVAEEVRRIVADCIDVTRVALDDGVFVPGGGAVPTAL 406
Cdd:cd03342 297 LSPECLGYAGLVYERTLGEEKYTFIEGVKNPKSCTILIKGPNDHTITQIKDAIRDGLRAVKNAIEDKCVVPGAGAFEVAL 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 407 AMDLAALSREIPDRTQLVFDGFGTALEALPRTLATNAGTDPLTTLTEIKQRHDAGAETVGVGPD-GHPRDMIDAGILEPA 485
Cdd:cd03342 377 YAHLKEFKKSVKGKAKLGVQAFADALLVIPKTLAENSGLDVQETLVKLQDEYAEGGQVGGVDLDtGEPMDPESEGIWDNY 456
|
490 500
....*....|....*....|....*
gi 499541764 486 AVFRSALQRAVAVVTQILRVDDVVR 510
Cdd:cd03342 457 SVKRQILHSATVIASQLLLVDEIIR 481
|
|
| chap_CCT_theta |
TIGR02346 |
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ... |
20-509 |
4.80e-60 |
|
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: 207.26 E-value: 4.80e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 20 AAGELADAIRTTLGPNGLDKMVVGENGTVIVTNDGSKIIEWMDITHPVGRLVEQAAAAQDNTVGDGTTTAVVLVGALLEE 99
Cdd:TIGR02346 26 ACKELSQITRTSLGPNGMNKMVINHLEKLFVTNDAATILRELEVQHPAAKLLVMASEMQENEIGDGTNLVLVLAGELLNK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 100 AATLRSAGLHPTTIIDGYGRAVEAA---LDQLAQYErGLHSRQDDRLTQIAKTAVTGRwDDASTDRFAELTLSALQAI-- 174
Cdd:TIGR02346 106 AEELIRMGLHPSEIIKGYEMALKKAmeiLEELVVWE-VKDLRDKDELIKALKASISSK-QYGNEDFLAQLVAQACSTVlp 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 175 ----GFDRSRLTLKSYPGGELRESVCLDGVLV--DLETSSTSLntlshprtrthDEPAIAMVDAEIGIEEPNNVESVELQ 248
Cdd:TIGR02346 184 knpqNFNVDNIRVCKILGGSLSNSEVLKGMVFnrEAEGSVKSV-----------KNAKVAVFSCPLDTATTETKGTVLIH 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 249 DATQRNAFQAHEQDRRTELVEQVVQSGVTVLLCQKSIDEAVRTALAQRGVLPVERTRRDEFDVIARATGSTPVMSVDDLT 328
Cdd:TIGR02346 253 NAEELLNYSKGEENQIEAMIKAIADSGVNVIVTGGSVGDMALHYLNKYNIMVLKIPSKFELRRLCKTVGATPLPRLGAPT 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 329 ADDTGTVGSVTQRTVGTAQTLVLQGCPEEHR-ATLLLRGGTPHVAEEVRRIVADCIDVTRVALDDGVFVPGGGAVPTALA 407
Cdd:TIGR02346 333 PEEIGYVDSVYVSEIGGDKVTVFKQENGDSKiSTIILRGSTDNLLDDIERAIDDGVNTVKALVKDGRLLPGAGATEIELA 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 408 MDLAALSREIPDRTQLVFDGFGTALEALPRTLATNAGTDPLTTLTEIKQRHDAGAETVGVGPDG---HPRDMIDAGILEP 484
Cdd:TIGR02346 413 SRLTKYGEKLPGLDQYAIKKFAEAFEIIPRTLAENAGLNANEVIPKLYAAHKKGNKSKGIDIEAesdGVKDASEAGIYDM 492
|
490 500
....*....|....*....|....*
gi 499541764 485 AAVFRSALQRAVAVVTQILRVDDVV 509
Cdd:TIGR02346 493 LATKKWAIKLATEAAVTVLRVDQII 517
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
24-517 |
2.64e-59 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 205.26 E-value: 2.64e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 24 LADAIRTTLGPNGLDKMVVG-----ENGTVIVTNDGSKIIEWMDITHPVGRLVEQAAAAQDNTVGDGTTTAVVLVGALLE 98
Cdd:PTZ00212 34 VADLVKTTLGPKGMDKILQPmsegpRSGNVTVTNDGATILKSVWLDNPAAKILVDISKTQDEEVGDGTTSVVVLAGELLR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 99 EAATLRSAGLHPTTIIDGYGRAVEAALDQL--AQYERGLHSRQ-DDRLTQIAKTAVTGRWDDASTDRFAELTLSALQAIG 175
Cdd:PTZ00212 114 EAEKLLDQKIHPQTIIEGWRMALDVARKALeeIAFDHGSDEEKfKEDLLNIARTTLSSKLLTVEKDHFAKLAVDAVLRLK 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 176 fDRSRL----TLKSyPGGELRESVCLDGVLVDLETsstslnTLSHPRTRTHDEPAIA---MVDAEIGIEEPN-NVESVEl 247
Cdd:PTZ00212 194 -GSGNLdyiqIIKK-PGGTLRDSYLEDGFILEKKI------GVGQPKRLENCKILVAntpMDTDKIKIYGAKvKVDSME- 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 248 qdatQRNAFQAHEQDRRTELVEQVVQSGVTVLLCQKSIDEAVRTALAQRGVLPVERTRRDEFDVIARATGSTPVMSVDDL 327
Cdd:PTZ00212 265 ----KVAEIEAAEKEKMKNKVDKILAHGCNVFINRQLIYNYPEQLFAEAGIMAIEHADFDGMERLAAALGAEIVSTFDTP 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 328 TADDTGTVGSVTQRTVGTAQTLVLQGCPEEHRATLLLRGGTPHVAEEVRRIVADCIDVTRVALDDGVFVPGGGAVPTALA 407
Cdd:PTZ00212 341 EKVKLGHCDLIEEIMIGEDKLIRFSGCAKGEACTIVLRGASTHILDEAERSLHDALCVLSQTVKDTRVVLGGGCSEMLMA 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 408 MDLAALSREIPDRTQLVFDGFGTALEALPRTLATNAGTDPLTTLTEIKQRHDAGAETVGVG-PDGHPRDMIDAGILEPAA 486
Cdd:PTZ00212 421 NAVEELAKKVEGKKSLAIEAFAKALRQIPTIIADNGGYDSAELVSKLRAEHYKGNKTAGIDmEKGTVGDMKELGITESYK 500
|
490 500 510
....*....|....*....|....*....|.
gi 499541764 487 VFRSALQRAVAVVTQILRVDDVVRTSTNERT 517
Cdd:PTZ00212 501 VKLSQLCSATEAAEMILRVDDIIRCAPRQRE 531
|
|
| TCP1_beta |
cd03336 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ... |
24-510 |
2.69e-55 |
|
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: 194.09 E-value: 2.69e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 24 LADAIRTTLGPNGLDKMV--VGENGTVIVTNDGSKIIEWMDITHPVGRLVEQAAAAQDNTVGDGTTTAVVLVGALLEEAA 101
Cdd:cd03336 25 IGDLVKTTLGPKGMDKILqsVGRSGGVTVTNDGATILKSIGVDNPAAKVLVDISKVQDDEVGDGTTSVTVLAAELLREAE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 102 TLRSAGLHPTTIIDGYGRAVEAALDQL---AQYERGLHSRQDDRLTQIAKTAVTGRWDDASTDRFAELtlsALQAIGFDR 178
Cdd:cd03336 105 KLVAQKIHPQTIIEGYRMATAAAREALlssAVDHSSDEEAFREDLLNIARTTLSSKILTQDKEHFAEL---AVDAVLRLK 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 179 SRLTLKSY-----PGGELRESVCLDGVLVDLETSSTSLNTLSHPR----TRTHDEPAIAMVDAEIgieepnNVESV---- 245
Cdd:cd03336 182 GSGNLDAIqiikkLGGSLKDSYLDEGFLLDKKIGVNQPKRIENAKiliaNTPMDTDKIKIFGAKV------RVDSTakva 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 246 ELQDAtqrnafqahEQDRRTELVEQVVQSGVTVLLCQKSIDEAVRTALAQRGVLPVERTRRDEFDVIARATGSTPVMSVD 325
Cdd:cd03336 256 EIEEA---------EKEKMKNKVEKILKHGINCFINRQLIYNYPEQLFADAGIMAIEHADFDGVERLALVTGGEIASTFD 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 326 DLTADDTGTVGSVTQRTVGTAQTLVLQGCPEEHRATLLLRGGTPHVAEEVRRIVADCIDVTRVALDDGVFVPGGGAVPTA 405
Cdd:cd03336 327 HPELVKLGTCKLIEEIMIGEDKLIRFSGVAAGEACTIVLRGASQQILDEAERSLHDALCVLAQTVKDTRVVLGGGCSEML 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 406 LAMDLAALSREIPDRTQLVFDGFGTALEALPRTLATNAGTDPLTTLTEIKQRHDAGAETVGVG-PDGHPRDMIDAGILEP 484
Cdd:cd03336 407 MAKAVEELAKKTPGKKSLAIEAFAKALRQLPTIIADNAGYDSAELVAQLRAAHYNGNTTAGLDmRKGTVGDMKELGITES 486
|
490 500
....*....|....*....|....*.
gi 499541764 485 AAVFRSALQRAVAVVTQILRVDDVVR 510
Cdd:cd03336 487 FKVKRQVLLSASEAAEMILRVDDIIK 512
|
|
| chap_CCT_beta |
TIGR02341 |
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ... |
24-516 |
1.63e-41 |
|
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: 156.17 E-value: 1.63e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 24 LADAIRTTLGPNGLDKMVV--GENGTVIVTNDGSKIIEWMDITHPVGRLVEQAAAAQDNTVGDGTTTAVVLVGALLEEAA 101
Cdd:TIGR02341 26 IGDLVKSTLGPKGMDKILQssSSDASIMVTNDGATILKSIGVDNPAAKVLVDMSKVQDDEVGDGTTSVTVLAAELLREAE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 102 TLRSAGLHPTTIIDGYGRAVEAALDQL--AQYERG---LHSRQDdrLTQIAKTAVTGRWDDASTDRFAELTLSA---LQA 173
Cdd:TIGR02341 106 KLINQKIHPQTIIAGYREATKAARDALlkSAVDNGsdeVKFRQD--LMNIARTTLSSKILSQHKDHFAQLAVDAvlrLKG 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 174 IGfDRSRLTLKSYPGGELRESVCLDGVLVDletsstslNTLSHPRTRTHDEPAIAMVDAEIGIEEPNNVESVELQDATQR 253
Cdd:TIGR02341 184 SG-NLEAIQIIKKLGGSLADSYLDEGFLLD--------KKIGVNQPKRIENAKILIANTGMDTDKVKIFGSRVRVDSTAK 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 254 NA-FQAHEQDRRTELVEQVVQSGVTVLLCQKSIDEAVRTALAQRGVLPVERTRRDEFDVIARATGSTPVMSVDDLTADDT 332
Cdd:TIGR02341 255 VAeLEHAEKEKMKEKVEKILKHGINCFINRQLIYNYPEQLFADAGVMAIEHADFEGVERLALVTGGEIVSTFDHPELVKL 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 333 GTVGSVTQRTVGTAQTLVLQGCPEEHRATLLLRGGTPHVAEEVRRIVADCIDVTRVALDDGVFVPGGGAVPTALAMDLAA 412
Cdd:TIGR02341 335 GSCDLIEEIMIGEDKLLKFSGVKLGEACTIVLRGATQQILDEAERSLHDALCVLSQTVKESRTVLGGGCSEMLMSKAVTQ 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 413 LSREIPDRTQLVFDGFGTALEALPRTLATNAGTDPLTTLTEIKQRHDAGAETVGVGPD-GHPRDMIDAGILEPAAVFRSA 491
Cdd:TIGR02341 415 EAQRTPGKEALAVEAFARALRQLPTIIADNAGFDSAELVAQLRAAHYNGNTTMGLDMNeGTIADMRQLGITESYKVKRAV 494
|
490 500
....*....|....*....|....*
gi 499541764 492 LQRAVAVVTQILRVDDVVRTSTNER 516
Cdd:TIGR02341 495 VSSAAEAAEVILRVDNIIKAAPRKR 519
|
|
| chaperonin_like |
cd03333 |
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ... |
143-392 |
7.53e-28 |
|
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: 110.63 E-value: 7.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 143 LTQIAKTAVT---GRWDDastdRFAELTLSALQAIG-----FDRSRLTLKSYPGGELRESVCLDGVLVDletsstslNTL 214
Cdd:cd03333 4 LLQVATTSLNsklSSWDD----FLGKLVVDAVLKVGpdnrmDDLGVIKVEKIPGGSLEDSELVVGVVFD--------KGY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 215 SHPRTRTHDE-PAIAMVDAEIGieepnnvesvelqdatqrnafqaheqdrrtelveqvvqsgvTVLLCQKSIDEAVRTAL 293
Cdd:cd03333 72 ASPYMPKRLEnAKILLLDCPLE-----------------------------------------YVVIAEKGIDDLALHYL 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 294 AQRGVLPVERTRRDEFDVIARATGSTPVMSVDDLTADDTGTVGSVTQRTVGTAQTLVLQGCPEEHRATLLLRGGTPHVAE 373
Cdd:cd03333 111 AKAGIMAVRRVKKEDLERIARATGATIVSSLEDLTPEDLGTAELVEETKIGEEKLTFIEGCKGGKAATILLRGATEVELD 190
|
250
....*....|....*....
gi 499541764 374 EVRRIVADCIDVTRVALDD 392
Cdd:cd03333 191 EVKRSLHDALCAVRAAVEE 209
|
|
| GroEL |
cd03344 |
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ... |
24-498 |
3.84e-24 |
|
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: 106.00 E-value: 3.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 24 LADAIRTTLGPNG----LDKMVvgenGTVIVTNDG---SKIIEWMDITHPVG-RLVEQAAAAQDNTVGDGTTTAVVLVGA 95
Cdd:cd03344 20 LADAVKVTLGPKGrnvvIEKSF----GSPKITKDGvtvAKEIELEDPFENMGaQLVKEVASKTNDVAGDGTTTATVLARA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 96 LLEEAATLRSAGLHPTTIIDGYGRAVEAALDQLAQYERGLHSRQDdrLTQIAKTAvtgrwddASTDRF-AELTLSALQAI 174
Cdd:cd03344 96 IIKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKPVKTKEE--IAQVATIS-------ANGDEEiGELIAEAMEKV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 175 GFdrsrltlksypggelresvclDGVlVDLETSSTslntlshprtrTHDEpaiamVDAEIGIEEP---------NNVES- 244
Cdd:cd03344 167 GK---------------------DGV-ITVEEGKT-----------LETE-----LEVVEGMQFDrgylspyfvTDPEKm 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 245 -VELQDA----TQR--NAFQaheqdrrtELV---EQVVQSGVTVLLCQKSIDEAVRTALA---QRGVLPV---------E 302
Cdd:cd03344 209 eVELENPyillTDKkiSSIQ--------ELLpilELVAKAGRPLLIIAEDVEGEALATLVvnkLRGGLKVcavkapgfgD 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 303 RtRRDEFDVIARATGSTPV-----MSVDDLTADDTGTVGSVtqrTVGTAQTLVLQG--------------------CPEE 357
Cdd:cd03344 281 R-RKAMLEDIAILTGGTVIseelgLKLEDVTLEDLGRAKKV---VVTKDDTTIIGGagdkaaikariaqirkqieeTTSD 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 358 HRATLL------LRGGTP--HV--AEEVR------RIVaDCIDVTRVALDDGVfVPGGGavpTAL---AMDLAALSREIP 418
Cdd:cd03344 357 YDKEKLqerlakLSGGVAviKVggATEVElkekkdRVE-DALNATRAAVEEGI-VPGGG---VALlraSPALDKLKALNG 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 419 DRT---QLVFDgfgtALEALPRTLATNAGTDPLTTLTEIKQRHDagaetvGVGPD---GHPRDMIDAGILEPAAVFRSAL 492
Cdd:cd03344 432 DEKlgiEIVRR----ALEAPLRQIAENAGVDGSVVVEKVLESPD------GFGYDaatGEYVDMIEAGIIDPTKVVRSAL 501
|
....*.
gi 499541764 493 QRAVAV 498
Cdd:cd03344 502 QNAASV 507
|
|
| groEL |
PRK12849 |
chaperonin GroEL; Reviewed |
24-503 |
3.10e-22 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237230 Cd Length: 542 Bit Score: 100.27 E-value: 3.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 24 LADAIRTTLGPNGLDKMVVGENGTVIVTNDGSKI---IEWMDITHPVG-RLVEQAAAAQDNTVGDGTTTAVVLVGALLEE 99
Cdd:PRK12849 22 LADAVKVTLGPKGRNVVIDKSFGAPTITKDGVSIakeIELEDPFENLGaQLVKEVASKTNDVAGDGTTTATVLAQALVQE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 100 AATLRSAGLHPTTIIDGYGRAVEAALDQLAQYERGLHSRQDdrLTQIAktAVTGRWDDASTDRFAEltlsALQAIGfdrs 179
Cdd:PRK12849 102 GLKNVAAGANPMDLKRGIDKAVEAVVEELKALARPVSGSEE--IAQVA--TISANGDEEIGELIAE----AMEKVG---- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 180 rltlksypggelresvcLDGVlVDLETSSTSLNTLS------------------HPRTRT--HDEPAIAMVDAEIgieep 239
Cdd:PRK12849 170 -----------------KDGV-ITVEESKTLETELEvtegmqfdrgylspyfvtDPERMEavLEDPLILLTDKKI----- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 240 nnvesVELQDATQrnafqaheqdrrteLVEQVVQSGVTVLLCQKSID-EAVRTALAQ--RGVLPVE-------RTRRDEF 309
Cdd:PRK12849 227 -----SSLQDLLP--------------LLEKVAQSGKPLLIIAEDVEgEALATLVVNklRGGLKVAavkapgfGDRRKAM 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 310 -DVIARATGSTPV-----MSVDDLTADDTGTVGSVtqrTVGTAQTLVLQGC--PE--EHRATLL---------------- 363
Cdd:PRK12849 288 lEDIAILTGGTVIsedlgLKLEEVTLDDLGRAKRV---TITKDNTTIVDGAgdKEaiEARVAQIrrqieettsdydrekl 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 364 ------LRGGTPHV----AEEV---RRI--VADCIDVTRVALDDGVfVPGGGAVPTALAMDLAALSREIPDRTQLVfDGF 428
Cdd:PRK12849 365 qerlakLAGGVAVIkvgaATEVelkERKdrVEDALNATRAAVEEGI-VPGGGVALLRAAKALDELAGLNGDQAAGV-EIV 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 429 GTALEALPRTLATNAGTDPlttlteikqrhDAGAETVGVGPDGHP--------RDMIDAGILEPAAVFRSALQRAVAVVT 500
Cdd:PRK12849 443 RRALEAPLRQIAENAGLDG-----------SVVVAKVLELEDGFGfnaatgeyGDLIAAGIIDPVKVTRSALQNAASVAG 511
|
...
gi 499541764 501 QIL 503
Cdd:PRK12849 512 LLL 514
|
|
| groEL |
PRK12850 |
chaperonin GroEL; Reviewed |
24-509 |
2.44e-20 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237231 Cd Length: 544 Bit Score: 94.40 E-value: 2.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 24 LADAIRTTLGPNGLDKMVVGENGTVIVTNDG---SKIIEWMDITHPVG-RLVEQAAAAQDNTVGDGTTTAVVLVGALLEE 99
Cdd:PRK12850 23 LANAVKVTLGPKGRNVVLEKSFGAPRITKDGvtvAKEIELEDKFENMGaQMVKEVASKTNDLAGDGTTTATVLAQAIVRE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 100 AATLRSAGLHPTTIIDGYGRAVEAALDQLAQYERGLHSRQDdrLTQIAKTAVTGrwDDASTDRFAEltlsALQAIGFDrS 179
Cdd:PRK12850 103 GAKLVAAGMNPMDLKRGIDLAVAAVVDELKKIAKKVTSSKE--IAQVATISANG--DESIGEMIAE----AMDKVGKE-G 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 180 RLTLKSYPGGELRESVcLDGVLVDLETSSTSLNTLSHPRTRTHDEPAIAMVDAEIGieepnnvesvELQDAtqrnafqah 259
Cdd:PRK12850 174 VITVEEAKTLGTELDV-VEGMQFDRGYLSPYFVTNPEKMRAELEDPYILLHEKKIS----------NLQDL--------- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 260 eqdrrTELVEQVVQSGVTVLLCQKSID-EAVRTALAQ--RGVLPV---------ERtRRDEFDVIARATGSTPVmsvddl 327
Cdd:PRK12850 234 -----LPILEAVVQSGRPLLIIAEDVEgEALATLVVNklRGGLKSvavkapgfgDR-RKAMLEDIAVLTGGQVI------ 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 328 tADDTG-TVGSVTQRTVGTAQTLV-----------------LQGCPEEHRA------------TLLLR------------ 365
Cdd:PRK12850 302 -SEDLGiKLENVTLDMLGRAKRVLitkenttiidgagdkknIEARVKQIRAqieettsdydreKLQERlaklaggvavir 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 366 --GGTPHVAEEVRRIVADCIDVTRVALDDGVfVPGGGavpTALAMD---LAALSREIPDRTQLVfDGFGTALEALPRTLA 440
Cdd:PRK12850 381 vgGATEVEVKEKKDRVDDALHATRAAVEEGI-VPGGG---VALLRArsaLRGLKGANADETAGI-DIVRRALEEPLRQIA 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 441 TNAGTDplttlteikqrhdaGAETVGV---GPDGHP--------RDMIDAGILEPAAVFRSALQRAVAVVTQILRVDDVV 509
Cdd:PRK12850 456 TNAGFE--------------GSVVVGKvaeLPGNFGfnaqtgeyGDMVEAGIIDPAKVTRTALQDAASIAALLITTEAMV 521
|
|
| groEL |
PRK12851 |
chaperonin GroEL; Reviewed |
24-509 |
3.00e-20 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 171770 Cd Length: 541 Bit Score: 94.04 E-value: 3.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 24 LADAIRTTLGPNGLDKMVVGENGTVIVTNDG---SKIIEWMDITHPVG-RLVEQAAAAQDNTVGDGTTTAVVLVGALLEE 99
Cdd:PRK12851 23 LADAVKVTLGPKGRNVVIDKSFGAPTITNDGvtiAKEIELEDKFENMGaQMVREVASKTNDVAGDGTTTATVLAQAIVRE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 100 AATLRSAGLHPTTIIDGYGRAVEAALDQLAQYERGLHSRQDdrltqIAKTAVTGRWDDAstdRFAELTLSALQAIGFDrS 179
Cdd:PRK12851 103 GAKAVAAGANPMDLKRGIDRAVAAVVEELKANARPVTTNAE-----IAQVATISANGDA---EIGRLVAEAMEKVGNE-G 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 180 RLTLKSYPGGELRESVcLDGVLVDLETSSTSLNTLSHPRTRTHDEPAIAMVDAEIGieepnnvesvELQDAtqrnafqah 259
Cdd:PRK12851 174 VITVEESKTAETELEV-VEGMQFDRGYLSPYFVTDADKMEAELEDPYILIHEKKIS----------NLQDL--------- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 260 eqdrrTELVEQVVQSGVTVLLCQKSID-EAVRTALAQ--RGVLPVERT--------RRDEFDVIARATGSTPV-----MS 323
Cdd:PRK12851 234 -----LPVLEAVVQSGKPLLIIAEDVEgEALATLVVNklRGGLKVAAVkapgfgdrRKAMLEDIAILTGGTVIsedlgIK 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 324 VDDLTADDTGTVGSVtqrTVGTAQTLVLQGCP----------------------------EEHRATL-----LLRGGTPH 370
Cdd:PRK12851 309 LENVTLEQLGRAKKV---VVEKENTTIIDGAGskteiegrvaqiraqieettsdydreklQERLAKLaggvaVIRVGAST 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 371 VAE--EVRRIVADCIDVTRVALDDGVfVPGGG-----AVPTALAMDLA----ALSREIPDRtqlvfdgfgtALEALPRTL 439
Cdd:PRK12851 386 EVEvkEKKDRVDDALHATRAAVEEGI-VPGGGvallrAVKALDKLETAngdqRTGVEIVRR----------ALEAPVRQI 454
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499541764 440 ATNAGTDP---LTTLTEIKQRHDAGAETVGVGpdghprDMIDAGILEPAAVFRSALQRAVAVVTQILRVDDVV 509
Cdd:PRK12851 455 AENAGAEGsvvVGKLREKPGGYGFNAATNEYG------DLYAQGVIDPVKVVRTALQNAASVAGLLLTTEAMV 521
|
|
| GroEL |
TIGR02348 |
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ... |
24-509 |
7.52e-20 |
|
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: 92.74 E-value: 7.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 24 LADAIRTTLGPNGldKMVVGEN--GTVIVTNDGSKI---IEWMDITHPVG-RLVEQAAAAQDNTVGDGTTTAVVLVGALL 97
Cdd:TIGR02348 21 LADAVKVTLGPKG--RNVVLEKsfGAPTITKDGVTVakeIELEDKFENMGaQLVKEVASKTNDVAGDGTTTATVLAQAIV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 98 EEAATLRSAGLHPTTIIDGYGRAVEAALDQLAQYERGLHSRQDdrltqIAKTAVTGRWDDastDRFAELTLSALQAIGFD 177
Cdd:TIGR02348 99 KEGLKNVAAGANPIELKRGIEKAVEAVVEELKKLSKPVKGKKE-----IAQVATISANND---EEIGSLIAEAMEKVGKD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 178 rSRLTLKSYPGGELRESVcLDGVLVDLETSSTSLNTLSHPRTRTHDEPAIAMVDAEIgieepNNVESVelqdatqrnafq 257
Cdd:TIGR02348 171 -GVITVEESKSLETELEV-VEGMQFDRGYISPYFVTDAEKMEVELENPYILITDKKI-----SNIKDL------------ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 258 aheqdrrTELVEQVVQSGVTVLLCQKSID-EAVRTALAQ--RGVLPV---------ERtRRDEFDVIARATGSTPV---- 321
Cdd:TIGR02348 232 -------LPLLEKVAQSGKPLLIIAEDVEgEALATLVVNklRGTLNVcavkapgfgDR-RKAMLEDIAILTGGQVIseel 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 322 -MSVDDLTADDTGTVGSVtqrTVGTAQTLVLQGCPEEH---------RATLL-----------------LRGGtphVA-- 372
Cdd:TIGR02348 304 gLKLEEVTLDDLGKAKKV---TVDKDNTTIVEGAGDKAaikarvaqiKAQIEettsdydreklqerlakLAGG---VAvi 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 373 ----------EEVRRIVADCIDVTRVALDDGVfVPGGGavpTALAMDLAALS--REIPDRTQLVFDGFGTALEALPRTLA 440
Cdd:TIGR02348 378 kvgaatetemKEKKLRIEDALNATRAAVEEGI-VPGGG---VALLRAAAALEglKGDGEDEAIGIDIVKRALEAPLRQIA 453
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499541764 441 TNAGTDPLTTLTEIKQRHDagaetvGVGPDGHP---RDMIDAGILEPAAVFRSALQRAVAVVTQILRVDDVV 509
Cdd:TIGR02348 454 ENAGLDGAVVAEKVKELKG------NFGFNAATgeyEDLVEAGIIDPTKVTRSALQNAASIAGLLLTTEAVV 519
|
|
| PTZ00114 |
PTZ00114 |
Heat shock protein 60; Provisional |
23-498 |
3.74e-19 |
|
Heat shock protein 60; Provisional
Pssm-ID: 185455 Cd Length: 555 Bit Score: 90.74 E-value: 3.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 23 ELADAIRTTLGPNGLDKMVVGENGTVIVTNDG---SKIIEWMDITHPVG-RLVEQAAAAQDNTVGDGTTTAVVLVGALLE 98
Cdd:PTZ00114 33 RLADAVAVTLGPKGRNVIIEQEYGSPKITKDGvtvAKAIEFSDRFENVGaQLIRQVASKTNDKAGDGTTTATILARAIFR 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 99 EAATLRSAGLHPTTIIDGYGRAVEAALDQLAQYERGLHSRQDdrLTQIAKTAvtgrwddASTDR-FAELTLSALQAIGfd 177
Cdd:PTZ00114 113 EGCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQSRPVKTKED--ILNVATIS-------ANGDVeIGSLIADAMDKVG-- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 178 rsrltlksypggelresvcLDGVlVDLETSSTSLNTLSHPRTRTHDEPAIA---MVDAEigieepnnVESVELQDA---- 250
Cdd:PTZ00114 182 -------------------KDGT-ITVEDGKTLEDELEVVEGMSFDRGYISpyfVTNEK--------TQKVELENPlilv 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 251 TQRNAFQAHEQDRrteLVEQVVQSGVTVLLCQKSIDEAVRTALA---QRGVLPV--------ERTRRDEFDVIARATGST 319
Cdd:PTZ00114 234 TDKKISSIQSILP---ILEHAVKNKRPLLIIAEDVEGEALQTLIinkLRGGLKVcavkapgfGDNRKDILQDIAVLTGAT 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 320 PV------MSVDDLTADDTGTVGSVTQRtvgTAQTLVLQGCPE----EHRATLL----------------------LRGG 367
Cdd:PTZ00114 311 VVsednvgLKLDDFDPSMLGSAKKVTVT---KDETVILTGGGDkaeiKERVELLrsqierttseydkeklkerlakLSGG 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 368 tphVA------------EEVRRIVADCIDVTRVALDDGVfVPGGGavpTAL-----AMD-LAALSREIPDRT---QLVFD 426
Cdd:PTZ00114 388 ---VAvikvggasevevNEKKDRIEDALNATRAAVEEGI-VPGGG---VALlraskLLDkLEEDNELTPDQRtgvKIVRN 460
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499541764 427 gfgtALEALPRTLATNAGTDPLTTLTEIKQRHDagaetVGVGPD---GHPRDMIDAGILEPAAVFRSALQRAVAV 498
Cdd:PTZ00114 461 ----ALRLPTKQIAENAGVEGAVVVEKILEKKD-----PSFGYDaqtGEYVNMFEAGIIDPTKVVRSALVDAASV 526
|
|
| groEL |
PRK12852 |
chaperonin GroEL; Reviewed |
24-509 |
1.87e-17 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237232 Cd Length: 545 Bit Score: 85.28 E-value: 1.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 24 LADAIRTTLGPNGLDKMVVGENGTVIVTNDG---SKIIEWMDITHPVG-RLVEQAAAAQDNTVGDGTTTAVVLVGALLEE 99
Cdd:PRK12852 23 LANAVKVTLGPKGRNVVIEKSFGAPRITKDGvtvAKEIELEDKFENMGaQMVREVASKTNDLAGDGTTTATVLAQAIVRE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 100 AATLRSAGLHPTTIIDGYGRAVEAALDQLAQYERGLHSRQDdrLTQIAKTAVTGrwdDASTDRfaeLTLSALQAIGfDRS 179
Cdd:PRK12852 103 GAKAVAAGMNPMDLKRGIDIAVAAVVKDIEKRAKPVASSAE--IAQVGTISANG---DAAIGK---MIAQAMQKVG-NEG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 180 RLTLKSYPGGELRESVcLDGVLVDLETSSTSLNTLSHPRTRTHDEPAIAMVDAEIGieepnnvesvELQDAtqrnafqah 259
Cdd:PRK12852 174 VITVEENKSLETEVDI-VEGMKFDRGYLSPYFVTNAEKMTVELDDAYILLHEKKLS----------GLQAM--------- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 260 eqdrrTELVEQVVQSGVTVLLCQKSID-EAVRTALAQ--RGVLPVERT--------RRDEFDVIARATGSTpvmsvddLT 328
Cdd:PRK12852 234 -----LPVLEAVVQSGKPLLIIAEDVEgEALATLVVNrlRGGLKVAAVkapgfgdrRKAMLEDIAILTGGQ-------LI 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 329 ADDTG-TVGSVTQRTVGTAQ--------TLVLQGCPEEHR-----------------------------------ATLLL 364
Cdd:PRK12852 302 SEDLGiKLENVTLKMLGRAKkvvidkenTTIVNGAGKKADiearvgqikaqieettsdydreklqerlaklaggvAVIRV 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 365 RGGTPHVAEEVRRIVADCIDVTRVALDDGVfVPGGGavpTALAMDLAALSREIPDRT--QLVFDGFGTALEALPRTLATN 442
Cdd:PRK12852 382 GGATEVEVKEKKDRVEDALNATRAAVQEGI-VPGGG---VALLRAKKAVGRINNDNAdvQAGINIVLKALEAPIRQIAEN 457
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499541764 443 AGTDPLTTLTEIKQRHDagaETVGV-GPDGHPRDMIDAGILEPAAVFRSALQRAVAVVTQILRVDDVV 509
Cdd:PRK12852 458 AGVEGSIVVGKILENKS---ETFGFdAQTEEYVDMVAKGIIDPAKVVRTALQDAASVAGLLVTTEAMV 522
|
|
| groEL |
CHL00093 |
chaperonin GroEL |
24-503 |
5.54e-17 |
|
chaperonin GroEL
Pssm-ID: 177025 Cd Length: 529 Bit Score: 84.00 E-value: 5.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 24 LADAIRTTLGPNGldKMVVGEN--GTVIVTNDG---SKIIEWMDITHPVG-RLVEQAAAAQDNTVGDGTTTAVVLVGALL 97
Cdd:CHL00093 22 LAEAVSVTLGPKG--RNVVLEKkyGSPQIVNDGvtiAKEIELEDHIENTGvALIRQAASKTNDVAGDGTTTATVLAYAIV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 98 EEAATLRSAGLHPTTIIDGYGRAVEAALDQLAQYERGLHSRQDdrLTQIAKTAVtgrwddASTDRFAELTLSALQAIGfd 177
Cdd:CHL00093 100 KQGMKNVAAGANPISLKRGIEKATQYVVSQIAEYARPVEDIQA--ITQVASISA------GNDEEVGSMIADAIEKVG-- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 178 rsrltlksypggelresvcLDGVLVDLETSSTSlntlshprtrTHDEPAIAMvDAEIGIEEPNNVESVELQDATQRNAFQ 257
Cdd:CHL00093 170 -------------------REGVISLEEGKSTV----------TELEITEGM-RFEKGFISPYFVTDTERMEVVQENPYI 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 258 AHeQDRRTELV--------EQVVQSGVTVLLCQKSID-EAVRTALAQ--RGVLPV---------ERtRRDEFDVIARATG 317
Cdd:CHL00093 220 LL-TDKKITLVqqdllpilEQVTKTKRPLLIIAEDVEkEALATLVLNklRGIVNVvavrapgfgDR-RKAMLEDIAILTG 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 318 STPV-----MSVDDLTADDTGTVGSVTQRTVGTaqTLVLQGCPEEHRA------TLLLRGGTPHVAEEVRRIVA------ 380
Cdd:CHL00093 298 GQVItedagLSLETIQLDLLGQARRIIVTKDST--TIIADGNEEQVKArceqlrKQIEIADSSYEKEKLQERLAklsggv 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 381 ---------------------DCIDVTRVALDDGVfVPGGGAVPTALAMDLAALSREIPDRTQLVfdG---FGTALEALP 436
Cdd:CHL00093 376 avikvgaatetemkdkklrleDAINATKAAVEEGI-VPGGGATLVHLSENLKTWAKNNLKEDELI--GaliVARAILAPL 452
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499541764 437 RTLATNAGTDPLTTLTEIKQR-----HDAGAETVGvgpdghprDMIDAGILEPAAVFRSALQRAVAVVTQIL 503
Cdd:CHL00093 453 KRIAENAGKNGSVIIEKVQEQdfeigYNAANNKFV--------NMYEAGIIDPAKVTRSALQNAASIASMIL 516
|
|
| PRK14104 |
PRK14104 |
chaperonin GroEL; Provisional |
24-509 |
7.78e-16 |
|
chaperonin GroEL; Provisional
Pssm-ID: 172594 Cd Length: 546 Bit Score: 80.46 E-value: 7.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 24 LADAIRTTLGPNGLDKMVVGENGTVIVTNDG---SKIIEWMDITHPVG-RLVEQAAAAQDNTVGDGTTTAVVLVGALLEE 99
Cdd:PRK14104 23 LANAVKVTLGPKGRNVVLDKSFGAPRITKDGvtvAKEIELEDKFENMGaQMVREVASKSADAAGDGTTTATVLAQAIVRE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 100 AATLRSAGLHPTTIIDGYGRAVEAALDQLAQYERGLHSrqDDRLTQIAKTAVTGrwdDASTDRFAEltlSALQAIGfDRS 179
Cdd:PRK14104 103 GAKSVAAGMNPMDLKRGIDLAVEAVVADLVKNSKKVTS--NDEIAQVGTISANG---DAEIGKFLA---DAMKKVG-NEG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 180 RLTLKsypggelrESVCLDGVLVDLETSSTSLNTLSHPRTRTHDEPAIAMVDAEIGIEEPNNVESVELqdatqrnafqah 259
Cdd:PRK14104 174 VITVE--------EAKSLETELDVVEGMQFDRGYISPYFVTNADKMRVEMDDAYILINEKKLSSLNEL------------ 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 260 eqdrrTELVEQVVQSGVTVLLCQKSID-EAVRTALAQ--RGVLPVERT--------RRDEFDVIARATGSTPV-----MS 323
Cdd:PRK14104 234 -----LPLLEAVVQTGKPLVIVAEDVEgEALATLVVNrlRGGLKVAAVkapgfgdrRKAMLQDIAILTGGQAIsedlgIK 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 324 VDDLT-------------ADDTGTVGSVTQRTVGTAQTLVLQGCPEEHR-------------------ATLLLRGGTPHV 371
Cdd:PRK14104 309 LENVTlqmlgrakkvmidKENTTIVNGAGKKADIEARVAQIKAQIEETTsdydreklqerlaklaggvAVIRVGGATEVE 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 372 AEEVRRIVADCIDVTRVALDDGVfVPGGGAVPTALAMDLAALSREIPDRTQLVfDGFGTALEALPRTLATNAGTDPLTTL 451
Cdd:PRK14104 389 VKERKDRVDDAMHATRAAVEEGI-VPGGGVALLRASEQLKGIKTKNDDQKTGV-EIVRKALSAPARQIAINAGEDGSVIV 466
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 452 TEI--KQRHDAGAETvgvgPDGHPRDMIDAGILEPAAVFRSALQRAVAVVTQILRVDDVV 509
Cdd:PRK14104 467 GKIleKEQYSYGFDS----QTGEYGNLVSKGIIDPTKVVRTAIQNAASVAALLITTEAMV 522
|
|
| PLN03167 |
PLN03167 |
Chaperonin-60 beta subunit; Provisional |
18-509 |
3.04e-15 |
|
Chaperonin-60 beta subunit; Provisional
Pssm-ID: 215611 [Multi-domain] Cd Length: 600 Bit Score: 78.43 E-value: 3.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 18 QTAAGELADAIRTTLGPNGLDKMVVGENGTVIVTNDGSKIIEWMDITHPV----GRLVEQAAAAQDNTVGDGTTTAVVLV 93
Cdd:PLN03167 72 QAGVNKLADLVGVTLGPKGRNVVLESKYGSPKIVNDGVTVAKEVELEDPVenigAKLVRQAAAKTNDLAGDGTTTSVVLA 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 94 GALLEEAATLRSAGLHPTTIIDGYGRAVEAALDQLAQYERGLhsrQDDRLTQIAktAVTGRWDDASTDRFAEltlsALQA 173
Cdd:PLN03167 152 QGLIAEGVKVVAAGANPVQITRGIEKTAKALVKELKKMSKEV---EDSELADVA--AVSAGNNYEVGNMIAE----AMSK 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 174 IGfDRSRLTLKSYPGGELRESVcLDGVLVDLETSSTSLNTLSHPRTRTHDEPAIAMVDAEIgieepnnvesvelqdATQR 253
Cdd:PLN03167 223 VG-RKGVVTLEEGKSAENNLYV-VEGMQFDRGYISPYFVTDSEKMSVEYDNCKLLLVDKKI---------------TNAR 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 254 NAFQaheqdrrteLVEQVVQSGVTVLLCQKSID-EAVRTALAQ--RGVLPVERTRRDEF--------DVIARATGSTPV- 321
Cdd:PLN03167 286 DLIG---------ILEDAIRGGYPLLIIAEDIEqEALATLVVNklRGSLKIAALKAPGFgerksqylDDIAILTGGTVIr 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 322 ----MSVDD-------------LTADDTGTVG------SVTQRtVGTAQTLVLQGCPEEHRATL-----LLRGG------ 367
Cdd:PLN03167 357 eevgLSLDKvgkevlgtaakvvLTKDTTTIVGdgstqeAVNKR-VAQIKNLIEAAEQDYEKEKLneriaKLSGGvaviqv 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 368 ---TPHVAEEVRRIVADCIDVTRVALDDGVFVpGGGAVPTALAMDLAALSREIPDRTQLV-FDGFGTALEALPRTLATNA 443
Cdd:PLN03167 436 gaqTETELKEKKLRVEDALNATKAAVEEGIVV-GGGCTLLRLASKVDAIKDTLENDEQKVgADIVKRALSYPLKLIAKNA 514
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 444 GTDPLT----TLTEIKQRHDAGAETvgvgpdGHPRDMIDAGILEPAAVFRSALQRAVAVVTQILRVDDVV 509
Cdd:PLN03167 515 GVNGSVvsekVLSNDNPKFGYNAAT------GKYEDLMAAGIIDPTKVVRCCLEHAASVAKTFLTSDCVV 578
|
|
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
24-498 |
3.26e-12 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 69.00 E-value: 3.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 24 LADAIRTTLGPNGLDkmVVGEN--GTVIVTNDGSKI---IEWMDITHPVG-RLVEQAAAAQDNTVGDGTTTAVVLVGALL 97
Cdd:PRK00013 22 LADAVKVTLGPKGRN--VVLEKsfGAPTITKDGVTVakeIELEDPFENMGaQLVKEVASKTNDVAGDGTTTATVLAQAIV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 98 EEAATLRSAGLHPTTIIDGYGRAVEAALDQLAQYERGLHSRQddrltQIAKTA-VTGRWDDASTDRFAE----------- 165
Cdd:PRK00013 100 REGLKNVAAGANPMDLKRGIDKAVEAAVEELKKISKPVEDKE-----EIAQVAtISANGDEEIGKLIAEamekvgkegvi 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 166 ---------LTLSALQAIGFDRSRLTlkSYpggelresvcldgVLVDLETSSTSLntlshprtrthDEPAIAMVDAEIgi 236
Cdd:PRK00013 175 tveeskgfeTELEVVEGMQFDRGYLS--PY-------------FVTDPEKMEAEL-----------ENPYILITDKKI-- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 237 eepNNVEsvelqdatqrnafqaheqdrrtELV---EQVVQSGVTVLLCQKSIDEAVRTALA---QRGVLPV--------- 301
Cdd:PRK00013 227 ---SNIQ----------------------DLLpvlEQVAQSGKPLLIIAEDVEGEALATLVvnkLRGTLKVvavkapgfg 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 302 ERtRRDEFDVIARATGSTPV-----MSVDDLTADDTGTVGSVtqrTVGTAQTLVLQGCPE----EHRATLL--------- 363
Cdd:PRK00013 282 DR-RKAMLEDIAILTGGTVIseelgLKLEDATLEDLGQAKKV---VVTKDNTTIVDGAGDkeaiKARVAQIkaqieetts 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 364 -------------LRGGtphVA------------EEVRRIVADCIDVTRVALDDGVfVPGGGavpTAL---AMDLAALSR 415
Cdd:PRK00013 358 dydreklqerlakLAGG---VAvikvgaatevemKEKKDRVEDALHATRAAVEEGI-VPGGG---VALlraAPALEALKG 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 416 EIPDRT---QLVFDgfgtALEALPRTLATNAGTDPLTTLTEIKQRHDAG----AETvgvgpdGHPRDMIDAGILEPAAVF 488
Cdd:PRK00013 431 LNGDEAtgiNIVLR----ALEAPLRQIAENAGLEGSVVVEKVKNGKGKGygynAAT------GEYVDMIEAGIIDPTKVT 500
|
570
....*....|
gi 499541764 489 RSALQRAVAV 498
Cdd:PRK00013 501 RSALQNAASV 510
|
|
| Fab1_TCP |
cd03334 |
TCP-1 like domain of the eukaryotic phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinase Fab1. ... |
183-379 |
1.39e-05 |
|
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: 46.83 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 183 LKSYPGGELRESVCLDGVLVdleTSSTSLNTLShprtRTHDEPAIAMVDAEIGIEEPNN----VESVELQdatqrnafqa 258
Cdd:cd03334 52 IKKIPGGSPSDSEVVDGVVF---TKNVAHKRMP----SKIKNPRILLLQGPLEYQRVENkllsLDPVILQ---------- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541764 259 hEQDRRTELVEQVVQSGVTVLLCQKSIDeavRTA---LAQRGVLPVERTRRDEFDVIARATGSTPVMSVDDLTADDT-GT 334
Cdd:cd03334 115 -EKEYLKNLVSRIVALRPDVILVEKSVS---RIAqdlLLEAGITLVLNVKPSVLERISRCTGADIISSMDDLLTSPKlGT 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 499541764 335 VGSVTQRTV----GTAQTLV-LQGCPEEHRATLLLRGGTPHVAEEVRRIV 379
Cdd:cd03334 191 CESFRVRTYveehGRSKTLMfFEGCPKELGCTILLRGGDLEELKKVKRVV 240
|
|
| |
